Structural basis for the in situ Ca(2+) sensitization of cardiac troponin C by positive feedback from force-generating myosin cross-bridges - Wikidata - awgldk - TriplyDB

Structural basis for the in situ Ca(2+) sensitization of cardiac troponin C by positive feedback from force-generating myosin cross-bridges

Structural basis for the in situ Ca(2+) sensitization of cardiac troponin C by positive feedback from force-generating myosin cross-bridges

http://www.wikidata.org/entity/Q28295508

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Regulatory domain of troponin moves dynamically during activation of cardiac muscle Targeting the sarcomere to correct muscle function Mechano-chemical Interactions in Cardiac Sarcomere Contraction: A Computational Modeling Study FRET study of the structural and kinetic effects of PKC phosphomimetic cardiac troponin T mutants on thin filament regulation.In situ time-resolved FRET reveals effects of sarcomere length on cardiac thin-filament activation.Mechanistic heterogeneity in contractile properties of α-tropomyosin (TPM1) mutants associated with inherited cardiomyopathies.A Spatially Detailed Model of Isometric Contraction Based on Competitive Binding of Troponin I Explains Cooperative Interactions between Tropomyosin and Crossbridges.Molecular effects of the myosin activator omecamtiv mecarbil on contractile properties of skinned myocardium lacking cardiac myosin binding protein-C Sarcomere length dependent effects on the interaction between cTnC and cTnI in skinned papillary muscle strips.The myosin-activated thin filament regulatory state, M⁻-open: a link to hypertrophic cardiomyopathy (HCM).The structural and functional effects of the familial hypertrophic cardiomyopathy-linked cardiac troponin C mutation, L29Q Cross-talk, cross-bridges, and calcium activation of cardiac contraction.Functional significance of C-terminal mobile domain of cardiac troponin I.Role of the C-terminus mobile domain of cardiac troponin I in the regulation of thin filament activation in skinned papillary muscle strips.

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P2860

Structural basis for the in situ Ca(2+) sensitization of cardiac troponin C by positive feedback from force-generating myosin cross-bridges

http://www.wikidata.org/entity/Q28295508

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2013 nî lūn-bûn

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2013 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2013年論文

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Structural basis for the in si ...... enerating myosin cross-bridges

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Structural basis for the in si ...... enerating myosin cross-bridges

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J.ABB.2013.07.013

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Archives of Biochemistry and Biophysics

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Structural basis for the in si ...... enerating myosin cross-bridges

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Daniel C Rieck

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King-Lun Li

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R John Solaro

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Wen-Ji Dong

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Yexin Ouyang

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P2860

Binding of cardiac troponin-I147-163 induces a structural opening in human cardiac troponin-C

Calcium-induced structural transition in the regulatory domain of human cardiac troponin C

Calcium, thin filaments, and the integrative biology of cardiac contractility

Structural based insights into the role of troponin in cardiac muscle pathophysiology

Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament

The C terminus of cardiac troponin I stabilizes the Ca2+-activated state of tropomyosin on actin filaments

Effects of calcium binding and the hypertrophic cardiomyopathy A8V mutation on the dynamic equilibrium between closed and open conformations of the regulatory N-domain of isolated cardiac troponin C

Effects of thin and thick filament proteins on calcium binding and exchange with cardiac troponin C

Regulation of contraction in striated muscle

Myosin binding-induced cooperative activation of the thin filament in cardiac myocytes and skeletal muscle fibers

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198-209

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10.1016/J.ABB.2013.07.013

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