Altered Order of Substrate Binding by DNA Polymerase X from African Swine Fever Virus-Reference-Cited by-同舟云学术

Altered Order of Substrate Binding by DNA Polymerase X from African Swine Fever Virus

Published:2008-07-01 Issue:30 Volume:47 Page:7875-7887
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kumar Sandeep¹,Bakhtina Marina¹,Tsai Ming-Daw¹

Affiliation:

1. Department of Chemistry, The Ohio State University, Columbus, Ohio 43210, and Genomics Research Center and Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi800731m

Reference47 articles.

1. The steady state kinetic parameters and non-processivity of Escherichia coli deoxyribonucleic acid polymerase I

2. Ordered sequential mechanism of substrate recognition and binding by KB cell DNA polymerase .alpha.

3. Studies on the mechanism of human immunodeficiency virus reverse transcriptase. Steady-state kinetics, processivity, and polynucleotide inhibition.

4. Steady-state kinetics of mouse DNA polymerase .beta.

5. Specificity of the catalytic interaction of human DNA polymerase .beta. with nucleic acid substrates

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