Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2005-6-17
pubmed:abstractText
Glutamate receptor ion channels mediate excitatory responses at the majority of CNS synapses. They are the only ligand-gated ion channels for which multiple high-resolution crystal structures have been solved. Highlights of information gained from mechanistic studies based on the crystal structures of their ligand-binding domains include explanations for strikingly diverse phenomena. These include the basis for subtype-specific agonist selectivity; mechanisms for desensitization and allosteric modulation; and mechanisms for partial agonist activity. In addition, multiple lines of evidence, including low-resolution electron microscopic studies, suggest that native AMPA receptors combine with an auxiliary subunit which regulates activity and trafficking. Functional studies suggest that glutamate receptor gating is distinct from that of structurally related voltage-gated ion channels.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0959-4388
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
282-8
pubmed:dateRevised
2005-11-16
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Glutamate receptor ion channels.
pubmed:affiliation
Laboratory of Cellular and Molecular Neurophysiology, Porter Neuroscience Research Center, Building 35 Room 3B 1002 MSC 3712, 35 Lincoln Drive, Bethesda, MD 20892-3712, USA. mayerm@mail.nih.gov
pubmed:publicationType
Journal Article, Review