Procollagen peptidase: an enzyme excising the coordination peptides of procollagen
about
Human Ehlers-Danlos syndrome type VII C and bovine dermatosparaxis are caused by mutations in the procollagen I N-proteinase geneADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS familyProcollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxisTransforming growth factor-beta induces secretion of activated ADAMTS-2. A procollagen III N-proteinase.Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3Fulvic acid supplementation and selenium deficiency disturb the structural integrity of mouse skeletal tissue. An animal model to study the molecular defects of Kashin-Beck diseaseTransgenic mice with inactive alleles for procollagen N-proteinase (ADAMTS-2) develop fragile skin and male sterilityEhlers-Danlos syndrome has varied molecular mechanisms.Inhibition of collagen secretion from bone and cultured fibroblasts by microtubular disruptive drugsIn vitro synthesis of procollagen on polysomes.Identification of a disulfide-linked procollagen as the biosynthetic precursor of chick-bone collagen.Genetics of the connective tissue proteins: assignment of the gene for human type I procollagen to chromosome 17 by analysis of cell hybrids and microcell hybridsSkin malformations in a neonatal foal tested homozygous positive for Warmblood Fragile Foal SyndromeCell-free synthesis of procollagen: L-929 fibroblasts as a cellular model for dermatosparaxis.Collagen and procollagen production by a clonal line of Schwann cellsHuman dermatosparaxis: a form of Ehlers-Danlos syndrome that results from failure to remove the amino-terminal propeptide of type I procollagen.The genetic and molecular bases of monogenic disorders affecting proteolytic systems.Phenotypic diversity of human diseases resulting from allelic series.Kniest dysplasia is characterized by an apparent abnormal processing of the C-propeptide of type II cartilage collagen resulting in imperfect fibril assemblycDNA cloning and expression of bovine procollagen I N-proteinase: a new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components.Role of collagenous matrices in the adhesion and growth of cellsAssembly of cartilage collagen fibrils is disrupted by overexpression of normal type II collagen in transgenic mice.Collagen biosynthesis.Acquired and heritable defects in collagen synthesis and fibrogenesis.Emerging Roles of ADAMTSs in Angiogenesis and Cancer.Calf tendon procollagen peptidase: its purification and endopeptidase mode of actionIdentification and partial characterization of the secreted form of the fourth component of human complement: evidence that it is different from major plasma form.Connective tissue diseases in the skin--from molecules to symptoms.Fibrous proteins: At the crossroads of genetic engineering and biotechnological applications.Molecular and clinical aspects of connective tissue.Isolation and characterization of collagen-synthesizing polysomes from chick embryos.Homeostasis in extracellular tissues: insights from studies on collagen.Structure of cultured fibroblasts from dermatosparaxic calves.Collagen metabolism: a comparison of diseases of collagen and diseases affecting collagen.Low rate of procollagen conversion in dermatosparactic sheep fibroblasts is paralleled by increased synthesis of type I and type III collagens.Procollagen alpha 2(I) mRNA in dermatosparactic fibroblasts: evidence for post-transcriptional regulation.A defective cell surface collagen-binding protein in dermatosparactic sheep fibroblasts.Heterogeneity in dermatosparaxis is shown by contraction of collagen gels.Influence of ascorbic acid on ribosomal patterns and collagen biosynthesis in healing wounds of scorbutic guinea pigs.Procollagen type III N-terminal endopeptidase in fibroblast culture.
P2860
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P2860
Procollagen peptidase: an enzyme excising the coordination peptides of procollagen
description
1971 nî lūn-bûn
@nan
1971 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1971 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1971年の論文
@ja
1971年論文
@yue
1971年論文
@zh-hant
1971年論文
@zh-hk
1971年論文
@zh-mo
1971年論文
@zh-tw
1971年论文
@wuu
name
Procollagen peptidase: an enzyme excising the coordination peptides of procollagen
@ast
Procollagen peptidase: an enzyme excising the coordination peptides of procollagen
@en
Procollagen peptidase: an enzyme excising the coordination peptides of procollagen
@nl
type
label
Procollagen peptidase: an enzyme excising the coordination peptides of procollagen
@ast
Procollagen peptidase: an enzyme excising the coordination peptides of procollagen
@en
Procollagen peptidase: an enzyme excising the coordination peptides of procollagen
@nl
prefLabel
Procollagen peptidase: an enzyme excising the coordination peptides of procollagen
@ast
Procollagen peptidase: an enzyme excising the coordination peptides of procollagen
@en
Procollagen peptidase: an enzyme excising the coordination peptides of procollagen
@nl
P2093
P2860
P356
P1476
Procollagen peptidase: an enzyme excising the coordination peptides of procollagen
@en
P2093
P2860
P304
P356
10.1073/PNAS.68.12.3054
P407
P577
1971-12-01T00:00:00Z