Linked Life Data

7691102

Source:http://linkedlifedata.com/resource/pubmed/id/7691102

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-11-1
pubmed:abstractText
Divalent cation blockade of cGMP-gated channels in photoreceptor cells ensures the low open channel noise required for a highly sensitive visual transduction process. This study identifies a divalent cation-binding site in the pore of a retinal cGMP-gated channel expressed in Xenopus oocytes. Substitution of a specific glutamate residue by a neutral amino acid renders the channel insensitive to external Mg2+ and Ca2+ and affects the conduction of Na+. The mutated channels remain sensitive to internal divalent cations. These results place the glutamate residue in the ion conduction pathway close to the extracellular surface.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0896-6273
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
459-66
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Identification of an external divalent cation-binding site in the pore of a cGMP-activated channel.
pubmed:affiliation
Department of Neurobiology, Harvard Medical School, Boston, Massachusetts 02115.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.