Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2004-2-27
pubmed:abstractText
The cGMP signalling pathway has been suggested to be involved in the signal transduction of various physiological functions in insects; olfaction, antidiuresis and eclosion. However, the cGMP signalling mechanism has remained elusive. We isolated two cDNAs of the cGMP dependent protein kinase, designated BmPKG-Ialpha and BmPKG-Ibeta. The deduced amino acid sequences indicate that both BmPKG-Ialpha and BmPKG-Ibeta appear to consist of an amino terminal region, a cGMP binding domain and a protein kinase domain. Transcripts of BmPKG-Ialpha and BmPKG-Ibeta were detected in various tissues: flight muscles, antennae, midgut, legs, head, thoracic ganglia and Malphighian tubules. Recombinant BmPKG-Ialpha bound to lipid membranes, while BmPKG-Ialpha with a deleted amino terminal region failed to bind to lipid membranes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0962-1075
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
621-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Molecular characterization of a membrane-bound cGMP dependent protein kinase from the silk moth Bombyx mori.
pubmed:affiliation
Department of Agricultural Life Sciences, Graduate School of Agricultural Sciences, University of Kyoto, Japan.
pubmed:publicationType
Journal Article, Comparative Study