Thermodynamic and Kinetic Analysis of Peptides Derived from CapZ, NDR, p53, HDM2, and HDM4 Binding to Human S100B-Reference-Cited by-同舟云学术

Thermodynamic and Kinetic Analysis of Peptides Derived from CapZ, NDR, p53, HDM2, and HDM4 Binding to Human S100B

Published:2012-08-29 Issue:36 Volume:51 Page:7189-7201
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Wafer Lucas N.¹,Streicher Werner W.¹,McCallum Scott A.¹,Makhatadze George I.¹

Affiliation:

1. Center for Biotechnology and Interdisciplinary Studies and Department of Biology, Rensselaer Polytechnic Institute, 110 8th Street, Troy, New York 12180, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi300865g

Reference114 articles.

1. The S100 family of EF-hand calcium-binding proteins: functions and pathology

2. Ca2+-dependent regulation of vascular smooth-muscle caldesmon by S.100 and related smooth-muscle proteins

3. S100B(ββ) inhibits the protein kinase C‐dependent phosphorylation of a peptide derived from p53 in a Ca 2+ ‐dependent manner

4. Ca2+ /S100 regulation of giant protein kinases

5. Structure of the Ca2+/S100B/NDR Kinase Peptide Complex: Insights into S100 Target Specificity and Activation of the Kinase

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