Publications

2018

Mapping Surface Hydrophobicity of alpha-Synuclein Oligomers at the Nanoscale
Lee, J., Sang J.C., Rodrigues M., Carr, A.R., Horrocks, M.H., De, S., Bongiovanni, M.N., Flagmeier, P., Dobson, C.M., Wales D.J., Lee, S.F., Klenerman, D.
Nano Letters, Just Published, 2018. http://dx.doi.org/10.1021/acs.nanolett.8b02916



Nanoscopic characterization of individual endogenous protein aggregates in human neuronal cells
Whiten, D.R., Zuo, Y., Calo, L., Choi, M., De, S., Flagmeier, P., Wirthensohn, D.C., Kundel, F., Ranasinghe, R.T., Sanchez, S.E., Athauda, D., Lee, S.F., Dobson, C.M., Gandhi, S., Spillantini, M., Klenerman, D., Horrocks, M.H.
ChemBioChem, Just Published, 2018. http://dx.doi.org/10.1002/cbic.201800209



Extrinsic Amyloid-Binding Dyes for the Detection of Individual Protein Aggregates in Solution
Taylor, C.G., Meisl, G., Horrocks, M.H., Zetterberg, H., Knowles, T.P.J., Klenerman, D.
Analytical Chemistry, Just Published, 2018. http://dx.doi.org/10.1021/acs.analchem.8b02226



Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic alpha-Synuclein Oligomers
Whiten, D.R., Dezerae, D., Horrocks, M.H., Taylor, C.G., De, S., Flagmeier, P., Tosatto, L., Kumita, J.R., Ecroyd, H., Dobson, C.M., Klenerman, D.
Cell Reports, 23, 3492-3500, 2018. http://dx.doi.org/10.1016/j.celrep.2018.05.074



alpha-Synuclein Oligomers Interact with ATP Synthase and Open the Permeability Transition Pore in Parkinson???s Disease
Ludtmann, M. H. R.*, Angelova, P. R.*, Horrocks, M. H.*, Choi, M. L., Rodrigues, M., Baev, A. Y., Berezhnov, A. V., Yao, Z., Little, D., Banushi, B., Al-Menhali, A.S., Ranasinghe, R.T., Whiten, D.R., Yapom, R., Dolt, K.S., Devine, M.J., Gissen, P., Kunath, T., Jaganjac, M., Pavlov, E.V., Klenerman, D., Abramov, A.Y., S. Gandhi, S. *Joint first authors
Nature Communications, 9 (1), 2293, 2018. http://dx.doi.org/10.1038/s41467-018-04422-2



A sticky situation: aberrant protein-protein interactions in Parkinson???s disease
Brown, J.W.P., Horrocks, M.H.
Seminars in Cell & Developmental Biology, Just Published, 2018. http://dx.doi.org/10.1016/j.semcdb.2018.05.006



Shedding light on aberrant interactions: A review of modern tools for studying protein aggregates
Kundel, F., Tosatto, L.T., Whiten, D.R., Wirthensohn, D.C., Horrocks, M.H.*, Klenerman, D.*
The FEBS Journal, 1742-4658, 2018. http://dx.doi.org/10.1111/febs.14409



Detecting RNA base methylations in single cells by in situ hybridization
Ranasinghe, R.T., Challand, M.R., Ganzinger, K.A., Lewis, B.W., Softley, C., Schmied, W.H., Horrocks, M.H., Shivji, N., Chin, J.W, Spencer, J., Klenerman, D.
Nature Communications, 9, 2018. http://dx.doi.org/10.1038/s41467-017-02714-7



The small heat shock protein Hsp27 binds alpha-synuclein fibrils, preventing elongation and cytotoxicity
Cox, D., Whiten, D.R., Brown, J.W.P., Horrocks, M.H., San Gil, R., Dobson, C.M., Klenerman, D., van Oijen, A.M., Ecroyd, H.
Journal of Biological Chemistry, 293(12) 4486 ???4497, 2018. http://dx.doi.org/10.1074/jbc.M117.813865



Hsp70 Inhibits the Nucleation and Elongation of Tau and Sequesters Tau Aggregates with High Affinity
Kundel, F., De, S., Flagmeier, P., Horrocks, M.H., Kjaergaard, M., Shammas, S.L., Jackson, S.E., Dobson, C.M., Klenerman, D.
ACS Chemical Biology, 13 (3), pp 636???646, 2018. http://dx.doi.org/10.1021/acschembio.7b01039



2017

Nanobodies raised against monomeric alpha-synuclein inhibit fibril formation and destabilize toxic oligomeric species.
Iljina, M., Hong, L, Horrocks, M.H., Ludtmann, M.H., Choi, M.L., Hughes, C.D. Ruggeri, F.S. Guilliams, T., Buell, A.K., Lee, J.E., Gandhi, S., Lee, S.F, Bryant, C.E., Vendruscolo, M., Knowles, T.P.J., Dobson, C.M., De Genst, E., Klenerman, D.
BMC Biology, 15, 57, 2017. http://dx.doi.org/10.1186/s12915-017-0390-6



PEGylated liposomes associate with Wnt3A protein and expand putative stem cells in human bone marrow populations.
Janeczek, AA, Scarpa, E., Horrocks M.H, Tare, R.S., Rowland, C.A., Jenner, D., Newman, T.A., Oreffo, R.O.C., Lee, S.F., Evans, N.D.
Nanomedicine, 12, 8, 2017. http://dx.doi.org/10.2217/nnm-2016-0386



Co-aggregation of κ-Casein and β-Lactoglobulin Produces Morphologically Distinct Amyloid Fibrils.
Raynes, J.K., Crepin, P., Horrocks, M.H., Carver, J.A., Day, L.
Small, 13, 14, 2017. http://dx.doi.org/10.1002/smll.201603591



2016

Multi-dimensional super-resolution imaging enables surface hydrophobicity mapping.
Bongiovanni, M.*, Godet, J.*,Horrocks, M.H.*, Tosatto, L., Carr, A.R, Wirthensohn, D.C., Ranasinghe, R.T., Lee, J., Ponjavic, A., Fritz, J.V., Dobson, C.M., Klenerman, D., Lee, S.F.
Nature Communications, 7, 2016. http://dx.doi.org/10.1038/ncomms13544



The remarkably low affinity of CD4/peptide-major histocompatibility complex class II protein interactions.
Jonsson P., Southcombe J., Mafalda A., Santos A.M., Fernandes R.A., McColl J., Chang V.C., Godkin A., Dunne P.D., Horrocks M.H., Palayret M., Fugger L., Xu X., Davis S.J., Klenerman D.
PNAS, 113, 20, 2016. http://dx.doi.org/10.1073/pnas.1513918113



PSD95 nanoclusters are postsynaptic building blocks in hippocampus circuits.
Broadhead M.J., Horrocks M.H., Zhu F., Muresan L., Benavides-Piccione R., DeFelipe J., Fricker D., Kopanitsa M.V., Duncan R.R., Klenerman D., Komiyama N.H., Lee S.F., Grant S.G.N.
Scientific Reports, 6, 2016. http://dx.doi.org/10.1038/srep24626



A kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading.
Iljina,M., Garciaa, G.A., Horrocks, M.H., Tosatto, L., Choi, M.L., Ganzinger, K.A., Abramov, A.Y., Gandhi, S., Wood, N.W., Cremades, N.,Dobson, C.M. , Knowles, T.P.J., Klenerman, D.
PNAS, 113, 9, 2016. http://dx.doi.org/10.1073/pnas.1524128113



Single-molecule imaging of individual amyloid protein aggregates in human biofluids.
Horrocks M. H., Lee S.F., Gandhi S., Magdalinou N.K., Chen S.W., Devine M.J., Toasatto, L., Kjaergaard M., Beckwith J.S., Zetterberg H., Iljina M., Cremades N., Dobson C.M., Wood N.W., Klenerman D.
ACS Chemical Neuroscience, 7, 3, 2016. http://dx.doi.org/10.1021/acschemneuro.5b00324



Calcium is a key factor in alpha-synuclein induced neurotoxicity.
Angelova, P., Ludtmann, M., Horrocks, M.H., Negoda, A., Cremades, N., Klenerman, D., Dobson, C.M., Wood, N., Pavlov, E., Gandhi, S., Abramov, A.
Journal of Cell Science, 129, 9, 2016. http://dx.doi.org/10.1242/jcs.180737



2015

Alpha-synuclein oligomers interact with metal ions to induce oxidative stress and neuronal death in Parkinson's disease.
Deas, E., Cremades, N., Angelova, P.R., Ludtmann, M., Yao, Z., Chen, S., Horrocks, M.H., Banushi, B., Little, D., Devine, M., Gissen P., Klenerman, D., Dobson, C.M., Wood, N., Gandhi, S., Abramov. A.Y.
Antioxidants and redox signaling, 24, 7, 2015. http://dx.doi.org/10.1089/ars.2015.6343



Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson's disease genetically related mutants.
Horrocks, M.H., Tosatto, L., Dear, A.J., Knowles, T.P.J., Dalla Serra, M., Dobson, C.M., Klenerman, D.
Scientific Reports, 5, 2015. http://dx.doi.org/10.1038/srep16696



Fast flow microfluidics and single-molecule fluorescence for the rapid characterization of alpha-synuclein oligomers.
Horrocks, M.H., Tosatto, L., Dear, A.J., Garcia, G.A., Iljina, M., Cremades, N., Dalla Serra, M., Knowles, T.P.J., Dobson, C.M., Klenerman, D.
Analytical Chemistry, 87, 17, 2015. http://dx.doi.org/10.1021/acs.analchem.5b01811



Aggregated alpha-synuclein and complex I deficiency: exploration of their relationship in differentiated neurons.
Reeve, A.K., Ludtmann, M.H.R, Angelova, P.R., Simcox, E.M., Horrocks, M.H., Klenerman, D., Gandhi, S., Turnbull, D.M., Abramov, A.Y.
Cell Disease and Death, 6, 2015. http://dx.doi.org/10.1038/cddis.2015.166



Lipid peroxidation is essential for alpha-synuclein-induced cell death.
Angelova, P.R., Horrocks, M.H., Klenerman D, Gandhi S, Abramov, A.Y., Shchepinov, M.S
Journal of Neurochemistry, 133, 4, 2015. http://dx.doi.org/10.1111/jnc.13024



A mechanistic model of tau amyloid aggregation based on direct observation of oligomers.
Shammas, S. L., Garcia, G. A., Kumar S., A., Kjaergaard M., Horrocks, M.H., Shivji N., Mandelkow, E., Knowles T.P.J., Mandelkow E., Klenerman, D..
Nature Communications, 6, 2015. http://dx.doi.org/10.1038/ncomms8025



2014

Bayesian Inference of Accurate Population Sizes and FRET Efficiencies from Single Diffusing Biomolecules.
Murphy, R.M., Danezis, D., Horrocks, M.H., Jackson, S.E., Klenerman, D.
Analytical Chemistry, 86, 17, 2014. http://dx.doi.org/10.1021/ac501188r



The changing point-spread function: single-molecule-based super-resolution imaging.
Horrocks, M.H., Palayret, M., Klenerman, D., Lee, S.F.
Histochemistry and Cell Biology, 141, 6, 2014. http://dx.doi.org/10.1007/s00418-014-1186-1



2013

Single-molecule measurements of transient biomolecular complexes through microfluidic dilution
Horrocks, M.H., Rajah, L., Jonsson, P., Kjaergaard, M., Vendruscolo, M., Knowles, T.P.J., Klenerman, D.
Analytical Chemistry, 85, 14, 2013. http://dx.doi.org/10.1021/ac4010875



2012

Ubiquitin chain conformation regulates recognition and activity of interacting proteins.
Ye, Y., Blaser, G., Horrocks, M.H., Ruedas-Rama, M.J., Ibrahim, S., Zhukov, A.A., Orte, A., Klenerman, D., Jackson, S.E., Komander, D.
Nature, 492, 7428, 2012. http://dx.doi.org/10.1038/nature11722



Single molecule fluorescence under conditions of fast flow.
Horrocks, M.H., Li, H., Shim, J.-U., Ranasinghe, R.T., Clarke, R.W., Huck, W.T.S., Abell, C., Klenerman, D.
Analytical Chemistry, 84, 1, 2012. http://dx.doi.org/10.1021/ac202313d



Patents

  1. (WO2016001644) Diagnosis and Treatment of Neurodegenerative Disorders