ArticleThe Journal of cell biology1991
Nucleotide specificity of the enzymatic and motile activities of dynein, kinesin, and heavy meromyosin.
Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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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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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
26 citing papers in PubMed, 80 citations in OpenAlex.
- ATPγS substantially defeats the biasing mechanism for kinesin steps.Nature communications · 2026Article
- Cardiac myosin contraction and mechanotransduction in health and disease.The Journal of biological chemistry · 2021Review
- Backstepping Mechanism of Kinesin-1.Biophysical journal · 2020Article
- The Kinetics of Nucleotide Binding to Isolated Chlamydomonas Axonemes Using UV-TIRF Microscopy.Biophysical journal · 2019Article
- Step Sizes and Rate Constants of Single-headed Cytoplasmic Dynein Measured with Optical Tweezers.Scientific reports · 2018Article
- Article
- Review: Mechanochemistry of the kinesin-1 ATPase.Biopolymers · 2016Review
- Transgenic overexpression of ribonucleotide reductase improves cardiac performance.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The speed of intracellular signal transfer for chloroplast movement.Plant signaling & behavior · 2010Article
- Link between the enzymatic kinetics and mechanical behavior in an actomyosin motor.Biophysical journal · 2001Article
- Allele-specific activators and inhibitors for kinesin.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- ATP analogs and muscle contraction: mechanics and kinetics of nucleoside triphosphate binding and hydrolysis.Biophysical journal · 1998Article
- Molecular requirements for bi-directional movement of phagosomes along microtubules.The Journal of cell biology · 1997Article
- The role of surface loops (residues 204-216 and 627-646) in the motor function of the myosin head.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Going mobile: microtubule motors and chromosome segregation.Proceedings of the National Academy of Sciences of the United States of America · 1996Review
- Mitotic HeLa cells contain a CENP-E-associated minus end-directed microtubule motor.The EMBO journal · 1995Article
- High-resolution tracking of microtubule motility driven by a single kinesin motor.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Centromere function on minichromosomes isolated from budding yeast.Molecular biology of the cell · 1993Article
- Inhibition of anaphase spindle elongation in vitro by a peptide antibody that recognizes kinesin motor domain.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- GTP gamma S inhibits organelle transport along axonal microtubules.The Journal of cell biology · 1993Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The substrate specificities of dynein, kinesin, and myosin substrate turnover activity and cytoskeletal filament-driven translocation were examined using 15 ATP analogues. The dyneins were more selective in their substrate utilization than bovine brain kinesin or muscle heavy meromyosin, and even different types of dyneins, such as 14S and 22S dynein from Tetrahymena cilia and the beta-heavy chain-containing particle from the outer-arm dynein of sea urchin flagella, could be distinguished by their substrate specificities. Although bovine brain kinesin and muscle heavy meromyosin both exhibited broad substrate specificities, kinesin-induced microtubule translocation varied over a 50-fold range in speed among the various substrates, whereas heavy meromyosin-induced actin translocation varied only by fourfold. With both kinesin and heavy meromyosin, the relative velocities of filament translocation did not correlate well with the relative filament-activated substrate turnover rates. Furthermore, some ATP analogues that did not support the filament translocation exhibited filament-activated substrate turnover rates. Filament-activated substrate turnover and power production, therefore, appear to become uncoupled with certain substrates. In conclusion, the substrate specificities and coupling to motility are distinct for different types of molecular motor proteins. Such nucleotide "fingerprints" of enzymatic activities of motor proteins may prove useful as a tool for identifying what type of motor is involved in powering a motility-related event that can be reconstituted in vitro.
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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.