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Pathogenesis of human immunodeficiency virus infectionCharacterization of the protease domain of Rice tungro bacilliform virus responsible for the processing of the capsid protein from the polyproteinEffect of the Active Site D25N Mutation on the Structure, Stability, and Ligand Binding of the Mature HIV-1 ProteaseHighly conserved glycine 86 and arginine 87 residues contribute differently to the structure and activity of the mature HIV-1 proteaseAutocatalytic maturation, physical/chemical properties, and crystal structure of group N HIV-1 protease: Relevance to drug resistanceNovel P2 Tris-tetrahydrofuran Group in Antiviral Compound 1 (GRL-0519) Fills the S2 Binding Pocket of Selected Mutants of HIV-1 ProteaseTerminal Interface Conformations Modulate Dimer Stability Prior to Amino Terminal Autoprocessing of HIV-1 ProteaseSelection of multiple human immunodeficiency virus type 1 variants that encode viral proteases with decreased sensitivity to an inhibitor of the viral 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.Replacement 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 proteaseUnderstanding HIV-1 protease autoprocessing for novel therapeutic development.Proteolytic processing of the p2/nucleocapsid cleavage site is critical for human immunodeficiency virus type 1 RNA dimer maturation.Novel macromolecular inhibitors of human immunodeficiency virus-1 protease.Total chemical synthesis of human T-cell leukemia virus type 1 protease via native chemical ligation.Molecular basis for substrate recognition and drug resistance from 1.1 to 1.6 angstroms resolution crystal structures of HIV-1 protease mutants with substrate analogs.Human immunodeficiency virus type 1 Gag proteins are processed in two cellular compartments.Molecular and phylogenetic analyses of a new amphotropic murine leukemia virus (MuLV-1313)Maturation of giardiavirus capsid protein involves posttranslational proteolytic processing by a cysteine proteaseAberrant Gag protein composition of a human immunodeficiency virus type 1 vif mutant produced in primary lymphocytesA p6Pol-protease fusion protein is present in mature particles of human immunodeficiency virus type 1.Expression and maturation of human foamy virus Gag precursor polypeptides.Determinants of the human immunodeficiency virus type 1 p15NC-RNA interaction that affect enhanced cleavage by the viral protease.A small region of the ecotropic murine leukemia virus (MuLV) gag gene profoundly influences the types of polytropic MuLVs generated in mice.Sequence requirements of the HIV-1 protease flap region determined by saturation mutagenesis and kinetic analysis of flap mutantsMechanism of dissociative inhibition of HIV protease and its autoprocessing from a precursor.A solution NMR study of the binding kinetics and the internal dynamics of an HIV-1 protease-substrate complex.Antiviral activity of human immunodeficiency virus type 1 protease inhibitors in a single cycle of infection: evidence for a role of protease in the early phase.A cysteine protease encoded by the baculovirus Bombyx mori nuclear polyhedrosis virus.The activity of the protease of human immunodeficiency virus type 1 is initiated at the membrane of infected cells before the release of viral proteins and is required for release to occur with maximum efficiency.Avian retroviral RNA encapsidation: reexamination of functional 5' RNA sequences and the role of nucleocapsid Cys-His motifs.Human immunodeficiency virus type 1 gag-protease fusion proteins are enzymatically active.Identification of proteolytic processing sites within the Gag and Pol polyproteins of feline immunodeficiency virus.Amino acids encoded downstream of gag are not required by Rous sarcoma virus protease during gag-mediated assembly.Amino acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site.Evolution under Drug Pressure Remodels the Folding Free-Energy Landscape of Mature HIV-1 ProteaseComputational Studies of a Mechanism for Binding and Drug Resistance in the Wild Type and Four Mutations of HIV-1 Protease with a GRL-0519 Inhibitor.Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymesOptimization of quantitative culture assay for human immunodeficiency virus from plasma. Plasma Viremia Group Laboratories of the AIDS Clinical Trials Group (National Institute of Allergy and Infectious Diseases)HIV-1 protease dimer interface mutations that compensate for viral reverse transcriptase instability in infectious virions.
P2860
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P2860
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
Retroviral proteinases.
@en
Retroviral proteinases.
@nl
type
label
Retroviral proteinases.
@en
Retroviral proteinases.
@nl
prefLabel
Retroviral proteinases.
@en
Retroviral proteinases.
@nl
P1476
Retroviral proteinases.
@en
P2093
R B Luftig
S Oroszlan
P304
P577
1990-01-01T00:00:00Z