Mechanistic Studies of Protein Tyrosine Phosphatases YopH and Cdc25A with m-Nitrobenzyl Phosphate-Reference-Cited by-同舟云学术

Mechanistic Studies of Protein Tyrosine Phosphatases YopH and Cdc25A with m-Nitrobenzyl Phosphate

Published:2004-06-01 Issue:25 Volume:43 Page:8256-8264
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

McCain Daniel F.¹,Grzyska Piotr K.¹,Wu Li¹,Hengge Alvan C.¹,Zhang Zhong-Yin¹

Affiliation:

1. Departments of Biochemistry and Molecular Pharmacology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, and Department of Chemistry and Biochemistry, Utah State University, Logan, Utah 84322

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi0496182

Reference38 articles.

1. Hengge, A. C., Sowa, G., Wu, L., and Zhang, Z.Y. (1995) Nature of the transition state of the protein-tyrosine phosphatase-catalyzed reaction,Biochemistry34, 13982−13987.

2. Hengge, A. C., Zhao, Y., Wu, L., and Zhang, Z.Y. (1997) Examination of the transition state of the low-molecular mass tyrosine phosphatase 1. Comparisons with other protein phosphatases,Biochemistry36, 7928−7936.

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