Interactions between the leucine-zipper motif of cGMP-dependent protein kinase and the C-terminal region of the targeting subunit of myosin light chain phosphatase
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Mechanisms of Vascular Smooth Muscle Contraction and the Basis for Pharmacologic Treatment of Smooth Muscle DisordersCrystal Structure of the cGMP-dependent Protein Kinase II Leucine Zipper and Rab11b Protein Complex Reveals Molecular Details of G-kinase-specific InteractionsPar-4: a new activator of myosin phosphataseIncreased degradation of MYPT1 contributes to the development of tolerance to nitric oxide in porcine pulmonary artery.A bioinformatic and computational study of myosin phosphatase subunit diversity.cGMP-dependent protein kinases and cGMP phosphodiesterases in nitric oxide and cGMP action.Prevention of PKG1α oxidation augments cardioprotection in the stressed heart.Structures of cGMP-Dependent Protein Kinase (PKG) Iα Leucine Zippers Reveal an Interchain Disulfide Bond Important for Dimer Stability.Smooth muscle signalling pathways in health and disease.Inhibition of MLC20 phosphorylation downstream of Ca2+ and RhoA: A novel mechanism involving phosphorylation of myosin phosphatase interacting protein (M-RIP) by PKG and stimulation of MLC phosphatase activity.Disulfide-activated protein kinase G Iα regulates cardiac diastolic relaxation and fine-tunes the Frank-Starling response.MYPT1 protein isoforms are differentially phosphorylated by protein kinase G.Interaction of Myosin Phosphatase Target Subunit (MYPT1) with Myosin Phosphatase-RhoA Interacting Protein (MRIP): A Role of Glutamic Acids in the InteractionHypoxia modulates the expression of leucine zipper-positive MYPT1 and its interaction with protein kinase G and Rho kinases in pulmonary arterial smooth muscle cells.Degradation of leucine zipper-positive isoform of MYPT1 may contribute to development of nitrate tolerance.Probing the interaction between the coiled coil leucine zipper of cGMP-dependent protein kinase Ialpha and the C terminus of the myosin binding subunit of the myosin light chain phosphatase.NMR insight into myosin-binding subunit coiled-coil structure reveals binding interface with protein kinase G-Iα leucine zipper in vascular function.An N-terminally truncated form of cyclic GMP-dependent protein kinase Iα (PKG Iα) is monomeric, autoinhibited, and provides a model for activation.
P2860
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P2860
Interactions between the leucine-zipper motif of cGMP-dependent protein kinase and the C-terminal region of the targeting subunit of myosin light chain phosphatase
description
2007 nî lūn-bûn
@nan
2007 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Interactions between the leuci ...... myosin light chain phosphatase
@ast
Interactions between the leuci ...... myosin light chain phosphatase
@en
type
label
Interactions between the leuci ...... myosin light chain phosphatase
@ast
Interactions between the leuci ...... myosin light chain phosphatase
@en
prefLabel
Interactions between the leuci ...... myosin light chain phosphatase
@ast
Interactions between the leuci ...... myosin light chain phosphatase
@en
P2093
P2860
P1476
Interactions between the leuci ...... myosin light chain phosphatase
@en
P2093
David B Hayes
Eunhee Lee
Knut Langsetmo
Terence C Tao
P2860
P304
P356
10.1016/J.JMB.2007.08.049
P407
P577
2007-08-25T00:00:00Z