12814565

Source:http://linkedlifedata.com/resource/pubmed/id/12814565

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0444519, umls-concept:C1548792, umls-concept:C2350229, umls-concept:C2607943, umls-concept:C2926606
pubmed:issue	12
pubmed:dateCreated	2003-6-19
pubmed:abstractText	TRPV and TRPM proteins have been shown to form temperature-responsive cation channels that act in nociception. Recent work on the mouse ANKTM1 and Drosophila Painless proteins shows that members of a third TRP subfamily, TRPN, also function in thermosensation.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/9107782
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels, http://linkedlifedata.com/resource/pubmed/chemical/Transient Receptor Potential..., http://linkedlifedata.com/resource/pubmed/chemical/painless protein, Drosophila
pubmed:status	MEDLINE
pubmed:month	Jun
pubmed:issn	0960-9822
pubmed:author	pubmed-author:MontellCraigC
pubmed:issnType	Print
pubmed:day	17
pubmed:volume	13
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	R476-8
pubmed:dateRevised	2010-11-18
pubmed:meshHeading	pubmed-meshheading:12814565-Animals, pubmed-meshheading:12814565-Cold Temperature, pubmed-meshheading:12814565-Drosophila Proteins, pubmed-meshheading:12814565-Ion Channels, pubmed-meshheading:12814565-Protein Structure, Tertiary, pubmed-meshheading:12814565-Thermosensing, pubmed-meshheading:12814565-Transient Receptor Potential Channels
pubmed:year	2003
pubmed:articleTitle	Thermosensation: hot findings make TRPNs very cool.
pubmed:affiliation	Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA. cmontell@jhmi.edu
pubmed:publicationType	Journal Article, Review