Article
A monoclonal antibody inhibits gelatinase B/MMP-9 by selective binding to part of the catalytic domain and not to the fibronectin or zinc binding domains.
Biochimica et biophysica acta - 1 Feb 2007
Martens Erik, Leyssen An, Van Aelst Ilse, Fiten Pierre, Piccard Helene, Hu Jialiang, Descamps Francis J, Van den Steen Philippe E, Proost Paul, Van Damme Jo, Liuzzi Grazia Maria, Riccio Paolo, Polverini Eugenia, Opdenakker Ghislain
Abstract excerpt
Gelatinase B/matrix metalloproteinase-9 (MMP-9) is a multidomain enzyme functioning in acute and chronic inflammatory and neoplastic diseases. It belongs to a family of more than 20 related zinc proteinases. Therefore, the discovery and the definition of the action mechanism of selective MMP inhibitors form the basis for future therapeutics. The monoclonal antibody REGA-3G12 is a most selective inhibitor of human...
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