Dr Brian Smith

  • Senior Lecturer (Molecular Biosciences)

telephone: 01413305167
email: Brian.Smith@glasgow.ac.uk

B4.20 Level B4, School of Molecular Biosciences, Joseph Black Building, Glasgow, G12 8QQ

Import to contacts

ORCID iDhttps://orcid.org/0000-0003-3363-4168

Research interests

NMR spectroscopy
Nuclear Magnetic Resonance spectroscopy is the only technique that can determine high-resolution structures of macromolecules in solution, and can also probe molecular motion and intermolecular interactions. Brian's group use the technique to study the structures and functions of proteins and nucleic acids involved in interesting processes in a variety of systems. They are also interested in developing NMR methodology. They have a recently updated 600 MHz NMR spectrometer (2013) equipped with a cryoprobe. High-resolution molecular structures are normally determined in vitro, but Brian was part of the team that solved the first structure of a protein inside living cells. We collaborate widely with other biologists and chemists and currently have particular interests in the biophysics and application of natural surfactant proteins, in fatty acid binding proteins from nematode parasites, in the structural basis of epigenetic gene regulation, in the regulation of viral life cycles, in the molecular basis of endotoxin sensing, and in ultraviolet light perception by plants.

Natural surfactant proteins
Surfactants are typically small molecule amphiphiles, but these are typically disruptive to cells. Proteins that act as cell compatible surfactants have arisen independently several times in evolution. Brian's group study ranaspumins found in the foam nests of tropical frogs and the salivary and airway surfactants, equine latherin and human SPLUNC1. The conformational transition that these proteins undergo to convert to their surface active forms sets them apart from other classes of protein surfactants. The group are also exploring biotechnological applications of surfactant proteins.
Collaborators: Prof Malcolm Kennedy, Dr Mathis Riehle, Prof Cait MacPhee (University of Edinburgh), Prof Matt Redinbo (UNC Chapel Hill, USA).


Figure 1 Three views of a cartoon of the structure of the solution form of the surfactant protein latherin showing the locations of the many leucine (yellow) and isoleucine (orange) residues as spheres. (PDB:3ZPM)

Novel fatty acid binding proteins
Brian's group studies the structures and ligand binding properties of novel fatty acid binding proteins from parasites. Parasitic nematodes are responsible for some of the most widespread and pernicious diseases in the developing world as well as causing losses in agriculture. The parasites must scavenge metabolites, including fatty acids and retinoids, from their hosts and maintain a reservoir of fatty acid binding proteins in their pseudocoelemic fluid. Brian's group have determined the structures of nematode polyprotein antigen subunits (NPAs) and fatty acid and retinoid binding proteins (FARs) and more typical FABP proteins and are examining their lipid binding in detail.
Collaborators: Prof Malcolm Kennedy, Prof Betina Córsico (INIBIOLP, Argentina).


Figure 2 Fatty acid binding by Na-FAR-1 followed by 15N HSQC NMR spectra. The peaks arising from the amide NH of each amino acid residue are seen to jump from one position to another as oleate is titrated into the protein indicating that it can bind multiple ligands, adopting a distinct conformation in each case.

Structural basis of epigenetic gene regulation
Epigenetics describes heritable changes in gene expression that do not involve an alteration of the DNA sequence. For example, as a complex organism develops, its cells differentiate from stem cells into specialised cell types in which groups of genes are down regulated in a heritable fashion. This down regulation requires specialised forms of chromatin (DNA and the proteins that package it) that prevents the transcription machinery from gaining access to the genes. Molecular signals including DNA methylation and modification of histone tails are key to these processes. Brian's group study the structures of the proteins that recognise and interpret these modifications.

Ultraviolet light perception
UVR8, the protein through which plants sense ultraviolet light, is unusual in using tryptophan residues, rather than an additional chromophore. The group are trying to understand the mechanism of UV perception and the conformational changes in the protein that effect downstream signalling.

Collaborators: Prof Gareth Jenkins, Prof John Christie.

 

Research groups

Publications

List by: Type | Date

Jump to: 2024 | 2023 | 2022 | 2021 | 2020 | 2019 | 2017 | 2016 | 2015 | 2014 | 2013 | 2012 | 2011 | 2010 | 2009 | 2008 | 2007 | 2006 | 2005 | 2004 | 2002 | 2001
Number of items: 76.

2024

Dearlove, E. L., Chatrin, C., Buetow, L., Ahmed, S. F. , Schmidt, T., Bushell, M. , Smith, B. O. and Huang, D. T. (2024) DTX3L ubiquitin ligase ubiquitinates single-stranded nucleic acids. eLife, 13, RP98070. (doi: 10.7554/elife.98070) (PMID:39377462)

Pal, S., Nare, Z., Rao, V. A., Smith, B. O. , Morrison, I., Fitzgerald, E. A., Scott, A., Bingham, M. J. and Pesnot, T. (2024) Accelerating BRPF1b hit identification with BioPhysical and Active Learning Screening (BioPALS). ChemMedChem, 19(6), e202300590. (doi: 10.1002/cmdc.202300590) (PMID:38372199)

2023

Adam, S., Zheng, D., Klein, A., Volz, C., Mullen, W. , Shirran, S. L., Smith, B. O. , Kalinina, O. V., Müller, R. and Koehnke, J. (2023) Unusual peptide-binding proteins guide pyrroloindoline alkaloid formation in crocagin biosynthesis. Nature Chemistry, 15(4), pp. 560-568. (doi: 10.1038/s41557-023-01153-w) (PMID:36894702) (PMCID:PMC10070186)

2022

Kowalczyk, D., Nakasone, M. A., Smith, B. O. and Huang, D. T. (2022) Bivalent binding of p14ARF to MDM2 RING and acidic domains inhibits E3 ligase function. Life Science Alliance, 5(12), e202201472. (doi: 10.26508/lsa.202201472) (PMID:35944929) (PMCID:PMC9366199)

Gracie, J., Zamberlan, F., Andrews, I. B., Smith, B. O. and Peveler, W. J. (2022) Growth of plasmonic nanoparticles for aging cask-matured whisky. ACS Applied Nano Materials, 5(10), pp. 15362-15368. (doi: 10.1021/acsanm.2c03406) (PMID:36338330)

Ryan, S. M. et al. (2022) Novel antiinflammatory biologics shaped by parasite–host coevolution. Proceedings of the National Academy of Sciences of the United States of America, 119(36), e220279511. (doi: 10.1073/pnas.2202795119) (PMID:36037362)

Kjeldsen, A. et al. (2022) The fluorescent protein iLOV as a reporter for screening of high‐yield production of antimicrobial peptides in Pichia pastoris. Microbial Biotechnology, 15(7), pp. 2126-2139. (doi: 10.1111/1751-7915.14034) (PMID:35312165) (PMCID:PMC9249318)

Torres Cabán, C. C., Yang, M., Lai, C., Yang, L., Subach, F. V., Smith, B. O. , Piatkevich, K. D. and Boyden, E. S. (2022) Tuning the sensitivity of genetically encoded fluorescent potassium indicators through structure-guided and genome mining strategies. ACS Sensors, 7(5), pp. 1336-1346. (doi: 10.1021/acssensors.1c02201) (PMID:35427452) (PMCID:PMC9150168)

Tibbo, A. J. et al. (2022) Phosphodiesterase type 4 anchoring regulates cAMP signaling to Popeye domain-containing proteins. Journal of Molecular and Cellular Cardiology, 165, pp. 86-102. (doi: 10.1016/j.yjmcc.2022.01.001) (PMID:34999055) (PMCID:PMC8986152)

Nakasone, M. A., Majorek, K. A., Gabrielsen, M. , Sibbet, G. J., Smith, B. O. and Huang, D. T. (2022) Structure of UBE2K-Ub/E3/polyUb reveals mechanisms of K48-linked Ub chain extension. Nature Chemical Biology, 18, pp. 422-431. (doi: 10.1038/s41589-021-00952-x) (PMID:35027744) (PMCID:PMC8964413)

Neckebroeck, A., Kelly, S. M. , Smith, B. O. and Clark, J. S. (2022) Synthesis of the prototypical cyclopropyl dipeptide mimic and evaluation of its turn-inducing capability. Journal of Organic Chemistry, 87(1), pp. 258-270. (doi: 10.1021/acs.joc.1c02344) (PMID:34913698)

2021

Prabhakar, A. T. et al. (2021) CK2 phosphorylation of human papillomavirus 16 E2 on serine 23 promotes interaction with TopBP1 and is critical for E2 interaction with mitotic chromatin and the viral life cycle. mBio, 12, e01163-21. (doi: 10.1128/mbio.01163-21) (PMID:34544280) (PMCID:PMC8546539)

Buist, H. K. et al. (2021) Identification and characterization of an affimer affinity reagent for the detection of the cAMP sensor, EPAC1. Cells, 10(9), 2307. (doi: 10.3390/cells10092307)

Morgan, D. C. et al. (2021) Stapled ACE2 peptidomimetics designed to target the SARS-CoV-2 spike protein do not prevent virus internalisation. Peptide Science, 113(4), e24217. (doi: 10.1002/pep2.24217) (PMID:33615115) (PMCID:PMC7883042)

Knuhtsen, A., Whiting, R., McWhinnie, F. S., Whitmore, C., Smith, B. O. , Green, A. C., Timperley, C. M., Kinnear, K. I. and Jamieson, A. G. (2021) μ-conotoxin KIIIA peptidomimetics that block human voltage-gated sodium channels. Peptide Science, 113(1), e24203. (doi: 10.1002/pep2.24203)

2020

Chatrin, C., Gabrielsen, M. , Buetow, L., Nakasone, M. A., Ahmed, S. F., Sumpton, D., Sibbet, G. J., Smith, B. O. and Huang, D. T. (2020) Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases. Science Advances, 6(38), eabc0418. (doi: 10.1126/sciadv.abc0418) (PMID:32948590) (PMCID:PMC7500938)

Crecente Garcia, S., Neckebroeck, A., Clark, J. S. , Smith, B. O. and Thomson, A. R. (2020) β-turn mimics by chemical ligation. Organic Letters, 22(11), pp. 4424-4428. (doi: 10.1021/acs.orglett.0c01427) (PMID:32406695) (PMCID:PMC7304061)

2019

Ibáñez-Shimabukuro, M. et al. (2019) Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode. Bioscience Reports, 39(7), BSR2019129. (doi: 10.1042/BSR20191292) (PMID:31273060) (PMCID:PMC6646235)

Knuhtsen, A., Whitmore, C., McWhinnie, F. S., McDougall, L., Whiting, R., Smith, B. O. , Timperley, C. M., Green, A. C., Kinnear, K. I. and Jamieson, A. G. (2019) α-conotoxin GI triazole-peptidomimetics: potent and stable blockers of a human acetylcholine receptor. Chemical Science, 10, pp. 1671-1676. (doi: 10.1039/C8SC04198A)

2017

Cooper, A., Vance, S. J., Smith, B. O. and Kennedy, M. W. (2017) Frog foams and natural protein surfactants. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 534, pp. 120-129. (doi: 10.1016/j.colsurfa.2017.01.049) (PMID:29276339) (PMCID:PMC5727673)

Gabrielsen, M. , Buetow, L., Nakasone, M. A., Ahmed, S. F., Sibbet, G. J., Smith, B. O. , Zhang, W., Sidhu, S. S. and Huang, D. T. (2017) A general strategy for discovery of inhibitors and activators of RING and U-box E3 ligases with ubiquitin variants. Molecular Cell, 68(2), 456-470.e10. (doi: 10.1016/j.molcel.2017.09.027) (PMID:29053960) (PMCID:PMC5655547)

Magennis, S. , Toulmin, A., Baltierra-Jasso, L. E., Morten, M. J., Sabir, T., McGlynn, P., Schröder, G. F., Smith, B. O. and Magennis, S. W. (2017) Conformational heterogeneity in a fully-complementary DNA three-way junction with a GC-rich branchpoint. Biochemistry, 56(37), pp. 4985-4991. (doi: 10.1021/acs.biochem.7b00677) (PMID:28820590)

Spies, M. and Smith, B. O. (2017) Protein-nucleic acids interactions: new ways of connecting structure, dynamics and function. Biophysical Reviews, 9(4), pp. 289-291. (doi: 10.1007/s12551-017-0284-4) (PMID:28776257)

Brandani, G. B., Vance, S. J., Schor, M., Cooper, A., Kennedy, M. W. , Smith, B. O. , MacPhee, C. E. and Cheung, D. L. (2017) Adsorption of the natural protein surfactant Rsn-2 onto liquid interfaces. Physical Chemistry Chemical Physics, 19(12), pp. 8584-8594. (doi: 10.1039/C6CP07261E) (PMID:28289744)

Parnell, E., McElroy, S. P., Wiejak, J., Baillie, G. L., Porter, A., Adams, D. R., Rehmann, H., Smith, B. O. and Yarwood, S. J. (2017) Identification of a novel, small molecule partial agonist for the cyclic AMP sensor, EPAC1. Scientific Reports, 7, 294. (doi: 10.1038/s41598-017-00455-7) (PMID:28331191) (PMCID:PMC5428521)

2016

Grinter, R. et al. (2016) Structure of the bacterial plant-ferredoxin receptor FusA. Nature Communications, 7, 13308. (doi: 10.1038/ncomms13308) (PMID:27796364) (PMCID:PMC5095587)

Heilmann, M., Velanis, C. N., Cloix, C., Smith, B. O. , Christie, J. M. and Jenkins, G. I. (2016) Dimer/monomer status and in vivo function of salt-bridge mutants of the plant UV-B photoreceptor UVR8. Plant Journal, 88(1), pp. 71-81. (doi: 10.1111/tpj.13260) (PMID:27385642) (PMCID:PMC5091643)

Morris, R. J., Brandani, G. B., Desai, V., Smith, B. O. , Schor, M. and MacPhee, C. E. (2016) The conformation of interfacially adsorbed Ranaspumin-2 Is an arrested state on the unfolding pathway. Biophysical Journal, 111(4), pp. 732-742. (doi: 10.1016/j.bpj.2016.06.006) (PMID:27558717)

Vance, S. J., Desai, V., Smith, B. O. , Kennedy, M. W. and Cooper, A. (2016) Aqueous solubilization of C60 fullerene by natural protein surfactants, latherin and ranaspumin-2. Biophysical Chemistry, 214-15, pp. 27-32. (doi: 10.1016/j.bpc.2016.05.003) (PMID:27214760) (PMCID:PMC4906151)

Ashraf, K. U., Josts, I., Mosbahi, K., Kelly, S. M. , Byron, O. , Smith, B. O. and Walker, D. (2016) The potassium binding protein Kbp is a cytoplasmic potassium sensor. Structure, 24(5), pp. 741-749. (doi: 10.1016/j.str.2016.03.017) (PMID:27112601)

2015

Rey, B. M.F. et al. (2015) Diversity in the structures and ligand binding sites of nematode fatty acid and retinol binding proteins revealed by Na-FAR-1 from Necator americanus. Biochemical Journal, 471(3), pp. 403-414. (doi: 10.1042/BJ20150068) (PMID:26318523) (PMCID:PMC4613501)

Thomson, R. and Smith, B. O. (2015) Solution structure of human MBD1 CXXC1. Journal of Biomolecular NMR, 63(3), pp. 309-314. (doi: 10.1007/s10858-015-9986-8) (PMID:26354109) (PMCID:PMC4642587)

Parnell, E., Smith, B. O. and Yarwood, S. J. (2015) The cAMP sensors, EPAC1 and EPAC2, display distinct subcellular distributions despite sharing a common nuclear pore localisation signal. Cellular Signalling, 27(5), pp. 989-996. (doi: 10.1016/j.cellsig.2015.02.009) (PMID:25683912) (PMCID:PMC4372255)

Buetow, L., Gabrielsen, M. , Anthony, N. G., Dou, H., Patel, A., Aitkenhead, H., Sibbet, G. J., Smith, B. O. and Huang, D. T. (2015) Activation of a primed RING E3-E2–ubiquitin complex by non-covalent ubiquitin. Molecular Cell, 58(2), pp. 297-310. (doi: 10.1016/j.molcel.2015.02.017) (PMID:25801170)

Shigemitsu, Y., Ikeya, T., Yamamoto, A., Tsuchie, Y., Mishima, M., Smith, B. O. , Güntert, P. and Ito, Y. (2015) Evaluation of the reliability of the maximum entropy method for reconstructing 3D and 4D NOESY-type NMR spectra of proteins. Biochemical and Biophysical Research Communications, 457(2), pp. 200-205. (doi: 10.1016/j.bbrc.2014.12.088) (PMID:25545060)

Franchini, G. R., Pórfido, J. L., Ibáñez Shimabukuro, M., Rey Burusco, M. F., Bélgamo, J. A., Smith, B. O. , Kennedy, M. W. and Córsico, B. (2015) The unusual lipid binding proteins of parasitic helminths and their potential roles in parasitism and as therapeutic targets. Prostaglandins, Leukotrienes and Essential Fatty Acids (PLEFA), 93, pp. 31-36. (doi: 10.1016/j.plefa.2014.08.003) (PMID:25282399)

Mathes, T. et al. (2015) Proton-coupled electron transfer constitutes the photoactivation mechanism of the plant photoreceptor UVR8. Journal of the American Chemical Society, 137(25), pp. 8113-8120. (doi: 10.1021/jacs.5b01177) (PMID:25955727)

2014

Beckham, K. S.H. et al. (2014) The metabolic enzyme AdhE controls the virulence of Escherichia coli O157:H7. Molecular Microbiology, 93(1), pp. 199-211. (doi: 10.1111/mmi.12651) (PMID:24846743) (PMCID:PMC4249723)

Cameron, R. T., Quinn, S. D. , Cairns, L. S., MacLeod, R., Samuel, I. D.W., Smith, B. O. , Penedo, J. C. and Baillie, G. S. (2014) The phosphorylation of Hsp20 enhances its association with amyloid-β to increase protection against neuronal cell death. Molecular and Cellular Neuroscience, 61, pp. 46-55. (doi: 10.1016/j.mcn.2014.05.002) (PMID:24859569) (PMCID:PMC4148482)

Ibáñez-Shimabukuro, M., Rey-Burusco, M.F., Cooper, A., Kennedy, M. W. , Córsico, B. and Smith, B. O. (2014) Resonance assignment of As-p18, a fatty acid binding protein secreted by developing larvae of the parasitic nematode Ascaris suum. Biomolecular NMR Assignments, 8(1), pp. 33-36. (doi: 10.1007/s12104-012-9447-1)

Vance, S. J., McDonald, R. E., Cooper, A., Kennedy, M. W. and Smith, B. O. (2014) Resonance assignments for latherin, a natural surfactant protein from horse sweat. Biomolecular NMR Assignments, 8(1), pp. 213-216. (doi: 10.1007/s12104-013-9485-3)

Yvon, C., Surman, A. J. , Hutin, M., Alex, J., Smith, B. O. , Long, D. L. and Cronin, L. (2014) Polyoxometalate clusters integrated into peptide chains and as inorganic amino acids: solution- and solid-phase approaches. Angewandte Chemie (International Edition), 53(13), pp. 3336-3341. (doi: 10.1002/anie.201311135)

Rey-Burusco, M.F., Ibañez-Shimabukuro, M., Cooper, A., Kennedy, M. W. , Córsico, B. and Smith, B. O. (2014) 1H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus. Biomolecular NMR Assignments, 8(1), pp. 19-21. (doi: 10.1007/s12104-012-9444-4)

McCaughey, L. C. et al. (2014) Lectin-like bacteriocins from Pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor. PLoS Pathogens, 10(2), e1003898. (doi: 10.1371/journal.ppat.1003898) (PMID:24516380) (PMCID:PMC3916391)

Caldwell, S.T. et al. (2014) Protein-mediated dethreading of a biotin-functionalised pseudorotaxane. Organic and Biomolecular Chemistry, 12(3), pp. 511-516. (doi: 10.1039/C3OB41612G) (PMID:24280954)

Josts, I., Grinter, R., Kelly, S. M. , Mosbahi, K., Roszak, A., Cogdell, R. , Smith, B. O. , Byron, O. and Walker, D. (2014) Recombinant expression, purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal DUF490963–1138 domain of TamB from Escherichia coli. Acta Crystallographica. Section F: Structural Biology Communications, 70(9), pp. 1272-1275. (doi: 10.1107/S2053230X14017403)

2013

Laird, J. et al. (2013) Identification of the domains of cauliflower mosaic virus protein P6 responsible for suppression of RNA silencing and salicylic acid signalling. Journal of General Virology, 94(12), pp. 2777-2789. (doi: 10.1099/vir.0.057729-0) (PMID:24088344) (PMCID:PMC3836500)

Hamatsu, J. et al. (2013) High-resolution heteronuclear multidimensional NMR of proteins in living insect cells using a baculovirus protein expression system. Journal of the American Chemical Society, 135(5), pp. 1688-1691. (doi: 10.1021/ja310928u)

Kennedy, M.W., Córsico, B., Cooper, A. and Smith, B.O. (2013) The unusual lipid-binding proteins of nematodes: NPAs, nemFABPs and FARs. In: Kennedy, M. and Harnett, m. (eds.) Parasitic Nematodes: Molecular Biology, Biochemistry and Immunology [2nd. ed.]. CABI; Wallingford; UK, pp. 397-412. ISBN 9781845937591 (doi: 10.1079/9781845937591.0397)

Vance, S.J., McDonald, R.E., Cooper, A., Smith, B.O. and Kennedy, M.W. (2013) The structure of latherin, a surfactant allergen protein from horse sweat and saliva. Journal of the Royal Society: Interface, 10(85), Art. 20130453. (doi: 10.1098/rsif.2013.0453)

2012

Cloix, C., Kaiserli, E. , Heilmann, M., Baxter, K.J. , Brown, B.A., O'Hara, A., Smith, B.O. , Christie, J.M. and Jenkins, G.I. (2012) C-terminal region of the UV-B photoreceptor UVR8 initiates signaling through interaction with the COP1 protein. Proceedings of the National Academy of Sciences of the United States of America, 109(40), pp. 16366-16370. (doi: 10.1073/pnas.1210898109)

Gabrielsen, M. , Rey-Burusco, M.F., Griffiths, K., Roe, A.J. , Cooper, A., Smith, B.O. , Kennedy, M.W. and Corsico, B. (2012) Two crystal forms of a helix-rich fatty acid- and retinol-binding protein, Na-FAR-1, from the parasitic nematodeNecator americanus. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, 68(7), pp. 835-838. (doi: 10.1107/S1744309112023597) (PMID:22750878) (PMCID:PMC3388935)

Parnell, E., Smith, B. O. , Palmer, T. M., Terrin, A., Zaccolo, M. and Yarwood, S. J. (2012) Regulation of the inflammatory response of vascular endothelial cells by EPAC1. British Journal of Pharmacology, 166(2), pp. 434-446. (doi: 10.1111/j.1476-5381.2011.01808.x)

Christie, J.M. et al. (2012) Plant UVR8 photoreceptor senses UV-B by tryptophan-mediated disruption of cross-dimer salt bridges. Science, 335(6075), pp. 1492-1496. (doi: 10.1126/science.1218091)

Gabrielsen, M. , Riboldi-Tunnicliffe, A., Ibáñez-Shimabukuro, M., Griffiths, K., Roe, A.J. , Cooper, A., Smith, B. , Córsico, B. and Kennedy, M.W. (2012) Useable diffraction data from a multiple microdomain-containing crystal of Ascaris suum As-p18 fatty-acid-binding protein using a microfocus beamline. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, 68, pp. 939-941. (doi: 10.1107/S1744309112026553) (PMID:22869127) (PMCID:PMC3412778)

Gabrielsen, M. , Riboldi-Tunnicliffe, A., Ibáñez-Shimabukuro, M., Griffiths, K., Roe, A.J. , Cooper, A., Smith, B.O. , Córsico, B. and Kennedy, M.W. (2012) Useable diffraction data from a multiple microdomain-containing crystal ofAscaris suumAs-p18 fatty-acid-binding protein using a microfocus beamline. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, 68(8), pp. 939-941. (doi: 10.1107/S1744309112026553) (PMID:22869127) (PMCID:PMC3412778)

2011

Wang, D. et al. (2011) Identification of bacterial target proteins for the salicylidene acylhydrazide class of virulence blocking compounds. Journal of Biological Chemistry, 286(34), pp. 29922-29931. (doi: 10.1074/jbc.M111.233858) (PMID:21724850) (PMCID:PMC3191033)

Meenan, N.A.G., Ball, G., Bromek, K., Uhrín, D., Cooper, A., Kennedy, M.W. and Smith, B.O. (2011) Solution structure of a repeated unit of the ABA-1 nematode polyprotein allergen of ascaris reveals a novel fold and two discrete lipid-binding sites. PLoS Neglected Tropical Diseases, 5(4), e1040. (doi: 10.1371/journal.pntd.0001040)

2010

Ikeya, T. et al. (2010) NMR protein structure determination in living E. coli cells using nonlinear sampling. Nature Protocols, 5(6), pp. 1051-1060. (doi: 10.1038/nprot.2010.69)

2009

MacKenzie, C.D., Smith, B.O., Meister, A., Blume, A., Zhao, X., Lu, J.R., Kennedy, M.W. and Cooper, A. (2009) Ranaspumin-2: structure and function of a surfactant protein from the foam nests of a tropical frog. Biophysical Journal, 96(12), pp. 4984-4992. (doi: 10.1016/j.bpj.2009.03.044)

Sakakibara, D. et al. (2009) Protein structure determination in living cells by in-cell NMR spectroscopy. Nature, 458(7234), pp. 102-105. (doi: 10.1038/nature07814)

Borland, G., Smith, B.O. and Yarwood, S.J. (2009) EPAC proteins transduce diverse cellular actions of cAMP. British Journal of Pharmacology, 158(1), pp. 70-86. (doi: 10.1111/j.1476-5381.2008.00087.x)

2008

dos Reis, F. C.G., Smith, B. O., Santos, C. C., Costa, T., F., Scharfstein, J., Coombs, G. H., Mottram, J. C. and Lima, A. P. C.A. (2008) The role of conserved residues of chagasin in the inhibition of cysteine peptidases. FEBS Letters, 582(4), pp. 485-490. (doi: 10.1016/j.febslet.2008.01.008)

Caldwell, S. T. , Cooke, G. , Cooper, A., Nutley, M., Rabani, G., Rotello, V., Smith, B. O. and Woisel, P. (2008) Tuneable pseudorotaxane formation between a biotin-avidin bioconjugate and CBPQT(4+). Chemical Communications(23), pp. 2650-2652. (doi: 10.1039/b803856b)

Caldwell, S. T. , Cooke, G. , Hewage, S. G., Mabruk, S., Rabani, G., Rotello, V., Smith, B.O. , Subramani, C. and Woisel, P. (2008) Model systems for flavoenzyme activity: intramolecular self-assembly of a flavin derivative via hydrogen bonding and aromatic interactions. Chemical Communications(35), pp. 4126-4128. (doi: 10.1039/b809762c)

2007

Alexander, A. et al. (2007) Probing the solvent-induced tautomerism of a redox-active ureidopyrimidinone. Chemical Communications, pp. 2246-2248. (doi: 10.1039/b703070c)

2006

Smith, B.O., Picken, N.C., Westrop, G.D., Bromek, K., Mottram, J.C. and Coombs, G.H. (2006) The structure of Leishmania mexicana ICP provides evidence for convergent evolution of cysteine peptidase inhibitors. Journal of Biological Chemistry, 281, pp. 5821-5828. (doi: 10.1074/jbc.M510868200)

Ball, G., Meenan, N., Bromek, K., Smith, B., Bella, J. and Uhrin, D. (2006) Measurement of one-bond C-13(alpha)-H-1(alpha) residual dipolar coupling constants in proteins by selective manipulation of (CH alpha)-H-alpha spins. Journal of Magnetic Resonance, 180, pp. 127-136. (doi: 10.1016/j.jmr.2006.01.017)

Smith, B.O., Westrop, G.D., Mottram, J.C. and Coombs, G.H. (2006) Chemical shift assignments of Leishmania mexicana ICP, a novel cysteine peptidase inhibitor. Journal of Biomolecular NMR, 36, p. 7. (doi: 10.1007/s10858-005-4739-8)

2005

Meenan, N.A.G., Cooper, A., Kennedy, M.W. and Smith, B. (2005) Resonance assignment of ABA-1A, from Ascaris suum nematode polyprotein allergen. Journal of Biomolecular NMR, 32(2), p. 176. (doi: 10.1007/s10858-005-6070-9)

2004

Weber, M.A. et al. (2004) Blood pressure dependent and independent effects of antihypertensive treatment on clinical events in the VALUE Trial. Lancet, 363(9426), pp. 2049-2051. (doi: 10.1016/S0140-6736(04)16456-8)

Smith, B. (2004) Structural analysis of the complement control protein (CCP) modules of GABAB receptor 1a: only one of the two ccp modules is compactly folded. Journal of Biological Chemistry, 279(46), pp. 48292-48306. (doi: 10.1074/jbc.M406540200)

2002

Bramham, J., Hodgkinson, J., Smith, B., Uhrin, D., Barlow, P. and Winder, S. (2002) Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin : calponin. Structure, 10, pp. 249-258.

Smith, B. (2002) Structure of the C3b binding site of CR1 (CD35), the immune adherence receptor. Cell, 108(6), pp. 769-780. (doi: 10.1016/S0092-8674(02)00672-4)

2001

Smith, B. (2001) DNA recognition by the methyl-CpG binding domain of MeCP2. Journal of Biological Chemistry, 276(5), pp. 3353-3360. (doi: 10.1074/jbc.M007224200)

Smith, B. (2001) Solution structure and dynamics of the central CCP module pair of a poxvirus complement control protein. Journal of Molecular Biology, 307(1), pp. 323-339. (doi: 10.1006/jmbi.2000.4477)

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Jump to: Articles | Book Sections
Number of items: 76.

Articles

Dearlove, E. L., Chatrin, C., Buetow, L., Ahmed, S. F. , Schmidt, T., Bushell, M. , Smith, B. O. and Huang, D. T. (2024) DTX3L ubiquitin ligase ubiquitinates single-stranded nucleic acids. eLife, 13, RP98070. (doi: 10.7554/elife.98070) (PMID:39377462)

Pal, S., Nare, Z., Rao, V. A., Smith, B. O. , Morrison, I., Fitzgerald, E. A., Scott, A., Bingham, M. J. and Pesnot, T. (2024) Accelerating BRPF1b hit identification with BioPhysical and Active Learning Screening (BioPALS). ChemMedChem, 19(6), e202300590. (doi: 10.1002/cmdc.202300590) (PMID:38372199)

Adam, S., Zheng, D., Klein, A., Volz, C., Mullen, W. , Shirran, S. L., Smith, B. O. , Kalinina, O. V., Müller, R. and Koehnke, J. (2023) Unusual peptide-binding proteins guide pyrroloindoline alkaloid formation in crocagin biosynthesis. Nature Chemistry, 15(4), pp. 560-568. (doi: 10.1038/s41557-023-01153-w) (PMID:36894702) (PMCID:PMC10070186)

Kowalczyk, D., Nakasone, M. A., Smith, B. O. and Huang, D. T. (2022) Bivalent binding of p14ARF to MDM2 RING and acidic domains inhibits E3 ligase function. Life Science Alliance, 5(12), e202201472. (doi: 10.26508/lsa.202201472) (PMID:35944929) (PMCID:PMC9366199)

Gracie, J., Zamberlan, F., Andrews, I. B., Smith, B. O. and Peveler, W. J. (2022) Growth of plasmonic nanoparticles for aging cask-matured whisky. ACS Applied Nano Materials, 5(10), pp. 15362-15368. (doi: 10.1021/acsanm.2c03406) (PMID:36338330)

Ryan, S. M. et al. (2022) Novel antiinflammatory biologics shaped by parasite–host coevolution. Proceedings of the National Academy of Sciences of the United States of America, 119(36), e220279511. (doi: 10.1073/pnas.2202795119) (PMID:36037362)

Kjeldsen, A. et al. (2022) The fluorescent protein iLOV as a reporter for screening of high‐yield production of antimicrobial peptides in Pichia pastoris. Microbial Biotechnology, 15(7), pp. 2126-2139. (doi: 10.1111/1751-7915.14034) (PMID:35312165) (PMCID:PMC9249318)

Torres Cabán, C. C., Yang, M., Lai, C., Yang, L., Subach, F. V., Smith, B. O. , Piatkevich, K. D. and Boyden, E. S. (2022) Tuning the sensitivity of genetically encoded fluorescent potassium indicators through structure-guided and genome mining strategies. ACS Sensors, 7(5), pp. 1336-1346. (doi: 10.1021/acssensors.1c02201) (PMID:35427452) (PMCID:PMC9150168)

Tibbo, A. J. et al. (2022) Phosphodiesterase type 4 anchoring regulates cAMP signaling to Popeye domain-containing proteins. Journal of Molecular and Cellular Cardiology, 165, pp. 86-102. (doi: 10.1016/j.yjmcc.2022.01.001) (PMID:34999055) (PMCID:PMC8986152)

Nakasone, M. A., Majorek, K. A., Gabrielsen, M. , Sibbet, G. J., Smith, B. O. and Huang, D. T. (2022) Structure of UBE2K-Ub/E3/polyUb reveals mechanisms of K48-linked Ub chain extension. Nature Chemical Biology, 18, pp. 422-431. (doi: 10.1038/s41589-021-00952-x) (PMID:35027744) (PMCID:PMC8964413)

Neckebroeck, A., Kelly, S. M. , Smith, B. O. and Clark, J. S. (2022) Synthesis of the prototypical cyclopropyl dipeptide mimic and evaluation of its turn-inducing capability. Journal of Organic Chemistry, 87(1), pp. 258-270. (doi: 10.1021/acs.joc.1c02344) (PMID:34913698)

Prabhakar, A. T. et al. (2021) CK2 phosphorylation of human papillomavirus 16 E2 on serine 23 promotes interaction with TopBP1 and is critical for E2 interaction with mitotic chromatin and the viral life cycle. mBio, 12, e01163-21. (doi: 10.1128/mbio.01163-21) (PMID:34544280) (PMCID:PMC8546539)

Buist, H. K. et al. (2021) Identification and characterization of an affimer affinity reagent for the detection of the cAMP sensor, EPAC1. Cells, 10(9), 2307. (doi: 10.3390/cells10092307)

Morgan, D. C. et al. (2021) Stapled ACE2 peptidomimetics designed to target the SARS-CoV-2 spike protein do not prevent virus internalisation. Peptide Science, 113(4), e24217. (doi: 10.1002/pep2.24217) (PMID:33615115) (PMCID:PMC7883042)

Knuhtsen, A., Whiting, R., McWhinnie, F. S., Whitmore, C., Smith, B. O. , Green, A. C., Timperley, C. M., Kinnear, K. I. and Jamieson, A. G. (2021) μ-conotoxin KIIIA peptidomimetics that block human voltage-gated sodium channels. Peptide Science, 113(1), e24203. (doi: 10.1002/pep2.24203)

Chatrin, C., Gabrielsen, M. , Buetow, L., Nakasone, M. A., Ahmed, S. F., Sumpton, D., Sibbet, G. J., Smith, B. O. and Huang, D. T. (2020) Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases. Science Advances, 6(38), eabc0418. (doi: 10.1126/sciadv.abc0418) (PMID:32948590) (PMCID:PMC7500938)

Crecente Garcia, S., Neckebroeck, A., Clark, J. S. , Smith, B. O. and Thomson, A. R. (2020) β-turn mimics by chemical ligation. Organic Letters, 22(11), pp. 4424-4428. (doi: 10.1021/acs.orglett.0c01427) (PMID:32406695) (PMCID:PMC7304061)

Ibáñez-Shimabukuro, M. et al. (2019) Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode. Bioscience Reports, 39(7), BSR2019129. (doi: 10.1042/BSR20191292) (PMID:31273060) (PMCID:PMC6646235)

Knuhtsen, A., Whitmore, C., McWhinnie, F. S., McDougall, L., Whiting, R., Smith, B. O. , Timperley, C. M., Green, A. C., Kinnear, K. I. and Jamieson, A. G. (2019) α-conotoxin GI triazole-peptidomimetics: potent and stable blockers of a human acetylcholine receptor. Chemical Science, 10, pp. 1671-1676. (doi: 10.1039/C8SC04198A)

Cooper, A., Vance, S. J., Smith, B. O. and Kennedy, M. W. (2017) Frog foams and natural protein surfactants. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 534, pp. 120-129. (doi: 10.1016/j.colsurfa.2017.01.049) (PMID:29276339) (PMCID:PMC5727673)

Gabrielsen, M. , Buetow, L., Nakasone, M. A., Ahmed, S. F., Sibbet, G. J., Smith, B. O. , Zhang, W., Sidhu, S. S. and Huang, D. T. (2017) A general strategy for discovery of inhibitors and activators of RING and U-box E3 ligases with ubiquitin variants. Molecular Cell, 68(2), 456-470.e10. (doi: 10.1016/j.molcel.2017.09.027) (PMID:29053960) (PMCID:PMC5655547)

Magennis, S. , Toulmin, A., Baltierra-Jasso, L. E., Morten, M. J., Sabir, T., McGlynn, P., Schröder, G. F., Smith, B. O. and Magennis, S. W. (2017) Conformational heterogeneity in a fully-complementary DNA three-way junction with a GC-rich branchpoint. Biochemistry, 56(37), pp. 4985-4991. (doi: 10.1021/acs.biochem.7b00677) (PMID:28820590)

Spies, M. and Smith, B. O. (2017) Protein-nucleic acids interactions: new ways of connecting structure, dynamics and function. Biophysical Reviews, 9(4), pp. 289-291. (doi: 10.1007/s12551-017-0284-4) (PMID:28776257)

Brandani, G. B., Vance, S. J., Schor, M., Cooper, A., Kennedy, M. W. , Smith, B. O. , MacPhee, C. E. and Cheung, D. L. (2017) Adsorption of the natural protein surfactant Rsn-2 onto liquid interfaces. Physical Chemistry Chemical Physics, 19(12), pp. 8584-8594. (doi: 10.1039/C6CP07261E) (PMID:28289744)

Parnell, E., McElroy, S. P., Wiejak, J., Baillie, G. L., Porter, A., Adams, D. R., Rehmann, H., Smith, B. O. and Yarwood, S. J. (2017) Identification of a novel, small molecule partial agonist for the cyclic AMP sensor, EPAC1. Scientific Reports, 7, 294. (doi: 10.1038/s41598-017-00455-7) (PMID:28331191) (PMCID:PMC5428521)

Grinter, R. et al. (2016) Structure of the bacterial plant-ferredoxin receptor FusA. Nature Communications, 7, 13308. (doi: 10.1038/ncomms13308) (PMID:27796364) (PMCID:PMC5095587)

Heilmann, M., Velanis, C. N., Cloix, C., Smith, B. O. , Christie, J. M. and Jenkins, G. I. (2016) Dimer/monomer status and in vivo function of salt-bridge mutants of the plant UV-B photoreceptor UVR8. Plant Journal, 88(1), pp. 71-81. (doi: 10.1111/tpj.13260) (PMID:27385642) (PMCID:PMC5091643)

Morris, R. J., Brandani, G. B., Desai, V., Smith, B. O. , Schor, M. and MacPhee, C. E. (2016) The conformation of interfacially adsorbed Ranaspumin-2 Is an arrested state on the unfolding pathway. Biophysical Journal, 111(4), pp. 732-742. (doi: 10.1016/j.bpj.2016.06.006) (PMID:27558717)

Vance, S. J., Desai, V., Smith, B. O. , Kennedy, M. W. and Cooper, A. (2016) Aqueous solubilization of C60 fullerene by natural protein surfactants, latherin and ranaspumin-2. Biophysical Chemistry, 214-15, pp. 27-32. (doi: 10.1016/j.bpc.2016.05.003) (PMID:27214760) (PMCID:PMC4906151)

Ashraf, K. U., Josts, I., Mosbahi, K., Kelly, S. M. , Byron, O. , Smith, B. O. and Walker, D. (2016) The potassium binding protein Kbp is a cytoplasmic potassium sensor. Structure, 24(5), pp. 741-749. (doi: 10.1016/j.str.2016.03.017) (PMID:27112601)

Rey, B. M.F. et al. (2015) Diversity in the structures and ligand binding sites of nematode fatty acid and retinol binding proteins revealed by Na-FAR-1 from Necator americanus. Biochemical Journal, 471(3), pp. 403-414. (doi: 10.1042/BJ20150068) (PMID:26318523) (PMCID:PMC4613501)

Thomson, R. and Smith, B. O. (2015) Solution structure of human MBD1 CXXC1. Journal of Biomolecular NMR, 63(3), pp. 309-314. (doi: 10.1007/s10858-015-9986-8) (PMID:26354109) (PMCID:PMC4642587)

Parnell, E., Smith, B. O. and Yarwood, S. J. (2015) The cAMP sensors, EPAC1 and EPAC2, display distinct subcellular distributions despite sharing a common nuclear pore localisation signal. Cellular Signalling, 27(5), pp. 989-996. (doi: 10.1016/j.cellsig.2015.02.009) (PMID:25683912) (PMCID:PMC4372255)

Buetow, L., Gabrielsen, M. , Anthony, N. G., Dou, H., Patel, A., Aitkenhead, H., Sibbet, G. J., Smith, B. O. and Huang, D. T. (2015) Activation of a primed RING E3-E2–ubiquitin complex by non-covalent ubiquitin. Molecular Cell, 58(2), pp. 297-310. (doi: 10.1016/j.molcel.2015.02.017) (PMID:25801170)

Shigemitsu, Y., Ikeya, T., Yamamoto, A., Tsuchie, Y., Mishima, M., Smith, B. O. , Güntert, P. and Ito, Y. (2015) Evaluation of the reliability of the maximum entropy method for reconstructing 3D and 4D NOESY-type NMR spectra of proteins. Biochemical and Biophysical Research Communications, 457(2), pp. 200-205. (doi: 10.1016/j.bbrc.2014.12.088) (PMID:25545060)

Franchini, G. R., Pórfido, J. L., Ibáñez Shimabukuro, M., Rey Burusco, M. F., Bélgamo, J. A., Smith, B. O. , Kennedy, M. W. and Córsico, B. (2015) The unusual lipid binding proteins of parasitic helminths and their potential roles in parasitism and as therapeutic targets. Prostaglandins, Leukotrienes and Essential Fatty Acids (PLEFA), 93, pp. 31-36. (doi: 10.1016/j.plefa.2014.08.003) (PMID:25282399)

Mathes, T. et al. (2015) Proton-coupled electron transfer constitutes the photoactivation mechanism of the plant photoreceptor UVR8. Journal of the American Chemical Society, 137(25), pp. 8113-8120. (doi: 10.1021/jacs.5b01177) (PMID:25955727)

Beckham, K. S.H. et al. (2014) The metabolic enzyme AdhE controls the virulence of Escherichia coli O157:H7. Molecular Microbiology, 93(1), pp. 199-211. (doi: 10.1111/mmi.12651) (PMID:24846743) (PMCID:PMC4249723)

Cameron, R. T., Quinn, S. D. , Cairns, L. S., MacLeod, R., Samuel, I. D.W., Smith, B. O. , Penedo, J. C. and Baillie, G. S. (2014) The phosphorylation of Hsp20 enhances its association with amyloid-β to increase protection against neuronal cell death. Molecular and Cellular Neuroscience, 61, pp. 46-55. (doi: 10.1016/j.mcn.2014.05.002) (PMID:24859569) (PMCID:PMC4148482)

Ibáñez-Shimabukuro, M., Rey-Burusco, M.F., Cooper, A., Kennedy, M. W. , Córsico, B. and Smith, B. O. (2014) Resonance assignment of As-p18, a fatty acid binding protein secreted by developing larvae of the parasitic nematode Ascaris suum. Biomolecular NMR Assignments, 8(1), pp. 33-36. (doi: 10.1007/s12104-012-9447-1)

Vance, S. J., McDonald, R. E., Cooper, A., Kennedy, M. W. and Smith, B. O. (2014) Resonance assignments for latherin, a natural surfactant protein from horse sweat. Biomolecular NMR Assignments, 8(1), pp. 213-216. (doi: 10.1007/s12104-013-9485-3)

Yvon, C., Surman, A. J. , Hutin, M., Alex, J., Smith, B. O. , Long, D. L. and Cronin, L. (2014) Polyoxometalate clusters integrated into peptide chains and as inorganic amino acids: solution- and solid-phase approaches. Angewandte Chemie (International Edition), 53(13), pp. 3336-3341. (doi: 10.1002/anie.201311135)

Rey-Burusco, M.F., Ibañez-Shimabukuro, M., Cooper, A., Kennedy, M. W. , Córsico, B. and Smith, B. O. (2014) 1H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus. Biomolecular NMR Assignments, 8(1), pp. 19-21. (doi: 10.1007/s12104-012-9444-4)

McCaughey, L. C. et al. (2014) Lectin-like bacteriocins from Pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor. PLoS Pathogens, 10(2), e1003898. (doi: 10.1371/journal.ppat.1003898) (PMID:24516380) (PMCID:PMC3916391)

Caldwell, S.T. et al. (2014) Protein-mediated dethreading of a biotin-functionalised pseudorotaxane. Organic and Biomolecular Chemistry, 12(3), pp. 511-516. (doi: 10.1039/C3OB41612G) (PMID:24280954)

Josts, I., Grinter, R., Kelly, S. M. , Mosbahi, K., Roszak, A., Cogdell, R. , Smith, B. O. , Byron, O. and Walker, D. (2014) Recombinant expression, purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal DUF490963–1138 domain of TamB from Escherichia coli. Acta Crystallographica. Section F: Structural Biology Communications, 70(9), pp. 1272-1275. (doi: 10.1107/S2053230X14017403)

Laird, J. et al. (2013) Identification of the domains of cauliflower mosaic virus protein P6 responsible for suppression of RNA silencing and salicylic acid signalling. Journal of General Virology, 94(12), pp. 2777-2789. (doi: 10.1099/vir.0.057729-0) (PMID:24088344) (PMCID:PMC3836500)

Hamatsu, J. et al. (2013) High-resolution heteronuclear multidimensional NMR of proteins in living insect cells using a baculovirus protein expression system. Journal of the American Chemical Society, 135(5), pp. 1688-1691. (doi: 10.1021/ja310928u)

Vance, S.J., McDonald, R.E., Cooper, A., Smith, B.O. and Kennedy, M.W. (2013) The structure of latherin, a surfactant allergen protein from horse sweat and saliva. Journal of the Royal Society: Interface, 10(85), Art. 20130453. (doi: 10.1098/rsif.2013.0453)

Cloix, C., Kaiserli, E. , Heilmann, M., Baxter, K.J. , Brown, B.A., O'Hara, A., Smith, B.O. , Christie, J.M. and Jenkins, G.I. (2012) C-terminal region of the UV-B photoreceptor UVR8 initiates signaling through interaction with the COP1 protein. Proceedings of the National Academy of Sciences of the United States of America, 109(40), pp. 16366-16370. (doi: 10.1073/pnas.1210898109)

Gabrielsen, M. , Rey-Burusco, M.F., Griffiths, K., Roe, A.J. , Cooper, A., Smith, B.O. , Kennedy, M.W. and Corsico, B. (2012) Two crystal forms of a helix-rich fatty acid- and retinol-binding protein, Na-FAR-1, from the parasitic nematodeNecator americanus. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, 68(7), pp. 835-838. (doi: 10.1107/S1744309112023597) (PMID:22750878) (PMCID:PMC3388935)

Parnell, E., Smith, B. O. , Palmer, T. M., Terrin, A., Zaccolo, M. and Yarwood, S. J. (2012) Regulation of the inflammatory response of vascular endothelial cells by EPAC1. British Journal of Pharmacology, 166(2), pp. 434-446. (doi: 10.1111/j.1476-5381.2011.01808.x)

Christie, J.M. et al. (2012) Plant UVR8 photoreceptor senses UV-B by tryptophan-mediated disruption of cross-dimer salt bridges. Science, 335(6075), pp. 1492-1496. (doi: 10.1126/science.1218091)

Gabrielsen, M. , Riboldi-Tunnicliffe, A., Ibáñez-Shimabukuro, M., Griffiths, K., Roe, A.J. , Cooper, A., Smith, B. , Córsico, B. and Kennedy, M.W. (2012) Useable diffraction data from a multiple microdomain-containing crystal of Ascaris suum As-p18 fatty-acid-binding protein using a microfocus beamline. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, 68, pp. 939-941. (doi: 10.1107/S1744309112026553) (PMID:22869127) (PMCID:PMC3412778)

Gabrielsen, M. , Riboldi-Tunnicliffe, A., Ibáñez-Shimabukuro, M., Griffiths, K., Roe, A.J. , Cooper, A., Smith, B.O. , Córsico, B. and Kennedy, M.W. (2012) Useable diffraction data from a multiple microdomain-containing crystal ofAscaris suumAs-p18 fatty-acid-binding protein using a microfocus beamline. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, 68(8), pp. 939-941. (doi: 10.1107/S1744309112026553) (PMID:22869127) (PMCID:PMC3412778)

Wang, D. et al. (2011) Identification of bacterial target proteins for the salicylidene acylhydrazide class of virulence blocking compounds. Journal of Biological Chemistry, 286(34), pp. 29922-29931. (doi: 10.1074/jbc.M111.233858) (PMID:21724850) (PMCID:PMC3191033)

Meenan, N.A.G., Ball, G., Bromek, K., Uhrín, D., Cooper, A., Kennedy, M.W. and Smith, B.O. (2011) Solution structure of a repeated unit of the ABA-1 nematode polyprotein allergen of ascaris reveals a novel fold and two discrete lipid-binding sites. PLoS Neglected Tropical Diseases, 5(4), e1040. (doi: 10.1371/journal.pntd.0001040)

Ikeya, T. et al. (2010) NMR protein structure determination in living E. coli cells using nonlinear sampling. Nature Protocols, 5(6), pp. 1051-1060. (doi: 10.1038/nprot.2010.69)

MacKenzie, C.D., Smith, B.O., Meister, A., Blume, A., Zhao, X., Lu, J.R., Kennedy, M.W. and Cooper, A. (2009) Ranaspumin-2: structure and function of a surfactant protein from the foam nests of a tropical frog. Biophysical Journal, 96(12), pp. 4984-4992. (doi: 10.1016/j.bpj.2009.03.044)

Sakakibara, D. et al. (2009) Protein structure determination in living cells by in-cell NMR spectroscopy. Nature, 458(7234), pp. 102-105. (doi: 10.1038/nature07814)

Borland, G., Smith, B.O. and Yarwood, S.J. (2009) EPAC proteins transduce diverse cellular actions of cAMP. British Journal of Pharmacology, 158(1), pp. 70-86. (doi: 10.1111/j.1476-5381.2008.00087.x)

dos Reis, F. C.G., Smith, B. O., Santos, C. C., Costa, T., F., Scharfstein, J., Coombs, G. H., Mottram, J. C. and Lima, A. P. C.A. (2008) The role of conserved residues of chagasin in the inhibition of cysteine peptidases. FEBS Letters, 582(4), pp. 485-490. (doi: 10.1016/j.febslet.2008.01.008)

Caldwell, S. T. , Cooke, G. , Cooper, A., Nutley, M., Rabani, G., Rotello, V., Smith, B. O. and Woisel, P. (2008) Tuneable pseudorotaxane formation between a biotin-avidin bioconjugate and CBPQT(4+). Chemical Communications(23), pp. 2650-2652. (doi: 10.1039/b803856b)

Caldwell, S. T. , Cooke, G. , Hewage, S. G., Mabruk, S., Rabani, G., Rotello, V., Smith, B.O. , Subramani, C. and Woisel, P. (2008) Model systems for flavoenzyme activity: intramolecular self-assembly of a flavin derivative via hydrogen bonding and aromatic interactions. Chemical Communications(35), pp. 4126-4128. (doi: 10.1039/b809762c)

Alexander, A. et al. (2007) Probing the solvent-induced tautomerism of a redox-active ureidopyrimidinone. Chemical Communications, pp. 2246-2248. (doi: 10.1039/b703070c)

Smith, B.O., Picken, N.C., Westrop, G.D., Bromek, K., Mottram, J.C. and Coombs, G.H. (2006) The structure of Leishmania mexicana ICP provides evidence for convergent evolution of cysteine peptidase inhibitors. Journal of Biological Chemistry, 281, pp. 5821-5828. (doi: 10.1074/jbc.M510868200)

Ball, G., Meenan, N., Bromek, K., Smith, B., Bella, J. and Uhrin, D. (2006) Measurement of one-bond C-13(alpha)-H-1(alpha) residual dipolar coupling constants in proteins by selective manipulation of (CH alpha)-H-alpha spins. Journal of Magnetic Resonance, 180, pp. 127-136. (doi: 10.1016/j.jmr.2006.01.017)

Smith, B.O., Westrop, G.D., Mottram, J.C. and Coombs, G.H. (2006) Chemical shift assignments of Leishmania mexicana ICP, a novel cysteine peptidase inhibitor. Journal of Biomolecular NMR, 36, p. 7. (doi: 10.1007/s10858-005-4739-8)

Meenan, N.A.G., Cooper, A., Kennedy, M.W. and Smith, B. (2005) Resonance assignment of ABA-1A, from Ascaris suum nematode polyprotein allergen. Journal of Biomolecular NMR, 32(2), p. 176. (doi: 10.1007/s10858-005-6070-9)

Weber, M.A. et al. (2004) Blood pressure dependent and independent effects of antihypertensive treatment on clinical events in the VALUE Trial. Lancet, 363(9426), pp. 2049-2051. (doi: 10.1016/S0140-6736(04)16456-8)

Smith, B. (2004) Structural analysis of the complement control protein (CCP) modules of GABAB receptor 1a: only one of the two ccp modules is compactly folded. Journal of Biological Chemistry, 279(46), pp. 48292-48306. (doi: 10.1074/jbc.M406540200)

Bramham, J., Hodgkinson, J., Smith, B., Uhrin, D., Barlow, P. and Winder, S. (2002) Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin : calponin. Structure, 10, pp. 249-258.

Smith, B. (2002) Structure of the C3b binding site of CR1 (CD35), the immune adherence receptor. Cell, 108(6), pp. 769-780. (doi: 10.1016/S0092-8674(02)00672-4)

Smith, B. (2001) DNA recognition by the methyl-CpG binding domain of MeCP2. Journal of Biological Chemistry, 276(5), pp. 3353-3360. (doi: 10.1074/jbc.M007224200)

Smith, B. (2001) Solution structure and dynamics of the central CCP module pair of a poxvirus complement control protein. Journal of Molecular Biology, 307(1), pp. 323-339. (doi: 10.1006/jmbi.2000.4477)

Book Sections

Kennedy, M.W., Córsico, B., Cooper, A. and Smith, B.O. (2013) The unusual lipid-binding proteins of nematodes: NPAs, nemFABPs and FARs. In: Kennedy, M. and Harnett, m. (eds.) Parasitic Nematodes: Molecular Biology, Biochemistry and Immunology [2nd. ed.]. CABI; Wallingford; UK, pp. 397-412. ISBN 9781845937591 (doi: 10.1079/9781845937591.0397)

This list was generated on Sun Nov 17 21:25:21 2024 GMT.

Grants

Grants and Awards listed are those received whilst working with the University of Glasgow.

  • Disarming Type 3 Secretion - elucidating the mechanism of action for aurodox
    Biotechnology and Biological Sciences Research Council
    2024 - 2027
     
  • Facilitate the use of NMR spectroscopy by scientists based in Scotland
    University of Edinburgh
    2022 - 2023
     
  • Co-ordinated Photoreceptor Engineering for Improved Biomass Production
    Biotechnology and Biological Sciences Research Council
    2020 - 2023
     
  • Role of reversible modification of methionine residues in the regulation of protein function
    Biotechnology and Biological Sciences Research Council
    2020 - 2023
     
  • Scottish High-Field NMR Facility
    Engineering and Physical Sciences Research Council (EPSRC)
    2018 - 2021
     
  • A novel mechanism of protein uptake in Gram-negative bacteria
    Biotechnology and Biological Sciences Research Council
    2014 - 2018
     
  • Assessing the predictive value of quantitative high-throughput NMR metabolomic analysis for CVD events in a major study of diabetes: ADVANCE
    Chest Heart and Stroke Scotland
    2013 - 2016
     
  • How does the plant UV-B photoreceptor UVR8 initiate signalling?
    Biotechnology and Biological Sciences Research Council
    2013 - 2016
     
  • Final structure refinement and functional analysis of Na-FAR-1
    Boehringer Ingelheim
    2012 - 2012
     
  • Structure determination and functional analysis through Nuclear Magnetic Resonance
    Boehringer Ingelheim
    2012 - 2012
     
  • The application of a high-throughput NMR metabolomics system to the study of insulin resistance (ISSF Catalyst)
    Wellcome Trust
    2011 - 2014
     
  • Interaction between the essential replication factor TopBP1 and human papillomavirus 16 E1: a novel antiviral target
    Cancer Research UK
    2011 - 2015
     
  • Identification of small molecule activators of EPAC1 to serve as novel anti-inflamatory agents in vascular endothelial cells
    Scottish Universities Life Sciences Alliance
    2011 - 2012
     
  • Quest for the Holy Grail of plant photobiology: a UV-B photoreceptor
    Leverhulme Trust
    2010 - 2014
     
  • Structural and biophysical analysis of novel lipid binding proteins from parasitic helminths
    Wellcome Trust
    2008 - 2012
     
  • The solution structures of newly discovered natural inhibitors of cystine peptidases from eukaryotic and bacterial pathogens
    Wellcome Trust
    2004 - 2008
     
  • Toward Understanding the structural basis of molecular recognition by methylated DNA binding proteins
    The Royal Society
    2004 - 2005
     
  • Establishment of high field NMR facility
    Wellcome Trust
    2003 - 2006
     

Research datasets

Jump to: 2017 | 2015
Number of items: 2.

2017

Gabrielsen, M., Buetow, L., Nakasone, M., Ahmed, S., Sibbet, G., Smith, B. , Zhang, W., Sidhu, S. and Huang, D. (2017) A general strategy for discovery of inhibitors and activators of RING and U-box E3 ligases with ubiquitin variants. [Data Collection]

2015

Buetow, L., Gabrielsen, M., Anthony, N., Dou, H., Patel, A., Aitkenhead, H., Sibbet, G., Smith, B. and Huang, D. (2015) Activation of a primed RING E3-E2-ubiquitn complex by non-covalent ubiquitin. [Data Collection]

This list was generated on Mon Nov 18 08:15:32 2024 GMT.

Additional information

Grant Advisory Board

  • 2001 - 2009: BBSRC - Member of Executive Committee of CCPN (A Collaborative Computing Project for the NMR Community). Committee Chair 2007-2009

Invited International Presentations

  • 2013: La Plata, Argentina - 8th International Conference on Lipid Binding Proteins: Session chair, Structural Biology of LBPs; Invited speaker, "Structures and ligand binding of all-alpha-helical lipid binding proteins from nematodes"
  • 2009: Ambleside, England - Meeting Chair, 9th CCPN Meeting; speaker, "An overview of fast NMR methods and their practical aspects"
  • 2008: Ambleside, England - Meeting Chair 8th CCPN Meeting
  • 2007: Tokyo, Japan - Invited speaker, Symposium: "Application of advanced analytical techniques to chemical substances", Tokyo Metropolitan University
  • 2007: Ambleside, England - Co-organiser and Session Chair 7th CCPN Meeting - NMR of problematic biological systems
  • 2006: Ambleside, England - Co-organiser and Session Chair 6th CCPN Meeting - Effective and Rapid Structure Determination by NMR
  • 2005: Ambleside, England - Co-organiser and Session Chair 5th CCPN Meeting - NMR and Molecular Interaction

Research Fellowship

  • 1999 - 2003: MRC Career Development Fellowship

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