(Q54624000)

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Specific amino acid substitutions in human collagenase cause decreased autoproteolysis and reveal a requirement for a second zinc atom for catalytic activity.

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7957937

Specific amino acid substitutions in human collagenase cause decreased autoproteolysis and reveal a requirement for a second zinc atom for catalytic activity. (English)

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7957937

author name string

Williams DH

1

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7957937

Murray EJ

2

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7957937

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publication date

1 November 1994

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7957937

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7957937

354

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7957937

3

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7957937

267-270

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7957937

Characterization of 58-kilodalton human neutrophil collagenase: comparison with human fibroblast collagenase

1 reference

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Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2

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The collagenase gene family in humans consists of at least four members

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Comparison of human stromelysin and collagenase by cloning and sequence analysis

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A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas

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An internal cysteine plays a role in the maintenance of the latency of human fibroblast collagenase.

1 reference

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

1 reference

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21 January 2018

Fragments of human fibroblast collagenase. Purification and characterization

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21 January 2018

Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2901136-2

21 January 2018

Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2901136-2

21 January 2018

Collagenase inhibitors: their design and potential therapeutic use.

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2901136-2

21 January 2018

Characterization of zinc-binding sites in human stromelysin-1: stoichiometry of the catalytic domain and identification of a cysteine ligand in the proenzyme

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2901136-2

21 January 2018

A quantitative collagen film collagenase assay for large numbers of samples

1 reference

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21 January 2018

Identifiers

10.1016/0014-5793(94)01136-2

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7957937

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7957937

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