The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Chemical Compound Review

AG-K-50018     (2S)-2-amino-3- hydroxysulfanyl-propanoic acid

Synonyms: CHEBI:41710, Cys(OH), AC1L4WIO, AC1Q5QNT, CTK1H0247, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of Cys-sulfenic acid

 

High impact information on Cys-sulfenic acid

 

Associations of Cys-sulfenic acid with other chemical compounds

 

Gene context of Cys-sulfenic acid

 

Analytical, diagnostic and therapeutic context of Cys-sulfenic acid

References

  1. Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence for asymmetric behavior on interaction with pyridine nucleotides. Luba, J., Charrier, V., Claiborne, A. Biochemistry (1999) [Pubmed]
  2. Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme. Dierks, T., Dickmanns, A., Preusser-Kunze, A., Schmidt, B., Mariappan, M., von Figura, K., Ficner, R., Rudolph, M.G. Cell (2005) [Pubmed]
  3. Flavin-linked peroxide reductases: protein-sulfenic acids and the oxidative stress response. Claiborne, A., Ross, R.P., Parsonage, D. Trends Biochem. Sci. (1992) [Pubmed]
  4. Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution. Choi, H.J., Kang, S.W., Yang, C.H., Rhee, S.G., Ryu, S.E. Nat. Struct. Biol. (1998) [Pubmed]
  5. Flavoprotein disulfide reductases: advances in chemistry and function. Argyrou, A., Blanchard, J.S. Prog. Nucleic Acid Res. Mol. Biol. (2004) [Pubmed]
  6. Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation. Claiborne, A., Miller, H., Parsonage, D., Ross, R.P. FASEB J. (1993) [Pubmed]
  7. Oxidation of active center cysteine of bovine 1-Cys peroxiredoxin to the cysteine sulfenic acid form by peroxide and peroxynitrite. Peshenko, I.V., Shichi, H. Free Radic. Biol. Med. (2001) [Pubmed]
  8. Peroxide modification of monoalkylated glutathione reductase. Stabilization of an active-site cysteine-sulfenic acid. Miller, H., Claiborne, A. J. Biol. Chem. (1991) [Pubmed]
  9. Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin comigratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide peroxidase C (AhpC) family. Jeong, W., Cha, M.K., Kim, I.H. J. Biol. Chem. (2000) [Pubmed]
  10. Purification and analysis of streptococcal NADH peroxidase expressed in Escherichia coli. Parsonage, D., Miller, H., Ross, R.P., Claiborne, A. J. Biol. Chem. (1993) [Pubmed]
 
WikiGenes - Universities