(Q40631335)

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Calcium‐induced activation and truncation of promatrix metalloproteinase‐9 linked to the core protein of chondroitin sulfate proteoglycans

scientific article published on October 1, 2003

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scholarly article

1 reference

Europe PubMed Central

22 September 2017

Calcium-induced activation and truncation of promatrix metalloproteinase-9 linked to the core protein of chondroitin sulfate proteoglycans (English)

1 reference

Europe PubMed Central

22 September 2017

Calcium‐induced activation and truncation of promatrix metalloproteinase‐9 linked to the core protein of chondroitin sulfate proteoglycans (English)

1 reference

10.1046/J.1432-1033.2003.03788.X

https://api.crossref.org/works/10.1046/J.1432-1033.2003.03788.X

14 March 2024

1 reference

10.1046/J.1432-1033.2003.03788.X

https://api.crossref.org/works/10.1046/J.1432-1033.2003.03788.X

14 March 2024

author name string

Jan-Olof Winberg

1

1 reference

Europe PubMed Central

22 September 2017

Eli Berg

2

1 reference

Europe PubMed Central

22 September 2017

Lars Uhlin-Hansen

4

1 reference

Europe PubMed Central

22 September 2017

Svein O. Kolset

3

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A14511382

14 March 2024

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publication date

1 October 2003

1 reference

Europe PubMed Central

22 September 2017

full work available at URL

https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1046%2Fj.1432-1033.2003.03788.x

1 reference

10.1046/J.1432-1033.2003.03788.X

https://api.crossref.org/works/10.1046/J.1432-1033.2003.03788.X

14 March 2024

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1046/j.1432-1033.2003.03788.x

1 reference

10.1046/J.1432-1033.2003.03788.X

https://api.crossref.org/works/10.1046/J.1432-1033.2003.03788.X

14 March 2024

1 reference

Europe PubMed Central

22 September 2017

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Europe PubMed Central

22 September 2017

3996-4007

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Europe PubMed Central

22 September 2017

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22 September 2017

Matrix metalloproteinases

1

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10.1046/J.1432-1033.2003.03788.X

https://api.crossref.org/works/10.1046/J.1432-1033.2003.03788.X

14 March 2024

Matrix metalloproteinases in tumor invasion

2

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Matrix metalloproteinases: a review

3

1 reference

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Matrix metalloproteinases and the development of cancer

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Expression of several matrix metalloproteinase genes in human monocytic cells

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Proteinases secreted by human mononuclear phagocytes

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Neutral metalloproteinases produced by human mononuclear phagocytes. Enzyme profile, regulation, and expression during cellular development

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Neutral proteinase expression by human mononuclear phagocytes: a prominent role of cellular differentiation

8

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Characterization of matrix metalloproteinases produced by rat alveolar macrophages

9

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The serpin alpha1-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 in vivo.

11

1 reference

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The matrix metalloproteinase-9 regulates the insulin-like growth factor-triggered autocrine response in DU-145 carcinoma cells

12

1 reference

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Metalloproteinases and their inhibitors in matrix remodeling

14

1 reference

10.1046/J.1432-1033.2003.03788.X

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The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family

16

1 reference

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Activation mechanisms of the precursors of matrix metalloproteinases 1, 2 and 3

17

1 reference

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A 25 kDa α2‐microglobulin‐related protein is a component of the 125 kDa form of human gelatinase

20

1 reference

10.1046/J.1432-1033.2003.03788.X

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Characterization of the monomeric and dimeric forms of latent and active matrix metalloproteinase-9. Differential rates for activation by stromelysin 1

22

1 reference

10.1046/J.1432-1033.2003.03788.X

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Macrophages secrete matrix metalloproteinase 9 covalently linked to the core protein of chondroitin sulphate proteoglycans

23

1 reference

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Structural basis of the adaptive molecular recognition by MMP9

24

1 reference

10.1046/J.1432-1033.2003.03788.X

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Proteoglycans: structures and interactions

25

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Serglycin secreted by leukocytes is efficiently eliminated from the circulation by sinusoidal scavenger endothelial cells in the liver

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1 reference

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The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study

28

1 reference

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The hemopexin-like domain (C domain) of human gelatinase A (matrix metalloproteinase-2) requires Ca2+ for fibronectin and heparin binding. Binding properties of recombinant gelatinase A C domain to extracellular matrix and basement membrane componen

29

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The function of Ca2+ in the action of mammalian collagenases

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Mechanism of activation of human neutrophil gelatinase B. Discriminating between the role of Ca2+ in activation and catalysis

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Mechanism of Ca2+-dependent activity of human neutrophil gelatinase B

33

1 reference

10.1046/J.1432-1033.2003.03788.X

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A spectrophotometric modification of a sensitive densitometric Safranin O assay for glycosaminoglycans

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1 reference

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Calibrating gelatin zymograms with human gelatinase standards

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Epidermolysis bullosa simplex: expression of gelatinase activity in cultured human skin fibroblasts

36

1 reference

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Gelatinase expression in generalized epidermolysis bullosa simplex fibroblasts

37

1 reference

10.1046/J.1432-1033.2003.03788.X

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Gelatinases A and B

38

1 reference

10.1046/J.1432-1033.2003.03788.X

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Interaction of alpha 2-macroglobulin with matrix metalloproteinases and its use for identification of their active forms

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1 reference

10.1046/J.1432-1033.2003.03788.X

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Serglycin-binding proteins in activated macrophages and platelets

40

1 reference

10.1046/J.1432-1033.2003.03788.X

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Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7)

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1 reference

10.1046/J.1432-1033.2003.03788.X

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Activation of the latent human neutrophil gelatinase by urea

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10.1046/J.1432-1033.2003.03788.X

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Mercurial activation of human PMN leucocyte type IV procollagenase (gelatinase)

43

1 reference

10.1046/J.1432-1033.2003.03788.X

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Disruption of the cysteine-75 and zinc ion coordination is not sufficient to activate the precursor of human matrix metalloproteinase 3 (stromelysin 1).

45

1 reference

10.1046/J.1432-1033.2003.03788.X

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APMA (4-aminophenylmercuric acetate) activation of stromelysin-1 involves protein interactions in addition to those with cysteine-75 in the propeptide.

46

1 reference

10.1046/J.1432-1033.2003.03788.X

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14 March 2024

Spontaneous propeptide processing of mini-stromelysin-1 mutants blocked by APMA ((4-Aminophenyl)mercuric acetate)

47

1 reference

10.1046/J.1432-1033.2003.03788.X

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Expression of human pro-matrix metalloproteinase 3 that lacks the N-terminal 34 residues in Escherichia coli: autoactivation and interaction with tissue inhibitor of metalloproteinase 1 (TIMP-1)

48

1 reference

10.1046/J.1432-1033.2003.03788.X

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The human neutrophil lipocalin supports the allosteric activation of matrix metalloproteinases

49

1 reference

10.1046/J.1432-1033.2003.03788.X

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14 March 2024

Identifiers

10.1046/J.1432-1033.2003.03788.X

1 reference

Europe PubMed Central

22 September 2017

1 reference

Europe PubMed Central

22 September 2017

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