Aimee Eggler
Purdue University
4 Papers
Aimee Eggler is an academic researcher from Purdue University. The author has contributed to research in topics: Ubiquitin ligase & DNA ligase. The author has an hindex of 3, co-authored 4 publications.
Chat about Author
Papers
Discovery, synthesis, and structure-based optimization of a series of N -(tert -Butyl)-2-(N -arylamido)-2-(pyridin-3-yl) acetamides (ML188) as potent noncovalent small molecule inhibitors of the severe acute respiratory syndrome coronavirus (SARS-CoV) 3CL protease
Jon Jacobs,Valerie Grum-Tokars,Ya Zhou,Mark Turlington,S. Adrian Saldanha,Peter Chase,Aimee Eggler,Eric S. Dawson,Yahira M. Báez-Santos,Sakshi Tomar,Anna M. Mielech,Susan C. Baker,Craig W. Lindsley,Peter Hodder,Andrew D. Mesecar,Shaun R. Stauffer +15 more
TL;DR: 16-(R) is a noncovalent SARS-CoV 3CL Pro inhibitor with moderate MW and good enzyme and antiviral inhibitory activity and provides an excellent starting point for the further design and refinement of 3CLpro inhibitors that act by a non covalent mechanism of action.
201
Development of an efficient E. coli expression and purification system for a catalytically active, human Cullin3-RINGBox1 protein complex and elucidation of its quaternary structure with Keap1
TL;DR: The design and construction of an optimized expression and purification system for the full-length, human Cullin3-RINGBox 1 (Rbx1) protein complex from Escherichia coli is described.
19
Non-covalent triazole-based inhibitors of the SARS main proteinase 3CLpro
Mark Turlington,Aspen Chun,Jon Jacobs,Eric S. Dawson,J. Scott Daniels,Adrian Saldanha,Peter Chase,Peter Hodder,Aimee Eggler,Valerie Tokars,Andrew D. Mesecar,Craig W. Lindsley,Shaun R. Stauffer +12 more
- 14 Mar 2013
TL;DR: Based on X-ray crystal data from a related inhibitor, ML300 is believed to interact within the 3CLpro enzyme active site via a novel binding mode distinct from both our first probe ML188 and other known peptidomimetic inhibitors as discussed by the authors.
Discovery of N-(benzo[1,2,3]triazol-1-yl)-N-(benzyl)acetamido)phenyl) carboxamides as severe acute respiratory syndrome coronavirus (SARS-CoV) 3CLpro inhibitors: identification of ML300 and noncovalent nanomolar inhibitors with an induced-fit binding.
Mark Turlington,Aspen Chun,Aspen Chun,Sakshi Tomar,Aimee Eggler,Valerie Grum-Tokars,Jon Jacobs,Jon Jacobs,J. Scott Daniels,J. Scott Daniels,Eric S. Dawson,Eric S. Dawson,Adrian Saldanha,Peter Chase,Yahira M. Báez-Santos,Craig W. Lindsley,Peter Hodder,Andrew D. Mesecar,Shaun R. Stauffer +18 more
TL;DR: The X-ray structure of SARS-CoV 3CLpro bound with a ML300 analog highlights a unique induced-fit reorganization of the S2–S4 binding pockets leading to the first sub-micromolar noncovalent3CLpro inhibitors retaining a single amide bond.