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1 etic protein-1 (BMP-1), also known as type I procollagen C-proteinase ().
2 romoted by the cleavage of the NC2 domain by procollagen C-proteinase.
3 o capable of competing for such binding with procollagen C-proteinases.
4                                              Procollagen C-proteinase-2 (pCP-2, mTld) is derived from
5 o as measured by a fluorogenic peptide based procollagen C-proteinase activity assay.
6 x in vertebrates, including provision of the procollagen C-proteinase activity that processes the maj
7 further show that the enzyme responsible for procollagen C-proteinase activity, bone morphogenetic pr
8 were efficiently secreted and exhibited full procollagen C-proteinase activity, but N332Q and N599Q e
9            Pro-lysyl oxidase is processed by procollagen C-proteinase activity, which also removes th
10 oteinases, and mTLL-1 has been shown to have procollagen C-proteinase activity.
11 ly uncleaved in PDAC ECM, suggesting reduced procollagen C-proteinase activity.
12 the physical interactions that occur between procollagen C-proteinases and their substrates.
13 enerate collagen II fibrils by cleavage with procollagen C-proteinase at 37 degrees C.
14 e we demonstrate that ADAMTS-2 can, like the procollagen C-proteinases, be regulated by transforming
15                   We showed that the minimal procollagen C-proteinase (BMP-1 lacking the EGF and CUB3
16  role of processing of the NC2 domain by the procollagen C-proteinase/BMP-1 in dimer assembly.
17 ss is promoted by the cleavage of the NC2 by procollagen C-proteinase/BMP1.
18 n and Western blotting studies revealed that procollagen C-proteinases bone morphogenic protein-1 and
19                    The Bmp1 gene encodes two procollagen C-proteinases: bone morphogenetic protein 1
20  acid sequences and isolated cDNA clones for procollagen C-proteinase (EC 3.4.24.19), an enzyme that
21                         The protein PCOLCE1 (procollagen C proteinase enhancer 1) is not a proteinase
22                                          The procollagen C-proteinase enhancer (PCPE) is a glycoprote
23 fibrogenic cultures, while expression of the procollagen C-proteinase enhancer (PCPE), a glycoprotein
24 with intact COOH termini are enhanced by the procollagen C-proteinase enhancer 1 (PCOLCE1) and that m
25  protein that has 43% identity to the Type I procollagen C-proteinase enhancer protein (PCOLCE1).
26 e sequences homologous to that of the type I procollagen C-proteinase enhancer protein (PCPE) gene.
27                         A novel human Type I procollagen C-proteinase enhancer protein-like gene, PCO
28 teinases, is itself subject to regulation by procollagen C-proteinase enhancer proteins (PCPEs) which
29 hogenic protein-1 and mammalians Tolloid and procollagen C-proteinase enhancer were expressed in MC3T
30 oblasts including procollagen C-proteinases, procollagen C-proteinase enhancer, and lysyl oxidase.
31  by mTLL-2 in the presence of high levels of procollagen C-proteinase enhancer-1 (PCPE-1), for reason
32 as supported by the reduction of galectin-3, procollagen C-proteinase enhancer-1, and endothelin-1 ex
33 rs of the processing activity, and implicate procollagen C-proteinase in this role.
34                 The results demonstrate that procollagen C-proteinase is identical to BMP-1.
35 r epidermal growth factor-like domains, have procollagen C-proteinase (pCP) activity and activity for
36 D), two proteinases encoded by Bmp1, provide procollagen C-proteinase (pCP) activity that converts pr
37 nc metalloproteinases, is a highly effective procollagen C-proteinase (PCP) and chordinase.
38 ting vertebrate matrix deposition; it is the procollagen C-proteinase (PCP) that processes procollage
39                                              Procollagen C proteinases (pCPs) cleave type I to III pr
40 ns prevent formation of stable assemblies of procollagen C-proteinase-processed mutants.
41 collagen maturation in osteoblasts including procollagen C-proteinases, procollagen C-proteinase enha
42  procollagen and potentiates its cleavage by procollagen C-proteinases, such as bone morphogenetic pr
43 f vertebrate extracellular matrix; it is the procollagen C-proteinase that processes the major fibril
44 which the N-propeptides had been removed) to procollagen C-proteinase (which acts by cleaving the C-p