Cleavage of human immunodeficiency virus type 1 proteinase from the N-terminally adjacent p6* protein is essential for efficient Gag polyprotein processing and viral infectivity.
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Terminal Interface Conformations Modulate Dimer Stability Prior to Amino Terminal Autoprocessing of HIV-1 ProteaseA Functional Interplay between Human Immunodeficiency Virus Type 1 Protease Residues 77 and 93 Involved in Differential Regulation of Precursor Autoprocessing and Mature Protease ActivityConstruction of a human immunodeficiency virus type 1 (HIV-1) library containing random combinations of amino acid substitutions in the HIV-1 protease due to resistance by protease inhibitors.Understanding HIV-1 protease autoprocessing for novel therapeutic development.Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease.Assembly and processing of human immunodeficiency virus Gag mutants containing a partial replacement of the matrix domain by the viral protease domainPlacement of leucine zipper motifs at the carboxyl terminus of HIV-1 protease significantly reduces virion production.Reversal by dithiothreitol treatment of the block in murine leukemia virus maturation induced by disulfide cross-linkingProline residues within spacer peptide p1 are important for human immunodeficiency virus type 1 infectivity, protein processing, and genomic RNA dimer stability.New findings in cleavage sites variability across groups, subtypes and recombinants of human immunodeficiency virus type 1Gag non-cleavage site mutations contribute to full recovery of viral fitness in protease inhibitor-resistant human immunodeficiency virus type 1.Gag-Pol Transframe Domain p6* Is Essential for HIV-1 Protease-Mediated Virus Maturation.Efavirenz enhances HIV-1 gag processing at the plasma membrane through Gag-Pol dimerizationHIV-1 protease dimer interface mutations that compensate for viral reverse transcriptase instability in infectious virions.Uncoupling human immunodeficiency virus type 1 Gag and Pol reading frames: role of the transframe protein p6* in viral replication.Modulation of human immunodeficiency virus type 1 protease autoprocessing by charge properties of surface residue 69.C-Terminal HIV-1 Transframe p6* Tetrapeptide Blocks Enhanced Gag Cleavage Incurred by Leucine Zipper Replacement of a Deleted p6* Domain.Flexible catalytic site conformations implicated in modulation of HIV-1 protease autoprocessing reactions.The dimer interfaces of protease and extra-protease domains influence the activation of protease and the specificity of GagPol cleavage.Cysteine 95 and other residues influence the regulatory effects of Histidine 69 mutations on Human Immunodeficiency Virus Type 1 protease autoprocessing.Variability at human immunodeficiency virus type 1 subtype C protease cleavage sites: an indication of viral fitness?Complementation in cells cotransfected with a mixture of wild-type and mutant human immunodeficiency virus (HIV) influences the replication capacities and phenotypes of mutant variants in a single-cycle HIV resistance assay.Importance of protease cleavage sites within and flanking human immunodeficiency virus type 1 transframe protein p6* for spatiotemporal regulation of protease activation.Mutations Proximal to Sites of Autoproteolysis and the α-Helix That Co-evolve under Drug Pressure Modulate the Autoprocessing and Vitality of HIV-1 Protease.Selection of resistance in protease inhibitor-experienced, human immunodeficiency virus type 1-infected subjects failing lopinavir- and ritonavir-based therapy: mutation patterns and baseline correlatesAutoprocessing of human immunodeficiency virus type 1 protease miniprecursor fusions in mammalian cells.HIV-1 protease with leucine zipper fused at N-terminus exhibits enhanced linker amino acid-dependent activity.Inhibition of the precursor and mature forms of HIV-1 protease as a tool for drug evaluation.
P2860
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P2860
Cleavage of human immunodeficiency virus type 1 proteinase from the N-terminally adjacent p6* protein is essential for efficient Gag polyprotein processing and viral infectivity.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Cleavage of human immunodefici ...... cessing and viral infectivity.
@en
Cleavage of human immunodefici ...... cessing and viral infectivity.
@nl
type
label
Cleavage of human immunodefici ...... cessing and viral infectivity.
@en
Cleavage of human immunodefici ...... cessing and viral infectivity.
@nl
prefLabel
Cleavage of human immunodefici ...... cessing and viral infectivity.
@en
Cleavage of human immunodefici ...... cessing and viral infectivity.
@nl
P2860
P1433
P1476
Cleavage of human immunodefici ...... cessing and viral infectivity.
@en
P2093
Kräusslich HG
P2860
P304
P407
P577
1998-04-01T00:00:00Z