Russell RL et al. (1977) "Mutants of acetylcholine metabolism in the nematode C. elegans."

Zwass MS, Scherer S, Rand JB, Russell RL, Johnson CD

[1977]

Radiochemical assays based on the selective extraction of either substrate or product from an aqueous reaction volume into an organic scintillator have been developed for acetylcholinesterase and choline acetyltransferase. These rapid, convenient assays have made it possible to screen large numbers of mutant lines for potential enzymatic defects. One mutant with a partial acetylcholinesterase defect and two more with choline acetyltransferase defective mutants have been identified. The acetylcholinesterase defective mutant lacks two of the four isozymic forms of acetylcholinesterase found in wild type C. elegans. Behaviorally, it is selectively defective in the propagation of contractile waves in the body region. Of the two mutants with choline acetyltransferase defects, one is remarkabley paralyzed and uncoordinated, while the other is behaviorally nearly normal.

Bodenmiller B et al. (2011) Methods Mol Biol "Phosphoproteome resource for systems biology research."

Aebersold R, Bodenmiller B

[Methods Mol Biol, 2011]

PhospoPep version 2.0 is a project to support systems biology signaling research by providing interactive interrogation of MS-derived phosphorylation data from four different organisms. Currently the database hosts phosphorylation data from the fly (Drosophila melanogaster), human (Homo sapiens), worm (Caenorhabditis elegans), and yeast (Saccharomyces cerevisiae). The following will give an overview of the content and usage of the PhosphoPep database.