Sequence analysis suggests the presence of an IG-like domain in the N-terminal region of α-dystroglycan which was crystallized after mutation of a protease susceptible site (Arg168 → His)-Reference-Cited by-同舟云学术

Sequence analysis suggests the presence of an IG-like domain in the N-terminal region of α-dystroglycan which was crystallized after mutation of a protease susceptible site (Arg168 → His)

Published:1998-11 Issue:7 Volume:17 Page:495-500
ISSN:0945-053X
Container-title:Matrix Biology
language:en
Short-container-title:Matrix Biology

Author:

Bozic Damir,Engel Jürgen,Brancaccio Andrea

Funder

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung

Publisher

Elsevier BV

Subject

Molecular Biology

Reference17 articles.

1. Site directed mutagenesis by double polymerase chain reaction. Megaprimer method;Barik,1993

2. Structure and distribution of modules in extracellular proteins;Bork;Quart. Rev. Biophys.,1996

3. Cloning and sequencing of mouse skeletal muscle α-dystroglycan;Brancaccio;Matrix Biol.,1995

4. Electron microscopic evidence for a mucin-like region in chick muscle α-dystroglycan;Brancaccio;FEBS Lett.,1995

5. The N-terminal region of α-dystroglycan is an autonomous globular domain;Brancaccio;Eur. J. Biochem.,1997

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