Matches in SemOpenAlex for { <https://semopenalex.org/work/W2022169084> ?p ?o ?g. }
Showing items 1 to 72 of
72
with 100 items per page.
- W2022169084 endingPage "7070" @default.
- W2022169084 startingPage "7064" @default.
- W2022169084 abstract "Trans-phosphorylation of rhodopsin refers to a reaction in which a rhodopsin kinase molecule that has been activated by a light-activated rhodopsin molecule collides with and phosphorylates a second molecule of rhodopsin that has not been activated by light. It has been invoked as a mechanism for high-gain phosphorylation, a phenomenon that is observed at low bleaching levels where up to several hundred moles of phosphate are added to the rhodopsin pool per mole of photolyzed rhodopsin. Trans-phosphorylation is an appealing mechanism to propose for high-gain phosphorylation, but it has not been tested directly because of the difficulty inherent in unambiguous identification of light-activated and dark forms of rhodopsin present in the same reaction mixture. We report here a direct assay for trans-phosphorylation of rhodopsin. The assay is based on the use of a split receptor mutant of rhodopsin, SR(1−4/5−7), in which the fully functional protein is assembled from two separately expressed fragments. Because of different electrophoretic mobilities, SR(1−4/5−7) and wild-type rhodopsin can be monitored independently for phosphorylation while in the same reaction mixture. Thus, if wild-type rhodopsin is exposed to light and then incubated in the dark with SR(1−4/5−7), ATP, and rhodopsin kinase, phosphorylation of SR(1−4/5−7) would be a clear demonstration that trans-phosphorylation has occurred. Despite numerous attempts using several different experimental configurations, we have been unable to detect trans-phosphorylation of dark rhodopsin with this system." @default.
- W2022169084 created "2016-06-24" @default.
- W2022169084 creator A5027551170 @default.
- W2022169084 creator A5041777143 @default.
- W2022169084 creator A5051180337 @default.
- W2022169084 creator A5027825766 @default.
- W2022169084 date "1997-06-01" @default.
- W2022169084 modified "2023-09-25" @default.
- W2022169084 title "In Vitro Assay for Trans-Phosphorylation of Rhodopsin by Rhodopsin Kinase" @default.
- W2022169084 cites W1245933497 @default.
- W2022169084 cites W1587185311 @default.
- W2022169084 cites W1890185838 @default.
- W2022169084 cites W1971273204 @default.
- W2022169084 cites W2072550433 @default.
- W2022169084 cites W2082803210 @default.
- W2022169084 cites W2104782686 @default.
- W2022169084 cites W2116313448 @default.
- W2022169084 cites W2149464986 @default.
- W2022169084 cites W2203881861 @default.
- W2022169084 cites W4241922471 @default.
- W2022169084 cites W4248947927 @default.
- W2022169084 cites W945913723 @default.
- W2022169084 cites W586225993 @default.
- W2022169084 doi "https://doi.org/10.1021/bi970470e" @default.
- W2022169084 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9188705" @default.
- W2022169084 hasPublicationYear "1997" @default.
- W2022169084 type Work @default.
- W2022169084 sameAs 2022169084 @default.
- W2022169084 citedByCount "12" @default.
- W2022169084 crossrefType "journal-article" @default.
- W2022169084 hasAuthorship W2022169084A5027551170 @default.
- W2022169084 hasAuthorship W2022169084A5027825766 @default.
- W2022169084 hasAuthorship W2022169084A5041777143 @default.
- W2022169084 hasAuthorship W2022169084A5051180337 @default.
- W2022169084 hasConcept C11960822 @default.
- W2022169084 hasConcept C12554922 @default.
- W2022169084 hasConcept C184235292 @default.
- W2022169084 hasConcept C185592680 @default.
- W2022169084 hasConcept C202033177 @default.
- W2022169084 hasConcept C2780827179 @default.
- W2022169084 hasConcept C55493867 @default.
- W2022169084 hasConcept C86803240 @default.
- W2022169084 hasConceptScore W2022169084C11960822 @default.
- W2022169084 hasConceptScore W2022169084C12554922 @default.
- W2022169084 hasConceptScore W2022169084C184235292 @default.
- W2022169084 hasConceptScore W2022169084C185592680 @default.
- W2022169084 hasConceptScore W2022169084C202033177 @default.
- W2022169084 hasConceptScore W2022169084C2780827179 @default.
- W2022169084 hasConceptScore W2022169084C55493867 @default.
- W2022169084 hasConceptScore W2022169084C86803240 @default.
- W2022169084 hasIssue "23" @default.
- W2022169084 hasLocation W20221690841 @default.
- W2022169084 hasLocation W20221690842 @default.
- W2022169084 hasOpenAccess W2022169084 @default.
- W2022169084 hasPrimaryLocation W20221690841 @default.
- W2022169084 hasRelatedWork W2022169084 @default.
- W2022169084 hasRelatedWork W2035391229 @default.
- W2022169084 hasRelatedWork W2057620252 @default.
- W2022169084 hasRelatedWork W2057650941 @default.
- W2022169084 hasRelatedWork W2057967888 @default.
- W2022169084 hasRelatedWork W2092074623 @default.
- W2022169084 hasRelatedWork W2150530449 @default.
- W2022169084 hasRelatedWork W2313440058 @default.
- W2022169084 hasRelatedWork W41831601 @default.
- W2022169084 hasRelatedWork W2136545008 @default.
- W2022169084 hasVolume "36" @default.
- W2022169084 isParatext "false" @default.
- W2022169084 isRetracted "false" @default.
- W2022169084 magId "2022169084" @default.
- W2022169084 workType "article" @default.