Professor Olwyn Byron

  • Professor of Biophysics (Bacteriology)
  • Director of Education (Immunology & Infection)

telephone: 01413303752
email: Olwyn.Byron@glasgow.ac.uk

B2-11, Sir Graeme Davies Building, University of Glasgow, 120 University Place, Glasgow, G12 8TA

Import to contacts

ORCID iDhttps://orcid.org/0000-0001-7857-4520

Research interests

Research Interests

We specialise in understanding the solution behaviour of biological macromolecules and their complexes. We do this by utilising a number of biophysical techniques to determine the solution shape of molecules and the strength, stoichiometry and architecture of the complexes they form.  We collaborate widely and offer expertise in the application of our core methodologies including:

  • Analytical ultracentrifugation (AUC)
  • Small angle X-ray scattering (SAXS)
  • Small angle neutron scattering (SANS)
  • Hydrodynamic bead modelling (HBM)

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Publications

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Number of items: 85.

2022

Miguel-Romero, L., Alqasmi, M., Bacarizo, J., Tan, J. A., Cogdell, R. J. , Chen, J., Byron, O. , Christie, G. E., Marina, A. and Penadés, J. R. (2022) Non-canonical Staphylococcus aureus pathogenicity island repression. Nucleic Acids Research, 50(19), pp. 11109-11127. (doi: 10.1093/nar/gkac855) (PMID:36200825) (PMCID:PMC9638917)

2021

Rocco, M., Brookes, E. and Byron, O. (2021) US-SOMO: Methods for Construction and Hydration of Macromolecular Hydrodynamic Models. In: Roberts, G., Watts, A. and European Biophysical Societies, (eds.) Encyclopedia of Biophysics. Springer: Berlin, Heidelberg. ISBN 9783642359439 (doi: 10.1007/978-3-642-35943-9_292-1)

2020

Azmi, L., Bragginton, E. C., Cadby, I. T., Byron, O. , Roe, A. J. , Lovering, A. L. and Gabrielsen, M. (2020) High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE. Acta Crystallographica. Section F: Structural Biology Communications, 76(9), pp. 414-421. (doi: 10.1107/S2053230X20010237)

Kim, G., Yang, J., Jang, J., Choi, J.-S., Roe, A. J. , Byron, O. , Seok, C. and Song, J.-J. (2020) Aldehyde-alcohol dehydrogenase undergoes structural transition to form extended spirosomes for substrate channeling. Communications Biology, 3, 298. (doi: 10.1038/s42003-020-1030-1) (PMID:32523125) (PMCID:PMC7286902)

Medina-Pritchard, B., Lazou, V., Zuo, J., Byron, O. , Abad, M. A., Rappsilber, J., Heun, P. and Jeyaprakash, A. A. (2020) Structural basis for centromere maintenance by Drosophila CENP-A chaperone CAL1. EMBO Journal, 39(7), e103234. (doi: 10.15252/embj.2019103234) (PMID:32134144) (PMCID:PMC7110144)

2019

Kim, G., Azmi, L., Jang, S., Jung, T., Hebert, H., Roe, A. J. , Byron, O. and Song, J.-J. (2019) Aldehyde-alcohol dehydrogenase forms a high-order spirosome architecture critical for its activity. Nature Communications, 10, 4527. (doi: 10.1038/s41467-019-12427-8) (PMID:31586059) (PMCID:PMC6778083)

Conley, M. J. , McElwee, M., Azmi, L., Gabrielsen, M. , Byron, O. , Goodfellow, I. G. and Bhella, D. (2019) Calicivirus VP2 forms a portal-like assembly following receptor engagement. Nature, 565(7739), pp. 377-381. (doi: 10.1038/s41586-018-0852-1) (PMID:30626974)

2018

Byron, O. , Nischang, I. and Patel, T. R. (2018) Analytical ultracentrifugation (AUC): a seminal tool offering multiple solutions. European Biophysics Journal, 47(7), pp. 693-696. (doi: 10.1007/s00249-018-1333-z) (PMID:30218114)

Dias Mirandela, G. et al. (2018) Merging in-solution x-ray and neutron scattering data allows fine structural analysis of membrane–protein detergent complexes. Journal of Physical Chemistry Letters, 9(14), pp. 3910-3914. (doi: 10.1021/acs.jpclett.8b01598) (PMID:29939747)

Marciano, G., Da Vela, S., Tria, G., Svergun, D. I., Byron, O. and Huang, D. T. (2018) Structure specific recognition protein-1 (SSRP1) is an elongated homodimer that binds histones. Journal of Biological Chemistry, 293(26), pp. 10071-10083. (doi: 10.1074/jbc.RA117.000994) (PMID:29764934) (PMCID:PMC6028955)

2017

Byron, O. and Lindsay, J. G. (2017) The pyruvate dehydrogenase complex and related assemblies in health and disease. In: Harris, J. R. and Marles-Wright, J. (eds.) Macromolecular Protein Complexes. Series: Subcellular biochemistry (83). Springer, pp. 523-550. ISBN 9783319465012 (doi: 10.1007/978-3-319-46503-6_19)

2016

Grinter, R. et al. (2016) Structure of the bacterial plant-ferredoxin receptor FusA. Nature Communications, 7, 13308. (doi: 10.1038/ncomms13308) (PMID:27796364) (PMCID:PMC5095587)

Klein, A., Wojdyla, J. A., Joshi, A., Josts, I., McCaughey, L. C. , Housden, N. G., Kaminska, R., Byron, O. , Walker, D. and Kleanthous, C. (2016) Structural and biophysical analysis of nuclease protein antibiotics. Biochemical Journal, 473(18), pp. 2799-2812. (doi: 10.1042/bcj20160544) (PMID:27402794) (PMCID:PMC5264503)

McCaughey, L. C. , Josts, I., Grinter, R., White, P., Byron, O. , Tucker, N. P., Matthews, J. M., Kleanthous, C., Whitchurch, C. and Walker, D. (2016) Discovery, characterization and in vivo activity of pyocin SD2, a protein antibiotic from Pseudomonas aeruginosa. Biochemical Journal, 473(15), pp. 2345-2358. (doi: 10.1042/bcj20160470) (PMID:27252387) (PMCID:PMC4964976)

Ashraf, K. U., Josts, I., Mosbahi, K., Kelly, S. M. , Byron, O. , Smith, B. O. and Walker, D. (2016) The potassium binding protein Kbp is a cytoplasmic potassium sensor. Structure, 24(5), pp. 741-749. (doi: 10.1016/j.str.2016.03.017) (PMID:27112601)

2015

Byron, O. and Vestergaard, B. (2015) Protein–protein interactions: a supra-structural phenomenon demanding trans-disciplinary biophysical approaches. Current Opinion in Structural Biology, 35, pp. 76-86. (doi: 10.1016/j.sbi.2015.09.003)

Rocco, M. and Byron, O. (2015) Computing translational diffusion and sedimentation coefficients: an evaluation of experimental data and programs. European Biophysics Journal, 44(6), pp. 417-431. (doi: 10.1007/s00249-015-1042-9)

Rocco, M. and Byron, O. (2015) Erratum to: Computing translational diffusion and sedimentation coefficients: an evaluation of experimental data and programs. European Biophysics Journal, 44(6), pp. 433-436. (doi: 10.1007/s00249-015-1058-1) (PMID:26187588)

Joshi, A. et al. (2015) Structures of the ultra-high-affinity protein–protein complexes of pyocins S2 and AP41 and their cognate immunity proteins from pseudomonas aeruginosa. Journal of Molecular Biology, 427(17), pp. 2852-2866. (doi: 10.1016/j.jmb.2015.07.014) (PMID:26215615) (PMCID:PMC4548480)

Fyfe, C.D., Grinter, R., Josts, I., Mosbahi, K., Roszak, A.W., Cogdell, R.J. , Wall, D.M. , Burchmore, R.J.S. , Byron, O. and Walker, D. (2015) Structure of protease-cleaved escherichia coliα-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment. Acta Crystallographica. Section D: Biological Crystallography, 71(7), pp. 1478-1486. (doi: 10.1107/s1399004715008548) (PMID:26143919) (PMCID:PMC4498604)

Rocco, M. and Byron, O. (2015) Hydrodynamic modeling and its application in AUC. Methods in Enzymology, 562, pp. 81-108. (doi: 10.1016/bs.mie.2015.04.010) (PMID:26412648)

Zhao, H. et al. (2015) A multilaboratory comparison of calibration accuracy and the performance of external references in analytical ultracentrifugation. PLoS ONE, 10(5), e0126420. (doi: 10.1371/journal.pone.0126420) (PMID:25997164) (PMCID:PMC4440767)

2014

English, G., Byron, O. , Cianfanelli, F. R., Prescott, A. R. and Coulthurst, S. J. (2014) Biochemical analysis of TssK, a core component of the bacterial Type VI secretion system, reveals distinct oligomeric states of TssK and identifies a TssK–TssFG subcomplex. Biochemical Journal, 461(2), pp. 291-304. (doi: 10.1042/BJ20131426)

Beckham, K. S.H. et al. (2014) The metabolic enzyme AdhE controls the virulence of Escherichia coli O157:H7. Molecular Microbiology, 93(1), pp. 199-211. (doi: 10.1111/mmi.12651) (PMID:24846743) (PMCID:PMC4249723)

Grinter, R., Josts, I., Zeth, K., Roszak, A. W., McCaughey, L. C. , Cogdell, R. J. , Milner, J. J. , Kelly, S. M., Byron, O. and Walker, D. (2014) Structure of the atypical bacteriocin pectocin M2 implies a novel mechanism of protein uptake. Molecular Microbiology, 93(2), pp. 234-246. (doi: 10.1111/mmi.12655) (PMID:24865810) (PMCID:PMC4671253)

McCaughey, L. C. et al. (2014) Lectin-like bacteriocins from Pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor. PLoS Pathogens, 10(2), e1003898. (doi: 10.1371/journal.ppat.1003898) (PMID:24516380) (PMCID:PMC3916391)

Dow, J.M., Grahl, S., Ward, R., Evans, R., Byron, O. , Norman, D.G., Palmer, T. and Sargent, F. (2014) Characterization of a periplasmic nitrate reductase in complex with its biosynthetic chaperone. FEBS Journal, 281(1), pp. 246-260. (doi: 10.1111/febs.12592)

Josts, I., Grinter, R., Kelly, S. M. , Mosbahi, K., Roszak, A., Cogdell, R. , Smith, B. O. , Byron, O. and Walker, D. (2014) Recombinant expression, purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal DUF490963–1138 domain of TamB from Escherichia coli. Acta Crystallographica. Section F: Structural Biology Communications, 70(9), pp. 1272-1275. (doi: 10.1107/S2053230X14017403)

Laine, L. M., Biddau, M. , Byron, O. and Müller, S. (2014) Biochemical and structural characterisation of the apicoplast dihydrolipoamide dehydrogenase of Plasmodium falciparum. Bioscience Reports, 35(1), e00171. (doi: 10.1042/BSR20140150) (PMID:25387830) (PMCID:PMC4293902)

2013

Rocco, M., Brookes, E. and Byron, O. (2013) US-SOMO: methods for construction and hydration of macromolecular hydrodynamic models. In: Roberts, G.K. (ed.) Encyclopedia of Biophysics. Springer, pp. 2707-2714. ISBN 9783642167126 (doi: 10.1007/978-3-642-16712-6_292)

2012

Beckham, K. S.H., Byron, O. , Roe, A. J. and Gabrielsen, M. (2012) The structure of an orthorhombic crystal form of a 'forced reduced' thiol peroxidase reveals lattice formation aided by the presence of the affinity tag. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, 68(5), pp. 522-526. (doi: 10.1107/S1744309112011487) (PMID:22691780) (PMCID:PMC3374505)

Gabrielsen, M. , Beckham, K.S., Feher, V.A., Zetterstrom, C.E., Wang, D., Muller, S., Elofsson, M., Amaro, R.E., Byron, O. and Roe, A.J. (2012) Structural characterisation of Tpx from yersinia pseudotuberculosis reveals insights into the binding of salicylidene acylhydrazide compounds. PLoS ONE, 7(2), e32217. (doi: 10.1371/journal.pone.0032217) (PMID:22384182) (PMCID:PMC3288085)

Gabrielsen, M. , Beckham, K.S.H., Cogdell, R.J. , Byron, O. and Roe, A.J. (2012) FolX from Pseudomonas aeruginosa is octameric in both crystal and solution. FEBS Letters, 586(8), pp. 1160-1165. (doi: 10.1016/j.febslet.2012.03.031) (PMID:22575651) (PMCID:PMC3405516)

2011

Rasmussen, L.C.V., Oliveira, C.L.P., Byron, O. , Jensen, J.M., Pedersen, J.S., Sperling-Petersen, H.U. and Mortensen, K.K. (2011) Structure and dimerization of translation initiation factor aIF5B in solution. Biochemical and Biophysical Research Communications, 416(1-2), pp. 140-145. (doi: 10.1016/j.bbrc.2011.11.012)

Wang, D. et al. (2011) Identification of bacterial target proteins for the salicylidene acylhydrazide class of virulence blocking compounds. Journal of Biological Chemistry, 286(34), pp. 29922-29931. (doi: 10.1074/jbc.M111.233858) (PMID:21724850) (PMCID:PMC3191033)

Vijayakrishnan, S. , Callow, P., Nutley, M.A., McGow, D.P., Kropholler, P., Cooper, A., Byron, O. and Lindsay, J.G. (2011) Variation in the organization and subunit composition of the mammalian pyruvate dehydrogenase complex E2/E3BP core assembly. Biochemical Journal, 437(3), pp. 565-574. (doi: 10.1042/BJ20101784)

Moore, V., Kanu, A., Byron, O. , Campbell, G., Danson, M.J., Hough, D.J. and Crennell, S.J. (2011) Contribution of inter-subunit interactions to the thermostability of Pyrococcus furiosus citrate synthase. Extremophiles, 15(3), pp. 327-336. (doi: 10.1007/s00792-011-0363-6)

2010

Vijayakrishnan, S. , Kelly, S.M., Gilbert, R.J.C., Callow, P., Bhella, D. , Forsyth, T., Lindsay, J.G. and Byron, O. (2010) Solution structure and characterisation of the human pyruvate dehydrogenase complex core assembly. Journal of Molecular Biology, 399(1), pp. 71-93. (doi: 10.1016/j.jmb.2010.03.043) (PMID:20361979) (PMCID:PMC2880790)

Cardinali, B., Profumo, A., Aprile, A., Byron, O., Morris, G., Harding, S.E., Stafford, W.F. and Rocco, M. (2010) Hydrodynamic and mass spectrometry analysis of nearly-intact human fibrinogen, chicken fibrinogen, and of a substantially monodisperse human fibrinogen fragment X. Archives of Biochemistry and Biophysics, 493(2), pp. 157-168. (doi: 10.1016/j.abb.2009.10.008)

2009

Kreiner, M., Byron, O., Domingues, D. and van der Walle, C.F. (2009) Oligomerisation and thermal stability of polyvalent integrin [alpha]5[beta]1 ligands. Biophysical Chemistry, 142(1-3), pp. 34-39. (doi: 10.1016/j.bpc.2009.03.001)

2008

Byron, O. (2008) Hydrodynamic modeling: the solution conformation of macromolecules and their complexes. In: Correia, J. J. and Detrich, III, H. W. (eds.) Biophysical Tools for Biologists, Volume One: In Vitro Techniques. Series: Methods in cell biology (84). Academic Press: Amsterdam ; London, pp. 327-373. ISBN 9780123725202 (doi: 10.1016/S0091-679X(07)84012-X)

2006

Smolle, M., Prior, A.E., Brown, A.E., Cooper, A., Byron, O. and Lindsay, J.G. (2006) A new level of architectural complexity in the human pyruvate dehydrogenase complex. Journal of Biological Chemistry, 281(28), pp. 19772-19780. (doi: 10.1074/jbc.M601140200)

Egan, C. et al. (2006) Lack of immunological cross-reactivity between parasite-derived and recombinant forms of ES-62, a secreted protein of Acanthocheilonema viteae. Parasitology, 132, pp. 263-274. (doi: 10.1017/S0031182005009005) (PMID:16216137)

2005

Nollmann, M., Byron, O. and Stark, W. (2005) Behavior of Tn3 resolvase in solution and its interaction with res. Biophysical Journal, 89, pp. 1920-1931. (doi: 10.1529/biophysj.104.058164)

Nollmann, M., Stark, W. and Byron, O. (2005) A global multi-technique approach to study low-resolution solution structures. Journal of Applied Crystallography, 38, pp. 874-887. (doi: 10.1107/S0021889805026191)

Rai, N., Nollmann, M., Spotorno, B., Tassara, G., Byron, O. and Rocco, M. (2005) SOMO(SOlution MOdeler): Differences between X-ray- and NMR-derived bead models suggest a role for side chain flexibility in protein hydrodynamics. Structure, 13, pp. 723-734. (doi: 10.1016/j.str.2005.02.012)

2004

Nöllmann, M., He, J., Byron, O. and Stark, W. M. (2004) Solution structure of the Tn3 resolvase-crossover site synaptic complex. Molecular Cell, 16(1), pp. 127-137. (doi: 10.1016/j.molcel.2004.09.027) (PMID:15469828)

Nöllmann, M., Gilbert, R., Mitchell, T., Sferrazza, M. and Byron, O. (2004) The role of cholesterol in the activity of pneumolysin, a bacterial protein toxin. Biophysical Journal, 86(5), pp. 3141-3151. (doi: 10.1016/S0006-3495(04)74362-3) (PMID:15111427) (PMCID:PMC1304179)

Nöllmann, M., Stark, W. M. and Byron, O. (2004) Low-resolution reconstruction of a synthetic DNA Holliday junction. Biophysical Journal, 86(5), pp. 3060-3069. (doi: 10.1016/S0006-3495(04)74355-6) (PMID:15111420) (PMCID:PMC1304172)

Smolle, M., Hay, R. and Byron, O. (2004) Hydrodynamic bead modelling of the 2 : 1 p50-I kappa B gamma complex. Biophysical Chemistry, 108, pp. 259-271. (doi: 10.1016/j.bpc.2003.10.032)

Solovyova, A., Nollmann, M., Mitchell, T. and Byron, O. (2004) The solution structure and oligomerization behavior of two bacterial toxins: Pneumolysin and perfringolysin O. Biophysical Journal, 87, pp. 540-552. (doi: 10.1529/biophysj.104.039974)

2003

Myszka, D.G. et al. (2003) The ABRF-MIRG'02 study: assembly state, thermodynamic, and kinetic analysis of an enzyme/inhibitor interaction. Journal of Biomolecular Techniques, 14(4), pp. 247-269. (PMID:14715884) (PMCID:PMC2279960)

Ackerman, C. J., Harnett, M. M. , Harnett, W., Kelly, S. M. , Svergun, D. I. and Byron, O. (2003) 19 angstrom solution structure of the filarial nematode immunomodulatory protein, ES-62. Biophysical Journal, 84(1), pp. 489-500. (doi: 10.1016/S0006-3495(03)74868-1) (PMID:12524301) (PMCID:PMC1302629)

Fowler, S., Byron, O., Jumel, K., Xing, D., Corbel, M. and Bolgiano, B. (2003) Novel configurations of high molecular weight species of the pertussis toxin vaccine component. Vaccine, 21, pp. 2678-2688. (doi: 10.1016/S0264-410X(03)00105-1)

Harnett, W., Harnett, M.M. and Byron, O. (2003) Structural/functional aspects of ES-62 - A secreted immunomodulatory phosphorylcholine-containing filarial nematode glycoprotein. Current Protein and Peptide Science, 4(1), pp. 59-71. (doi: 10.2174/1389203033380368) (PMID:12570785)

Solovyova, A.S., Meenan, N., McDermott, L., Garofalo, A., Bradley, J.E., Kennedy, M.W. and Byron, O. (2003) The polyprotein and FAR lipid binding proteins of nematodes: shape and monomer/dimer states in ligand-free and bound forms. European Biophysics Journal with Biophysics Letters, 32, pp. 465-476. (doi: 10.1007/s00249-003-0297-8)

2002

Scott, D., Grossmann, J., Tames, J., Byron, O., Wilson, K. and Otto, B. (2002) Low resolution solution structure of the apo form of Escherichia coli haemoglobin protease Hbp. Journal of Molecular Biology, 315, pp. 1179-1187. (doi: 10.1006/jmbi.2001.5306)

2001

Short, B., Preisinger, C., Körner, R., Kopajtich, R., Byron, O. and Barr, F. A. (2001) A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic. Journal of Cell Biology, 155(6), pp. 877-883. (doi: 10.1083/jcb.200108079) (PMID:11739401) (PMCID:PMC2150909)

Kim, M., Chen, B., Hussey, R.E., Chishti, Y., Montefiori, D., Hoxie, J.A., Byron, O. , Campbell, G., Harrison, S.C. and Reinherz, E.L. (2001) The stoichiometry of trimeric SIV glycoprotein interaction with CD4 differs from that of anti-envelope antibody Fab fragments. Journal of Biological Chemistry, 276(46), pp. 42667-42676. (doi: 10.1074/jbc.m104166200) (PMID:11544255)

Kim, M., Sun, Z.-Y. J., Byron, O. , Campbell, G., Wagner, G., Wang, J.-h. and Reinherz, E. L. (2001) Molecular dissection of the CD2-C58 counter-receptor interface identifies CD2 Tyr86 and CD58 Lys34 residues as the functional 'hot spot'. Journal of Molecular Biology, 312(4), pp. 711-720. (doi: 10.1006/jmbi.2001.4980) (PMID:11575926)

Atanasiu, C., Byron, O. , McMiken, H., Sturrock, S.S. and Dryden, D.T.F. (2001) Characterisation of the structure of ocr, the gene 0.3 protein of bacteriophage T7. Nucleic Acids Research, 29(14), pp. 3059-3068. (doi: 10.1093/nar/29.14.3059) (PMID:11452031) (PMCID:PMC55801)

Bonev, B. B., Gilbert, R. J.C., Andrew, P. W., Byron, O. and Watts, A. (2001) Structural analysis of the protein/lipid complexes associated with pore formation by the bacterial toxin pneumolysin. Journal of Biological Chemistry, 276(8), pp. 5714-5719. (doi: 10.1074/jbc.M005126200) (PMID:11076935)

Kim, M., Sun, Z., Byron, O., Campbell, G., Wagner, G., Wang, J. and Reinherz, E. (2001) Molecular dissection of the CD2-CD58 counter-receptor interface identifies CD2 Tyr86 and CD58 Lys34 residues as the functional "hot spot". Journal of Molecular Biology, 312, pp. 711-720.

2000

Marfatia, S. M., Byron, O. , Campbell, G., Liu, S.-C. and Chishti, A. H. (2000) Human homologue of the drosophila discs large tumor suppressor protein forms an oligomer in solution. IDENTIFICATION OF THE SELF-ASSOCIATION SITE. Journal of Biological Chemistry, 275(18), pp. 13759-13770. (doi: 10.1074/jbc.275.18.13759) (PMID:10788497)

Byron, O. and Gilbert, R. J.C. (2000) Neutron scattering: good news for biotechnology. Current Opinion in Biotechnology, 11(1), pp. 72-80. (doi: 10.1016/s0958-1669(99)00057-9) (PMID:10679336)

Byron, O. (2000) Hydrodynamic bead modeling of biological macromolecules. Methods in Enzymology, 321, pp. 278-304. (doi: 10.1016/S0076-6879(00)21199-3) (PMID:10909063)

1999

Carrasco, B., de la Torre, J. G., Byron, O. , King, D., Walters, C., Jones, S. and Harding, S. E. (1999) Novel size-independent modeling of the dilute solution conformation of the immunoglobulin IgG Fab′ domain using SOLPRO and ELLIPS. Biophysical Journal, 77(6), pp. 2902-2910. (doi: 10.1016/S0006-3495(99)77123-7) (PMID:10585914) (PMCID:PMC1300563)

Gilbert, R. J.C., Heenan, R. K., Timmins, P. A., Gingles, N. A., Mitchell, T. J., Rowe, A. J., Rossjohn, J., Parker, M. W., Andrew, P. W. and Byron, O. (1999) Studies on the structure and mechanism of a bacterial protein toxin by analytical ultracentrifugation and small-angle neutron scattering. Journal of Molecular Biology, 293(5), pp. 1145-1160. (doi: 10.1006/jmbi.1999.3210) (PMID:10547292)

Bayliss, R. I., Errington, N., Byron, O. , Svensson, A. and Rowe, A. (1999) A conformation spectrum analysis of the morphological states of myosin S1 in the presence of effectors. Progress in Colloid and Polymer Science, 113, pp. 158-163. (doi: 10.1007/3-540-48703-4_22)

Errington, N., Byron, O. and Rowe, A. J. (1999) Conformational spectra — probing protein conformational changes. Biophysical Chemistry, 80(3), pp. 189-197. (doi: 10.1016/S0301-4622(99)00077-0) (PMID:17030326)

1998

Gilbert, R. J.C., Rossjohn, J., Parker, M. W., Tweten, R. K., Morgan, P. J., Mitchell, T. J., Errington, N., Rowe, A. J., Andrew, P. W. and Byron, O. (1998) Self-interaction of pneumolysin, the pore-forming protein toxin of Streptococcus pneumoniae. Journal of Molecular Biology, 284(4), pp. 1223-1237. (doi: 10.1006/jmbi.1998.2258) (PMID:9837740)

Nairn, J., Duncan, D., Gray, L. M., Urquhart, G., Binnie, M., Byron, O. , Fothergill-Gilmore, L. A. and Price, N. C. (1998) Purification and characterization of pyruvate kinase from schizosaccharomyces pombe: evidence for an unusual quaternary structure. Protein Expression and Purification, 14(2), pp. 247-253. (doi: 10.1006/prep.1998.0938) (PMID:9790887)

1997

Tharia, H. A., Rowe, A., Byron, O. and Wells, C. (1997) Physical characterization and ATPase activity of 14S dynein fractions from tetrahymena thermophila. Journal of Muscle Research and Cell Motility, 18(6), pp. 697-709. (doi: 10.1023/A:1018640007999) (PMID:9429162)

Marfatia, S. M., Morais-Cabral, J. H., Kim, A. C., Byron, O. and Chishti, A. H. (1997) The PDZ domain of human erythrocyte p55 mediates its binding to the cytoplasmic carboxyl terminus of glycophorin C: analysis of the binding interface by in vitromutagenesis. Journal of Biological Chemistry, 272(39), pp. 24191-24197. (doi: 10.1074/jbc.272.39.24191) (PMID:9305870)

Byron, O. , Mistry, P., Suter, D. and Skelly, J. (1997) DT diaphorase exists as a dimer-tetramer equilibrium in solution. European Biophysics Journal with Biophysics Letters, 25(5-6), pp. 423-430. (doi: 10.1007/s002490050056) (PMID:9188164)

Dryden, D. T. F., Cooper, L. P., Thorpe, P. H. and Byron, O. (1997) The in vitro assembly of the EcoKI Type I DNA restriction/modification enzyme and its in vivo implications. Biochemistry, 36(5), pp. 1065-1076. (doi: 10.1021/bi9619435) (PMID:9033396)

Byron, O. (1997) Construction of hydrodynamic bead models from high-resolution X-ray crystallographic or nuclear magnetic resonance data. Biophysical Journal, 72(1), pp. 408-415. (doi: 10.1016/S0006-3495(97)78681-8) (PMID:8994627) (PMCID:PMC1184331)

1996

Brownleader, M. D., Byron, O. , Rowe, A., Trevan, M., Welhan, K. and Dey, P. M. (1996) Investigations into the molecular size and shape of tomato extensin. Biochemical Journal, 320(2), pp. 577-583. (doi: 10.1042/bj3200577)

Cabral, J. H. M., Petosa, C., Sutcliffe, M. J., Raza, S., Byron, O. , Poy, F., Marfatia, S. M., Chishti, A. H. and Liddington, R. C. (1996) Crystal structure of a PDZ domain. Nature, 382(6592), pp. 649-652. (doi: 10.1038/382649a0) (PMID:8757139)

1995

Silkowski, H., Byron, O. , Davis, S. J., Barclay, A. N., Daies, E. A., Rowe, A. J. and Harding, S. E. (1995) Estimation of the dissociation constant of the cell adhesion molecules srCD2 and srCD48 using analytical ultracentrifugation. Biochemical Society Transactions, 23(3), 435S. (doi: 10.1042/bst023435s) (PMID:8566323)

Silkowski, H., Davis, S. J., Barclay, A. N., Rowe, A. J., Harding, S. E. and Byron, O. (1995) Characterisation of the low affinity interaction between rat cell adhesion molecules CD2 and CD48 by analytical ultracentrifugation. European Biophysics Journal with Biophysics Letters, 25(5-6), pp. 455-462. (doi: 10.1007/s002490050060) (PMID:9188168)

Byron, O. (1995) Hydrodynamic modelling of the solution conformation of 10 S myosin. In: Behlke, J. (ed.) Analytical Ultracentrifugation. Series: Progress in colloid and polymer science (99). Steinkopff: Darmstadt, pp. 82-86. ISBN 9783798510388 (doi: 10.1007/BFb0114074)

1994

Morgan, P. J., Hyman, S. C., Byron, O. , Andrew, P. W., Mitchell, T. J. and Rowe, A. J. (1994) Modeling the bacterial protein toxin, pneumolysin, in its monomeric and oligomeric form. Journal of Biological Chemistry, 269(41), pp. 25315-25320. (doi: 10.1016/S0021-9258(18)47249-3) (PMID:7929224)

1993

King, D. J. et al. (1993) Expression, purification and characterization of B72.3 Fv fragments. Biochemical Journal, 290(3), pp. 723-729. (doi: 10.1042/bj2900723) (PMID:8457200)

1990

Byron, O. , Harding, S. and Rhind, S. (1990) A preliminary investigation of the hydrodynamic properties of two novel monoclonal antibodies. Biochemical Society Transactions, 18(5), pp. 1030-1031. (doi: 10.1042/bst0181030) (PMID:2083650)

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Number of items: 85.

Articles

Miguel-Romero, L., Alqasmi, M., Bacarizo, J., Tan, J. A., Cogdell, R. J. , Chen, J., Byron, O. , Christie, G. E., Marina, A. and Penadés, J. R. (2022) Non-canonical Staphylococcus aureus pathogenicity island repression. Nucleic Acids Research, 50(19), pp. 11109-11127. (doi: 10.1093/nar/gkac855) (PMID:36200825) (PMCID:PMC9638917)

Azmi, L., Bragginton, E. C., Cadby, I. T., Byron, O. , Roe, A. J. , Lovering, A. L. and Gabrielsen, M. (2020) High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE. Acta Crystallographica. Section F: Structural Biology Communications, 76(9), pp. 414-421. (doi: 10.1107/S2053230X20010237)

Kim, G., Yang, J., Jang, J., Choi, J.-S., Roe, A. J. , Byron, O. , Seok, C. and Song, J.-J. (2020) Aldehyde-alcohol dehydrogenase undergoes structural transition to form extended spirosomes for substrate channeling. Communications Biology, 3, 298. (doi: 10.1038/s42003-020-1030-1) (PMID:32523125) (PMCID:PMC7286902)

Medina-Pritchard, B., Lazou, V., Zuo, J., Byron, O. , Abad, M. A., Rappsilber, J., Heun, P. and Jeyaprakash, A. A. (2020) Structural basis for centromere maintenance by Drosophila CENP-A chaperone CAL1. EMBO Journal, 39(7), e103234. (doi: 10.15252/embj.2019103234) (PMID:32134144) (PMCID:PMC7110144)

Kim, G., Azmi, L., Jang, S., Jung, T., Hebert, H., Roe, A. J. , Byron, O. and Song, J.-J. (2019) Aldehyde-alcohol dehydrogenase forms a high-order spirosome architecture critical for its activity. Nature Communications, 10, 4527. (doi: 10.1038/s41467-019-12427-8) (PMID:31586059) (PMCID:PMC6778083)

Conley, M. J. , McElwee, M., Azmi, L., Gabrielsen, M. , Byron, O. , Goodfellow, I. G. and Bhella, D. (2019) Calicivirus VP2 forms a portal-like assembly following receptor engagement. Nature, 565(7739), pp. 377-381. (doi: 10.1038/s41586-018-0852-1) (PMID:30626974)

Byron, O. , Nischang, I. and Patel, T. R. (2018) Analytical ultracentrifugation (AUC): a seminal tool offering multiple solutions. European Biophysics Journal, 47(7), pp. 693-696. (doi: 10.1007/s00249-018-1333-z) (PMID:30218114)

Dias Mirandela, G. et al. (2018) Merging in-solution x-ray and neutron scattering data allows fine structural analysis of membrane–protein detergent complexes. Journal of Physical Chemistry Letters, 9(14), pp. 3910-3914. (doi: 10.1021/acs.jpclett.8b01598) (PMID:29939747)

Marciano, G., Da Vela, S., Tria, G., Svergun, D. I., Byron, O. and Huang, D. T. (2018) Structure specific recognition protein-1 (SSRP1) is an elongated homodimer that binds histones. Journal of Biological Chemistry, 293(26), pp. 10071-10083. (doi: 10.1074/jbc.RA117.000994) (PMID:29764934) (PMCID:PMC6028955)

Grinter, R. et al. (2016) Structure of the bacterial plant-ferredoxin receptor FusA. Nature Communications, 7, 13308. (doi: 10.1038/ncomms13308) (PMID:27796364) (PMCID:PMC5095587)

Klein, A., Wojdyla, J. A., Joshi, A., Josts, I., McCaughey, L. C. , Housden, N. G., Kaminska, R., Byron, O. , Walker, D. and Kleanthous, C. (2016) Structural and biophysical analysis of nuclease protein antibiotics. Biochemical Journal, 473(18), pp. 2799-2812. (doi: 10.1042/bcj20160544) (PMID:27402794) (PMCID:PMC5264503)

McCaughey, L. C. , Josts, I., Grinter, R., White, P., Byron, O. , Tucker, N. P., Matthews, J. M., Kleanthous, C., Whitchurch, C. and Walker, D. (2016) Discovery, characterization and in vivo activity of pyocin SD2, a protein antibiotic from Pseudomonas aeruginosa. Biochemical Journal, 473(15), pp. 2345-2358. (doi: 10.1042/bcj20160470) (PMID:27252387) (PMCID:PMC4964976)

Ashraf, K. U., Josts, I., Mosbahi, K., Kelly, S. M. , Byron, O. , Smith, B. O. and Walker, D. (2016) The potassium binding protein Kbp is a cytoplasmic potassium sensor. Structure, 24(5), pp. 741-749. (doi: 10.1016/j.str.2016.03.017) (PMID:27112601)

Byron, O. and Vestergaard, B. (2015) Protein–protein interactions: a supra-structural phenomenon demanding trans-disciplinary biophysical approaches. Current Opinion in Structural Biology, 35, pp. 76-86. (doi: 10.1016/j.sbi.2015.09.003)

Rocco, M. and Byron, O. (2015) Computing translational diffusion and sedimentation coefficients: an evaluation of experimental data and programs. European Biophysics Journal, 44(6), pp. 417-431. (doi: 10.1007/s00249-015-1042-9)

Rocco, M. and Byron, O. (2015) Erratum to: Computing translational diffusion and sedimentation coefficients: an evaluation of experimental data and programs. European Biophysics Journal, 44(6), pp. 433-436. (doi: 10.1007/s00249-015-1058-1) (PMID:26187588)

Joshi, A. et al. (2015) Structures of the ultra-high-affinity protein–protein complexes of pyocins S2 and AP41 and their cognate immunity proteins from pseudomonas aeruginosa. Journal of Molecular Biology, 427(17), pp. 2852-2866. (doi: 10.1016/j.jmb.2015.07.014) (PMID:26215615) (PMCID:PMC4548480)

Fyfe, C.D., Grinter, R., Josts, I., Mosbahi, K., Roszak, A.W., Cogdell, R.J. , Wall, D.M. , Burchmore, R.J.S. , Byron, O. and Walker, D. (2015) Structure of protease-cleaved escherichia coliα-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment. Acta Crystallographica. Section D: Biological Crystallography, 71(7), pp. 1478-1486. (doi: 10.1107/s1399004715008548) (PMID:26143919) (PMCID:PMC4498604)

Rocco, M. and Byron, O. (2015) Hydrodynamic modeling and its application in AUC. Methods in Enzymology, 562, pp. 81-108. (doi: 10.1016/bs.mie.2015.04.010) (PMID:26412648)

Zhao, H. et al. (2015) A multilaboratory comparison of calibration accuracy and the performance of external references in analytical ultracentrifugation. PLoS ONE, 10(5), e0126420. (doi: 10.1371/journal.pone.0126420) (PMID:25997164) (PMCID:PMC4440767)

English, G., Byron, O. , Cianfanelli, F. R., Prescott, A. R. and Coulthurst, S. J. (2014) Biochemical analysis of TssK, a core component of the bacterial Type VI secretion system, reveals distinct oligomeric states of TssK and identifies a TssK–TssFG subcomplex. Biochemical Journal, 461(2), pp. 291-304. (doi: 10.1042/BJ20131426)

Beckham, K. S.H. et al. (2014) The metabolic enzyme AdhE controls the virulence of Escherichia coli O157:H7. Molecular Microbiology, 93(1), pp. 199-211. (doi: 10.1111/mmi.12651) (PMID:24846743) (PMCID:PMC4249723)

Grinter, R., Josts, I., Zeth, K., Roszak, A. W., McCaughey, L. C. , Cogdell, R. J. , Milner, J. J. , Kelly, S. M., Byron, O. and Walker, D. (2014) Structure of the atypical bacteriocin pectocin M2 implies a novel mechanism of protein uptake. Molecular Microbiology, 93(2), pp. 234-246. (doi: 10.1111/mmi.12655) (PMID:24865810) (PMCID:PMC4671253)

McCaughey, L. C. et al. (2014) Lectin-like bacteriocins from Pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor. PLoS Pathogens, 10(2), e1003898. (doi: 10.1371/journal.ppat.1003898) (PMID:24516380) (PMCID:PMC3916391)

Dow, J.M., Grahl, S., Ward, R., Evans, R., Byron, O. , Norman, D.G., Palmer, T. and Sargent, F. (2014) Characterization of a periplasmic nitrate reductase in complex with its biosynthetic chaperone. FEBS Journal, 281(1), pp. 246-260. (doi: 10.1111/febs.12592)

Josts, I., Grinter, R., Kelly, S. M. , Mosbahi, K., Roszak, A., Cogdell, R. , Smith, B. O. , Byron, O. and Walker, D. (2014) Recombinant expression, purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal DUF490963–1138 domain of TamB from Escherichia coli. Acta Crystallographica. Section F: Structural Biology Communications, 70(9), pp. 1272-1275. (doi: 10.1107/S2053230X14017403)

Laine, L. M., Biddau, M. , Byron, O. and Müller, S. (2014) Biochemical and structural characterisation of the apicoplast dihydrolipoamide dehydrogenase of Plasmodium falciparum. Bioscience Reports, 35(1), e00171. (doi: 10.1042/BSR20140150) (PMID:25387830) (PMCID:PMC4293902)

Beckham, K. S.H., Byron, O. , Roe, A. J. and Gabrielsen, M. (2012) The structure of an orthorhombic crystal form of a 'forced reduced' thiol peroxidase reveals lattice formation aided by the presence of the affinity tag. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, 68(5), pp. 522-526. (doi: 10.1107/S1744309112011487) (PMID:22691780) (PMCID:PMC3374505)

Gabrielsen, M. , Beckham, K.S., Feher, V.A., Zetterstrom, C.E., Wang, D., Muller, S., Elofsson, M., Amaro, R.E., Byron, O. and Roe, A.J. (2012) Structural characterisation of Tpx from yersinia pseudotuberculosis reveals insights into the binding of salicylidene acylhydrazide compounds. PLoS ONE, 7(2), e32217. (doi: 10.1371/journal.pone.0032217) (PMID:22384182) (PMCID:PMC3288085)

Gabrielsen, M. , Beckham, K.S.H., Cogdell, R.J. , Byron, O. and Roe, A.J. (2012) FolX from Pseudomonas aeruginosa is octameric in both crystal and solution. FEBS Letters, 586(8), pp. 1160-1165. (doi: 10.1016/j.febslet.2012.03.031) (PMID:22575651) (PMCID:PMC3405516)

Rasmussen, L.C.V., Oliveira, C.L.P., Byron, O. , Jensen, J.M., Pedersen, J.S., Sperling-Petersen, H.U. and Mortensen, K.K. (2011) Structure and dimerization of translation initiation factor aIF5B in solution. Biochemical and Biophysical Research Communications, 416(1-2), pp. 140-145. (doi: 10.1016/j.bbrc.2011.11.012)

Wang, D. et al. (2011) Identification of bacterial target proteins for the salicylidene acylhydrazide class of virulence blocking compounds. Journal of Biological Chemistry, 286(34), pp. 29922-29931. (doi: 10.1074/jbc.M111.233858) (PMID:21724850) (PMCID:PMC3191033)

Vijayakrishnan, S. , Callow, P., Nutley, M.A., McGow, D.P., Kropholler, P., Cooper, A., Byron, O. and Lindsay, J.G. (2011) Variation in the organization and subunit composition of the mammalian pyruvate dehydrogenase complex E2/E3BP core assembly. Biochemical Journal, 437(3), pp. 565-574. (doi: 10.1042/BJ20101784)

Moore, V., Kanu, A., Byron, O. , Campbell, G., Danson, M.J., Hough, D.J. and Crennell, S.J. (2011) Contribution of inter-subunit interactions to the thermostability of Pyrococcus furiosus citrate synthase. Extremophiles, 15(3), pp. 327-336. (doi: 10.1007/s00792-011-0363-6)

Vijayakrishnan, S. , Kelly, S.M., Gilbert, R.J.C., Callow, P., Bhella, D. , Forsyth, T., Lindsay, J.G. and Byron, O. (2010) Solution structure and characterisation of the human pyruvate dehydrogenase complex core assembly. Journal of Molecular Biology, 399(1), pp. 71-93. (doi: 10.1016/j.jmb.2010.03.043) (PMID:20361979) (PMCID:PMC2880790)

Cardinali, B., Profumo, A., Aprile, A., Byron, O., Morris, G., Harding, S.E., Stafford, W.F. and Rocco, M. (2010) Hydrodynamic and mass spectrometry analysis of nearly-intact human fibrinogen, chicken fibrinogen, and of a substantially monodisperse human fibrinogen fragment X. Archives of Biochemistry and Biophysics, 493(2), pp. 157-168. (doi: 10.1016/j.abb.2009.10.008)

Kreiner, M., Byron, O., Domingues, D. and van der Walle, C.F. (2009) Oligomerisation and thermal stability of polyvalent integrin [alpha]5[beta]1 ligands. Biophysical Chemistry, 142(1-3), pp. 34-39. (doi: 10.1016/j.bpc.2009.03.001)

Smolle, M., Prior, A.E., Brown, A.E., Cooper, A., Byron, O. and Lindsay, J.G. (2006) A new level of architectural complexity in the human pyruvate dehydrogenase complex. Journal of Biological Chemistry, 281(28), pp. 19772-19780. (doi: 10.1074/jbc.M601140200)

Egan, C. et al. (2006) Lack of immunological cross-reactivity between parasite-derived and recombinant forms of ES-62, a secreted protein of Acanthocheilonema viteae. Parasitology, 132, pp. 263-274. (doi: 10.1017/S0031182005009005) (PMID:16216137)

Nollmann, M., Byron, O. and Stark, W. (2005) Behavior of Tn3 resolvase in solution and its interaction with res. Biophysical Journal, 89, pp. 1920-1931. (doi: 10.1529/biophysj.104.058164)

Nollmann, M., Stark, W. and Byron, O. (2005) A global multi-technique approach to study low-resolution solution structures. Journal of Applied Crystallography, 38, pp. 874-887. (doi: 10.1107/S0021889805026191)

Rai, N., Nollmann, M., Spotorno, B., Tassara, G., Byron, O. and Rocco, M. (2005) SOMO(SOlution MOdeler): Differences between X-ray- and NMR-derived bead models suggest a role for side chain flexibility in protein hydrodynamics. Structure, 13, pp. 723-734. (doi: 10.1016/j.str.2005.02.012)

Nöllmann, M., He, J., Byron, O. and Stark, W. M. (2004) Solution structure of the Tn3 resolvase-crossover site synaptic complex. Molecular Cell, 16(1), pp. 127-137. (doi: 10.1016/j.molcel.2004.09.027) (PMID:15469828)

Nöllmann, M., Gilbert, R., Mitchell, T., Sferrazza, M. and Byron, O. (2004) The role of cholesterol in the activity of pneumolysin, a bacterial protein toxin. Biophysical Journal, 86(5), pp. 3141-3151. (doi: 10.1016/S0006-3495(04)74362-3) (PMID:15111427) (PMCID:PMC1304179)

Nöllmann, M., Stark, W. M. and Byron, O. (2004) Low-resolution reconstruction of a synthetic DNA Holliday junction. Biophysical Journal, 86(5), pp. 3060-3069. (doi: 10.1016/S0006-3495(04)74355-6) (PMID:15111420) (PMCID:PMC1304172)

Smolle, M., Hay, R. and Byron, O. (2004) Hydrodynamic bead modelling of the 2 : 1 p50-I kappa B gamma complex. Biophysical Chemistry, 108, pp. 259-271. (doi: 10.1016/j.bpc.2003.10.032)

Solovyova, A., Nollmann, M., Mitchell, T. and Byron, O. (2004) The solution structure and oligomerization behavior of two bacterial toxins: Pneumolysin and perfringolysin O. Biophysical Journal, 87, pp. 540-552. (doi: 10.1529/biophysj.104.039974)

Myszka, D.G. et al. (2003) The ABRF-MIRG'02 study: assembly state, thermodynamic, and kinetic analysis of an enzyme/inhibitor interaction. Journal of Biomolecular Techniques, 14(4), pp. 247-269. (PMID:14715884) (PMCID:PMC2279960)

Ackerman, C. J., Harnett, M. M. , Harnett, W., Kelly, S. M. , Svergun, D. I. and Byron, O. (2003) 19 angstrom solution structure of the filarial nematode immunomodulatory protein, ES-62. Biophysical Journal, 84(1), pp. 489-500. (doi: 10.1016/S0006-3495(03)74868-1) (PMID:12524301) (PMCID:PMC1302629)

Fowler, S., Byron, O., Jumel, K., Xing, D., Corbel, M. and Bolgiano, B. (2003) Novel configurations of high molecular weight species of the pertussis toxin vaccine component. Vaccine, 21, pp. 2678-2688. (doi: 10.1016/S0264-410X(03)00105-1)

Harnett, W., Harnett, M.M. and Byron, O. (2003) Structural/functional aspects of ES-62 - A secreted immunomodulatory phosphorylcholine-containing filarial nematode glycoprotein. Current Protein and Peptide Science, 4(1), pp. 59-71. (doi: 10.2174/1389203033380368) (PMID:12570785)

Solovyova, A.S., Meenan, N., McDermott, L., Garofalo, A., Bradley, J.E., Kennedy, M.W. and Byron, O. (2003) The polyprotein and FAR lipid binding proteins of nematodes: shape and monomer/dimer states in ligand-free and bound forms. European Biophysics Journal with Biophysics Letters, 32, pp. 465-476. (doi: 10.1007/s00249-003-0297-8)

Scott, D., Grossmann, J., Tames, J., Byron, O., Wilson, K. and Otto, B. (2002) Low resolution solution structure of the apo form of Escherichia coli haemoglobin protease Hbp. Journal of Molecular Biology, 315, pp. 1179-1187. (doi: 10.1006/jmbi.2001.5306)

Short, B., Preisinger, C., Körner, R., Kopajtich, R., Byron, O. and Barr, F. A. (2001) A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic. Journal of Cell Biology, 155(6), pp. 877-883. (doi: 10.1083/jcb.200108079) (PMID:11739401) (PMCID:PMC2150909)

Kim, M., Chen, B., Hussey, R.E., Chishti, Y., Montefiori, D., Hoxie, J.A., Byron, O. , Campbell, G., Harrison, S.C. and Reinherz, E.L. (2001) The stoichiometry of trimeric SIV glycoprotein interaction with CD4 differs from that of anti-envelope antibody Fab fragments. Journal of Biological Chemistry, 276(46), pp. 42667-42676. (doi: 10.1074/jbc.m104166200) (PMID:11544255)

Kim, M., Sun, Z.-Y. J., Byron, O. , Campbell, G., Wagner, G., Wang, J.-h. and Reinherz, E. L. (2001) Molecular dissection of the CD2-C58 counter-receptor interface identifies CD2 Tyr86 and CD58 Lys34 residues as the functional 'hot spot'. Journal of Molecular Biology, 312(4), pp. 711-720. (doi: 10.1006/jmbi.2001.4980) (PMID:11575926)

Atanasiu, C., Byron, O. , McMiken, H., Sturrock, S.S. and Dryden, D.T.F. (2001) Characterisation of the structure of ocr, the gene 0.3 protein of bacteriophage T7. Nucleic Acids Research, 29(14), pp. 3059-3068. (doi: 10.1093/nar/29.14.3059) (PMID:11452031) (PMCID:PMC55801)

Bonev, B. B., Gilbert, R. J.C., Andrew, P. W., Byron, O. and Watts, A. (2001) Structural analysis of the protein/lipid complexes associated with pore formation by the bacterial toxin pneumolysin. Journal of Biological Chemistry, 276(8), pp. 5714-5719. (doi: 10.1074/jbc.M005126200) (PMID:11076935)

Kim, M., Sun, Z., Byron, O., Campbell, G., Wagner, G., Wang, J. and Reinherz, E. (2001) Molecular dissection of the CD2-CD58 counter-receptor interface identifies CD2 Tyr86 and CD58 Lys34 residues as the functional "hot spot". Journal of Molecular Biology, 312, pp. 711-720.

Marfatia, S. M., Byron, O. , Campbell, G., Liu, S.-C. and Chishti, A. H. (2000) Human homologue of the drosophila discs large tumor suppressor protein forms an oligomer in solution. IDENTIFICATION OF THE SELF-ASSOCIATION SITE. Journal of Biological Chemistry, 275(18), pp. 13759-13770. (doi: 10.1074/jbc.275.18.13759) (PMID:10788497)

Byron, O. and Gilbert, R. J.C. (2000) Neutron scattering: good news for biotechnology. Current Opinion in Biotechnology, 11(1), pp. 72-80. (doi: 10.1016/s0958-1669(99)00057-9) (PMID:10679336)

Byron, O. (2000) Hydrodynamic bead modeling of biological macromolecules. Methods in Enzymology, 321, pp. 278-304. (doi: 10.1016/S0076-6879(00)21199-3) (PMID:10909063)

Carrasco, B., de la Torre, J. G., Byron, O. , King, D., Walters, C., Jones, S. and Harding, S. E. (1999) Novel size-independent modeling of the dilute solution conformation of the immunoglobulin IgG Fab′ domain using SOLPRO and ELLIPS. Biophysical Journal, 77(6), pp. 2902-2910. (doi: 10.1016/S0006-3495(99)77123-7) (PMID:10585914) (PMCID:PMC1300563)

Gilbert, R. J.C., Heenan, R. K., Timmins, P. A., Gingles, N. A., Mitchell, T. J., Rowe, A. J., Rossjohn, J., Parker, M. W., Andrew, P. W. and Byron, O. (1999) Studies on the structure and mechanism of a bacterial protein toxin by analytical ultracentrifugation and small-angle neutron scattering. Journal of Molecular Biology, 293(5), pp. 1145-1160. (doi: 10.1006/jmbi.1999.3210) (PMID:10547292)

Bayliss, R. I., Errington, N., Byron, O. , Svensson, A. and Rowe, A. (1999) A conformation spectrum analysis of the morphological states of myosin S1 in the presence of effectors. Progress in Colloid and Polymer Science, 113, pp. 158-163. (doi: 10.1007/3-540-48703-4_22)

Errington, N., Byron, O. and Rowe, A. J. (1999) Conformational spectra — probing protein conformational changes. Biophysical Chemistry, 80(3), pp. 189-197. (doi: 10.1016/S0301-4622(99)00077-0) (PMID:17030326)

Gilbert, R. J.C., Rossjohn, J., Parker, M. W., Tweten, R. K., Morgan, P. J., Mitchell, T. J., Errington, N., Rowe, A. J., Andrew, P. W. and Byron, O. (1998) Self-interaction of pneumolysin, the pore-forming protein toxin of Streptococcus pneumoniae. Journal of Molecular Biology, 284(4), pp. 1223-1237. (doi: 10.1006/jmbi.1998.2258) (PMID:9837740)

Nairn, J., Duncan, D., Gray, L. M., Urquhart, G., Binnie, M., Byron, O. , Fothergill-Gilmore, L. A. and Price, N. C. (1998) Purification and characterization of pyruvate kinase from schizosaccharomyces pombe: evidence for an unusual quaternary structure. Protein Expression and Purification, 14(2), pp. 247-253. (doi: 10.1006/prep.1998.0938) (PMID:9790887)

Tharia, H. A., Rowe, A., Byron, O. and Wells, C. (1997) Physical characterization and ATPase activity of 14S dynein fractions from tetrahymena thermophila. Journal of Muscle Research and Cell Motility, 18(6), pp. 697-709. (doi: 10.1023/A:1018640007999) (PMID:9429162)

Marfatia, S. M., Morais-Cabral, J. H., Kim, A. C., Byron, O. and Chishti, A. H. (1997) The PDZ domain of human erythrocyte p55 mediates its binding to the cytoplasmic carboxyl terminus of glycophorin C: analysis of the binding interface by in vitromutagenesis. Journal of Biological Chemistry, 272(39), pp. 24191-24197. (doi: 10.1074/jbc.272.39.24191) (PMID:9305870)

Byron, O. , Mistry, P., Suter, D. and Skelly, J. (1997) DT diaphorase exists as a dimer-tetramer equilibrium in solution. European Biophysics Journal with Biophysics Letters, 25(5-6), pp. 423-430. (doi: 10.1007/s002490050056) (PMID:9188164)

Dryden, D. T. F., Cooper, L. P., Thorpe, P. H. and Byron, O. (1997) The in vitro assembly of the EcoKI Type I DNA restriction/modification enzyme and its in vivo implications. Biochemistry, 36(5), pp. 1065-1076. (doi: 10.1021/bi9619435) (PMID:9033396)

Byron, O. (1997) Construction of hydrodynamic bead models from high-resolution X-ray crystallographic or nuclear magnetic resonance data. Biophysical Journal, 72(1), pp. 408-415. (doi: 10.1016/S0006-3495(97)78681-8) (PMID:8994627) (PMCID:PMC1184331)

Brownleader, M. D., Byron, O. , Rowe, A., Trevan, M., Welhan, K. and Dey, P. M. (1996) Investigations into the molecular size and shape of tomato extensin. Biochemical Journal, 320(2), pp. 577-583. (doi: 10.1042/bj3200577)

Cabral, J. H. M., Petosa, C., Sutcliffe, M. J., Raza, S., Byron, O. , Poy, F., Marfatia, S. M., Chishti, A. H. and Liddington, R. C. (1996) Crystal structure of a PDZ domain. Nature, 382(6592), pp. 649-652. (doi: 10.1038/382649a0) (PMID:8757139)

Silkowski, H., Byron, O. , Davis, S. J., Barclay, A. N., Daies, E. A., Rowe, A. J. and Harding, S. E. (1995) Estimation of the dissociation constant of the cell adhesion molecules srCD2 and srCD48 using analytical ultracentrifugation. Biochemical Society Transactions, 23(3), 435S. (doi: 10.1042/bst023435s) (PMID:8566323)

Silkowski, H., Davis, S. J., Barclay, A. N., Rowe, A. J., Harding, S. E. and Byron, O. (1995) Characterisation of the low affinity interaction between rat cell adhesion molecules CD2 and CD48 by analytical ultracentrifugation. European Biophysics Journal with Biophysics Letters, 25(5-6), pp. 455-462. (doi: 10.1007/s002490050060) (PMID:9188168)

Morgan, P. J., Hyman, S. C., Byron, O. , Andrew, P. W., Mitchell, T. J. and Rowe, A. J. (1994) Modeling the bacterial protein toxin, pneumolysin, in its monomeric and oligomeric form. Journal of Biological Chemistry, 269(41), pp. 25315-25320. (doi: 10.1016/S0021-9258(18)47249-3) (PMID:7929224)

King, D. J. et al. (1993) Expression, purification and characterization of B72.3 Fv fragments. Biochemical Journal, 290(3), pp. 723-729. (doi: 10.1042/bj2900723) (PMID:8457200)

Byron, O. , Harding, S. and Rhind, S. (1990) A preliminary investigation of the hydrodynamic properties of two novel monoclonal antibodies. Biochemical Society Transactions, 18(5), pp. 1030-1031. (doi: 10.1042/bst0181030) (PMID:2083650)

Book Sections

Rocco, M., Brookes, E. and Byron, O. (2021) US-SOMO: Methods for Construction and Hydration of Macromolecular Hydrodynamic Models. In: Roberts, G., Watts, A. and European Biophysical Societies, (eds.) Encyclopedia of Biophysics. Springer: Berlin, Heidelberg. ISBN 9783642359439 (doi: 10.1007/978-3-642-35943-9_292-1)

Byron, O. and Lindsay, J. G. (2017) The pyruvate dehydrogenase complex and related assemblies in health and disease. In: Harris, J. R. and Marles-Wright, J. (eds.) Macromolecular Protein Complexes. Series: Subcellular biochemistry (83). Springer, pp. 523-550. ISBN 9783319465012 (doi: 10.1007/978-3-319-46503-6_19)

Rocco, M., Brookes, E. and Byron, O. (2013) US-SOMO: methods for construction and hydration of macromolecular hydrodynamic models. In: Roberts, G.K. (ed.) Encyclopedia of Biophysics. Springer, pp. 2707-2714. ISBN 9783642167126 (doi: 10.1007/978-3-642-16712-6_292)

Byron, O. (2008) Hydrodynamic modeling: the solution conformation of macromolecules and their complexes. In: Correia, J. J. and Detrich, III, H. W. (eds.) Biophysical Tools for Biologists, Volume One: In Vitro Techniques. Series: Methods in cell biology (84). Academic Press: Amsterdam ; London, pp. 327-373. ISBN 9780123725202 (doi: 10.1016/S0091-679X(07)84012-X)

Byron, O. (1995) Hydrodynamic modelling of the solution conformation of 10 S myosin. In: Behlke, J. (ed.) Analytical Ultracentrifugation. Series: Progress in colloid and polymer science (99). Steinkopff: Darmstadt, pp. 82-86. ISBN 9783798510388 (doi: 10.1007/BFb0114074)

This list was generated on Mon Nov 18 14:47:46 2024 GMT.

Grants

Grants and Awards listed are those received whilst working with the University of Glasgow.

  • Exploring a new method for a better screening of anti-virulence compounds to treat Enterohemorrhagic Escherichia Coli (EHEC) infections.
    Glasgow Children`s Hospital Charity
    2023 - 2023
     
  • Dynamics, Function, Structure - Deciphering complex machineries that produce ribosomally synthesised natural products
    Biotechnology and Biological Sciences Research Council
    2022 - 2024
     
  • Characterising AdhE: a new twist on drug design
    Biotechnology and Biological Sciences Research Council
    2021 - 2024
     
  • Where and Why: The Influence of Host Metabolism on Bacterial Niche Specificity
    Biotechnology and Biological Sciences Research Council
    2016 - 2019
     
  • A novel mechanism of protein uptake in Gram-negative bacteria
    Biotechnology and Biological Sciences Research Council
    2014 - 2018
     
  • Solution and structure of human PDC [Pyruvate Dehydrogenase Complex] Core
    Council for the Central Laboratory of the Research Councils
    2007 - 2007
     

Teaching

Undergraduate Teaching

Level 1 Microbiology and Virology lectures
Level 2 Contemporary Issues in Biology PBL tutorials
Level 2 Head of College Scholars List tutorials
Level 3 Medical Microbiology lectures, labs and tutorials
Level 4 Core Skills in Microbiology lectures and tutorials
Level 4 Grand Challenges in Microbiology lectures
Level 4 Personal Development Planning lectures
Level 4 Honours Project supervision

Postgraduate Teaching

MSc Bioinformatics lectures and project supervision
MSc Biomedical Sciences project supervision

Pastoral Care

Adviser of Studies

Academic Leadership

Deputy Head of Learning and Teaching (for Infection Biology), School of Life Sciences
Coordinator, Level 4 Core Skills in Microbiology Option
Coordinator, School of Life Sciences MSci with Work Placement Programme

School and University Committee Membership

School of Life Sciences Athena SWAN Committee
School of Life Sciences Learning and Teaching Committee
School of Life Sciences Mentoring and Career Development Group
School of Life Sciences Infection Biology Degree Group Committee, Convenor
School of Life Sciences Degree Group D Staff-Student Liaison Committee, Convenor
St Andrew's Society of the State of New York Scholarship interview panel
University Senate

Professional activities & recognition

Prizes, awards & distinctions

  • 2020: Rosalind Franklin Medal and Prize, Awarded to PoLNet2 steering group for contributions made to catalysing substantive growth of UK Physics of Life community by stimulating new, adventurous partnerships between multiple researchers in UK biological physics (Institute of Physics)

Grant committees & research advisory boards

  • 2018: European Synchrotron Radiation Facility (ESRF), Academic Member UK Delegation, Council
  • 2018: EMBL, Member, Hamburg Structural Biology Unit Review Panel
  • 2017 - 2017: Swedish Research Council (Vetenskapsradet), Vice-Chair, Panel NT-9 (Biochemistry and Structural Biology)
  • 2017 - 2021: Diamond Light Source, Member, Facility peer review panel for non-crystalline diffraction, solution state SAXS and circular dichroism
  • 2016: Engineering and Physical Sciences Research Council (EPSRC), Physics of Life Network Steering Group, Member
  • 2014: NRC Kurchatov Institute, Gatchina, Russia, Neutron Science Advisory Committee, Member
  • 2014: Science & Technology Facilities Council (STFC), Member, Consolidated Grants Implementation Review Panel
  • 2019: UKRI, Future Leaders Fellowships Sift Panel
  • 2019: UKRI, Future Leaders Fellowships Interview Panel
  • 2020: Physics of Medicine Network, Member, Steering Group
  • 2021: UKRI, Physics of Life Strategic Priority Fund Programme Mid-Term Evaluation Board

Editorial boards

  • 2014: Frontiers in Structural Biology. Review Editorial Board

Professional & learned societies

  • 2018: Chair, British Biophysical Society
  • 2016: Committee Member, British Biochemical Society
  • 2020 - 2023: Biophysical Society Ambassador for the United Kingdom, Biophysical Society

Selected international presentations

  • 2018: Invited plenary speaker, Physics of Life Summer School: New Approaches to Biomolecular Structure, Dynamics and Function. Microbiophysics: using biophysics to understand microbiology at a molecular level (Durham, UK)
  • 2018: Chair, Awards Lectures, British Biophysical Society Biennial Meeting (Southampton, UK)
  • 2017: Invited lecturer, EMBO Global Exchange Lecture Course on Structural and Biophysical Methods for Biological Macromolecules in solution. Combination of scattering and biophysical methods; Analytical ultracentrifugation (Singapore)
  • 2017: Scientific programme and organisation committee member, 19th International Union for Pure and Applied Biophysics (IUPAB) Congress and 11th European Biophysical Association Societies (EBSA) Congress (Edinburgh, UK)
  • 2017: Invited lecturer, EMBO Practical Course on Small Angle Neutron and X-ray Scattering from Proteins in Solution. Structural information obtained from analytical ultracentrifugation. (Grenoble, France)
  • 2017: Invited plenary speaker, High Brilliance Neutron Source Science Workshop. High-Brilliance Neutron Sources (HBS) & the Life Sciences (Unkel, Germany)
  • 2017: Chair, AUC 2017 - 23rd International AUC Workshop and Symposium (Glasgow, Scotland, UK)
  • 2017: Chair, Svedberg Lecture, AUC 2017 - 23rd International AUC Workshop and Symposium (Glasgow, Scotland, UK)
  • 2017: Co-Chair, Complementary Methods A: Small Angle Scattering, AUC (Glasgow, Scotland, UK)
  • 2016: Invited lecturer, EMBO Practical Course on solution scattering from biological macromolecules.Joint applications of SAXS/SANS and hydrodynamic methods in the studies of biomacromolecular solutions (Hamburg, Germany)
  • 2016: Invited lecturer, EMBO Global Exchange Lecture Course on Structural and Biophysical Methods for Biological Macromolecules in solution. Combination of scattering and biophysical methods; Analytical ultracentrifugation (Seoul & Gyeongbuk, Korea)
  • 2015: Invited lecturer, EMBO Practical Course on Small Angle Neutron and X-ray Scattering from Proteins in Solution. Structural information obtained from analytical ultracentrifugation. (Grenoble, France)
  • 2015: International programme committee member, 22nd International Conference on Analytical Ultracentrifugation (AUC2015) (Melbourne, Australia)
  • 2015: Invited plenary speaker, Workshop on Trends in Neutron Science, MLZ User Meeting.Small-angle neutron scattering: a pivotal role in biomolecular structure-function determination (Ismaning, Germany)
  • 2015: Invited lecturer, EMBO Global Exchange Lecture Course on Structural and Biophysical Methods for Biological Macromolecules in solution.Combination of scattering and biophysical methods; Analytical ultracentrifugation (Taipei, Taiwan)
  • 2014: Invited lecturer, EMBO Practical Course on solution scattering from biological macromolecules.Joint applications of SAXS/SANS and hydrodynamic methods in the studies of biomacromolecular solutions (Hamburg, Germany)
  • 2014: Invited speaker, "Current State-of-Art to Study Biomolecular Interactions and Assemblies in Life Sciences".Biomolecular interactions observed and quantified with AUC and SAS (Brno, Czech Republic)
  • 2014: Invited speaker, BBS Symposium on Complementary Non-Diffraction Techniques in Structural Biology.Multitasking like a woman: the emergence of simultaneous methodologies in small-angle scattering and hydrodynamics (London, UK)
  • 2014: Session co-chair, British Biophysical Society Biennial Meeting (Warwick, England, UK)
  • 2014: Invited speaker and organising committee member, ICNS Satellite Meeting: Neutrons in Biology and Biotechnology.Architecture of human pyruvate dehydrogenase complex determined with SAXS, SANS and AUC (Grenoble, France)
  • 2014: Invited lecturer, EMBO Global Exchange Lecture Course on Structural and Biophysical Methods for Biological Macromolecules in solution.Combination of scattering and biophysical methods; Analytical ultracentrifugation (Sao Paulo, Brazil)
  • 2018: Invited lecturer, FEBS Advanced Course: Hydrodynamic and thermodynamic analysis of biological macromolecules and their interactions (Prague, Czech Republic)
  • 2018: Invited lecturer, EMBO Practical Course on solution scattering from biological macromolecules (Hamburg, Germany)
  • 2019: Session co-chair, AUC 2019 (Canterbury, New Zealand)
  • 2019: Invited speaker, AUC 2019 (Canterbury, New Zealand)
  • 2019: Session co-chair, Queenstown Research Week (Queenstown, New Zealand)
  • 2019: Invited speaker, Queenstown Research Week (Queenstown, New Zealand)
  • 2019: Invited speaker, EMBO Practical Course on Small Angle Neutron and X-ray Scattering from Proteins in Solution (Grenoble, France)
  • 2019: Invited lecturer, EMBO Global Exchange Lecture Course on Structural and Biophysical Methods for Biological Macromolecules in Solution (Santiago, Chile)
  • 2020: Session chair, British Biophysical Society Biennial Meeting (Zoom)
  • 2021: Invited speaker (Memphis, USA)
  • 2020: Session co-chair, Launch meeting: Physics of Life and Medicine (Zoom)
  • 2021: Invited speaker, Modern Concepts in Structural Biology seminar series (Vienna, Austria)