Christodoulou, John - Birkbeck, University of London - Department of Biological Sciences

研究领域

Studies of co-translational protein folding and misfolding processes on intact ribosomes NMR studies of intact cells Studies of intrinsically unstructured proteins involved in neurodegenerative disease NMR studies to characterize disease-related protein metastability in serpins Biomolecular NMR spectroscopy

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Cassaignau, A.M., Launay, H.M., Karyadi, M.E., Wang, X., Waudby, C.A., Deckert, A., ...Cabrita, L.D. (2016). A strategy for co-translational folding studies of ribosome-bound nascent chain complexes using NMR spectroscopy.. Nature protocols, 11 (8), 1492-1507. Cabrita, L.D., Cassaignau, A.M.E., Launay, H.M.M., Waudby, C.A., Wlodarski, T., Camilloni, C., ...Wentink, A.S. (2016). A structural ensemble of a ribosome-nascent chain complex during cotranslational protein folding. Nature Structural and Molecular Biology, 23 (4), 278-285. doi:10.1038/nsmb.3182 Valleix, S., Verona, G., Jourde-Chiche, N., Nedelec, B., Mangione, P.P., Bridoux, F., ...Lhomme, M. (2016). D25V apolipoprotein C-III variant causes dominant hereditary systemic amyloidosis and confers cardiovascular protective lipoprotein profile. NATURE COMMUNICATIONS, 7 doi:10.1038/ncomms10353 Deckert, A., Waudby, C.A., Wlodarski, T., Wentink, A.S., Wang, X., Kirkpatrick, J.P., ...Dobson, C.M. (2016). Structural characterization of the interaction of alpha-synuclein nascent chains with the ribosomal surface and trigger factor. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 113 (18), 5012-5017. doi:10.1073/pnas.1519124113 Ahn, M., Hagan, C.L., Bernardo-Gancedo, A., De Genst, E., Newby, F.N., Christodoulou, J., ...Dobson, C.M. (2016). The Significance of the Location of Mutations for the Native-State Dynamics of Human Lysozyme.. Biophys J, 111 (11), 2358-2367. doi:10.1016/j.bpj.2016.10.028 Waudby, C.A., Ramos, A., Cabrita, L.D., Christodoulou, J. (2016). Two-Dimensional NMR Lineshape Analysis. Scientific Reports, 6 doi:10.1038/srep24826 Nyon, M.P., Prentice, T., Day, J., Kirkpatrick, J., Sivalingam, G.N., Levy, G., ...Christodoulou, J. (2015). An integrative approach combining ion mobility mass spectrometry, X-ray crystallography, and nuclear magnetic resonance spectroscopy to study the conformational dynamics of (1)-antitrypsin upon ligand binding. PROTEIN SCIENCE, 24 (8), 1301-1312. doi:10.1002/pro.2706 Yu, C.W.-.H., Chu, L., Wang, X., Waudby, C.A., Christodoulou, J., Cabrita, L.D. (2015). Co-translational protein folding studies of alpha-1 antitrypsin. Chan, S.H.S., Waudby, C.A., Cassaignau, A.M.E., Cabrita, L.D., Christodoulou, J. (2015). Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosome-nascent chain complexes. JOURNAL OF BIOMOLECULAR NMR, 63 (2), 151-163. doi:10.1007/s10858-015-9968-x Wlodarski, T., Waudby, C., Sammy, C., Vendruscolo, M., Christodoulou, J. (2015). The Computational Studies of Co-Translational Protein Folding. Porcari, R., Proukakis, C., Waudby, C.A., Bolognesi, B., Mangione, P.P., Paton, J.F., ...Relini, A. (2015). The H50Q mutation induces a 10-fold decrease in the solubility of α-synuclein.. JOURNAL OF BIOLOGICAL CHEMISTRY, 290 (4), 2395-2404. doi:10.1074/jbc.M114.610527 Allison, J.R., Rivers, R.C., Christodoulou, J.C., Vendruscolo, M., Dobson, C.M. (2014). A Relationship between the Transient Structure in the Monomeric State and the Aggregation Propensities of α-Synuclein and β-Synuclein. Biochemistry, 53 (46), 7170-7183. doi:10.1021/bi5009326 Blombach, F., Launay, H., Snijders, A.P., Zorraquino, V., Wu, H., de Koning, B., ...Cavalli, A. (2014). Archaeal MBF1 binds to 30S and 70S ribosomes via its helix-turn-helix domain.. BIOCHEMICAL JOURNAL, 462 373-384. doi:10.1042/BJ20131474 Cassaignau, A., Cabrita, L., Waudby, C., Wang, X., Launay, H., Camilloni, C., ...Dobson, C. (2014). Structural investigation of the folding of an immunoglobulin domain on the ribosome using NMR Spectroscopy. FASEB JOURNAL, 28 (1), Christodoulou, J. (2014). Structure and dynamics of ribosome-bound nascent chains: insights from NMR spectroscopy. Tóth, G., Gardai, S.J., Zago, W., Bertoncini, C.W., Cremades, N., Roy, S.L., ...Skibinski, G. (2014). Targeting the intrinsically disordered structural ensemble of α-synuclein by small molecules as a potential therapeutic strategy for Parkinson's disease.. PLOS ONE, 9 (2), doi:10.1371/journal.pone.0087133 De Genst, E., Chan, P.H., Pardon, E., Hsu, S.T., Kumita, J.R., Christodoulou, J., ...Muyldermans, S. (2013). A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation.. JOURNAL OF PHYSICAL CHEMISTRY B, 117 (42), 13245-13258. doi:10.1021/jp403425z Christodoulou, J. (2013). Co-Translational Protein Folding on the Ribosome: using NMR Spectroscopy to Provide Structure and Dynamics of Ribosome-Nascent Chains. Waudby, C.A., Camilloni, C., Fitzpatrick, A.W., Cabrita, L.D., Dobson, C.M., Vendruscolo, M., Christodoulou, J. (2013). In-cell NMR characterization of the secondary structure populations of a disordered conformation of α-synuclein within E. coli cells.. PLOS ONE, 8 (8), doi:10.1371/journal.pone.0072286 Guilliams, T., El-Turk, F., Buell, A.K., O'Day, E.M., Aprile, F.A., Esbjörner, E.K., ...Wyns, L. (2013). Nanobodies raised against monomeric α-synuclein distinguish between fibrils at different maturation stages.. Journal of molecular biology, 425 (14), 2397-2411. Christodoulou, J., Waudby, C.A. (2013). NMR of Biomolecules: Towards Mechanistic Systems Biology. Edited by Ivano Bertini, Kathleen S. McGreevy and Giacomo Parigi.. ChemBioChem, 14 (14), 1906. doi:10.1002/cbic.201300209 Waudby, C.A., Launay, H., Cabrita, L.D., Christodoulou, J. (2013). Protein folding on the ribosome studied using NMR spectroscopy.. PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY, 74 57-75. doi:10.1016/j.pnmrs.2013.07.003 Waudby, C.A., Christodoulou, J. (2012). An analysis of NMR sensitivity enhancements obtained using non-uniform weighted sampling, and the application to protein NMR.. JOURNAL OF MAGNETIC RESONANCE, 219 46-52. doi:10.1016/j.jmr.2012.04.013 Waudby, C.A., Mantle, M.D., Cabrita, L.D., Gladden, L.F., Dobson, C.M., Christodoulou, J. (2012). Rapid distinction of intracellular and extracellular proteins using NMR diffusion measurements.. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 134 (28), 11312-11315. doi:10.1021/ja304912c Nyon, M.P., Segu, L., Cabrita, L.D., Lévy, G.R., Kirkpatrick, J., Roussel, B.D., ...Kerr, R. (2012). Structural dynamics associated with intermediate formation in an archetypal conformational disease.. STRUCTURE, 20 (3), 504-512. doi:10.1016/j.str.2012.01.012