Deleting nebulin's C-terminus reveals its importance to sarcomeric structure and function and is sufficient to invoke nemaline myopathy
Author:
Affiliation:
1. Department of Cellular and Molecular Medicine, University of Arizona, Tucson, Arizona, USA
2. Department of Applied Physiology and Kinesiology, University of Florida, Gainesville, Florida, USA
Funder
National Institute of Arthritis and Musculoskeletal and Skin Diseases
Foundation Building Strength
Publisher
Oxford University Press (OUP)
Subject
Genetics (clinical),Genetics,Molecular Biology,General Medicine
Link
http://academic.oup.com/hmg/article-pdf/28/10/1709/28548824/ddz016.pdf
Reference48 articles.
1. Nebulin, a helical actin binding protein;Pfuhl;EMBO J.,1994
2. Evidence that nebulin is a protein-ruler in muscle thin filaments;Labeit;FEBS Lett.,1991
3. The complete primary structure of human nebulinand its correlation to muscle structure;Labeit;J. Mol. Biol.,1995
4. Human skeletal muscle nebulin sequence encodes a blueprint for thin filament architecture. Sequence motifs and affinity profiles of tandem repeats and terminal SH3;Wang;J. Biol. Chem.,1996
5. Nebulin as a length regulator of thin-filaments of vertebrate skeletal-muscles—correlation of thin filament length, nebulin size, and epitope profile;Kruger;J. Cell Biol.,1991
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