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Rene Frank Group
In situ molecular structures of the brain


Papers

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

Peukes J, Lovatt M, 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
Preprint (2021) Biorxiv DOI: https://doi.org/10.1101/2021.02.19.432002

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.
Cdellular 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

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