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

Kourie, Joseph; Henry, Christine; Farrelly, Peter

Description

1. 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.contributor.authorKourie, Joseph
dc.contributor.authorHenry, Christine
dc.contributor.authorFarrelly, Peter
dc.date.accessioned2015-12-10T23:16:47Z
dc.identifier.issn0272-4340
dc.identifier.urihttp://hdl.handle.net/1885/65219
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.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.description.notesImported from ARIES
local.description.refereedYes
local.identifier.citationvolume21
dc.date.issued2001
local.identifier.absfor030505 - Physical Organic Chemistry
local.identifier.ariespublicationMigratedxPub1072
local.type.statusPublished Version
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.description.embargo2037-12-31
local.bibliographicCitation.issue3
local.bibliographicCitation.startpage255
local.bibliographicCitation.lastpage284
local.identifier.doi10.1023/A:1010995121153
dc.date.updated2015-12-10T09:56:50Z
local.identifier.scopusID2-s2.0-0034856924
CollectionsANU Research Publications

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