about
Biglycan is a new extracellular component of the Chordin-BMP4 signaling pathwayGDF11 forms a bone morphogenetic protein 1-activated latent complex that can modulate nerve growth factor-induced differentiation of PC12 cellsMammalian tolloid proteinases: role in growth factor signallingTransforming growth factor-beta induces secretion of activated ADAMTS-2. A procollagen III N-proteinase.Decorin is processed by three isoforms of bone morphogenetic protein-1 (BMP1)Identification and characterization of asporin. a novel member of the leucine-rich repeat protein family closely related to decorin and biglycanBone morphogenetic protein-1 (BMP-1). Identification of the minimal domain structure for procollagen C-proteinase activityMarked differences between metalloproteases meprin A and B in substrate and peptide bond specificityIdentification of amino acid residues in bone morphogenetic protein-1 important for procollagen C-proteinase activityBiosynthetic processing of the pro-alpha 1(V)2pro-alpha 2(V) collagen heterotrimer by bone morphogenetic protein-1 and furin-like proprotein convertasesBone morphogenetic protein-1/Tolloid-like proteinases process dentin matrix protein-1Proteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagenPost-translational modification of bone morphogenetic protein-1 is required for secretion and stability of the proteinProbing the active sites and mechanisms of rat metalloproteases meprin A and BBMP-1-mediated proteolytic processing of alternatively spliced isoforms of collagen type XITsukushi functions as an organizer inducer by inhibition of BMP activity in cooperation with chordin.Bone morphogenetic protein 1 processes prolactin to a 17-kDa antiangiogenic factor.Induced ablation of Bmp1 and Tll1 produces osteogenesis imperfecta in mice.Multiple bone morphogenetic protein 1-related mammalian metalloproteinases process pro-lysyl oxidase at the correct physiological site and control lysyl oxidase activation in mouse embryo fibroblast cultures.Soluble biglycan as a biomarker of inflammatory renal diseases.Low resolution structure determination shows procollagen C-proteinase enhancer to be an elongated multidomain glycoprotein.Procollagen C proteinase enhancer 1 genes are important determinants of the mechanical properties and geometry of bone and the ultrastructure of connective tissues.Biosynthetic processing of the Pro-alpha1(V)Pro-alpha2(V)Pro-alpha3(V) procollagen heterotrimer.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).Proteoglycans in Normal and Healing Skin.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.Inhibition of bone morphogenetic protein 1 by native and altered forms of alpha2-macroglobulin.Activation of latent myostatin by the BMP-1/tolloid family of metalloproteinasesUse of Bmp1/Tll1 doubly homozygous null mice and proteomics to identify and validate in vivo substrates of bone morphogenetic protein 1/tolloid-like metalloproteinasesBone morphogenetic protein-1 processes insulin-like growth factor-binding protein 3Metalloproteinases in Drosophila to humans that are central players in developmental processes.Inhibition of collagen fibril formation.Small leucine-rich proteoglycans orchestrate receptor crosstalk during inflammation.Diverse biological functions of extracellular collagen processing enzymesBiglycan: a multivalent proteoglycan providing structure and signalsCritical amino acids in the active site of meprin metalloproteinases for substrate and peptide bond specificity.Collagen VI deficiency reduces muscle pathology, but does not improve muscle function, in the γ-sarcoglycan-null mouseThe bone morphogenetic protein 1/Tolloid-like metalloproteinasesBiglycan overexpression on tooth enamel formation in transgenic mice.Enhanced biglycan gene expression in the adipose tissues of obese women and its association with obesity-related genes and metabolic parameters.
P2860
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P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Bone morphogenetic protein-1 processes probiglycan.
@ast
Bone morphogenetic protein-1 processes probiglycan.
@en
type
label
Bone morphogenetic protein-1 processes probiglycan.
@ast
Bone morphogenetic protein-1 processes probiglycan.
@en
prefLabel
Bone morphogenetic protein-1 processes probiglycan.
@ast
Bone morphogenetic protein-1 processes probiglycan.
@en
P2093
P2860
P356
P1476
Bone morphogenetic protein-1 processes probiglycan.
@en
P2093
Greenspan DS
Pappano WN
Recklies AD
Roughley PJ
Troedel JM
P2860
P304
30504-30511
P356
10.1074/JBC.M004846200
P407
P577
2000-09-01T00:00:00Z