ライフサイエンスコーパス: procollagen C-proteinase

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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 were efficiently secreted and exhibited full procollagen C-proteinase activity, but N332Q and N599Q e

8 Pro-lysyl oxidase is processed by procollagen C-proteinase activity, which also removes th

9 oteinases, and mTLL-1 has been shown to have procollagen C-proteinase activity.

10 the physical interactions that occur between procollagen C-proteinases and their substrates.

11 enerate collagen II fibrils by cleavage with procollagen C-proteinase at 37 degrees C.

12 e we demonstrate that ADAMTS-2 can, like the procollagen C-proteinases, be regulated by transforming

13 We showed that the minimal procollagen C-proteinase (BMP-1 lacking the EGF and CUB3

14 role of processing of the NC2 domain by the procollagen C-proteinase/BMP-1 in dimer assembly.

15 ss is promoted by the cleavage of the NC2 by procollagen C-proteinase/BMP1.

16 n and Western blotting studies revealed that procollagen C-proteinases bone morphogenic protein-1 and

17 The Bmp1 gene encodes two procollagen C-proteinases: bone morphogenetic protein 1

18 acid sequences and isolated cDNA clones for procollagen C-proteinase (EC 3.4.24.19), an enzyme that

19 The protein PCOLCE1 (procollagen C proteinase enhancer 1) is not a proteinase

20 The procollagen C-proteinase enhancer (PCPE) is a glycoprote

21 fibrogenic cultures, while expression of the procollagen C-proteinase enhancer (PCPE), a glycoprotein

22 with intact COOH termini are enhanced by the procollagen C-proteinase enhancer 1 (PCOLCE1) and that m

23 protein that has 43% identity to the Type I procollagen C-proteinase enhancer protein (PCOLCE1).

24 e sequences homologous to that of the type I procollagen C-proteinase enhancer protein (PCPE) gene.

25 A novel human Type I procollagen C-proteinase enhancer protein-like gene, PCO

26 teinases, is itself subject to regulation by procollagen C-proteinase enhancer proteins (PCPEs) which

27 hogenic protein-1 and mammalians Tolloid and procollagen C-proteinase enhancer were expressed in MC3T

28 oblasts including procollagen C-proteinases, procollagen C-proteinase enhancer, and lysyl oxidase.

29 by mTLL-2 in the presence of high levels of procollagen C-proteinase enhancer-1 (PCPE-1), for reason

30 rs of the processing activity, and implicate procollagen C-proteinase in this role.

31 The results demonstrate that procollagen C-proteinase is identical to BMP-1.

32 r epidermal growth factor-like domains, have procollagen C-proteinase (pCP) activity and activity for

33 D), two proteinases encoded by Bmp1, provide procollagen C-proteinase (pCP) activity that converts pr

34 nc metalloproteinases, is a highly effective procollagen C-proteinase (PCP) and chordinase.

35 ting vertebrate matrix deposition; it is the procollagen C-proteinase (PCP) that processes procollage

36 Procollagen C proteinases (pCPs) cleave type I to III pr

37 ns prevent formation of stable assemblies of procollagen C-proteinase-processed mutants.

38 collagen maturation in osteoblasts including procollagen C-proteinases, procollagen C-proteinase enha

39 procollagen and potentiates its cleavage by procollagen C-proteinases, such as bone morphogenetic pr

40 f vertebrate extracellular matrix; it is the procollagen C-proteinase that processes the major fibril

41 which the N-propeptides had been removed) to procollagen C-proteinase (which acts by cleaving the C-p

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