Discovery and characterization of a novel, widely expressed metalloprotease, ADAMTS10, and its proteolytic activation (Q28280996)

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Language	Label	Description	Also known as
English	Discovery and characterization of a novel, widely expressed metalloprotease, ADAMTS10, and its proteolytic activation	scientific article

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scholarly article

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Discovery and characterization of a novel, widely expressed metalloprotease, ADAMTS10, and its proteolytic activation (English)

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author name string

Robert P T Somerville

1

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Katherine A Jungers

2

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Suneel S Apte

3

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language of work or name

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publication date

3 December 2004

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Journal of Biological Chemistry

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279

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49

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51208-17

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cDNA 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.

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

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

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A defect in a novel ADAMTS family member is the cause of the belted white-spotting mutation.

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

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Brain-enriched hyaluronan binding (BEHAB)/brevican cleavage in a glioma cell line is mediated by a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) family member

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Versican V1 proteolysis in human aorta in vivo occurs at the Glu441-Ala442 bond, a site that is cleaved by recombinant ADAMTS-1 and ADAMTS-4

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

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Structure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpura

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Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3

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Activation of the proteolytic activity of ADAMTS4 (aggrecanase-1) by C-terminal truncation

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

1 reference

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ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors

1 reference

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ADAMTS7B, the full-length product of the ADAMTS7 gene, is a chondroitin sulfate proteoglycan containing a mucin domain

1 reference

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A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family

1 reference

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ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS family

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ADAM-TS8, a novel metalloprotease of the ADAM-TS family located on mouse chromosome 9 and human chromosome 11

1 reference

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Sites of aggrecan cleavage by recombinant human aggrecanase-1 (ADAMTS-4)

1 reference

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The scanning model for translation: an update

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The signal peptide

1 reference

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Proprotein convertase furin interacts with and cleaves pro-ADAMTS4 (Aggrecanase-1) in the trans-Golgi network

1 reference

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Expression of lacunin, a large multidomain extracellular matrix protein, accompanies morphogenesis of epithelial monolayers in Manduca sexta

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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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Alpha2-macroglobulin is a novel substrate for ADAMTS-4 and ADAMTS-5 and represents an endogenous inhibitor of these enzymes

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The crystal structure of the proprotein processing proteinase furin explains its stringent specificity

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Subtilase-like pro-protein convertases: from molecular specificity to therapeutic applications

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Characterization of METH-1/ADAMTS1 processing reveals two distinct active forms

1 reference

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ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate

1 reference

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Altered proteolytic activities of ADAMTS-4 expressed by C-terminal processing

1 reference

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Identifiers

10.1074/JBC.M409036200

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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