Alteration of Tropomyosin Function and Folding by a Nemaline Myopathy-Causing Mutation
- 1 December 2000
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 79 (6) , 3217-3225
- https://doi.org/10.1016/s0006-3495(00)76554-4
Abstract
No abstract availableKeywords
This publication has 58 references indexed in Scilit:
- Tropomodulin Increases the Critical Concentration of Barbed End-capped Actin Filaments by Converting ADP·Pi-actin to ADP-actin at All Pointed Filament EndsJournal of Biological Chemistry, 1999
- The muscle thin filament as a classical cooperative/allosteric regulatory systemJournal of Molecular Biology, 1998
- MOLMOL: A program for display and analysis of macromolecular structuresJournal of Molecular Graphics, 1996
- Mapping the Functional Domains within the Carboxyl Terminus of α-Tropomyosin Encoded by the Alternatively Spliced Ninth ExonPublished by Elsevier ,1996
- A mutation in the α tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathyNature Genetics, 1995
- Tropomodulin is associated with the free (pointed) ends of the thin filaments in rat skeletal muscle.The Journal of cell biology, 1993
- X-Ray Structure of the GCN4 Leucine Zipper, a Two-Stranded, Parallel Coiled CoilScience, 1991
- Organization of the hTMnm geneJournal of Molecular Biology, 1988
- Tropomyosin Binding to F-Actin Induced by Myosin HeadsScience, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970