1. Hydroxamate-based inhibitors of low affinity IgE receptor (CD23) processing
- Author
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Brian Bolognese, Pearl Louis-Flamberg, Andrew Faller, Mark McCord, Lisa Marshall, Smith David Glynn, Ruth J. Mayer, Stuart Bailey, Derek Richard Buckle, and Sally Jackson
- Subjects
Phenylalanine ,Clinical Biochemistry ,Pharmaceutical Science ,Thiophenes ,Immunoglobulin E ,Hydroxamic Acids ,Biochemistry ,chemistry.chemical_compound ,Structure-Activity Relationship ,Drug Discovery ,Humans ,Protease Inhibitors ,Molecular Biology ,chemistry.chemical_classification ,Metalloproteinase ,Hydroxamic acid ,biology ,Chemistry ,Receptors, IgE ,Organic Chemistry ,CD23 ,In vitro ,Enzyme ,Enzyme inhibitor ,biology.protein ,Molecular Medicine ,Batimastat ,Protein Processing, Post-Translational - Abstract
A series of hydroxamic acids related to the non-selective matrix metalloprotease inhibitor Batimastat is described, which inhibits the proteolytic cleavage of the low affinity IgE receptor from cell membrane preparations. Limited SAR studies suggest that the structural requirements for effective inhibition are distinct from those required for the inhibition of collagenase. We have examined the P 1′ requirements for hydroxamate based inhibitors of the novel metalloprotease responsible for processing of the low affinity IgE receptor (CD23). more...
- Published
- 1999