Evidence map›Paper›PMID 19920153›Full record

ArticleThe Journal of biological chemistry2010

Troponin regulatory function and dynamics revealed by H/D exchange-mass spectrometry.

Devanand Kowlessur, Larry S Tobacman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. The missing links within troponin.Archives of biochemistry and biophysics · 2019
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Atomic resolution probe for allostery in the regulatory thin filament.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
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  16. Article
  17. Review
  18. 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

2 authors at 1 institution in 1 country.

Devanand KowlessurDepartment of Medicine, University of Illinois at Chicago, Chicago, Illinois 60612, USA.
Larry S Tobacman
University of Illinois Chicago · US

Funding

THIN FILAMENTS WITH CARDIOMYOPATHIC MUTANT PROTEINSR01HL063774 · NHLBI · UNIVERSITY OF IOWA · PI TOBACMAN, LARRY S · 2000 to 2014
$4.5M
CARDIAC CONTRACTILE PROTEIN COOPERATIVITYR01HL038834 · NHLBI · UNIVERSITY OF IOWA · PI TOBACMAN, LARRY S · 1992 to 2009
$3.6M
CARDIAC CONTRACTILE PROTEIN COOPERATIVITYR29HL038834 · NHLBI · UNIVERSITY OF IOWA · PI TOBACMAN, LARRY S · 1987 to 1991
–
NHLBI NIH HHS HL038834NHLBI NIH HHS HL063774NHLBI NIH HHS R01 HL038834NHLBI NIH HHS R01 HL063774
6 · The paper itself

Abstract

Muscle contraction is tightly regulated by Ca(2+) binding to the thin filament protein troponin. The mechanism of this regulation was investigated by detailed mapping of the dynamic properties of cardiac troponin using amide hydrogen exchange-mass spectrometry. Results were obtained in the presence of either saturation or non-saturation of the regulatory Ca(2+) binding site in the NH(2) domain of subunit TnC. Troponin was found to be highly dynamic, with 60% of amides exchanging H for D within seconds of exposure to D(2)O. In contrast, portions of the TnT-TnI coiled-coil exhibited high protection from exchange, despite 6 h in D(2)O. The data indicate that the most stable portion of the trimeric troponin complex is the coiled-coil. Regulatory site Ca(2+) binding altered dynamic properties (i.e. H/D exchange protection) locally, near the binding site and in the TnI switch helix that attaches to the Ca(2+)-saturated TnC NH(2) domain. More notably, Ca(2+) also altered the dynamic properties of other parts of troponin: the TnI inhibitory peptide region that binds to actin, the TnT-TnI coiled-coil, and the TnC COOH domain that contains the regulatory Ca(2+) sites in many invertebrate as opposed to vertebrate troponins. Mapping of these affected regions onto the troponin highly extended structure suggests that cardiac troponin switches between alternative sets of intramolecular interactions, similar to previous intermediate resolution x-ray data of skeletal muscle troponin.

Indexed as

Actin CytoskeletonAmino Acid SequenceBinding SitesCalciumDeuterium Exchange MeasurementHumansHydrogenMass SpectrometryMolecular Sequence DataMuscle, StriatedMyocardiumProtein Structure, TertiaryTroponinTroponin CTroponin ITroponin TCalciumHydrogenTroponinTroponin CTroponin ITroponin T

Identifiers

PMID19920153
PMCPMC2807325
OpenAlexW2037377963

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.