| pubmed-article:20736794 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20736794 | lifeskim:mentions | umls-concept:C0016658 | lld:lifeskim |
| pubmed-article:20736794 | lifeskim:mentions | umls-concept:C0040300 | lld:lifeskim |
| pubmed-article:20736794 | lifeskim:mentions | umls-concept:C0262950 | lld:lifeskim |
| pubmed-article:20736794 | lifeskim:mentions | umls-concept:C0205242 | lld:lifeskim |
| pubmed-article:20736794 | lifeskim:mentions | umls-concept:C0623362 | lld:lifeskim |
| pubmed-article:20736794 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
| pubmed-article:20736794 | lifeskim:mentions | umls-concept:C0333959 | lld:lifeskim |
| pubmed-article:20736794 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:20736794 | lifeskim:mentions | umls-concept:C0205250 | lld:lifeskim |
| pubmed-article:20736794 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:20736794 | pubmed:dateCreated | 2010-8-25 | lld:pubmed |
| pubmed-article:20736794 | pubmed:abstractText | A delayed union or a nonunion of a fracture is a potentially adverse complication. Understanding the mechanisms of nonunion development may lead to improved treatment modalities. Proteases such as the matrix metalloproteinases play important roles in bone remodeling and repair, in which an imbalance or a nonfunctioning enzyme may lead to defects in bone healing (nonunion). The purpose of this pilot study was twofold: first to define an mRNA expression profile of all the matrix metalloproteinases (MMPs), a disintegrin and metalloproteinases with thrombospondin motif (ADAMTS) enzymes, and their inhibitors (TIMPs) within fracture nonunion tissue, and second to compare this profile with mineralized fracture callus. | lld:pubmed |
| pubmed-article:20736794 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20736794 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20736794 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20736794 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20736794 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20736794 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20736794 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20736794 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20736794 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:20736794 | pubmed:issn | 1531-2291 | lld:pubmed |
| pubmed-article:20736794 | pubmed:author | pubmed-author:EgolKenneth... | lld:pubmed |
| pubmed-article:20736794 | pubmed:author | pubmed-author:LiuChuan-JuCJ | lld:pubmed |
| pubmed-article:20736794 | pubmed:author | pubmed-author:FajardoMarcM | lld:pubmed |
| pubmed-article:20736794 | pubmed:author | pubmed-author:IlalovKirillK | lld:pubmed |
| pubmed-article:20736794 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20736794 | pubmed:volume | 24 | lld:pubmed |
| pubmed-article:20736794 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20736794 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20736794 | pubmed:pagination | 557-63 | lld:pubmed |
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| pubmed-article:20736794 | pubmed:meshHeading | pubmed-meshheading:20736794... | lld:pubmed |
| pubmed-article:20736794 | pubmed:meshHeading | pubmed-meshheading:20736794... | lld:pubmed |
| pubmed-article:20736794 | pubmed:meshHeading | pubmed-meshheading:20736794... | lld:pubmed |
| pubmed-article:20736794 | pubmed:meshHeading | pubmed-meshheading:20736794... | lld:pubmed |
| pubmed-article:20736794 | pubmed:meshHeading | pubmed-meshheading:20736794... | lld:pubmed |
| pubmed-article:20736794 | pubmed:meshHeading | pubmed-meshheading:20736794... | lld:pubmed |
| pubmed-article:20736794 | pubmed:meshHeading | pubmed-meshheading:20736794... | lld:pubmed |
| pubmed-article:20736794 | pubmed:meshHeading | pubmed-meshheading:20736794... | lld:pubmed |
| pubmed-article:20736794 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20736794 | pubmed:articleTitle | Matrix metalloproteinases that associate with and cleave bone morphogenetic protein-2 in vitro are elevated in hypertrophic fracture nonunion tissue. | lld:pubmed |
| pubmed-article:20736794 | pubmed:affiliation | Musculoskeletal Research Institute and The Bone Healing Center, New York University Hospital for Joint Diseases, New York, NY 10003, USA. | lld:pubmed |
| pubmed-article:20736794 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20736794 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20736794 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20736794 | lld:entrezgene |
