Evidence map›Paper›PMID 17293397›Full record

ArticleBiophysical journal2007

Effects of thin and thick filament proteins on calcium binding and exchange with cardiac troponin C.

Jonathan P Davis, Catalina Norman, Tomoyoshi Kobayashi, R John Solaro, Darl R Swartz, Svetlana B Tikunova

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 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

85 citing papers in PubMed, 114 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Mouse Models of Cardiomyopathies Caused by Mutations in Troponin C.International journal of molecular sciences · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Pressing physiology to move our understanding of cytosolic calcium dynamics.Journal of applied physiology (Bethesda, Md. : 1985) · 2022
    Article
  14. International journal of molecular sciences · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

25 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 1 country.

Jonathan P DavisDepartment of Physiology and Cell Biology, The Ohio State University, Columbus, Ohio 43210, USA. davis.812@osu.edu
Catalina Norman
Tomoyoshi Kobayashi
R John Solaro
Darl R Swartz
Svetlana B Tikunova
The Ohio State University · USPurdue University West Lafayette · US

Funding

MODULATION OF CALCIUM CONTROL OF CARDIAC MYOFIBRILSR01HL022231 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI GUPTA, MADHU, SOLARO, R JOHN · 1985 to 2014
$2.9M
MODULATION OF CALCIUM CONTROL OF CARDIAC MYOFIBRILSR37HL022231 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI SOLARO, R JOHN · 1999 to 2006
$2.2M
Myofibrillar Determinants of Striated Muscle RelaxationR01AR020792 · NIAMS · OHIO STATE UNIVERSITY · PI RALL, JACK A · 1986 to 2009
$2.2M
Signal Transduction Along Cardiac Thin FilamentsR01HL073828 · NHLBI · PURDUE UNIVERSITY · PI SWARTZ, DARL RAY · 2005 to 2009
$1.7M
Role of troponin C in cardiac muscle relaxationF32HL073600 · NHLBI · OHIO STATE UNIVERSITY · PI TIKUNOVA, SVETLANA B · 2003 to 2005
$147k
NHLBI NIH HHS F32 HL073600NHLBI NIH HHS HL022231NHLBI NIH HHS HL073600NHLBI NIH HHS HL073828NHLBI NIH HHS R01 HL022231NHLBI NIH HHS R01 HL073828NHLBI NIH HHS R37 HL022231NIAMS NIH HHS AR020792NIAMS NIH HHS R01 AR020792
6 · The paper itself

Abstract

Understanding the effects of thin and thick filament proteins on the kinetics of Ca(2+) exchange with cardiac troponin C is essential to elucidating the Ca(2+)-dependent mechanisms controlling cardiac muscle contraction and relaxation. Unlike labeling of the endogenous Cys-84, labeling of cardiac troponin C at a novel engineered Cys-53 with 2-(4'-iodoacetamidoanilo)napthalene-6-sulfonic acid allowed us to accurately measure the rate of calcium dissociation from the regulatory domain of troponin C upon incorporation into the troponin complex. Neither tropomyosin nor actin alone affected the Ca(2+) binding properties of the troponin complex. However, addition of actin-tropomyosin to the troponin complex decreased the Ca(2+) sensitivity ( approximately 7.4-fold) and accelerated the rate of Ca(2+) dissociation from the regulatory domain of troponin C ( approximately 2.5-fold). Subsequent addition of myosin S1 to the reconstituted thin filaments (actin-tropomyosin-troponin) increased the Ca(2+) sensitivity ( approximately 6.2-fold) and decreased the rate of Ca(2+) dissociation from the regulatory domain of troponin C ( approximately 8.1-fold), which was completely reversed by ATP. Consistent with physiological data, replacement of cardiac troponin I with slow skeletal troponin I led to higher Ca(2+) sensitivities and slower Ca(2+) dissociation rates from troponin C in all the systems studied. Thus, both thin and thick filament proteins influence the ability of cardiac troponin C to sense and respond to Ca(2+). These results imply that both cross-bridge kinetics and Ca(2+) dissociation from troponin C work together to modulate the rate of cardiac muscle relaxation.

Indexed as

ActinsAnimalsCalciumCells, CulturedMaleMyocardial ContractionMyocytes, CardiacMyosinsProtein BindingRatsSarcomeresTroponin CActinsCalciumMyosinsTroponin C

Identifiers

PMID17293397
PMCPMC1852344
OpenAlexW1996547062

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.