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).
about
Decorin is processed by three isoforms of bone morphogenetic protein-1 (BMP1)Enzymatic regulation of pattern: BMP4 binds CUB domains of Tolloids and inhibits proteinase activity.Role of the netrin-like domain of procollagen C-proteinase enhancer-1 in the control of metalloproteinase activity.First evidence of bone morphogenetic protein 1 expression and activity in sheep ovarian follicles.Procollagen C proteinase enhancer 1 genes are important determinants of the mechanical properties and geometry of bone and the ultrastructure of connective tissues.Mammalian tolloid-like 1 binds procollagen C-proteinase enhancer protein 1 and differs from bone morphogenetic protein 1 in the functional roles of homologous protein domains.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.Metalloproteinases in Drosophila to humans that are central players in developmental processes.Procollagen C-proteinase enhancer grasps the stalk of the C-propeptide trimer to boost collagen precursor maturation.The bone morphogenetic protein 1/Tolloid-like metalloproteinasesMechanical injury and cytokines cause loss of cartilage integrity and upregulate proteins associated with catabolism, immunity, inflammation, and repairBone morphogenetic protein 1 is expressed in porcine ovarian follicles and promotes oocyte maturation and early embryonic development.Diversity between mammalian tolloid proteinases: Oligomerisation and non-catalytic domains influence activity and specificity.Fell Muir Lecture: Collagen fibril formation in vitro and in vivo.Procollagen C-proteinase enhancer stimulates procollagen processing by binding to the C-propeptide region only.Structural and functional evidence for a substrate exclusion mechanism in mammalian tolloid like-1 (TLL-1) proteinase.The protease domain of procollagen C-proteinase (BMP1) lacks substrate selectivity, which is conferred by non-proteolytic domains.Dentin sialophosphoprotein (DSPP) is cleaved into its two natural dentin matrix products by three isoforms of bone morphogenetic protein-1 (BMP1).A complete domain structure of Drosophila tolloid is required for cleavage of short gastrulation.Sizzled is unique among secreted frizzled-related proteins for its ability to specifically inhibit bone morphogenetic protein-1 (BMP-1)/tolloid-like proteinases.Molecular determinants of Xolloid action in vivo.
P2860
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P2860
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).
description
2005 nî lūn-bûn
@nan
2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Identification of the minimal ...... roteinase enhancer-1 (PCPE-1).
@ast
Identification of the minimal ...... roteinase enhancer-1 (PCPE-1).
@en
Identification of the minimal domain structure of bone morphogenetic protein-1
@nl
type
label
Identification of the minimal ...... roteinase enhancer-1 (PCPE-1).
@ast
Identification of the minimal ...... roteinase enhancer-1 (PCPE-1).
@en
Identification of the minimal domain structure of bone morphogenetic protein-1
@nl
prefLabel
Identification of the minimal ...... roteinase enhancer-1 (PCPE-1).
@ast
Identification of the minimal ...... roteinase enhancer-1 (PCPE-1).
@en
Identification of the minimal domain structure of bone morphogenetic protein-1
@nl
P2860
P356
P1476
Identification of the minimal ...... roteinase enhancer-1 (PCPE-1).
@en
P2093
Vasiliki Petropoulou
P2860
P304
22616-22623
P356
10.1074/JBC.M413468200
P407
P577
2005-04-07T00:00:00Z