ArticleProceedings of the National Academy of Sciences of the United States of America1997
Kinetics of force generation by single kinesin molecules activated by laser photolysis of caged ATP.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- An Overview of Contrasting Experimental Results on Dynamics of Kinesin-1 Molecular Motors: Insight into the Underlying Mechanism.Biomolecules · 2025Review
- Surface-limited reactions for spatial control of kinesin-microtubule motility assays using indirect irradiation of an electron beam.Biomicrofluidics · 2022Article
- Extensile to contractile transition in active microtubule-actin composites generates layered asters with programmable lifetimes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A highly conserved 3Science advances · 2021Article
- Strategies to expand peptide functionality through hybridisation with a small molecule component.RSC chemical biology · 2021Review
- Thermodynamic Efficiency of Somatic Exocytosis of Serotonin.Frontiers in physiology · 2019Article
- Presenilin PS1∆E9 disrupts mobility of secretory organelles in rat astrocytes.Acta physiologica (Oxford, England) · 2018Article
- Force per cross-sectional area from molecules to muscles: a general property of biological motors.Royal Society open science · 2016Article
- Highly loaded behavior of kinesins increases the robustness of transport under high resisting loads.PLoS computational biology · 2015Article
- Article
- Motor proteins and molecular motors: how to operate machines at the nanoscale.Journal of physics. Condensed matter : an Institute of Physics journal · 2013Review
- Signal processing for molecular and cellular biological physics: an emerging field.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2013Article
- Structure-based molecular simulations reveal the enhancement of biased Brownian motions in single-headed kinesin.PLoS computational biology · 2013Article
- Transport properties of melanosomes along microtubules interpreted by a tug-of-war model with loose mechanical coupling.PloS one · 2012Article
- The nucleotide-binding state of microtubules modulates kinesin processivity and the ability of Tau to inhibit kinesin-mediated transport.The Journal of biological chemistry · 2011Article
- Mechanical properties of organelles driven by microtubule-dependent molecular motors in living cells.PloS one · 2011Article
- Direct observation of the myosin Va recovery stroke that contributes to unidirectional stepping along actin.PLoS biology · 2011Article
- Illuminating the chemistry of life: design, synthesis, and applications of "caged" and related photoresponsive compounds.ACS chemical biology · 2009Review
- Myosin V and Kinesin act as tethers to enhance each others' processivity.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- What kinesin does at roadblocks: the coordination mechanism for molecular walking.The EMBO journal · 2004Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To relate transients of force by single kinesin molecules with the elementary steps of the ATPase cycle, we measured the time to force generation by kinesin after photorelease of ATP from caged ATP. Kinesin-coated beads were trapped by an infrared laser and brought onto microtubules fixed to a coverslip. Tension was applied to a kinesin-microtubule rigor complex using the optical trap, and ATP was released by flash photolysis of caged ATP with a UV laser. Kinesin started to generate force and move stepwise with a step size of 8 nm at average times of 31, 45, and 79 ms after photorelease of 450, 90, and 18 microM ATP, respectively. The kinetics of force generation were consistent with a two-step reaction: ATP binding, with an apparent second-order rate constant of 0.7 microM-1.s-1, followed by force generation at 45 s-1 per kinesin molecule. The transient rate of force generation was close to the rate of the ATPase cycle in solution, suggesting that the rate-limiting step of ATPase cycle is involved with the force generation.
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