Outputs (16)

Determination of hATG8 Binding Selectivity of AIM (Autophagy-Interacting Motif) Peptides Using Native Electrospray Ionization Mass Spectrometry (2024)
Book Chapter
Brennan, A., Oldham, N., Layfield, R., & Scott, D. (2024). Determination of hATG8 Binding Selectivity of AIM (Autophagy-Interacting Motif) Peptides Using Native Electrospray Ionization Mass Spectrometry. In I. P. Nezis (Ed.), Selective autophagy: methods and protocols (237-246). Springer. https://doi.org/10.1007/978-1-0716-4067-8_19

Establishing the hATG8 binding selectivity of AIM (autophagy-interacting motif) sequences found within autophagy system proteins provides insights into their biological roles, and in the case of disease-associated AIM mutations, potential pathophysio... Read More about Determination of hATG8 Binding Selectivity of AIM (Autophagy-Interacting Motif) Peptides Using Native Electrospray Ionization Mass Spectrometry.

Antibody-based sex determination of human skeletal remains (2023)
Journal Article
Shaw, B., Foggin, S., Hamilton-Stanley, P., Barlow, A., Pickard, C., Fibiger, L., Oldham, N., Tighe, P., Kootker, L. M., Schrader, S., & Layfield, R. (2023). Antibody-based sex determination of human skeletal remains. iScience, 26(11), Article 108191. https://doi.org/10.1016/j.isci.2023.108191

Assignment of biological sex to skeletal remains is critical in the accurate reconstruction of the past. Analysis of sex-chromosome encoded AMELX and AMELY peptides from the enamel protein amelogenin underpins a minimally destructive mass spectrometr... Read More about Antibody-based sex determination of human skeletal remains.

Osteological, multi-isotope and proteomic analysis of poorly-preserved human remains from a Dutch East India Company burial ground in South Africa (2023)
Journal Article
Olszewski, J., Hall, R. A., Kootker, L. M., Oldham, N. J., Layfield, R., Shaw, B., Derksen, L., Manders, M., Hart, T., & Schrader, S. A. (2023). Osteological, multi-isotope and proteomic analysis of poorly-preserved human remains from a Dutch East India Company burial ground in South Africa. Scientific Reports, 13, Article 14666. https://doi.org/10.1038/s41598-023-41503-9

Skeletal remains discovered in Simon’s Town, South Africa, were hypothesised as being associated with a former Dutch East India Company (VOC) hospital. We report a novel combined osteological and biochemical approach to these poorly-preserved remains... Read More about Osteological, multi-isotope and proteomic analysis of poorly-preserved human remains from a Dutch East India Company burial ground in South Africa.

Cysteine-Selective Modification of Peptides and Proteins via Desulfurative C−C Bond Formation (2023)
Journal Article
Griffiths, R. C., Smith, F. R., Li, D., Wyatt, J., Rogers, D. M., Long, J. E., Cusin, L. M. L., Tighe, P. J., Layfield, R., Hirst, J. D., Muller, M. M., & Mitchell, N. (2023). Cysteine-Selective Modification of Peptides and Proteins via Desulfurative C−C Bond Formation. Chemistry - A European Journal, 29(16), Article e202202503. https://doi.org/10.1002/chem.202202503

The site-selective modification of peptides and proteins facilitates the preparation of targeted therapeutic agents and tools to interrogate biochemical pathways. Among the numerous bioconjugation techniques developed to install groups of interest, t... Read More about Cysteine-Selective Modification of Peptides and Proteins via Desulfurative C−C Bond Formation.

Comparative analysis of protein expression systems and PTM landscape in the study of transcription factor ELK-1 (2022)
Journal Article
Ducker, C., Ratnam, M., Shaw, P. E., & Layfield, R. (2023). Comparative analysis of protein expression systems and PTM landscape in the study of transcription factor ELK-1. Protein Expression and Purification, 203, Article 106216. https://doi.org/10.1016/j.pep.2022.106216

Post-translational modifications (PTMs) are important for protein folding and activity, and the ability to recreate physiologically relevant PTM profiles on recombinantly-expressed proteins is vital for meaningful functional analysis. The ETS transcr... Read More about Comparative analysis of protein expression systems and PTM landscape in the study of transcription factor ELK-1.

Developing Porous Ortho- and Pyrophosphate-Containing Glass Microspheres; Structural and Cytocompatibility Characterisation (2022)
Journal Article
Milborne, B., Murrell, L., Cardillo-Zallo, I., Titman, J., Briggs, L., Scotchford, C., Thompson, A., Layfield, R., & Ahmed, I. (2022). Developing Porous Ortho- and Pyrophosphate-Containing Glass Microspheres; Structural and Cytocompatibility Characterisation. Bioengineering, 9(11), Article 611. https://doi.org/10.3390/bioengineering9110611

Phosphate-based glasses (PBGs) are promising materials for bone repair and regeneration as they can be formulated to be compositionally similar to the inorganic components of bone. Alterations to the PBG formulation can be used to tailor their degrad... Read More about Developing Porous Ortho- and Pyrophosphate-Containing Glass Microspheres; Structural and Cytocompatibility Characterisation.

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., Layfield, R., & 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., Layfield, R., & 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.

Site‐Selective Modification of Peptides and Proteins via Interception of Free‐Radical‐Mediated Dechalcogenation (2020)
Journal Article
Griffiths, R. C., Smith, F. R., Long, J. E., Williams, H. E. L., Layfield, R., & Mitchell, N. J. (2020). Site‐Selective Modification of Peptides and Proteins via Interception of Free‐Radical‐Mediated Dechalcogenation. Angewandte Chemie, 132(52), 23867-23875. https://doi.org/10.1002/ange.202006260

The development of site-selective chemistry targeting the canonical amino acids enables the controlled installation of desired functionalities into native peptides and proteins. Such techniques facilitate the development of polypeptide conjugates to... Read More about Site‐Selective Modification of Peptides and Proteins via Interception of Free‐Radical‐Mediated Dechalcogenation.