pubmed-article:17255107 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17255107 | lifeskim:mentions | umls-concept:C0527443 | lld:lifeskim |
pubmed-article:17255107 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
pubmed-article:17255107 | lifeskim:mentions | umls-concept:C0377148 | lld:lifeskim |
pubmed-article:17255107 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
pubmed-article:17255107 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
pubmed-article:17255107 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:17255107 | pubmed:issue | 12 | lld:pubmed |
pubmed-article:17255107 | pubmed:dateCreated | 2007-3-19 | lld:pubmed |
pubmed-article:17255107 | pubmed:abstractText | Highly purified fractions of bone extracts capable of inducing ectopic bone formation have been reported to contain peptides corresponding to the mature active regions of the TGF-beta-like bone morphogenetic proteins (BMPs) 2-7, and to the prodomain region of the metalloproteinase BMP1. Co-purification of BMPs 2-7 with BMP1 prodomain sequences through the multiple biochemical steps used in these previous reports has suggested the possibility of interactions between the BMP1 prodomain and BMPs 2-7. Here we demonstrate that the BMP1 prodomain binds BMPs 2 and 4 with high specificity and with a KD of approximately 11 nM, in the physiological range. It is further demonstrated that the BMP1 prodomain is capable of modulating signaling by BMPs 2 and 4 in vitro and in vivo, and that endogenous BMP1 prodomain-BMP4 complexes exist in cell culture media and in tissues. | lld:pubmed |
pubmed-article:17255107 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17255107 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17255107 | pubmed:language | eng | lld:pubmed |
pubmed-article:17255107 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17255107 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17255107 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17255107 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17255107 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17255107 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17255107 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17255107 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17255107 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17255107 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17255107 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17255107 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17255107 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17255107 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17255107 | pubmed:month | Mar | lld:pubmed |
pubmed-article:17255107 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:17255107 | pubmed:author | pubmed-author:GreenspanDani... | lld:pubmed |
pubmed-article:17255107 | pubmed:author | pubmed-author:GeGaoxiangG | lld:pubmed |
pubmed-article:17255107 | pubmed:author | pubmed-author:PelegriFranci... | lld:pubmed |
pubmed-article:17255107 | pubmed:author | pubmed-author:JasujaReemaR | lld:pubmed |
pubmed-article:17255107 | pubmed:author | pubmed-author:Lyman-Gingeri... | lld:pubmed |
pubmed-article:17255107 | pubmed:author | pubmed-author:VossNikolas... | lld:pubmed |
pubmed-article:17255107 | pubmed:author | pubmed-author:BranamAmanda... | lld:pubmed |
pubmed-article:17255107 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17255107 | pubmed:day | 23 | lld:pubmed |
pubmed-article:17255107 | pubmed:volume | 282 | lld:pubmed |
pubmed-article:17255107 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17255107 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17255107 | pubmed:pagination | 9053-62 | lld:pubmed |
pubmed-article:17255107 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:17255107 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17255107 | pubmed:articleTitle | Bone morphogenetic protein 1 prodomain specifically binds and regulates signaling by bone morphogenetic proteins 2 and 4. | lld:pubmed |
pubmed-article:17255107 | pubmed:affiliation | Program in Molecular and Cellular Pharmacology, University of Wisconsin, Madison, Wisconsin 53706, USA. | lld:pubmed |
pubmed-article:17255107 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17255107 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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