RedoxDB-a curated database for experimentally verified protein oxidative modification

Bioinformatics

Volumn 28, Issue 19, 2012, Pages 2551-2552

  Sun, Ming An ^a   Wang, Yejun ^a   Cheng, Han ^a   Zhang, Qing ^a   Ge, Wei ^a   Guo, Dianjing ^a  

^a CHINESE UNIVERSITY OF HONG KONG   (Hong Kong)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; PROTEIN; THIOL DERIVATIVE;

ARTICLE; BIOLOGY; CHEMISTRY; COMPUTER INTERFACE; OXIDATION REDUCTION REACTION; PROTEIN DATABASE; PROTEIN PROCESSING;

COMPUTATIONAL BIOLOGY; CYSTEINE; DATABASES, PROTEIN; OXIDATION-REDUCTION; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEINS; SULFHYDRYL COMPOUNDS; USER-COMPUTER INTERFACE;

EID: 84867313408     PISSN: 13674803     EISSN: 14602059     Source Type: Journal    
DOI: 10.1093/bioinformatics/bts468     Document Type: Article

References (16)

1. Altschul, S.F. et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res., 25, 3389-3402.
2. Antelmann, H. and Helmann, J.D. (2011) Thiol-based redox switches and gene regulation. Antioxid. Redox Signal., 14, 1049-1063.
3. Chiarugi, P. and Buricchi, F. (2007) Protein tyrosine phosphorylation and reversible oxidation: two cross-talking posttranslation modifications. Antioxid. Redox Signal., 9, 1-24.
4. Chouchani, E.T. et al. (2011) Proteomic approaches to the characterization of protein thiol modification. Curr. Opin. Chem. Biol., 15, 120-128.
5. Fomenko, D.E. et al. (2007) High-throughput identification of catalytic redox-active cysteine residues. Science (New York, NY), 315, 387-389.
6. Forman, H.J. et al. (2010) Signaling functions of reactive oxygen species. Biochemistry, 49, 835-842.
7. Imlay, J.A. (2003) Pathways of oxidative damage. Annu.Rev.Microbiol., 57, 395-418.
8. Lindahl, M. et al. (2011) The disulfide proteome and other reactive cysteine proteomes: analysis andfunctional significance. Antioxid. Redox Signal., 14, 2581-2642.
9. Marino, S.M. and Gladyshev, V.N. (2009) A structure-based approach for detection of thiol oxidoreductases and their catalytic redox-active cysteine residues. PLoS Comput. Biol., 5, e1000383.
10. Meyer, Y. et al. (2009) Thioredoxins and glutaredoxins: unifying elements in redox biology. Annu. Rev. Genet., 43, 335-367.
11. Reddie, K.G. and Carroll, K.S. (2008) Expanding the functional diversity of proteins through cysteine oxidation. Curr. Opin. Chem. Biol., 12, 746-754.
12. Sanchez, R. et al. (2008) Prediction of reversibly oxidized protein cysteine thiols using protein structure properties. Protein Sci., 17, 473-481.
13. Sarsour, E.H. et al. (2009) Redox control of the cell cycle in health and disease. Antioxid. Redox Signal., 11, 2985-3011.
14. Weerapana, E. et al. (2010) Quantitative reactivity profiling predicts functional cysteines in proteomes. Nature, 468, 790-795.
15. Westbrook, J. et al. (2002) The Protein Data Bank: unifying the archive. Nucleic Acids Res., 30, 245-248.
16. Wu, C.H. et al. (2006) The Universal Protein Resource (UniProt): an expanding universe of protein information. Nucleic Acids Res., 34, D187-D191.