ArticleProceedings of the National Academy of Sciences of the United States of America1996
Three-dimensional cryoelectron microscopy of dimeric kinesin and ncd motor domains on microtubules.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
44 citing papers in PubMed, 132 citations in OpenAlex.
- Bound ion effects: Using machine learning method to study the kinesin Ncd's binding with microtubule.Biophysical journal · 2024Article
- Intracellular Organization by Jumbo Bacteriophages.Journal of bacteriology · 2020Review
- Automated tracing of helical assemblies from electron cryo-micrographs.Journal of structural biology · 2018Article
- Profile of Joachim Frank, Richard Henderson, and Jacques Dubochet, 2017 Nobel Laureates in Chemistry.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Dear microtubule, I see you.Molecular biology of the cell · 2016Article
- Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines.Biophysical reviews · 2015Article
- Common mechanistic themes for the powerstroke of kinesin-14 motors.Journal of structural biology · 2013Article
- Kinesin Kar3Cik1 ATPase pathway for microtubule cross-linking.The Journal of biological chemistry · 2011Article
- Moving into the cell: single-molecule studies of molecular motors in complex environments.Nature reviews. Molecular cell biology · 2011Review
- Spatial organization of intracellular communication: insights from imaging.Nature reviews. Molecular cell biology · 2010Review
- FRET measurements of kinesin neck orientation reveal a structural basis for processivity and asymmetry.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Insights into the Mechanical Properties of the Kinesin Neck Linker Domain from Sequence Analysis and Molecular Dynamics Simulations.Cellular and molecular bioengineering · 2009Article
- Pressure-induced changes in the structure and function of the kinesin-microtubule complex.Biophysical journal · 2009Article
- A cool look at the structural changes in kinesin motor domains.Journal of cell science · 2007Article
- Kinesin's biased stepping mechanism: amplification of neck linker zippering.Biophysical journal · 2006Article
- Article
- Interaction of kinesin motors, microtubules, and MAPs.Journal of muscle research and cell motility · 2006Review
- Rotation of the stalk/neck and one head in a new crystal structure of the kinesin motor protein, Ncd.The EMBO journal · 2003Article
- Nucleotide-induced conformations in the neck region of dimeric kinesin.The EMBO journal · 2003Article
- Repeat motifs of tau bind to the insides of microtubules in the absence of taxol.The EMBO journal · 2003Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kinesin and ncd motor proteins are homologous in sequence yet move in opposite directions along microtubules. We have previously shown that monomeric kinesin and ncd bind in the same orientation on equivalent sites relative to the ends of tubulin sheets of known polarity. We now report cryoelectron microscope images of 16-protofilament microtubules decorated with both single- and double-headed kinesin and double-headed ncd. Three-dimensional density maps and difference maps show that, in adenosine 5'-[beta,gamma-imido]triphosphate, both dimeric motors bind tightly to microtubules via one head, leaving the other free, though apparently in a fixed position. The attached heads of dimers bind to tubulin in the same way as single kinesin heads. The second heads are connected to the tops of the first but, whereas the second kinesin head is closely associated with the first, pairs of ncd heads are splayed apart. There is also a distinct difference in orientation: the second kinesin head is tilted toward the microtubule plus end, while the second head of ncd points toward the minus end.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.