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dc.contributor.authorNamadurai, Sivakumar
dc.contributor.authorYereddi, Nikitha R
dc.contributor.authorCusdin, Fiona S
dc.contributor.authorHuang, Christopher
dc.contributor.authorChirgadze, Dima
dc.contributor.authorJackson, Antony
dc.date.accessioned2018-09-20T12:04:10Z
dc.date.available2018-09-20T12:04:10Z
dc.date.issued2015-01
dc.identifier.issn2046-2441
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/280463
dc.description.abstractVoltage-gated sodium (Nav) channels are intrinsic plasma membrane proteins that initiate the action potential in electrically excitable cells. They are a major focus of research in neurobiology, structural biology, membrane biology and pharmacology. Mutations in Nav channels are implicated in a wide variety of inherited pathologies, including cardiac conduction diseases, myotonic conditions, epilepsy and chronic pain syndromes. Drugs active against Nav channels are used as local anaesthetics, anti-arrhythmics, analgesics and anti-convulsants. The Nav channels are composed of a pore-forming α subunit and associated β subunits. The β subunits are members of the immunoglobulin (Ig) domain family of cell-adhesion molecules. They modulate multiple aspects of Nav channel behaviour and play critical roles in controlling neuronal excitability. The recently published atomic resolution structures of the human β3 and β4 subunit Ig domains open a new chapter in the study of these molecules. In particular, the discovery that β3 subunits form trimers suggests that Nav channel oligomerization may contribute to the functional properties of some β subunits.
dc.format.mediumPrint
dc.languageeng
dc.publisherThe Royal Society
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectAnimals
dc.subjectHumans
dc.subjectEvolution, Molecular
dc.subjectIon Channel Gating
dc.subjectAmino Acid Sequence
dc.subjectAction Potentials
dc.subjectMolecular Sequence Data
dc.subjectVoltage-Gated Sodium Channel beta Subunits
dc.titleA new look at sodium channel β subunits.
dc.typeArticle
prism.issueIdentifier1
prism.publicationDate2015
prism.publicationNameOpen Biol
prism.startingPage140192
prism.volume5
dc.identifier.doi10.17863/CAM.27834
rioxxterms.versionofrecord10.1098/rsob.140192
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2015-01
dc.contributor.orcidHuang, Christopher [0000-0001-9553-6112]
dc.contributor.orcidChirgadze, Dima [0000-0001-9942-0993]
dc.contributor.orcidJackson, Antony [0000-0002-2895-7387]
dc.identifier.eissn2046-2441
rioxxterms.typeJournal Article/Review
pubs.funder-project-idMedical Research Council (MR/M001288/1)
pubs.funder-project-idBritish Heart Foundation (None)
cam.issuedOnline2015-01


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Attribution 4.0 International
Except where otherwise noted, this item's licence is described as Attribution 4.0 International