Gräwert, Melissa Ann, Gallastegui, Nerea, Stein, Martin, Schmidt, Boris, Kloetzel, Peter-Michael, Huber, Robert and Groll, Michael 2011. Elucidation of the alpha-keto-aldehyde binding mechanism: a lead structure motif for proteasome inhibition. Angewandte Chemie - International Edition 50 (2) , pp. 542-544. 10.1002/anie.201005488 |
Official URL: http://dx.doi.org/10.1002/anie.201005488
Abstract
Lead role: The role of peptidyl alpha-keto aldehydes as proteasome inhibitors is well established, yet their molecular binding mode requires additional investigation. A cyclization mechanism that proceeds through hemiketal and Schiff base formation with the nucleophilic N-terminal threonine of β5 is shown to result in the reversible formation of a 5,6-dihydro-2H-1,4-oxazine ring. This agent serves as a new lead for the development of anticancer drugs
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Biosciences |
Subjects: | Q Science > Q Science (General) Q Science > QD Chemistry |
Uncontrolled Keywords: | drug discovery; peptidyl glyoxals; proteasomes; reversible inhibition; structure elucidation |
Additional Information: | Article first published online: 9 DEC 2010 |
Publisher: | Wiley-Blackwell |
ISSN: | 1433-7851 |
Last Modified: | 24 Jun 2017 08:43 |
URI: | https://orca.cardiff.ac.uk/id/eprint/18211 |
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