pubmed-article:8570652 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8570652 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:8570652 | lifeskim:mentions | umls-concept:C0040690 | lld:lifeskim |
pubmed-article:8570652 | lifeskim:mentions | umls-concept:C0681797 | lld:lifeskim |
pubmed-article:8570652 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:8570652 | lifeskim:mentions | umls-concept:C0450363 | lld:lifeskim |
pubmed-article:8570652 | lifeskim:mentions | umls-concept:C1883220 | lld:lifeskim |
pubmed-article:8570652 | lifeskim:mentions | umls-concept:C0599660 | lld:lifeskim |
pubmed-article:8570652 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:8570652 | pubmed:dateCreated | 1996-3-1 | lld:pubmed |
pubmed-article:8570652 | pubmed:abstractText | We report the three-dimensional structure of osteogenic protein 1 (OP-1, also known as bone morphogenetic protein 7) to 2.8-A resolution. OP-1 is a member of the transforming growth factor beta (TGF-beta) superfamily of proteins and is able to induce new bone formation in vivo. Members of this superfamily share sequence similarity in their C-terminal regions and are implicated in embryonic development and adult tissue repair. Our crystal structure makes possible the structural comparison between two members of the TGF-beta superfamily. We find that although there is limited sequence identity between OP-1 and TGF-beta 2, they share a common polypeptide fold. These results establish a basis for proposing the OP-1/TGF-beta 2 fold as the primary structural motif for the TGF-beta superfamily as a whole. Detailed comparison of the OP-1 and TGF-beta 2 structures has revealed striking differences that provide insights into how these growth factors interact with their receptors. | lld:pubmed |
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pubmed-article:8570652 | pubmed:language | eng | lld:pubmed |
pubmed-article:8570652 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8570652 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8570652 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8570652 | pubmed:month | Jan | lld:pubmed |
pubmed-article:8570652 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:8570652 | pubmed:author | pubmed-author:RuegerD CDC | lld:pubmed |
pubmed-article:8570652 | pubmed:author | pubmed-author:GriffithD LDL | lld:pubmed |
pubmed-article:8570652 | pubmed:author | pubmed-author:SampathT KTK | lld:pubmed |
pubmed-article:8570652 | pubmed:author | pubmed-author:CarlsonW DWD | lld:pubmed |
pubmed-article:8570652 | pubmed:author | pubmed-author:KeckP CPC | lld:pubmed |
pubmed-article:8570652 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8570652 | pubmed:day | 23 | lld:pubmed |
pubmed-article:8570652 | pubmed:volume | 93 | lld:pubmed |
pubmed-article:8570652 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8570652 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8570652 | pubmed:pagination | 878-83 | lld:pubmed |
pubmed-article:8570652 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
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pubmed-article:8570652 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8570652 | pubmed:articleTitle | Three-dimensional structure of recombinant human osteogenic protein 1: structural paradigm for the transforming growth factor beta superfamily. | lld:pubmed |
pubmed-article:8570652 | pubmed:affiliation | Rosenstiel Basic Medical Research Center, Brandeis University, Waltham, MA 02254, USA. | lld:pubmed |
pubmed-article:8570652 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8570652 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:8570652 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:655 | entrezgene:pubmed | pubmed-article:8570652 | lld:entrezgene |
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