(Q27498357)

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Influence of the RNase H domain of retroviral reverse transcriptases on the metal specificity and substrate selection of their polymerase domains

scientific article (publication date: 2009)

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Influence of the RNase H domain of retroviral reverse transcriptases on the metal specificity and substrate selection of their polymerase domains (English)

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author name string

Tanaji T Talele

1

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Alok Upadhyay

2

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Virendra N Pandey

3

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publication date

2009

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Virology Journal

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6

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1

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159

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describes a project that uses

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Image Quant

1 reference

CZ Software Mentions: A large dataset of software mentions in the biomedical literature

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1 reference

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Co-crystal of Escherichia coli RNase HI with Mn2+ ions reveals two divalent metals bound in the active site

1 reference

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1 reference

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DNA sequencing with chain-terminating inhibitors

1 reference

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20 March 2017

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1 reference

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20 March 2017

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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2 June 2018

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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Substituting a conserved residue of the ribonuclease H domain alters substrate hydrolysis by retroviral reverse transcriptase

1 reference

https://pubmed.ncbi.nlm.nih.gov/19814799

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Mutations within the primer grip region of HIV-1 reverse transcriptase result in loss of RNase H function

1 reference

https://pubmed.ncbi.nlm.nih.gov/19814799

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A detailed model of reverse transcription and tests of crucial aspects

1 reference

https://pubmed.ncbi.nlm.nih.gov/19814799

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1186/1743-422X-6-159

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Dimensions Publication ID

1 reference

9 September 2019

https://scigraph.springernature.com/pub.10.1186/1743-422x-6-159

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PubMed publication ID

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