Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism.
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Processing sites in the human immunodeficiency virus type 1 (HIV-1) Gag-Pro-Pol precursor are cleaved by the viral protease at different rates.HIV Genome-Wide Protein Associations: a Review of 30 Years of ResearchThe choreography of HIV-1 proteolytic processing and virion assemblyThe intracellular plasma membrane-connected compartment in the assembly of HIV-1 in human macrophages.Crystal structure of an FIV/HIV chimeric protease complexed with the broad-based inhibitor, TL-3Nine crystal structures determine the substrate envelope of the MDR HIV-1 proteaseTerminal Interface Conformations Modulate Dimer Stability Prior to Amino Terminal Autoprocessing of HIV-1 ProteaseGag-Pol processing during HIV-1 virion maturation: a systems biology approachHIV-1 Nef inhibits Protease activity and its absence alters protein content of mature viral particlesA Functional Interplay between Human Immunodeficiency Virus Type 1 Protease Residues 77 and 93 Involved in Differential Regulation of Precursor Autoprocessing and Mature Protease ActivityKinetic characterization of the critical step in HIV-1 protease maturationUnderstanding HIV-1 protease autoprocessing for novel therapeutic development.Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease.The mutation T477A in HIV-1 reverse transcriptase (RT) restores normal proteolytic processing of RT in virus with Gag-Pol mutated in the p51-RNH cleavage siteThe initial step in human immunodeficiency virus type 1 GagProPol processing can be regulated by reversible oxidationFeline immunodeficiency virus (FIV) as a model for study of lentivirus infections: parallels with HIV.Mutations that abrogate human immunodeficiency virus type 1 reverse transcriptase dimerization affect maturation of the reverse transcriptase heterodimer.Virion instability of human immunodeficiency virus type 1 reverse transcriptase (RT) mutated in the protease cleavage site between RT p51 and the RT RNase H domain.Drug-associated changes in amino acid residues in Gag p2, p7(NC), and p6(Gag)/p6(Pol) in human immunodeficiency virus type 1 (HIV-1) display a dominant effect on replicative fitness and drug response.Dimerization of HIV-1 protease occurs through two steps relating to the mechanism of protease dimerization inhibition by darunavir.Placement of leucine zipper motifs at the carboxyl terminus of HIV-1 protease significantly reduces virion production.The nature of the N-terminal amino acid residue of HIV-1 RNase H is critical for the stability of reverse transcriptase in viral particles.Inhibition of autoprocessing of natural variants and multidrug resistant mutant precursors of HIV-1 protease by clinical inhibitors.Chaperone role for proteins p618 and p892 in the extracellular tail development of Acidianus two-tailed virus.Membrane-Active Sequences within gp41 Membrane Proximal External Region (MPER) Modulate MPER-Containing Peptidyl Fusion Inhibitor Activity and the Biosynthesis of HIV-1 Structural ProteinsActivity of human immunodeficiency virus type 1 protease inhibitors against the initial autocleavage in Gag-Pol polyprotein processingA critical subset model provides a conceptual basis for the high antiviral activity of major HIV drugsMolecular mechanisms of FIV infection.Suboptimal inhibition of protease activity in human immunodeficiency virus type 1: effects on virion morphogenesis and RNA maturationThe N-end rule and retroviral infection: no effect on integrase.Binding of Clinical Inhibitors to a Model Precursor of a Rationally Selected Multidrug Resistant HIV-1 Protease Is Significantly Weaker Than That to the Released Mature EnzymeUncoupling human immunodeficiency virus type 1 Gag and Pol reading frames: role of the transframe protein p6* in viral replication.Analysis of human immunodeficiency virus matrix domain replacements.Analysis and characterization of dimerization inhibition of a multi-drug-resistant human immunodeficiency virus type 1 protease using a novel size-exclusion chromatographic approachHIV-1 Gag processing intermediates trans-dominantly interfere with HIV-1 infectivity.Formation of the tRNALys packaging complex in HIV-1.Targets for inhibition of HIV replication: entry, enzyme action, release and maturation.Human Immunodeficiency Virus Gag and protease: partners in resistance.Flexible catalytic site conformations implicated in modulation of HIV-1 protease autoprocessing reactions.Importance of protease cleavage sites within and flanking human immunodeficiency virus type 1 transframe protein p6* for spatiotemporal regulation of protease activation.
P2860
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P2860
Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
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2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
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name
Initial cleavage of the human ...... y an intramolecular mechanism.
@en
type
label
Initial cleavage of the human ...... y an intramolecular mechanism.
@en
prefLabel
Initial cleavage of the human ...... y an intramolecular mechanism.
@en
P2093
P2860
P1433
P1476
Initial cleavage of the human ...... y an intramolecular mechanism.
@en
P2093
Andrew H Kaplan
Ben M Dunn
Lorraine E Everitt
Steven C Pettit
Sumana Choudhury
P2860
P304
P356
10.1128/JVI.78.16.8477-8485.2004
P407
P577
2004-08-01T00:00:00Z