Role of Vif in stability of the human immunodeficiency virus type 1 core
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 VifHIV-1 Vif and APOBEC3G: multiple roads to one goalComprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virionsEarly steps of retrovirus replicative cycleHIV Genome-Wide Protein Associations: a Review of 30 Years of ResearchRoles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactionsThe human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity.APOBEC3G inhibits elongation of HIV-1 reverse transcripts.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.Intravirion 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.Mechanistic aspects of HIV-1 reverse transcription initiation.Charting HIV's remarkable voyage through the cell: Basic science as a passport to future therapy.RING domain mutations uncouple TRIM5α restriction of HIV-1 from inhibition of reverse transcription and acceleration of uncoatingVif is a RNA chaperone that could temporally regulate RNA dimerization and the early steps of HIV-1 reverse transcription.Identification and characterization of a new type of inhibitor against the human immunodeficiency virus type-1 nucleocapsid protein.Inhibition of reverse transcriptase activity increases stability of the HIV-1 core.Influence of primate lentiviral Vif and proteasome inhibitors on human immunodeficiency virus type 1 virion packaging of APOBEC3G.Tumultuous relationship between the human immunodeficiency virus type 1 viral infectivity factor (Vif) and the human APOBEC-3G and APOBEC-3F restriction factors.Measles virus phosphoprotein gene products: conformational flexibility of the P/V protein amino-terminal domain and C protein infectivity factor functionAmino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging.Differential contribution of basic residues to HIV-1 nucleocapsid protein's nucleic acid chaperone function and retroviral replication.Host restriction of lentiviruses and viral countermeasures: APOBEC3 and Vif.RNA and DNA binding properties of HIV-1 Vif protein: a fluorescence study.Vif is an auxiliary factor of the HIV-1 reverse transcriptase and facilitates abasic site bypass.Mutational analysis of the HIV-1 auxiliary protein Vif identifies independent domains important for the physical and functional interaction with HIV-1 reverse transcriptase.High level expression of human immunodeficiency virus type-1 Vif inhibits viral infectivity by modulating proteolytic processing of the Gag precursor at the p2/nucleocapsid processing site.Requirements for nucleocapsid-mediated regulation of reverse transcription during the late steps of HIV-1 assembly.Simultaneous mutations in CA and Vif of Maedi-Visna virus cause attenuated replication in macrophages and reduced infectivity in vivo.Functional neutralization of HIV-1 Vif protein by intracellular immunization inhibits reverse transcription and viral replication.HIV-1 Capsid Stabilization Assay.Importance of the proline-rich multimerization domain on the oligomerization and nucleic acid binding properties of HIV-1 VifIsolated HIV-1 core is active for reverse transcription.A carboxy-terminally truncated human CPSF6 lacking residues encoded by exon 6 inhibits HIV-1 cDNA synthesis and promotes capsid disassemblyHuman cytosolic extracts stabilize the HIV-1 core
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P2860
Role of Vif in stability of the human immunodeficiency virus type 1 core
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
Role of Vif in stability of the human immunodeficiency virus type 1 core
@en
Role of Vif in stability of the human immunodeficiency virus type 1 core.
@nl
type
label
Role of Vif in stability of the human immunodeficiency virus type 1 core
@en
Role of Vif in stability of the human immunodeficiency virus type 1 core.
@nl
prefLabel
Role of Vif in stability of the human immunodeficiency virus type 1 core
@en
Role of Vif in stability of the human immunodeficiency virus type 1 core.
@nl
P2860
P1433
P1476
Role of Vif in stability of the human immunodeficiency virus type 1 core
@en
P2093
P2860
P304
11055-11066
P356
10.1128/JVI.74.23.11055-11066.2000
P407
P577
2000-12-01T00:00:00Z