Title : Bone morphogenetic protein-1 (BMP-1) mediates C-terminal processing of procollagen V homotrimer.

Pub. Date : 2001 Jul 20

PMID : 11358968






5 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 The latter, which cleaves the C-propeptides of the fibrillar procollagens I-III, is identical to the previously described bone morphogenetic protein-1 (BMP-1). c-propeptides bone morphogenetic protein 1 Homo sapiens
2 The latter, which cleaves the C-propeptides of the fibrillar procollagens I-III, is identical to the previously described bone morphogenetic protein-1 (BMP-1). c-propeptides bone morphogenetic protein 1 Homo sapiens
3 The trimeric C-propeptide fragment, resulting from the furin cleavage, still encompassed the predicted BMP-1 cleavage sites. trimeric c bone morphogenetic protein 1 Homo sapiens
4 The trimeric C-propeptide fragment, resulting from the furin cleavage, still encompassed the predicted BMP-1 cleavage sites. propeptide bone morphogenetic protein 1 Homo sapiens
5 In parallel, the release of the C-propeptide in the culture medium was inhibited by the addition of a specific furin inhibitor, allowing the re-examination of BMP-1 activity on the intact molecule. c-propeptide bone morphogenetic protein 1 Homo sapiens