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Front Cover: Profiling the Protein Targets of Unmodified Bio‐Active Molecules with Drug Affinity Responsive Target Stability and Liquid Chromatography/Tandem Mass Spectrometry
Author(s) -
Hwang HuiYun,
Kim Tae Young,
Szász Marcell A.,
Dome Balazs,
Malm Johan,
MarkoVarga Gyorgy,
Kwon Ho Jeong
Publication year - 2020
Publication title -
proteomics
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.202070061
Subject(s) - chemistry , front cover , tandem mass spectrometry , mass spectrometry , chromatography , drug discovery , proteomics , small molecule , tandem , liquid chromatography–mass spectrometry , affinity chromatography , target protein , drug , computational biology , biochemistry , cover (algebra) , enzyme , biology , pharmacology , mechanical engineering , materials science , engineering , composite material , gene
DOI: 10.1002/pmic.201900325 Identifying the target proteins of bioactive small molecules is a key step in understanding the mode‐of‐action of a drug and addressing the underlying mechanisms responsible for a particular phenotype. In article number 1900325 by Hui‐Yun Hwang et al., a robust method utilizing drug affinity responsive target stability (DARTS) and liquid chromatography/tandem mass spectrometry (LC‐MS/MS) plus other proteomic approaches is discussed as effective way to select the biologically relevant target proteins of bioactive small molecules.
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