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)

Phosphorylase kinase phosphorylation of skeletal-muscle troponin T.

Rabbit skeletal-muscle troponin T was phosphorylated by a standard preparation of phosphorylase kinase [Cohen (1973) Eur. J. Biochem. 34, 1--14] and by fractions obtained after chromatography of phosphorylase kinase on phosphocellulose. The original preparation of phosphorylase kinase phosphorylated at least two sites, one of which was serine-1. The second and probably the third sites were presumably located in the peptide flanked by amino-acid residues 147 and 161 of troponin T. Fractions of phosphorylase kinase was adsorbed on phosphocellulose phosphorylated only the second site. Tightly adsorbed fractions possessed high troponin T kinase and phosvitin kinase activities and phosphorylated only serine-1 of troponin T. The results suggest that standard preparations of phosphorylase kinase are contaminated by troponin T kinase, which can phosphorylate serine-1 of troponin T.[1]


  1. Phosphorylase kinase phosphorylation of skeletal-muscle troponin T. Risnik, V.V., Dobrovolskii, A.B., Gusev, N.B., Severin, S.E. Biochem. J. (1980) [Pubmed]
WikiGenes - Universities