Mechanism of Folding and Binding of the N-Terminal SH2 Domain from SHP2
Author:
Affiliation:
1. Istituto Pasteur, Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche “A. Rossi Fanelli” and Istituto di Biologia e Patologia Molecolari del CNR, Sapienza Università di Roma, 00185, Rome, Italy
Funder
Ministero dell?Istruzione, dell?Universit? e della Ricerca
Sapienza Universit? di Roma
Associazione Italiana per la Ricerca sul Cancro
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.8b05651
Reference36 articles.
1. What Have We Learned from SH2 Domains?
2. Aberrant Folding of a Mutant Stat5b Causes Growth Hormone Insensitivity and Proteasomal Dysfunction
3. Phosphorylated Calmodulin Promotes PI3K Activation by Binding to the SH2 Domains
4. Sialic acids and autoimmune disease
5. Targeting SH2 domains in breast cancer
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3. Fluorescence Anisotropy and Polarization in the Characterization of Biomolecular Association Processes and Their Application to Study SH2 Domain Binding Affinity;Methods in Molecular Biology;2023
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