Thermodynamic Basis for Promiscuity and Selectivity in Protein−Protein Interactions: PDZ Domains, a Case Study-Reference-Cited by-同舟云学术

Thermodynamic Basis for Promiscuity and Selectivity in Protein−Protein Interactions: PDZ Domains, a Case Study

Published:2006-09-09 Issue:39 Volume:128 Page:12766-12777
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Basdevant Nathalie¹,Weinstein Harel¹,Ceruso Marco¹

Affiliation:

1. Contribution from the Department of Chemistry, CUNY College of Staten Island, 2800 Victory Boulevard, Staten Island, New York 10314, Department of Physiology and Biophysics, and HRH Prince Alwaleed Bin Talal Bin Abdulaziz Alsaud Institute for Computational Biomedicine, Weill Medical College of Cornell University, 1300 York Avenue, New York, New York 10021

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja060830y

Reference94 articles.

1. Modular Protein Domains

2. From Src Homology domains to other signaling modules: proposal of the `protein recognition code'

3. Crystal Structures of a Complexed and Peptide-Free Membrane Protein–Binding Domain: Molecular Basis of Peptide Recognition by PDZ

4. PDZ domains - common players in the cell signaling.

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