Daniel Scott

Contact

• workRoom D42 Medical School Building
  Queen's Medical Centre
  Nottingham
  NG7 2UH
  UK
• Daniel.Scott@nottingham.ac.uk

Research Summary

An MND Assocation Junior Non-Clinical Fellow investigating N-end autophagy in ALS pathogenesis.

Selected Publications

• MANZI L, BARROW AS, SCOTT D, LAYFIELD R, WRIGHT TG, MOSES JE and OLDHAM NJ, 2016. Carbene footprinting accurately maps binding sites in protein-ligand and protein-protein interactions. Nature Communications. 7, 13288
• GOODE A, BUTLER K, LONG J, CAVEY J, SCOTT D, SHAW B, SOLLENBERGER J, GELL C, JOHANSEN T, OLDHAM NJ, SEARLE MS and LAYFIELD R, 2016. Defective recognition of LC3B by mutant SQSTM1/p62 implicates impairment of autophagy as a pathogenic mechanism in ALS-FTLD. Autophagy. 12(7), 1094-104
• SCOTT, DANIEL, OLDHAM, NEIL J., STRACHAN, JO, SEARLE, MARK S. and LAYFIELD, ROBERT, 2015. Ubiquitin-binding domains: Mechanisms of ubiquitin recognition and use as tools to investigate ubiquitin-modified proteomes PROTEOMICS. 15(5-6), 844-861

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• GOODE A, BUTLER K, LONG J, CAVEY J, SCOTT D, SHAW B, SOLLENBERGER J, GELL C, JOHANSEN T, OLDHAM NJ, SEARLE MS and LAYFIELD R, 2016. Defective recognition of LC3B by mutant SQSTM1/p62 implicates impairment of autophagy as a pathogenic mechanism in ALS-FTLD. Autophagy. 12(7), 1094-104
• SCOTT D, STRACHAN J, KRISHNA VG, SHAW B, TOOTH DJ, SEARLE MS, OLDHAM NJ and LAYFIELD R, 2016. Method for the Purification of Endogenous Unanchored Polyubiquitin Chains. Methods in Molecular Biology. 1449, 203-13
• MANZI L, BARROW AS, SCOTT D, LAYFIELD R, WRIGHT TG, MOSES JE and OLDHAM NJ, 2016. Carbene footprinting accurately maps binding sites in protein-ligand and protein-protein interactions. Nature Communications. 7, 13288
• SCOTT D, GARNER TP, LONG J, STRACHAN J, MISTRY SC, BOTTRILL AR, TOOTH DJ, SEARLE MS, OLDHAM NJ and LAYFIELD R, 2016. Mass spectrometry insights into a tandem ubiquitin-binding domain hybrid engineered for the selective recognition of unanchored polyubiquitin. Proteomics. 16(14), 1961-9
• SCOTT D, LAYFIELD R and OLDHAM NJ, 2015. Structural Insights into Interactions between Ubiquitin Specific Protease 5 and its Polyubiquitin substrates by Mass Spectrometry and Ion Mobility Spectrometry. Protein Science. 24(8), 1257-63
• SCOTT, DANIEL, LAYFIELD, ROBERT and OLDHAM, NEIL J., 2015. Ion mobility-mass spectrometry reveals conformational flexibility in the deubiquitinating enzyme USP5. PROTEOMICS. 15(16), 2835-2841
• SCOTT, DANIEL, OLDHAM, NEIL J., STRACHAN, JO, SEARLE, MARK S. and LAYFIELD, ROBERT, 2015. Ubiquitin-binding domains: Mechanisms of ubiquitin recognition and use as tools to investigate ubiquitin-modified proteomes PROTEOMICS. 15(5-6), 844-861