The WW Domain of Dystrophin Requires EF-Hands Region to Interact with β-Dystroglycan
Author:
Publisher
Walter de Gruyter GmbH
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
Link
https://www.degruyter.com/document/doi/10.1515/BC.1999.057/pdf
Reference59 articles.
1. An intact cysteine-rich domain is required for dystrophin function.
2. An efficient method for anchoring fmoc-anino acids to hydroxyl-functionalised solid supports
3. The WW domain: a signalling site in dystrophin?
4. A cDNA clone from the Duchenne/Becker muscular dystrophy gene
5. Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains.
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