Mechanistic Study of Protein Phosphatase-1 (PP1), A Catalytically Promiscuous Enzyme-Reference-Cited by-同舟云学术

Mechanistic Study of Protein Phosphatase-1 (PP1), A Catalytically Promiscuous Enzyme

Published:2008-09-18 Issue:41 Volume:130 Page:13673-13682
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

McWhirter Claire¹,Lund Elizabeth A.¹,Tanifum Eric A.¹,Feng Guoqiang¹,Sheikh Qaiser I.¹,Hengge Alvan C.¹,Williams Nicholas H.¹

Affiliation:

1. Department of Chemistry and Biochemistry, Utah State University, Logan, Utah 84322-0300, and Centre for Chemical Biology, Department of Chemistry, University of Sheffield, Sheffield, U.K. S3 7HF

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja803612z

Reference49 articles.

1. Inhibitory effect of okadaic acid on the p-nitrophenyl phosphate phosphatase activity of protein phosphatases

2. Crystal Structure of the Catalytic Subunit of Human Protein Phosphatase 1 and its Complex with Tungstate

3. Crystal structures of human calcineurin and the human FKBP12–FK506–calcineurin complex

4. Structural Basis for the Catalytic Activity of Human Serine/Threonine Protein Phosphatase-5

5. Identification of Protein-Phosphatase-1-Binding Domains on the Glycogen and Myofibrillar Targetting Subunits

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