The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Direction of microtubule movement is an intrinsic property of the motor domains of kinesin heavy chain and Drosophila ncd protein.
Open accessAbstract
The kinesin heavy chain and the ncd (non-claret disjunctional) gene product of Drosophila are microtubule-associated motor proteins related by sequence similarity within an approximately 340-aa domain. Despite the sequence similarity, the kinesin heavy chain and ncd protein move in opposite directions on microtubules. To investigate the molecular basis for direction of movement, we created a series of truncated kinesin heavy chain and ncd proteins. We found that the conserved domain of both proteins has microtubule motor activity, although the efficiency with which ATP hydrolysis is coupled to microtubule movement declines dramatically with increasing truncation. Further, the direction of movement is intrinsic to the conserved motor domains, rather than being a consequence of domain organization or adjacent sequences.
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Evidence that the Head of Kinesin Is Sufficient for Force Generation and Motility in Vitro
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Kinbara, K., & Aida, T. (2005) · Chemical Reviews · doi:10.1021/cr030071r · Cited by 880
Direct observation of single kinesin molecules moving along microtubules
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Physical Properties Determining Self-Organization of Motors and Microtubules
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Metadata
- Authors
- Stewart, R. J., Thaler, J. P., & Goldstein, L. S.
- Affiliations
- Harvard University (US)
- ORCID
- Goldstein, L S
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1993-06
- Volume
- 90
- Issue
- 11
- Pages
- 5209-5213
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC46685
- OpenAlex
- W2056695965
- Cited by
- 145
- References
- 17
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 2 · 2021: 1 · 2020: 1 · 2019: 2 · 2016: 1 · 2012: 2
- FWCI
- 7.40
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- kinesin heavy chain, microtubule motor proteins, motor domain, ATP hydrolysis, truncated protein, Drosophila, sequence similarity
- MeSH terms
- Animals, Drosophila, Glutathione Transferase, Microtubule Proteins, Microtubules, Plasmids, Recombinant Fusion Proteins, Spectrin, Restriction Mapping, Kinesins, Drosophila Proteins, Macromolecular Substances
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