Altered inhibitory and troponin C-binding activities in cardiac troponin I mutants known to cause hypertrophic cardiomyopathy

Altered inhibitory and troponin C-binding activities in cardiac troponin I mutants known to cause hypertrophic cardiomyopathy

Xehetasun bibliografikoak
Egile Nagusiak:	Elliott, K, Watkins, H, Redwood, C
Formatua:	Journal article
Argitaratua:	2000

Antzeko izenburuak

Altered regulatory properties of human cardiac troponin I mutants that cause hypertrophic cardiomyopathy.
nork: Elliott, K, et al.
Argitaratua: (2000)

Alterations in thin filament regulation induced by a human cardiac troponin T mutant that causes dilated cardiomyopathy are distinct from those induced by troponin T mutants that cause hypertrophic cardiomyopathy.
nork: Robinson, P, et al.
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A troponin I mutant known to cause hypertrophic cardiomyopathy shows reduced inhibition of Ca2+ independent tension
nork: Burton, D, et al.
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The effect of HCM mutations in troponin T and troponin I on the calcium binding of human cardiac troponin
nork: Redwood, C, et al.
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Two mutations in human cardiac troponin I known to cause hypertrophic cardiomyopathy have different effects on cardiac muscle contraction
nork: Burton, D, et al.
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Investigation of troponin I mutations causing familial hypertrophic cardiomyopathy
nork: Abdulrazzak, H, et al.
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Two mutations in troponin I that cause hypertrophic cardiomyopathy have contrasting effects on cardiac muscle contractility.
nork: Burton, D, et al.
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Effects of hypertrophic cardiomyopathy mutations in troponin I on contractility of skinned cardiac muscle fibres
nork: Burton, D, et al.
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Comparison of the functional effects of mutations in troponin T which cause dilated and hypertrophic cardiomyopathies
nork: Robinson, P, et al.
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Investigating the Effect of Cardiomyopathy-Causing Mutations in Cardiac Troponin-T on Calcium Buffering In Situ
nork: Robinson, P, et al.
Argitaratua: (2010)

Investigation of a truncated cardiac troponin T that causes familial hypertrophic cardiomyopathy: Ca(2+) regulatory properties of reconstituted thin filaments depend on the ratio of mutant to wild-type protein.
nork: Redwood, C, et al.
Argitaratua: (2000)

Dilated and hypertrophic cardiomyopathy mutations in troponin and alpha-tropomyosin have opposing effects on the calcium affinity of cardiac thin filaments.
nork: Robinson, P, et al.
Argitaratua: (2007)

DCM troponin C mutant Gly159Asp blunts the response to troponin phosphorylation.
nork: Preston, L, et al.
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Dilated cardiomyopathy causing mutations in cardiac troponin T (TNT), cardiac troponin C (TNC), and alpha tropomyosin (TM) reduce CA(2+) sensitivity and maximum calcium activation
nork: Redwood, C, et al.
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Myofibrillar Ca(2+) sensitivity is uncoupled from troponin I phosphorylation in hypertrophic obstructive cardiomyopathy due to abnormal troponin T.
nork: Bayliss, C, et al.
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Severe disease expression of cardiac troponin C and T mutations in patients with idiopathic dilated cardiomyopathy.
nork: Mogensen, J, et al.
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Functional effects of mutations in troponin T and tropomyosin which cause dilated cardiomyopathy
nork: Robinson, P, et al.
Argitaratua: (2003)

Using fluorescence emission spectroscopy to asses the Ca2+ affinity of reconstituted troponin and thin filaments containing cardiomyopathy causing mutations of troponin and alpha-tropomyosin
nork: Robinson, P, et al.
Argitaratua: (2007)

Hypertrophic and dilated cardiomyopathycausing mutations of troponin and alpha-tropomyosin have opposite effects on thin filament calcium binding
nork: Robinson, P, et al.
Argitaratua: (2007)

A revised method of troponin exchange in permeabilised cardiac trabeculae using vanadate: functional consequences of a HCM-causing mutation in troponin I.
nork: Preston, L, et al.
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Mutations in troponin T associated with Hypertrophic Cardiomyopathy increase Ca2+-sensitivity and suppress the modulation of Ca2+-sensitivity by troponin I phosphorylation
nork: Messer, A, et al.
Argitaratua: (2016)

Structure-function relationships of eight mutations in troponin and tropomyosin that cause dilated cardiomyopathy
nork: Mirza, M, et al.
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Elevated high-sensitivity troponin T levels are associated with adverse cardiac remodelling and myocardial fibrosis in hypertrophic cardiomyopathy
nork: Stefanie Hasler, et al.
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Elevated high-sensitivity cardiac troponin is associated with hypertrophy and fibrosis assessed with CMR in patients with hypertrophic cardiomyopathy
nork: Gommans Frank, et al.
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Mutations in fast skeletal troponin I, troponin T, and beta-tropomyosin that cause distal arthrogryposis all increase contractile function.
nork: Robinson, P, et al.
Argitaratua: (2007)

Identification and functional analysis of cardiac troponin I as a novel disease gene in autosomal dominant familial dilated cardiomyopathy
nork: Carballo, S, et al.
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Effect of hypertrophic cardiomyopathy mutations in human cardiac muscle alpha -tropomyosin (Asp175Asn and Glu180Gly) on the regulatory properties of human cardiac troponin determined by in vitro motility assay.
nork: Bing, W, et al.
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Focus on cardiac troponin complex: From gene expression to cardiomyopathy
nork: Rosetta Ragusa, et al.
Argitaratua: (2024-11-01)

Nutraceuticals silybin B, resveratrol, and epigallocatechin-3 gallate-bind to cardiac muscle troponin to restore the loss of lusitropy caused by cardiomyopathy mutations in vitro, in vivo, and in silico
nork: Zeyu Yang, et al.
Argitaratua: (2024-12-01)

Functional effects of the DCM mutant Gly159Asp troponin C in skinned muscle fibres.
nork: Preston, L, et al.
Argitaratua: (2007)

High-sensitive cardiac troponin T and NT-proBNP are associated with the left ventricular apical thickness in apical hypertrophic cardiomyopathy
nork: Meng Zhang, et al.
Argitaratua: (2025-01-01)

Nutraceuticals silybin B, resveratrol, and epigallocatechin-3 gallate-bind to cardiac muscle troponin to restore the loss of lusitropy caused by cardiomyopathy mutations in vitro, in vivo, and in silico
nork: Yang, Z, et al.
Argitaratua: (2024)

Ca2+regulatory properties of a truncated troponin T that causes FHC depend on the ratio of mutant to wild-type peptide.
nork: Redwood, C, et al.
Argitaratua: (2000)

Identification and functional characterization of cardiac troponin I as a novel disease gene in autosomal dominant dilated cardiomyopathy.
nork: Carballo, S, et al.
Argitaratua: (2009)

Mutations in fast skeletal troponin I, troponin T and beta-tropomyosin that cause distal arthrogryposis all enhance thin filament activation
nork: Robinson, P, et al.
Argitaratua: (2005)

Cardiac troponin I is a potential novel substrate for AMP-activated protein kinase
nork: Oliveira, S, et al.
Argitaratua: (2007)

Exercise‐Induced Cardiac Troponin I Elevation Is Associated With Regional Alterations in Left Ventricular Strain in High‐Troponin Responders
nork: Christine Bjørkvik Erevik, et al.
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AMP-Activated Protein Kinase Phosphorylates Cardiac Troponin I and Alters Contractility of Murine Ventricular Myocytes
nork: Oliveira, S, et al.
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AMP-Activated protein kinase phosphorylates cardiac troponin i and alters contractility of murine ventricular myocytes
nork: Oliveira, S, et al.
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AMP-activated protein kinase phosphorylates cardiac troponin I and alters contractility of murine ventricular myocytes.
nork: Oliveira, S, et al.
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