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Previous Volume 351:424-426 July 29, 2004 Number 5 Next

	Since this article has no abstract, we have provided an extract of the first 100 words of the full text and any section headings.

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In humans, myosins comprise a superfamily of more than 30 individual proteins. Structurally, myosin contains a highly conserved globular head, which, in turn, contains the ATPase and actin-binding sites, and a rod-like tail that modulates assembly and protein–protein interactions. Although the role of myosin as the molecular motor that drives striated-muscle contraction is well understood, myosins are also found in virtually all eukaryotic cells, where they are involved in a broad range of intracellular functions, including organelle transport, endocytosis, cytokinesis, and cytoskeletal support. In the past 10 years, research in a number of fields has revealed many of the underlying . . . [Full Text of this Article]

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From the Departments of Medicine and Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, N.Y.

Related Letters:

Mutation of Perinatal Myosin Heavy Chain
Stratakis C. A., Bertherat J., Carney J. A., Brown M. A., Morita H., Nagai R., Basson C. T., Veugelers M., McDermott D. A.
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N Engl J Med 2004; 351:2556-2558, Dec 9, 2004. Correspondence

This article has been cited by other articles:

• Stratakis, C. A., Bertherat, J., Carney, J. A., Brown, M. A., Morita, H., Nagai, R., Basson, C. T., Veugelers, M., McDermott, D. A. (2004). Mutation of Perinatal Myosin Heavy Chain. NEJM 351: 2556-2558 [Full Text]