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Phosphorylation Status of 72 kDa MMP-2 Determines Its Structure and Activity in Response to Peroxyni...

Phosphorylation Status of 72 kDa MMP-2 Determines Its Structure and Activity in Response to Peroxyni...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1428305620

Phosphorylation Status of 72 kDa MMP-2 Determines Its Structure and Activity in Response to Peroxynitrite

About this item

Full title

Phosphorylation Status of 72 kDa MMP-2 Determines Its Structure and Activity in Response to Peroxynitrite

Publisher

United States: Public Library of Science

Journal title

PloS one, 2013-08, Vol.8 (8), p.e71794

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

Matrix metalloproteinase-2 (MMP-2) is a key intra- and extra-cellular protease which contributes to several oxidative stress related pathologies. A molecular understanding of 72 kDa MMP-2 activity, directly mediated by S-glutathiolation of its cysteine residues in the presence of peroxynitrite (ONOO(-)) and by phosphorylation of its serine and thre...

Alternative Titles

Full title

Phosphorylation Status of 72 kDa MMP-2 Determines Its Structure and Activity in Response to Peroxynitrite

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1428305620

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1428305620

Other Identifiers

ISSN

1932-6203

E-ISSN

1932-6203

DOI

10.1371/journal.pone.0071794

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