RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/12907679http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12907679http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12907679http://www.w3.org/2000/01/rdf-schema#comment"The bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterized channel proteins. The human genome codes for four bestrophins, each of which confers a distinctive plasma membrane conductance on transfected 293 cells. Extracellular treatment with methanethiosulfonate ethyltrimethylammonium (MTSET) of a series of substitution mutants that eliminate one or more cysteines from human bestrophin1 demonstrates that cysteine 69 is the single endogenous cysteine responsible for MTSET inhibition of whole-cell current. Cysteines introduced between positions 78-99 and 223-226 are also accessible to external MTSET, with MTSET modification at positions 79, 80, 83, and 90 producing a 2-6-fold increase in whole-cell current. The latter set of four cysteine-substitution mutants define a region that appears to mediate allosteric control of channel activity. Mapping of transmembrane topography by insertion of N-linked glycosylation sites and tobacco etch virus protease cleavage sites provides evidence for cytosolic N and C termini and an unexpected transmembrane topography with at least three extracellular loops that include positions 60-63, 212-227, and 261-267. These experiments provide the first structural analysis of the bestrophin channel family."xsd:string
http://purl.uniprot.org/citations/12907679http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m306150200"xsd:string
http://purl.uniprot.org/citations/12907679http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m306150200"xsd:string
http://purl.uniprot.org/citations/12907679http://purl.org/dc/terms/identifier"doi:10.1074/jbc.M306150200"xsd:string
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/author"Sun H."xsd:string
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/author"Sun H."xsd:string
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/author"Williams J."xsd:string
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/author"Williams J."xsd:string
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/author"Nathans J."xsd:string
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/author"Nathans J."xsd:string
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/author"Yau K.W."xsd:string
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/author"Cahill H."xsd:string
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/author"Cahill H."xsd:string
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/author"Smallwood P."xsd:string
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/author"Smallwood P."xsd:string
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/author"Tsunenari T."xsd:string
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/author"Tsunenari T."xsd:string
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/author"Yau K.-W."xsd:string
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/author"Yau K.-W."xsd:string
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12907679http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string