Evidence map›Paper›PMID 18676638›Full record

ArticleBiophysical journal2008

The cardiac Ca2+-sensitive regulatory switch, a system in dynamic equilibrium.

John M Robinson, Herbert C Cheung, Wenji Dong

Abstract read
In one paragraph

Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. The molecular basis for diminished muscle function in acidosis: a proposal.Journal of muscle research and cell motility · 2020
    Article
  3. CaBiophysical journal · 2018
    Article
  4. Article
  5. Article
  6. Article
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  11. Article
  12. Ala scanning of the inhibitory region of cardiac troponin I.The Journal of biological chemistry · 2009
    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

3 authors.

John M RobinsonDepartment of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, Alabama, USA. jmr@uab.edu
Herbert C Cheung
Wenji Dong

Funding

Kinetics of Cardiac Myofilament ActivationR01HL080186 · NHLBI · WASHINGTON STATE UNIVERSITY · PI DONG, WEN-JI · 2005 to 2013
$3.4M
REGULATORY MECHANISMS OF CARDIAC MUSCLER01HL052508 · NHLBI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI CHEUNG, HERBERT C · 1996 to 2008
$2.6M
NHLBI NIH HHS HL052508NHLBI NIH HHS HL80186NHLBI NIH HHS R01 HL052508NHLBI NIH HHS R01 HL080186
6 · The paper itself

Abstract

The Ca(2+)-sensitive regulatory switch of cardiac muscle is a paradigmatic example of protein assemblies that communicate ligand binding through allosteric change. The switch is a dimeric complex of troponin C (TnC), an allosteric sensor for Ca(2+), and troponin I (TnI), an allosteric reporter. Time-resolved equilibrium Förster resonance energy transfer (FRET) measurements suggest that the switch activates in two steps: a TnI-independent Ca(2+)-priming step followed by TnI-dependent opening. To resolve the mechanistic role of TnI in activation we performed stopped-flow FRET measurements of activation after rapid addition of a lacking component (Ca(2+) or TnI) and deactivation after rapid chelation of Ca(2+). Time-resolved measurements, stopped-flow measurements, and Ca(2+)-titration measurements were globally analyzed in terms of a new quantitative dynamic model of TnC-TnI allostery. The analysis provided a mesoscopic parameterization of distance changes, free energy changes, and transition rates among the accessible coarse-grained states of the system. The results reveal that 1), the Ca(2+)-induced priming step, which precedes opening, is the rate-limiting step in activation; 2), closing is the rate-limiting step in de-activation; 3), TnI induces opening; 4), there is an incompletely deactivated population when regulatory Ca(2+) is not bound, which generates an accessory pathway of activation; and 5), there is incomplete activation by Ca(2+)-when regulatory Ca(2+) is bound, a 3:2 mixture of dynamically interconverting open (active) and primed-closed (partially active) conformers is observed (15 degrees C). Temperature-dependent stopped-flow FRET experiments provide a near complete thermokinetic parameterization of opening: the enthalpy change (DeltaH = -33.4 kJ/mol), entropy change (DeltaS = -0.110 kJ/mol/K), heat capacity change (DeltaC(p) = -7.6 kJ/mol/K), the enthalpy of activation (delta(double dagger) = 10.6 kJ/mol) and the effective barrier crossing attempt frequency (nu(adj) = 1.8 x 10(4) s(-1)).

Indexed as

Models, BiologicalAnimalsCalciumCalcium SignalingComputer SimulationFeedbackHeartHumansModels, ChemicalMyocardial ContractionTroponinCalciumTroponin

Identifiers

PMID18676638
PMCPMC2576382

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.