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An enhanced recombinant amino-terminal acetylation system and novel in vivo high-throughput screen for molecules affection alpha-synuclein oligomerisation

Eastwood, T., Baker, Karen, Brooker, Holly, Frank, Stefanie, Mulvihill, Daniel P. (2017) An enhanced recombinant amino-terminal acetylation system and novel in vivo high-throughput screen for molecules affection alpha-synuclein oligomerisation. FEBS letters, 591 (6). pp. 833-841. ISSN 0014-5793. (doi:10.1002/1873-3468.12597) (KAR id:60373)

Abstract

Amino terminal acetylation is a ubiquitous protein modification affecting the majority of eukaryote proteins to regulate stability and function. We describe an optimised recombinant expression system for rapid production of aminoterminal-acetylated proteins within bacteria. We go on to describe the

system’s use in a fluorescence based in vivo assay for use in the highthroughput screen to identify drugs that impact amino-terminal acetylation

dependent oligomerisation. These new tools and protocols will allow researchers to enhance routine recombinant protein production and identify

new molecules for use in research and clinical applications.

Item Type: Article
DOI/Identification number: 10.1002/1873-3468.12597
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Susan Davies
Date Deposited: 14 Feb 2017 16:13 UTC
Last Modified: 04 Mar 2024 19:35 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/60373 (The current URI for this page, for reference purposes)

University of Kent Author Information

Eastwood, T..

Creator's ORCID:
CReDIT Contributor Roles:

Baker, Karen.

Creator's ORCID:
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Brooker, Holly.

Creator's ORCID:
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Frank, Stefanie.

Creator's ORCID:
CReDIT Contributor Roles:

Mulvihill, Daniel P..

Creator's ORCID: https://orcid.org/0000-0003-2502-5274
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