Activation of procollagenases is a key control point in cartilage collagen degradation: interaction of serine and metalloproteinase pathways (Q43760463)

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English	Activation of procollagenases is a key control point in cartilage collagen degradation: interaction of serine and metalloproteinase pathways	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

26 November 2017

Activation of procollagenases is a key control point in cartilage collagen degradation: interaction of serine and metalloproteinase pathways (English)

1 reference

Europe PubMed Central

PubMed publication ID

26 November 2017

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based on heuristic

inferred from title

author name string

Milner JM

1

1 reference

Europe PubMed Central

PubMed publication ID

26 November 2017

Elliott SF

2

1 reference

Europe PubMed Central

PubMed publication ID

26 November 2017

Cawston TE

3

1 reference

Europe PubMed Central

PubMed publication ID

26 November 2017

publication date

1 September 2001

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Europe PubMed Central

PubMed publication ID

26 November 2017

Arthritis & Rheumatology

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Europe PubMed Central

PubMed publication ID

26 November 2017

44

1 reference

Europe PubMed Central

PubMed publication ID

26 November 2017

9

1 reference

Europe PubMed Central

PubMed publication ID

26 November 2017

2084-2096

1 reference

Europe PubMed Central

PubMed publication ID

26 November 2017

The chondrocyte, architect of cartilage. Biomechanics, structure, function and molecular biology of cartilage matrix macromolecules

1 reference

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In vivo studies of articular tissue damage mediated by catabolin/interleukin 1.

1 reference

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Pig catabolin is a form of interleukin 1. Cartilage and bone resorb, fibroblasts make prostaglandin and collagenase, and thymocyte proliferation is augmented in response to one protein.

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In vivo studies of cartilage regeneration after damage induced by catabolin/interleukin-1.

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Matrix metalloproteinases: a review

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The matrix-degrading metalloproteinases

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Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments.

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21 January 2018

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10.1002/1529-0131(200109)44:9<2084::AID-ART359>3.0.CO;2-R

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Europe PubMed Central

PubMed publication ID

26 November 2017

release_ue3o5ccb6vcxhoqlgigvsmiax4

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https://api.fatcat.wiki/v0/release/ue3o5ccb6vcxhoqlgigvsmiax4

24 November 2022

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PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

26 November 2017

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