Kinetic Isotope Effects Support the Twisted Amide Mechanism of Pin1 Peptidyl-Prolyl Isomerase-Reference-Cited by-同舟云学术

Kinetic Isotope Effects Support the Twisted Amide Mechanism of Pin1 Peptidyl-Prolyl Isomerase

Published:2013-10-24 Issue:44 Volume:52 Page:7707-7713
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Mercedes-Camacho Ana Y.¹²,Mullins Ashley B.¹,Mason Matthew D.¹,Xu Guoyan G.¹,Mahoney Brendan J.³,Wang Xingsheng³,Peng Jeffrey W.³,Etzkorn Felicia A.¹²

Affiliation:

1. Department of Chemistry, Virginia Tech, Blacksburg, Virginia 24061, United States

2. Department of Biochemistry, Virginia Tech, Blacksburg, Virginia 24061, United States

3. Department of Chemistry and Biochemistry, University of Notre Dame, 251 Nieuwland Science Hall, Notre Dame, Indiana 46556, United States

Funder

NIH Office of the Director

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi400700b

Reference43 articles.

1. A human peptidyl–prolyl isomerase essential for regulation of mitosis

2. Sequence-Specific and Phosphorylation-Dependent Proline Isomerization: A Potential Mitotic Regulatory Mechanism

3. Peptidyl-Prolylcis/trans Isomerases and Their Effectors

4. Structural and Functional Analysis of the Mitotic Rotamase Pin1 Suggests Substrate Recognition Is Phosphorylation Dependent

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