Regulation of Human ADAM 12 Protease by the Prodomain (Q58460385)

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5 December 2019

title

Regulation of human ADAM 12 protease by the prodomain. Evidence for a functional cysteine switch (English)

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5 December 2019

author

Michael Toft Overgaard

2

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5 December 2019

Claus Oxvig

3

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5 December 2019

Reidar Albrechtsen

4

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5 December 2019

author name string

F Loechel

1

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5 December 2019

U M Wewer

5

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5 December 2019

language of work or name

English

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publication date

1 May 1999

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Journal of Biological Chemistry

5 December 2019

published in

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5 December 2019

volume

274

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5 December 2019

issue

19

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5 December 2019

page(s)

13427-13433

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ADAMs in fertilization and development

5 December 2019

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Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha

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Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation

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

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A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells

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Proteolytic and non-proteolytic activation of human neutrophil progelatinase B

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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).

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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.

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

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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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A novel, secreted form of human ADAM 12 (meltrin alpha) provokes myogenesis in vivo

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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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The Proteinase‐Binding Reaction of α2M

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Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme

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Inhibition of alpha-lytic protease by pro region C-terminal steric occlusion of the active site

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Pro region C-terminus:protease active site interactions are critical in catalyzing the folding of alpha-lytic protease

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Role of the prodomain in folding and secretion of rat pancreatic carboxypeptidase A1.

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ADAMs: focus on the protease domain

21 January 2018

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Crystallisation and preliminary X-ray analysis of the receptor-binding domain of human and bovine alpha 2-macroglobulin

21 January 2018

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TNF-alpha converting enzyme (TACE) is inhibited by TIMP-3

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.274.19.13427

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10224107%20AND%20SRC:MED&resulttype=core&format=json

5 December 2019

1 reference