| pubmed-article:15788652 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15788652 | lifeskim:mentions | umls-concept:C0033235 | lld:lifeskim |
| pubmed-article:15788652 | lifeskim:mentions | umls-concept:C0599896 | lld:lifeskim |
| pubmed-article:15788652 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:15788652 | pubmed:issue | Pt 7 | lld:pubmed |
| pubmed-article:15788652 | pubmed:dateCreated | 2005-3-24 | lld:pubmed |
| pubmed-article:15788652 | pubmed:abstractText | Collagen fibrils in the extracellular matrix allow connective tissues such as tendon, skin and bone to withstand tensile forces. The fibrils are indeterminate in length, insoluble and form elaborate three-dimensional arrays that extend over numerous cell lengths. Studies of the molecular basis of collagen fibrillogenesis have provided insight into the trafficking of procollagen (the precursor of collagen) through the cellular secretory pathway, the conversion of procollagen to collagen by the procollagen metalloproteinases, and the directional deposition of fibrils involving the plasma membrane and late secretory pathway. Fibril-associated molecules are targeted to the surface of collagen fibrils, and these molecules play an important role in regulating the diameter and interactions between the fibrils. | lld:pubmed |
| pubmed-article:15788652 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15788652 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15788652 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15788652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15788652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15788652 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15788652 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:15788652 | pubmed:issn | 0021-9533 | lld:pubmed |
| pubmed-article:15788652 | pubmed:author | pubmed-author:KadlerKarl... | lld:pubmed |
| pubmed-article:15788652 | pubmed:author | pubmed-author:CantyElizabet... | lld:pubmed |
| pubmed-article:15788652 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15788652 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:15788652 | pubmed:volume | 118 | lld:pubmed |
| pubmed-article:15788652 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15788652 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15788652 | pubmed:pagination | 1341-53 | lld:pubmed |
| pubmed-article:15788652 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:15788652 | pubmed:meshHeading | pubmed-meshheading:15788652... | lld:pubmed |
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| pubmed-article:15788652 | pubmed:meshHeading | pubmed-meshheading:15788652... | lld:pubmed |
| pubmed-article:15788652 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15788652 | pubmed:articleTitle | Procollagen trafficking, processing and fibrillogenesis. | lld:pubmed |
| pubmed-article:15788652 | pubmed:affiliation | Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, The University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, UK. elizabeth.g.canty@manchester.ac.uk | lld:pubmed |
| pubmed-article:15788652 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15788652 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:15788652 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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