Transforming growth factor-beta induces secretion of activated ADAMTS-2. A procollagen III N-proteinase (Q27919635)

PubMed

PubMed publication ID

12646579

26 November 2016

title

Transforming growth factor-beta induces secretion of activated ADAMTS-2. A procollagen III N-proteinase (English)

1 reference

PubMed

PubMed publication ID

26 November 2016

0 references

Wei-Man Wang

1

0 references

Seungbok Lee

2

0 references

Mitchell C Brenner

7

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M Leah Allen

6

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Kazuhiko Takahara

8

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Ian C Scott

4

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Daniel S Greenspan

9

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Carter C Lebares

5

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Barry M Steiglitz

Journal of Biological Chemistry

3

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language of work or name

English

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publication date

23 May 2003

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published in

1 reference

Collagens: molecular biology, diseases, and potentials for therapy

PubMed

volume

278

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issue

21

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page(s)

19549-57

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cites work

1 reference

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Mammalian BMP-1/Tolloid-related metalloproteinases, including novel family member mammalian Tolloid-like 2, have differential enzymatic activities and distributions of expression relevant to patterning and skeletogenesis

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The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1

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The astacin family of metalloendopeptidases

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Procollagen peptidase: an enzyme excising the coordination peptides of procollagen

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Purification of human procollagen type III N-proteinase from placenta and preparation of antiserum

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Procollagen type III N-terminal endopeptidase in fibroblast culture

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Human Ehlers-Danlos syndrome type VII C and bovine dermatosparaxis are caused by mutations in the procollagen I N-proteinase gene

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Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains

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Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1

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ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region

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Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins

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Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family

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ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan

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METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity

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Control of organ shape by a secreted metalloprotease in the nematode Caenorhabditis elegans

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Mutations in a member of the ADAMTS gene family cause thrombotic thrombocytopenic purpura

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Properties of the extracellular calcium binding module of the proteoglycan testican

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Bone morphogenetic protein-1 processes probiglycan

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Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 gamma 2 chain

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Proteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagen

21 January 2018

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Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites

21 January 2018

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The proprotein convertases

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M300767200

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

12646579

1 reference

Consolidated OpenCitations Corpus – April 2017