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Long term ablation of protein kinase A (PKA)-mediated cardiac troponin I phosphorylation leads to excitation-contraction uncoupling and diastolic dysfunction in a knock-in mouse model of hypertrophic cardiomyopathyA mutation in TNNC1-encoded cardiac troponin C, TNNC1-A31S, predisposes to hypertrophic cardiomyopathy and ventricular fibrillationMolecular and functional characterization of novel hypertrophic cardiomyopathy susceptibility mutations in TNNC1-encoded troponin CAllosteric Transmission along a Loosely Structured Backbone Allows a Cardiac Troponin C Mutant to Function with Only One Ca2+ Ion.Myofilament Ca2+ sensitization causes susceptibility to cardiac arrhythmia in mice.Correcting diastolic dysfunction by Ca2+ desensitizing troponin in a transgenic mouse model of restrictive cardiomyopathyHypertrophic 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 CA dilated cardiomyopathy troponin C mutation lowers contractile force by reducing strong myosin-actin bindingGenotype-specific pathogenic effects in human dilated cardiomyopathy.Strong cross-bridges potentiate the Ca(2+) affinity changes produced by hypertrophic cardiomyopathy cardiac troponin C mutants in myofilaments: a fast kinetic approach.Structural and protein interaction effects of hypertrophic and dilated cardiomyopathic mutations in alpha-tropomyosin.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 approachFunctional characterization of TNNC1 rare variants identified in dilated cardiomyopathy.Constitutive phosphorylation of cardiac myosin regulatory light chain in vivoAbsence of myocardial thyroid hormone inactivating deiodinase results in restrictive cardiomyopathy in miceFluorescent Protein-Based Ca2+ Sensor Reveals Global, Divalent Cation-Dependent Conformational Changes in Cardiac Troponin CIn Vivo Analysis of Troponin C Knock-In (A8V) Mice: Evidence that TNNC1 Is a Hypertrophic Cardiomyopathy Susceptibility GeneS-Nitrosylation of Sarcomeric Proteins Depresses Myofilament Ca2+)Sensitivity in Intact Cardiomyocytes.Functional consequences of the human cardiac troponin I hypertrophic cardiomyopathy mutation R145G in transgenic miceAnalysis of the molecular pathogenesis of cardiomyopathy-causing cTnT mutants I79N, ΔE96, and ΔK210.Myofilament calcium de-sensitization and contractile uncoupling prevent pause-triggered ventricular tachycardia in mouse hearts with chronic myocardial infarctionEnhanced troponin I binding explains the functional changes produced by the hypertrophic cardiomyopathy mutation A8V of cardiac troponin CA functional and structural study of troponin C mutations related to hypertrophic cardiomyopathy.Will you still need me (Ca2+ , TnT, and DHPR), will you still cleave me (calpain), when I'm 64?Increases of desmin and α-actinin in mouse cardiac myofibrils as a response to diastolic dysfunction.Myosin cross-bridges do not form precise rigor bonds in hypertrophic heart muscle carrying troponin T mutations.Pathogenesis associated with a restrictive cardiomyopathy mutant in cardiac troponin T is due to reduced protein stability and greatly increased myofilament Ca2+ sensitivity.Troponin C Mutations Partially Stabilize the Active State of Regulated Actin and Fully Stabilize the Active State When Paired with Δ14 TnT.Ca(2+) and Mg(2+) binding to weak sites of TnC C-domain induces exposure of a large hydrophobic surface that leads to loss of TnC from the thin filament.Pathogenesis of depression- and anxiety-like behavior in an animal model of hypertrophic cardiomyopathy.Chemical treatment of mica for atomic force microscopy can affect biological sample conformation.Correction to Troponin C Mutations Partially Stabilize the Active State of Regulated Actin and Fully Stabilize the Active State When Paired with Δ14 TnT.Troponin through the looking-glass: emerging roles beyond regulation of striated muscle contraction.Hypertrophic cardiomyopathy-linked mutation in troponin T causes myofibrillar disarray and pro-arrhythmic action potential changes in human iPSC cardiomyocytes.Myosin Rod Hypophosphorylation and CB Kinetics in Papillary Muscles from a TnC-A8V KI Mouse Model.Oxidative Stress in Muscle Diseases: Current and Future Therapy.Structural and functional impact of troponin C-mediated Ca2+ sensitization on myofilament lattice spacing and cross-bridge mechanics in mouse cardiac muscleIonic interventions that alter the association of troponin C C-domain with the thin filaments of vertebrate striated muscleRedox state of troponin C cysteine in the D/E helix alters the C-domain affinity for the thin filament of vertebrate striated muscle
P50
Q28242903-B8D7F4B8-34F4-4B08-925A-FFAF59A60338Q28271478-26DC7B5D-88F6-4D77-B671-5DA43CB92CBBQ28284750-BE564537-386B-421C-9646-4C87DC2899ACQ30397033-4EB6099D-0EDA-4C05-A579-9321EAB99E92Q30484558-9BCCB0AE-00AF-40AE-967B-7372327E9E01Q33573193-5DB49F1A-171B-4E62-8EAC-C12B46F961E7Q33580919-6A6025FC-18F3-4242-96B9-474DF4F53F71Q33677442-CE4FD361-7161-4D47-840C-6805F86BEDB9Q33885078-69D44083-45FA-49CE-A18B-AB12443FFAAFQ33903336-1C9D6C2E-096F-490A-A8C0-6D96E3EFB7D7Q34488809-D1967BAD-6249-4452-89C8-BFC9560F54B9Q34608346-64CC3164-576D-4B2B-B561-F6E43D3003D4Q35063399-C6B3C1BD-0766-4647-B71B-7851BE596757Q35311290-6E69B795-7F0B-411C-8CBA-AD5082FF240FQ35536235-FEFFBDE9-9082-4B29-AE95-F2CCFCA224E8Q35970123-188DA96E-F376-4821-B519-BF3305718ABAQ36162541-456D4687-4649-4409-8FC8-8197028B7C50Q36200058-89C83ACE-EABD-4329-B884-09D8613269FBQ36291728-5E0BD2F4-D987-4EAF-BD13-B0DE3FDF1DA9Q36761860-8C438D70-36E6-44F7-9AE5-B3480739C458Q36824519-537FAD8C-3956-45A0-BE3C-BF122E68E8A9Q36931825-EBBB5E0B-DC9F-45BB-A751-96A47CDD112BQ36984342-056A7534-6CCB-458A-8C12-87DACD797BE6Q37254027-E6C941F7-9937-472F-B7C3-7981BE6768F1Q37678236-F7652A5E-0C05-4413-955B-23EB4505C4ABQ40361803-7DD3EDD1-56C4-4920-9559-2D396BA45A35Q41836543-6A401B58-5A78-495A-850C-7FEA2C14382FQ41949346-A677BC6F-5C6D-43B2-8A36-674E944A3A30Q46362689-A2C671FB-3EC7-4B30-84EF-A72ED91DD795Q46720169-6E32C9B0-1E23-4BA4-8A5D-22BD68D585DBQ47340487-84C3CC01-23D5-4736-B6DB-845230131DCFQ47835649-9035C9A4-5BE1-4F55-B9BA-31148ED27334Q48137054-39359F66-66C3-4C18-A4DF-232C0B38DB17Q49376239-48AE6C44-81D5-45AE-9058-B7E7A2DDE1D4Q50022359-572C8CA6-929E-4D65-86C6-5F5CAB0DBBD4Q51033685-D597C10F-EEEF-4ACE-8915-B89845D356A8Q55191328-7BC9316C-39E2-4450-8042-5B77D517701CQ58903690-EC74D22C-7708-4A52-AA96-FED1408ED7B9Q81510669-E1F7E32C-9D8A-459A-8C9D-12B426BBE989Q82824958-B0FF7FD2-DE84-48C1-BE16-A76F11ED0203
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
José Renato Pinto
@ast
José Renato Pinto
@en
José Renato Pinto
@es
José Renato Pinto
@nl
José Renato Pinto
@sl
type
label
José Renato Pinto
@ast
José Renato Pinto
@en
José Renato Pinto
@es
José Renato Pinto
@nl
José Renato Pinto
@sl
prefLabel
José Renato Pinto
@ast
José Renato Pinto
@en
José Renato Pinto
@es
José Renato Pinto
@nl
José Renato Pinto
@sl
P1053
H-2631-2017
P106
P21
P2798
P31
P3829
P496
0000-0001-9092-4976