Probing H2O2-mediated Structural Dynamics of the Human 26S Proteasome Using Quantitative Cross-linking Mass Spectrometry (QXL-MS)期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

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Probing H2O2-mediated Structural Dynamics of the Human 26S Proteasome Using Quantitative Cross-linking Mass Spectrometry (QXL-MS)

Institution:	From the 3Department of Physiology & Biophysics, University of California, Irvine, Irvine, CA 92694;;4Thermo Fisher, 355 River Oaks Parkway, San Jose, CA 95134;;5Department of Chemistry, University of California, Irvine, Irvine, CA 92694

Abstract:	Download : Download high-res image (128KB) Download : Download full-size image Highlights ?Two-step cross-linking coupled with affinity purification to facilitate structural analysis of protein complexes. ?Integrated QXL-MS workflow for studying condition-dependent structural changes of protein complexes. ?Mechanistic insights on in vivo H₂O₂-induced conformational dynamics of proteasome complexes.

Keywords:	Protein Cross-linking* Protein-Protein Interactions* Protein Conformation* Protein complex analysis Quantification Oxidative stress 26S proteasome quantitative cross-linking mass spectrometry structural dynamics
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