Intrinsic activity of precursor forms of HIV-1 proteinase.
about
Multiple functions of pro-parts of aspartic proteinase zymogens.A p6Pol-protease fusion protein is present in mature particles of human immunodeficiency virus type 1.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.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.Importance of protease cleavage sites within and flanking human immunodeficiency virus type 1 transframe protein p6* for spatiotemporal regulation of protease activation.Competitive inhibition of human immunodeficiency virus type-1 protease by the Gag-Pol transframe protein.Activity of tethered human immunodeficiency virus 1 protease containing mutations in the flap region of one subunit.Ribosomal frameshifting at the Gag-Pol junction in avian leukemia sarcoma virus forms a novel cleavage site.Proteolytic processing of HIV-1 protease precursor, kinetics and mechanism.
P2860
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P2860
Intrinsic activity of precursor forms of HIV-1 proteinase.
description
1992 nî lūn-bûn
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1992年の論文
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1992年学术文章
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1992年学术文章
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name
Intrinsic activity of precursor forms of HIV-1 proteinase.
@en
Intrinsic activity of precursor forms of HIV-1 proteinase.
@nl
type
label
Intrinsic activity of precursor forms of HIV-1 proteinase.
@en
Intrinsic activity of precursor forms of HIV-1 proteinase.
@nl
prefLabel
Intrinsic activity of precursor forms of HIV-1 proteinase.
@en
Intrinsic activity of precursor forms of HIV-1 proteinase.
@nl
P2093
P2860
P1433
P1476
Intrinsic activity of precursor forms of HIV-1 proteinase.
@en
P2093
P2860
P304
P356
10.1016/0014-5793(92)81524-P
P407
P577
1992-12-01T00:00:00Z