The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
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Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodiesEvidence for restriction of ancient primate gammaretroviruses by APOBEC3 but not TRIM5alpha proteinsAncient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3GT cell responses to human endogenous retroviruses in HIV-1 infectionRing finger protein ZIN interacts with human immunodeficiency virus type 1 VifTRIM5α and Species Tropism of HIV/SIVAPOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 restrict human T-lymphotropic virus type 1Sole copy of Z2-type human cytidine deaminase APOBEC3H has inhibitory activity against retrotransposons and HIV-1Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradationHIV-1 replication through hHR23A-mediated interaction of Vpr with 26S proteasomeMutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into their DNA target site specificitiesDifferential sensitivity of murine leukemia virus to APOBEC3-mediated inhibition is governed by virion exclusion.Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylasesRole and mechanism of action of the APOBEC3 family of antiretroviral resistance factorsDifferential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F.The human and African green monkey TRIM5alpha genes encode Ref1 and Lv1 retroviral restriction factor activitiesHuman APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replicationHIV-1 Vif and APOBEC3G: multiple roads to one goalA second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteinsA single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletionHow SAMHD1 changes our view of viral restrictionDifferential anti-APOBEC3G activity of HIV-1 Vif proteins derived from different subtypesStructural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3GAPOBEC3G contributes to HIV-1 variation through sublethal mutagenesisHIV-1 Vif versus the APOBEC3 cytidine deaminases: an intracellular duel between pathogen and host restriction factorsRestriction of retroviral replication by APOBEC3G/F and TRIM5alphaTurning up the volume on mutational pressure: is more of a good thing always better? (A case study of HIV-1 Vif and APOBEC3)HIV-1 Vif, APOBEC, and intrinsic immunityAPOBEC3G-UBA2 fusion as a potential strategy for stable expression of APOBEC3G and inhibition of HIV-1 replicationHuman cytidine deaminase APOBEC3H restricts HIV-1 replicationA single amino acid difference in human APOBEC3H variants determines HIV-1 Vif sensitivityThe HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradationStructural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assemblyIdentification of APOBEC3DE as another antiretroviral factor from the human APOBEC familyIdentification of amino acid residues in APOBEC3G required for regulation by human immunodeficiency virus type 1 Vif and Virion encapsidation7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3GEarly steps of retrovirus replicative cycleProduction of infectious human immunodeficiency virus type 1 does not require depletion of APOBEC3G from virus-producing cellsIntracellular immunity to HIV-1: newly defined retroviral battles inside infected cells.APOBEC3G targets human T-cell leukemia virus type 1.
P2860
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P2860
The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
description
2003 nî lūn-bûn
@nan
2003 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
@ast
The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
@en
type
label
The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
@ast
The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
@en
prefLabel
The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
@ast
The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
@en
P2093
P3181
P356
P1433
P1476
The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
@en
P2093
P2888
P304
P3181
P356
10.1038/NM945
P407
P577
2003-11-01T00:00:00Z
P5875
P6179
1028021791