(Q28618916)

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Human progelatinase A can be activated by matrilysin

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3 February 2017

Human progelatinase A can be activated by matrilysin (English)

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3 February 2017

T. Crabbe

1

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3 February 2017

B. Smith

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2

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3 February 2017

J. O'Connell

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3

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3 February 2017

A. Docherty

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4

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3 February 2017

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English

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23 May 1994

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3 February 2017

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3 February 2017

345

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1

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14–16

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3 February 2017

Substrate specificities and activation mechanisms of matrix metalloproteinases

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21 January 2018

Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties

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21 January 2018

Biochemical characterization of matrilysin. Activation conforms to the stepwise mechanisms proposed for other matrix metalloproteinases

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21 January 2018

Purification of recombinant human prostromelysin. Studies on heat activation to give high-Mr and low-Mr active forms, and a comparison of recombinant with natural stromelysin activities

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21 January 2018

The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity

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21 January 2018

The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A.

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21 January 2018

The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases

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21 January 2018

Human progelatinase A can be activated by autolysis at a rate that is concentration-dependent and enhanced by heparin bound to the C-terminal domain

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21 January 2018

A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases

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21 January 2018

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DOI

10.1016/0014-5793(94)00412-9

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1 reference

3 February 2017

ResearchGate publication ID

15003857

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(Q28618916)

Human progelatinase A can be activated by matrilysin

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