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January 1, 2001Journal of Biological ChemistryOpen Access

The N-terminal End of Nebulin Interacts with Tropomodulin at the Pointed Ends of the Thin Filaments

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Authors

AMAbigail McElhinnyCox & Company (United States)BKBernhard KolmererEuropean Molecular Biology Laboratory VFVelia M. FowlerHeart Failure & Transplant

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Implication

Nebulin may template thin filament length with Tmod; leaves open its role in cardiac sarcomere disorders.

Key Points

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Cite This Study

McElhinny et al. (2001) studied this question.

synapsesocial.com/papers/6a7c7424112960c341fd6356 https://doi.org/10.1074/jbc.m005693200

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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

1Calmodulin-Sensitive Interaction of Human Nebulin Fragments with Actin and Myosin1994 · 82 citations
2Nebulette: A 107 kD nebulin‐like protein in cardiac muscle1995 · 165 citations
3Identification of a Novel Tropomodulin Isoform, Skeletal Tropomodulin, That Caps Actin Filament Pointed Ends in Fast Skeletal Muscle1999 · 116 citations
4Tropomyosin prevents depolymerization of actin filaments from the pointed end.1990 · 115 citations
5DEFINING ACTIN FILAMENT LENGTH IN STRIATED MUSCLE: Rulers and Caps or Dynamic Stability?1998 · 140 citations