Myofilament Calcium Sensitivity: Mechanistic Insight into TnI Ser-23/24 and Ser-150 Phosphorylation Integration. - Wikidata - wikimedia - TriplyDB

Myofilament Calcium Sensitivity: Mechanistic Insight into TnI Ser-23/24 and Ser-150 Phosphorylation Integration.

Myofilament Calcium Sensitivity: Mechanistic Insight into TnI Ser-23/24 and Ser-150 Phosphorylation Integration.

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Myofilament Calcium Sensitivity: Role in Regulation of In vivo Cardiac Contraction and Relaxation Myofilament Calcium Sensitivity: Consequences of the Effective Concentration of Troponin I.

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Myofilament Calcium Sensitivity: Mechanistic Insight into TnI Ser-23/24 and Ser-150 Phosphorylation Integration.

http://www.wikidata.org/entity/Q37503779

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 15 December 2016

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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Myofilament Calcium Sensitivit ...... 0 Phosphorylation Integration.

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Myofilament Calcium Sensitivit ...... 0 Phosphorylation Integration.

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Myofilament Calcium Sensitivit ...... 0 Phosphorylation Integration.

@en

Myofilament Calcium Sensitivit ...... 0 Phosphorylation Integration.

@nl

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Myofilament Calcium Sensitivit ...... 0 Phosphorylation Integration.

@en

Myofilament Calcium Sensitivit ...... 0 Phosphorylation Integration.

@nl

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FPHYS.2016.00567

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Frontiers in Physiology

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Myofilament Calcium Sensitivit ...... 0 Phosphorylation Integration.

@en

P2093

Brandon J Biesiadecki

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Elizabeth A Brundage

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Hussam E Salhi

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Jalal K Siddiqui

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Jonathan P Davis

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Mark T Ziolo

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Nathan C Hassel

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Paul M L Janssen

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P2860

Rationally engineered Troponin C modulates in vivo cardiac function and performance in health and disease

Phosphorylation-dependent conformational transition of the cardiac specific N-extension of troponin I in cardiac troponin

Myofilament Calcium Sensitivity: Role in Regulation of In vivo Cardiac Contraction and Relaxation

Identification of a functionally critical protein kinase C phosphorylation residue of cardiac troponin T

A proteolytic NH2-terminal truncation of cardiac troponin I that is up-regulated in simulated microgravity

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

The cardiac-specific N-terminal region of troponin I positions the regulatory domain of troponin C

Proteolytic N-terminal truncation of cardiac troponin I enhances ventricular diastolic function

A non-equilibrium isoelectric focusing method to determine states of phosphorylation of cardiac troponin I: identification of Ser-23 and Ser-24 as significant sites of phosphorylation by protein kinase C

Multiple Reaction Monitoring to Identify Site-Specific Troponin I Phosphorylated Residues in the Failing Human Heart

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scholarly article

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10.3389/FPHYS.2016.00567

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7

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2016-12-15T00:00:00Z

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phosphorylation

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5156683

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