Linked Life Data

10367728

Source:http://linkedlifedata.com/resource/pubmed/id/10367728

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-8-12
pubmed:abstractText
Laminins are the most abundant structural non-collagenous glycoproteins ubiquitously present in basement membranes. They are multidomain molecules constituting a family of possibly more than 50 members. Some members such as laminins 5, 6 and 10 are specific of the basal lamina present under stratified epithelia. Although only few intact laminin isoforms have been purified from cultivated cells or tissues, genetic engineering has opened the way for a rapid development of laminin structural biology. Moreover, the phenotypes resulting from gene targeting in mouse or from laminin defects in acquired or inherited human diseases highlight the pivotal role of laminins in morphogenesis, development, and physiology. Indeed, the laminins display a remarkable repertoire of functions, most importantly as structural elements forming a network throughout the basement membrane to which other collagenous or non-collagenous glycoproteins and proteoglycans attach. Furthermore, they are signaling molecules providing adjacent cells with diverse information by interacting with cell surface components.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0945-053X
pubmed:author
pubmed:issnType
Print
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19-28
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Laminins of the dermo-epidermal junction.
pubmed:affiliation
Institut II für Biochemie, Medical Faculty, Cologne, Germany. aumailley@uni-koeln.de
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't