A Miniprotein Scaffold Used to Assemble the Polyproline II Binding Epitope Recognized by SH3 Domains
- 3 September 2004
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 342 (1) , 355-365
- https://doi.org/10.1016/j.jmb.2004.06.078
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Thermodynamic Dissection of the Binding Energetics of Proline-rich Peptides to the Abl-SH3 Domain: Implications for Rational Ligand DesignJournal of Molecular Biology, 2004
- Rational Development of Cell‐Penetrating High Affinity SH3 Domain Binding Peptides That Selectively Disrupt the Signal Transduction of Crk Family AdaptersAnnals of the New York Academy of Sciences, 1999
- Crystal structure of the abl-SH3 domain complexed with a designed high-affinity peptide ligand: implications for SH3-ligand interactionsJournal of Molecular Biology, 1998
- An intramolecular SH3-domain interaction regulates c-Abl activityNature Genetics, 1998
- Three-dimensional structure of the tyrosine kinase c-SrcNature, 1997
- Rational Design of Specific High-Affinity Peptide Ligands for the Abl-SH3 DomainBiochemistry, 1996
- Characterization of the Interaction of Natural Proline-Rich Peptides with Five Different SH3 DomainsBiochemistry, 1994
- Identification of a Ten-Amino Acid Proline-Rich SH3 Binding SiteScience, 1993
- Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1992
- Heat capacity of proteinsJournal of Molecular Biology, 1990