A novel 2D-based approach to the discovery of candidate substrates for the metalloendopeptidase meprin
Author:
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1742-4658.2008.06592.x/fullpdf
Reference51 articles.
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2. N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: a metalloendopeptidase of the human intestinal microvillus membrane which degrades biologically active peptides;Sterchi;Arch Biochem Biophys,1988
3. Purification and characterization of a metallo-endoproteinase from mouse kidney;Beynon;Biochem J,1981
4. Microvillar membrane neutral endopeptidases;Kenny;Acta Biol Med Ger,1981
5. Expression of the alpha subunit of PABA peptide hydrolase (EC 3.4.24.18) in MDCK cells;Grünberg;FEBS Lett,1993
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1. LC-MS-based metabolomics analysis to identify meprin-β-associated changes in kidney tissue from mice with STZ-induced type 1 diabetes and diabetic kidney injury;American Journal of Physiology-Renal Physiology;2019-10-01
2. Meprin A;Handbook of Proteolytic Enzymes;2013
3. Profiling protease activities by dynamic proteomics workflows;PROTEOMICS;2012-01-23
4. Villin and actin in the mouse kidney brush-border membrane bind to and are degraded by meprins, an interaction that contributes to injury in ischemia-reperfusion;American Journal of Physiology-Renal Physiology;2011-10
5. Balance of meprin A and B in mice affects the progression of experimental inflammatory bowel disease;American Journal of Physiology-Gastrointestinal and Liver Physiology;2011-02
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