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|Relevance||Furin is a member of the proprotein convertase (PC)2 family of calcium-dependent serine proteases that have structural homology to subtilisin/kexin-type proteases and are characterized by their recognition of a distinctive P4 Arg-X-Arg/Lys-P1 Arg consensus cleavage site. PCs perform the intracellular and pericellular processing of a large number of peptide and protein precursors transiting the constitutive and regulated protein secretion pathways, including prohormones, growth factors, and their receptors, matrix metalloproteases and integrins. PCs are thus pivotal in the control of cell signaling, proliferation, motility, and adhesion. PC dysfunction is associated with a broad spectrum of diseases, including cancer, autoimmunity, and Alzheimer disease. In addition, a number of significant human infectious organisms take advantage of host PC activity to promote their growth. PCs have been considered promising therapeutic drug targets, and the development of specific inhibitors is being intensely pursued.|
|Antigen/Gene or Protein Targets||Non-furin Proprotein Convertases (PC4, PC5, PACE4, and PC7)_x000D_|
Non-furin specific inhibitor (α1-MDW) is invented by creating chimeric protein containing α1-PDX and Serpin B8 P6-P5 segment with K222Y and L224E mutation.
α1-MDW has a 20-60 fold higher reactivity with non-Furin PCs than with furin.
|Research Area||Adhesion, Cancer, Cell Signaling & Signal Transduction, Cell Structure and Motility, Drug Discovery & Development, Virology|
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