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

Ischemia/reperfusion-induced myosin light chain 1 phosphorylation increases its degradation by matrix metalloproteinase 2

(2012) Virgilio J. J. Cadete et al.   FEBS Journal

Phosphorylation status of matrix metalloproteinase 2 in myocardial ischaemia–reperfusion injury

(2012) Meltem Sariahmetoglu et al.   HEART

Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling

(2011) Jisun Lee et al.   BIOCHEMICAL JOURNAL

Mechanisms of cytosolic targeting of matrix metalloproteinase-2

(2011) Mohammad A.M. Ali et al.   JOURNAL OF CELLULAR PHYSIOLOGY

Intracellular substrate cleavage: a novel dimension in the biochemistry, biology and pathology of matrix metalloproteinases

(2010) Bénédicte Cauwe et al.   CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY

Towards understanding secondary structure transitions: phosphorylation and metal coordination in model peptides

(2010) Malgorzata Broncel et al.   ORGANIC & BIOMOLECULAR CHEMISTRY

Matrix metalloproteinase-2 and myocardial oxidative stress injury: beyond the matrix

(2009) A. D. Kandasamy et al.   CARDIOVASCULAR RESEARCH

Redox modulation of global phosphatase activity and protein phosphorylation in intact skeletal muscle

(2009) Valerie P. Wright et al.   JOURNAL OF PHYSIOLOGY-LONDON

Activation and modulation of 72kDa matrix metalloproteinase-2 by peroxynitrite and glutathione

(2008) Serena Viappiani et al.   BIOCHEMICAL PHARMACOLOGY

Structural Bases for Substrate and Inhibitor Recognition by Matrix Metalloproteinases

(2008) Loretta Aureli et al.   CURRENT MEDICINAL CHEMISTRY