| pubmed-article:2844605 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2844605 | lifeskim:mentions | umls-concept:C0206427 | lld:lifeskim |
| pubmed-article:2844605 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:2844605 | lifeskim:mentions | umls-concept:C0035331 | lld:lifeskim |
| pubmed-article:2844605 | lifeskim:mentions | umls-concept:C0104230 | lld:lifeskim |
| pubmed-article:2844605 | lifeskim:mentions | umls-concept:C0441472 | lld:lifeskim |
| pubmed-article:2844605 | lifeskim:mentions | umls-concept:C1882365 | lld:lifeskim |
| pubmed-article:2844605 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2844605 | pubmed:dateCreated | 1988-11-14 | lld:pubmed |
| pubmed-article:2844605 | pubmed:abstractText | The target proteins for arrestin (48 kDa protein) action during the quench of cGMP phosphodiesterase (PDE) activation in retinal rod disk membranes were identified by the use of a cross-linking reagent. A heterobifunctional, cleavable, photo-activatable cross-linker (sulfo-SADP) was coupled to purified arrestin. Under precise weak visible light bleach and nucleotide conditions of quench, the cross-linker was UV flash-activated at a time when quench was well established. The target proteins covalently linked to arrestin by cross-linker activation were identified by immunoblotting. In the presence of ATP arrestin cross-linked to both PDE and rhodopsin during the quench phenomenon. Removal of ATP from the reaction mixture essentially abolished the cross-link with PDE, just as ATP omission abolishes quench, but significantly increased the cross-link to rhodopsin. The absence of a cross-link to the plentiful beta-subunit of transductin, as well as the results of competition studies employing arrestin without attached cross-linker, suggest that the observed cross-links are specific and reflect true binding interactions of arrestin during quench. The data are consistent with a model of quench in which photolyzed rhodopsin (R*) catalyzes the formation of an activated form of arrestin, which dissociates from R* in the presence of ATP, and binds to PDEs, thereby deactivating them. | lld:pubmed |
| pubmed-article:2844605 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2844605 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2844605 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2844605 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2844605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2844605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2844605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2844605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2844605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2844605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2844605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2844605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2844605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2844605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2844605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2844605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2844605 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2844605 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:2844605 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:2844605 | pubmed:author | pubmed-author:ZuckermanRR | lld:pubmed |
| pubmed-article:2844605 | pubmed:author | pubmed-author:CheastyJ EJE | lld:pubmed |
| pubmed-article:2844605 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2844605 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:2844605 | pubmed:volume | 238 | lld:pubmed |
| pubmed-article:2844605 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2844605 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2844605 | pubmed:pagination | 379-84 | lld:pubmed |
| pubmed-article:2844605 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:2844605 | pubmed:meshHeading | pubmed-meshheading:2844605-... | lld:pubmed |
| pubmed-article:2844605 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:2844605 | pubmed:articleTitle | Sites of arrestin action during the quench phenomenon in retinal rods. | lld:pubmed |
| pubmed-article:2844605 | pubmed:affiliation | Department of Ophthalmology, Scheie Eye Institute, University of Pennsylvania School of Medicine, Philadelphia 19104. | lld:pubmed |
| pubmed-article:2844605 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2844605 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2844605 | lld:pubmed |
