Linked Life Data

18373252

Source:http://linkedlifedata.com/resource/pubmed/id/18373252

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2008-3-31
pubmed:abstractText
Collagens represent a large family of structurally related extracellular matrix proteins containing unique triple helical structure. One of the characteristics of this structural protein is its extensive post-translational modifications that have major effects on molecular assembly, stability, and metabolism. Hydroxylation of specific lysine residues is one of such unique modifications found in collagen, and the pattern/extent of this modification influences fibrillogenesis, cross-linking, and matrix mineralization. The formation of covalent intermolecular cross-linking is the final modification in collagen biosynthesis and is critical for the stability of collagen. The process of cross-linking is dynamic and the pathways vary depending on the tissues and tissue's physiological state. This tissue specificity of cross-linking pattern may in part be the results of differential expression of various isoforms of lysyl hydroxylases and lysyl oxidases that have been recently identified and partially characterized. This chapter concentrates on recent research progress on these two modifications and the methods for analysis we have developed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1064-3745
pubmed:author
pubmed:issnType
Print
pubmed:volume
446
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
95-108
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Lysine hydroxylation and cross-linking of collagen.
pubmed:affiliation
Dental Research Center, University of North Carolina, Chapel Hill, NC, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, N.I.H., Extramural