About: A role for C-protein in the regulation of contraction and intracellular Ca2+ in intact rat ventricular myocytes

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About: A role for C-protein in the regulation of contraction and intracellular Ca2+ in intact rat ventricular myocytes Goto Sponge NotDistinct Permalink

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scientific article published on 01 October 2000

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в жовтні 2000 (uk) im Oktober 2000 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'ochobre de 2000 (ast) scientific article published on 01 October 2000 (en)
publication date	wds:Q73038647-4F8BF828-EF01-47B7-ADE2-6924CE5C6DCF
publication date	2000-10-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q73038647-8B6E6EA0-0E75-45B1-B795-17C9C9D25B50
language of work or name	English
cites work	wds:Q73038647-009D04E0-D4AE-4D91-ADD9-E5AB1B1BEBB1 wds:Q73038647-09110184-A898-4A59-AF90-5562FFC0723F wds:Q73038647-0EA9EA8D-2675-4992-B091-8CDBC6DE6B94 wds:Q73038647-16FE36AF-E8B6-408D-8EB2-388A153BD867 wds:Q73038647-238D9EE2-76C0-45C4-A4F0-A2348880D928 wds:Q73038647-26134B49-80D8-4C9C-9438-77A5B9D461E9 wds:Q73038647-2DB251EF-120C-41D0-AB1B-22F949AD85C3 wds:Q73038647-3B50FFA1-255E-400C-9313-B78BC841CD21 wds:Q73038647-45102F25-E266-408C-97E4-94303300FEE6 wds:Q73038647-51DFDA41-3C73-4A0C-884E-A3A2D9EE6EB2 wds:Q73038647-83275722-5675-4C2C-933E-27EA0E1FB572 wds:Q73038647-8877E6E7-2F63-4BDF-BC21-91774AC94F31 wds:Q73038647-9B3CDBA7-D534-4A31-A51D-5D73C0B7C226 wds:Q73038647-B5AD2FF1-4496-4EC8-8E23-CEF88F701077 wds:Q73038647-BAB9F6DE-D66D-48D7-AB19-7049E053E85E wds:Q73038647-BF366583-4861-44FD-8FC7-16557802F953 wds:Q73038647-CE7B45A5-CC73-46DB-9A9F-A084DEA4C66B wds:Q73038647-D48B2E07-71DD-4971-A9AB-97A3807403F1 wds:Q73038647-D9EC32A3-A8B3-4439-A1B2-D7EC0094E405 wds:Q73038647-DD22611E-9E8C-47FC-AE00-2B5BF07D71BA wds:Q73038647-EE559C58-76BF-4D78-90E8-A2053CAE2EE8 wds:Q73038647-F7F651D0-E0BD-4831-96CB-37BFC3D44FB3
cites work	Comparison of putative cooperative mechanisms in cardiac muscle: length dependence and dynamic responses The interaction of C-protein with heavy meromyosin and subfragment-2 Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle Alterations in Ca2+ sensitive tension due to partial extraction of C-protein from rat skinned cardiac myocytes and rabbit skeletal muscle fibers Interaction of C-protein with myosin, myosin rod and light meromyosin The major myosin-binding domain of skeletal muscle MyBP-C (C protein) resides in the COOH-terminal, immunoglobulin C2 motif. cAPK-phosphorylation controls the interaction of the regulatory domain of cardiac myosin binding protein C with myosin-S2 in an on-off fashion Phosphorylation of purified cardiac muscle C-protein by purified cAMP-dependent and endogenous Ca2+-calmodulin-dependent protein kinases Cardiac myosin binding protein C The C-protein (myosin binding protein C) family: regulators of contraction and sarcomere formation? Steric-model for activation of muscle thin filaments 1 1 Edited by P.E. Wright Co-ordinated changes in cAMP, phosphorylated phospholamban, Ca2+ and contraction following beta-adrenergic stimulation of rat heart. Contractile protein mutations and heart disease Phosphorylation of a myofibrillar protein of Mr 150 000 in perfused rat heart, and the tentative indentification of this as C-protein A mouse model of myosin binding protein C human familial hypertrophic cardiomyopathy The role of calcium in the response of cardiac muscle to stretch Myosin binding protein C, a phosphorylation-dependent force regulator in muscle that controls the attachment of myosin heads by its interaction with myosin S2 A method for reversible permeabilization of isolated rat ventricular myocytes. Cardiac Myosin-binding protein C and hypertrophic cardiomyopathy. Approximate dimensions of membrane lesions produced by streptolysin S and streptolysin O Diastolic, systolic and sarcoplasmic reticulum [Ca2+] during inotropic interventions in isolated rat myocytes Crystalline tubes of myosin subfragment-2 showing the coiled-coil and molecular interaction geometry
author name string	wds:Q73038647-1103D804-C847-4299-AB0A-5B01345F956B wds:Q73038647-43F699DE-6100-47BE-9DE8-B71F50159C53 wds:Q73038647-9230B080-AE77-4249-8577-6D7CFBC30830 wds:Q73038647-B89E4B3E-FFD2-45C7-9E63-F1A3372E617A
author name string	E White S C Calaghan J Trinick P J Knight
rdfs:label	A role for C-protein in the regulation of contraction and intracellular Ca2+ in intact rat ventricular myocytes (en) A role for C-protein in the regulation of contraction and intracellular Ca2+ in intact rat ventricular myocytes (nl)
skos:prefLabel	A role for C-protein in the regulation of contraction and intracellular Ca2+ in intact rat ventricular myocytes (en) A role for C-protein in the regulation of contraction and intracellular Ca2+ in intact rat ventricular myocytes (nl)
name	A role for C-protein in the regulation of contraction and intracellular Ca2+ in intact rat ventricular myocytes (en) A role for C-protein in the regulation of contraction and intracellular Ca2+ in intact rat ventricular myocytes (nl)
title	wds:Q73038647-82E94B74-15E2-4ABE-AC95-439F28C900DB
title	A role for C-protein in the regulation of contraction and intracellular Ca2+ in intact rat ventricular myocytes (en)
page(s)	wds:Q73038647-BDC36166-0D42-45C8-82FA-7CFB12EC74E7
page(s)	151-156
instance of	wds:Q73038647-0CDE2D84-19BE-46F6-AA5B-76D5BDAA261C
instance of	scholarly article
PubMed ID	wds:Q73038647-8676CECB-5A4C-4CD9-A60A-9C803F08C4DC
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11018113
PubMed ID	11018113
published in	wds:Q73038647-47AEF50F-7EC8-487A-B4B4-B885386F0119
published in	Journal of Physiology
volume	wds:Q73038647-99ADC952-3B9F-4C41-BDFA-00F598B2B86E
volume	528 Pt 1
DOI	wds:Q73038647-43B80584-16A1-4632-A70B-014B306097A2
DOI	http://dx.doi.org/10.1111/J.1469-7793.2000.00151.X
DOI	10.1111/J.1469-7793.2000.00151.X
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q73038647
is cites work of	Cardiac myosin binding protein C: its role in physiology and disease Ablation of myosin-binding protein-C accelerates force development in mouse myocardium Structural evidence for the interaction of C-protein (MyBP-C) with actin and sequence identification of a possible actin-binding domain. Cardiac myosin binding protein C and its phosphorylation regulate multiple steps in the cross-bridge cycle of muscle contraction The extent of cardiac myosin binding protein-C phosphorylation modulates actomyosin function in a graded manner Cardiac myosin binding protein-C modulates actomyosin binding and kinetics in the in vitro motility assay Structure, interactions and function of the N-terminus of cardiac myosin binding protein C (MyBP-C): who does what, with what, and to whom? Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin The myosin-binding protein C motif binds to F-actin in a phosphorylation-sensitive manner Contribution of the myosin binding protein C motif to functional effects in permeabilized rat trabeculae Radial displacement of myosin cross-bridges in mouse myocardium due to ablation of myosin binding protein-C Effect of MyBP-C binding to actin on contractility in heart muscle Myosin binding protein-C: a regulator of actomyosin interaction in striated muscle Resolving myoarchitectural disarray in the mouse ventricular wall with diffusion spectrum magnetic resonance imaging. C0 and C1 N-terminal Ig domains of myosin binding protein C exert different effects on thin filament activation.

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