Linked Life Data

20688161

Source:http://linkedlifedata.com/resource/pubmed/id/20688161

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2010-10-11
pubmed:abstractText
Laminins are multidomain glycoproteins that play important roles in development and maintenance of the extracellular matrix via their numerous interactions with other proteins. Several receptors for the laminin short arms revealed their importance in network formation and intercellular signaling. However, both the detailed structure of the laminin ?-1 short arm and its organization within the complexes is poorly understood due to the complexity of the molecule and the lack of a high-resolution structure. The presented data provide the first subatomic resolution structure for the laminin ?-1 short arm in solution. This was achieved using an integrated approach that combined a number of complementary biophysical techniques such as small angle X-ray scattering (SAXS), analytical ultracentrifugation, dynamic light scattering and electron microscopy. As a result of this study, we have obtained a significantly improved model for the laminin ?-1 short arm that represents a major step forward in molecular understanding of laminin-mediated complex formations.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1569-1802
pubmed:author
pubmed:copyrightInfo
Crown Copyright © 2010. Published by Elsevier B.V. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
565-72
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Nano-structure of the laminin ?-1 short arm reveals an extended and curved multidomain assembly.
pubmed:affiliation
Department of Chemistry, University of Manitoba, 144 Dysart Road, Winnipeg, Manitoba, Canada R3T 2N2.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't