Evidence map›Paper›PMID 15568820›Full record

ArticleBiochemistry2004

The Delta 14 mutation of human cardiac troponin T enhances ATPase activity and alters the cooperative binding of S1-ADP to regulated actin.

Boris Gafurov, Scott Fredricksen, Anmei Cai, Bernhard Brenner, P Bryant Chase, Joseph M Chalovich

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed, 1 pooled it
0.4field-weighted citation impact, top 35% 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

32 citing papers in PubMed, 1 synthesis or guideline pooled it, 41 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Creatine Kinase Equilibration and ΔGInternational journal of molecular sciences · 2023
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  19. Slowed Dynamics of Thin Filament Regulatory Units Reduces CaCellular and molecular bioengineering · 2013
    Article
  20. Review
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.

Boris GafurovDepartment of Biochemistry and Molecular Biology, Brody School of Medicine, East Carolina University, 600 Moye Boulevard, Greenville, North Carolina 27858-4354, USA.
Scott Fredricksen
Anmei Cai
Bernhard Brenner
P Bryant Chase
Joseph M Chalovich
Florida State University · USEast Carolina University · US

Funding

Acting Based Regulation of Smooth Muscle ContractionR01AR035216 · NIAMS · EAST CAROLINA UNIVERSITY · PI CHALOVICH, JOSEPH M · 1986 to 2007
$1.5M
ALTERED CALCIUM REGULATION IN CARDIOMYOPATHIESR01HL063974 · NHLBI · UNIVERSITY OF WASHINGTON · PI CHASE, P. BRYANT · 2001 to 2004
$1.3M
WEAKLY BOUND CROSSBRIDGES AND MUSCLE CONTRACTIONR01AR040540 · NIAMS · EAST CAROLINA UNIVERSITY · PI CHALOVICH, JOSEPH M · 1991 to 1994
–
NHLBI NIH HHS HL63974NHLBI NIH HHS R01 HL063974NIAMS NIH HHS AR40540NIAMS NIH HHS R01 AR035216
6 · The paper itself

Abstract

The complex of tropomyosin and troponin binds to actin and inhibits activation of myosin ATPase activity and force production of striated muscles at low free Ca(2+) concentrations. Ca(2+) stimulates ATP activity, and at subsaturating actin concentrations, the binding of NEM-modified S1 to actin-tropomyosin-troponin increases the rate of ATP hydrolysis even further. We show here that the Delta14 mutation of troponin T, associated with familial hypertrophic cardiomyopathy, results in an increase in ATPase rate like that seen with wild-type troponin in the presence of NEM-S1. The enhanced ATPase activity was not due to a decreased incorporation of mutant troponin T with troponin I and troponin C to form an active troponin complex. The activating effect was more prominent with a hybrid troponin (skeletal TnI, TnC, and cardiac TnT) than with all cardiac troponin. Thus it appears that changes in the troponin-troponin contacts that result from mutations or from forming hybrids stabilize a more active state of regulated actin. An analysis of the effect of the Delta14 mutation on the equilibrium binding of S1-ADP to actin was consistent with stabilization of an active state of actin. This change in activation may be important in the development of cardiac disease.

Indexed as

MutationActinsAdenosine DiphosphateAdenosine TriphosphatasesAnimalsCattleEnzyme ActivationHumansMuscle, SkeletalMyocardiumMyosinsMyosin SubfragmentsProtein BindingRabbitsRatsSequence DeletionActinsAdenosine DiphosphateAdenosine TriphosphatasesMyosinsMyosin SubfragmentsTroponin TNon-programmatic

Identifiers

PMID15568820
PMCPMC1351011
OpenAlexW1975054272

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.