Article

An E2-ubiquitin thioester-driven approach to identify substrates modified with ubiquitin and ubiquitin-like molecules

2018-10-10

Abstract excerpt

Covalent modifications of proteins with ubiquitin and ubiquitin-like molecules are instrumental to many biological processes. However, identifying the E3 ligase responsible for these modifications remains a major bottleneck in ubiquitin research. Here, we present an E2-thioester-driven identification (E2~dID) method for the targeted identification of substrates of specific E2 and E3 enzyme pairs. E2~dID exploits t...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 974348ca-381a-54d9-9950-fe7e86f9b359
DOI: 10.1101/387670

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

An E2-ubiquitin thioester-driven approach to identify substrates modified with ubiquitin and ubiquitin-like moleculesDOI 10.1101/387670Read

E2 enzymes: more than just middle menSemantic proximity Read

A comprehensive framework of E2-RING E3 interactions of the human ubiquitin-proteasome system.Semantic proximity Read

Ubiquitin becomes ubiquitous in cancerSemantic proximity Read

The use of ubiquitin lysine mutants to characterize E2-E3 linkage specificity: Mass spectrometry offers a cautionary "tail".Semantic proximity Read

Protein degradation by small tag artificial bacterial E3 ligaseSemantic proximity Read

New Insights into the Role of E2s in the Pathogenesis of Diseases: Lessons Learned from UBE2O.Semantic proximity Read

Proteome-wide identification of SUMO2 modification sites.Semantic proximity Read

Defining the SUMO-modified proteome by multiple approaches in Saccharomyces cerevisiae.Semantic proximity Read

A ubiquitin-specific, proximity-based labeling approach for the identification of ubiquitin ligase substratesSemantic proximity Read

Improved identification of SUMO attachment sites using C-terminal SUMO mutants and tailored protease digestion strategies.Semantic proximity Read

In Vivo Identification of Human Small Ubiquitin-like Modifier Polymerization Sites by High Accuracy Mass Spectrometry and an in Vitro to in Vivo StrategySemantic proximity Read

Structural and biophysical characterisation of ubiquitin variants that specifically inhibit the ubiquitin conjugating enzyme Ube2d2Semantic proximity Read