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Faraday Discussions In press (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
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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
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Fernandez, E, Collins, M.O., Frank, R.A.W., Zhu, F., Kopanitsa, M.V.,
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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
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Frank R.A.W., Grant S.G.N. (2017). Supramolecular organisation of NMDA
receptors and the postsynaptic density.
Current Opinions in
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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.
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Frank, R.A.W. (2011) Endogenous ion channel complexes: the NMDA receptor
Biochemical Society
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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,
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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,
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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,
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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,
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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.
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