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

2

M

Pratta

1 reference

28 March 2023

R Q Liu

3

R Q

Liu

1 reference

28 March 2023

J Austin

4

J

Austin

1 reference

28 March 2023

O H Ross

5

O H

Ross

1 reference

28 March 2023

I Abbaszade

6

I

Abbaszade

1 reference

28 March 2023

T Burn

7

T

Burn

1 reference

28 March 2023

E Arner

8

E

Journal of Biological Chemistry

Arner

1 reference

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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page(s)

18566-73

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issue

24

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Extended and globular protein domains in cartilage proteoglycans

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

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

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Mechanism of catabolism of aggrecan by articular cartilage

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

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Cytokine-induced cartilage proteoglycan degradation is mediated by aggrecanase.

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

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

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

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

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

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

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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

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