Autoprocessing of the HIV-1 protease using purified wild-type and mutated fusion proteins expressed at high levels in Escherichia coli.
about
Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fusedSingle amino acid substitutions on the surface of Escherichia coli maltose-binding protein can have a profound impact on the solubility of fusion proteinsAntiviral properties of aminodiol inhibitors against human immunodeficiency virus and proteaseCharacterization of a human immunodeficiency virus type 1 variant with reduced sensitivity to an aminodiol protease inhibitorEffect of substrate residues on the P2' preference of retroviral proteinasesHuman immunodeficiency virus type 1 viral background plays a major role in development of resistance to protease inhibitorsAdaptive control strategy for maintaining dissolved oxygen concentration in high density growth of recombinant E. coli.Understanding HIV-1 protease autoprocessing for novel therapeutic development.A circularly permuted recombinant interleukin 4 toxin with increased activity.Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyproteinProteolytic 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.Human immunodeficiency virus type 1 gag-protease fusion proteins are enzymatically active.Processing of avian retroviral gag polyprotein precursors is blocked by a mutation at the NC-PR cleavage site.HIV-1 protease dimer interface mutations that compensate for viral reverse transcriptase instability in infectious virions.Importance of the N terminus of rous sarcoma virus protease for structure and enzymatic function.Human immunodeficiency virus type 1 (HIV-1) protein Vif inhibits the activity of HIV-1 protease in bacteria and in vitro.The gag precursor contains a specific HIV-1 protease cleavage site between the NC (P7) and P1 proteins.Efavirenz enhances the proteolytic processing of an HIV-1 pol polyprotein precursor and reverse transcriptase homodimer formation.Comparison of the substrate specificity of the human T-cell leukemia virus and human immunodeficiency virus proteinases.Stabilization from autoproteolysis and kinetic characterization of the human T-cell leukemia virus type 1 proteinase.Context-dependent autoprocessing of human immunodeficiency virus type 1 protease precursors.Effect of glucose supply strategy on acetate accumulation, growth, and recombinant protein production by Escherichia coli BL21 (lambdaDE3) and Escherichia coli JM109.A transient precursor of the HIV-1 protease. Isolation, characterization, and kinetics of maturation.
P2860
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P2860
Autoprocessing of the HIV-1 protease using purified wild-type and mutated fusion proteins expressed at high levels in Escherichia coli.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
1991年學術文章
@zh
1991年學術文章
@zh-hant
name
Autoprocessing of the HIV-1 pr ...... gh levels in Escherichia coli.
@en
type
label
Autoprocessing of the HIV-1 pr ...... gh levels in Escherichia coli.
@en
prefLabel
Autoprocessing of the HIV-1 pr ...... gh levels in Escherichia coli.
@en
P2093
P2860
P1433
P1476
Autoprocessing of the HIV-1 pr ...... gh levels in Escherichia coli.
@en
P2093
D M Jerina
E M Wondrak
N T Nashed
R A McDonald
S Oroszlan
P2860
P304
P356
10.1111/J.1432-1033.1991.TB16132.X
P407
P577
1991-07-01T00:00:00Z