Pathogenic properties of the N-terminal region of cardiac myosin binding protein-C in vitro
about
Post-translational control of cardiac hemodynamics through myosin binding protein CGSK3β phosphorylates newly identified site in the proline-alanine-rich region of cardiac myosin-binding protein C and alters cross-bridge cycling kinetics in human: short communicationMyocardial infarction-induced N-terminal fragment of cardiac myosin-binding protein C (cMyBP-C) impairs myofilament function in human myocardiumSingle molecule force spectroscopy on titin implicates immunoglobulin domain stability as a cardiac disease mechanism.Cardiac Myosin Binding Protein-C Autoantibodies are Potential Early Indicators of Cardiac Dysfunction and Patient Outcome in Acute Coronary SyndromeSurviving the infarct: A profile of cardiac myosin binding protein-C pathogenicity, diagnostic utility, and proteomics in the ischemic myocardium.Chemokine (C-X-C motif) receptor 4 and atypical chemokine receptor 3 regulate vascular α₁-adrenergic receptor function.A hypertrophic cardiomyopathy-associated MYBPC3 mutation common in populations of South Asian descent causes contractile dysfunctionIncrease in cardiac myosin binding protein-C plasma levels is a sensitive and cardiac-specific biomarker of myocardial infarction.Characterization of the cardiac myosin binding protein-C phosphoproteome in healthy and failing human heartsA gain-of-function mutation in the M-domain of cardiac myosin-binding protein-C increases binding to actin.An endogenously produced fragment of cardiac myosin-binding protein C is pathogenic and can lead to heart failureRelease kinetics of circulating cardiac myosin binding protein-C following cardiac injury.MYBPC3's alternate ending: consequences and therapeutic implications of a highly prevalent 25 bp deletion mutationContractile dysfunction in a mouse model expressing a heterozygous MYBPC3 mutation associated with hypertrophic cardiomyopathy.Hypertrophic cardiomyopathy and the myosin mesa: viewing an old disease in a new light.N-terminal fragment of cardiac myosin binding protein-C triggers pro-inflammatory responses in vitro.Skeletal myosin binding protein-C isoforms regulate thin filament activity in a Ca2+-dependent manner.Sarcomeric protein modification during adrenergic stress enhances cross-bridge kinetics and cardiac output.
P2860
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P2860
Pathogenic properties of the N-terminal region of cardiac myosin binding protein-C in vitro
description
2012 nî lūn-bûn
@nan
2012 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Pathogenic properties of the N ...... sin binding protein-C in vitro
@ast
Pathogenic properties of the N ...... sin binding protein-C in vitro
@en
Pathogenic properties of the N ...... sin binding protein-C in vitro
@nl
type
label
Pathogenic properties of the N ...... sin binding protein-C in vitro
@ast
Pathogenic properties of the N ...... sin binding protein-C in vitro
@en
Pathogenic properties of the N ...... sin binding protein-C in vitro
@nl
prefLabel
Pathogenic properties of the N ...... sin binding protein-C in vitro
@ast
Pathogenic properties of the N ...... sin binding protein-C in vitro
@en
Pathogenic properties of the N ...... sin binding protein-C in vitro
@nl
P2093
P2860
P1476
Pathogenic properties of the N ...... sin binding protein-C in vitro
@en
P2093
Jason Sarkey
Mahesh P Gupta
Nagalingam R Sundaresan
Pieter P de Tombe
Sakthivel Sadayappan
Suresh Govindan
P2860
P2888
P356
10.1007/S10974-012-9292-Y
P407
P577
2012-05-01T00:00:00Z
P5875
P6179
1036036412