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Cited by 2,070

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Three-dimensional structure of myosin subfragment-1: a molecular motor

Rayment, I, Rypniewski, W., Schmidt-Base, K, Smith, R, Tomchick, D., Benning, M., Winkelmann, D., Wesenberg, G, Holden, H.·1993·Science

Abstract

Directed movement is a characteristic of many living organisms and occurs as a result of the transformation of chemical energy into mechanical energy. Myosin is one of three families of molecular motors that are responsible for cellular motility. The three-dimensional structure of the head portion of myosin, or subfragment-1, which contains both the actin and nucleotide binding sites, is described. This structure of a molecular motor was determined by single crystal x-ray diffraction. The data provide a structural framework for understanding the molecular basis of motility.

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Crossref · 10.1126/science.8316857

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Metadata

Authors
Rayment, I., Rypniewski, W., Schmidt-Base, K., Smith, R., Tomchick, D., Benning, M., Winkelmann, D., Wesenberg, G., & Holden, H.
Venue
Science
Published
1993-07-02
Volume
261
Issue
5117
Pages
50-58
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2069953906
Cited by
2,070
References
1
FWCI
117.00
Type
journal article
Language
en
Open access
closed

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.