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Dataset associated with 'The effect of mutation on an aggregation-prone protein: An in vivo, in vitro and in silico analysis'.

Guthertz, N. and Van der Kant, R. and Smit, H. and Martinez, M. and Xu, Y. and Trinh, C. and Iorga, B.I. and Rousseau, F. and Schymkowitz, J. and Brockwell, D.J. and Radford, S.E. (2022) Dataset associated with 'The effect of mutation on an aggregation-prone protein: An in vivo, in vitro and in silico analysis'. University of Leeds. [Dataset] https://doi.org/10.5518/1073

Dataset description

Aggregation of initially stably structured proteins is involved in more than 20 human amyloid diseases. Despite intense research, however, how this class of proteins assembles into amyloid fibrils remains poorly understood. We address this question using β2-microglobulin (β2m) as a model system, focusing on D76N-β2m that is involved in hereditary amyloidosis. Here, we identify the residues key to protect β2m from aggregation and we show that residue 76 has a unique ability to drive β2m aggregation in vivo and in vitro.

Keywords: Amyloid, protein aggregation, β2-microglobulin, aggregation prone region
Subjects: C000 - Biological sciences > C700 - Molecular biology, biophysics & biochemistry > C790 - Molecular biology, biophysics & biochemistry not elsewhere classified
Divisions: Faculty of Biological Sciences > School of Biology
Faculty of Biological Sciences > School of Molecular and Cellular Biology
Related resources:
LocationType
https://doi.org/10.1073/pnas.2200468119Publication
https://eprints.whiterose.ac.uk/186372/Publication
License: Creative Commons Attribution 4.0 International (CC BY 4.0)
Date deposited: 24 May 2022 17:03
URI: http://archive.researchdata.leeds.ac.uk/id/eprint/967

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