Complete List of all our publications, with links to full texts where available
Machin, J.M., Kalli, A.C., Ranson, N.A. et al. Protein–lipid charge interactions control the folding of outer membrane proteins into asymmetric membranes. Nat. Chem. 15, 1754–1764 (2023). https://doi.org/10.1038/s41557-023-01319-6
White, J.B.R., Silale, A., Feasey, M. et al. Outer membrane utilisomes mediate glycan uptake in gut Bacteroidetes. Nature 618, 583–589 (2023). https://doi.org/10.1038/s41586-023-06146-w
Leistner, C., Wilkinson, M., Burgess, A. et al. The in-tissue molecular architecture of β-amyloid pathology in the mammalian brain. Nat Commun 14, 2833 (2023). https://doi.org/10.1038/s41467-023-38495-5
Chase, O., Javed, A., Byrne, M.J. et al. CryoEM and stability analysis of virus-like particles of potyvirus and ipomovirus infecting a common host. Commun Biol 6, 433 (2023). https://doi.org/10.1038/s42003-023-04799-x PMID: 37076658 PMCID: PMC10115852
Wilkinson M, Gallardo RU, Martinez RM, Guthertz N, So M, Aubrey LD, Radford SE, Ranson NA. Disease-relevant β2-microglobulin variants share a common amyloid fold. Nat Commun. 2023 Mar 2;14(1):1190. doi: 10.1038/s41467-023-36791-8. PMID: 36864041; PMCID: PMC9981686.
Kingston NJ, Grehan K, Snowden JS, Hassall M, Alzahrani J, Paesen GC, Sherry L, Hayward C, Roe A, Stephen S, Tomlinson D, Zeltina A, Doores KJ, Ranson NA, Stacey M, Page M, Rose NJ, Bowden TA, Rowlands DJ, Stonehouse NJ. VelcroVax: a "Bolt-On" Vaccine Platform for Glycoprotein Display. mSphere. 2023 Feb 21;8(1):e0056822. doi: 10.1128/msphere.00568-22. Epub 2023 Jan 31. PMID: 36719225; PMCID: PMC9942589.
Marr L, Biswas D, Daly LA, Browning C, Vial SCM, Maskell DP, Hudson C, Bertrand JA, Pollard J, Ranson NA, Khatter H, Eyers CE, Sakamoto K, Zeqiraj E. Mechanism of glycogen synthase inactivation and interaction with glycogenin. Nat Commun. 2022 Jun 11;13(1):3372. doi: 10.1038/s41467-022-31109-6. PMID: 35690592; PMCID: PMC9188544.
Wang C, Hesketh EL, Shamorkina TM, Li W, Franken PJ, Drabek D, van Haperen R, Townend S, van Kuppeveld FJM, Grosveld F, Ranson NA, Snijder J, de Groot RJ, Hurdiss DL, Bosch BJ. Antigenic structure of the human coronavirus OC43 spike reveals exposed and occluded neutralizing epitopes. Nat Commun. 2022 May 25;13(1):2921. doi: 10.1038/s41467-022-30658-0. PMID: 35614127; PMCID: PMC9132891.
Mohamad M, Nicholson D, Saha CK, Hauryliuk V, Edwards TA, Atkinson GC, Ranson NA, O'Neill AJ. Sal-type ABC-F proteins: intrinsic and common mediators of pleuromutilin resistance by target protection in staphylococci. Nucleic Acids Res. 2022 Feb 28;50(4):2128-2142. doi: 10.1093/nar/gkac058. PMID: 35137182; PMCID: PMC8887462.
Nicholson D, Salamina M, Panek J, Helena-Bueno K, Brown CR, Hirt RP, Ranson NA, Melnikov SV. Adaptation to genome decay in the structure of the smallest eukaryotic ribosome. Nat Commun. 2022 Feb 1;13(1):591. doi: 10.1038/s41467-022-28281-0. PMID: 35105900; PMCID: PMC8807834.
Patel N, Clark S, Weiß EU, Mata CP, Bohon J, Farquhar ER, Maskell DP, Ranson NA, Twarock R, Stockley PG. In vitro functional analysis of gRNA sites regulating assembly of hepatitis B virus. Commun Biol. 2021 Dec 16;4(1):1407. doi: 10.1038/s42003-021-02897-2. PMID: 34916604; PMCID: PMC8677749.
Johansson E, Caraballo R, Hurdiss DL, Mistry N, Andersson CD, Thompson RF, Ranson NA, Zocher G, Stehle T, Arnberg N, Elofsson M. Exploring the Effect of Structure-Based Scaffold Hopping on the Inhibition of Coxsackievirus A24v Transduction by Pentavalent N-Acetylneuraminic Acid Conjugates. Int J Mol Sci. 2021 Aug 5;22(16):8418. doi: 10.3390/ijms22168418. PMID: 34445134; PMCID: PMC8395083.
White, P., Haysom, S.F., Iadanza, M.G., Higgins, A.J., Machin, J.M., Whitehouse, J.M., Horne, J.E., Schiffrin, B., Carpenter-Platt, C., Calabrese, A.N., Storek, K.M., Rutherford, S.T., Brockwell, D.J., Ranson, N.A. & Radford, S.E. (2021). The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding. Nat Commun., 12:4174. https://doi.org/10.1038/s41467-021-24432-x.
Castells-Graells, R., Ribeiro, J.R.S., Domitrovic, T. et al. Plant-expressed virus-like particles reveal the intricate maturation process of a eukaryotic virus. Communications Biology, 4, 619 (2021). https://doi.org/10.1038/s42003-021-02134-w
Thuenemann, E.C.; Byrne, M.J.; Peyret, H.; Saunders, K.; Castells-Graells, R.; Ferriol, I.; Santoni, M.; Steele, J.F.C.; Ranson, N.A.; Avesani, L.; Lopez-Moya, J.J.; Lomonossoff, G.P. A Replicating Viral Vector Greatly Enhances Accumulation of Helical Virus-Like Particles in Plants. Viruses 2021, 13, 885. https://doi.org/10.3390/v13050885
Snowden, J.S., Alzahrani,H, Sherry, L., Stacey, M., Rowlands, D.J. Ranson, N.A. & Stonehouse, N.J. (2021). Structural insight into Pichia pastoris fatty acid synthase. Scientific Reports 11 (1), 1-11. https://www.nature.com/articles/s41598-021-89196-2
Klebl, D.P., Feasey, M.C., Hesketh, E.L., Ranson, N.A., Wurdak, H., Sobott, F., Bon, R.S., & Muench, S.P. (2020). Cryo-EM structure of human mitochondrial HSPD1. iScience, 102022. https://www.cell.com/iscience/fulltext/S2589-0042(20)31219-0
Swainsbury, D.J.K., Qian, P., Jackson, P.J., Faries, K.M., Niedzwiedzki, D.M., Martin, E.C., Farmer, D.A., Malone, L.A., Thompson, R.F., Ranson, N.A., Canniffe, D.P., Dickman, M.J., Holten, D., Kirmaier, C., Hitchcock, A. & Hunter, C.N. (2020). Cryo-EM structures of Rhodopseudomonas palustris RC-LH1 complexes with and without protein W. Science Advances 7 (3), eabe2631. https://advances.sciencemag.org/content/7/3/eabe2631/tab-article-info
Gray, D., White, J., Oluwole, A., Rath, P., Glenwright, A., Mazur, A., Zahn, M., Basle, A., Morland, C., Evans, S., Cartmell, A., Robinson, C.V., Hiller, S., Ranson, N.A., Bolam, D. & van den Berg, B. (2020). Insights into glycan import by a prominent gut symbiont. Nature Communications, 12, 1-14. https://www.nature.com/articles/s41467-020-20285-y
Scarff, C.A., Carrington, G.S., Casas-Mao, D., Chalovich, J., Knight, P.J., Ranson, N.A. & Peckham, M. (2020). Structure of the shutdown state of myosin-2. Nature, DOI:10.1038/s41586-020-2990-5. https://www.nature.com/articles/s41586-020-2990-5
Chandler-Bostock, R., Mata, C.P., Bingham, R.J., Dykeman, E.C., Meng, B., Tuthill, T.J., Rowlands, D.J., Ranson, N.A., Twarock, R. & Stockley, P.G. (2020). Assembly of Infectious Enteroviruses Depends on Multiple, Conserved Genomic RNA-Coat Protein Contacts. PLoS Pathogens 16 (12), e1009146. https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1009146
Iadanza, M.G., Schiffrin, B., White, P., Watson, M.A., Higgins, A.J., Calabrese, A.N., Brockwell, D.J., Tuma, R., Kalli, A., Radford, S.E. & Ranson, N.A. (2020). Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs. Communications Biology, 3, 1-14. https://www.nature.com/articles/s42003-020-01419-w
Gallardo, R., Iadanza, M.G., Xu, Y., Heath, G.R., Foster, R., Radford, S.E. & Ranson, N.A. (2020). The structures of wild-type amylin and its diabetes-related variant reveal a diversity of amyloid folds and a molecular basis for surface templated aggregation. Nature Structural & Molecular Biology, 27, p1048. https://www.nature.com/articles/s41594-020-0496-3
Nicholson, D., Edwards, T.A., O’Neill, A.J. & Ranson, N.A. (2020). Structure of the 70S ribosome from the human pathogen Acinetobacter baumannii in complex with clinically-relevant antibiotics. Structure, DOI: https://doi.org/10.1016/j.str.2020.08.004. https://www.cell.com/structure/fulltext/S0969-2126(20)30286-0
Madej, M., White, J., Nowakowska, Z., Rawson, S.D., Pothula, K., Scavenius, C., Enghild, J., Kleinekathoefer, U., Ranson, N.A.,Potempa, J. & van den Berg, B. (2020). Structural and functional insights into oligopeptide acquisition by the RagAB transporter from Porphyromonas gingivalis. Nature Microbiology, DOI:10.1038/s41564-020-0716-y. https://www.nature.com/articles/s41564-020-0716-y
Snowden, J.S., Hurdiss, D.L., Adeyemi, O.O., Ranson, N.A., Herod, M.R. & Stonehouse, N.J. (2020). Dynamics in the murine norovirus capsid revealed by high-resolution cryo-EM. PLoS Biology, DOI:10.1371/ journal.pbio.3000649. https://journals.plos.org/plosbiology/article?id=10.1371/journal.pbio.3000649
Malone, L.A., Qian, P., Mayneord, G.E., Hitchcock, A., Farmer, D.A., Thompson, R.F., Swainsbury, D.J.K., Ranson, N.A., Hunter, C.N. & Johnson, M.P. (2019). Cryo-EM structure of the spinach cytochrome b6f complex at 3.6 Å resolution. Nature, 575, 535-39. https://www.nature.com/articles/s41586-019-1746-6
Ohmann, A., Göpfrich, K., Joshi, H., Thompson, R.F., Ranson, N.A., Aksimentiev, A. & Keyser, U.F. (2019). Controlling aggregation of cholesterol-modified DNA nanostructures. Nucleic Acid Res. 10.1093/nar/gkz914. https://academic.oup.com/nar/article/47/21/11441/5603226
Gallardo, R., Ranson, N.A. ‡ & Radford, S.E. ‡ (2019). Amyloid Structures: Much More Than Just A Cross-Beta Fold. Curr. Opin. Struct. Biol., 60, 7-16. https://www.sciencedirect.com/science/article/pii/S0959440X19301022
Byrne, M.J., Steele, J.C., Hesketh, E.L, Walden, M., Thompson, R.F, Lomonossoff, G.P. & Ranson, N.A. (2019). Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles. Structure, 27, 1-10. https://www.cell.com/structure/fulltext/S0969-2126(19)30316-8
Marsian, J., Hurdiss, D.L., Ranson, N.A., Ritala, A.M., Paley, R.K., Cejas, I.C. & Lomonossoff, G.P. (2019). Plant-made Nervous Necrosis Virus-like particles protect fish against disease. Front. Plant. Sci. DOI:10.3389/fpls.2019.00880. https://www.frontiersin.org/articles/10.3389/fpls.2019.00880/full
Hesketh, E.L., Tiede. C., Adamson, H., Adams, T.L., Byrne, M.J., Meshcheriakova, Y., Kruse, I., McPherson, M.J., Lomonossoff, G.P., Tomlinson, D.C. & Ranson, N.A. (2019). Affimer reagents as tools in diagnosing plant virus diseases. Scientific Reports, DOI:10.1038/s41598-019-43945-6. https://www.nature.com/articles/s41598-019-43945-6
Walden, M., Lei, T., Sykora, U, Hesketh, E.L. Byrne, D., Masandi, S.K., Cassel, J., George, R., Ault, J., Pawłowski, K., Eyers, P., Ranson, N.A., Salvino, J., Greenberg, R., & Zeqiraj, E. (2019). Metabolic control of SHMT2 oligomerization regulates the deubiquitinylating activity of BRCC36 and ubiquitin-dependent cytokine signalling. Nature, 570:194-199. https://www.nature.com/articles/s41586-019-1232-1
Leng, J., Shoura, M., McLeish, T., Real, A., Hardey, M., McCafferty, J., Ranson, N.A. & Harris, S.A. (2019). Securing the Future of Research Computing in the Biosciences. PLoS Comp. Biol., DOI:10.1371/ journal.pcbi.1006958.https://journals.plos.org/ploscompbiol/article?id=10.1371/journal.pcbi.1006958
Bayfield, O.W., Klimuk, E., Winkler, D.C., Hesketh, E.L., Chechik, M., Cheng, N., Dykeman, E.C., Minakhin, L., Ranson, N.A., Severinov, K., Steven, A.C. & Antson, A.A. (2019). Cryo-EM structure and in vitro DNA packaging of a thermophilic virus with supersized T=7 capsids Proc. Natl. Acad. Sci. USA., DOI:10.1073/pnas.1813204116.https://www.pnas.org/content/116/9/3556
Thompson, R.F., Iadanza, M.G., Hesketh, E.L., Rawson, S.D. & Ranson, N.A. (2019). Collection, pre-processing, and on-the-fly analysis of data for high-resolution, single-particle cryo-electron microscopy. Nature Protocols. https://doi.org/10.1038/s41596-018-0084-8
Iadanza, M.G., Silvers, R., Boardman, J., Smith, H., Karamanos, T., Griffin, R.G., Ranson, N.A.and Radford, S.E.. (2018). The cryo-EM structure of a b-2-microglobulin fibril shows the molecular basis of a common amyloid architecture. Nature Communications, https://doi.org/10.1038/s41467-018-06761-6
Iadanza, M.G., Jackson, M.P., Hewitt, E.W., Ranson, N.A.& Radford, S.E. (2018) Seeing Amyloid Structures: A New Era for Understanding Amyloid Disease. Nat. Rev. Mol. Cell Biol., https://doi.org/10.1038/s41580-018-0060-8
Hesketh, E.L, Saunders, K., Fisher, C., Potze, J., Stanley, J., Lomonossoff, G.P. & Ranson, N.A.(2018). How to build a geminate virus capsid. Nature Communications, 9, 2369. https://www.nature.com/articles/s41467-018-04793-6.pdf
Drulyte, I., Johnson, R., Hesketh, E.L, Hurdiss, D.L, Scarff, C.A., Ranson, N.A., Muench, S.P. & Thompson, R.F. (2018). Approaches to altering particle distributions in cryo-electron microscopy. Acta Cryst. D., 74, 560-71. http://journals.iucr.org/d/issues/2018/06/00/ic5104/ic5104.pdf
Hurdiss, D.L., Martin, F., Snowden, J.S., Macdonald, A. & Ranson, N.A.(2018) The structure of human BK polyomavirus and its interactions with distinct cellular receptors. Structure, 26, p1-9. https://www.sciencedirect.com/science/article/pii/S0969212618301230?via%3Dihub
Panou, M.M., Prescott, E., Hurdiss, D., Swinscoe, G., Hollinshead, M., Caller, L., Morgan, E., Carlisle, L., Muller, M., Antoni, M., Kealy, D., Ranson, N.A., Crump, C. & Macdonald, A. (2018). Agnoprotein is an essential egress factor during BK polyomavirus infection. Int. J. Mol. Sci., DOI:10.3390/ ijms19030902. http://www.mdpi.com/1422-0067/19/3/902
Baggen, J.*, Hurdiss, D.L.*, Zocher, G., Mistry, N., Roberts, R.W., Slager, J.J., van Vliet, A.L.W., Casasnovas, J.M., Arnberg, N., Stehle, T., Ranson, N.A., Thibaut, H.J., & van Kuppeveld, F.J.M, (2017). The role of evolutionary enhancement of receptor binding in the emergence of pandemic viral conjunctivitis. Proc. Natl. Acad. Sci. U.S.A., 115, p397-402 http://www.pnas.org/content/115/2/397.long
Lomonossoff, G.P., Meshcheriakova, Y., Durrant, A., Hesketh, E.L. & Ranson, N.A. (2017). Combining high resolution cryo-electron microscopy and mutagenesis to develop cowpea mosaic virus for bionanotechnology. Biochem Soc. Transactions. DOI:10.1042/bst20160312 http://www.biochemsoctrans.org/content/ppbiost/early/2017/11/01/BST20160312.full.pdf
Patel, N.*, White, S.J.*, Thompson, R.F., Weiß, E.U., Bingham, R., Zlotnick, A., Dykeman, E., Twarock, R.,‡ Ranson, N.A.‡ & Stockley, P.G.‡ (2017). The HBV RNA pregenome encodes specific interactions with the viral core protein that can promote nucleocapsid assembly. Nature Microbiology, doi:10.1038/nmicrobiol.2017.98 https://www.nature.com/articles/nmicrobiol201798
Hesketh, E. L., Meshcheriakova, Y., Thompson, R. F., Lomonossoff, G. P., & Ranson, N. A. (2017). The structures of a naturally empty cowpea mosaic virus particle and its genome-containing counterpart by cryo-electron microscopy. Scientific Reports, 7(1), 539. DOI:10.1038/s41598-017-00533-w. https://www.nature.com/articles/s41598-017-00533-w
Dobson, C.L., Higazi, D.R., Lloyd, C., Phillips, J.J., Devine, P., Popovic, B., Buchanan, A., Lewis, A., Goodman, J., van der Walle, C., Tracka, M., Iadanza, M.G., Ranson, N.A., Ashcroft, A.E., Kippen, A.D., Vaughan, T.J., Radford, S.E.*, and Lowe, D.C.* (2016). Engineering the surface properties of a human monoclonal antibody prevents self-association & enhances tissue specificity. Scientific Reports, 6(1), 38644. DOI: /10.1038/srep38644 http://www.nature.com/articles/srep38644
Iadanza, M.G*., Higgins, A.J.*, Schiffrin, R., Calabrese, A., Brockwell, D.J., Ashcroft, A.E. Radford, S.E. ‡ & Ranson, N.A.‡ (2016). Lateral opening of the intact β-barrel assembly machinery captured by cryo-EM. Nature Comms. DOI:10.1038/ncomms12865. http://www.nature.com/articles/ncomms12865
Huynh, N., Hesketh, E.L., Saxena, P., Meshcheriakova, Y., Ku, Y-C., Hoang, L., Johnson, J.E., Ranson, N.A., Lomonossoff, G.P. & Reddy, V.S. (2016) Crystal structure and proteomics analysis of empty virus like particles of Cowpea mosaic virus. Structure, DOI: 10.1016/j.str.2016.02.011. http://www.sciencedirect.com/science/article/pii/S0969212616000708?via%3Dihub
Stockley, P.G., White, S.J., Dykeman, E., Manfield, I., Rolfsson, I., Patel, N., Bingham, R., Barker, A., Wroblewski, E., Chandler-Bostock, R., Weiß, E.U. Ranson, N.A., Tuma, R., & Twarock, R. (2016). Bacteriophage MS2 Genomic RNA Encodes an Assembly Instruction Manual for Its Capsid. Bacteriophage. DOI:10.1080/21597081.2016.1157666. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4836477/
Rawson S., Iadanza M.G., Ranson N.A. & Muench S.P. (2016). Multiple methods to account for movement and flexibility in cryo-EM data processing. Methods. DOI: 10.1016/ j.ymeth.2016.03.011. http://www.sciencedirect.com/science/article/pii/S1046202316300445?via%3Dihub
Thompson, R.F., Walker, M.L., Siebert, C.A., Muench, S.P. & Ranson, N.A. (2016). Electron microscopy methods in the wake of the ‘resolution revolution’. Methods, DOI:10.1016/ j.ymeth.2016.02.017. http://www.sciencedirect.com/science/article/pii/S1046202316300330?via%3Dihub
Hurdiss, D.L., Thompson, R.F., Morgan, E.L., Prescott, E.L., Panou, M.M., Macdonald, A. & Ranson, N.A. (2016). New structural insights into the genome and minor capsid proteins of BK polyomavirus using cryo-electron microscopy. Structure, DOI:10.1016/ j.str.2016.02.008. http://www.sciencedirect.com/science/article/pii/S0969212616000538?via%3Dihub
Iadanza, M.G, Jackson, M., Radford, S.E. & Ranson, N.A. (2016). MpUL-multi: Software for Calculation of Amyloid Fibril Mass per Unit Length from TB-TEM Images. Sci. Reports., DOI: 10.1038/srep21078. http://www.nature.com/articles/srep21078
Hesketh, E.L., Meshcheriakova, Y., Dent, K.C., Saxena, P., Thompson, R.F., Cockburn, J.J.B, Lomonossoff, G.P. & Ranson, N.A. (2015). Mechanisms of assembly and genome packaging in an RNA virus revealed by high-resolution cryo-EM. Nature Comms., DOI:10.1038/ncomms10113. http://www.nature.com/articles/ncomms10113
Rolfsson, O., Middleton, S., Manfield, U., White, S.J., Fan, B., Vaughan, R., Ranson, N.A., Dykeman, E., Twarock, R., Ford, F., Kao, C.C. & Stockley, P.G. (2015). Direct Evidence for Packaging Signal-mediated Assembly of Bacteriophage MS2. J. Mol. Biol., DOI:10.1016/j.jmb.2015.11.014. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4751978/
Tipping, K.W., Karamanos, T.K., Jakhira, T., Iadanza, M., Goodchild, S.C., Tuma, R., Ranson, N.A., Hewitt, E.W. & Radford, S.E. (2015). pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers. Proc. Natl. Acad. Sci. U.S.A., 112, 5691-6. http://www.pnas.org/content/112/18/5691
Geraets, J.A., Dykeman, E.C., Stockley, P.G., Ranson, N.A. & Twarock, R. (2015). Asymmetric genome organization in an RNA virus revealed via graph-theoretical analysis of tomographic data. PLoS Comp. Biol. DOI:10.1371/journal.pcbi.1004146. http://journals.plos.org/ploscompbiol/article?id=10.1371/journal.pcbi.1004146
Patel, N., Dykeman, E.C., Coutts, R.H.A., Lomonossoff, G., Rowlands, D.J., Phillips, S.E.V., Ranson, N.A., Twarock, R., Tuma, R. & Stockley, P.G. (2015). Revealing the density of encoded functions in a viral RNA. Proc. Natl. Acad. Sci. U.S.A., 112, p2227-32. http://www.pnas.org/content/112/7/2227.short
Goodchild, S.C., Sheynis, T., Thompson, R., Tipping, K.W., Xue, W.F., Ranson, N.A., Beales, P.A., Hewitt, E.W. & Radford, S.E. (2014). β2-Microglobulin Amyloid Fibril-Induced Membrane Disruption Is Enhanced by Endosomal Lipids and Acidic pH. PLoS One, 9 (8), e104492. http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0104492
Bakker, S.E., Groppelli, E., Pearson, A.R., Stockley, S.G., Rowlands, D.J. & Ranson, N.A. (2014). Limits of Structural Plasticity in a Picornavirus Capsid Revealed by a Massively Expanded Equine Rhinitis A Virus Particle. J. Virol., 88, p6093 http://jvi.asm.org/content/88/11/6093.long
Young, A., Stoilova-McPhie, S., Rothnie, A., Vallis, Y., Harvey-Smith, P., Ranson, N.A., Kent, H., Brodsky, F.M.,Pearse, B.M.F., Roseman, A.M., & Smith, C.J. (2013). Hsc70- induced changes in clathrin-auxilin cage structure suggest a role for clathrin light chains in cage disassembly. Traffic, 14, p867. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3776051/
Dent, K.C., Thompson, R., Barker, A.M., Barr, J.N., Hiscox, J.A., Stockley, P.G. & Ranson, N.A. (2013). The asymmetric structure of an icosahedral virus bound to its receptor suggests a mechanism for genome release. Structure, 21, p1225. http://www.sciencedirect.com/science/article/pii/S0969212613001949?via%3Dihub
Stockley, P.G., Twarock, R.T., Bakker, S.E., Barker, A.M., Borodavka, A., Dykeman, E., Ford, R.J., Pearson, A.R., Phillips, S.E.V., Ranson, N.A. & Tuma, R. (2013). Packaging signals in single-stranded RNA viruses: Nature’s alternative to a purely electrostatic assembly mechanism. J. Biol. Phys., 39, p277. https://link.springer.com/article/10.1007%2Fs10867-013-9313-0
Stockley, P.G., Ranson, N.A. & Twarock (2013). A new paradigm for the roles of the genome in ssRNA viruses. Future Virology, 8, p531. https://www.futuremedicine.com/doi/abs/10.2217/fvl.12.84
Ariza, A., Tanner, S.J., Walter, C.T., Dent, K.C., Shepherd, D.A., Wu, W., Matthews, S.V., Hiscox, J.A., Green, T.J., Luo, M., Elliott, R.M., Fooks, A.R., Ashcroft, A.E., Stonehouse, N.J., Ranson, N.A., Barr, J.N. & Edwards, T.A. (2013). Nucleocapsid protein structures from orthobunyaviruses reveal insight into ribonucleoprotein architecture and RNA polymerization. Nucleic Acid. Res., 41, p5912. https://academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkt268
Keef, T., Wardman, J.P., Ranson, N.A., Stockley, P.G. & Twarock, R. (2013). Structural constraints on the 3D Geometry of simple viruses: case studies of a new predictive tool. Acta. Cryst. Sect. A., 69, p140. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3571114/
Ford, R.J., Barker, A.M, Bakker, S.E., Coutts, R.H., Ranson, N.A., Phillips, S.E.V, Pearson, A.R. & Stockley, P.G. (2013). Sequence-specific, RNA–protein interactions overcome electrostatic barriers preventing assembly of satellite tobacco necrosis virus coat protein. J. Mol. Biol., 425, p1050. http://www.sciencedirect.com/science/article/pii/S0022283613000077?via%3Dihub
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