12895415

Source:http://linkedlifedata.com/resource/pubmed/id/12895415

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0678594, umls-concept:C1522634, umls-concept:C1706817
pubmed:issue	3
pubmed:dateCreated	2003-8-4
pubmed:abstractText	The recent landmark structures of KvAP, a voltage-gated potassium (Kv) channel, provide the first high-resolution experimental structural models of this class of proteins. Previous extensive studies of Kv channels provide a means to evaluate and interpret the KvAP structures. In this minireview, we survey different experimental approaches to Kv channels and map these findings to KvAP, showing that the relationship between the KvAP structures and other Kv channels is uncertain.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/8809320
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Voltage-Gated
pubmed:status	MEDLINE
pubmed:month	Jul
pubmed:issn	0896-6273
pubmed:author	pubmed-author:CohenBruce EBE, pubmed-author:GrabeMichaelM, pubmed-author:JanLily YehLY
pubmed:issnType	Print
pubmed:day	31
pubmed:volume	39
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	395-400
pubmed:dateRevised	2005-11-16
pubmed:meshHeading	pubmed-meshheading:12895415-Animals, pubmed-meshheading:12895415-Humans, pubmed-meshheading:12895415-Ion Channel Gating, pubmed-meshheading:12895415-Mutation, pubmed-meshheading:12895415-Potassium Channels, Voltage-Gated, pubmed-meshheading:12895415-Structure-Activity Relationship
pubmed:year	2003
pubmed:articleTitle	Answers and questions from the KvAP structures.
pubmed:affiliation	Howard Hughes Medical Institute and Departments of Physiology and Biochemistry, University of California, San Francisco, San Francisco, California 94143, USA.
pubmed:publicationType	Journal Article, Review