Two defective forms of reverse transcriptase can complement to restore retroviral infectivity
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RNase H activity: structure, specificity, and function in reverse transcriptionRibonuclease H: properties, substrate specificity and roles in retroviral reverse transcriptionCommon and unique features of viral RNA-dependent polymerasesHIV-1 reverse transcriptionStructural and Binding Analysis of Pyrimidinol Carboxylic Acid and N-Hydroxy Quinazolinedione HIV-1 RNase H InhibitorsTracking interspecies transmission and long-term evolution of an ancient retrovirus using the genomes of modern mammalsRelative rates of retroviral reverse transcriptase template switching during RNA- and DNA-dependent DNA synthesis.A map of interactions between the proteins of a retrotransposonIn vitro analysis of human immunodeficiency virus type 1 minus-strand strong-stop DNA synthesis and genomic RNA processing.A Ty1 reverse transcriptase active-site aspartate mutation blocks transposition but not polymerizationReplication of phenotypically mixed human immunodeficiency virus type 1 virions containing catalytically active and catalytically inactive reverse transcriptase.Mutations that abrogate human immunodeficiency virus type 1 reverse transcriptase dimerization affect maturation of the reverse transcriptase heterodimer.Dynamic copy choice: steady state between murine leukemia virus polymerase and polymerase-dependent RNase H activity determines frequency of in vivo template switching.Mutations in the RNase H domain of HIV-1 reverse transcriptase affect the initiation of DNA synthesis and the specificity of RNase H cleavage in vivo.Reduced fitness in cell culture of HIV-1 with nonnucleoside reverse transcriptase inhibitor-resistant mutations correlates with relative levels of reverse transcriptase content and RNase H activity in virions.HIV-1 Ribonuclease H: Structure, Catalytic Mechanism and Inhibitors.Mutation of the catalytic domain of the foamy virus reverse transcriptase leads to loss of processivity and infectivity.Crystal structure of the moloney murine leukemia virus RNase H domainUnique progressive cleavage mechanism of HIV reverse transcriptase RNase HBiochemical, inhibition and inhibitor resistance studies of xenotropic murine leukemia virus-related virus reverse transcriptase.Multiple effects of mutations in human immunodeficiency virus type 1 integrase on viral replicationEffects on DNA synthesis and translocation caused by mutations in the RNase H domain of Moloney murine leukemia virus reverse transcriptaseDetection of an RNase H activity associated with hepadnaviruses.RNase H domain of Moloney murine leukemia virus reverse transcriptase retains activity but requires the polymerase domain for specificity.The remarkable frequency of human immunodeficiency virus type 1 genetic recombinationRNase H activity is required for high-frequency repeat deletion during Moloney murine leukemia virus replication.Mutations of the RNase H C helix of the Moloney murine leukemia virus reverse transcriptase reveal defects in polypurine tract recognition.
P2860
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P2860
Two defective forms of reverse transcriptase can complement to restore retroviral infectivity
description
1993 nî lūn-bûn
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1993年の論文
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1993年学术文章
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1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
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1993年學術文章
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name
Two defective forms of reverse ...... restore retroviral infectivity
@en
type
label
Two defective forms of reverse ...... restore retroviral infectivity
@en
prefLabel
Two defective forms of reverse ...... restore retroviral infectivity
@en
P2860
P1433
P1476
Two defective forms of reverse ...... restore retroviral infectivity
@en
P2093
A Telesnitsky
P2860
P304
P356
10.1002/J.1460-2075.1993.TB06128.X
P407
P577
1993-11-01T00:00:00Z