Journal
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
Volume 23, Issue 17, Pages 4832-4836Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2013.07.024
Keywords
Endoplasmic reticulum aminopeptidase; ERAP1; ERAP2; IRAP; Selective inhibitor; Rational design; Molecular modeling
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Funding
- Action 'Supporting Postdoctoral Researchers' grant of the Operational Program 'Education and Lifelong Learning' [LS7_2199]
- 'ARISTEIA I' action grant [986]
- European Social Fund (ESF)
- General Secretariat for Research and Technology of Greece
- French 'Agence Nationale de Recherche', ANR for the IRAP-DC [NT09_522096]
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Endoplasmic reticulum aminopeptidases, ERAP1 and ERAP2, as well as Insulin regulated aminopeptidase (IRAP) play key roles in antigen processing, and have recently emerged as biologically important targets for manipulation of antigen presentation. Taking advantage of the available structural and substrate-selectivity data for these enzymes, we have rationally designed a new series of inhibitors that display low micromolar activity. The selectivity profile for these three highly homologous aminopeptidases provides a promising avenue for modulating intracellular antigen processing. (C) 2013 Elsevier Ltd. All rights reserved.
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