Property Summary

NCBI Gene PubMed Count 335
PubMed Score 642.19
PubTator Score 538.69

Knowledge Summary

Patent

No data available

Expression

  Differential Expression (22)

Disease log2 FC p
chronic lymphocytic leukemia 1.218 1.1e-02
malignant mesothelioma 3.900 1.4e-09
cutaneous lupus erythematosus 2.700 9.3e-05
osteosarcoma -2.397 1.6e-03
glioblastoma 1.400 6.6e-03
astrocytoma -1.200 2.5e-02
adrenocortical carcinoma -1.280 2.5e-02
chronic kidney disease 1.200 3.8e-02
tuberculosis and treatment for 6 months -1.300 5.4e-05
lung cancer -2.400 4.9e-04
active Crohn's disease 1.480 7.0e-03
Breast cancer 1.800 4.5e-02
adult high grade glioma 1.200 5.9e-03
pilocytic astrocytoma 1.200 4.7e-05
primary Sjogren syndrome 2.400 1.4e-04
subependymal giant cell astrocytoma 2.007 4.5e-02
invasive ductal carcinoma 1.023 9.5e-03
psoriasis 1.100 2.4e-05
lung carcinoma -1.700 1.0e-18
ulcerative colitis 2.600 2.6e-05
ovarian cancer -1.100 9.6e-05
pituitary cancer 2.000 3.7e-05

MLP Assay (12)

AID Type Active / Inconclusive / Inactive Description
493012 screening 933 / 0 / 330928 uHTS identification of APOBEC3G DNA Deaminase Inhibitors via a fluorescence-based single-stranded DNA deaminase assay
493028 summary 0 / 0 / 0 Summary assay for APOBEC3G DNA Deaminase Inhibitors
493152 screening 644 / 0 / 247 Single concentration confirmation of uHTS for APOBEC3G DNA Deaminase Inhibitors via a fluorescence-based single-stranded DNA deaminase assay
504719 confirmatory 449 / 0 / 10 Dose Response confirmation of small molecule APOBEC3G DNA Deaminase Inhibitors via a fluorescence-based single-stranded DNA deaminase assay
504723 confirmatory 438 / 0 / 10 Dose Response confirmation of APOBEC3A DNA Deaminase Inhibitors via a A3G counterscreen
588379 confirmatory 11 / 36 / 1344 qHTS for inhibitors of Vif-A3G interactions: Validation
588444 summary 0 / 0 / 0 qHTS for inhibitors of Vif-A3G interactions: Summary
602136 confirmatory 17 / 0 / 82 SAR analysis of small molecule inhibitors of APOBEC3G DNA Deaminase via a fluorescence-based single-stranded DNA deaminase assay
602310 confirmatory 311 / 8292 / 398161 qHTS for Inhibitors of Vif-A3G Interactions: qHTS
624087 confirmatory 20 / 0 / 23 SAR analysis of small molecule inhibitors of APOBEC3G DNA Deaminase via a fluorescence-based single-stranded DNA deaminase assay - Set 2
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Gene RIF (614)

PMID Text
27003258 STAT3 plays an important role in IFN-induced A3G production, and HBsAg may correlated with poor response to IFN treatment
26772882 USF1 gene can take part in basal transcription regulation of the human A3G gene in hepatocyte, and the identified E-box represented a binding site for the USF1.
26741797 This study demonstrates an association of rs6001417, rs8177832, and rs35228531 of APOBEC3G with HIV-1 infection in a population from Burkina Faso.
26668372 Data show that restriction factor APOBEC3G (A3G) is susceptible to degradation by the HIV-1 Vif protein, whereas restriction factor APOBEC3B (A3B) is resistant to Vif.
26503602 Atomic Force spectroscopy revealed two distinct binding modes by which A3G interacts with ssDNA. One mode requires sequence specificity, as demonstrated by stronger and more stable complexes with deaminase specific ssDNA than with nonspecific ssDNA.
26482266 Findings support a role for APOBEC3G/F proteins in the generation of plasma drug-resistant minority human immunodeficiency virus type 1 variants (DRMVs). However, this role seems to be limited to a small subset of mutations and does not explain most of the DRMVs evaluated.
26460502 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
26424853 The data predicts a mechanistic model of RNA inhibition of ssDNA binding to APOBEC3G in which competitive and allosteric interactions determine RNA-bound versus ssDNA-bound conformational states.
26385832 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
26275799 Results were consistent with Pokeweed antiviral protein activity inhibiting translation of Vif, which in turn reduces the effect of Vif to inactivate the host restriction factor APOBEC3G.
26241003 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
26178819 results demonstrate that the up-regulation of A3G in pancreatic cancer cells induces anoikis resistance, and they provide novel insight into the mechanism by which A3G affects the malignant behavior of pancreatic cancer cells
26105074 This study identifies a new cellular complex, HDAC6/A3G, involved in the autophagic degradation of Vif, and suggests that HDAC6 represents a new antiviral factor capable of controlling HIV-1 infectiveness by counteracting Vif and its functions.
26105074 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
26055363 Incomplete APOBEC3G/F neutralization by a single Vif amino acid substitution.
26055363 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
26048885 APOBEC3G is more efficient at mutating retroviral DNA than APOBEC3F.
26016442 A3G and A3F inhibit porcine endogenous retrovirus replication.
25985400 This study showed a high level of APOBEC3F/3G editing in HIV-2 sequences from antiretroviral-naive patients.
25984970 The human APOBEC3G N-terminal domain is bound by HIV-1 Vif.
25984970 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25974865 These results highlight that the N-terminal domain of the full length A3G protein has an important influence on its DNA sequence specificity and mutator activity.
25912140 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25901786 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25847768 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25827531 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25811715 Human APOBEC3G C-terminal directly binds hepatitis C virus non-structural protein NS3 at its C-terminus.
25807049 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25724652 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25717111 No single viral polymorphism could explain the reduced anti-APOBEC3G activity of elite controllers-derived Vif, suggesting that various combinations of minor polymorphisms may underlie these effects.
25717111 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25590131 The rather indiscriminate RNA binding characteristics of A3G and A3F promote functionality by enabling recruitment into a wide range of retroviral particles whose packaged RNA genomes comprise divergent sequences.
25590131 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25579575 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25501566 A3 shifts the balance, from the fast antibody response mediated by marginal zone B cells with little affinity maturation, to a more sustained germinal center B-cell response
25489169 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25461536 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25424878 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25408426 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25384438 upregulated in the skin of Lichen planus patients
25352838 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25330146 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25304135 Vif continues to protect HIV-1 from the deleterious effects of APOBEC3G, even after packaging of APOBEC3G has occurred.
25304135 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25275135 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25213124 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25206352 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25200749 Vpr downregulated APOBEC3G through Vpr-binding protein (VprBP)-mediated proteasomal degradation, and further confirmed that the reduction of APOBEC3G encapsidation associated with Vpr was due to Vpr's degradation-inducing activity.
25200749 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25196417 It may be concluded hepatitis B virus up-regulates HBD-3 and A3G expression in vivo and in vitro in placental trophoblast and lack of this up-regulation is possibly associated with intrauterine transmission of hepatitis B.
25169827 In APOBEC3G-expressing but not in APOBEC3G-deficient T cell lines.
25169827 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25127418 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25124760 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25080100 APOBEC3 induced mutation of human immunodeficiency virus type-1 contributes to adaptation and evolution in natural infection.
25038404 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
25008917 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24986077 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24942576 Authors found that APOBEA3G, APOBEA3F, and APOBEA3H-hapII, but not APOBEA3D, were susceptible to HIV-2 Vif-induced degradation.
24899191 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24859335 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24851906 Both A3A and A3G restrict infection by murine retroviruses: A3G was packaged into virions and caused extensive deamination of the retrovirus genomes while A3A was not packaged and instead restricted infection when expressed in target cells.
24851906 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24810617 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24772904 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24722422 APOBEC3G/F mutational hotspots in the human immunodeficiency virus genome have roles in reducing recognition by CD8+ T cells
24657093 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24651717 we demonstrate key differences in the impact of APOBEC3F- and APOBEC3G-induced mutagenesis on HIV-1
24623435 99.3% of the antiviral effect of APOBEC3G is dependent on its deaminase activity, whereas 30.2% of the antiviral effect of APOBEC3F is attributed to deaminase-independent ability.
24586139 develop a new Bayesian approach to the detection of APOBEC3-mediated hypermutation, and use it to compare simian foamy virus sequences from human and primate hosts living in close proximity in Bangladesh
24553842 These studies disclosed that antiviral IFN-induced MxA and APOBEC3G/3F mRNA levels were increased after IL-32gamma treatment of peripheral blood mononuclear cells.
24522927 Authors propose that CBFbeta acts as a chaperone to stabilize HIV-1 Vif during and after synthesis and to facilitate interaction of Vif with cellular cofactors required for the efficient degradation of APOBEC3G.
24522927 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24503066 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24500029 A3G inhibits the growth of human hepatoma cells.
24498164 The motif-dependent mutation of G within the HIV genome by members of the APOBEC3 family other than APOBEC3G was limited to GA-->AA changes
24478136 A new real-time NMR method has been developed to examine the nonspecific binding and the sliding processes explicitly, and it was applied to the analysis of the deamination by A3G.
24422669 N-terminal mutants of HIV-1 vif that demonstrated reduced Cul5 binding were also unable to degrade APOBEC3G as well as APOBEC3F.
24418547 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24418540 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24400003 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24390335 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24390320 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24367644 inhibitory activities of hA3G against Alu and L1 retrotransposition
24361275 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24352440 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24345943 show that APOBEC3G initially binds ssDNA with rapid on-off rates and subsequently converts to a slowly dissociating mode
24248339 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24246762 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24245672 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24227842 APOBEC3 deaminases upregulated by IFN-beta induce E2 hypermutation of HPV16 in cervical keratinocytes.
24198285 A3G interacts physically with GANP wih activated T4 cells, which facilitates its packaging into HIV-1 cores. It catalyzes G-->A hypermutation in the viral genome & suppresses HIV-1 infectivity.
24198285 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24189052 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24185281 An amphipathic surface that is conserved in APOBEC3 proteins is critical for HIV-1 Vif susceptibility.
24158820 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24146808 Vif-positive viruses with more host APOBEC3G expressed were found to have decreased virion infectivity ex vivo.
24139399 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24098356 Lipid raft-associated LMM A3G complex functions as the cellular source of viral hA3G
24098115 APOBEC3G polymorphism as a selective barrier to cross-species transmission and emergence of pathogenic SIV and AIDS in a primate host.
24089548 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
24055458 A3G oligomers dissociate spontaneously into monomers and this process primarily occurs through a monomer dissociation pathway.
24010642 This result suggests that genetic variations in APOBEC3 cytidine deaminases do not predispose to chronicity but may modulate the course of persistent hepatitis B virus infection.
23988114 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23986590 Authors show that Vif proteins from distinct lineages bind to the same APOBEC3G loop, which includes positions 128 and 129.
23986590 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23926332 Authors conclude that HIV-1 virion incorporation and the antiviral activities of Mov10 and APOBEC3G do not require their localization to P bodies.
23926332 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23890083 APOBEC3G inhibits DND1 function to regulate microRNA activity.
23870316 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23831493 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23825473 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23787464 [review] APOBEC3G (A3) is a two-domain deaminase with a Z2 and a Z1 domain. A3 proteins occur as monomers, dimers, and large oligomeric complexes; relevance for A3 complex formation and activity remains a matter of debate.
23787464 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23760237 Prototype foamy virus Bet counteracts APOBEC3G by: (i) preventing encapsidation of APOBEC3G by blocking APOBEC3G dimerization, and (ii) sequestering APOBEC3G in immobile complexes, impairing its ability to interact with nascent virions.
23724012 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23717565 The deamination-independent inhibition of reverse transcriptase can be a mechanism used by APOBEC3G to slow down HIV1 proviral DNA formation.
23717565 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23707381 Overall, the results of this study indicate that the HIV-1 Vif residue I107 is important for its anti-APOBEC3G activity and viral replication, which may have implications for viral fitness in vivo.
23707381 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23696735 UNG excises uracil residues from the viral genome during or after cccDNA formation in the nucleus and imply that BER pathway activities decrease the antiviral effect of APOBEC3-mediated hypermutation.
23689841 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23640893 A novel role for IL-2 in regulating production of infectious HIV-1 virions in HTLV-1-infected cells through the induction of APOBEC3G.
23621690 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23598277 Studies indicate that APOBEC3B (A3B) was identified as the mutational source in breast cancer cells, and APOBEC3G (A3G) was predominantly expressed in lymphoma cells and involved in DNA repair.
23596292 H216 is responsible for pH dependence of APOBEC3G, suggesting that protonation of H216 could play a key role in substrate binding, and protonation of H216 appeared important for HIV-1 restriction activity.
23576497 Cellular APOBEC3G impairs the multimerization of the HIV-1 Vif protein.
23576497 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23545135 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23536679 APOBEC3F/G-specific responses in HIV-1-infected patients are CD8+ T cell mediated.
23432984 This study indicates that despite very low levels of both A3G in liver and the number of positive subjects, A3G has a potential role to restrict the in vivo replication of HBV.
23430691 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23428096 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23411593 We provide convincing evidence for a novel breast cancer locus at the APOBEC3 genes. This CNV is one of the strongest common genetic risk variants identified so far for breast cancer.
23330719 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23318957 Data indicate that internal lysines are the dominant ubquuitin (Ub) acceptor sites in both APOBEC3F(A3F) and APOBEC3G (A3G).
23318957 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23316055 Vif co-encapsidation with APOBEC3G can promote sublethal mutagenesis of HIV-1 proviral DNA.
23316055 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23300442 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23255806 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23202519 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23189135 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23175372 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23152537 Detailed analyses of mutation spectra in viral cDNA strongly imply that one particular APOBEC3 protein, APOBEC3G, provides the bulk of the antiviral phenotype in CD4(+) T cells, with the effects of APOBEC3F and APOBEC3D being less significant.
23138837 In this study, we found that the presence of APOBEC3G-F119F and H186R genetic variants were associated with altered HIV-1 disease progression in children.
23097438 The authors conclude that APOBEC3G exerts a greater restriction effect on HIV-1 than APOBEC3F and APOBEC3DE.
23097438 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23080486 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23043103 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23043100 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
23028129 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22999946 Studies indicate that restriction factors APOBEC3G, TRIM5, Tetherin and SAMHD1 exhibit direct antiviral activity.
22970171 This analysis further detects two new potential interaction surfaces in the N-and C-terminal domain of Apobec3G for interaction with Vif and Gag or for Apobec3G dimerization.
22970171 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22915799 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22912627 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22894923 These data suggest that Vif and A3G are not serine/threonine phosphorylated in human cells and phosphorylation is not linked to their functional activities.
22894923 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22855686 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22828015 Glyco-gag dependent restriction for xenotropic murine leukemia virus-related virus in human cells appears to be APOBEC3-independent.
22809226 APOBEC3G monomers, dimers, and higher-order oligomers can bind ssDNA substrates in a manner independent of strand polarity and availability of free ssDNA ends.
22807680 endogenous levels of APOBEC3D, APOBEC3F, and APOBEC3G combine to restrict Vif-deficient HIV-1 and cause the hallmark dinucleotide hypermutation patterns in in the nonpermissive T cell line CEM2n
22791714 APOBEC3G inhibits microRNA-mediated repression of translation by interfering with the interaction between Argonaute-2 and MOV10
22787460 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22728817 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22725134 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22720156 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22695298 M184I and E138K resistance-associated mutations may pre-exist in proviral reservoir prior to drug exposure, as a result of APOBEC3 editing. Incomplete neutralization of APOBEC3 proteins may favor viral escape to rilpivirine-emtricitabine.
22695298 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22647704 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22645179 APOBEC3G activity involved processing of DNA flanking a DSB in an integrated reporter cassette. Atomic force microscopy indicated that APOBEC3G multimers associate with ssDNA termini, triggering multimer disassembly to multiple catalytic units.
22579353 These results indicate that APOBEC3G deaminase-dependent activity above a threshold level, and its deaminase-independent functions, contribute to decreasing Vif-positive HIV virus replication in vivo.
22555953 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22553496 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22509177 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22421880 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22379088 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22369580 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22362763 Data show that deamination polarity occurs as a consequence of APOBEC3G (Apo3G) binding to ssDNA in two orientations, one that is catalytically favorable, with the other disfavorable.
22347227 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22346743 Developed a multi-scale computational system that models human APOBEC3G and HIV-1 Vif interactions, including HIV replication.
22346743 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22339232 In summary, our results cast doubt on all previous structure-function predictions for APOBEC3G that were based on the crystal structure of APOBEC2.
22315404 APOBEC3G/3F and BST-2 mRNA expression was significantly elevated during IFN-alpha/riba treatment in patient-derived CD4+ T cells (P < 0.04 and P < 0.008, paired Wilcoxon), and extent of BST-2 induction was correlated with reduction in HIV-1 viral load.
22301159 The cellular APOBEC3G interacts with HIV-1 reverse transcriptase and inhibits its function during viral replication.
22301159 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22291694 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22286874 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22274659 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22272271 Data suggest that positive selection was apparent along a few branches which differed compared to positive selection in the carboxy-terminal of APOBEC3G (A3G) that clusters with APOBEC3A (A3A) among cytidine deaminases.
22264516 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22218868 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22205746 Vif proteins of human and simian immunodeficiency viruses require cellular CBFbeta to degrade APOBEC3G.
22205746 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22203821 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22190037 CBF-beta is required for Vif-mediated degradation of APOBEC3G and therefore for preserving HIV-1 infectivity
22190037 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22190036 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22152111 Xenotropic murine leukemia virus induced downregulation of A3G may represent a new pathway by which retroviruses counteract antiviral effects of A3 (specifically, APOBEC3G) proteins in human cells.
22017399 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
22013041 Most Vif proteins counteract APOBEC3G and APOBEC3F efficiently but display differences with respect to the inhibition of APOBEC3H.
22013041 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21994608 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21994586 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21994560 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21985787 novel mechanism in which APOBEC3G promotes colorectal cancer hepatic metastasis through inhibition of miR-29-mediated suppression of MMP2
21972557 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21971250 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21935481 Study propose that RPA plays a role in the protection of the human genome cell from A3G and other deaminases when they are inadvertently diverged from their natural targets.
21934670 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21897871 levels of A3G and A3F expression and induced G-to-A hypermutation in a group of children with distinct profiles of disease progression
21874023 report that viral protein R (Vpr), which interacts with a uracil glycosylase, also counteracted APOBEC3G by diminishing the incorporation of uridine
21874023 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21856286 The data provided direct evidence that A3G binding to cellular RNAs constituted a substantial impediment to the enzyme's ability to interact with ssDNA.
21835787 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21784078 Therapy-naive HIV-1 patients tended to have lower expression levels of APOBEC3G and TRIM5alpha than HIV-1 negative controls.
21763507 virion-associated Vif could serve as a last line of defense, protecting the virus against Apobec3G antiviral activity.
21763507 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21752914 The authors conclude that endogenous APOBEC3G complexes in producer cells decrease HIV-1 production if not degraded by Vif.
21752914 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21741003 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21737457 deaminase-dependent antiviral activity of A3G in vivo may require a critical concentration of A3G in viral particles that will promote oligomerization on ssDNA during reverse transcriptio
21734566 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21734563 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21698207 Silencing of APOBEC3G in DC abrogated the HIV inhibitory effect mediated by ApoAct.
21659520 Phosphorylation directly regulates the intrinsic DNA cytidine deaminase activity of activation-induced deaminase and APOBEC3G protein
21573951 G-to-A mutations on V3 HIV peptide caused by APOBEC3F and APOBEC3G facilitate co-receptor switch of HIV from R5 to X4 strains.
21571098 Vif alterations may contribute to a rapid AIDS onset and Vif variability could be influenced by APOBEC3G and CUL5 polymorphisms in children
21489586 Two cytidine deaminase domains of APOBEC3G were functionally equivalent in virion encapsidation and the interaction with HIV-1 Vif.
21489586 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21480314 hA3G appears to be a cellular restrict factor against HCV and could be a potential target for drug discovery.
21480314 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21393191 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21373976 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21370050 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21345952 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21300806 the balance between the jumping and sliding of Apo3G is needed for efficient mutational inactivation of HIV-1.
21279453 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21239176 Studies suggest that APOBEC3G (A3G) has the potential to act as a double agent in HIV infection.
21239176 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21228271 overexpression of HSP70 inhibited APOBEC3G binding to HIV-1 Vif.
21228271 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21217078 NGF increases HIV-1 replication in primary monocyte-derived macrophages by engaging its classic TrKA signaling and down-regulating the synthesis of the HIV-1 natural restriction factor APOBEC3G
21182427 A significant inhibition of HIV-1 infection was observed in PBMCs and macrophages transduced with R14-88 APOBEC3G mutant fusion proteins.
21182427 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21152581 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21149631 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21147467 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21147461 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
21123176 APOBEC3G exchanges between oligomeric forms in solution with monomers predominating and that this equilibrium shifts toward dimerization upon binding ssDNA.
21078663 NFAT and IRF proteins regulate transcription of the anti-HIV gene, APOBEC3G.
20939174 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20874421 human APOBEC3G (A3G) protein activity obstructs retrovirus infection by inducing mutations of guanosines to adenosines (G --> A) in the viral DNA
20844042 HIV-1 central polypurine tract functions as a second line of defense against APOBEC3G and APOBEC3F.
20833716 Data show that Viruses produced from cells expressing APOBEC3G and Vif proteins from different subtypes showed relatively different viral infectivities.
20833716 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20712566 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20702622 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20686027 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20668529 Findings confirm and extend recently published data that show restriction of XMRV infection by hA3G.
20668078 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20642434 tested the effect of APOBEC3G expression on the HIV-1 infection of cells derived from purified CD34+ cells; data implies that when APOBEC3G is expressed high enough, it can escape the inhibition from Vif, thereby exerting its antiviral activity
20642434 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20638642 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20636339 TLR3 acativation by polyI:C resulted in inhibition of HIV infections in macrophages via induction of type 1 interferon antiviral factors, tetherin and APOBEC3G.
20624919 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20610708 These results provide the evidence indicating that endogenous APOBEC3s, including APOBEC3G, are associated with G-to-A mutation of HIV-1 provirus in vivo, which can result in the abrogation of HIV-1 infection.
20610708 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20592083 T(Q/D/E)x(5)ADx(2)(I/L) motif of HIV1 Vif protein is a critical motif for interaction with APOBEC3G and APOBEC3F.
20592083 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20592068 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20571604 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20538015 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20523896 the cytokine storm associated with chronic inflammatory responses to hepatitis B and C clearly up regulates a number of A3 genes with A3G clearly being a major restriction factor for hepatitis B
20510315 These results suggest the possibility that APOBEC3G is incorporated into HBV viral particles via direct binding with hepatitis B virus core protein.
20463080 These data indicate that APOBEC3G-dependent restriction of HIV-1 can result in viable viral progeny that harbor sublethal levels of G-to-A mutations.
20463080 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20463074 Data suggest that HTLV-1-infected cells likely take advantage of human APOBEC3G to escape from the host immune system by losing expression of viral proteins.
20463065 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20363737 analysis of how small molecular compounds inhibit HIV-1 replication through specifically stabilizing APOBEC3G
20363737 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20338830 the sequence selectivity of APOBEC family of enzymes
20335268 hiv1 VIF sequences (81)LGxGxxIxW(89) and (171)EDRW(174) are two novel functional domains that are very critical for Vif function and Vif binding to both A3G and A3F
20335268 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20299747 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20219927 The authors observed that both APOBEC3F and APOBEC3G inhibit HIV-1 DNA synthesis and integration, but APOBEC3F is more potent than APOBEC3G in preventing HIV-1 DNA integration.
20219919 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20212048 Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G.
20174454 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20153011 exosomes secreted by CD4(+)H9 T cells and mature monocyte-derived dendritic cells encapsidate APOBEC3G and APOBEC3F and inhibit L1 and Alu retrotransposition
20152150 crystal structure of the catalytically active C-terminal domain of APOBEC3G was determined to 2.25 A.
20147392 These data suggest that polyubiquitination of APOBEC3G, not that of HIV-1 Vif, is crucial for APOBEC3G degradation.
20147392 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20128960 APOBEC3G is upregulated in the PBMCs of chronic hepatitis B patients.
20104108 Higher expression levels of hA3G and hA3B mRNA in the peripheral blood mononuclear cells of Chinese HIV-infected individuals were found to be associated with slower HIV disease progression.
20096141 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20038599 a novel function for A3G, acting not only as an intrinsic antiviral factor but also as an inducer of the adaptive immune system.
20023216 CCR6 ligands inhibit HIV by inducing APOBEC3G.
20023216 CCR6 ligands induce APOBEC3G expression, and inhibit HIV infection in highly susceptible CCR6+ cells
20018238 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20015971 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20012529 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
20012521 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19996938 During primary infection, APOBEC3G expression levels in peripheral blood mononuclear cells do not correlate with viral loads or CD4 T-cell counts.
19996938 Observational study of gene-disease association. (HuGE Navigator)
19944180 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19939923 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19910370 In vitro translation evidenced that Vif inhibited APOBEC-3G translation by two mechanisms: a main time-independent process requiring the 5'UTR and an additional time-dependent, UTR-independent process.
19887642 four Lys residues in the CTD of APOBEC3G that are required for Vif-mediated polyubiquitination and degradation were identified.
19887642 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19886996 These results confirm that W127 and Y124 residues in APOBEC3G are important for encapsidation into HIV-1 virions and the data establish a novel correlation between genomic RNA binding, lipid raft association, and viral packaging of APOBEC3G.
19841153 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19837465 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19826902 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19776130 These results reveal the importance of a predicted RNA binding dimerization interface of APOBEC3G both for packaging into HIV-1 virions and inhibition of both HIV-1 infection and Alu transposition.
19776130 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19717177 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19694548 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19669862 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19649317 APOBEC3G levels are both low and variable within individual cells of the CEM-T4 line, thus providing a reasonable molecular explanation for the permissive phenotype of this cell line.
19649317 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19587057 APOBEC3G and APOBEC3F gene expression in immune system and hematopoietic system cells
19585516 Alloimmune-induced APOBEC3G was found to be significantly increased in CD45RA(-), CCR5(+) and CD45RA(-)CCR7(-) subsets of effector memory T cells.
19561087 When recognition loop of 9-11 amino acids is grafted from the donor APOBEC3F or 3G proteins into the acceptor scaffold of AID, the mutational signature of AID changes toward that of the donor proteins.
19535450 Amino acids K22, K26, Y30, and Y40 were found to be important for the Vif-induced degradation and suppression of cellular APOBEC3G.
19535450 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19535447 Thus, (21)WxSLVK(26) is a novel functional domain that regulates Vif activity toward both APOBEC3F and APOBEC3G and is a potential drug target to inhibit Vif activity and block HIV-1 replication.
19535447 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19535442 The comparison between activated Th1 and Th2 cells indicates that cytoplasmic APOBEC3G in activated Th1 cells partially restricts reverse transcription and integration of incoming Vif-positive, APOBEC3G-negative HIV-1.
19497112 These studies show that A3G forms multimers in cells and that this multimerization is dependent on RNA binding. Association of A3G with HIV-1 Gag is dependent on RNA binding.
19494012 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19487726 relationship between the human immunodeficiency virus type 1 viral infectivity factor (Vif) and the human APOBEC-3G and APOBEC-3F restriction factors [Review]
19487726 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19401538 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19389408 Contrary to predictions, this structurally constrained model suggested that the two domains are tethered by structured residues and that the N- and C-terminal beta2 regions are too distant from each other to participate in this interaction.
19371434 Although strongly induced, APOBEC3G does not negatively affect influenza A virus propagation.
19357165 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19345973 This study demonstrated that HIV-1 and SARS-CoV nucleocapside chimeras are capable of packaging large amounts of human APOBEC3G (hA3G) and that hA3G is capable of associating with different species of viral structural proteins through a common mechanism.
19345973 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19344514 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19343218 investigated APOBEC3G mutation footprints in HIV-1 evolution & potential risk for known drug resistance from sublethal G-to-A mutations; we detected evolutionary APOBEC3G mutation footprints in the HIV-1 genome
19324886 Nef7.A3G can effectively restrict HIV infection and replication by restoring the virion incorporation of A3G, even in the presence of Vif.
19304304 Cytidine deamination is the mechanism by which APOBEC3G restricts HIV-1.
19304304 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19300495 our results do not support a role for APOBEC3G in restriction of HIV-1 in quiescent CD4+ T-cells
19297501 A pyrimidine at nucleotide 200 in the untranslated leader region contributed to resistance by increasing virus particle production, which resulted in fewer APOBEC3G molecules per particle
19266078 tyr-124 & trp-127 in the N-terminal CDA domain mediate A3G oligomerization; this coincides with packaging into HIV-1 virions; propose occupation of positively charged pocket by RNA promotes A3G oligomerization, packaging into virions & antiviral function
19254362 The results suggest that exposure to HIV may trigger APOBEC3G expression in PBMCs, in the absence of infection.
19216784 the HIV-1 Vif mutant was severely defective in an APOBEC3G-expressing T cell line and exhibited a significant delay in replication kinetics
19216784 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19211937 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19197360 results demonstrate that physiological regulation of APOBEC3G does restrict vif-positive HIV-1, as well as vif-negative HIV-1
19169351 analysis of genetic editing of HBV DNA by monodomain human APOBEC3G and F cytidine deaminases
19153609 analysis of the enzymatic reaction of wild-type APOBEC3G
19149995 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19149577 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19136562 Dissecting APOBEC3G substrate specificity by nucleoside analog interference.
19128510 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19109396 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19088851 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19057663 study finds that although reverse transcription initiates in the presence of APOBEC3G (A3G), elongation of the cDNA product is impeded; data support the model that A3G reduces HIV-1 cDNA levels by inhibiting synthesis rather than by inducing degradation
19057663 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19050398 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19038776 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19036809 The authors found that the APOBEC3G domain that interacts with the Vif YRHHY region is located between amino acids 126 and 132 of A3G, which is consistent with the conclusions reported in previous studies.
19036809 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19027180 There is intracellular expression and regulation of functional APOBEC3G in the neuronal cells, which may be one of innate defense mechanisms involved in the neuronal protection in the CNS.
19020832 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19008196 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19004943 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
19004939 The results suggest that HIV-1 Vif preferentially induces degradation of newly synthesized APOBEC3G but indiscriminately inhibits encapsidation of "old" and "new" APOBEC3G.
19004939 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18987139 enzymatic activity of encapsidated APOBEC3G does not correlate with the observed limited cytidine deamination in HIV-1 DNA, suggesting that APOBEC3G-laden exosomes restrict HIV-1 through a nonenzymatic mechanism.
18987139 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18976920 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18976462 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18971252 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18851679 Thus, hA3G might be restricting viral growth in infected individuals through a mechanism that is independent of the cytidine deaminase activities of hA3G.
18849968 high-resolution crystal structure of the carboxy-terminal deaminase domain of APOBEC3G (APOBEC3G-CD2)
18846074 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18843993 There was difference found in the hA3G mRNA levels of four groups in the HIV popular area in central China and hA3G mRNA levels of HIV long term nonprogressors as well as in HIV slow progressors were found.
18842592 N-terminal domains of hA3G were unable to multimerize but remained functional for Gag and viral infectivity factor (Vif) interactions when expressed apart from the C terminus.
18836454 These data imply that protein kinase A-mediated phosphorylation of APOBEC3G can regulate the interaction between APOBEC3G and Vif.
18836454 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18827027 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18819469 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18809921 These data indicate that NF-IL6 is a natural inhibitor of APOBEC3G that facilitates HIV-1 replication.
18809921 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18806783 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18789977 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18684817 Results show that the prolyl isomerase Pin1 modulates APOBEC3G expression.
18680593 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18675436 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18667511 two regions of APOBEC3G combine to mediate an intermolecular interaction that controls subcellular localization
18652534 No genetic H186R polymorphism in exon 4 of APOBEC3G gene is found and therefore neither neither associated with differential susceptibility to HIV-1 infection/progression among North Indians.
18647522 Of the 5 SNPs studied, none were associated with persistant HBV infection. However, the rs8177832 polymorphism may be involved in inhibiting HBV replication.
18639915 Here, the authors demonstrate that the ability to bind to Gag and package into HIV-1 virions is entirely contained within the amino-terminal half of A3G.
18639915 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18619467 A VxIPLx(4-5)LxPhix(2)YWxL motif in HIV-1 Vif is identified, which is required for efficient interaction between Vif and APOBEC3G (A3G), Vif-mediated A3G degradation and virion exclusion, and functional suppression of the A3G antiviral activity.
18619467 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18604271 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18603011 results here have indicated that at least two distinct regions in the N-terminal half of HIV-1 Vif are critical for binding and exclusion of APOBEC3G/F
18603011 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18597676 The binding of APOBEC3G to 7SL RNA through its Alu domain suggests a mechanism for APOBEC-mediated inhibition of Alu retrotransposition. However 7SL RNA is not essential for the HIV-1 virion recruitment of the antiviral cytidine deaminase.
18577210 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18572219 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18541215 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18501607 APOBEC3G-expressing T cells were infected with Vif-deficient HIV-1. Resistance occurred by a novel tolerance mechanism.
18501607 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18499212 Vif binds APOBEC3G (A3G) and a Cullin5-ElonginBC E3 ubiquitin ligase complex which results in the proteasomal degradation of A3G. Failure of a Vif mutant to bind A3G resulted in A3G incorporation into assembling virions with loss of viral infectivity.
18499212 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18495196 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18480459 The paper provides evidence that the N-terminal domain of APOBEC3G is required for packaging into HBV nucleocapsids.
18456846 RNA binding by APOBEC3G is key for initiation of APOBEC3G:nucleocapsid complex formation in vitro.
18456846 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18448538 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18420796 These results indicate that APOBEC3G, APOBEC3C and APOBEC3H have the ability to edit HBV DNA and that each protein is likely to contribute to various degrees to the generation of modified genomes in human liver cells.
18414697 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18414671 Vpr14-88-Apobec3G fusion protein is efficiently incorporated into Vif-positive HIV-1 particles and inhibits viral infection
18414671 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18391217 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18367521 define a number of subtle differences between the ribonucleoprotein complexes associated with APOBEC3F and APOBEC3G and speculate
18366335 Study presents recent advances detailing the mechanisms of the Vif-Apobec3G regulatory circuit.
18366335 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18362149 diverse A3G oligomerization modes contribute to the human immunodeficiency virus, type 1, proviral DNA mutational bias
18338854 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18326044 polyubiquitylated Vif might serve as a vehicle to transport APOBEC3G into proteasomes for degradation
18326044 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18308358 APOBEC3G has important restriction activity in the cytoplasm and progressively diminishes viral cytoplasmic and nuclear cDNA forms with increasing magnitude during restriction.
18304004 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18298807 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18288108 solution structure of the human APOBEC3G catalytic domain
18272764 Our data indicate that plasmacytoid dendritic cells are protected by an IFN-alpha mediated upregulation of APOBEC3G type of innate immunity from HIV-1 infection.
18262674 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18184715 absolute requirement for the catalytic glutamate of APOBEC3G in Ty1, MusD, and HIV-1 restriction strongly indicates that DNA cytosine deamination is an essential part of the mechanism
18184715 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18165230 CRS enables hA3G to interact with cytoplasmic factors, and thereby enables hA3G to serve in host cell defense by restricting an antiviral sentinel to the cytoplasm.
18077705 enhanced APOBEC3 activity alone cannot explain the ability of elite suppressors to control viremia
18036235 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
18023836 Our results expose a novel function of Vif that promotes the assembly of APO3G into presumably packaging-incompetent high moelcular mass complexes.
18023836 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17959647 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17942420 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17928335 We conclude that efficient inhibition of vif-defective human immunodeficiency virus type 1 requires catalytically active APO3G.
17928335 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17916373 Inhibition of hA3G degradation by the C-terminal hA3G fragment 157-384 appears to be related to its ability to prevent the polyubiquitination of hA3G induced by Vif, a process that is required for Vif-mediated proteosomal degradation of hA3G.
17916373 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17898068 Cell-based binding assays confirmed these results and demonstrated that residues 40 to 71 in the N terminus of Vif contain a nonlinear binding site for APOBEC3G.
17898068 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17892323 T cells, unlike epithelial-derived cell lines, express an unidentified RNase-resistant factor that inhibits APOBEC3G (A3G) deaminase activity.
17886715 The localization of the expressed GFP-APOBEC3G was observed in the cytoplasm of CD4+ HeLa cells.
17881443 7SL RNA that is encapsidated into diverse retroviruses is a key cofactor of the antiviral APOBEC3G.
17881443 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17869271 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17869248 corroborated an APOBEC2-based structural model for the catalytic domain of APOBEC3G indicating that most non-essential residues are solvent accessible and most essential residues cluster within the protein core
17855362 This report demonstrates that the reduction of late viral DNA synthesis is due to the inhibition by human APOBEC3G of the strand transfer steps that occur during reverse transcription.
17849022 these data constitute the first proof-of-principle demonstration that APOBEC3 proteins can be used to fortify the innate anti-viral defenses of cells to prevent the zoonotic transmission of an endogenous retrovirus
17848567 the major cellular function of A3G, in addition to inhibiting the mobility of retrotransposons and replication of endogenous retroviruses, is most likely to prevent the decay of miRNA-targeted mRNA in processing bodies
17825339 intracellular degradation of APO3G may not be the sole activity of Vif required for the production of infectious virions from APO3G-expressing cells
17825339 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17824250 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17727729 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17670826 interaction of APOBEC3G with HIV1gp2 nucleocapsid is required for the inhibition of reverse transcription initiation
17670826 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17631688 RNAs tested in this study were packaged into viruses or virus-like particles we failed to identify a correlation between APO3G encapsidation and the packaging of these cellular RNAs.
17631688 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17609216 Vif binding to RNA and DNA offers several non-exclusive ways to counteract APOBEC3G/3F factors, in addition to the well documented Vif-induced degradation by the proteasome and to the Vif-mediated repression of translation of these antiviral factors
17586316 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17522216 Results reveal two distinct Vif determinants, amino acids Y(40)RHHY(44) and D(14)RMR(17), which are essential for binding to APOBEC3G and APOBEC3F, respectively.
17522216 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17522211 These results demonstrate that targeting of APO3G to proteasome degradation and interference with viral encapsidation are distinct functional properties of Vif.
17522211 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17517765 A GC-box of the human APOBEC3G gene represents a binding site for the ubiquitous transcription factors specificity protein (Sp) 1 and Sp3.
17459442 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17440614 structure model identifies a cluster of residues important for packaging of APOBEC3G into virions, and may serve to guide functional analysis of APOBEC3G
17428847 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17374143 investigation of possible anti-HIV activity of hA3G (APOBEC3G); hA3G mRNA levels follow a hierarchical order of long-term nonprogressors>HIV-uninfected>Progressors; hA3G mRNA abundance correlates with surrogates of HIV disease progression
17344295 our results indicate that APOBEC3G multimerizes in an RNA-dependent fashion and that RNA-APOBEC3G multimers are recruited to the plasma membrane and subsequently into virion particles by Gag.
17344295 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17338854 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17331040 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17314171 The inhibitory effect of APOBEC3 proteins on Hepatits B virus replication is mainly at the DNA level at very early stages during viral reverse transcription, with only a minor effect on viral RNA packaging.
17303427 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17291161 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17272283 the degradation of APOBEC3G-edited viral DNA mediated by virion-associated UNG2 and APE during or after reverse transcription could be partially responsible for the potent anti-HIV-1 effect by APOBEC3G in the absence of vif
17267497 we confirm the central role played by the aspartic acid at position 128 and identify proline 129 and aspartic acid 130 as important contributory residues for interaction with HIV-1 Vif.
17267497 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17259974 mouse A3-containing and human A3G-containing virions showed a marked decrease in titre
17251560 Our results suggest that APOBEC3G, upregulated by IFNs, has a dual effect on HBV: induction of hypermutation and reduction of virus synthesis.
17237417 Ligation of cell surface CCR5 receptors by CCL3 or CD40 by CD40L activated the ERK1/2 and p38 MAPK signaling pathways that induced APOBEC3G mRNA expression and production of the APOBEC3G protein
17212712 Expression upregulated by inflammatory cytokines, such as interferon, interleukin-6, and tumor necrosis factor.
17166910 APOBEC3G associates with RNPs that are found throughout the cytosol as well as in discrete microdomains.
17161027 cytoplasmically expressed DNA deaminase APOBEC3G acts in a processive manner, possibly suggesting that evolutionary pressure has altered the ability of DNA deaminases to act in a processive or distributive manner, depending on the physiological need
17145955 Findings highlight a role for APOBEC3G/3F in explaining the resistance of most dendritic cells to HIV-1 infection, as well as the susceptibility of a fraction of immature dendritic cells.
17142455 APOBEC3F and APOBEC3G complexes undergo dynamic conversion during HIV-1 infection
17135358 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17126871 it is concluded that approximately 7 (+/-4) molecules of A3G are incorporated into Deltavif HIV-1 virions produced from PBMCs; results indicate that virion incorporation of only a few molecules of A3G is sufficient to inhibit HIV-1 replication
17126871 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17079235 presents low resolution structures of hA3G in HMM and LMM forms determined by small angle x-ray scattering and advanced shape reconstruction methods
17079095 APOBEC3G selectively inhibits Alu retrotransposition in an ORF1p-independent manner. An active cytidine deaminase site is not required for the inhibition of Alu retrotransposition and the resultant integration events lack G to A or C to T hypermutation.
17067930 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17064466 APOBEC3G suppresses hepatitis B virus and duck hepatitis B virus replication and also suppresses HBsAg and HBeAg expression.
17052331 data indicate that APOBEC3G is not a restriction factor for vaccinia virus replication nor is vaccinia virus able to degrade APOBEC3G
17049578 These findings support APOBEC3G degradation as a requirement for HIV-1 Vif function.
17049578 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17036163 We demonstrated an increased expression of APOBEC3G in both hepatocytes and lymphocytes of chronic hepatitis patients infected with HCV.
17030807 Data identify nonautonomous Alu and hY retroelements as cellular targets of APOBEC3G (A3G) and suggest how different forms of A3G protect cells from exogenous retroviruses (LMM A3G) and endogenous retroelements (HMM A3G).
17023652 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
17020885 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
16988524 Observational study of gene-disease association. (HuGE Navigator)
16988524 might be a role for APOBEC3G in susceptibility to HIV-1 infection
16971427 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
16940537 APOBEC3G-induced HIV-1 hypermutation represents a potent host antiviral factor in vivo
16940537 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
16887808 APOBEC3G binds HIV-1 RNA and messenger RNAs that shuttle between polysomes and stress granules
16874860 These findings indicate that APOBEC3G could suppress HBV replication and antigen expression both in vivo and in vitro, promising an advance in treatment of HBV infection.
16822376 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
16731938 molecular analysis of the deaminase and nucleic acid binding activities of human APOBEC3G
16699599 novel link between innate immunity against retroviruses and P-bodies suggesting that APOBEC3G and APOBEC3F could function in the context of P-bodies to restrict HIV-1 replication.
16699599 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
16678488 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
16641889 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
16641260 results provide novel insights into the catalytic function and antiviral property of APOBEC3G
16631224 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
16622407 G --> A mutational gradient generated in viral genomic DNA in vivo could result from an intrinsic processive directional attack by APOBEC3G on single-stranded cDNA
16501124 Most of the highly conserved tryptophan residues were required for efficient suppression of both APOBEC3G (A3G) and APOBEC3F (A3F), but some of these residues were selectively required for the suppression of A3F but not A3G.
16501124 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
16460778 APOBEC3F was less potent than APOBEC3G in inhibitinhg HIV-1; Vif proteins appeared more potent & specific when APOBEC3G is the target rather than APOBEC3F
16460778 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
16426578 APOBEC3G is induced by IFN stimulation in human hepatocytes and thus could be involved in host defense mechanisms directed against hepatitis viruses
16418394 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
16414984 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
16354571 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
16303161 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
16250885 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
16000409 APOBEC3G hypermutates genomic DNA and inhibits Ty1 retrotransposition in yeast.
15943885 APOBEC3G is incorporated into HTLV-1 virions and inhibits the infection of HTLV-1 through different mechanisms from that on HIV-1
15823539 APOBEC3G potently inhibits replication of the Ty1 LTR retrotransposon in yeast.
15781449 the E3 ubiquitin ligase activity of the Vif-BC-Cul5 complex is essential for Vif function against APOBEC3G
15721369 Using APOBEC3G deletion and point mutants, we mapped the encapsidation determinant to the Zn(2+) coordination residues of the N-terminal catalytic domain (CD1).
15674295 APOBEC3G, by editing viral genetic material, provides an ancestral wide cellular defence against endogenous and exogenous invaders
15647250 only the C-terminal domain of APOBEC3F and -3G dictates the retroviral minus strand 5'-TC and 5'-CC dinucleotide hypermutation preferences.
15613310 Functional analysis of Vif protein shows less restriction of human immunodeficiency virus type 2 by APOBEC3G.
15611076 Induces degradation of APOBEC3G by bringing to relevance that deaminase inhibition can also result from a direct interaction with Vif protein.
15611076 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15609224 Observational study of gene-disease association. (HuGE Navigator)
15581898 ubiquitination of APOBEC3G by Nedd4-1 favors its targeting to the virus assembly site where APOBEC3G interacts with Gag and is packaged into HIV-1 particles in the absence of Vif
15578976 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15574592 Vif targets APOBEC3G for degradation by forming an SCF-like E3 ubiquitin ligase containing Cullin 5 and Elongins B and C (Cul5-EloB-EloC) through a novel SOCS-box
15537645 cytoplasmic Vif-APOBEC3G interactions are required but are not sufficient for Vif to modulate APOBEC3G and can be monitored by co-localization in vivo
15537645 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15479846 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15479826 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15464836 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15452227 Observational study of gene-disease association. (HuGE Navigator)
15383144 Depletion of APOBEC3G is not the sole protective mechanism of Vif and additional mechanisms exerted by this protein can be envisioned which counteract APOBEC3G and enhance HIV infectivity.
15383144 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15373943 Depletion of APOBEC3G from Vif expressing cells is not a universal property of Vif and thus is not imperative for the production of infectious virions.
15373943 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15358144 Results demonstrate that the expression of HIV-1 Gag is sufficient to induce the packaging of human APOBEC3G into Gag particles.
15358144 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15353294 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15297452 expression of the antiviral APOBEC3G editing enzyme is dynamically controlled by the PKCalpha/betaI/MEK/ERK protein kinase cascade in human T lymphocytes
15286366 observations allow speculation (i) that APOBEC-mediated C-to-U editing may contribute to the sequence variation of viruses that replicate entirely through RNA, and (ii) that additional cellular RNA substrates might exist for the APOBEC enzymes
15269786 APOBEC3G gene has been subject to strong positive selection throughout the history of primate evolution
15245742 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15215254 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15210704 APOBEC3G interactions with HIV-1 and nonviral RNAs that are packaged into viral particles are sufficient for APOBEC3G virion incorporation
15177194 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15168739 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15159405 cytoplasmic apolipoprotein B mRNA editing enzyme(APOBEC3G) becomes membrane-bound in cells expressing HIV-1 Gag, and its incorporation into Gag viral-like particles (VLPs) is proportional to the amount of APOBEC3G expressed in the cell
15159405 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15156567 APOBEC3G inhibits HIV-1 infection through interference with reverse transcription.
15156567 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15116720 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15080177 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15054139 A single amino acid substitution mutant of human APOBEC3G (D128K) can interact with HIV-1 Vif but is not depleted from cells; thus, it inhibits HIV-1 replication in an HIV-1 Vif-resistant manner.
15054139 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
15031497 inhibits hepatitis B virus replication; block of HBV DNA accumulation by APOBEC3G seems to result from an inhibition of viral pregenomic RNA packaging
14999100 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
14978281 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
14966139 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
14747572 HIV-1 Vif could induce rapid degradation of human APOBEC3G that was blocked by the proteasome inhibitor MG132. The efficiency of Vif-induced downregulation of APOBEC3G expression depended on the level of Vif expression.
14747572 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
14672928 results suggest that Vif functions by targeting APOBEC3G for degradation via the ubiquitin-proteasome pathway and implicate the proteasome as a site of dynamic interplay between microbial and cellular defenses.
14672928 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
14614829 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
14564014 ability of HIV-1 Vif to suppress antiviral activity of APOBEC3G was specifically dependent on Cul5-SCF function, allowing Vif to interact with APOBEC3G and induce its ubiquitination and degradation
14564014 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
14557625 Vif inhibits packaging of APOBEC3G into virus particles in a dose-dependent manner and reduces its intracellular expression level.
14557625 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
14528301 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
14528300 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
14527406 Viral infectivity factor prevents virion incorporation of endogenous APOBEC3G by effectively depleting the intracellular levels of this enzyme in HIV-1-infected T cells.
14527406 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
12970355 mutagenesis analysis on two cytidine deaminase motifs in CEM15/Apobec-3G indicates that the enzymatic activity of this protein is essential but not a sole determinant of the HIV-1 antiviral activity
12970355 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
12920286 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
12914693 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
12859895 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
12840737 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
12830140 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
12809610 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
12808466 APOBEC3G exerts its antiviral effect during reverse transcription to trigger G-to-A hypermutation in the nascent HIV DNA
12808466 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
12808465 a cytidine deaminase that is able to induce G to A hypermutation in newly synthesized HIV-1 DNA
12808465 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
12750511 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
12719574 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
12167863 Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein.
12167863 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
9846577 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay
9811770 HIV-1 Vif interacts with APOBEC3G as demonstrated by co-immunoprecipitation assay

AA Sequence

MKPHFRNTVERMYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPPLDAKIFRGQVYSELKYHPEMRF      1 - 70
FHWFSKWRKLHRDQEYEVTWYISWSPCTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQ     71 - 140
KRDGPRATMKIMNYDEFQHCWSKFVYSQRELFEPWNNLPKYYILLHIMLGEILRHSMDPPTFTFNFNNEP    141 - 210
WVRGRHETYLCYEVERMHNDTWVLLNQRRGFLCNQAPHKHGFLEGRHAELCFLDVIPFWKLDLDQDYRVT    211 - 280
CFTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIYDDQGRCQEGLRTLAEAGAKISIMTYSEFKHCWDTF    281 - 350
VDHQGCPFQPWDGLDEHSQDLSGRLRAILQNQEN                                        351 - 384
//

Text Mined References (348)

PMID Year Title
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26772882 2016 Basal transcription of APOBEC3G is regulated by USF1 gene in hepatocyte.
26741797 2016 APOBEC3G Variants and Protection against HIV-1 Infection in Burkina Faso.
26668372 2015 Specific induction of endogenous viral restriction factors using CRISPR/Cas-derived transcriptional activators.
26503602 2015 APOBEC3G Interacts with ssDNA by Two Modes: AFM Studies.
26482266 2016 Contribution of APOBEC3G/F activity to the development of low-abundance drug-resistant human immunodeficiency virus type 1 variants.
26424853 2015 RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates.
26275799 2015 Pokeweed antiviral protein restores levels of cellular APOBEC3G during HIV-1 infection by depurinating Vif mRNA.
26178819 2015 The virus-induced protein APOBEC3G inhibits anoikis by activation of Akt kinase in pancreatic cancer cells.
26105074 2015 The HDAC6/APOBEC3G complex regulates HIV-1 infectiveness by inducing Vif autophagic degradation.
26055363 2015 Incomplete APOBEC3G/F Neutralization by HIV-1 Vif Mutants Facilitates the Genetic Evolution from CCR5 to CXCR4 Usage.
26048885 2015 Comparative analysis of the gene-inactivating potential of retroviral restriction factors APOBEC3F and APOBEC3G.
26016442 2015 Differential sensitivity of porcine endogenous retrovirus to APOBEC3-mediated inhibition.
25985400 2015 High level of APOBEC3F/3G editing in HIV-2 DNA vif and pol sequences from antiretroviral-naive patients.
25984970 2015 Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G.
25974865 2015 RNA-binding residues in the N-terminus of APOBEC3G influence its DNA sequence specificity and retrovirus restriction efficiency.
25811715 2015 Host APOBEC3G protein inhibits HCV replication through direct binding at NS3.
25717111 2015 Anti-APOBEC3G activity of HIV-1 Vif protein is attenuated in elite controllers.
25590131 2015 Promiscuous RNA binding ensures effective encapsidation of APOBEC3 proteins by HIV-1.
25501566 2015 APOBEC3 enzymes restrict marginal zone B cells.
25384438 2015 Human endogenous retrovirus expression is inversely related with the up-regulation of interferon-inducible genes in the skin of patients with lichen planus.
25304135 2014 HIV-1 Vif inhibits G to A hypermutations catalyzed by virus-encapsidated APOBEC3G to maintain HIV-1 infectivity.
25200749 2015 The HIV-1 accessory protein Vpr induces the degradation of the anti-HIV-1 agent APOBEC3G through a VprBP-mediated proteasomal pathway.
25196417 2015 Potential roles of placental human beta-defensin-3 and apolipoprotein B mRNA-editing enzyme catalytic polypeptide 3G in prevention of intrauterine transmission of hepatitis B virus.
25169827 2014 A functional conserved intronic G run in HIV-1 intron 3 is critical to counteract APOBEC3G-mediated host restriction.
25080100 2014 Human APOBEC3 induced mutation of human immunodeficiency virus type-1 contributes to adaptation and evolution in natural infection.
24942576 2014 HIV-1 and HIV-2 Vif interact with human APOBEC3 proteins using completely different determinants.
24851906 2014 Different modes of retrovirus restriction by human APOBEC3A and APOBEC3G in vivo.
24722422 2014 Positioning of APOBEC3G/F mutational hotspots in the human immunodeficiency virus genome favors reduced recognition by CD8+ T cells.
24651717 2014 Different mutagenic potential of HIV-1 restriction factors APOBEC3G and APOBEC3F is determined by distinct single-stranded DNA scanning mechanisms.
24623435 2014 Quantification of deaminase activity-dependent and -independent restriction of HIV-1 replication mediated by APOBEC3F and APOBEC3G through experimental-mathematical investigation.
24586139 2014 A novel Bayesian method for detection of APOBEC3-mediated hypermutation and its application to zoonotic transmission of simian foamy viruses.
24553842 2014 Interleukin-32 isoforms: expression, interaction with interferon-regulated genes and clinical significance in chronically HIV-1-infected patients.
24522927 2014 CBF? enhances de novo protein biosynthesis of its binding partners HIV-1 Vif and RUNX1 and potentiates the Vif-induced degradation of APOBEC3G.
24500029 2014 APOBEC3G exerts tumor suppressive effects in human hepatocellular carcinoma.
24498164 2014 Insights into the motif preference of APOBEC3 enzymes.
24478136 2014 Quantitative analysis of location- and sequence-dependent deamination by APOBEC3G using real-time NMR spectroscopy.
24422669 2014 HIV-1 Vif N-terminal motif is required for recruitment of Cul5 to suppress APOBEC3.
24367644 2013 APOBEC3G oligomerization is associated with the inhibition of both Alu and LINE-1 retrotransposition.
24345943 2014 Oligomerization transforms human APOBEC3G from an efficient enzyme to a slowly dissociating nucleic acid-binding protein.
24227842 2014 APOBEC3 deaminases induce hypermutation in human papillomavirus 16 DNA upon beta interferon stimulation.
24198285 2013 GANP interacts with APOBEC3G and facilitates its encapsidation into the virions to reduce HIV-1 infectivity.
24185281 2013 Structural determinants of HIV-1 Vif susceptibility and DNA binding in APOBEC3F.
24146808 2013 Lower HIV provirus levels are associated with more APOBEC3G protein in blood resting memory CD4+ T lymphocytes of controllers in vivo.
24098356 2013 The roles of APOBEC3G complexes in the incorporation of APOBEC3G into HIV-1.
24098115 2013 APOBEC3G polymorphism as a selective barrier to cross-species transmission and emergence of pathogenic SIV and AIDS in a primate host.
24055458 2013 Atomic force microscopy studies of APOBEC3G oligomerization and dynamics.
24010642 2013 Polymorphic APOBEC3 modulates chronic hepatitis B in Moroccan population.
23986590 2013 Vif proteins from diverse primate lentiviral lineages use the same binding site in APOBEC3G.
23926332 2013 Mov10 and APOBEC3G localization to processing bodies is not required for virion incorporation and antiviral activity.
23890083 2013 APOBEC3 inhibits DEAD-END function to regulate microRNA activity.
23787464 2013 Structural features of antiviral DNA cytidine deaminases.
23760237 2013 Prototype foamy virus Bet impairs the dimerization and cytosolic solubility of human APOBEC3G.
23717565 2013 Retroviral restriction factor APOBEC3G delays the initiation of DNA synthesis by HIV-1 reverse transcriptase.
23707381 2013 A naturally occurring Vif mutant (I107T) attenuates anti-APOBEC3G activity and HIV-1 replication.
23696735 2013 Uracil DNA glycosylase counteracts APOBEC3G-induced hypermutation of hepatitis B viral genomes: excision repair of covalently closed circular DNA.
23640893 2013 Interleukin-2 inhibits HIV-1 replication in some human T cell lymphotrophic virus-1-infected cell lines via the induction and incorporation of APOBEC3G into the virion.
23598277 2013 APOBEC3 cytidine deaminases in double-strand DNA break repair and cancer promotion.
23596292 2013 Impact of H216 on the DNA binding and catalytic activities of the HIV restriction factor APOBEC3G.
23576497 2013 APOBEC3G impairs the multimerization of the HIV-1 Vif protein in living cells.
23555255 2013 HIV restriction by APOBEC3 in humanized mice.
23536679 2013 T cells target APOBEC3 proteins in human immunodeficiency virus type 1-infected humans and simian immunodeficiency virus-infected Indian rhesus macaques.
23432984 2012 The potential role of APOBEC3G in limiting replication of hepatitis B virus.
23411593 2013 A common deletion in the APOBEC3 genes and breast cancer risk.
23318957 2013 Dispersed sites of HIV Vif-dependent polyubiquitination in the DNA deaminase APOBEC3F.
23316055 2013 HIV-1 viral infectivity factor (Vif) alters processive single-stranded DNA scanning of the retroviral restriction factor APOBEC3G.
23152537 2013 Suppression of HIV-1 infection by APOBEC3 proteins in primary human CD4(+) T cells is associated with inhibition of processive reverse transcription as well as excessive cytidine deamination.
23138837 2013 Genetic variants in the host restriction factor APOBEC3G are associated with HIV-1-related disease progression and central nervous system impairment in children.
23128233 2012 Host-microbe interactions have shaped the genetic architecture of inflammatory bowel disease.
23097438 2013 APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and APOBEC3DE in human primary CD4+ T cells and macrophages.
22999946 2012 Intrinsic cellular defenses against human immunodeficiency viruses.
22970171 2012 Random mutagenesis MAPPIT analysis identifies binding sites for Vif and Gag in both cytidine deaminase domains of Apobec3G.
22915799 2012 HIV-1 replication and APOBEC3 antiviral activity are not regulated by P bodies.
22912627 2012 Retroelements versus APOBEC3 family members: No great escape from the magnificent seven.
22894923 2012 Interaction of human immunodeficiency virus type 1 Vif with APOBEC3G is not dependent on serine/threonine phosphorylation status.
22828015 2012 Moloney murine leukemia virus glyco-gag facilitates xenotropic murine leukemia virus-related virus replication through human APOBEC3-independent mechanisms.
22809226 2012 Nanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA.
22807680 2012 Endogenous origins of HIV-1 G-to-A hypermutation and restriction in the nonpermissive T cell line CEM2n.
22791714 2012 APOBEC3G inhibits microRNA-mediated repression of translation by interfering with the interaction between Argonaute-2 and MOV10.
22787460 2012 Antiviral Mechanism and Biochemical Basis of the Human APOBEC3 Family.
22695298 2012 E138K and M184I mutations in HIV-1 reverse transcriptase coemerge as a result of APOBEC3 editing in the absence of drug exposure.
22645179 2012 APOBEC3G enhances lymphoma cell radioresistance by promoting cytidine deaminase-dependent DNA repair.
22579353 2012 APOBEC3G expression and hypermutation are inversely associated with human immunodeficiency virus type 1 (HIV-1) burden in vivo.
22546055 2012 Emerging complexities of APOBEC3G action on immunity and viral fitness during HIV infection and treatment.
22362763 2012 Single-stranded DNA scanning and deamination by APOBEC3G cytidine deaminase at single molecule resolution.
22346743 2012 Multi-scale modeling of HIV infection in vitro and APOBEC3G-based anti-retroviral therapy.
22339232 2012 APOBEC2 is a monomer in solution: implications for APOBEC3G models.
22315404 2012 Role of retroviral restriction factors in the interferon-?-mediated suppression of HIV-1 in vivo.
22301159 2012 The cellular antiviral protein APOBEC3G interacts with HIV-1 reverse transcriptase and inhibits its function during viral replication.
22272271 2012 Evolution of the primate APOBEC3A cytidine deaminase gene and identification of related coding regions.
22205746 2012 Vif proteins of human and simian immunodeficiency viruses require cellular CBF? to degrade APOBEC3 restriction factors.
22190037 2011 Vif hijacks CBF-? to degrade APOBEC3G and promote HIV-1 infection.
22181350 2012 First-in-class small molecule inhibitors of the single-strand DNA cytosine deaminase APOBEC3G.
22152111 2011 Downregulation of APOBEC3G by xenotropic murine leukemia-virus related virus (XMRV) in prostate cancer cells.
22013041 2012 The activity spectrum of Vif from multiple HIV-1 subtypes against APOBEC3G, APOBEC3F, and APOBEC3H.
22001110 2012 Functions and regulation of the APOBEC family of proteins.
21985787 2011 APOBEC3G promotes liver metastasis in an orthotopic mouse model of colorectal cancer and predicts human hepatic metastasis.
21935481 2011 Replication protein A (RPA) hampers the processive action of APOBEC3G cytosine deaminase on single-stranded DNA.
21897871 2011 Expression of APOBEC3G/3F and G-to-A hypermutation levels in HIV-1-infected children with different profiles of disease progression.
21874023 2011 The antiviral factor APOBEC3G enhances the recognition of HIV-infected primary T cells by natural killer cells.
21856286 2011 Direct evidence that RNA inhibits APOBEC3G ssDNA cytidine deaminase activity.
21835787 2011 Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a conserved capacity to restrict Vif-deficient HIV-1.
21784078 2011 Intracellular detection of differential APOBEC3G, TRIM5alpha, and LEDGF/p75 protein expression in peripheral blood by flow cytometry.
21763507 2011 Multifaceted counter-APOBEC3G mechanisms employed by HIV-1 Vif.
21752914 2011 APOBEC3G complexes decrease human immunodeficiency virus type 1 production.
21737457 2011 Deaminase activity on single-stranded DNA (ssDNA) occurs in vitro when APOBEC3G cytidine deaminase forms homotetramers and higher-order complexes.
21698207 2011 Exposure to apoptotic activated CD4+ T cells induces maturation and APOBEC3G-mediated inhibition of HIV-1 infection in dendritic cells.
21659520 2011 Phosphorylation directly regulates the intrinsic DNA cytidine deaminase activity of activation-induced deaminase and APOBEC3G protein.
21573951 2012 APOBEC3G/F as one possible driving force for co-receptor switch of the human immunodeficiency virus-1.
21571098 2011 Effect of HIV-1 Vif variability on progression to pediatric AIDS and its association with APOBEC3G and CUL5 polymorphisms.
21489586 2011 Functional analysis of the two cytidine deaminase domains in APOBEC3G.
21480314 2011 Host apolipoprotein B messenger RNA-editing enzyme catalytic polypeptide-like 3G is an innate defensive factor and drug target against hepatitis C virus.
21396348 2011 Repression of porcine endogenous retrovirus infection by human APOBEC3 proteins.
21300806 2011 Intensity of deoxycytidine deamination of HIV-1 proviral DNA by the retroviral restriction factor APOBEC3G is mediated by the noncatalytic domain.
21239176 2011 APOBEC3G: a double agent in defense.
21228271 2011 Heat shock protein 70 inhibits HIV-1 Vif-mediated ubiquitination and degradation of APOBEC3G.
21217078 2011 The nerve growth factor reduces APOBEC3G synthesis and enhances HIV-1 transcription and replication in human primary macrophages.
21182427 2011 Characterization of anti-HIV activity mediated by R88-APOBEC3G mutant fusion proteins in CD4+ T cells, peripheral blood mononuclear cells, and macrophages.
21123384 2011 Structure-function analyses point to a polynucleotide-accommodating groove essential for APOBEC3A restriction activities.
21123176 2011 Atomic force microscopy studies provide direct evidence for dimerization of the HIV restriction factor APOBEC3G.
21078663 2011 NFAT and IRF proteins regulate transcription of the anti-HIV gene, APOBEC3G.
20874421 2011 Loci polymorphisms of the APOBEC3G gene in HIV type 1-infected Brazilians.
20844042 2010 The HIV-1 central polypurine tract functions as a second line of defense against APOBEC3G/F.
20833716 2010 Differential anti-APOBEC3G activity of HIV-1 Vif proteins derived from different subtypes.
20668529 2010 Apobec 3G efficiently reduces infectivity of the human exogenous gammaretrovirus XMRV.
20642434 2010 Regulation of HIV-1 infection in cells derived from purified CD34+ cells through manipulation of APOBEC3G expression.
20636339 2010 A critical function of toll-like receptor-3 in the induction of anti-human immunodeficiency virus activities in macrophages.
20610708 2010 Remarkable lethal G-to-A mutations in vif-proficient HIV-1 provirus by individual APOBEC3 proteins in humanized mice.
20592083 2010 Identification of a critical T(Q/D/E)x5ADx2(I/L) motif from primate lentivirus Vif proteins that regulate APOBEC3G and APOBEC3F neutralizing activity.
20523896 2010 Massive APOBEC3 editing of hepatitis B viral DNA in cirrhosis.
20510315 2010 APOBEC3G directly binds Hepatitis B virus core protein in cell and cell free systems.
20463080 2010 APOBEC3G contributes to HIV-1 variation through sublethal mutagenesis.
20463074 2010 APOBEC3G generates nonsense mutations in human T-cell leukemia virus type 1 proviral genomes in vivo.
20363737 2010 Small molecular compounds inhibit HIV-1 replication through specifically stabilizing APOBEC3G.
20338830 2010 Determinants of sequence-specificity within human AID and APOBEC3G.
20335268 2010 Identification of 81LGxGxxIxW89 and 171EDRW174 domains from human immunodeficiency virus type 1 Vif that regulate APOBEC3G and APOBEC3F neutralizing activity.
20335265 2010 Inhibition of xenotropic murine leukemia virus-related virus by APOBEC3 proteins and antiviral drugs.
20308164 2010 Quantitative profiling of the full APOBEC3 mRNA repertoire in lymphocytes and tissues: implications for HIV-1 restriction.
20219927 2010 APOBEC3F and APOBEC3G inhibit HIV-1 DNA integration by different mechanisms.
20212048 2010 Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G.
20153011 2010 Inhibition of LINE-1 and Alu retrotransposition by exosomes encapsidating APOBEC3G and APOBEC3F.
20152150 2010 Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfaces.
20147392 2010 Polyubiquitination of APOBEC3G is essential for its degradation by HIV-1 Vif.
20128960 2010 [Expression and subcellular localization of APOBEC3G in peripheral blood mononuclear cells and liver tissues of chronic HBV patients].
20104108 2010 The associations of hA3G and hA3B mRNA levels with HIV disease progression among HIV-infected individuals of China.
20038599 2010 The antiviral factor APOBEC3G improves CTL recognition of cultured HIV-infected T cells.
20023216 2010 CCR6 ligands inhibit HIV by inducing APOBEC3G.
19996938 2010 APOBEC3G expression is dysregulated in primary HIV-1 infection and polymorphic variants influence CD4+ T-cell counts and plasma viral load.
19910370 2010 HIV-1 Vif binds to APOBEC3G mRNA and inhibits its translation.
19887642 2009 HIV-1 Vif-mediated ubiquitination/degradation of APOBEC3G involves four critical lysine residues in its C-terminal domain.
19886996 2009 Encapsidation of APOBEC3G into HIV-1 virions involves lipid raft association and does not correlate with APOBEC3G oligomerization.
19776130 2009 Functional analysis and structural modeling of human APOBEC3G reveal the role of evolutionarily conserved elements in the inhibition of human immunodeficiency virus type 1 infection and Alu transposition.
19649317 2009 CEM-T4 cells do not lack an APOBEC3G cofactor.
19587057 2009 Defining APOBEC3 expression patterns in human tissues and hematopoietic cell subsets.
19585516 2009 The effect of allogeneic in vitro stimulation and in vivo immunization on memory CD4(+) T-cell APOBEC3G expression and HIV-1 infectivity.
19561087 2009 A portable hot spot recognition loop transfers sequence preferences from APOBEC family members to activation-induced cytidine deaminase.
19535450 2009 A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 Vif SLVx4Yx9Y motif influences its interaction with APOBEC3G.
19535447 2009 Identification of a novel WxSLVK motif in the N terminus of human immunodeficiency virus and simian immunodeficiency virus Vif that is critical for APOBEC3G and APOBEC3F neutralization.
19535442 2009 Cytoplasmic APOBEC3G restricts incoming Vif-positive human immunodeficiency virus type 1 and increases two-long terminal repeat circle formation in activated T-helper-subtype cells.
19497112 2009 Intracellular interactions between APOBEC3G, RNA, and HIV-1 Gag: APOBEC3G multimerization is dependent on its association with RNA.
19487726 2009 Tumultuous relationship between the human immunodeficiency virus type 1 viral infectivity factor (Vif) and the human APOBEC-3G and APOBEC-3F restriction factors.
19458006 2009 Restriction of equine infectious anemia virus by equine APOBEC3 cytidine deaminases.
19389408 2009 An extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme model.
19371434 2009 High level expression of the anti-retroviral protein APOBEC3G is induced by influenza A virus but does not confer antiviral activity.
19345973 2009 APOBEC3G cytidine deaminase association with coronavirus nucleocapsid protein.
19343218 2009 Likely role of APOBEC3G-mediated G-to-A mutations in HIV-1 evolution and drug resistance.
19324886 2009 Inhibition of HIV-1 infection and replication by enhancing viral incorporation of innate anti-HIV-1 protein A3G: a non-pathogenic Nef mutant-based anti-HIV strategy.
19304304 2009 Restriction of HIV-1 by APOBEC3G is cytidine deaminase-dependent.
19300495 2009 Reassessing the role of APOBEC3G in human immunodeficiency virus type 1 infection of quiescent CD4+ T-cells.
19297501 2009 Optimal translation initiation enables Vif-deficient human immunodeficiency virus type 1 to escape restriction by APOBEC3G.
19266078 2009 RNA-dependent oligomerization of APOBEC3G is required for restriction of HIV-1.
19254362 2009 APOBEC3G mRNA expression in exposed seronegative and early stage HIV infected individuals decreases with removal of exposure and with disease progression.
19216784 2009 APOBEC3G induces a hypermutation gradient: purifying selection at multiple steps during HIV-1 replication results in levels of G-to-A mutations that are high in DNA, intermediate in cellular viral RNA, and low in virion RNA.
19197360 2009 Differences in APOBEC3G expression in CD4+ T helper lymphocyte subtypes modulate HIV-1 infectivity.
19169351 2009 Genetic editing of HBV DNA by monodomain human APOBEC3 cytidine deaminases and the recombinant nature of APOBEC3G.
19153609 2009 Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G.
19136562 2009 Dissecting APOBEC3G substrate specificity by nucleoside analog interference.
19057663 2008 APOBEC3G inhibits elongation of HIV-1 reverse transcripts.
19036809 2009 Distinct domains within APOBEC3G and APOBEC3F interact with separate regions of human immunodeficiency virus type 1 Vif.
19027180 2009 Expression and regulation of antiviral protein APOBEC3G in human neuronal cells.
19008196 2009 APOBEC3G: an intracellular centurion.
19004939 2009 Differential sensitivity of "old" versus "new" APOBEC3G to human immunodeficiency virus type 1 vif.
18987139 2009 Exosomes packaging APOBEC3G confer human immunodeficiency virus resistance to recipient cells.
18851679 2008 The level of APOBEC3G (hA3G)-related G-to-A mutations does not correlate with viral load in HIV type 1-infected individuals.
18849968 2008 Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications.
18843993 2008 [Study on the difference of the APOBEC3G mRNA levels among HIV long-term nonprogressors, slow progressors, people at high risks and normal people].
18842592 2008 APOBEC3G subunits self-associate via the C-terminal deaminase domain.
18836454 2008 Phosphorylation of APOBEC3G by protein kinase A regulates its interaction with HIV-1 Vif.
18809921 2008 NF-IL6 (C/EBPbeta) induces HIV-1 replication by inhibiting cytidine deaminase APOBEC3G.
18684817 2008 Human immunodeficiency virus type 1 replication and regulation of APOBEC3G by peptidyl prolyl isomerase Pin1.
18667511 2008 Two regions within the amino-terminal half of APOBEC3G cooperate to determine cytoplasmic localization.
18652534 2008 Absence of H186R polymorphism in exon 4 of the APOBEC3G gene among North Indian individuals.
18647522 2008 [The associations between polymorphisms of APOBEC3G and different outcomes of persistent HBV infection].
18639915 2008 Functional domain organization of human APOBEC3G.
18619467 2008 Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction.
18603011 Identification of amino acid residues in HIV-1 Vif critical for binding and exclusion of APOBEC3G/F.
18597676 2008 Characterization of APOBEC3G binding to 7SL RNA.
18501607 2008 Evolution of HIV-1 isolates that use a novel Vif-independent mechanism to resist restriction by human APOBEC3G.
18499212 2008 The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation.
18480459 2008 Reverse transcriptase- and RNA packaging signal-dependent incorporation of APOBEC3G into hepatitis B virus nucleocapsids.
18456846 2008 Single-stranded RNA facilitates nucleocapsid: APOBEC3G complex formation.
18448976 2008 Hepatitis B: modern concepts in pathogenesis--APOBEC3 cytidine deaminases as effectors in innate immunity against the hepatitis B virus.
18420796 2008 Hypermutation of hepatitis B virus genomes by APOBEC3G, APOBEC3C and APOBEC3H.
18414671 2008 Vpr14-88-Apobec3G fusion protein is efficiently incorporated into Vif-positive HIV-1 particles and inhibits viral infection.
18367521 2008 Comparison of cellular ribonucleoprotein complexes associated with the APOBEC3F and APOBEC3G antiviral proteins.
18366335 2008 Vif and Apobec3G in the innate immune response to HIV: a tale of two proteins.
18362149 2008 A model for oligomeric regulation of APOBEC3G cytosine deaminase-dependent restriction of HIV.
18326044 2008 APOBEC3G is degraded by the proteasomal pathway in a Vif-dependent manner without being polyubiquitylated.
18308358 2008 APOBEC3G restricts early HIV-1 replication in the cytoplasm of target cells.
18304004 2008 The APOBEC3 cytidine deaminases: an innate defensive network opposing exogenous retroviruses and endogenous retroelements.
18288108 2008 Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G.
18272764 2008 APOBEC3G upregulation by alpha interferon restricts human immunodeficiency virus type 1 infection in human peripheral plasmacytoid dendritic cells.
18184715 2008 The DNA deaminase activity of human APOBEC3G is required for Ty1, MusD, and human immunodeficiency virus type 1 restriction.
18165230 2008 Nuclear Exclusion of the HIV-1 host defense factor APOBEC3G requires a novel cytoplasmic retention signal and is not dependent on RNA binding.
18077705 2008 Role of APOBEC3G/F-mediated hypermutation in the control of human immunodeficiency virus type 1 in elite suppressors.
18029348 2008 Toward a confocal subcellular atlas of the human proteome.
18023836 2008 HIV-1 Vif promotes the formation of high molecular mass APOBEC3G complexes.
17928335 2007 Enzymatically active APOBEC3G is required for efficient inhibition of human immunodeficiency virus type 1.
17916373 2008 Function analysis of sequences in human APOBEC3G involved in Vif-mediated degradation.
17898068 2007 Identification of an APOBEC3G binding site in human immunodeficiency virus type 1 Vif and inhibitors of Vif-APOBEC3G binding.
17892323 2007 T cells contain an RNase-insensitive inhibitor of APOBEC3G deaminase activity.
17886715 2007 [Subcellular localization of APOBEC3G by confocal laser scanning microscope (CLSM)].
17881443 2007 7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3G.
17869248 2007 Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G.
17855362 2007 APOBEC3G inhibits DNA strand transfer during HIV-1 reverse transcription.
17849022 2007 The restriction of zoonotic PERV transmission by human APOBEC3G.
17848567 2007 Derepression of microRNA-mediated protein translation inhibition by apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G (APOBEC3G) and its family members.
17825339 2007 Production of infectious virus and degradation of APOBEC3G are separable functional properties of human immunodeficiency virus type 1 Vif.
17670826 2007 The interaction of APOBEC3G with human immunodeficiency virus type 1 nucleocapsid inhibits tRNA3Lys annealing to viral RNA.
17631688 2007 Analysis of the contribution of cellular and viral RNA to the packaging of APOBEC3G into HIV-1 virions.
17609216 2007 RNA and DNA binding properties of HIV-1 Vif protein: a fluorescence study.
17522216 2007 Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F.
17522211 2007 Human immunodeficiency virus type 1 Vif inhibits packaging and antiviral activity of a degradation-resistant APOBEC3G variant.
17517765 2007 Sp1 and Sp3 regulate basal transcription of the human APOBEC3G gene.
17440614 2007 Model structure of human APOBEC3G.
17374143 2007 APOBEC3G levels predict rates of progression to AIDS.
17344295 2007 APOBEC3G multimers are recruited to the plasma membrane for packaging into human immunodeficiency virus type 1 virus-like particles in an RNA-dependent process requiring the NC basic linker.
17314171 2007 Deamination-independent inhibition of hepatitis B virus reverse transcription by APOBEC3G.
17272283 2007 Virion-associated uracil DNA glycosylase-2 and apurinic/apyrimidinic endonuclease are involved in the degradation of APOBEC3G-edited nascent HIV-1 DNA.
17267497 2007 Identification of amino acid residues in APOBEC3G required for regulation by human immunodeficiency virus type 1 Vif and Virion encapsidation.
17259974 2007 APOBEC3 inhibits mouse mammary tumour virus replication in vivo.
17251560 2007 Dual effect of APOBEC3G on Hepatitis B virus.
17237417 2007 Stimulation of cell surface CCR5 and CD40 molecules by their ligands or by HSP70 up-regulates APOBEC3G expression in CD4(+) T cells and dendritic cells.
17212712 2007 Expression of APOBEC3G in kidney cells.
17166910 2007 Antiviral protein APOBEC3G localizes to ribonucleoprotein complexes found in P bodies and stress granules.
17161027 2007 The nuclear DNA deaminase AID functions distributively whereas cytoplasmic APOBEC3G has a processive mode of action.
17145955 2006 APOBEC3G/3F mediates intrinsic resistance of monocyte-derived dendritic cells to HIV-1 infection.
17142455 2007 Biochemical differentiation of APOBEC3F and APOBEC3G proteins associated with HIV-1 life cycle.
17126871 2007 Stoichiometry of the antiviral protein APOBEC3G in HIV-1 virions.
17121840 2007 APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G.
17083721 2006 The cell biology of HIV-1 and other retroviruses.
17079235 2006 Nanostructures of APOBEC3G support a hierarchical assembly model of high molecular mass ribonucleoprotein particles from dimeric subunits.
17079095 2007 Selective inhibition of Alu retrotransposition by APOBEC3G.
17067930 2006 Natural resistance to HIV infection: The Vif-APOBEC interaction.
17065315 2006 Generation of HIV-1 derivatives that productively infect macaque monkey lymphoid cells.
17064466 2006 [Inhibition of hepatitis B and duck hepatitis B virus replication by APOBEC3G].
17052331 2006 Vaccinia virus replication is not affected by APOBEC3 family members.
17049578 2007 Analysis of Vif-induced APOBEC3G degradation using an alpha-complementation assay.
17036163 2006 High expression of APOBEC3G in patients infected with hepatitis C virus.
17030807 2006 High-molecular-mass APOBEC3G complexes restrict Alu retrotransposition.
17020885 2006 Reversed functional organization of mouse and human APOBEC3 cytidine deaminase domains.
16988524 2006 APOBEC3G genetic variants and their association with risk of HIV infection in highly exposed Caucasians.
16940537 2006 Population level analysis of human immunodeficiency virus type 1 hypermutation and its relationship with APOBEC3G and vif genetic variation.
16887808 2006 The anti-HIV-1 editing enzyme APOBEC3G binds HIV-1 RNA and messenger RNAs that shuttle between polysomes and stress granules.
16874860 2006 Inhibition of hepatitis B virus replication by APOBEC3G in vitro and in vivo.
16731938 2006 Biochemical activities of highly purified, catalytically active human APOBEC3G: correlation with antiviral effect.
16710452 2006 Effect of DNA repair protein Rad18 on viral infection.
16699599 2006 Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies.
16678488 2006 Multifaceted antiviral actions of APOBEC3 cytidine deaminases.
16641889 2006 APOBEC deaminases as cellular antiviral factors: a novel natural host defense mechanism.
16641260 2006 Monomeric APOBEC3G is catalytically active and has antiviral activity.
16622407 2006 APOBEC3G DNA deaminase acts processively 3' --> 5' on single-stranded DNA.
16571802 2006 Adaptive evolution and antiviral activity of the conserved mammalian cytidine deaminase APOBEC3H.
16527742 2006 APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons.
16501124 2006 Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F.
16460778 2006 Comparative analysis of the antiretroviral activity of APOBEC3G and APOBEC3F from primates.
16426578 2006 Anti-viral protein APOBEC3G is induced by interferon-alpha stimulation in human hepatocytes.
16414984 2006 Role and mechanism of action of the APOBEC3 family of antiretroviral resistance factors.
16378963 2006 Restriction of foamy viruses by APOBEC cytidine deaminases.
16354571 Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions.
16344560 2006 Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.
16250885 2005 HIV-1 Vif: HIV's weapon against the cellular defense factor APOBEC3G.
16000409 2005 APOBEC3G hypermutates genomic DNA and inhibits Ty1 retrotransposition in yeast.
15943885 2005 APOBEC3G targets human T-cell leukemia virus type 1.
15823539 2005 Inhibition of a yeast LTR retrotransposon by human APOBEC3 cytidine deaminases.
15781449 2005 Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function.
15721369 2005 Complementary function of the two catalytic domains of APOBEC3G.
15674295 2005 APOBEC3G cytidine deaminase inhibits retrotransposition of endogenous retroviruses.
15647250 2005 The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain.
15613310 2005 Functional analysis of Vif protein shows less restriction of human immunodeficiency virus type 2 by APOBEC3G.
15611076 2005 HIV-1 Vif can directly inhibit apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G-mediated cytidine deamination by using a single amino acid interaction and without protein degradation.
15609224 2005 Exhaustive genotyping of the CEM15 (APOBEC3G) gene and absence of association with AIDS progression in a French cohort.
15581898 2005 APOBEC3G ubiquitination by Nedd4-1 favors its packaging into HIV-1 particles.
15578976 2004 Blocking HIV-1 Vif restores a natural mechanism of intracellular antiviral defense.
15574592 2004 Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation.
15537645 2005 Analysis of HIV-1 viral infectivity factor-mediated proteasome-dependent depletion of APOBEC3G: correlating function and subcellular localization.
15489334 2004 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
15479846 2004 APOBEC3G incorporation into human immunodeficiency virus type 1 particles.
15461802 2004 A genome annotation-driven approach to cloning the human ORFeome.
15452227 2004 APOBEC3G genetic variants and their influence on the progression to AIDS.
15383144 2004 HIV-1 Vif and APOBEC3G: multiple roads to one goal.
15373943 2004 Production of infectious human immunodeficiency virus type 1 does not require depletion of APOBEC3G from virus-producing cells.
15358144 2004 HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles.
15353294 2004 Role of viral regulatory and accessory proteins in HIV-1 replication.
15297452 2004 Transcriptional regulation of APOBEC3G, a cytidine deaminase that hypermutates human immunodeficiency virus.
15286366 2004 APOBEC-mediated editing of viral RNA.
15269786 2004 Ancient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3G.
15245742 2004 Recent insights into HIV-1 Vif.
15210704 2004 Human apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-like 3G (APOBEC3G) is incorporated into HIV-1 virions through interactions with viral and nonviral RNAs.
15177194 2004 The viral infectivity factor (Vif) of HIV-1 unveiled.
15168739 New insights into the role of Vif in HIV-1 replication.
15159405 2004 The interaction between HIV-1 Gag and APOBEC3G.
15156567 2004 Functional domains of APOBEC3G required for antiviral activity.
15152192 2004 A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins.
15116720 2004 HIV-1 Vif versus APOBEC3G: newly appreciated warriors in the ancient battle between virus and host.
15098018 2004 Single-strand specificity of APOBEC3G accounts for minus-strand deamination of the HIV genome.
15080177 2003 Virus-host interactions: role of HIV proteins Vif, Tat, and Rev.
15054139 2004 A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion.
15031497 2004 Inhibition of hepatitis B virus replication by APOBEC3G.
14747572 2004 Influence of primate lentiviral Vif and proteasome inhibitors on human immunodeficiency virus type 1 virion packaging of APOBEC3G.
14702039 2004 Complete sequencing and characterization of 21,243 full-length human cDNAs.
14672928 2004 Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway.
14614829 2003 The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G.
14565218 2003 HIV-1 Vif: counteracting innate antiretroviral defenses.
14564014 2003 Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex.
14557625 2003 The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity.
14557052 2003 Death and the retrovirus.
14528301 2003 HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation.
14528300 2003 The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif.
14527406 2003 HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability.
12970355 2003 The enzymatic activity of CEM15/Apobec-3G is essential for the regulation of the infectivity of HIV-1 virion but not a sole determinant of its antiviral activity.
12920286 2003 Virology. Weapons of mutational destruction.
12914693 2003 Death by deamination: a novel host restriction system for HIV-1.
12859895 2003 Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.
12840737 2003 Good to CU.
12830140 2003 DNA deamination: not just a trigger for antibody diversification but also a mechanism for defense against retroviruses.
12809610 2003 DNA deamination mediates innate immunity to retroviral infection.
12808466 2003 Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts.
12808465 2003 The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA.
12750511 2003 Hypermutation of HIV-1 DNA in the absence of the Vif protein.
12719574 2003 Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions.
12683974 2003 Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business.
12477932 2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.
12167863 2002 Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein.
11863358 2002 An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22.
10591208 1999 The DNA sequence of human chromosome 22.
9846577 1998 Evidence for a newly discovered cellular anti-HIV-1 phenotype.
9811770 1998 An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein.