Peukes J, Lovatt C, Leistner C, Boulanger J, Morado D, Kukulski W, Zhu F, Komiyama NH, Briggs JAG, Grant SGN, Frank RAW. The molecular infrastructure of glutamatergic synapses in the mammalian forebrain
Elife accepted (2024) DOI: https://doi.org/10.7554/eLife.100335.1
Preprint (2021) Biorxiv DOI: https://doi.org/10.1101/2021.02.19.432002
Lovatt C, O'Sullivan TJ, Ortega-de San Luis C, Ryan TJ, Frank RAW. Memory engram synapse 3D molecular architecture visualized by cryoCLEM-guided cryoET.
Preprint (2024) Biorxiv DOI: https://doi.org/10.1101/2025.01.09.632151
Gilbert MAG, Fatima N, Jenkins J, O'Sullivan TJ, Schertel A, Halfon Y, Wilkinson M, Morrema THJ, Geibel M, Read RJ, Ranson NA, Radford SE, Hoozemans JJM, Frank RAW.
CryoET of β-amyloid and tau within postmortem Alzheimer's disease brain
Nature 631: 913 (2024). https://www.nature.com/articles/s41586-024-07680-x
Leistner C, Wilkinson M, Burgess A, Lovatt M, Goodbody S, Xu Y, Deuchars S, Radford SE, Ranson NA, Frank RAW.
The in-tissue molecular architecture of β-amyloid pathology in the mammalian brain
Nature Communications 14: 2833 (2023). https://www.nature.com/articles/s41467-023-38495-5
Lovatt M, Leistner C, Frank RAW. Bridging length scales from molecules to the whole organisms.
Bridging length scales from molecules to the whole organism by cryoCLEM and cryoET.
Faraday Discussions 240: 114 (2022). https://pubs.rsc.org/en/content/articlelanding/2022/fd/d2fd00081d
Andrews A, Murphy AE, Stofella M, Maslen S, Almeida-Souza L, Skene NG, Sobott F, Frank RAW. Multidimensional dynamics of the proteome in the neurodegenerative and aging mammalian brain.
Cellular and Molecular Proteomics 21, 100192 (2022) PubMed DOI: https://www.mcponline.org/article/S1535-9476(21)00164-X/fulltext
Almeida-Souza L., Frank R.A.W, Garcia-Nafria J., Colussi A., Gunawardana N., Johnson C.M., Yu M., Howard G., Andrews B., Vallis Y., McMahon H.T. A flat BAR protein promotes actin polymerisation at the base of clathrin-coated pits.
Cell 74, 325 (2018) PubMed DOI: 10.1016/j.cell.2018.05.020
Fernandez, E, Collins, M.O., Frank, R.A.W., Zhu, F., Kopanitsa, M.V., Nithianantharajah, J., Lempriere, S.A., Fricker, D., Elsegood, K.A., McLaughlin, C.L., Croning, M.D.R., Mclean, C., Armstrong, J.D., Hill, W.D., Deary, I.J., Cencelli, G., Bagni, C., Fromer, M., Purcell, S.M., Pocklington A.J., Choudhary, J.S., Komiyama, N.H., Grant, S.G.N. (2017). Arc Requires PSD95 for Assembly into Postsynaptic Complexes Involved with Neural Dysfunction and Intelligence.
Cell Reports 45, 139-147 (2017) PubMed DOI: 10.1016/j.celrep.2017.09.045
Frank R.A.W., Grant S.G.N. (2017). Supramolecular organisation of NMDA receptors and the postsynaptic density.
Current Opinions in Neurobiology 142, 139-147 (2017) PubMed DOI: 10.1016/j.conb.2017.05.019
Frank R.A.W., Komiyama N.H., Grant S.G.N. Hierarchical organisation and genetically separable subfamilies of PSD95 postsynaptic supercomplexes.
Journal of Neurochemistry 142, 504-511 (2017) PubMed DOI: 10.1111/jnc.14056
Frank R.A.W., Komiyama N.H., Ryan T.J., Zhu F., O’Dell T., Grant S.G.N. (2016). NMDA receptors are selectively partitioned into complexes and supercomplexes during synapse maturation.
Nature Communications 7, 11624 (2016) PubMed DOI: 10.1038/ncomms11264
Frank, R.A.W. (2011) Endogenous ion channel complexes: the NMDA receptor
Biochemical Society Transactions 39, 707 (2011) PubMed DOI: 10.1042/BST0390707
Frank, R.A.W., McRae, A.F., Pocklington, A.J., van de Lagemaat, L.N., Navarro, P., Croning, M.D., Komiyama, N.H., Bradley, S.J., Challiss, R.A., Armstrong, J.D., Finn, R.D., Malloy, M.P., MacLean, A.W., Harris, S.E., Starr, J.M., Bhaskar, S.S., Howard, E.K., Hunt, S.E., Coffey, A.J., Ranganath, V., Deloukas, P., Rogers, J., Muir, W.J., Deary, I.J., Blackwood, D.H., Visscher, P.M., Grant, S.G. Clustered coding variants in the glutamate receptor complexes of individuals with schizophrenia and bipolar disorder.
PLoS One 6, e19011 (2011) PubMed DOI: 10.1371/journal.pone.0019011
Pei X.Y., Titman C.M., Frank R.A.W., Leeper F.J., Luisi B.F.. Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multienzyme complex
Structure 16, 1860 (2008) PubMed DOI: 10.1016/j.str.2008.10.009
Frank, R.A.W., Kay, C., Hirst, J., Luisi, B.F. An off-pathway, thiamine-dependent radical in the Krebs cycle.
Journal of the American Chemical Society 30, 1662 (2008) PubMed DOI: 10.1021/ja076468k
Frank R.A.W., Leeper F.J., Luisi B.F. Structure, mechanism and catalytic duality of thiamine-dependent enzymes.
Cellular and Molecular Life Sciences 64, 892 (2007) PubMed DOI: 10.1007/s00018-007-6423-5
Frank, R.A.W., Price, A., Northrop, F., Perham, R.N., Luis0,i B. F. Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate
dehydrogenase multienzyme complex.
Journal of Molecular Biology 368, 63 (2007) PubMed DOI: 10.1016/j.jmb.2007.01.080
Frank, R.A.W., Pratap, V., Yuan Pei, X., Luisi B.F., Perham, R.N. The molecular origin of specificity in the assembly of a multienzyme complex.
Structure 13, 1119 (2005) PubMed DOI: 10.1016/j.str.2005.04.021
Frank, R.A.W., Pratap, V., Titman, C., Luisi, B.F., Perham, R.N.
A molecular switch and proton-wire synchronize the active sites in thiamine enzymes.
Science 306, 872-876 (2004) PubMed DOI: 10.1126/science.1101030