Evidence map›Paper›PMID 24358137›Full record

ArticlePloS one2013

X-ray solution scattering of squid heavy meromyosin: strengthening the evidence for an ancient compact off state.

Richard E Gillilan, V S Senthil Kumar, Elizabeth O'Neall-Hennessey, Carolyn Cohen, Jerry H Brown

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.4field-weighted citation impact, top 33% 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

8 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  5. Review
  6. Article
  7. Article
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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

5 authors at 2 institutions in 1 country.

Richard E GillilanMacromolecular Diffraction Facility, Cornell High Energy Synchrotron Source, Ithaca, New York, United States of America.
V S Senthil KumarRosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts, United States of America.
Elizabeth O'Neall-HennesseyRosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts, United States of America.
Carolyn CohenRosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts, United States of America.
Jerry H BrownRosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts, United States of America.
Brandeis University · USCornell High Energy Synchrotron Source

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
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 AR017346NIGMS NIH HHS GM-103485NIGMS NIH HHS P41 GM103485
6 · The paper itself

Abstract

The overall conformations of regulated myosins or heavy meromyosins from chicken/turkey, scallop, tarantula, limulus, and scorpion sources have been studied by a number of techniques, including electron microscopy, sedimentation, and pulsed electron paramagnetic resonance. These studies have indicated that the binding of regulatory ions changes the conformation of the molecule from a compact shape found in the "off" state of the muscle to extended relationships between the tail and independently mobile heads that predominate in the "on" state. Here we strengthen the argument for the generality of this conformational change by using small angle X-ray scattering on heavy meromyosin from squid. Small angle X-ray scattering allows the protein to be visualized in solution under mild and relatively physiological conditions, and squid differs from the other species studied by at least 500 million years of evolution. Analysis of the data indicates that upon addition of Ca(2+) the radius of gyration increases. Differences in the squid "on" and "off" states are clearly distinguishable as bimodal and unimodal pair distance distribution functions respectively. These observations are consistent with a Ca(2+)-free squid heavy meromyosin that is compact, but which becomes extended when Ca(2+) is bound. Further, the scattering profile derived from the current model of tarantula heavy meromyosin in the "off" state is in excellent agreement with the measured "off" state scattering profile for squid heavy meromyosin. The previous and current studies together provide significant evidence that regulated myosin's compact off-state conformation is an ancient trait, inherited from a common ancestor during divergent evolution.

Indexed as

AnimalsDecapodiformesMusclesMyosin SubfragmentsProtein ConformationScattering, RadiationMyosin Subfragments

Identifiers

PMID24358137
PMCPMC3866118
OpenAlexW1970586356

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.