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 Peroxynitrite
About this item
Full title
Author / Creator
Publisher
United States: Public Library of Science
Journal title
Language
English
Formats
Publication information
Publisher
United States: Public Library of Science
Subjects
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
Authors, Artists and Contributors
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