This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. 'A nicotinic acetylcholine receptor from Caenorhabditis elegans, which is present in muscles and neurons, has been purified to apparent homogeneity, including accessory proteins. These additional proteins do co-sediment with the receptor as an 11 S complex upon glycerol gradient centrifugation, confirming their tight association. To our knowledge, this is the first time that nicotinic receptors could be purified together with associated proteins. It is thus of major interest, not only for the C. elegans community, to identify these proteins, some of which may be involved in regulating the function and/or expression of nicotinic receptors. This should be straightforward, since the C. elegans genome sequence is known. The functional characterization of these potentially novel proteins will be highly aided by the possibilities to use RNA-mediated interference and reverse genetics in the C. elegans system.'
Showing the most recent 10 out of 583 publications