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)

Covalent structure of bovine brain calreticulin.

The covalent structure of bovine brain calreticulin, a major Ca(2+)-binding protein in the lumen of the endoplasmic reticulum, was determined by analysis of the purified protein. The protein consisted of 400 amino acids, with an N-linked oligosaccharide attached to the polypeptide chain. The polypeptide sequence determined was compatible with the sequence of calreticulin deduced from cDNA of different sources, with a number of differences presumably due to species-specific amino acid substitutions. The protein retained the C-terminal tetrapeptide, KDEL, involved in retention of proteins resident in the endoplasmic reticulum, whereas the N-terminal signal peptide predicted from the cDNA sequence had been removed in the purified protein. The bovine brain protein contained a high-mannose type of oligosaccharide attached to Asn162, which is typical of resident endoplasmic reticulum proteins. The carbohydrate moiety was heterogeneous and had the composition GlcNAc2Man4-9, of which GlcNAc2Man5 was the most abundant in the bovine brain preparation. Glycosylation of calreticulin, however, appeared to be a species-specific modification, as Asn162 is replaced by Asp in the sequences already determined for a number of species. Analysis of the purified protein also identified an intramolecular disulphide bridge between Cys120 and Cys146.[1]


  1. Covalent structure of bovine brain calreticulin. Matsuoka, K., Seta, K., Yamakawa, Y., Okuyama, T., Shinoda, T., Isobe, T. Biochem. J. (1994) [Pubmed]
WikiGenes - Universities