Myosin alkali light chain and heavy chain variations correlate with altered shortening velocity of isolated skeletal muscle fibers.

This publication has 22 references indexed in Scilit:

• The multiplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibres. Rabbit soleus muscle
  Biochemical Journal, 1987
• ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle.
  Proceedings of the National Academy of Sciences, 1985
• Characterization of rabbit masseter muscle fibers
  Muscle & Nerve, 1984
• Mechanical properties and myosin light chain composition of skinned muscle fibres from adult and new‐born rabbits.
  The Journal of Physiology, 1981
• Distribution of light chains in fast skeletal myosin
  Nature, 1979
• Studies on the Actin Activation of Myosin Subfragment‐1 Isoenzymes and the Role of Myosin Light Chains
  European Journal of Biochemistry, 1979
• The velocity of unloaded shortening and its relation to sarcomere length and isometric force in vertebrate muscle fibres.
  The Journal of Physiology, 1979
• Chemically skinned mammalian skeletal muscle I. The structure of skinned rabbit psoas
  Tissue and Cell, 1979
• Studies on the role of myosin alkali light chains
  Journal of Molecular Biology, 1977
• Electrophoretic analysis of multiple forms of myosin in fast-twitch and slow-twitch muscles of the chick
  Biochemical Journal, 1976