Revealing Protein Aggregates Under Thapsigargin-Induced ER Stress Using an ER-Targeted Thioflavin 期刊名称： ACS Sensors
大贺典雄作者： Peter Verwilst,Kyutae Kim,Kyoung Sunwoo,Hye-Ri Kim,Jong Seung Kim
年份： 2019年
期号： 第XXXX期necklace怎么读
毛遂自荐翻译关键词： chemical chaperones;thioflavin;fluorescence;ER stress;protein
aggregation
navigator是什么意思>the call摘要：ER-ThT, a thioflavin T-bad fluorescent chemonsor, was developed to detect protein aggregates in the endoplasmic reticulum (ER) and was applied to live cells under various forms of ER stress. Upon DTT-induced reductive denaturation of lysozyme and albumin, the intensity was incread in a protein concentration-dependent way, following a nonfluores-cent lag pha. ER-ThT detects protein aggregates rather than unfolded proteins in solution and the protein aggregation can be
经典英语歌曲>structure是什么意思
visualized in the prence of lipid membranes or native proteins. Within live HeLa cells, ER-ThT is localized in the ER and its fluorescence was dramatically incread upon ER stress induction by DTT, Thapsigargin or Brefeldin A. Moreover,英语考试>tln
in the prence of ER stress modulators (TUDCA, TMAO or PBA), also known as chemical chaperones, the
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although
