Folding and activity of recombinant human procollagen C-proteinase enhancer.
about
PCOLCE2 encodes a functional procollagen C-proteinase enhancer (PCPE2) that is a collagen-binding protein differing in distribution of expression and post-translational modification from the previously described PCPE1Extended interaction network of procollagen C-proteinase enhancer-1 in the extracellular matrixBiophysical characterization of the C-propeptide trimer from human procollagen III reveals a tri-lobed structure.Role of the netrin-like domain of procollagen C-proteinase enhancer-1 in the control of metalloproteinase activity.Interaction properties of the procollagen C-proteinase enhancer protein shed light on the mechanism of stimulation of BMP-1.Low resolution structure determination shows procollagen C-proteinase enhancer to be an elongated multidomain glycoprotein.Identification of the minimal domain structure of bone morphogenetic protein-1 (BMP-1) for chordinase activity: chordinase activity is not enhanced by procollagen C-proteinase enhancer-1 (PCPE-1).Insights into how CUB domains can exert specific functions while sharing a common fold: conserved and specific features of the CUB1 domain contribute to the molecular basis of procollagen C-proteinase enhancer-1 activity.Circulating bone morphogenetic protein 1-3 isoform increases renal fibrosisLoss of fibulin-4 disrupts collagen synthesis and maturation: implications for pathology resulting from EFEMP2 mutationsProcollagen C-proteinase enhancer grasps the stalk of the C-propeptide trimer to boost collagen precursor maturation.Procollagen C-proteinase enhancer stimulates procollagen processing by binding to the C-propeptide region only.Binding of procollagen C-proteinase enhancer-1 (PCPE-1) to heparin/heparan sulfate: properties and role in PCPE-1 interaction with cells.Dentin sialophosphoprotein (DSPP) is cleaved into its two natural dentin matrix products by three isoforms of bone morphogenetic protein-1 (BMP1).Substrate-specific modulation of a multisubstrate proteinase. C-terminal processing of fibrillar procollagens is the only BMP-1-dependent activity to be enhanced by PCPE-1.Data comparing the plasma levels of procollagen C-proteinase enhancer 1 (PCPE-1) in healthy individuals and liver fibrosis patients.Enzymatic cleavage specificity of the proalpha1(V) chain processing analysed by site-directed mutagenesis.Lysyl oxidase-like protein from bovine aorta. Isolation and maturation to an active form by bone morphogenetic protein-1.GLUT1 is highly expressed in cementoblasts but not in osteoblasts.Identification of binding partners interacting with the α1-N-propeptide of type V collagen.
P2860
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P2860
Folding and activity of recombinant human procollagen C-proteinase enhancer.
description
2001 nî lūn-bûn
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2001年の論文
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2001年論文
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2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
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2001年論文
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2001年论文
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name
Folding and activity of recombinant human procollagen C-proteinase enhancer.
@en
type
label
Folding and activity of recombinant human procollagen C-proteinase enhancer.
@en
prefLabel
Folding and activity of recombinant human procollagen C-proteinase enhancer.
@en
P2093
P2860
P1433
P1476
Folding and activity of recombinant human procollagen C-proteinase enhancer
@en
P2093
D Eichenberger
L Moschcovich
S Bernocco
P2860
P304
P356
10.1046/J.1432-1327.2001.02189.X
P407
P577
2001-05-01T00:00:00Z