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An ALS-associated variant of the autophagy receptor SQSTM1/p62 reprograms binding selectivity toward the autophagy-related hATG8 proteins (2021)
Journal Article
Brennan, A., Layfield, R., Long, J., Williams, H. E., Oldham, N. J., Scott, D., & Searle, M. S. (2022). An ALS-associated variant of the autophagy receptor SQSTM1/p62 reprograms binding selectivity toward the autophagy-related hATG8 proteins. Journal of Biological Chemistry, 298(2), Article 101514. https://doi.org/10.1016/j.jbc.2021.101514

Recognition of human autophagy-related 8 (hATG8) proteins by autophagy receptors represents a critical step within this cellular quality control system. Autophagy impairment is known to be a pathogenic mechanism in the motor neuron disorder amyotroph... Read More about An ALS-associated variant of the autophagy receptor SQSTM1/p62 reprograms binding selectivity toward the autophagy-related hATG8 proteins.

Site-Selective Installation of Nϵ-Modified Sidechains into Peptide and Protein Scaffolds via Visible-Light-Mediated Desulfurative C–C Bond Formation (2021)
Journal Article
Griffiths, R. C., Smith, F. R., Long, J. E., Scott, D., Williams, H. E., Oldham, N. J., …Mitchell, N. J. (2022). Site-Selective Installation of Nϵ-Modified Sidechains into Peptide and Protein Scaffolds via Visible-Light-Mediated Desulfurative C–C Bond Formation. Angewandte Chemie International Edition, 61(2), Article e202110223. https://doi.org/10.1002/anie.202110223

Post-translational modifications (PTMs) enhance the repertoire of protein function and mediate or influence the activity of many cellular processes. The preparation of site-specifically and homogeneously modified proteins, to apply as tools to unders... Read More about Site-Selective Installation of Nϵ-Modified Sidechains into Peptide and Protein Scaffolds via Visible-Light-Mediated Desulfurative C–C Bond Formation.

Site‐Selective Installation of Nϵ ‐Modified Sidechains into Peptide and Protein Scaffolds via Visible‐Light‐Mediated Desulfurative C–C Bond Formation (2021)
Journal Article
Griffiths, R. C., Smith, F. R., Long, J. E., Scott, D., Williams, H. E. L., Oldham, N. J., …Mitchell, N. J. (2022). Site‐Selective Installation of Nϵ ‐Modified Sidechains into Peptide and Protein Scaffolds via Visible‐Light‐Mediated Desulfurative C–C Bond Formation. Angewandte Chemie, 134(2), Article e202110223. https://doi.org/10.1002/ange.202110223

Post-translational modifications (PTMs) enhance the repertoire of protein function and mediate or influence the activity of many cellular processes. The preparation of site-specifically and homogeneously modified proteins, to apply as tools to unders... Read More about Site‐Selective Installation of Nϵ ‐Modified Sidechains into Peptide and Protein Scaffolds via Visible‐Light‐Mediated Desulfurative C–C Bond Formation.

Modification of small ubiquitin-related modifier 2 (SUMO2) by phosphoubiquitin in HEK293T cells (2021)
Journal Article
Dongdem, J. T., Dawson, S. P., & Layfield, R. (2021). Modification of small ubiquitin-related modifier 2 (SUMO2) by phosphoubiquitin in HEK293T cells. Proteomics, 21(15), Article 2000234. https://doi.org/10.1002/pmic.202000234

Additional complexity in the post-translational modification of proteins by ubiquitin is achieved by ubiquitin phosphorylation, for example within PINK1-parkin mediated mitophagy. We performed a preliminary proteomic analysis to identify proteins dif... Read More about Modification of small ubiquitin-related modifier 2 (SUMO2) by phosphoubiquitin in HEK293T cells.

p62 overexpression induces TDP-43 cytoplasmic mislocalisation, aggregation and cleavage and neuronal death (2021)
Journal Article
Foster, A. D., Flynn, L. L., Cluning, C., Cheng, F., Davidson, J. M., Lee, A., …Rea, S. L. (2021). p62 overexpression induces TDP-43 cytoplasmic mislocalisation, aggregation and cleavage and neuronal death. Scientific Reports, 11(1), Article 11474. https://doi.org/10.1038/s41598-021-90822-2

Amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD) that exist on a spectrum of neurodegenerative disease. A hallmark of pathology is cytoplasmic TDP-43 aggregates within neurons, observed in 97% of ALS cases and ~ 50% of... Read More about p62 overexpression induces TDP-43 cytoplasmic mislocalisation, aggregation and cleavage and neuronal death.