Visualizing the Induced Binding of SH2-Phosphopeptide-Reference-Cited by-同舟云学术

Visualizing the Induced Binding of SH2-Phosphopeptide

Published:2012-03-15 Issue:4 Volume:8 Page:1171-1175
ISSN:1549-9618
Container-title:Journal of Chemical Theory and Computation
language:en
Short-container-title:J. Chem. Theory Comput.

Author:

Giorgino T.¹²,Buch I.¹,De Fabritiis G.¹

Affiliation:

1. Computational Biochemistry and Biophysics Laboratory (GRIB-IMIM), Universitat Pompeu Fabra, Barcelona Biomedical Research Park, C/Dr. Aiguader 88, 08003 Barcelona, Spain

2. Institute of Biomedical Engineering, CNR - National Research Council of Italy, Corso Stati Uniti 4, 35127 Padova, Italy

Publisher

American Chemical Society (ACS)

Subject

Physical and Theoretical Chemistry,Computer Science Applications

Link

https://pubs.acs.org/doi/pdf/10.1021/ct300003f

Reference29 articles.

1. The Human and Mouse Complement of SH2 Domain Proteins—Establishing the Boundaries of Phosphotyrosine Signaling

2. Kinetics of p56lck and p60src Src homology 2 domain binding to tyrosine-phosphorylated peptides determined by a competition assay or surface plasmon resonance.

3. SH2-Directed Ligands of the Lck Tyrosine Kinase

4. Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck

5. Structural and Thermodynamic Basis for the Interaction of the Src SH2 Domain with the Activated Form of the PDGF β-receptor

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