Procollagen N-proteinase and procollagen C-proteinase. Two unusual metalloproteinases that are essential for procollagen processing probably have important roles in development and cell signaling.
about
ADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and functionAdipocyte extracellular matrix composition, dynamics and role in obesityLARP6 Meets Collagen mRNA: Specific Regulation of Type I Collagen ExpressionBiochemical and structural characterization of neocartilage formed by mesenchymal stem cells in alginate hydrogelsIn Vitro Bone Cell Models: Impact of Fluid Shear Stress on Bone FormationCloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3Proteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagenTransgenic mice with inactive alleles for procollagen N-proteinase (ADAMTS-2) develop fragile skin and male sterilityThe NH2-terminal propeptide of type I procollagen acts intracellularly to modulate cell functionBMP-1-mediated proteolytic processing of alternatively spliced isoforms of collagen type XIMutational and structural characteristics of four novel heterozygous C-propeptide mutations in the proα1(I) collagen gene in Chinese osteogenesis imperfecta patients.Distinct maturations of N-propeptide domains in fibrillar procollagen molecules involved in the formation of heterotypic fibrils in adult sea urchin collagenous tissues.Biophysical characterization of the C-propeptide trimer from human procollagen III reveals a tri-lobed structure.A Marfan syndrome gene expression phenotype in cultured skin fibroblasts.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.Type IIB procollagen NH(2)-propeptide induces death of tumor cells via interaction with integrins alpha(V)beta(3) and alpha(V)beta(5).Laminins: structure and genetic regulation.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.Growth factors secreted by fibroblasts: role in healing diabetic foot ulcers.Collagens and collagen-related diseases.Recent advances in the use of serological bone formation markers to monitor callus development and fracture healingDiverse biological functions of extracellular collagen processing enzymesType IIA procollagen containing the cysteine-rich amino propeptide is deposited in the extracellular matrix of prechondrogenic tissue and binds to TGF-beta1 and BMP-2.Collagen I and the fibroblast: high protein expression requires a new paradigm of post-transcriptional, feedback regulation.Comparison of Gene Expression Profiles between Keratinocytes, Melanocytes and Fibroblasts.Zinc in wound healing: theoretical, experimental, and clinical aspects.Absence of the ER Cation Channel TMEM38B/TRIC-B Disrupts Intracellular Calcium Homeostasis and Dysregulates Collagen Synthesis in Recessive Osteogenesis Imperfecta.Lysyl oxidase: a potential target for cancer therapy.Dentin: structure, composition and mineralizationThe extracellular matrix of the dermis: flexible structures with dynamic functions.Antiangiogenic and anticancer molecules in cartilage.Molecular cloning of type I collagen cDNA and nutritional regulation of type I collagen mRNA expression in grass carp.A novel subcellular collagen organization process visualized by total internal reflection fluorescence microscopy.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.Bone morphogenetic protein-1 (BMP-1) mediates C-terminal processing of procollagen V homotrimer.Folding and activity of recombinant human procollagen C-proteinase enhancer.Ascorbic acid promotes a TGFβ1-induced myofibroblast phenotype switchAdhesion of Lactobacilli and their anti-infectivity potential.Enzymatic cleavage specificity of the proalpha1(V) chain processing analysed by site-directed mutagenesis.
P2860
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P2860
Procollagen N-proteinase and procollagen C-proteinase. Two unusual metalloproteinases that are essential for procollagen processing probably have important roles in development and cell signaling.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Procollagen N-proteinase and p ...... evelopment and cell signaling.
@en
type
label
Procollagen N-proteinase and p ...... evelopment and cell signaling.
@en
prefLabel
Procollagen N-proteinase and p ...... evelopment and cell signaling.
@en
P2093
P1433
P1476
Procollagen N-proteinase and p ...... evelopment and cell signaling.
@en
P2093
P304
P356
10.1016/S0945-053X(98)90013-0
P577
1998-02-01T00:00:00Z