Role of basic residues in the phosphorylation of synthetic peptides by myosin light chain kinase.
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Identification of cardiac-specific myosin light chain kinaseDevelopment of an intracellularly acting inhibitory peptide selective for PKN.Molecular characterization of a mammalian smooth muscle myosin light chain kinase.220- and 130-kDa MLCKs have distinct tissue distributions and intracellular localization patternsIdentification of basic residues involved in activation and calmodulin binding of rabbit smooth muscle myosin light chain kinase.Regulatory and structural motifs of chicken gizzard myosin light chain kinase.Dictyostelium discoideum myosin: isolation and characterization of cDNAs encoding the regulatory light chain.Cloning and characterization of mammalian myosin regulatory light chain (RLC) cDNA: the RLC gene is expressed in smooth, sarcomeric, and nonmuscle tissues.Myosin light chain-activating phosphorylation sites are required for oogenesis in Drosophila.Vascular smooth muscle myosin light chain diphosphorylation: mechanism, function, and pathological implications.Trafficking of lysosomal enzymes in normal and disease states.Myosin light chain kinase steady-state kinetics: comparison of smooth muscle myosin II and nonmuscle myosin IIB as substrates.Pseudosubstrate sequence may not be critical for autoinhibition of smooth muscle myosin light chain kinase.Purification, characterization and substrate specificity of calmodulin-dependent myosin light-chain kinase from bovine brainInhibition of calmodulin-dependent myosin light-chain kinase by growth-hormone-releasing factor and vasoactive intestinal peptide.Minimum requirements for inhibition of smooth-muscle myosin light-chain kinase by synthetic peptides.The smooth muscle 132 kDa cyclic GMP-dependent protein kinase substrate is not myosin light chain kinase or caldesmon.Myosin light chain kinase- and PKC-dependent contraction of LES and esophageal smooth muscle.Primary structure required for the inhibition of smooth muscle myosin light chain kinase.Inhibitory properties of the regulatory domains of human protein kinase Calpha and mouse protein kinase Cepsilon.The mechanism of p21-activated kinase 2 autoactivation.
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Role of basic residues in the phosphorylation of synthetic peptides by myosin light chain kinase.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1983
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Role of basic residues in the ...... by myosin light chain kinase.
@en
Role of basic residues in the ...... by myosin light chain kinase.
@nl
type
label
Role of basic residues in the ...... by myosin light chain kinase.
@en
Role of basic residues in the ...... by myosin light chain kinase.
@nl
prefLabel
Role of basic residues in the ...... by myosin light chain kinase.
@en
Role of basic residues in the ...... by myosin light chain kinase.
@nl
P2860
P356
P1476
Role of basic residues in the ...... s by myosin light chain kinase
@en
P2093
P2860
P304
P356
10.1073/PNAS.80.24.7471
P407
P50
P577
1983-12-01T00:00:00Z