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August 1, 1994Journal of Applied Physiology

Myosin isoforms in mammalian skeletal muscle

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Population

Mammalian skeletal muscle

Design

Review

Authors

SSStefano SchiaffinoGeneral CardiologyCRCarlo ReggianiGeneral Cardiology

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Overview

May refine skeletal muscle models; leaves open validation in cardiac or clinical contexts.

Structured PICO

P
Population
Mammalian skeletal muscle

This review summarizes the distribution, regulation, and functional role of myosin heavy and light chain isoforms in determining the contractile properties of mammalian skeletal muscle fibers.

Cite This Study

Schiaffino et al. (1994) studied this question.

synapsesocial.com/papers/6a81b2aeebcdd2e0baf1f986https://doi.org/10.1152/jappl.1994.77.2.493
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Also Consider

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

  1. 1Characterization of human myosin light chains 1sa and 3nm: implications for isoform evolution and function.1990 · 51 citations
  2. 2Identification of a novel type 2 fiber population in mammalian skeletal muscle by combined use of histochemical myosin ATPase and anti-myosin monoclonal antibodies.1990 · 279 citations
  3. 3Polymorphism of myofibrillar proteins of rabbit skeletal-muscle fibres. An electrophoretic study of single fibres1982 · 119 citations
  4. 4Myosin alkali light chain and heavy chain variations correlate with altered shortening velocity of isolated skeletal muscle fibers.1988 · 238 citations
  5. 5Organization of the human skeletal myosin heavy chain gene cluster.1992 · 52 citations