ArticleBiophysical chemistry2011
Two-state displacement by the kinesin-14 Ncd stalk.
Article in Biophysical chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Structure and dynamics of motor-driven microtubule bundles.Soft matter · 2024Article
- In Vitro FRET- and Fluorescence-Based Assays to Study Protein Conformation and Protein-Protein Interactions in Mitosis.Methods in molecular biology (Clifton, N.J.) · 2020Article
- An estimate to the first approximation of microtubule rupture force.European biophysics journal : EBJ · 2019Article
- Working stroke of the kinesin-14, ncd, comprises two substeps of different direction.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Force generation by kinesin and myosin cytoskeletal motor proteins.Journal of cell science · 2013Review
- Altered nucleotide-microtubule coupling and increased mechanical output by a kinesin mutant.PloS one · 2012Article
- Neck-motor interactions trigger rotation of the kinesin stalk.Scientific reports · 2012Article
- Hysteresis-based mechanism for the directed motility of the Ncd motor.Biophysical journal · 2011Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
Abstract
The nonprocessive kinesin-14 Ncd motor binds to microtubules and hydrolyzes ATP, undergoing a single displacement before releasing the microtubule. A lever-like rotation of the coiled-coil stalk is thought to drive Ncd displacements or steps along microtubules. Crystal structures and cryoelectron microscopy reconstructions imply that stalk rotation is correlated with ADP release and microtubule binding by the motor. Here we report FRET assays showing that the end of the stalk is more than ~9nm from the microtubule when wild-type Ncd binds microtubules without added nucleotide, but the stalk is within ~6nm of the microtubule surface when the microtubule-bound motor binds an ATP analogue, matching the rotated state observed in crystal structures. We propose that the stalk rotation is initiated when the motor binds to microtubules and releases ADP, and is completed when ATP binds.
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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.