| Literature DB >> 23503679 |
Jian Zhu1,2,3, H Benjamin Larman1,4,5,2,3, Geng Gao1,2,3, Romel Somwar6, Zijuan Zhang7, Uri Laserson4,2,8, Alberto Ciccia1,2,3, Natalya Pavlova1,2,3, George Church4,2, Wei Zhang7, Santosh Kesari9, Stephen J Elledge1,2,3.
Abstract
Identifying physical interactions between proteins and other molecules is a critical aspect of biological analysis. Here we describe PLATO, an in vitro method for mapping such interactions by affinity enrichment of a library of full-length open reading frames displayed on ribosomes, followed by massively parallel analysis using DNA sequencing. We demonstrate the broad utility of the method for human proteins by identifying known and previously unidentified interacting partners of LYN kinase, patient autoantibodies, and the small-molecules gefitinib and dasatinib.Entities:
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Year: 2013 PMID： 23503679 PMCID： PMC4110636 DOI： 10.1038/nbt.2539
Source DB: PubMed Journal: Nat Biotechnol ISSN： 1087-0156 Impact factor: 54.908