期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
卷 1754, 期 1-2, 页码 183-190出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2005.07.028
关键词
protein kinase; chemical proteomic; affinity purification; mass spectrometry; inhibitor selectivity; target identification
Low-molecular-weight inhibitors of protein kinases are extensively used as research tools in signal transduction analysis and constitute a rapidly growing class of therapeutics for targeted intervention in human diseases. To determine how kinase-selective drugs interfere with cellular physiology on the molecular level, experimental strategies relying on the affinity capture of cellular targets in combination with protein identification by mass spectrometry have been established for a variety of kinase inhibitors. Importantly, these chemical proteomic methods permit the direct analysis of kinase inhibitor selectivity in biological systems and have led to new insights into the cellular modes of action of kinase-selective small molecule antagonists. (c) 2005 Elsevier B.V All rights reserved.
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