Structural basis for the binding of proline-rich peptides to SH3 domains
Open Access
- 1 March 1994
- journal article
- research article
- Published by Elsevier BV in Cell
- Vol. 76 (5), 933-945
- https://doi.org/10.1016/0092-8674(94)90367-0
Abstract
No abstract availableThis publication has 53 references indexed in Scilit:
- Biased combinatorial libraries: novel ligands for the SH3 domain of phosphatidylinositol 3-kinaseJournal of the American Chemical Society, 1993
- SH2 and SH3 domainsCurrent Biology, 1993
- 1H and 15N assignments and secondary structure of the PI3K SH3 domainFEBS Letters, 1993
- Identification of a Ten-Amino Acid Proline-Rich SH3 Binding SiteScience, 1993
- Left-handed Polyproline II Helices Commonly Occur in Globular ProteinsJournal of Molecular Biology, 1993
- Phosphatidylinositol 3-kinase: Structure and expression of the 110 kd catalytic subunitCell, 1992
- SH3 — an abundant protein domain in search of a functionFEBS Letters, 1992
- Cloning of PI3 kinase-associated p85 utilizing a novel method for expression/cloning of target proteins for receptor tyrosine kinasesCell, 1991
- The colony stimulating factor-1 receptor associates with and activates phosphatidylinositol-3 kinaseNature, 1989
- Primary structure of human proacrosin deduced from its cDNA sequenceFEBS Letters, 1989