scholarly journals Identification of the first enantiopure Rac1–Tiam1 protein–protein interaction inhibitor and its optimized synthesis via phosphine free remote group directed hydroarylation

MedChemComm ◽  
2019 ◽  
Vol 10 (2) ◽  
pp. 310-314 ◽  
Author(s):  
Alessandro Ruffoni ◽  
Nicola Ferri ◽  
Andrea Pinto ◽  
Sara Pellegrino ◽  
Alessandro Contini ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Protein Protein Interaction ◽  
Remote Substituent

The remote substituent regiocontrol of phosphine free Heck hydroarylation has been exploited for the preparation of the first enantiopure inhibitor of Rac1–Tiam1 PPI.

Protein protein interaction of p53 and p73 with YY1 in human hepatocellular carcinoma

2011 ◽  
Vol 49 (01) ◽  
Author(s):  
LC Koenig ◽  
C Sandig ◽  
MH Bender ◽  
W Stremmel ◽  
M Müller-Schilling
Keyword(s):  
Hepatocellular Carcinoma ◽  
Protein Interaction ◽  
Human Hepatocellular Carcinoma ◽  
Protein Protein Interaction

An efficient transient assays system using Agrobacterium-mediated transformation of onion (Allium cepa) epidermal cells

2020 ◽  
Vol 80 (03) ◽  
Author(s):  
Yu-Miao Zhang ◽  
Jun Wang ◽  
Tao Wu
Keyword(s):  
Subcellular Localization ◽  
Protein Interaction ◽  
Protein Interactions ◽  
Epidermal Cells ◽  
Cyclin Dependent Kinase ◽  
Protein Subcellular Localization ◽  
Protein Protein Interactions ◽  
Efficient System ◽  
Protein Protein Interaction ◽  
Onion Epidermal Cells

In this study, the Agrobacterium infection medium, infection duration, detergent, and cell density were optimized. The sorghum-based infection medium (SbIM), 10-20 min infection time, addition of 0.01% Silwet L-77, and Agrobacterium optical density at 600 nm (OD600), improved the competence of onion epidermal cells to support Agrobacterium infection at >90% efficiency. Cyclin-dependent kinase D-2 (CDKD-2) and cytochrome c-type biogenesis protein (CYCH), protein-protein interactions were localized. The optimized procedure is a quick and efficient system for examining protein subcellular localization and protein-protein interaction.

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