| pubmed-article:20025291 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20025291 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:20025291 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:20025291 | lifeskim:mentions | umls-concept:C0009325 | lld:lifeskim |
| pubmed-article:20025291 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:20025291 | lifeskim:mentions | umls-concept:C0486616 | lld:lifeskim |
| pubmed-article:20025291 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:20025291 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:20025291 | lifeskim:mentions | umls-concept:C2348205 | lld:lifeskim |
| pubmed-article:20025291 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:20025291 | pubmed:dateCreated | 2010-2-8 | lld:pubmed |
| pubmed-article:20025291 | pubmed:abstractText | The presence of the (Gly-Xaa-Yaa)(n) open reading frames in different bacteria predicts the existence of an expanded family of collagen-like proteins. To further explore the triple-helix motif and stabilization mechanisms in the absence of hydroxyproline (Hyp), predicted novel collagen-like proteins from Gram-positive and -negative bacteria were expressed in Escherichia coli and characterized. Soluble proteins capable of successful folding and in vitro refolding were observed for collagen proteins from Methylobacterium sp 4-46, Rhodopseudomonas palustris and Solibacter usitatus . In contrast, all protein constructs from Clostridium perfringens were found predominantly in inclusion bodies. However, attachment of a heterologous N-terminal or C-terminal noncollagenous folding domain induced the Clostridium perfringens collagen domain to fold and become soluble. The soluble constructs from different bacteria had typical collagen triple-helical features and showed surprisingly similar thermal stabilities despite diverse amino acid compositions. These collagen-like proteins provide a resource for the development of biomaterials with new properties. | lld:pubmed |
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| pubmed-article:20025291 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20025291 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20025291 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20025291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20025291 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20025291 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:20025291 | pubmed:issn | 1526-4602 | lld:pubmed |
| pubmed-article:20025291 | pubmed:author | pubmed-author:InouyeMasayor... | lld:pubmed |
| pubmed-article:20025291 | pubmed:author | pubmed-author:Mirochnitchen... | lld:pubmed |
| pubmed-article:20025291 | pubmed:author | pubmed-author:BrodskyBarbar... | lld:pubmed |
| pubmed-article:20025291 | pubmed:author | pubmed-author:XuChunyingC | lld:pubmed |
| pubmed-article:20025291 | pubmed:author | pubmed-author:YuZhuoxinZ | lld:pubmed |
| pubmed-article:20025291 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20025291 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:20025291 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:20025291 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20025291 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20025291 | pubmed:pagination | 348-56 | lld:pubmed |
| pubmed-article:20025291 | pubmed:dateRevised | 2011-8-1 | lld:pubmed |
| pubmed-article:20025291 | pubmed:meshHeading | pubmed-meshheading:20025291... | lld:pubmed |
| pubmed-article:20025291 | pubmed:meshHeading | pubmed-meshheading:20025291... | lld:pubmed |
| pubmed-article:20025291 | pubmed:meshHeading | pubmed-meshheading:20025291... | lld:pubmed |
| pubmed-article:20025291 | pubmed:meshHeading | pubmed-meshheading:20025291... | lld:pubmed |
| pubmed-article:20025291 | pubmed:meshHeading | pubmed-meshheading:20025291... | lld:pubmed |
| pubmed-article:20025291 | pubmed:meshHeading | pubmed-meshheading:20025291... | lld:pubmed |
| pubmed-article:20025291 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20025291 | pubmed:articleTitle | Expanding the family of collagen proteins: recombinant bacterial collagens of varying composition form triple-helices of similar stability. | lld:pubmed |
| pubmed-article:20025291 | pubmed:affiliation | Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Piscataway, 08854, USA. | lld:pubmed |
| pubmed-article:20025291 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20025291 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:20025291 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:20025291 | lld:pubmed |
