Structural Basis for High-Affinity Peptide Inhibition of Human Pin1-Reference-Cited by-同舟云学术

Structural Basis for High-Affinity Peptide Inhibition of Human Pin1

Published:2007-05-01 Issue:5 Volume:2 Page:320-328
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Zhang Yan¹,Daum Sebastian²,Wildemann Dirk²,Zhou Xiao Zhen³,Verdecia Mark A.¹,Bowman Marianne E.¹,Lücke Christian²,Hunter Tony⁴,Lu Kun-Ping³,Fischer Gunter²,Noel Joseph P.¹

Affiliation:

1. Howard Hughes Medical Institute, The Jack H. Skirball Center for Chemical Biology and Proteomics, The Salk Institute for Biological Studies, La Jolla, California 92037

2. Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle/Saale, Germany

3. Cancer Biology Program, Division of Hematology/Oncology, Department of Medicine, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts 02215

4. Molecular and Cell Biology Laboratory, The Salk Institute for Biological Studies, La Jolla, California 92037

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/cb7000044

Reference55 articles.

1. Protein folding: Prolyl isomerases join the fold

2. Pharmacological Targeting of Catalyzed Protein Folding: The Example of Peptide Bond cis/trans Isomerases

3. Targeting carcinogenesis: A role for the prolyl isomerase Pin1?

4. Pin1 Flips Alzheimer’s Switch

5. Cyclophilin: A Specific Cytosolic Binding Protein for Cyclosporin A

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