Linked Life Data

11102870

Source:http://linkedlifedata.com/resource/pubmed/id/11102870

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2001-2-2
pubmed:abstractText
During the past year, remarkable progress has been made in understanding how periplasmic chaperones fold and protect protein modules that are destined for assembly into adhesive pili in Gram-negative bacteria. The first two three-dimensional structures of complexes of periplasmic chaperones with substrate pilus subunits have revealed much about the structural basis for chaperone-mediated folding and aggregation prevention, and have provided insight into the structure of adhesive pili.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1367-5931
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
653-60
pubmed:dateRevised
2009-8-25
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Bacterial adhesins: structural studies reveal chaperone function and pilus biogenesis.
pubmed:affiliation
Swedish University of Agricultural Sciences, Uppsala Biomedical Center, Department of Molecular Biology, PO Box 590, SE 751 24, Uppsala, Sweden. stefan@xray.bmc.uu.se
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't