All Outputs (13)

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.

A convenient model of serum-induced reactivity of human astrocytes to investigate astrocyte-derived extracellular vesicles (2024)
Journal Article
White, K. E., Bailey, H. L., Shaw, B. S., Geiszler, P. C., Mesquita-Ribeiro, R., Scott, D., Layfield, R., & Serres, S. (2024). A convenient model of serum-induced reactivity of human astrocytes to investigate astrocyte-derived extracellular vesicles. Frontiers in Cellular Neuroscience, 18, Article 1414142. https://doi.org/10.3389/fncel.2024.1414142

Extracellular vesicles (EVs) are secreted by all cells in the CNS, including neurons and astrocytes. EVs are lipid membrane enclosed particles loaded with various bioactive cargoes reflecting the dynamic activities of cells of origin. In contrast to... Read More about A convenient model of serum-induced reactivity of human astrocytes to investigate astrocyte-derived extracellular vesicles.

Spaceflight Induces Strength Decline in Caenorhabditis elegans (2023)
Journal Article
Soni, P., Edwards, H., Anupom, T., Rahman, M., Lesanpezeshki, L., Blawzdziewicz, J., Cope, H., Gharahdaghi, N., Scott, D., Toh, L. S., Williams, P. M., Etheridge, T., Szewczyk, N., Willis, C. R. G., & Vanapalli, S. A. (2023). Spaceflight Induces Strength Decline in Caenorhabditis elegans. Cells, 12(20), Article 2470. https://doi.org/10.3390/cells12202470

Background: Understanding and countering the well-established negative health consequences of spaceflight remains a primary challenge preventing safe deep space exploration. Targeted/personalized therapeutics are at the forefront of space medicine st... Read More about Spaceflight Induces Strength Decline in Caenorhabditis elegans.

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.

Enhanced Cellular Transduction of Nanoparticles Resistant to Rapidly Forming Plasma Protein Coronas (2020)
Journal Article
Blokpoel Ferreras, L. A., Scott, D., Vazquez Reina, S., Roach, P., Torres, T. E., Goya, G. F., Shakesheff, K. M., & Dixon, J. E. (2020). Enhanced Cellular Transduction of Nanoparticles Resistant to Rapidly Forming Plasma Protein Coronas. Advanced Biosystems, 4(10), Article 2000162. https://doi.org/10.1002/adbi.202000162

© 2020 The Authors. Published by Wiley-VCH GmbH Nanoparticles (NPs) are increasingly being developed as biomedical platforms for drug/nucleic acid delivery and imaging. However, in biological fluids, NPs interact with a wide range of proteins that fo... Read More about Enhanced Cellular Transduction of Nanoparticles Resistant to Rapidly Forming Plasma Protein Coronas.

Design, synthesis and evaluation of E2-25K derived stapled peptides (2020)
Journal Article
Watson, M. E., Scott, D., Jamieson, C., Layfield, R., & Mason, A. M. (2021). Design, synthesis and evaluation of E2-25K derived stapled peptides. Peptide Science, 113(1), Article e24158. https://doi.org/10.1002/pep2.24158

© 2020 The Authors. Peptide Science published by Wiley Periodicals, Inc. Stabilised peptides are now established as potential drug candidates to probe previously intractable molecular targets, such as protein-protein interactions. Herein, we report t... Read More about Design, synthesis and evaluation of E2-25K derived stapled peptides.

Molecular insights into an ancient form of Paget's disease of bone (2019)
Journal Article
Shaw, B., Burrell, C. L., Green, D., Navarro-Martinez, A., Scott, D., Daroszewska, A., van't Hof, R., Smith, L., Hargrave, F., Mistry, S., Bottrill, A., Kessler, B., Fisher, R., Singh, A., Dalmay, T., Fraser, W. D., Henneberger, K., King, T., Gonzalez, S., & Layfield, R. (2019). Molecular insights into an ancient form of Paget's disease of bone. Proceedings of the National Academy of Sciences, 116(21), 10463-10472. https://doi.org/10.1073/pnas.1820556116

We identify an ancient and atypical form of Paget’s disease of bone (PDB) in a collection of medieval skeletons exhibiting unusually extensive pathological changes, high disease prevalence, and low age-at-death estimations. Proteomic analysis of anci... Read More about Molecular insights into an ancient form of Paget's disease of bone.

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., Tooth, D. J., Searle, M. S., Oldham, N. J., & 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.

Defective recognition of LC3B by mutant SQSTM1/p62 implicates impairment of autophagy as a pathogenic mechanism in ALS-FTLD (2016)
Journal Article
Goode, A., Butler, K., Long, J., Cavey, J., Scott, D., Shaw, B., Sollenberger, J., Gell, C., Johansen, T., Oldham, N. J., Searle, M., & 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), 1094-1104. https://doi.org/10.1080/15548627.2016.1170257

Growing evidence implicates impairment of autophagy as a candidate pathogenic mechanism in the spectrum of neurodegenerative disorders which includes amyotrophic lateral sclerosis and frontotemporal lobar degeneration (ALS-FTLD). SQSTM1, which encode... Read More about Defective recognition of LC3B by mutant SQSTM1/p62 implicates impairment of autophagy as a pathogenic mechanism in ALS-FTLD.

Ion mobility-mass spectrometry reveals conformational flexibility in the deubiquitinating enzyme USP5 (2015)
Journal Article
Scott, D., Layfield, R., & Oldham, N. J. (2015). Ion mobility-mass spectrometry reveals conformational flexibility in the deubiquitinating enzyme USP5. Proteomics, 15(16), https://doi.org/10.1002/pmic.201400457

Many proteins exhibit conformation flexibility as part of their biological function, whether through the presence of a series of well-defined states or by the existence of intrinsic disorder. Ion mobility spectrometry, in combination with MS (IM–MS),... Read More about Ion mobility-mass spectrometry reveals conformational flexibility in the deubiquitinating enzyme USP5.