The human immunodeficiency virus type 1 Vif protein modulates the postpenetration stability of viral nucleoprotein complexes
about
The dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3GRing finger protein ZIN interacts with human immunodeficiency virus type 1 VifThe cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNARole and mechanism of action of the APOBEC3 family of antiretroviral resistance factorsHIV-1 Vif versus the APOBEC3 cytidine deaminases: an intracellular duel between pathogen and host restriction factorsInhibition of tRNA₃(Lys)-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replicationComprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virionsHuman immunodeficiency virus type 1 cDNAs produced in the presence of APOBEC3G exhibit defects in plus-strand DNA transfer and integrationProduction of infectious human immunodeficiency virus type 1 does not require depletion of APOBEC3G from virus-producing cellsContribution of the C-terminal tri-lysine regions of human immunodeficiency virus type 1 integrase for efficient reverse transcription and viral DNA nuclear importHIV Genome-Wide Protein Associations: a Review of 30 Years of ResearchFeline immunodeficiency virus Vif localizes to the nucleusMulti-scale modeling of HIV infection in vitro and APOBEC3G-based anti-retroviral therapyImplication of the lymphocyte-specific nuclear body protein Sp140 in an innate response to human immunodeficiency virus type 1.The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity.Going wild: lessons from naturally occurring T-lymphotropic lentivirusesVpr14-88-Apobec3G fusion protein is efficiently incorporated into Vif-positive HIV-1 particles and inhibits viral infection.APOBEC3G inhibits elongation of HIV-1 reverse transcripts.Proteasome inhibitors act as bifunctional antagonists of human immunodeficiency virus type 1 latency and replication.Association of human immunodeficiency virus type 1 Vif with RNA and its role in reverse transcriptionG-->A hypermutation in protease and reverse transcriptase regions of human immunodeficiency virus type 1 residing in resting CD4+ T cells in vivoRole of matrix in an early postentry step in the human immunodeficiency virus type 1 life cycle.The S2 gene of equine infectious anemia virus is dispensable for viral replication in vitroCellular and viral specificities of human immunodeficiency virus type 1 vif protein.Reversion of a human immunodeficiency virus type 1 matrix mutation affecting Gag membrane binding, endogenous reverse transcriptase activity, and virus infectivity.Interactions of host APOBEC3 restriction factors with HIV-1 in vivo: implications for therapeutics.Species-specific, postentry barriers to primate immunodeficiency virus infection.Vif is largely absent from human immunodeficiency virus type 1 mature virions and associates mainly with viral particles containing unprocessed gag.Human immunodeficiency virus type 1 Vif protein is packaged into the nucleoprotein complex through an interaction with viral genomic RNA.Uracil DNA glycosylase is dispensable for human immunodeficiency virus type 1 replication and does not contribute to the antiviral effects of the cytidine deaminase Apobec3G.Characterization of producer cell-dependent restriction of murine leukemia virus replicationIntravirion processing of the human immunodeficiency virus type 1 Vif protein by the viral protease may be correlated with Vif function.Human immunodeficiency virus type 1 Vif is efficiently packaged into virions during productive but not chronic infection.Amino acid residues 88 and 89 in the central hydrophilic region of human immunodeficiency virus type 1 Vif are critical for viral infectivity by enhancing the steady-state expression of Vif.Antiviral protein APOBEC3G localizes to ribonucleoprotein complexes found in P bodies and stress granulesAPOBEC3G-Augmented Stem Cell Therapy to Modulate HIV Replication: A Computational Study.APOBEC3G: a double agent in defenseCharacterization of anti-HIV activity mediated by R88-APOBEC3G mutant fusion proteins in CD4+ T cells, peripheral blood mononuclear cells, and macrophages.The HDAC6/APOBEC3G complex regulates HIV-1 infectiveness by inducing Vif autophagic degradation.Human immunodeficiency virus type 1 Vif does not influence expression or virion incorporation of gag-, pol-, and env-encoded proteins.
P2860
Q21245195-9B714BC3-D2F0-4DD8-B09F-90875DC3E0DEQ24304030-3F0C1349-4A1D-43A7-8D74-461FEBDD21B3Q24305266-09088423-CEF3-4430-8C28-082561D4FA70Q24537623-86119179-DE1A-47F5-8F56-DE0299226DCFQ24619114-21D094A9-F79F-4F2B-8654-5420BB4FA762Q24669993-09CE04F6-A474-4CE8-B5B4-9BEC4E3124B1Q24678970-9FFD9B9A-77EF-4BE2-8753-57F48092F4D9Q24684279-10F8A97F-6C77-4016-B09D-937CCAB6AD8BQ24796626-1CAF554E-28E2-4685-A7B3-16D11D1C4F10Q24814060-003B40C0-6723-4283-8FFA-59C38B71FF0EQ26746070-17E0A923-C3FE-44C7-8963-90AFD55A85C1Q27469637-D63D6E0C-739D-45E6-9494-F49EAFAB9BF2Q28480578-515D05D6-F317-4E4C-800F-091EAAD8A8C9Q30860339-5732F032-D3A1-458E-9F4B-CF382E4CABEDQ31011512-CAE53A81-5538-409B-B280-3A5AE205F43FQ31066870-B1CFAA70-4CFD-4828-8877-2B2EEAFC0D39Q33328499-EC3B10AE-F8E8-4D40-B32E-4DD1040DDC29Q33389841-CA9C5E6D-11C3-4323-ABBF-C548F9CCB578Q33589167-F28AFF40-5957-4146-BE05-DC21C6EE5660Q33604247-0AACAB2C-95D7-4D6F-913B-067B57A82182Q33718616-A8D6E9E5-2F5C-4220-93EA-489CD49E01A4Q33782781-68C6AD71-1221-4FBA-B8FB-BEA81D68F9F5Q33785006-7CF70AD4-7321-4A4F-8AFF-990FEE0F0B32Q33806688-0FF94E29-058E-49D0-88B7-D0756A262FB6Q33813747-890F6D92-C250-4ED6-BBA5-6E5390A1D806Q33815187-12FC047D-2280-4F80-B6FC-C79F5A8C7217Q33824990-35B98D0D-F415-4266-95A2-4F6733B9CC2BQ33841920-B2875FDC-DA8B-40B4-B843-5569FBC886E0Q33852465-801D96A0-490F-4281-A8CD-61A3CDC349A8Q34301892-719AEC5E-3E5C-4380-8FDD-C6B7BB1F062DQ34341128-37BD071E-3849-41F1-9692-B96F9314552DQ34345408-48A839A9-A7C7-4C41-BB25-5C5B9C6468BFQ34465108-5B3122BF-CE9F-4593-BC63-B2BCBF2B8F5DQ34465355-ADC96AD4-7FC5-439E-900F-40BCA962C906Q34590679-FA3750B6-4C1A-4D75-8FD8-B55F7E2D0B0EQ34749384-C63DB537-E83B-4CB5-9D4C-673336D594F4Q34917194-A9F5F100-0364-4AFB-9A68-AD6AB94813AFQ35496476-BD68E922-D927-4801-9CFD-DF55BB9CBC9DQ35776289-98AE25EC-D2BE-4E09-B192-D793C6D44478Q35873067-0339F361-C826-4A12-8E15-D15D8F4AD9B5
P2860
The human immunodeficiency virus type 1 Vif protein modulates the postpenetration stability of viral nucleoprotein complexes
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
The human immunodeficiency vir ...... viral nucleoprotein complexes
@ast
The human immunodeficiency vir ...... viral nucleoprotein complexes
@en
type
label
The human immunodeficiency vir ...... viral nucleoprotein complexes
@ast
The human immunodeficiency vir ...... viral nucleoprotein complexes
@en
prefLabel
The human immunodeficiency vir ...... viral nucleoprotein complexes
@ast
The human immunodeficiency vir ...... viral nucleoprotein complexes
@en
P2860
P1433
P1476
The human immunodeficiency vir ...... viral nucleoprotein complexes
@en
P2093
P2860
P304
P407
P577
1996-08-01T00:00:00Z