Sensitive, soluble chromogenic substrates for HIV-1 proteinase
about
Enzymatic and structural analysis of the I47A mutation contributing to the reduced susceptibility to HIV protease inhibitor lopinavirStructural and biochemical characterization of the inhibitor complexes of xenotropic murine leukemia virus-related virus proteaseMutations in HIV-1 gag and pol Compensate for the Loss of Viral Fitness Caused by a Highly Mutated ProteaseSDZ PRI 053, an orally bioavailable human immunodeficiency virus type 1 proteinase inhibitor containing the 2-aminobenzylstatine moietyProtein structure-based design of potent orally bioavailable, nonpeptide inhibitors of human immunodeficiency virus proteaseAntiviral and resistance studies of AG1343, an orally bioavailable inhibitor of human immunodeficiency virus proteaseReplacement 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 proteaseAlteration of substrate and inhibitor specificity of feline immunodeficiency virus protease.Altered substrate specificity of drug-resistant human immunodeficiency virus type 1 protease.Conserved cysteines of the human immunodeficiency virus type 1 protease are involved in regulation of polyprotein processing and viral maturation of immature virionsRevealing the dimer dissociation and existence of a folded monomer of the mature HIV-2 proteaseThe initial step in human immunodeficiency virus type 1 GagProPol processing can be regulated by reversible oxidationStability and activity of human immunodeficiency virus protease: comparison of the natural dimer with a homologous, single-chain tethered dimer.beta-Galactosidase containing a human immunodeficiency virus protease cleavage site is cleaved and inactivated by human immunodeficiency virus proteaseIonic derivatives of betulinic acid as novel HIV-1 protease inhibitors.Design, synthesis and evaluation of a potent substrate analog inhibitor identified by scanning Ala/Phe mutagenesis, mimicking substrate co-evolution, against multidrug-resistant HIV-1 protease.Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyproteinMechanism of dissociative inhibition of HIV protease and its autoprocessing from a precursor.Proteolytic activity of novel human immunodeficiency virus type 1 proteinase proteins from a precursor with a blocking mutation at the N terminus of the PR domain.Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymesBinding 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 EnzymeIdentification of active-site residues of the adenovirus endopeptidase.A genetic system for studying the activity of a proteolytic enzyme.A yeast-based growth assay for the analysis of site-specific proteases.Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites.Characterization of the protease of a fish retrovirus, walleye dermal sarcoma virus.The spacer peptide between human immunodeficiency virus capsid and nucleocapsid proteins is essential for ordered assembly and viral infectivityAn active-site mutation in the human immunodeficiency virus type 1 proteinase (PR) causes reduced PR activity and loss of PR-mediated cytotoxicity without apparent effect on virus maturation and infectivityAnalysis of cleavage site mutations between the NC and PR Gag domains of Rous sarcoma virusThe p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions.Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism.Triggering HIV polyprotein processing by light using rapid photodegradation of a tight-binding protease inhibitor.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.Ordered processing of the human immunodeficiency virus type 1 GagPol precursor is influenced by the context of the embedded viral proteaseSystematic mutational analysis of the active-site threonine of HIV-1 proteinase: rethinking the "fireman's grip" hypothesis.Exploration of subsite binding specificity of human cathepsin D through kinetics and rule-based molecular modeling.Sensitive, hydrosoluble, macromolecular fluorogenic substrates for human immunodeficiency virus 1 proteinase
P2860
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P2860
Sensitive, soluble chromogenic substrates for HIV-1 proteinase
description
1990 nî lūn-bûn
@nan
1990 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Sensitive, soluble chromogenic substrates for HIV-1 proteinase
@ast
Sensitive, soluble chromogenic substrates for HIV-1 proteinase
@en
Sensitive, soluble chromogenic substrates for HIV-1 proteinase
@nl
type
label
Sensitive, soluble chromogenic substrates for HIV-1 proteinase
@ast
Sensitive, soluble chromogenic substrates for HIV-1 proteinase
@en
Sensitive, soluble chromogenic substrates for HIV-1 proteinase
@nl
prefLabel
Sensitive, soluble chromogenic substrates for HIV-1 proteinase
@ast
Sensitive, soluble chromogenic substrates for HIV-1 proteinase
@en
Sensitive, soluble chromogenic substrates for HIV-1 proteinase
@nl
P2093
P1476
Sensitive, soluble chromogenic substrates for HIV-1 proteinase
@en
P2093
Farmerie WG
Pavlickova L
Richards AD
Scarborough PE
P304
P407
P577
1990-05-01T00:00:00Z