DNA Polymerase β: Structure−Fidelity Relationship from Pre-Steady-State Kinetic Analyses of All Possible Correct and Incorrect Base Pairs for Wild Type and R283A Mutant-Reference-Cited by-同舟云学术

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DNA Polymerase β: Structure−Fidelity Relationship from Pre-Steady-State Kinetic Analyses of All Possible Correct and Incorrect Base Pairs for Wild Type and R283A Mutant

Published:1997-02-01 Issue:5 Volume:36 Page:1100-1107
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Ahn Jinwoo¹,Werneburg Brian G.¹,Tsai Ming-Daw¹

Affiliation:

1. Department of Chemistry, The Ohio State University, Columbus, Ohio 43210

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi961653o

Reference28 articles.

1. The fidelity of DNA synthesis catalyzed by derivatives of Escherichia coli DNA polymerase I.

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2. Structural Insights into Phosphorylation-Mediated Polymerase Function Loss for DNA Polymerase β Bound to Gapped DNA;International Journal of Molecular Sciences;2023-05-19

3. Dynamic basis for dA•dGTP and dA•d8OGTP misincorporation via Hoogsteen base pairs;Nature Chemical Biology;2023-04-24

4. Dynamic basis for dA-dGTP and dA-d8OGTP misincorporation via Hoogsteen base pairs;2022-09-12

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