Linked Life Data

11018527

Source:http://linkedlifedata.com/resource/pubmed/id/11018527

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2000-11-8
pubmed:abstractText
An essential step in the pathogenesis of Salmonella enterica infections is bacterial entry into non-phagocytic cells of the intestinal epithelium. Proteins injected by Salmonella into host cells stimulate cellular responses that lead to extensive actin cytoskeleton reorganization and subsequent bacterial uptake. One of these proteins, SipA, modulates actin dynamics by directly binding to F-actin. We have biophysically characterized a C-terminal fragment, SipA(446-684), which has previously been shown to retain activity. Our results show that SipA(446-684) exhibits an elongated shape with a predominantly helical conformation and predict the existence of a coiled-coil domain. We suggest that the protein is able to span two adjacent actin monomers in a filament and propose a model that is consistent with the observed effects of SipA(446-684) on actin dynamics and F-actin stability and morphology.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
482
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
81-4
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Biophysical characterization of SipA, an actin-binding protein from Salmonella enterica.
pubmed:affiliation
Department of Cell Biology, Yale University, New Haven, CT 06510, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't