Rapid Discovery of Potent and Selective Glycosidase-Inhibiting De Novo Peptides
- 1 March 2017
- journal article
- research article
- Published by Elsevier in Cell Chemical Biology
- Vol. 24 (3) , 381-390
Abstract
No abstract availableKeywords
Funding Information
- Biological and Environmental Research
- National Institutes of Health
- Japan Agency for Medical Research and Development
- U.S. Department of Energy
- Japan Society for the Promotion of Science (P13026)
- National Institute of General Medical Sciences (P41GM103393)
- Basic Energy Sciences (DE-AC02-76SF00515)
- Office of Science
This publication has 53 references indexed in Scilit:
- Glucosyl epi‐cyclophellitol allows mechanism‐based inactivation and structural analysis of human pancreatic α‐amylaseFEBS Letters, 2016
- Human α‐amylase and starch digestion: An interesting marriageStarch - Stärke, 2011
- Carbohydrate-mimetic peptides: structural aspects of mimicry and therapeutic implicationsExpert Opinion on Biological Therapy, 2011
- PHENIX: a comprehensive Python-based system for macromolecular structure solutionActa Crystallographica Section D Structural Biology, 2010
- De Novo Design of α-Amylase Inhibitor: A Small Linear Mimetic of Macromolecular Proteinaceous LigandsChemistry & Biology, 2005
- Coot: model-building tools for molecular graphicsActa Crystallographica Section D Structural Biology, 2004
- Three Camelid VHH Domains in Complex with Porcine Pancreatic α-AmylaseJournal of Biological Chemistry, 2002
- Substrate−Inhibitor Interactions in the Kinetics of α-Amylase Inhibition by Ragi α-amylase/Trypsin Inhibitor (RATI) and Its Various N-Terminal FragmentsBiochemistry, 2001
- The structure of human pancreaticα-amylase at 1.8 Å resolution and comparisons with related enzymesProtein Science, 1995
- Cyclic Hexapeptides and Chimeric Peptides as Mimics of TendamistatJournal of the American Chemical Society, 1994