| pubmed-article:11874457 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11874457 | lifeskim:mentions | umls-concept:C0766823 | lld:lifeskim |
| pubmed-article:11874457 | lifeskim:mentions | umls-concept:C0972255 | lld:lifeskim |
| pubmed-article:11874457 | lifeskim:mentions | umls-concept:C0009325 | lld:lifeskim |
| pubmed-article:11874457 | lifeskim:mentions | umls-concept:C0010511 | lld:lifeskim |
| pubmed-article:11874457 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:11874457 | lifeskim:mentions | umls-concept:C0057252 | lld:lifeskim |
| pubmed-article:11874457 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:11874457 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:11874457 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
| pubmed-article:11874457 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:11874457 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:11874457 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:11874457 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:11874457 | pubmed:dateCreated | 2002-3-4 | lld:pubmed |
| pubmed-article:11874457 | pubmed:abstractText | Decorin is a small leucine-rich chondroitin/dermatan sulfate proteoglycan reported to interact with fibrillar collagens through its protein core and to localize at d and e bands of the collagen fibril banding pattern. Using a solid-phase assay, we have determined the interaction of peptides derived by CNBr cleavage of type I and type II collagen with decorin extracted from bovine tendon and its protein core and with a recombinant decorin preparation. At least five peptides have been found to interact with all three decorin samples. The interaction of peptides with tendon decorin has a dissociation constant in the nanomolar range. The triple helical conformation of the peptide trimeric species is a necessary requisite for the binding. All positive peptides have a region within the d and e bands of collagen fibrils. Two chemical derivatives of collagens and of positive peptides were prepared by N-acetylation and N-methylation of the primary amino group of Lys/Hyl side chains. Chemical modifications performed in mild conditions do not significantly alter the thermal stability of peptide trimeric species whereas they affect the interaction with decorin: N-acetylation eliminates both the positive charge and the binding to decorin, whereas N-methylation preserves the cationic character and modulates the binding. We conclude that decorin makes contacts with multiple sites in type I collagen and probably also in type II collagen and that some collagen Lys/Hyl residues are essential for the binding. | lld:pubmed |
| pubmed-article:11874457 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11874457 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11874457 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11874457 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11874457 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11874457 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11874457 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11874457 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11874457 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11874457 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11874457 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:11874457 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:11874457 | pubmed:author | pubmed-author:RossiAntonioA | lld:pubmed |
| pubmed-article:11874457 | pubmed:author | pubmed-author:TenniRuggeroR | lld:pubmed |
| pubmed-article:11874457 | pubmed:author | pubmed-author:ViolaManuelaM | lld:pubmed |
| pubmed-article:11874457 | pubmed:author | pubmed-author:WelserFranzF | lld:pubmed |
| pubmed-article:11874457 | pubmed:author | pubmed-author:SiniPatriziaP | lld:pubmed |
| pubmed-article:11874457 | pubmed:author | pubmed-author:GiudiciCamill... | lld:pubmed |
| pubmed-article:11874457 | pubmed:author | pubmed-author:TiraM... | lld:pubmed |
| pubmed-article:11874457 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11874457 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:11874457 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11874457 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11874457 | pubmed:pagination | 1428-37 | lld:pubmed |
| pubmed-article:11874457 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:11874457 | pubmed:meshHeading | pubmed-meshheading:11874457... | lld:pubmed |
| pubmed-article:11874457 | pubmed:meshHeading | pubmed-meshheading:11874457... | lld:pubmed |
| pubmed-article:11874457 | pubmed:meshHeading | pubmed-meshheading:11874457... | lld:pubmed |
| pubmed-article:11874457 | pubmed:meshHeading | pubmed-meshheading:11874457... | lld:pubmed |
| pubmed-article:11874457 | pubmed:meshHeading | pubmed-meshheading:11874457... | lld:pubmed |
| pubmed-article:11874457 | pubmed:meshHeading | pubmed-meshheading:11874457... | lld:pubmed |
| pubmed-article:11874457 | pubmed:meshHeading | pubmed-meshheading:11874457... | lld:pubmed |
| pubmed-article:11874457 | pubmed:meshHeading | pubmed-meshheading:11874457... | lld:pubmed |
| pubmed-article:11874457 | pubmed:meshHeading | pubmed-meshheading:11874457... | lld:pubmed |
| pubmed-article:11874457 | pubmed:meshHeading | pubmed-meshheading:11874457... | lld:pubmed |
| pubmed-article:11874457 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11874457 | pubmed:articleTitle | Interaction of decorin with CNBr peptides from collagens I and II. Evidence for multiple binding sites and essential lysyl residues in collagen. | lld:pubmed |
| pubmed-article:11874457 | pubmed:affiliation | Dipartimento di Biochimica A. Castellani, University of Pavia, Italy. rtenni@unipv.it | lld:pubmed |
| pubmed-article:11874457 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11874457 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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