Development and biological evaluation of acyl protein thioesterase 1 (APT1) inhibitors

被引：19

作者：

Deck, P

Pendzialek, D

Biel, M

Wagner, M

Popkirova, B

Ludolph, B

Kragol, G

Kuhlmann, J ^{[1
]}

Giannis, A

Waldmann, H

机构：

[1] Max Planck Inst Mol Physiol, Dept Biol Struct, Otto Hahn Str 11, D-44227 Dortmund, Germany

[2] Univ Leipzig, Inst Organ Chem, D-04103 Leipzig, Germany

[3] Max Planck Inst Mol Physiol, Dept Biol Chem, D-44227 Dortmund, Germany

[4] Univ Dortmund, Fachbereich Chem, Dortmund, Germany

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2005年 / 44卷 / 31期

关键词：

biological activity; enzyme inhibitors; esterases; peptidomimetics; proteins;

D O I：

10.1002/anie.200462625

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

It works both ways: The development of potent peptidomimetic acyl protein thioesterase 1 (APT1) inhibitors, such as Raspalin 3 (see structure), and their use in biological and biochemical investigations are reported. The results show that the enzyme can deacylate and acylate Ras proteins. (Chemical Equation Presented). © 2005 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：4975 / 4980

页数：6

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