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

Paul Gottschall

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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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 on Syndecan-1

John Sandy

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A Disintegrin and Metalloproteinase with Thrombospondin Motifs-5 (ADAMTS-5) Forms Catalytically Active Oligomers

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ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro

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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

Peter Roughley

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ADAMTS-4 (aggrecanase-1): N-Terminal activation mechanisms

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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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Biochimica et Biophysica Acta (BBA) - General Subjects, 2009

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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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N-Glycans of ADAMTS13 modulate its secretion and von Willebrand factor cleaving activity

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Domains and Maturation Processes That Regulate the Activity of ADAMTS-2, a Metalloproteinase Cleaving the Aminopropeptide of Fibrillar Procollagens Types I-III and V

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Involvement of ADAMTS5 and hyaluronidase in aggrecan degradation and release from OSM-stimulated cartilage

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Proteoglycan degradation by the ADAMTS family of proteinases

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Substrate Conformation Modulates Aggrecanase (ADAMTS-4) Affinity and Sequence Specificity: SUGGESTION OF A COMMON TOPOLOGICAL SPECIFICITY FOR FUNCTIONALLY DIVERSE PROTEASES

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Expression and activity of ADAMTS-5 in synovium

Ingunn Holen

European Journal of Biochemistry, 2001

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Karena Last

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ADAMTS5-mediated aggrecanolysis in murine epiphyseal chondrocyte cultures

Matthew Stewart

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Aggrecanase: A Target for the Design of Inhibitors of Cartilage Degradation

Robert Newton

Annals of the New York Academy of Sciences, 1999

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Identification of substrates of the extracellular protease ADAMTS1 by DIGE proteomic analysis

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Aggrecanase versus matrix metalloproteinases in the catabolism of the interglobular domain of aggrecan in vitro

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ADAMTS-7: a metalloproteinase that directly binds to and degrades cartilage oligomeric matrix protein

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Structure–function and regulation of ADAMTS‐13 protease

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Biosynthesis and Expression of a Disintegrin-like and Metalloproteinase Domain with Thrombospondin-1 Repeats-15: A NOVEL VERSICAN-CLEAVING PROTEOGLYCANASE

Daniel McCulloch

Journal of Biological Chemistry, 2013

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Structure analysis reveals the flexibility of the ADAMTS-5 active site

James Kiefer

2011

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Exosite inhibition of A Disintegrin And Metalloproteinase with Thrombospondin motif (ADAMTS)-5 by a glycoconjugated arylsulfonamide

Elisa Nuti

2020

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Induction of aggrecanase 1 (ADAM-TS4) by interleukin-1 occurs through activation of constitutively produced protein

Peggy Scherle

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Reactive-site mutants of N-TIMP-3 that selectively inhibit ADAMTS-4 and ADAMTS-5: biological and structural implications

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