Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO - Test2 - elhamkhani - TriplyDB

Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO

Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO

http://www.wikidata.org/entity/Q33944345

about

Hypernitrosylated ryanodine receptor calcium release channels are leaky in dystrophic muscle Human 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 oxide Potential molecular mechanisms underlying muscle fatigue mediated by reactive oxygen and nitrogen species Molecular mechanism of acrylamide neurotoxicity: lessons learned from organic chemistry A protein microarray-based analysis of S-nitrosylation.Characterization of potential S-nitrosylation sites in the myocardium The cysteine proteome Upregulation of the CaV 1.1-ryanodine receptor complex in a rat model of critical illness myopathy S-nitrosylation inhibits pannexin 1 channel function NO/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 muscle Bacterial 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 4 Angiotensin II modulates mouse skeletal muscle resting conductance to chloride and potassium ions and calcium homeostasis via the AT1 receptor and NADPH oxidase SNOSID, 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 oxide Altered Ca(2+) signaling in skeletal muscle fibers of the R6/2 mouse, a model of Huntington's disease Stabilization of the skeletal muscle ryanodine receptor ion channel-FKBP12 complex by the 1,4-benzothiazepine derivative S107 S-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 capture Structural 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 discovery Protein 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

Q24308714-555BA9F1-F9FD-4FA1-98DC-804661C2BB8F Q24656420-28CE8030-780F-499B-A5F4-25EF9AFFA47D Q24680520-C383BC70-2C1A-4D5C-AAD0-FD0236D487D3 Q26782966-90C33AA3-15C9-49F3-B022-5F978A1D9843 Q26999354-C1EDAC79-C1CF-4155-A0AF-3576585D3C56 Q27936604-8F2D2120-2D4C-4D58-8163-D369885F51F2 Q28304250-FDC64850-2DEE-45A1-A3CE-DCFD6B38F4D1 Q28395817-99051FFE-3224-4DD8-A27E-3EE5F1F156C6 Q28573445-EE29F5C1-FC70-418C-97E8-4D58EABC4303 Q30416310-D3852417-E022-407B-A5DC-FF33BBCF501F Q30475784-80D3B4F0-0739-4F5E-9CF7-30E4A3E12AC1 Q31079409-F30894B1-6F6D-4EFA-A8D3-2093DF724DF4 Q33346240-4712E139-E801-4A03-99B7-0226D11B2E62 Q33646894-576ACE32-6EB5-475D-98AF-2E8DE47CE2B1 Q33784924-837826D7-5094-4CAC-9673-A8AEC60523AC Q33862264-C7D9E4FC-EF79-4C2F-8D6D-6DA294EEA06A Q33911083-1A852909-90B5-4E76-9CC1-2EC0F737E725 Q34024377-9590E57F-6641-4610-95B1-81B60D94DE57 Q34037128-984DF02F-EE5C-422B-A85B-CE4E00705FA0 Q34193659-902B45F5-7322-427E-8B4B-EBC856197D5F Q34206348-545DDEF2-FA10-4DDD-B4D5-AA6467BD5241 Q34213979-9275FAE2-AE9A-412B-878A-433470036846 Q34295366-E21FD31A-08D1-4161-BA84-AF25CE8CECBE Q34304784-26E51E0F-C930-46DD-A6D8-408A446BDC99 Q34359135-EDF406F1-6D8C-41F8-9C64-D5DDEB74CDEF Q34393813-2B60BAE8-86F1-4012-9FDB-960E4D2C7B52 Q34409630-113AFAAD-F7DC-4182-B190-6DBBB20D2DF2 Q34562748-EDDC11B8-B6F8-4D82-8DC7-BCEA64919E4B Q34574752-DFC4D478-D1ED-42A7-9FCE-DDD5FDBC44B4 Q34579428-4F4E4A4D-2F7A-41CC-AA44-7FAA9746B8D0 Q34590481-DB8CBDAF-9EC4-431C-A499-02C8789051D3 Q34703655-AA2E577E-F83A-467A-8038-FFD3DE92BFDD Q34979253-C9B0628A-CCD2-43E1-9F59-4AF3D3DE5349 Q34985557-48EC619A-EFEC-4752-9A05-464C13BC736B Q34993637-CCB7F868-C91A-4A9B-B9E7-93630B7ECFC0 Q35001796-0EDE63A7-1AFF-48FD-9DA2-42F0FE870FC1 Q35020178-25DF2320-47CA-4667-B6E7-E0AE7DFFDB38 Q35033112-A927E41C-E804-4349-B7F0-76DD812C5608 Q35060310-F0FBBCFE-EA47-46A5-AE8E-43FB11549BA0 Q35149107-7D86C2C6-8890-44CA-98A5-0E0EA973C527

P2860

Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO

http://www.wikidata.org/entity/Q33944345

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

P1433

Q33944345-70157C85-5AB0-4F62-B4AF-C0AC3A233146

P1476

Q33944345-457B8C3E-5954-474C-BBE8-207B2C740DB5

P2093

Q33944345-105F9D57-BFD9-4764-AC09-A6AAAB9ACBBC

Q33944345-4EA5AF74-9030-426F-84F2-6142B0C7C591

Q33944345-847D5825-5509-40D8-8371-5D9AC5727E70

Q33944345-B1D0C910-7D6E-477E-85B0-BC21EAB9AEC9

Q33944345-E99E37A9-755F-4500-95E2-F97AFDFC869D

P2860

Q33944345-0249717F-7263-462A-A84F-F605BDED26D0

Q33944345-04871B7A-21F9-45CF-B4E9-144943627389

Q33944345-0F40D090-2894-49B5-A4A1-2D8F15611968

Q33944345-185B7E0D-9CCD-4699-987A-D11C9D384D19

Q33944345-1E2B2282-A1F3-4CA9-BA42-07FDFAEC7D7B

Q33944345-31C8DD17-0476-4194-8EE9-96AE69AAA732

Q33944345-3C381142-FF27-416D-BF23-9704786FF9AD

Q33944345-438D8D9B-DF02-4509-B683-C89059A5F5AC

Q33944345-445146A7-59B8-4402-82B0-1E97D661DACF

Q33944345-46506AE4-6272-44C1-9A4C-2293A9D96FFF

P304

Q33944345-F57C3F86-A980-43CC-A678-FD884BFAF765

P31

Q33944345-564CD7C1-F2D6-4031-A9F4-0304AE7AA90D

P356

Q33944345-3C654484-FA5E-4D52-A295-E4769BF4F859

P407

Q33944345-61A28F26-6323-471E-8EB2-D64E2BAC8A04

P433

Q33944345-F56C94A3-2A1C-41CC-A6BC-64D684A4D7C8

P478

Q33944345-2FAF3FC0-47FC-47EE-9A94-D15362EB979C

P577

Q33944345-8D5AA9ED-143F-44BA-AB6D-673104D1F01B

P5875

Q33944345-27C1E6D2-F564-463A-AB34-ACE26B1E61A0

P698

Q33944345-F7AFA8E9-969A-4FA7-9F3B-2065E8EF5F34

P932

Q33944345-AC07E03D-16EE-497E-875B-A9BFEB80B167

P356

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO

@en

P2093

C Xin

http://www.w3.org/2001/XMLSchema#string

G Meissner

http://www.w3.org/2001/XMLSchema#string

J P Eu

http://www.w3.org/2001/XMLSchema#string

J S Stamler

http://www.w3.org/2001/XMLSchema#string

J Sun

http://www.w3.org/2001/XMLSchema#string

P2860

S-nitrosylation of proteins.

Calmodulin activation and inhibition of skeletal muscle Ca2+ release channel (ryanodine receptor)

Physiology of nitric oxide in skeletal muscle.

Regulation of ryanodine receptors by reactive nitrogen species.

Molecular interaction between nitric oxide and ryanodine receptors of skeletal and cardiac sarcoplasmic reticulum.

Evidence for a role of the lumenal M3-M4 loop in skeletal muscle Ca(2+) release channel (ryanodine receptor) activity and conductance.

Ryanodine receptors of striated muscles: a complex channel capable of multiple interactions.

Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor.

An autocatalytic mechanism of protein nitrosylation

Accelerated reaction of nitric oxide with O2 within the hydrophobic interior of biological membranes.

P304

11158-11162

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.201289098

http://www.w3.org/2001/XMLSchema#string

P407

P433

20

http://www.w3.org/2001/XMLSchema#string

P478

98

http://www.w3.org/2001/XMLSchema#string

P577

2001-09-18T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

11786482

http://www.w3.org/2001/XMLSchema#string

P698

11562475

http://www.w3.org/2001/XMLSchema#string

P932

58700

http://www.w3.org/2001/XMLSchema#string