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首页> 外文期刊>Mass Spectrometry Reviews >A multi-angular mass spectrometric view at cyclic nucleotide dependent protein kinases: In vivo characterization and structure/function relationship
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A multi-angular mass spectrometric view at cyclic nucleotide dependent protein kinases: In vivo characterization and structure/function relationship

机译:环状核苷酸依赖性蛋白激酶的多角度质谱图:体内特征与结构/功能关系

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摘要

Mass spectrometry has evolved in recent years to a well-accepted and increasingly important complementary technique in molecular and structural biology. Here we review the many contributions mass spectrometry based studies have made in recent years in our understanding of the important cyclic nucleotide activated protein kinase A (PKA) and protein kinase G (PKG). We both describe the characterization of kinase isozymes, substrate phosphorylation, binding partners and post-translational modifications by proteomics based methodologies as well as their structural and functional properties as revealed by native mass spectrometry, H/D exchange MS and ion mobility. Combining all these mass spectrometry based data with other biophysical and biochemical data has been of great help to unravel the intricate regulation of kinase function in the cell in all its magnificent complexity.
机译:近年来,质谱技术已发展成为分子和结构生物学中广为接受且日益重要的补充技术。在这里,我们回顾了近年来基于质谱的研究在我们对重要的环状核苷酸激活的蛋白激酶A(PKA)和蛋白激酶G(PKG)的理解方面所做出的许多贡献。我们都描述了基于蛋白质组学的方法对激酶同工酶,底物磷酸化,结合伴侣和翻译后修饰的表征,以及它们的结构和功能特性,如通过自然质谱,H / D交换质谱和离子迁移所揭示的。将所有这些基于质谱的数据与其他生物物理和生化数据相结合,对于揭示细胞中所有复杂功能的激酶功能的复杂调控都具有极大的帮助。

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