Dr Matthew Jackson

Research Fellow
School of Molecular and Cellular Biology

Contact: 9.56e, +44(0) 113 34 37823, email address for  

Martin EM, Jackson MP, Gamerdinger M, Gense K, Karamanos TK, Humes JR, Deuerling E, Ashcroft AE, Radford SE Conformational flexibility within the nascent polypeptide-associated complex enables its interactions with structurally diverse client proteins. The Journal of biological chemistry, 2018
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Doherty CPA, Young LM, Karamanos TK, Smith HI, Jackson MP, Radford SE, Brockwell DJ A peptide-display protein scaffold to facilitate single molecule force studies of aggregation-prone peptides. Protein science : a publication of the Protein Society, 2018
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Jackson MP, Hewitt EW Why are functional amyloids non‐toxic in humans? Biomolecules 7, 2017
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Jackson MP, Hewitt EW Cellular proteostasis: Degradation of misfolded proteins by lysosomes Essays in Biochemistry 60 173-180, 2016
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Iadanza MG, Jackson MP, Radford SE, Ranson NA MpUL-multi: Software for Calculation of Amyloid Fibril Mass per Unit Length from TB-TEM Images Scientific Reports 6, 2016
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Saunders JC, Young LM, Mahood RA, Jackson MP, Revill CH, Foster RJ, Smith DA, Ashcroft AE, Brockwell DJ, Radford SE An in vivo platform for identifying inhibitors of protein aggregation Nature Chemical Biology 12 94-101, 2016
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Jakhria T, Hellewell AL, Porter MY, Jackson MP, Tipping KW, Xue WF, Radford SE, Hewitt EW β2-microglobulin amyloid fibrils are nanoparticles that disrupt lysosomal membrane protein trafficking and inhibit protein degradation by lysosomes Journal of Biological Chemistry 289 35781-35794, 2014
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