Linked Life Data

19056345

Source:http://linkedlifedata.com/resource/pubmed/id/19056345

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2008-12-29
pubmed:abstractText
The effect of the electrical charge or the size of the amino acid residue at the pore center of a slowly activation component of the delayed rectifier potassium channel: KCNQ1 was studied. K(+) currents were measured after transfection of one of four KCNQ1 mutants: substituting Isoleucine with Lysine, Glutamate, Valine or Glycine and then transfected in COS-7 cells. Both the negatively- and positive charged residue I313K and I313E showed a loss of function when expressed alone and a dominant negative suppression when co-expressed with wild type KCNQ1. When the site was substituted with the smallest neutral amino acid residue: I313G, there was a small reduction of current when transfected alone and a gain of function when co-transfected with the wild type. I313V showed no difference from the wild type. Changes of amino acid residue at the pore center of KCNQ1 may alter the channel function but this depends on the electrical charge or the size of amino acid residue.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
16
pubmed:volume
378
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
589-94
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Evaluation of channel function after alteration of amino acid residues at the pore center of KCNQ1 channel.
pubmed:affiliation
Division of Cardiology, First Department of Internal Medicine, Niigata University Graduate School of Medical and Dental Sciences, 1-754 Asahimachi Dori, Chuo-ku, Niigata 951-8510, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't