Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide.

Literature DB >> 7788289

Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide.

Abstract

The recent high-resolution solution structures of human and Escherichia coli thioredoxin in their oxidized and reduced states support a catalytic model of protein disulfide reduction involving binding of a target protein and nucleophilic attack by the active-site Cys32 thiolate to form a transition state mixed disulfide.

Entities: Chemical Gene Species

Mesh：

Substances：

Year: 1995 PMID： 7788289 DOI： 10.1016/s0969-2126(01)00153-8

Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006

Keyword Cloud
Cited

94 in total

1. Characterization of the redox activity and disulfide bond formation in apurinic/apyrimidinic endonuclease.

Authors: Meihua Luo; Jun Zhang; Hongzhen He; Dian Su; Qiujia Chen; Michael L Gross; Mark R Kelley; Millie M Georgiadis
Journal: Biochemistry Date: 2012-01-04 Impact factor: 3.162

2. An integrated structural and computational study of the thermostability of two thioredoxin mutants from Alicyclobacillus acidocaldarius.

Authors: Simonetta Bartolucci; Giuseppina De Simone; Stefania Galdiero; Roberto Improta; Valeria Menchise; Carlo Pedone; Emilia Pedone; Michele Saviano
Journal: J Bacteriol Date: 2003-07 Impact factor: 3.490

3. Functional modulation of estrogen receptor by redox state with reference to thioredoxin as a mediator.

Authors: S Hayashi; K Hajiro-Nakanishi; Y Makino; H Eguchi; J Yodoi; H Tanaka
Journal: Nucleic Acids Res Date: 1997-10-15 Impact factor: 16.971

4. Enzymatic reduction of disulfide bonds in lysosomes: characterization of a gamma-interferon-inducible lysosomal thiol reductase (GILT).

Authors: B Arunachalam; U T Phan; H J Geuze; P Cresswell
Journal: Proc Natl Acad Sci U S A Date: 2000-01-18 Impact factor: 11.205

Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide.

1. Characterization of the redox activity and disulfide bond formation in apurinic/apyrimidinic endonuclease.

2. An integrated structural and computational study of the thermostability of two thioredoxin mutants from Alicyclobacillus acidocaldarius.

3. Functional modulation of estrogen receptor by redox state with reference to thioredoxin as a mediator.

4. Enzymatic reduction of disulfide bonds in lysosomes: characterization of a gamma-interferon-inducible lysosomal thiol reductase (GILT).

5. Gold-containing indoles as anticancer agents that potentiate the cytotoxic effects of ionizing radiation.

6. The origami of thioredoxin-like folds.

7. Probing the chemistry of thioredoxin catalysis with force.

8. A novel mouse model for the identification of thioredoxin-1 protein interactions.

9. Thioredoxin and thioredoxin reductase control tissue factor activity by thiol redox-dependent mechanism.

10. Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily.