ArticleBiophysical journal2011
Chemomechanical coupling and motor cycles of myosin V.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed.
- Braess' Paradox in Enzyme Kinetics: Asymmetry from Population Balance without Direct Cooperativity.Journal of chemical theory and computation · 2026Article
- Specificity and tunability of efflux pumps: A new role for the proton gradient?PLoS computational biology · 2025Article
- Information flow, gating, and energetics in dimeric molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Dynamics of ATP-dependent and ATP-independent steppings of myosin-V on actin: catch-bond characteristics.Journal of the Royal Society, Interface · 2020Article
- Article
- A model for the chemomechanical coupling of myosin-V molecular motors.RSC advances · 2019Article
- A Unified Walking Model for Dimeric Motor Proteins.Biophysical journal · 2018Article
- Structural conditions on complex networks for the Michaelis-Menten input-output response.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Myosin V: Chemomechanical-coupling ratchet with load-induced mechanical slip.Scientific reports · 2017Article
- Chemomechanical regulation of myosin Ic cross-bridges: Deducing the elastic properties of an ensemble from single-molecule mechanisms.PLoS computational biology · 2017Article
- Design principles governing chemomechanical coupling of kinesin.Scientific reports · 2017Article
- Simulating the dynamics of the mechanochemical cycle of myosin-V.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
- Design principles governing the motility of myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Dwell time distributions of the molecular motor myosin V.PloS one · 2013Article
- Global fit analysis of myosin-5b motility reveals thermodynamics of Mg2+-sensitive acto-myosin-ADP states.PloS one · 2013Article
- A branched kinetic scheme describes the mechanochemical coupling of Myosin Va processivity in response to substrate.Biophysical journal · 2012Article
- Myosin-V as a mechanical sensor: an elastic network study.Biophysical journal · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The molecular motor myosin V has been studied extensively both in bulk and single molecule experiments. Based on the chemical states of the motor, we construct a systematic network theory that includes experimental observations about the stepping behavior of myosin V. We utilize constraints arising from nonequilibrium thermodynamics to determine motor parameters and demonstrate that the motor behavior is governed by three chemomechanical motor cycles. The competition between these cycles can be understood via the influence of external load forces onto the chemical transition rates for the binding of adenosine triphosphate and adenosine diphosphate. In addition, we also investigate the functional dependence of the mechanical stepping rates on these forces. For substall forces, the dominant pathway of the motor network is profoundly different from the one for superstall forces, which leads to a stepping behavior that is in agreement with the experimental observations. Our theory provides a unified description of the experimental data as obtained for myosin V in single motor experiments.
Indexed as
Identifiers
What OpenQuestion holds
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.