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A Versatile Platform to Analyze Low-Af

Resource A Versatile Platform to Analyze Low-Affinity and Transient Protein-Protein Interactions in Living Cells in Real Time

Graphical Abstract

Highlights

ReBiL is able to detect low-affinity,transient protein-protein in-teractions in cells

ReBiL has a superior signal-to-noise ratio compared to other available methods

ReBiL reveals the kinetics of PPI disruption by antagonists

ReBiL reveals the mode of action of stapled peptides Authors

Yao-Cheng Li,Luo Wei Rodewald,..., Kenneth F.Wertman,Geoffrey M.Wahl

Correspondence

wahl@http://batistapd.com/doc/f798c81f02768e9950e73804.html

In Brief

Li et al.developed a recombinase-enhanced bimolecular luciferase comple-mentation platform,termed ReBiL,to evaluate low-affinity protein-protein inter-actions(PPIs)that are not detectable by other methods and to analyze PPI antag-onists in living cells.ReBiL showed that small-molecule p53-Mdm2antagonists disrupt their intended targets effectively in cells,whereas stapled peptides did not.Stapled peptides unexpectedly induced cell membrane disruption result-ing in p53-independent death associated with cytoplasmic leakage.ReBiL is also valuable for high-throughput screening and for deciphering signaling mecha-nisms mediated by protein

A Versatile Platform to Analyze Low-Af

interactions. Li et al.,2014,Cell Reports9,1–13

December11,2014ª2014The Authors

http://batistapd.com/doc/f798c81f02768e9950e73804.html/10.1016/j.celrep.2014.10.058