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Anthony Persechini
Researcher at University of Missouri–Kansas City
Publications - 55
Citations - 3729
Anthony Persechini is an academic researcher from University of Missouri–Kansas City. The author has contributed to research in topics: Calmodulin & Myosin light-chain kinase. The author has an hindex of 31, co-authored 55 publications receiving 3631 citations. Previous affiliations of Anthony Persechini include University of Rochester & University of Texas Southwestern Medical Center.
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Detection in Living Cells of Ca2+-dependent Changes in the Fluorescence Emission of an Indicator Composed of Two Green Fluorescent Protein Variants Linked by a Calmodulin-binding Sequence A NEW CLASS OF FLUORESCENT INDICATORS
TL;DR: This observation suggests that the activity of a calmodulin target with a typical 1 nmaffinity for (Ca2+)4-calmodulin is responsive to changes in the intracellular Ca2+ concentration over the physiological range.
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The EF-hand family of calcium-modulated proteins.
TL;DR: The EF-hand homolog proteins bind calcium (Ca2+) with dissociation constants in the micromolar range and are modulated by stimulus-induced increases in cytosolic free Ca2+.
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The effect of myosin phosphorylation on the contractile properties of skinned rabbit skeletal muscle fibers.
TL;DR: The results suggest that in vertebrate skeletal muscle, P-light chain phosphorylation increases the force level at submaximal Ca2+ concentrations, probably by affecting the interaction between the myosin cross-bridge and the thin filament.
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The central helix of calmodulin functions as a flexible tether.
TL;DR: Using site-directed mutagenesis, an altered calmodulin is created in which Gln-3 and Thr-146 have both been replaced by cysteines, indicating that one role for the central helix may be to serve as a flexible tether between the cal modulin lobes.
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Different phosphorylated forms of myosin in contracting tracheal smooth muscle
TL;DR: The relationship between the extent of P-light chain phosphorylation (measured directly or calculated) and the relative amount of MP2 is consistent with a randomosphorylation process.