Sites of aggrecan cleavage by recombinant human aggrecanase-1 (ADAMTS-4) (Q22253473)

28 March 2023

M Pratta

Pratta

1 reference

28 March 2023

R Q Liu

R Q

Liu

1 reference

28 March 2023

J Austin

Austin

1 reference

28 March 2023

O H Ross

O H

Ross

1 reference

28 March 2023

I Abbaszade

Abbaszade

1 reference

28 March 2023

T Burn

Burn

1 reference

28 March 2023

E Arner

Arner

1 reference

Journal of Biological Chemistry

28 March 2023

language of work or name

English

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publication date

16 June 2000

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published in

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volume

275

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issue

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page(s)

18566-73

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cites work

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M909383199

Extended and globular protein domains in cartilage proteoglycans

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M909383199

Fibroblast and neutrophil collagenases cleave at two sites in the cartilage aggrecan interglobular domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M909383199

N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1-treated articular-cartilage cultures. Putative site(s) of enzymic cleavage

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M909383199

Mechanism of catabolism of aggrecan by articular cartilage

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M909383199

Cell-mediated catabolism of aggrecan. Evidence that cleavage at the "aggrecanase" site (Glu373-Ala374) is a primary event in proteolysis of the interglobular domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M909383199

Cytokine-induced cartilage proteoglycan degradation is mediated by aggrecanase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M909383199

Characterization of aggrecan retained and lost from the extracellular matrix of articular cartilage. Involvement of carboxyl-terminal processing in the catabolism of aggrecan

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M909383199

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M909383199

Monoclonal antibodies that specifically recognize neoepitope sequences generated by 'aggrecanase' and matrix metalloproteinase cleavage of aggrecan: application to catabolism in situ and in vitro

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M909383199

Development of a cleavage-site-specific monoclonal antibody for detecting metalloproteinase-derived aggrecan fragments: detection of fragments in human synovial fluids

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M909383199

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M909383199

Neutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage aggrecan

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M909383199

Degradation of cartilage aggrecan by collagenase-3 (MMP-13)

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M909383199

Cleavage of native cartilage aggrecan by neutrophil collagenase (MMP-8) is distinct from endogenous cleavage by aggrecanase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M909383199

The interglobular domain of cartilage aggrecan is cleaved by hemorrhagic metalloproteinase HT-d (atrolysin C) at the matrix metalloproteinase and aggrecanase sites

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M909383199

21 January 2018

Identifiers

DOI

10.1074/JBC.M909383199

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