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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2004-7-14
pubmed:abstractText
The activation of heterotrimeric G-proteins is tightly regulated by the exchange of GTP for GDP in the alpha-subunit; mostly--but not exclusively--seven-transmembrane receptors function as the guanine nucleotide exchange factors (GEFs). A research goal may be to determine which G-protein alpha-subunit is activated by the receptor under investigation. In a membrane preparation obtained from cells or tissues this can be achieved in a seemingly straightforward manner by determining if the receptor increases the covalent incorporation of GTP analogs into G-protein alpha-subunits. Because the GTP analogs may be labeled to high specific radioactivity the alpha-subunit can then be identified with the use of specific antibodies. One of the compounds we present here (2',3'-dialdehyde-GTP) can also be employed to block receptor-mediated G-protein activation and to disrupt the cognate signaling pathway.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1064-3745
pubmed:author
pubmed:issnType
Print
pubmed:volume
259
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
183-95
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Covalent modification of G-proteins by affinity labeling.
pubmed:affiliation
Institute of Pharmacology, Vienna University, Austria.
pubmed:publicationType
Journal Article