Evidence map›Paper›PMID 17028139›Full record

ArticleBiophysical journal2007

Dynamics of the nucleotide pocket of myosin measured by spin-labeled nucleotides.

Nariman Naber, Thomas J Purcell, Edward Pate, Roger Cooke

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Molecular mechanisms underlying deoxy-ADP.Pi activation of pre-powerstroke myosin.Protein science : a publication of the Protein Society · 2017
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  7. Early stages of the recovery stroke in myosin II studied by molecular dynamics simulations.Protein science : a publication of the Protein Society · 2011
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  8. Article
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  12. Structural kinetics of myosin by transient time-resolved FRET.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  13. Article
  14. Article
  15. Review
  16. Actin-binding cleft closure in myosin II probed by site-directed spin labeling and pulsed EPR.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  17. Characterization of the pre-force-generation state in the actomyosin cross-bridge cycle.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
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

4 authors at 2 institutions in 1 country.

Nariman NaberDepartment of Biochemistry and Biophysics, University of California, San Francisco, California 94158, USA. nariman.naber@ucsf.edu
Thomas J Purcell
Edward Pate
Roger Cooke
University of California, San Francisco · USWashington State University · US

Funding

STRUCTURE/FUNCTION OF MOLECULAR MOTORSP01AR042895 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI COOKE, ROGER A · 1994 to 2008
$9.8M
CROSS-BRIDGE MECHANICSR01AR039643 · NIAMS · WASHINGTON STATE UNIVERSITY · PI PATE, EDWARD F · 1989 to 2004
$873k
NIAMS NIH HHS AR39643NIAMS NIH HHS AR42895NIAMS NIH HHS P01 AR042895NIAMS NIH HHS R01 AR039643
6 · The paper itself

Abstract

We have used electron paramagnetic probes attached to the ribose of ATP (SL-ATP) to monitor conformational changes in the nucleotide pocket of myosin. Spectra for analogs bound to myosin in the absence of actin showed a high degree of immobilization, indicating a closed nucleotide pocket. In the Actin.Myosin.SL-AMPPNP, Actin.Myosin.SL-ADP.BeF(3), and Actin.Myosin.SL-ADP.AlF(4) complexes, which mimic weakly binding states near the beginning of the power stroke, the nucleotide pocket remained closed. The spectra of the strongly bound Actin.Myosin.SL-ADP complex consisted of two components, one similar to the closed pocket and one with increased probe mobility, indicating a more open pocket, The temperature dependence of the spectra showed that the two conformations of the nucleotide pocket were in equilibrium, with the open conformation more favorable at higher temperatures. These results, which show that opening of the pocket occurs only in the strongly bound states, appear reasonable, as this would tend to keep ADP bound until the end of the power stroke. This conclusion also suggests that force is initially generated by a myosin with a closed nucleotide pocket.

Indexed as

ActinsActomyosinAdenosine DiphosphateAdenosine TriphosphateAnimalsChymotrypsinElectron Spin Resonance SpectroscopyModels, BiologicalMolecular ConformationMyosinsNucleotidesRabbitsSpin LabelsTemperatureThermodynamicsActinsActomyosinAdenosine DiphosphateAdenosine Triphosphatealpha-chymotrypsinChymotrypsinMyosinsNucleotidesSpin Labels

Identifiers

PMID17028139
PMCPMC1697850
OpenAlexW1967572198

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.