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
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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Citations
Cites
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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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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
