Linked Life Data

12885418

Source:http://linkedlifedata.com/resource/pubmed/id/12885418

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
2003-7-29
pubmed:abstractText
The small G protein adenosine diphosphate ribosylation factor-1 (ARF1) is activated by cell membrane binding of a self-folding N-terminal domain. We present a model of the human ARF1 N-terminal peptide in planar lipid bilayers, determined from neutron lamellar diffraction and circular dichroism data with molecular modelling. This amphipathic domain lies at a shallow membrane depth, ideal for regulation of the ARF1 bio-timer by rapid, reversible membrane binding. The helical region does not elongate upon membrane binding, leaving the connecting flexible linker region's length unchanged.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
548
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
119-24
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
The membrane bound N-terminal domain of human adenosine diphosphate ribosylation factor-1 (ARF1).
pubmed:affiliation
Department of Preclinical Veterinary Sciences, R.(D.)S.V.S., University of Edinburgh, Summerhall, Edinburgh, EH9 1QH, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't