The DOI matches its Crossref record; 309 of the 309 references it cites were found in a registry or an index.
Muscle Giants: Molecular Scaffolds in Sarcomerogenesis
Open accessAbstract
Myofibrillogenesis in striated muscles is a highly complex process that depends on the coordinated assembly and integration of a large number of contractile, cytoskeletal, and signaling proteins into regular arrays, the sarcomeres. It is also associated with the stereotypical assembly of the sarcoplasmic reticulum and the transverse tubules around each sarcomere. Three giant, muscle-specific proteins, titin (3–4 MDa), nebulin (600–800 kDa), and obscurin (∼720–900 kDa), have been proposed to play important roles in the assembly and stabilization of sarcomeres. There is a large amount of data showing that each of these molecules interacts with several to many different protein ligands, regulating their activity and localizing them to particular sites within or surrounding sarcomeres. Consistent with this, mutations in each of these proteins have been linked to skeletal and cardiac myopathies or to muscular dystrophies. The evidence that any of them plays a role as a “molecular template,” “molecular blueprint,” or “molecular ruler” is less definitive, however. Here we review the structure and function of titin, nebulin, and obscurin, with the literature supporting a role for them as scaffolding molecules and the contradictory evidence regarding their roles as molecular guides in sarcomerogenesis.
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Truncations of titin causing dilated cardiomyopathy
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Advances in the Genetic Basis and Pathogenesis of Sarcomere Cardiomyopathies
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Metadata
- Authors
- Kontrogianni-Konstantopoulos, A., Ackermann, M. A., Bowman, A. L., Yap, S. V., & Bloch, R. J.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2009-10
- Volume
- 89
- Issue
- 4
- Pages
- 1217-1267
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W1971161141
- Cited by
- 259
- References
- 309
- FWCI
- 0.88
- Type
- journal article
- Language
- en
- Open access
- green
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