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Christian Andresen

Researcher at University of Düsseldorf

Publications -  9
Citations -  1046

Christian Andresen is an academic researcher from University of Düsseldorf. The author has contributed to research in topics: Titin & Obscurin. The author has an hindex of 8, co-authored 8 publications receiving 919 citations. Previous affiliations of Christian Andresen include University of Münster & Ruhr University Bochum.

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Protein Kinase G Modulates Human Myocardial Passive Stiffness by Phosphorylation of the Titin Springs

TL;DR: Reducing titin stiffness by PKG-dependent phosphorylation of the N2-Bus can benefit diastolic function, and phosphorylated titin sites could affect protein–protein interactions.
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Isoform Diversity of Giant Proteins in Relation to Passive and Active Contractile Properties of Rabbit Skeletal Muscles

TL;DR: A low correlation exists between the active and passive mechanical properties of skeletal muscle fibers and titin, which contributes substantially to total passive stiffness, but this contribution varies greatly among muscles.
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Smyd2 controls cytoplasmic lysine methylation of Hsp90 and myofilament organization

TL;DR: A cytoplasmic protein network that employs lysine methylation for the maintenance and function of skeletal muscle is revealed and deficiency in Smyd2 results in the loss of Hsp90 methylation, impaired titin stability, and altered muscle function.
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Lysine methyltransferase Smyd2 regulates Hsp90-mediated protection of the sarcomeric titin springs and cardiac function

TL;DR: It is concluded that Smyd2 and presumably several other Smyd family members are lysine methyltransferases which have, next to their nuclear activity, specific regulatory functions in the cytoplasm of heart and skeletal muscle cells.
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Diabetes-Induced Cardiomyocyte Passive Stiffening Is Caused by Impaired Insulin-Dependent Titin Modification and Can Be Modulated by Neuregulin-1

TL;DR: Chronic NRG-1 application is a promising approach to modulate titin properties in heart failure with preserved ejection fraction associated with type-2 diabetes mellitus by restoring normal kinase activities of PKG, ERK1/2, and PKC&agr;, and by reducing cardiomyocyte passive tension.