Determinants of the human immunodeficiency virus type 1 p15NC-RNA interaction that affect enhanced cleavage by the viral protease.
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Is HIV-1 RNA dimerization a prerequisite for packaging? Yes, no, probably?Processing sites in the human immunodeficiency virus type 1 (HIV-1) Gag-Pro-Pol precursor are cleaved by the viral protease at different rates.The choreography of HIV-1 proteolytic processing and virion assemblyHIV-1 protease and reverse transcriptase control the architecture of their nucleocapsid partnerReplacement of the P1 amino acid of human immunodeficiency virus type 1 Gag processing sites can inhibit or enhance the rate of cleavage by the viral proteaseConserved cysteines of the human immunodeficiency virus type 1 protease are involved in regulation of polyprotein processing and viral maturation of immature virionsDistinct nucleic acid interaction properties of HIV-1 nucleocapsid protein precursor NCp15 explain reduced viral infectivity.Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA.Generation of infectious feline immunodeficiency virus (FIV) encoding FIV/human immunodeficiency virus chimeric protease.Positive and negative aspects of the human immunodeficiency virus protease: development of inhibitors versus its role in AIDS pathogenesisCD4+-T-cell and CD20+-B-cell changes predict rapid disease progression after simian-human immunodeficiency virus infection in macaques.HIV-1 RNA dimerization: It takes two to tangoFeatures, processing states, and heterologous protein interactions in the modulation of the retroviral nucleocapsid protein function.Altered gag polyprotein cleavage specificity of feline immunodeficiency virus/human immunodeficiency virus mutant proteases as demonstrated in a cell-based expression system.HIV-1 matrix domain removal ameliorates virus assembly and processing defects incurred by positive nucleocapsid charge elimination.Gag non-cleavage site mutations contribute to full recovery of viral fitness in protease inhibitor-resistant human immunodeficiency virus type 1.Context surrounding processing sites is crucial in determining cleavage rate of a subset of processing sites in HIV-1 Gag and Gag-Pro-Pol polyprotein precursors by viral protease.Mutational analysis of the C-terminal gag cleavage sites in human immunodeficiency virus type 1Selection of drug-resistant feline immunodeficiency virus (FIV) encoding FIV/HIV chimeric protease in the presence of HIV-specific protease inhibitorsNucleocapsid protein function in early infection processes.The A-rich RNA sequences of HIV-1 pol are important for the synthesis of viral cDNA.Human immunodeficiency virus type 1 protease-correlated cleavage site mutations enhance inhibitor resistance.Tumultuous relationship between the human immunodeficiency virus type 1 viral infectivity factor (Vif) and the human APOBEC-3G and APOBEC-3F restriction factors.Changes in human immunodeficiency virus type 1 Gag at positions L449 and P453 are linked to I50V protease mutants in vivo and cause reduction of sensitivity to amprenavir and improved viral fitness in vitro.The conserved N-terminal basic residues and zinc-finger motifs of HIV-1 nucleocapsid restrict the viral cDNA synthesis during virus formation and maturation.Nucleocapsid mutations turn HIV-1 into a DNA-containing virus.Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism.A Direct Interaction with RNA Dramatically Enhances the Catalytic Activity of the HIV-1 Protease In VitroResolving fast and slow motions in the internal loop containing stem-loop 1 of HIV-1 that are modulated by Mg2+ binding: role in the kissing-duplex structural transition.
P2860
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P2860
Determinants of the human immunodeficiency virus type 1 p15NC-RNA interaction that affect enhanced cleavage by the viral protease.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Determinants of the human immu ...... leavage by the viral protease.
@ast
Determinants of the human immu ...... leavage by the viral protease.
@en
type
label
Determinants of the human immu ...... leavage by the viral protease.
@ast
Determinants of the human immu ...... leavage by the viral protease.
@en
prefLabel
Determinants of the human immu ...... leavage by the viral protease.
@ast
Determinants of the human immu ...... leavage by the viral protease.
@en
P2093
P2860
P1433
P1476
Determinants of the human immu ...... cleavage by the viral protease
@en
P2093
D H Ozturk
M M Rayner
R J Tritch
R Swanstrom
S C Pettit
S Erickson-Viitanen
P2860
P304
P407
P577
1997-08-01T00:00:00Z