Cover Feature: New 4‐Amino‐1,2,3‐Triazole Inhibitors of Indoleamine 2,3‐Dioxygenase Form a Long‐Lived Complex with the Enzyme and Display Exquisite Cellular Potency (ChemBioChem 6/2018)

The cover feature picture shows a representation of the strong union between a 4‐amino‐1,2,3‐triazole bound to the haem iron of indoleamine 1,3‐dioxygenase (IDO). Alongside is a molecule of alanine, which occupies the amino acid binding site of the enzyme. In the full paper by J. A. C. Alexandre et ...

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Published inChembiochem : a European journal of chemical biology Vol. 19; no. 6; p. 528
Main Authors Alexandre, Julie Anne Christine, Swan, Michael Kenneth, Latchem, Mike John, Boyall, Dean, Pollard, John Robert, Hughes, Stuart Wynn, Westcott, James
Format Journal Article
LanguageEnglish
Published 16.03.2018
Subjects
cancer
enzymes
inhibitors
kinetics
porphyrins
triazoles
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Summary:The cover feature picture shows a representation of the strong union between a 4‐amino‐1,2,3‐triazole bound to the haem iron of indoleamine 1,3‐dioxygenase (IDO). Alongside is a molecule of alanine, which occupies the amino acid binding site of the enzyme. In the full paper by J. A. C. Alexandre et al., structural, spectroscopic and kinetic techniques demonstrate the tight and long‐lived nature of this complex, which help explain the exquisite cellular potency observed for this series. Cover art by J.W.; the background, “Oxford Spires—November” by Tejvan Pettinger, is used under CC‐BY 2.0. More details can be found on page 552 in Issue 6, 2018 (DOI: 10.1002/cbic.201700560).
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.201800103