210107-38-3Relevant articles and documents
Photoaffinity palladium reagents for capture of protein-protein interactions
Zheng, Qizhen,Pang, Zhengyuan,Liu, Jingwei,Zhou, Yi,Sun, Yang,Yin, Zheng,Lou, Zhiyong
supporting information, p. 6369 - 6373 (2019/07/09)
Protein-protein interactions (PPIs) are indispensable in almost all cellular processes. Probing of complex PPIs provides new insights into the biological system of interest and paves the way for the development of therapeutics. Herein, we report a strategy for the capture of protein-protein interactions using photoaffinity palladium reagents. First, the palladium-mediated reagent site specifically transferred a photoaffinity modified aryl group to the designated cysteine residue. Next, the photoaffinity group was activated by UV radiation to trap the proximal protein residue for the formation of a crosslink. This strategy was used to capture the PYL-ABA-PP2C interaction, which is at the core of the abscisic acid (ABA) signalling pathway. Our results indicated that this palladium-mediated strategy can serve as an alternative for incorporating an increasing number of diverse substrates for protein crosslinking through cysteine modifications and can be explored for use in mapping protein-peptide or protein-protein interaction surfaces and in trapping potential interacting partners.
Compounds, Compositions and Methods
-
Page/Page column 19, (2010/11/28)
Compounds useful for treating cellular proliferative diseases and disorders by modulating the activity of KSP are disclosed.
Synthesis of a new photo-cross-linking nucleoside analogue containing an aryl(trifluoromethyl)diazirine group: Application for EcoRII and MvaI restriction-modification enzymes
Topin, Andrey N.,Gritsenko, Oxana M.,Brevnov, Maxim G.,Gromova, Elisaveta S.,Korshunova, Galina A.
, p. 1163 - 1175 (2007/10/03)
A new photo-cross-linking dU analog, 5-[4-(3-(trifluoromethyl)-3H- diazirin-3-yl)phenyl]-2'-deoxyuridine, was synthesized and incorporated into the recognition site of EcoRII and MvaI restriction-modification enzymes. The resulting base-modified 14-mer su