Thermal profiling reveals phenylalanine hydroxylase as an off-target of panobinostat

被引:0
作者
Isabelle Becher
Thilo Werner
Carola Doce
Esther A Zaal
Ina Tögel
Crystal A Khan
Anne Rueger
Marcel Muelbaier
Elsa Salzer
Celia R Berkers
Paul F Fitzpatrick
Marcus Bantscheff
Mikhail M Savitski
机构
[1] Cellzome GmbH,Department of Biochemistry
[2] Genome Biology Unit,undefined
[3] European Molecular Biology Laboratory,undefined
[4] Biomolecular Mass Spectrometry and Proteomics,undefined
[5] Utrecht University,undefined
[6] University of Texas Health Science Center,undefined
来源
Nature Chemical Biology | 2016年 / 12卷
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摘要
A chemoproteomics approach utilizing the thermal shift assay and quantitative MS resulted in the identification of phenylalanine hydroxylase as an off-target of the histone deacetylase inhibitor panobinostat.[graphic not available: see fulltext]
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页码:908 / 910
页数:2
相关论文
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  • [1] Simon GM(2013)undefined Nat. Chem. Biol. 9 200-205
  • [2] Niphakis MJ(2013)undefined Science 341 84-87
  • [3] Cravatt BF(2016)undefined Annu. Rev. Pharmacol. Toxicol. 56 141-161
  • [4] Martinez Molina D(2014)undefined Science 346 1255784-1057
  • [5] Martinez Molina D(2015)undefined Nat. Methods 12 1055-1978
  • [6] Nordlund P(2012)undefined Bioorg. Med. Chem. 20 1973-240
  • [7] Savitski MM(2013)undefined Nat. Chem. Biol. 9 232-2792
  • [8] Huber KV(2013)undefined Angew. Chem. Int. Edn Engl. 52 2744-241
  • [9] Bantscheff M(2009)undefined Cancer Lett. 280 233-276
  • [10] Drewes G(2015)undefined J. Blood Med. 6 269-2203