A functional and structural study of troponin C mutations related to hypertrophic cardiomyopathy. - Wikidata - awgldk - TriplyDB

A functional and structural study of troponin C mutations related to hypertrophic cardiomyopathy.

A functional and structural study of troponin C mutations related to hypertrophic cardiomyopathy.

http://www.wikidata.org/entity/Q37254027

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Gene regulation, alternative splicing, and posttranslational modification of troponin subunits in cardiac development and adaptation: a focused review The cardiac muscle duplex as a method to study myocardial heterogeneity Molecular basis of calcium-sensitizing and desensitizing mutations of the human cardiac troponin C regulatory domain: a multi-scale simulation study Cardiac Troponin and Tropomyosin: Structural and Cellular Perspectives to Unveil the Hypertrophic Cardiomyopathy Phenotype Why Is there a Limit to the Changes in Myofilament Ca2+-Sensitivity Associated with Myopathy Causing Mutations?A mutation in TNNC1-encoded cardiac troponin C, TNNC1-A31S, predisposes to hypertrophic cardiomyopathy and ventricular fibrillation Structure and function of cardiac troponin C (TNNC1): Implications for heart failure, cardiomyopathies, and troponin modulating drugs Allosteric Transmission along a Loosely Structured Backbone Allows a Cardiac Troponin C Mutant to Function with Only One Ca2+ Ion.Pathogenic peptide deviations support a model of adaptive evolution of chordate cardiac performance by troponin mutations.In vivo cardiovascular magnetic resonance diffusion tensor imaging shows evidence of abnormal myocardial laminar orientations and mobility in hypertrophic cardiomyopathy.Hypertrophic Cardiomyopathy Cardiac Troponin C Mutations Differentially Affect Slow Skeletal and Cardiac Muscle Regulation.Amide hydrogens reveal a temperature-dependent structural transition that enhances site-II Ca2+-binding affinity in a C-domain mutant of cardiac troponin C Effect of calcium-sensitizing mutations on calcium binding and exchange with troponin C in increasingly complex biochemical systems.A dilated cardiomyopathy troponin C mutation lowers contractile force by reducing strong myosin-actin binding The RCK1 domain of the human BKCa channel transduces Ca2+ binding into structural rearrangements Genetics of hypertrophic cardiomyopathy.Predicting cardiomyopathic phenotypes by altering Ca2+ affinity of cardiac troponin C.Strong cross-bridges potentiate the Ca(2+) affinity changes produced by hypertrophic cardiomyopathy cardiac troponin C mutants in myofilaments: a fast kinetic approach.Familial hypertrophic cardiomyopathy related cardiac troponin C L29Q mutation alters length-dependent activation and functional effects of phosphomimetic troponin I*Fetal cardiac troponin isoforms rescue the increased Ca2+ sensitivity produced by a novel double deletion in cardiac troponin T linked to restrictive cardiomyopathy: a clinical, genetic, and functional approach Functional characterization of TNNC1 rare variants identified in dilated cardiomyopathy.S-Nitrosylation of Calcium-Handling Proteins in Cardiac Adrenergic Signaling and Hypertrophy In Vivo Analysis of Troponin C Knock-In (A8V) Mice: Evidence that TNNC1 Is a Hypertrophic Cardiomyopathy Susceptibility Gene Enhanced troponin I binding explains the functional changes produced by the hypertrophic cardiomyopathy mutation A8V of cardiac troponin C Molecular basis of hereditary cardiomyopathy: abnormalities in calcium sensitivity, stretch response, stress response and beyond.The myosin-activated thin filament regulatory state, M⁻-open: a link to hypertrophic cardiomyopathy (HCM).Biochemical characterisation of Troponin C mutations causing hypertrophic and dilated cardiomyopathies.Cardiac troponin structure-function and the influence of hypertrophic cardiomyopathy associated mutations on modulation of contractility.Changes in the dynamics of the cardiac troponin C molecule explain the effects of Ca2+-sensitizing mutations.Hypertrophic cardiomyopathy-linked mutation D145E drastically alters calcium binding by the C-domain of cardiac troponin C.Effect of hypertrophic cardiomyopathy-linked troponin C mutations on the response of reconstituted thin filaments to calcium upon troponin I phosphorylation.Pathogenesis associated with a restrictive cardiomyopathy mutant in cardiac troponin T is due to reduced protein stability and greatly increased myofilament Ca2+ sensitivity.Beyond the cardiac myofilament: hypertrophic cardiomyopathy- associated mutations in genes that encode calcium-handling proteins.Characterization of Zebrafish Cardiac and Slow Skeletal Troponin C Paralogs by MD Simulation and ITC.Evidence for troponin C (TNNC1) as a gene for autosomal recessive restrictive cardiomyopathy with fatal outcome in infancy.

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A functional and structural study of troponin C mutations related to hypertrophic cardiomyopathy.

http://www.wikidata.org/entity/Q37254027

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

@tr

scientific article published on 12 May 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

@cs

name

A functional and structural st ...... o hypertrophic cardiomyopathy.

@en

A functional and structural st ...... o hypertrophic cardiomyopathy.

@nl

type

label

A functional and structural st ...... o hypertrophic cardiomyopathy.

@en

A functional and structural st ...... o hypertrophic cardiomyopathy.

@nl

prefLabel

A functional and structural st ...... o hypertrophic cardiomyopathy.

@en

A functional and structural st ...... o hypertrophic cardiomyopathy.

@nl

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JBC.M109.007021

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Journal of Biological Chemistry

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A functional and structural st ...... to hypertrophic cardiomyopathy

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James D Potter

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Jingsheng Liang

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Michael J Ackerman

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Michelle A Jones

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Michelle S Parvatiyar

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P2860

Familial hypertrophic cardiomyopathy mutations in the regulatory light chains of myosin affect their structure, Ca2+ binding, and phosphorylation

Cardiac troponin T isoforms affect the Ca2+ sensitivity and inhibition of force development. Insights into the role of troponin T isoforms in the heart

A troponin T mutation that causes infantile restrictive cardiomyopathy increases Ca2+ sensitivity of force development and impairs the inhibitory properties of troponin

Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form

Crystal structure of troponin C in complex with troponin I fragment at 2.3-A resolution

Refined structure of chicken skeletal muscle troponin C in the two-calcium state at 2-A resolution

Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 A resolution

First mutation in cardiac troponin C, L29Q, in a patient with hypertrophic cardiomyopathy

The failing heart

Calcium plays distinctive structural roles in the N- and C-terminal domains of cardiac troponin C

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19090-19100

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scholarly article

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10.1074/JBC.M109.007021

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28

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284

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José Renato Pinto

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2009-05-12T00:00:00Z

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19439414

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