Outputs (9)

Antibody-based sex determination of human skeletal remains (2023)
Journal Article
Shaw, B., Foggin, S., Hamilton-Stanley, P., Barlow, A., Pickard, C., Fibiger, L., …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., …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.

Ferric quinate (QPLEX) interacts with the major outer membrane protein (MOMP) of Campylobacter jejuni and enters through the porin channel into the periplasmic space (2022)
Journal Article
Okoye, J. C., Bellamy-Carter, J., Oldham, N. J., Oldfield, N. J., Mahdavi, J., & Soultanas, P. (2022). Ferric quinate (QPLEX) interacts with the major outer membrane protein (MOMP) of Campylobacter jejuni and enters through the porin channel into the periplasmic space. Computational and Structural Biotechnology Journal, 20, 5355-5363. https://doi.org/10.1016/j.csbj.2022.09.032

Ferric chelates like ferric tyrosinate (TYPLEX) and the closely related ferric quinate (QPLEX) are structural mimics of bacterial siderophores. TYPLEX has been trialled as a feed additive in farming of commercial broilers, reducing Campylobacter load... Read More about Ferric quinate (QPLEX) interacts with the major outer membrane protein (MOMP) of Campylobacter jejuni and enters through the porin channel into the periplasmic space.

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.

Carbene footprinting accurately maps binding sites in protein–ligand and protein–protein interactions (2016)
Journal Article
Manzi, L., Barrow, A. S., Scott, D., Layfield, R., Wright, T. G., Moses, J. E., & Oldham, N. J. (2016). Carbene footprinting accurately maps binding sites in protein–ligand and protein–protein interactions. Nature Communications, 7, Article 13288. https://doi.org/10.1038/ncomms13288

Specific interactions between proteins and their binding partners are fundamental to life processes. The ability to detect protein complexes, and map their sites of binding, is crucial to understanding basic biology at the molecular level. Methods th... Read More about Carbene footprinting accurately maps binding sites in protein–ligand and protein–protein interactions.

Mass spectrometry insights into a tandem ubiquitin-binding domain hybrid engineered for the selective recognition of unanchored polyubiquitin (2016)
Journal Article
Scott, D., Garner, T. P., Long, J., Strachan, J., Mistry, S. C., Bottrill, A. R., …Layfield, R. (in press). Mass spectrometry insights into a tandem ubiquitin-binding domain hybrid engineered for the selective recognition of unanchored polyubiquitin. Proteomics, 16(14), https://doi.org/10.1002/pmic.201600067

Unanchored polyubiquitin chains are emerging as importanregulators of cellular physiology with diverse roles paralleling those of substrate-conjugated polyubiquitin. However tools able to discriminate unanchored polyubiquitin chains of different isop... Read More about Mass spectrometry insights into a tandem ubiquitin-binding domain hybrid engineered for the selective recognition of unanchored polyubiquitin.

Genomic analysis of serogroup Y Neisseria meningitidis isolates reveals extensive similarities between carriage and disease-associated organisms (2016)
Journal Article
Oldfield, N. J., Harrison, O. B., Bayliss, C. D., Maiden, M. C., Ala'Aldeen, D. A., & Turner, D. P. (2016). Genomic analysis of serogroup Y Neisseria meningitidis isolates reveals extensive similarities between carriage and disease-associated organisms. Journal of Infectious Diseases, 213(11), 1777-1785. https://doi.org/10.1093/infdis/jiw008

Background. Neisseria meningitidis is a frequent colonizer of the human nasopharynx with asymptomatic carriage providing the reservoir for invasive, disease-causing strains. Serogroup Y (MenY) strains are a major cause of meningococcal disease. High... Read More about Genomic analysis of serogroup Y Neisseria meningitidis isolates reveals extensive similarities between carriage and disease-associated organisms.