Evidence map›Paper›PMID 32652059›Full record

ArticleBiophysical journal2020

Positional Isomers of a Non-Nucleoside Substrate Differentially Affect Myosin Function.

Mike Woodward, Eric Ostrander, Seung P Jeong, Xiarong Liu, Brent Scott, Matt Unger, Jianhan Chen, Dhandapani Venkataraman, Edward P Debold

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Mike WoodwardDepartment of Kinesiology, Muscle Biophysics Lab, University of Massachusetts Amherst, Amherst, Massachusetts.
Eric OstranderDepartment of Chemistry, Advanced Laboratory for Iontronic, Electronic and Nanomaterials, University of Massachusetts Amherst, Amherst, Massachusetts.
Seung P JeongDepartment of Chemistry, Advanced Laboratory for Iontronic, Electronic and Nanomaterials, University of Massachusetts Amherst, Amherst, Massachusetts.
Xiarong LiuDepartment of Chemistry, Computational Biophysics and Biomaterials Group, University of Massachusetts Amherst, Amherst, Massachusetts.
Brent ScottDepartment of Kinesiology, Muscle Biophysics Lab, University of Massachusetts Amherst, Amherst, Massachusetts.
Matt UngerDepartment of Kinesiology, Muscle Biophysics Lab, University of Massachusetts Amherst, Amherst, Massachusetts.
Jianhan ChenDepartment of Chemistry, Computational Biophysics and Biomaterials Group, University of Massachusetts Amherst, Amherst, Massachusetts.
Dhandapani VenkataramanDepartment of Chemistry, Advanced Laboratory for Iontronic, Electronic and Nanomaterials, University of Massachusetts Amherst, Amherst, Massachusetts.
Edward P DeboldDepartment of Kinesiology, Muscle Biophysics Lab, University of Massachusetts Amherst, Amherst, Massachusetts. Electronic address: edebold@kin.umass.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Molecular motors have evolved to transduce chemical energy from ATP into mechanical work to drive essential cellular processes, from muscle contraction to vesicular transport. Dysfunction of these motors is a root cause of many pathologies necessitating the need for intrinsic control over molecular motor function. Herein, we demonstrate that positional isomerism can be used as a simple and powerful tool to control the molecular motor of muscle, myosin. Using three isomers of a synthetic non-nucleoside triphosphate, we demonstrate that myosin's force- and motion-generating capacity can be dramatically altered at both the ensemble and single-molecule levels. By correlating our experimental results with computation, we show that each isomer exerts intrinsic control by affecting distinct steps in myosin's mechanochemical cycle. Our studies demonstrate that subtle variations in the structure of an abiotic energy source can be used to control the force and motility of myosin without altering myosin's structure.

Indexed as

Muscle ContractionMyosinsActinsAdenosine TriphosphateIsomerismMechanical PhenomenaMusclesActinsAdenosine TriphosphateMyosins

Identifiers

PMID32652059
PMCPMC7401181

What OpenQuestion holds

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Registered trials

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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.