Characterization of the WW Domain of Human Yes-associated Protein and Its Polyproline-containing Ligands
Open Access
- 1 July 1997
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (27) , 17070-17077
- https://doi.org/10.1074/jbc.272.27.17070
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptideNature, 1996
- Towards prediction of cognate complexes between the WW domain and proline‐rich ligandsFEBS Letters, 1996
- Liddle disease caused by a missense mutation of beta subunit of the epithelial sodium channel gene.Journal of Clinical Investigation, 1996
- Structure and function of the WW domainProgress in Biophysics and Molecular Biology, 1996
- Characterization of a novel protein‐binding module — the WW domainFEBS Letters, 1995
- An Alternative to SH2 Domains for Binding Tyrosine-Phosphorylated ProteinsScience, 1994
- Alveolar soft‐part sarcoma: evidence for its myogenic origin and for the involvement of 17q25Histopathology, 1993
- SH2 and SH3 domainsCurrent Biology, 1993
- SH2 domains recognize specific phosphopeptide sequencesPublished by Elsevier ,1993
- MOLSCRIPT: a program to produce both detailed and schematic plots of protein structuresJournal of Applied Crystallography, 1991