Evidence map›Paper›PMID 21149681›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Visualizing key hinges and a potential major source of compliance in the lever arm of myosin.

Jerry H Brown, V S Senthil Kumar, Elizabeth O'Neall-Hennessey, Ludmila Reshetnikova, Howard Robinson, Michelle Nguyen-McCarty, Andrew G Szent-Györgyi, Carolyn Cohen

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 12% of its field
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

23 citing papers in PubMed, 30 citations in OpenAlex.

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  17. Mammalian myosin-18A, a highly divergent myosin.The Journal of biological chemistry · 2013
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Jerry H BrownRosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454-9110, USA.
V S Senthil Kumar
Elizabeth O'Neall-Hennessey
Ludmila Reshetnikova
Howard Robinson
Michelle Nguyen-McCarty
Andrew G Szent-Györgyi
Carolyn Cohen
Brandeis University · USBrookhaven National Laboratory · US

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
MUSCLE STRUCTURE AND THE CONTRACTILE MECHANISMR01AR017346 · NIAMS · BRANDEIS UNIVERSITY · PI COHEN, CAROLYN · 1986 to 2012
$7.6M
MUSCLE STRUCTURE AND THE CONTRACTILE MECHANISMR37AR017346 · NIAMS · BRANDEIS UNIVERSITY · PI COHEN, CAROLYN · 1990 to 1999
–
NIAMS NIH HHS AR017346NIAMS NIH HHS R01 AR017346NIAMS NIH HHS R37 AR017346NIBIB NIH HHS P30 EB009998
6 · The paper itself

Abstract

We have determined the 2.3-Å-resolution crystal structure of a myosin light chain domain, corresponding to one type found in sea scallop catch ("smooth") muscle. This structure reveals hinges that may function in the "on" and "off" states of myosin. The molecule adopts two different conformations about the heavy chain "hook" and regulatory light chain (RLC) helix D. This conformational change results in extended and compressed forms of the lever arm whose lengths differ by 10 Å. The heavy chain hook and RLC helix D hinges could thus serve as a potential major and localized source of cross-bridge compliance during the contractile cycle. In addition, in one of the molecules of the crystal, part of the RLC N-terminal extension is seen in atomic detail and forms a one-turn alpha-helix that interacts with RLC helix D. This extension, whose sequence is highly variable in different myosins, may thus modulate the flexibility of the lever arm. Moreover, the relative proximity of the phosphorylation site to the helix D hinge suggests a potential role for conformational changes about this hinge in the transition between the on and off states of regulated myosins.

Indexed as

Models, MolecularProtein ConformationActinsAdenosine TriphosphatasesAnimalsBiomechanical PhenomenaBivalviaCrystallizationMuscle, SmoothMyosin Type IIActinsAdenosine TriphosphatasesMyosin Type II

Identifiers

PMID21149681
PMCPMC3017161
OpenAlexW2067592976

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.