scholarly journals Bacterial cupredoxin azurin hijacks cellular signaling networks: Protein-protein interactions and cancer therapy

2017 ◽  
Vol 26 (12) ◽  
pp. 2334-2341 ◽  
Author(s):  
Meng Gao ◽  
Jingjing Zhou ◽  
Zhengding Su ◽  
Yongqi Huang
Author(s):  
Alexander Goncearenco ◽  
Minghui Li ◽  
Franco L. Simonetti ◽  
Benjamin A. Shoemaker ◽  
Anna R. Panchenko

2005 ◽  
Vol 83 (12) ◽  
pp. 955-963 ◽  
Author(s):  
David C. Fry ◽  
Lyubomir T. Vassilev

2018 ◽  
Vol 120 ◽  
pp. S67 ◽  
Author(s):  
Eva Griesser ◽  
Uladzimir Barayeu ◽  
Jörg Flemmig ◽  
Dolores Perez-Sala ◽  
Maria Fedorova

Molecules ◽  
2018 ◽  
Vol 23 (9) ◽  
pp. 2256 ◽  
Author(s):  
Mariarosaria Ferraro ◽  
Giorgio Colombo

Investigating protein-protein interactions (PPIs) holds great potential for therapeutic applications, since they mediate intricate cell signaling networks in physiological and disease states. However, their complex and multifaceted nature poses a major challenge for biochemistry and medicinal chemistry, thereby limiting the druggability of biological partners participating in PPIs. Molecular Dynamics (MD) provides a solid framework to study the reciprocal shaping of proteins’ interacting surfaces. Here, we review successful applications of MD-based methods developed in our group to predict interfacial areas involved in PPIs of pharmaceutical interest. We report two interesting examples of how structural, dynamic and energetic information can be combined into efficient strategies which, complemented by experiments, can lead to the design of new small molecules with promising activities against cancer and infections. Our advances in targeting key PPIs in angiogenic pathways and antigen-antibody recognition events will be discussed for their role in drug discovery and chemical biology.


2019 ◽  
Author(s):  
Tae-Wuk Kim ◽  
Chan Ho Park ◽  
Chuan-Chih Hsu ◽  
Jia-Ying Zhu ◽  
Yuchun Hsiao ◽  
...  

AbstractTransient protein-protein interactions (PPIs), such as those between posttranslational modifying enzymes and their substrates, play key roles in cellular regulation, but are difficult to identify. Here we demonstrate the application of enzyme-catalyzed proximity labeling (PL), using the engineered promiscuous biotin ligase TurboID, as a sensitive method for characterizing PPIs in signaling networks. We show that TurboID fused with the GSK3-like kinase BIN2 or a PP2A phosphatase biotinylates their known substrate, the BZR1 transcription factor, with high specificity and efficiency. We optimized the protocol of biotin labeling and affinity purification in transgenic Arabidopsis expressing a BIN2-TurboID fusion protein. Subsequent quantitative mass spectrometry (MS) analysis identified about three hundred proteins biotinylated by BIN2-TurboID more efficiently than the YFP-TurboID control. These include a significant subset of previously proven BIN2 interactors and a large number of new BIN2-proximal proteins that uncover a broad BIN2 signaling network. Our study illustrates that PL-MS using TurboID is a powerful tool for mapping signaling networks, and reveals broad roles of BIN2 kinase in cellular signaling and regulation in plants.Impact StatementTurboID-mediated proximity labeling is a powerful tool for protein interactomics in plants.


BMC Genomics ◽  
2014 ◽  
Vol 15 (Suppl 12) ◽  
pp. S7 ◽  
Author(s):  
Olga Popik ◽  
Olga Saik ◽  
Evgeny Petrovskiy ◽  
Björn Sommer ◽  
Ralf Hofestädt ◽  
...  

2014 ◽  
Vol 131 (2) ◽  
pp. 239-250 ◽  
Author(s):  
Lauran Reyniers ◽  
Maria Grazia Del Giudice ◽  
Laura Civiero ◽  
Elisa Belluzzi ◽  
Evy Lobbestael ◽  
...  

Cell Cycle ◽  
2008 ◽  
Vol 7 (11) ◽  
pp. 1569-1574 ◽  
Author(s):  
Tomoyuki Tanaka ◽  
Terence H. Rabbitts

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