Diversity of Amyloid β Protein Fragment [1-40]-Formed Channels

dc.contributor.authorKourie, Joseph
dc.contributor.authorHenry, Christine
dc.contributor.authorFarrelly, Peter
dc.date.accessioned2015-12-10T23:16:47Z
dc.date.issued2001
dc.date.updated2015-12-10T09:56:50Z
dc.description.abstract1. The lipid bilayer technique was used to characterize the biophysical and pharmacological properties of several ion channels formed by incorporating amyloid beta protein fragment (AβP) 1-40 into lipid membranes. Based on the conductance, kinetics, sele
dc.identifier.issn0272-4340
dc.identifier.urihttp://hdl.handle.net/1885/65219
dc.publisherKluwer Academic Publishers
dc.sourceCellular and Molecular Neurobiology
dc.subjectKeywords: amyloid beta protein; ion channel; potassium chloride; zinc chloride; article; cell membrane conductance; cell membrane transport; channel gating; degenerative disease; human; learning; molecular dynamics; neurobiology; nonhuman; priority journal; signal Alzheimer's disease; Channel-forming peptides; Entangles; Memory and learning; Neurodegenerative diseases; Signal transduction
dc.titleDiversity of Amyloid β Protein Fragment [1-40]-Formed Channels
dc.typeJournal article
local.bibliographicCitation.issue3
local.bibliographicCitation.lastpage284
local.bibliographicCitation.startpage255
local.contributor.affiliationKourie, Joseph, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationHenry, Christine, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationFarrelly, Peter, College of Physical and Mathematical Sciences, ANU
local.contributor.authoremailrepository.admin@anu.edu.au
local.contributor.authoruidKourie, Joseph, u9111360
local.contributor.authoruidHenry, Christine, u9902065
local.contributor.authoruidFarrelly, Peter, u9909159
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.absfor030505 - Physical Organic Chemistry
local.identifier.ariespublicationMigratedxPub1072
local.identifier.citationvolume21
local.identifier.doi10.1023/A:1010995121153
local.identifier.scopusID2-s2.0-0034856924
local.identifier.uidSubmittedByMigrated
local.type.statusPublished Version

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