Altered Proteolytic Activities of ADAMTS-4 Expressed by C-terminal Processing (original) (raw)
Activation of the Proteolytic Activity of ADAMTS4 (Aggrecanase-1) by C-terminal Truncation
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Journal of Biological Chemistry, 2002
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ADAMTS4 Cleaves at the Aggrecanase Site (Glu373-Ala374) and Secondarily at the Matrix Metalloproteinase Site (Asn341-Phe342) in the Aggrecan Interglobular Domain
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A Disintegrin and Metalloproteinase with Thrombospondin Motifs-5 (ADAMTS-5) Forms Catalytically Active Oligomers
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ADAMTS-9 in Mouse Cartilage Has Aggrecanase Activity That Is Distinct from ADAMTS-4 and ADAMTS-5
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The Interglobular Domain of Cartilage Aggrecan Is Cleaved by Hemorrhagic Metalloproteinase HT-d (Atrolysin C) at the Matrix Metalloproteinase and Aggrecanase Sites
Jay Fox
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MMPs are less efficient than ADAMTS5 in cleaving aggrecan core protein
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α2-Macroglobulin Is a Novel Substrate for ADAMTS-4 and ADAMTS-5 and Represents an Endogenous Inhibitor of These Enzymes
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Conserved sequence in the aggrecan interglobular domain modulates cleavage by ADAMTS-4 and ADAMTS-5
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Recombinant Human Aggrecan G1-G2 Exhibits Native Binding Properties and Substrate Specificity for Matrix Metalloproteinases and Aggrecanase
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Involvement of ADAMTS5 and hyaluronidase in aggrecan degradation and release from OSM-stimulated cartilage
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Structure analysis reveals the flexibility of the ADAMTS-5 active site
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2011
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Exosite inhibition of A Disintegrin And Metalloproteinase with Thrombospondin motif (ADAMTS)-5 by a glycoconjugated arylsulfonamide
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Induction of aggrecanase 1 (ADAM-TS4) by interleukin-1 occurs through activation of constitutively produced protein
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