10378264

Source:http://linkedlifedata.com/resource/pubmed/id/10378264

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0012625, umls-concept:C0233494, umls-concept:C0439799
pubmed:issue	5
pubmed:dateCreated	1999-8-6
pubmed:abstractText	The crystal structure of a bacterial MscL shows how this homopentameric channel protein is held tightly shut to prevent leakage whilst at rest. By inference, the structure also shows how a stretch force in the lipid bilayer causes the channel to open. We now have a concrete picture as to how a stimulus 'gates' an ion channel.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101087697
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels, http://linkedlifedata.com/resource/pubmed/chemical/MscL protein, E coli
pubmed:status	MEDLINE
pubmed:month	May
pubmed:issn	0969-2126
pubmed:author	pubmed-author:BatizaA FAF, pubmed-author:KunoKK, pubmed-author:RaymentII
pubmed:issnType	Print
pubmed:volume	7
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	R99-103
pubmed:dateRevised	2005-12-29
pubmed:meshHeading	pubmed-meshheading:10378264-Amino Acid Sequence, pubmed-meshheading:10378264-Escherichia coli Proteins, pubmed-meshheading:10378264-Ion Channel Gating, pubmed-meshheading:10378264-Ion Channels, pubmed-meshheading:10378264-Molecular Sequence Data, pubmed-meshheading:10378264-Protein Conformation
pubmed:year	1999
pubmed:articleTitle	Channel gate! Tension, leak and disclosure.
pubmed:affiliation	Laboratory of Molecular Biology, University of Wisconsin, Madison 53706, USA.
pubmed:publicationType	Journal Article, Review