Matches in SemOpenAlex for { <https://semopenalex.org/work/W2116880855> ?p ?o ?g. }
- W2116880855 endingPage "434" @default.
- W2116880855 startingPage "417" @default.
- W2116880855 abstract "Phototransduction in vertebrate photoreceptor cells mediated by rhodopsin is one of the most comprehensively examined G protein-coupled receptor (GPCR) signaling pathways. The signal transduction pathway can be mapped from the initial absorption of light to conformational changes within rhodopsin, through activation of the G protein transducin, and to the ultimate closure of the cation cGMP-gated channels in the plasma membrane. Furthermore, phototransduction has become an intensely studied model system for understanding the desensitizing processes that allow reduced non-linear responses of photoreceptor cells to increasing levels of illumination. Although some general themes appear to occur in GPCR systems, the details of these desensitizing processes are likely to be specific to each of the receptors. These differences are attributed to the fact that each receptor has unique kinetic constraints, amplification levels, tolerance to basal constitutive activity, intracellular internalization and recycling, redundancy of isoforms, and morphologies of the cell of their expression. One of the biochemical processes that are believed to be a common part of this desensitization of the GPCR-mediated cascade is receptor phosphorylation catalyzed by members of a small family of the GPCR kinases. The enzymatic, physiological and genetic aspects of rhodopsin phosphorylation and rhodopsin kinase have been characterized extensively over the last 30 yr. However, new structurally based approaches to examining rhodopsin kinase and rhodopsin phosphorylation are still awaiting further investigations. We present here a summary of the current understanding of rhodopsin phosphorylation and the properties of rhodopsin kinase, along with some expectations of future investigations into these topics." @default.
- W2116880855 created "2016-06-24" @default.
- W2116880855 creator A5033845279 @default.
- W2116880855 creator A5042148986 @default.
- W2116880855 creator A5045657649 @default.
- W2116880855 date "2003-07-01" @default.
- W2116880855 modified "2023-10-17" @default.
- W2116880855 title "Rhodopsin phosphorylation: 30 years later" @default.
- W2116880855 cites W1178593131 @default.
- W2116880855 cites W1495244568 @default.
- W2116880855 cites W150052835 @default.
- W2116880855 cites W1509709236 @default.
- W2116880855 cites W1515512367 @default.
- W2116880855 cites W1530935792 @default.
- W2116880855 cites W1533788848 @default.
- W2116880855 cites W1558733231 @default.
- W2116880855 cites W1560667802 @default.
- W2116880855 cites W1563425172 @default.
- W2116880855 cites W1564149292 @default.
- W2116880855 cites W1567325248 @default.
- W2116880855 cites W1568722752 @default.
- W2116880855 cites W1576144424 @default.
- W2116880855 cites W1585566332 @default.
- W2116880855 cites W1585690431 @default.
- W2116880855 cites W1587185311 @default.
- W2116880855 cites W1601522037 @default.
- W2116880855 cites W1602103265 @default.
- W2116880855 cites W1603853902 @default.
- W2116880855 cites W1655831458 @default.
- W2116880855 cites W167412706 @default.
- W2116880855 cites W1729414464 @default.
- W2116880855 cites W183114978 @default.
- W2116880855 cites W1846247956 @default.
- W2116880855 cites W1850214287 @default.
- W2116880855 cites W1869743569 @default.
- W2116880855 cites W1904128007 @default.
- W2116880855 cites W1953109900 @default.
- W2116880855 cites W1965205594 @default.
- W2116880855 cites W1967556830 @default.
- W2116880855 cites W1967623345 @default.
- W2116880855 cites W1969025414 @default.
- W2116880855 cites W1969595890 @default.
- W2116880855 cites W1970390357 @default.
- W2116880855 cites W1971273204 @default.
- W2116880855 cites W1971874730 @default.
- W2116880855 cites W1972051226 @default.
- W2116880855 cites W1972961295 @default.
- W2116880855 cites W1973330221 @default.
- W2116880855 cites W1973505127 @default.
- W2116880855 cites W1973586968 @default.
- W2116880855 cites W1974004650 @default.
- W2116880855 cites W1974799596 @default.
- W2116880855 cites W1974910395 @default.
- W2116880855 cites W1979664176 @default.
- W2116880855 cites W1981783745 @default.
- W2116880855 cites W1981995076 @default.
- W2116880855 cites W1982713293 @default.
- W2116880855 cites W1984101571 @default.
- W2116880855 cites W1984838744 @default.
- W2116880855 cites W1985172044 @default.
- W2116880855 cites W1985580256 @default.
- W2116880855 cites W1986925105 @default.
- W2116880855 cites W1990129321 @default.
- W2116880855 cites W1991350528 @default.
- W2116880855 cites W1993160436 @default.
- W2116880855 cites W1993697025 @default.
- W2116880855 cites W1993755473 @default.
- W2116880855 cites W1995686520 @default.
- W2116880855 cites W1995864935 @default.
- W2116880855 cites W1998261085 @default.
- W2116880855 cites W1998811652 @default.
- W2116880855 cites W1999130956 @default.
- W2116880855 cites W1999179844 @default.
- W2116880855 cites W1999314849 @default.
- W2116880855 cites W1999801438 @default.
- W2116880855 cites W2001975667 @default.
- W2116880855 cites W2003835543 @default.
- W2116880855 cites W2004759988 @default.
- W2116880855 cites W2006718599 @default.
- W2116880855 cites W2006728906 @default.
- W2116880855 cites W2008485465 @default.
- W2116880855 cites W2009156962 @default.
- W2116880855 cites W2009169885 @default.
- W2116880855 cites W2009259360 @default.
- W2116880855 cites W2009407133 @default.
- W2116880855 cites W2010646533 @default.
- W2116880855 cites W2012987770 @default.
- W2116880855 cites W2013596647 @default.
- W2116880855 cites W2014033644 @default.
- W2116880855 cites W2014899116 @default.
- W2116880855 cites W2016537683 @default.
- W2116880855 cites W2016542329 @default.
- W2116880855 cites W2019281085 @default.
- W2116880855 cites W2022169084 @default.
- W2116880855 cites W2023343036 @default.
- W2116880855 cites W2025692747 @default.
- W2116880855 cites W2029087881 @default.
- W2116880855 cites W2032597695 @default.