Substrate requirements for secondary cleavage by HIV-1 reverse transcriptase RNase H.
about
Two-metal ion mechanism of RNA cleavage by HIV RNase H and mechanism-based design of selective HIV RNase H inhibitorsRNase H activity: structure, specificity, and function in reverse transcriptionRibonuclease H: properties, substrate specificity and roles in retroviral reverse transcriptionDuplex structural differences and not 2'-hydroxyls explain the more stable binding of HIV-reverse transcriptase to RNA-DNA versus DNA-DNA.Subtype-associated differences in HIV-1 reverse transcription affect the viral replication.Sequence, distance, and accessibility are determinants of 5'-end-directed cleavages by retroviral RNases H.HIV-1 reverse transcriptase connection subdomain mutations reduce template RNA degradation and enhance AZT excisionSpecific cleavages by RNase H facilitate initiation of plus-strand RNA synthesis by Moloney murine leukemia virus.Human immunodeficiency virus type 2 reverse transcriptase activity in model systems that mimic steps in reverse transcription.Reverse transcriptase and integrase of the Saccharomyces cerevisiae Ty1 element.Zinc finger function of HIV-1 nucleocapsid protein is required for removal of 5'-terminal genomic RNA fragments: a paradigm for RNA removal reactions in HIV-1 reverse transcription.Structure/function mapping of amino acids in the N-terminal zinc finger of the human immunodeficiency virus type 1 nucleocapsid protein: residues responsible for nucleic acid helix destabilizing activityA new role for HIV nucleocapsid protein in modulating the specificity of plus strand priming.Efavirenz stimulates HIV-1 reverse transcriptase RNase H activity by a mechanism involving increased substrate binding and secondary cleavage activity.Preferred sequences within a defined cleavage window specify DNA 3' end-directed cleavages by retroviral RNases HTemplate dimerization promotes an acceptor invasion-induced transfer mechanism during human immunodeficiency virus type 1 minus-strand synthesis.Dissection of a circumscribed recombination hot spot in HIV-1 after a single infectious cycle.Extension and cleavage of the polypurine tract plus-strand primer by Ty1 reverse transcriptase.Developing and evaluating inhibitors against the RNase H active site of HIV-1 RT.Mechanisms that prevent template inactivation by HIV-1 reverse transcriptase RNase H cleavages.Mechanistic analysis of pause site-dependent and -independent recombinogenic strand transfer from structurally diverse regions of the HIV genome.Evidence that HIV-1 reverse transcriptase employs the DNA 3' end-directed primary/secondary RNase H cleavage mechanism during synthesis and strand transfer.
P2860
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P2860
Substrate requirements for secondary cleavage by HIV-1 reverse transcriptase RNase H.
description
2002 nî lūn-bûn
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2002年の論文
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2002年学术文章
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name
Substrate requirements for secondary cleavage by HIV-1 reverse transcriptase RNase H.
@en
Substrate requirements for secondary cleavage by HIV-1 reverse transcriptase RNase H.
@nl
type
label
Substrate requirements for secondary cleavage by HIV-1 reverse transcriptase RNase H.
@en
Substrate requirements for secondary cleavage by HIV-1 reverse transcriptase RNase H.
@nl
prefLabel
Substrate requirements for secondary cleavage by HIV-1 reverse transcriptase RNase H.
@en
Substrate requirements for secondary cleavage by HIV-1 reverse transcriptase RNase H.
@nl
P2093
P2860
P356
P1476
Substrate requirements for secondary cleavage by HIV-1 reverse transcriptase RNase H.
@en
P2093
Bernard P Roques
Chockalingam Palaniappan
Michele Wisniewski
Mini Balakrishnan
Philip J Fay
Robert A Bambara
P2860
P304
28400-28410
P356
10.1074/JBC.M201645200
P407
P577
2002-05-21T00:00:00Z