Titin-actin interaction: PEVK-actin-based viscosity in a large animal
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Small and large animal models in cardiac contraction research: advantages and disadvantagesSingle molecule force spectroscopy on titin implicates immunoglobulin domain stability as a cardiac disease mechanism.A novel three-filament model of force generation in eccentric contraction of skeletal muscles.Conformational dynamics of titin PEVK explored with FRET spectroscopy.The multifunctional Ca(2+)/calmodulin-dependent protein kinase II delta (CaMKIIδ) phosphorylates cardiac titin's spring elements.Temperature and transmural region influence functional measurements in unloaded left ventricular cardiomyocytes.Increased myocardial short-range forces in a rodent model of diabetes reflect elevated content of β myosin heavy chain.Cell- and molecular-level mechanisms contributing to diastolic dysfunction in HFpEFResidual Force Enhancement Following Eccentric Contractions: A New Mechanism Involving Titin.The multiple roles of titin in muscle contraction and force production.
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Titin-actin interaction: PEVK-actin-based viscosity in a large animal
description
2011 nî lūn-bûn
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2011年の論文
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2011年論文
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2011年論文
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2011年論文
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2011年論文
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2011年論文
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2011年论文
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2011年论文
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2011年论文
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name
Titin-actin interaction: PEVK-actin-based viscosity in a large animal
@ast
Titin-actin interaction: PEVK-actin-based viscosity in a large animal
@en
type
label
Titin-actin interaction: PEVK-actin-based viscosity in a large animal
@ast
Titin-actin interaction: PEVK-actin-based viscosity in a large animal
@en
prefLabel
Titin-actin interaction: PEVK-actin-based viscosity in a large animal
@ast
Titin-actin interaction: PEVK-actin-based viscosity in a large animal
@en
P2093
P2860
P356
P1476
Titin-actin interaction: PEVK-actin-based viscosity in a large animal
@en
P2093
Alexander Gasch
Carlos G Hidalgo
Henk L Granzier
Siegfried Labeit
P2860
P304
P356
10.1155/2011/310791
P577
2011-11-15T00:00:00Z