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),ChemBioChem

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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)
ChemBioChem ( IF 2.6 ) Pub Date : 2018-02-28 , DOI: 10.1002/cbic.201800103
Julie Anne Christine Alexandre ₁ , Michael Kenneth Swan ₁ , Mike John Latchem ₁ , Dean Boyall ₁ , John Robert Pollard ₁ , Stuart Wynn Hughes ₁ , James Westcott ₁

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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).

中文翻译：

封面功能：吲哚胺2,3-二加氧酶的新型4-氨基1,2,3-三唑抑制剂与酶形成长寿复合物，并具有出色的细胞效价（ChemBioChem 6/2018）

封面特征图片显示了与吲哚胺1,3-二加氧酶（IDO）的血红素铁结合的4-氨基-1,2,3-三唑之间的强结合。旁边是丙氨酸分子，它占据了酶的氨基酸结合位点。在J.A.C.Alexandre等人的全文中，结构，光谱和动力学技术证明了该复合物的紧密和长寿命特性，这有助于解释该系列中观察到的精妙细胞力。JW的封面艺术；在CC‐BY 2.0下使用的背景是Tejvan Pettinger的“牛津尖顶-11月”。可以在2018年第6期的第552页上找到更多详细信息（DOI：10.1002 / cbic.201700560）。

更新日期：2018-02-28

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