About: Cooperation within actin filament in vertebrate skeletal muscle

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About: Cooperation within actin filament in vertebrate skeletal muscle Goto Sponge NotDistinct Permalink

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scientific article published on 01 July 1972

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в липні 1972 (uk) im Juli 1972 veröffentlichter wissenschaftlicher Artikel (de) scientific article published on 01 July 1972 (en) artículu científicu espublizáu en xunetu de 1972 (ast)
publication date	wds:Q68494566-D5299ECB-6A12-4630-8A98-56B6619C8200
publication date	1972-07-01 00:00:00Z (xsd:dateTime)
cites work	wds:Q68494566-068F59C6-3C2A-4C32-A738-2D82483FCAC3 wds:Q68494566-0D4B944D-6EBD-4492-BC51-B70D4A7CCF5C wds:Q68494566-1CD0CD7C-17C5-45D6-A2C5-C3A19224CF4E wds:Q68494566-271A6933-D24B-4298-B8B5-52BF00716C4E wds:Q68494566-282C8EEB-ACA5-40C8-BC44-DFD30E5AEE1E wds:Q68494566-31E03A42-3E72-4C2A-8810-0F0F0B771EE2 wds:Q68494566-4377FC4D-D8B3-4D00-A495-86652EDC935A wds:Q68494566-44906B5A-3F21-44BA-8C29-B5C9B4534A8D wds:Q68494566-491D7AE6-F28E-41EA-8633-E6B7B8557C02 wds:Q68494566-578031AE-1BE2-41BF-BE65-FD3E78FFE73B wds:Q68494566-61DF69B6-444E-4116-8C28-58192BE4490A wds:Q68494566-658C49DC-54DF-4690-BE08-07E2B0E4236D wds:Q68494566-6E149EB1-13C0-4E65-990B-CF1DC3B045BD wds:Q68494566-90689303-085C-4B1A-9B42-5FDB81958AF3 wds:Q68494566-A6BACA2C-B5EB-42C1-82D2-7CACD291C697 wds:Q68494566-AA34B0C6-75F2-46CC-BC03-B0E697AA36AF wds:Q68494566-B1E0E7A6-5B09-467F-89D9-B7BCEB893769 wds:Q68494566-BA4CB5F0-5D5F-4031-BA40-DA8CE44B0AF0 wds:Q68494566-C681EFB0-2846-4B93-AB49-D5C849A57767 wds:Q68494566-D13A0BCB-D525-40D4-A32A-1E6E6620A125 wds:Q68494566-D89C5E52-2642-4E8A-BA87-3634B4C14183 wds:Q68494566-FB5F6ED1-9B53-4487-ABFA-207ACAAB5EBD
cites work	Mechanism of adenosine triphosphate hydrolysis by actomyosin THE REGULATION OF MYOFIBRILLAR ACTIVITY BY CALCIUM A NEW PROTEIN COMPONENT PARTICIPATING IN THE SUPERPRECIPITATION OF MYOSIN B Quantitative studies on the structure of cross-striated myofibrils. II. Investigations by biochemical techniques Troponin and Its Components* The role of magnesium in the relaxation of myofibrils Optical diffraction studies of myofibrillar structure. Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation Conformational changes in the molecular control of muscle contraction. Control of muscle contraction Regulation in molluscan muscles Periodic distribution of troponin along the thin filament. Studies on the structural basis of the interaction of myosin and actin Troponin. I. Preparation and physiological function The contractile and control sites of natural actomyosin Regulation of tension in the skinned crayfish muscle fiber. I. Contraction and relaxation in the absence of Ca (pCa is greater than 9) Rigor contraction and the effect of various phosphate compounds on glycerinated insect flight and vertebrate muscle. Equilibrium binding of adenosine diphosphate to myosin. The binding of adenosine triphosphate to myosin. The site of calcium binding in relation to the activation of myofibrillar contraction Calcium binding by the troponin complex, and the purification and properties of troponin A Actin and bound-nucleotide stoichiometry
author name string	wds:Q68494566-14F176A2-A6B2-4032-914B-ADD39098EBB0 wds:Q68494566-8B032B92-1248-44AB-9214-2AADE15D6E6F
author name string	A Weber R D Bremel
rdfs:label	Cooperation within actin filament in vertebrate skeletal muscle (en) Cooperation within actin filament in vertebrate skeletal muscle (nl)
skos:prefLabel	Cooperation within actin filament in vertebrate skeletal muscle (en) Cooperation within actin filament in vertebrate skeletal muscle (nl)
name	Cooperation within actin filament in vertebrate skeletal muscle (en) Cooperation within actin filament in vertebrate skeletal muscle (nl)
title	wds:Q68494566-2772319D-66F1-4E7F-A1B6-55E10F08981F
title	Cooperation within actin filament in vertebrate skeletal muscle (en)
page(s)	wds:Q68494566-F92B7F2B-3C04-4DE5-ADB6-484D9A20B28B
page(s)	97-101
instance of	wds:Q68494566-957844BC-B201-4F98-9A7F-1C89C2DA0DFD
instance of	scholarly article
main subject	wds:Q68494566-4FD39819-5A44-4614-ACA0-DC441C4999EF wds:Q68494566-B4815047-28EB-402C-A26E-D11F170E26F8
main subject	cooperation actin filament
PubMed ID	wds:Q68494566-6AFD121F-B8C7-4B6F-9D29-7B9AA35D853A
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4261616
PubMed ID	4261616
published in	wds:Q68494566-70573674-A3E6-4525-BF99-91B7F022C999
published in	Nature: New Biology
issue	wds:Q68494566-EE0AB7D0-93DD-4192-A4FD-549136A02ADD
volume	wds:Q68494566-9D1194F2-83AF-4293-837A-9A837C6CF399
issue	82
volume	238
DOI	wds:Q68494566-24855575-EFA0-42C2-8896-5F4E403947CF
DOI	http://dx.doi.org/10.1038/NEWBIO238097A0
DOI	10.1038/NEWBIO238097A0
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q68494566
is cites work of	Multi-scale computational models of familial hypertrophic cardiomyopathy: genotype to phenotype Ca2+ dependence of tension and ADP production in segments of chemically skinned muscle fibers Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers. Implications for twitch potentiation in intact muscle Alterations in Ca2+ sensitive tension due to partial extraction of C-protein from rat skinned cardiac myocytes and rabbit skeletal muscle fibers The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase Regulation of actomyosin ATPase by a single calcium-binding site on troponin C from crayfish Ca-activation and stretch-activation in insect flight muscle. The effect of partial extraction of troponin C on the elementary steps of the cross-bridge cycle in rabbit psoas muscle fibers Can the binding of Ca2+ to two regulatory sites on troponin C determine the steep pCa/tension relationship of skeletal muscle? Two rigor states in skinned crayfish single muscle fibers A fluorescence stopped flow analysis of Ca2+ exchange with troponin C Calcium-independent activation of skeletal muscle fibers by a modified form of cardiac troponin C Tension in mechanically disrupted mammalian cardiac cells: effects of magnesium adenosine triphosphate Changes of intracellular milieu with fatigue or hypoxia depress contraction of skinned rabbit skeletal and cardiac muscle Changes in force and cytosolic Ca2+ concentration after length changes in isolated rat ventricular trabeculae

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