Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO
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Hypernitrosylated ryanodine receptor calcium release channels are leaky in dystrophic muscleHuman spermatozoa contain multiple targets for protein S-nitrosylation: an alternative mechanism of the modulation of sperm function by nitric oxide?Balancing reactivity against selectivity: the evolution of protein S-nitrosylation as an effector of cell signaling by nitric oxidePotential molecular mechanisms underlying muscle fatigue mediated by reactive oxygen and nitrogen speciesMolecular mechanism of acrylamide neurotoxicity: lessons learned from organic chemistryA protein microarray-based analysis of S-nitrosylation.Characterization of potential S-nitrosylation sites in the myocardiumThe cysteine proteomeUpregulation of the CaV 1.1-ryanodine receptor complex in a rat model of critical illness myopathyS-nitrosylation inhibits pannexin 1 channel functionNO/redox disequilibrium in the failing heart and cardiovascular system.Identification of hyperreactive cysteines within ryanodine receptor type 1 by mass spectrometry.Nitric oxide mediates stretch-induced Ca2+ release via activation of phosphatidylinositol 3-kinase-Akt pathway in smooth muscleBacterial nitric oxide detoxification prevents host cell S-nitrosothiol formation: a novel mechanism of bacterial pathogenesis.Redox-sensitivity and site-specificity of S- and N- denitrosation in proteins.S-nitrosoglutathione reductase deficiency-induced S-nitrosylation results in neuromuscular dysfunction.Structural requirements for differential sensitivity of KCNQ K+ channels to modulation by Ca2+/calmodulin.Ryanodine receptors: structure, expression, molecular details, and function in calcium release.Focusing of nitric oxide mediated nitrosation and oxidative nitrosylation as a consequence of reaction with superoxide.Redox regulatory mechanism of transnitrosylation by thioredoxin.Methionine oxidation in the calmodulin-binding domain of calcineurin disrupts calmodulin binding and calcineurin activation.Oxygen-coupled redox regulation of the skeletal muscle ryanodine receptor-Ca2+ release channel by NADPH oxidase 4Angiotensin II modulates mouse skeletal muscle resting conductance to chloride and potassium ions and calcium homeostasis via the AT1 receptor and NADPH oxidaseSNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures.Ryanodine receptor regulation by intramolecular interaction between cytoplasmic and transmembrane domains.Concerted regulation of skeletal muscle contractility by oxygen tension and endogenous nitric oxideAltered Ca(2+) signaling in skeletal muscle fibers of the R6/2 mouse, a model of Huntington's diseaseStabilization of the skeletal muscle ryanodine receptor ion channel-FKBP12 complex by the 1,4-benzothiazepine derivative S107S-nitrosylation and permeation through connexin 43 hemichannels in astrocytes: induction by oxidant stress and reversal by reducing agents.The SNO-proteome: causation and classifications.Simultaneous measurement of protein oxidation and S-nitrosylation during preconditioning and ischemia/reperfusion injury with resin-assisted captureStructural analysis of cysteine S-nitrosylation: a modified acid-based motif and the emerging role of trans-nitrosylation.Modulation of sarcoplasmic reticulum Ca2+ release in skeletal muscle expressing ryanodine receptor impaired in regulation by calmodulin and S100A1.Mass spectrometric analysis and mutagenesis predict involvement of multiple cysteines in redox regulation of the skeletal muscle ryanodine receptor ion channel complex.Detailed map of oxidative post-translational modifications of human p21ras using Fourier transform mass spectrometry.Cysteine-mediated redox signaling: chemistry, biology, and tools for discoveryProtein S-nitrosylation in health and disease: a current perspective.Regulation of Ryanodine Receptor Ion Channels Through Posttranslational Modifications.Detection of protein S-nitrosylation with the biotin-switch technique.Mutation of a putative S-nitrosylation site of TRPV4 protein facilitates the channel activates
P2860
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P2860
Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO
description
2001 nî lūn-bûn
@nan
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO
@ast
Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO
@en
type
label
Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO
@ast
Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO
@en
prefLabel
Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO
@ast
Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO
@en
P2093
P2860
P356
P1476
Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO
@en
P2093
P2860
P304
11158-11162
P356
10.1073/PNAS.201289098
P407
P577
2001-09-18T00:00:00Z