Cilia and flagella of eukaryotes.
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fallen away as a meaningless phrase . . .A cilium is manifestly a highly complex and compound organ, and . . .morphological description is clearly only a beginning .
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Dynein is the only molecule known to interact with microtubules to generate motive force.
“Dynein is the only molecule known to interact with microtubules to generate motive force (Gibbons, 1981)”
From Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility (1985) · cites this paper as Gibbons, 1981
The Functional Mechanisms section says dynein arms generate shearing force between adjacent microtubule doublets, supporting dynein’s role in motility. It does not establish the broader claim that dynein is the only molecule known to generate motive force through interaction with microtubules. (LLM, conf=0.84)
Experimental — accuracy not yet measuredDynein is the only protein known to bind to microtubules and perform work.
“Dynein is the only protein known to bind to microtubules and perform work (Gibbons, 1981).”
From Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility (1985) · cites this paper as Gibbons, 1981
The Composition section says dynein can rebind to axonemal doublets and restore flagellar beating; Functional Mechanisms describes dynein arms generating active shearing stress between doublet microtubules. These passages support binding and mechanical work, but do not establish that dynein is the only protein known to do both. (LLM, conf=0.84)
Experimental — accuracy not yet measuredMyosin and dynein generate force in only one direction with respect to their filamentous substrates.
“Myosin (Sheetz and Spudich, 1983) and dynein (Gibbons, 1981) generate force in only one direction with respect to their filamentous substrates.”
From Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility (1985) · cites this paper as Gibbons, 1981
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Research works printed but not linked: 22
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Cited by
Sorted by citations
Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
VALE, R., REESE, T., & SHEETZ, M. (1985) · Cell · doi:10.1016/s0092-8674(85)80099-4 · Cited by 1,993
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Metadata
- Authors
- Gibbons, I. R.
- Affiliations
- University of Hawaiʻi at Mānoa (US)
- Corresponding author
- Gibbons, I R
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1981-02-22
- Volume
- 91
- Issue
- 3
- Pages
- 107s-124s
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2112791
- OpenAlex
- W2009887778
- Cited by
- 626
- References
- 0
- Citations by year
- 2026: 3 · 2025: 13 · 2024: 9 · 2023: 13 · 2022: 11 · 2021: 5 · 2020: 15 · 2019: 13 · 2018: 13 · 2017: 12 · 2016: 18 · 2015: 16 · 2014: 17 · 2013: 15 · 2012: 13
- FWCI
- 2.00
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institute of Child Health and Human Development
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Cystic Fibrosis Research Advances
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- cilia, flagella, ciliary ultrastructure
- MeSH terms
- Adenosine Triphosphatases, Adenosine Triphosphate, Animals, Calcium, Cilia, Dyneins, Flagella, Humans, Microtubules, Models, Biological, Movement, Proteins, Tubulin
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