pubmed-article:8794093 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8794093 | lifeskim:mentions | umls-concept:C0006675 | lld:lifeskim |
pubmed-article:8794093 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:8794093 | lifeskim:mentions | umls-concept:C0031760 | lld:lifeskim |
pubmed-article:8794093 | lifeskim:mentions | umls-concept:C0041249 | lld:lifeskim |
pubmed-article:8794093 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
pubmed-article:8794093 | lifeskim:mentions | umls-concept:C0013138 | lld:lifeskim |
pubmed-article:8794093 | lifeskim:mentions | umls-concept:C1998811 | lld:lifeskim |
pubmed-article:8794093 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:8794093 | pubmed:dateCreated | 1996-12-16 | lld:pubmed |
pubmed-article:8794093 | pubmed:abstractText | Invertebrate photoreceptors use the ubiquitous inositol-lipid signaling pathway for phototransduction. This pathway depends on Ca2+ release from internal stores and on Ca2+ entry via light-activated channels to replenish the loss of Ca2+ in those stores. The Drosophila transient receptor potential (TRP) protein is essential for the high Ca2+ permeability and other biophysical properties of these light-activated channels, which affect both excitation and adaptation in photoreceptor cells. Physiological and heterologous expression studies indicate that TRP is a putative subunit of a surface membrane channel that can be activated by depletion of internal Ca2+ stores. Furthermore, trp is an archetypal member of a multigene family whose products share a structure that is highly conserved throughout evolution, from worms to humans. | lld:pubmed |
pubmed-article:8794093 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8794093 | pubmed:language | eng | lld:pubmed |
pubmed-article:8794093 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8794093 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8794093 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8794093 | pubmed:month | Aug | lld:pubmed |
pubmed-article:8794093 | pubmed:issn | 0959-4388 | lld:pubmed |
pubmed-article:8794093 | pubmed:author | pubmed-author:MinkeBB | lld:pubmed |
pubmed-article:8794093 | pubmed:author | pubmed-author:SelingerZZ | lld:pubmed |
pubmed-article:8794093 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8794093 | pubmed:volume | 6 | lld:pubmed |
pubmed-article:8794093 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8794093 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8794093 | pubmed:pagination | 459-66 | lld:pubmed |
pubmed-article:8794093 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:8794093 | pubmed:meshHeading | pubmed-meshheading:8794093-... | lld:pubmed |
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pubmed-article:8794093 | pubmed:meshHeading | pubmed-meshheading:8794093-... | lld:pubmed |
pubmed-article:8794093 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8794093 | pubmed:articleTitle | The roles of trp and calcium in regulating photoreceptor function in Drosophila. | lld:pubmed |
pubmed-article:8794093 | pubmed:affiliation | Department of Physiology, The Hebrew University - Hadassah Medical School, Jerusalem 91120, Israel. minke@md2.huji.ac.il | lld:pubmed |
pubmed-article:8794093 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8794093 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:8794093 | pubmed:publicationType | Review | lld:pubmed |
pubmed-article:8794093 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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