Chemical Biology Toolbox to Visualize Protein Aggregation in Live Cells

ChemBioChem ◽  
2021 ◽  
Author(s):  
Di Shen ◽  
Yulong Bai ◽  
Yu Liu
Author(s):  
Rachel Spokoini ◽  
Maya Shamir ◽  
Alma Keness ◽  
Daniel Kaganovich

2015 ◽  
Vol 51 (41) ◽  
pp. 8652-8655 ◽  
Author(s):  
Ruei-Yu He ◽  
Yi-Chen Huang ◽  
Chao-Wei Chiang ◽  
Yu-Ju Tsai ◽  
Ting-Juan Ye ◽  
...  

Q/N- and G-rich polypeptides from the TDP-43 C-terminus formed amyloid fibers in vitro and induced the aggregation of the transfected TDP-43-EGFP in live cells.


Methods ◽  
2018 ◽  
Vol 140-141 ◽  
pp. 172-177 ◽  
Author(s):  
Rory Nolan ◽  
Maro Iliopoulou ◽  
Luis Alvarez ◽  
Sergi Padilla-Parra

2020 ◽  
Author(s):  
Noah Bissonnette ◽  
Keun Ah Ryu ◽  
Tamara Reyes-Robles ◽  
Sharon Wilhelm ◽  
Erik Hett ◽  
...  

<p>Despite the growing utilization of visible light photochemistry in both chemistry and biology, a general low-heat photoreactor for use across these different disciplines does not exist. Herein, we describe the design and utilization of a standardized photoreactor for visible light driven activation and photocatalytic chemical transformations. Using this single benchtop photoreactor, we perform photoredox reactions across multiple visible light wavelengths, a high throughput photocatalytic cross coupling reaction, and <i>in vitro</i> labeling of proteins and live cells. Given the success of this reactor in all tested applications, we envision that this multi-use photoreactor will be widely used in biology, chemical biology, and medicinal chemistry settings.</p>


2009 ◽  
Vol 96 (3) ◽  
pp. 88a
Author(s):  
Giulia Ossato ◽  
Michelle Digman ◽  
Charity Aiken ◽  
Lawrence Marsh ◽  
Enrico Gratton

2013 ◽  
Vol 9 (5) ◽  
pp. 862 ◽  
Author(s):  
Deokho Jung ◽  
Kyoungmi Min ◽  
Juyeon Jung ◽  
Wonhee Jang ◽  
Youngeun Kwon

2011 ◽  
Vol 100 (3) ◽  
pp. 774-783 ◽  
Author(s):  
V. Vetri ◽  
G. Ossato ◽  
V. Militello ◽  
M.A. Digman ◽  
M. Leone ◽  
...  

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Keisuke Kitakaze ◽  
Shusuke Taniuchi ◽  
Eri Kawano ◽  
Yoshimasa Hamada ◽  
Masato Miyake ◽  
...  

The endoplasmic reticulum (ER) is responsible for folding secretory and membrane proteins, but disturbed ER proteostasis may lead to protein aggregation and subsequent cellular and clinical pathologies. Chemical chaperones have recently emerged as a potential therapeutic approach for ER stress-related diseases. Here, we identified 2-phenylimidazo[2,1-b]benzothiazole derivatives (IBTs) as chemical chaperones in a cell-based high-throughput screen. Biochemical and chemical biology approaches revealed that IBT21 directly binds to unfolded or misfolded proteins and inhibits protein aggregation. Finally, IBT21 prevented cell death caused by chemically induced ER stress and by a proteotoxin, an aggression-prone prion protein. Taken together, our data show the promise of IBTs as potent chemical chaperones that can ameliorate diseases resulting from protein aggregation under ER stress.


2021 ◽  
Author(s):  
Sicheng Tang ◽  
Songtao Ye ◽  
Xin Zhang

There is an unmet demand for research tools to monitor the multistep protein aggregation process in live cells, a process that has been associated with a growing number of human diseases. Recently, AIEgens have been developed to directly monitor the entire protein aggregation process in test tubes and live cells. Future application of AIEgens is expected to shed light on both diagnosis and treatment of disease rooted in protein aggregation.


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