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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. 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.

Combined Chemical Modification and Collision Induced Unfolding Using Native Ion Mobility‐Mass Spectrometry Provides Insights into Protein Gas‐Phase Structure (2021)
Journal Article
Al‐jabiry, A., Palmer, M., Langridge, J., Bellamy‐Carter, J., Robinson, D., & Oldham, N. J. (2021). Combined Chemical Modification and Collision Induced Unfolding Using Native Ion Mobility‐Mass Spectrometry Provides Insights into Protein Gas‐Phase Structure. Chemistry - A European Journal, 27(55), 13783-13792. https://doi.org/10.1002/chem.202101857

Native mass spectrometry is now an important tool in structural biology. Thus, the nature of higher protein structure in the vacuum of the mass spectrometer is an area of significant interest. One of the major goals in the study of gas-phase protein... Read More about Combined Chemical Modification and Collision Induced Unfolding Using Native Ion Mobility‐Mass Spectrometry Provides Insights into Protein Gas‐Phase Structure.

Iridoid Sex Pheromone Biosynthesis in Aphids Mimics Iridoid‐Producing Plants (2021)
Journal Article
Partridge, S. J., Withall, D. M., Caulfield, J. C., Pickett, J. A., Stockman, R. A., Oldham, N. J., & Birkett, M. A. (2021). Iridoid Sex Pheromone Biosynthesis in Aphids Mimics Iridoid‐Producing Plants. Chemistry - A European Journal, 27(25), 7231-7234. https://doi.org/10.1002/chem.202001356

Biosynthesis of (1R,4aS,7S,7aR)‐nepetalactol (1) and (4aS,7S,7aR)‐nepetalactone (2) in plants involves iridoid synthase (ISY), an atypical reductive cyclase that catalyses the reduction of 8‐oxogeranial into the reactive enol of (S)‐8‐oxocitronellal,... Read More about Iridoid Sex Pheromone Biosynthesis in Aphids Mimics Iridoid‐Producing Plants.