Mutations in the RNase H primer grip domain of murine leukemia virus reverse transcriptase decrease efficiency and accuracy of plus-strand DNA transfer. - Wikidata - wikimedia - TriplyDB

Mutations in the RNase H primer grip domain of murine leukemia virus reverse transcriptase decrease efficiency and accuracy of plus-strand DNA transfer.

Mutations in the RNase H primer grip domain of murine leukemia virus reverse transcriptase decrease efficiency and accuracy of plus-strand DNA transfer.

http://www.wikidata.org/entity/Q37747347

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Thermostable DNA polymerase from a viral metagenome is a potent RT-PCR enzyme RNase H activity: structure, specificity, and function in reverse transcription Ribonuclease H: properties, substrate specificity and roles in retroviral reverse transcription Mutations in the connection domain of HIV-1 reverse transcriptase increase 3'-azido-3'-deoxythymidine resistance Mutation rates and intrinsic fidelity of retroviral reverse transcriptases.Altered error specificity of RNase H-deficient HIV-1 reverse transcriptases during DNA-dependent DNA synthesis.Examining Interactions of HIV-1 Reverse Transcriptase with Single-stranded Template Nucleotides by Nucleoside Analog Interference

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Mutations in the RNase H primer grip domain of murine leukemia virus reverse transcriptase decrease efficiency and accuracy of plus-strand DNA transfer.

http://www.wikidata.org/entity/Q37747347

description

article científic

@ca

article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on January 2005

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vedecký článok

@sk

vetenskaplig artikel

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videnskabelig artikel

@da

vědecký článek

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name

Mutations in the RNase H prime ...... y of plus-strand DNA transfer.

@en

Mutations in the RNase H prime ...... y of plus-strand DNA transfer.

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type

label

Mutations in the RNase H prime ...... y of plus-strand DNA transfer.

@en

Mutations in the RNase H prime ...... y of plus-strand DNA transfer.

@nl

prefLabel

Mutations in the RNase H prime ...... y of plus-strand DNA transfer.

@en

Mutations in the RNase H prime ...... y of plus-strand DNA transfer.

@nl

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JVI.79.1.419-427.2005

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Journal of Virology

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Mutations in the RNase H prime ...... y of plus-strand DNA transfer.

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Galina N Nikolenko

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Jean L Mbisa

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Vinay K Pathak

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P2860

Crystal structure of HIV-1 reverse transcriptase in complex with a polypurine tract RNA:DNA

Structure of chimeric duplex junctions: solution conformation of the retroviral Okazaki-like fragment r(ccca)d(AATGA).d(TCATTTGGG) from Moloney murine leukemia virus

Structural variation among retroviral primer-DNA junctions: solution structure of the HIV-1 (-)-strand Okazaki fragment r(gcca)d(CTGC).d(GCAGTGGC)

Crystal structure of an eight-base pair duplex containing the 3'-DNA-RNA-5' junction formed during initiation of minus-strand synthesis of HIV replication

Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance

Novel mutations in reverse transcriptase of human immunodeficiency virus type 1 reduce susceptibility to foscarnet in laboratory and clinical isolates

HIV population dynamics in vivo: implications for genetic variation, pathogenesis, and therapy

Influence of reverse transcriptase variants, drugs, and Vpr on human immunodeficiency virus type 1 mutant frequencies.

3'-Azido-3'-deoxythymidine (AZT) and AZT-resistant reverse transcriptase can increase the in vivo mutation rate of human immunodeficiency virus type 1.

Broad spectrum of in vivo forward mutations, hypermutations, and mutational hotspots in a retroviral shuttle vector after a single replication cycle: deletions and deletions with insertions.

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419-427

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10.1128/JVI.79.1.419-427.2005

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