Nitric oxide, NOC-12, and S-nitrosoglutathione modulate the skeletal muscle calcium release channel/ryanodine receptor by different mechanisms. An allosteric function for O2 in S-nitrosylation of the channel (Q44267719)

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English	Nitric oxide, NOC-12, and S-nitrosoglutathione modulate the skeletal muscle calcium release channel/ryanodine receptor by different mechanisms. An allosteric function for O2 in S-nitrosylation of the channel	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

Nitric oxide, NOC-12, and S-nitrosoglutathione modulate the skeletal muscle calcium release channel/ryanodine receptor by different mechanisms. An allosteric function for O2 in S-nitrosylation of the channel (English)

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

author name string

Junhui Sun

1

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

Le Xu

2

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

Jerry P Eu

3

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

Jonathan S Stamler

4

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

Gerhard Meissner

5

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

language of work or name

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publication date

30 December 2002

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Europe PubMed Central

PubMed publication ID

1 December 2017

number of pages

6

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inferred from page(s)

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

1 December 2017

278

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Europe PubMed Central

PubMed publication ID

1 December 2017

10

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Europe PubMed Central

PubMed publication ID

1 December 2017

8184-8189

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

Classes of thiols that influence the activity of the skeletal muscle calcium release channel

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

Transmembrane redox sensor of ryanodine receptor complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

Skeletal muscle ryanodine receptor is a redox sensor with a well defined redox potential that is sensitive to channel modulators.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

Identification of apocalmodulin and Ca2+-calmodulin regulatory domain in skeletal muscle Ca2+ release channel, ryanodine receptor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

The use of nitric oxide donors in pharmacological studies.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

Inhibition of the skeletal muscle ryanodine receptor calcium release channel by nitric oxide.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

Nitric oxide activates or inhibits skeletal muscle ryanodine receptors depending on its concentration, membrane potential and ligand binding.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

The biochemistry and physiology of S-nitrosothiols

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

Diazeniumdiolates: pro- and antioxidant applications of the "NONOates".

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

Determination of microgram quantities of protein in the presence of milligram levels of lipid with amido black 10B.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

New nitric oxide-releasing zwitterions derived from polyamines

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

The chemistry of the S-nitrosoglutathione/glutathione system

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

Ryanodine receptor/Ca2+ release channels and their regulation by endogenous effectors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

Calmodulin binding and inhibition of cardiac muscle calcium release channel (ryanodine receptor).

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

Critical sulfhydryls regulate calcium release from sarcoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

Further characterization of the type 3 ryanodine receptor (RyR3) purified from rabbit diaphragm

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

Functional role of hyperreactive sulfhydryl moieties within the ryanodine receptor complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

How many cysteine residues regulate ryanodine receptor channel activity?

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

S-nitrosylation: spectrum and specificity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

Nitrosylation. the prototypic redox-based signaling mechanism.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

OxyR: a molecular code for redox-related signaling

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211940200

21 January 2018

Identifiers

10.1074/JBC.M211940200

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

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