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  • Journal article
    Bolanos-Garcia VM, Chayen NE, 2009,

    , PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, Vol: 101, Pages: 3-12, ISSN: 0079-6107
  • Journal article
    Hu Y, Guimond SE, Travers P, Cadman S, Hohenester E, Turnbull JE, Kim S-H, Bouloux P-Met al., 2009,

    , JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 284, Pages: 29905-29920
  • Journal article
    Boehm M, Nield J, Zhang P, Aro E-M, Komenda J, Nixon PJet al., 2009,

    , JOURNAL OF BACTERIOLOGY, Vol: 191, Pages: 6425-6435, ISSN: 0021-9193
  • Journal article
    Webb AJ, Karatsa-Dodgson M, Grundling A, 2009,

    , MOLECULAR MICROBIOLOGY, Vol: 74, Pages: 299-314, ISSN: 0950-382X
  • Journal article
    Hare S, Cherepanov P, Wang J, 2009,

    , ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, Vol: 65, Pages: 966-973, ISSN: 2059-7983
  • Journal article
    Liu Y, Garnett JA, Leon E, Allman SA, Friedrich N, Saouros S, Curry S, Soldati-Favre D, Davis BG, Feizi T, Matthews Set al., 2009,

    Detailed insights from microarray and crystallographic studies into carbohydrate recognition by microneme protein 1 (MIC1) of Toxoplasma gondii

    , Protein Sci., Vol: 18, Pages: 1935-1947

    The intracellular protozoan Toxoplasma gondii is among the most widespread parasites. The broad host cell range of the parasite can be explained by carbohydrate microarray screening analyses that have demonstrated the ability of the T. gondii adhesive protein, TgMIC1, to bind to a wide spectrum of sialyl oligosaccharide ligands. Here, we investigate by further microarray analyses in a dose-response format the differential binding of TgMIC1 to 2-3- and 2-6-linked sialyl carbohydrates. Interestingly, two novel synthetic fluorinated analogs of 3'SiaLacNAc(1-4) and 3'SiaLacNAc(1-3) were identified as highly potent ligands. To understand the structural basis of the carbohydrate binding specificity of TgMIC1, we have determined the crystal structures of TgMIC1 micronemal adhesive repeat (MAR)-region (TgMIC1-MARR) in complex with five sialyl-N-acetyllactosamine analogs. These crystal structures have revealed a specific, water-mediated hydrogen bond network that accounts for the preferential binding of TgMIC1-MARR to arrayed 2-3-linked sialyl oligosaccharides and the high potency of the fluorinated analogs. Furthermore, we provide strong evidence for the first observation of a C--F...H--O hydrogen bond within a lectin-carbohydrate complex. Finally, detailed comparison with other oligosaccharide-protein complexes in the Protein Data Bank (PDB) reveals a new family of sialic-acid binding sites from lectins in parasites, bacteria, and viruses

  • Journal article
    Luther PK, 2009,

    , JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY, Vol: 30, Pages: 171-185, ISSN: 0142-4319
  • Journal article
    Gulati S, Rouilly V, Niu X, Chappell J, Kitney RI, Edel JB, Freemont PS, deMello AJet al., 2009,

    , JOURNAL OF THE ROYAL SOCIETY INTERFACE, Vol: 6, ISSN: 1742-5689
  • Journal article
    Mota LJ, Ramsden AE, Liu M, Castle JD, Holden DWet al., 2009,

    , CELLULAR MICROBIOLOGY, Vol: 11, Pages: 1236-1253, ISSN: 1462-5814
  • Journal article
    Curry S, Kotik-Kogan O, Conte MR, Brick Pet al., 2009,

    , BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS, Vol: 1789, Pages: 653-666, ISSN: 1874-9399
  • Journal article
    Xu Y, Liu M, Simpson PJ, Isaacson R, Cota E, Marchant J, Yang D, Zhang X, Freemont P, Matthews Set al., 2009,

    , JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, Vol: 131, Pages: 9480-+, ISSN: 0002-7863
  • Journal article
    Hare S, Di Nunzio F, Labeja A, Wang J, Engelman A, Cherepanov Pet al., 2009,

    , PLOS PATHOGENS, Vol: 5, ISSN: 1553-7366
  • Book chapter
    Lou HB, Beis K, Naismith JH, 2009,

    Bacterial Membrane Proteins: The New Soluble Proteins?

    , Membrane Protein Crystallization, Editors: Delucas, Publisher: Academic Pr, Pages: 269-297, ISBN: 9780123749871

    This volume of Current Topics in Membranes focuses on Membrane Protein Crystallization, beginning with a review of past successes and general trends, then ...

  • Journal article
    Mikkelsen H, Ball G, Giraud C, Filloux Aet al., 2009,

    , PLoS ONE, Vol: 4, ISSN: 1932-6203

    Pseudomonas aeruginosa is a gram-negative pathogenic bacterium with a high adaptive potential that allows proliferation in a broad range of hosts or niches. It is also the causative agent of both acute and chronic biofilm-related infections in humans. Three cup gene clusters (cupA-C), involved in the assembly of cell surface fimbriae, have been shown to be involved in biofilm formation by the P. aeruginosa strains PAO1 or PAK. In PA14 isolates, a fourth cluster, named cupD, was identified within a pathogenicity island, PAPI-I, and may contribute to the higher virulence of this strain. Expression of the cupA genes is controlled by the HNS-like protein MvaT, whereas the cupB and cupC genes are under the control of the RocS1A1R two-component system. In this study, we show that cupD gene expression is positively controlled by the response regulator RcsB. As a consequence, CupD fimbriae are assembled on the cell surface, which results in a number of phenotypes such as a small colony morphotype, increased biofilm formation and decreased motility. These behaviors are compatible with the sessile bacterial lifestyle. The balance between planktonic and sessile lifestyles is known to be linked to the intracellular levels of c-di-GMP with high levels favoring biofilm formation. We showed that the EAL domain-containing PvrR response regulator counteracts the activity of RcsB on cupD gene expression. The action of PvrR is likely to involve c-di-GMP degradation through phosphodiesterase activity, confirming the key role of this second messenger in the balance between bacterial lifestyles. The regulatory network between RcsB and PvrR remains to be elucidated, but it stands as a potential model system to study how the equilibrium between the two lifestyles could be influenced by therapeutic agents that favor the planktonic lifestyle. This would render the pathogen accessible for the immune system or conventional antibiotic treatment.

  • Journal article
    Baldwin GS, Brooks NJ, Robson RE, Wynveen A, Goldar A, Leikin S, Seddon JM, Kornyshev AAet al., 2009,

    DNA Double Helices Recognize Mutual Sequence Homology in a Protein Free Environment

    , JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, Vol: 26, Pages: 880-880, ISSN: 0739-1102
  • Journal article
    Asanithi P, Saridakis E, Govada L, Jurewicz I, Brunner EW, Ponnusamy R, Cleaver JAS, Dalton AB, Chayen NE, Sear RPet al., 2009,

    , ACS APPLIED MATERIALS & INTERFACES, Vol: 1, Pages: 1203-1210, ISSN: 1944-8244
  • Conference paper
    Murray JW, Barber J, 2009,

    , Annual Meeting of the Society-for-Experimental-Biology, Publisher: ELSEVIER SCIENCE INC, Pages: S177-S177, ISSN: 1095-6433
  • Journal article
    Chan KLA, Govada L, Bill RM, Chayen NE, Kazarian SGet al., 2009,

    , ANALYTICAL CHEMISTRY, Vol: 81, Pages: 3769-3775, ISSN: 0003-2700
  • Journal article
    Thomas M, Holden DW, 2009,

    , CELL HOST & MICROBE, Vol: 5, Pages: 309-311, ISSN: 1931-3128
  • Journal article
    Boussac A, Sugiura M, Rutherford AW, Dorlet Pet al., 2009,

    , J Am Chem Soc, Vol: 131, Pages: 5050-5051

    Despite crystallographic structures now available and intensive work in the past decades, little is known about the higher redox states of the catalytic cycle of Photosystem II, the enzyme responsible for the presence of O(2) on Earth and at the beginning of the process that has produced both the biomass and the fossil fuels. In one of the highest oxidation states, the S(3)-state, only signals at g-values higher than 4 have been detected so far at the X-band. In this work, we report for the first time the complete X-band EPR spectrum for the S(3)-state of Photosystem II. Simulations show that, for a spin state S = 1, as was previously suggested for S(3), it is not possible to account for all the features observed. A satisfactory simulated spectrum was obtained for a spin state S = 3 with zero-field splitting parameters D = 0.175 cm(-1) and E/D = 0.275. The detection of the full EPR signal for S(3) opens the door for new investigations and a better understanding of the catalytic cycle of Photosystem II.

  • Journal article
    Yoon CH, Bodvarsson B, Klim S, Morkebjerg M, Mortensen S, Chen J, Maclaren JR, Luther PK, Squire JM, Bones PJ, Millane RPet al., 2009,

    , IEEE TRANSACTIONS ON IMAGE PROCESSING, Vol: 18, Pages: 831-839, ISSN: 1057-7149
  • Journal article
    Burrows PC, Joly N, Cannon WV, Camara BP, Rappas M, Zhang X, Dawes K, Nixon BT, Wigneshweraraj SR, Buck Met al., 2009,

    , JOURNAL OF MOLECULAR BIOLOGY, Vol: 387, Pages: 306-319, ISSN: 0022-2836
  • Journal article
    Yan N, Cherepanov P, Daigle JE, Engelman A, Lieberman Jet al., 2009,

    , PLOS PATHOGENS, Vol: 5, ISSN: 1553-7366
  • Journal article
    Zaitseva L, Cherepanov P, Leyens L, Wilson SJ, Rasaiyaah J, Fassati Aet al., 2009,

    , RETROVIROLOGY, Vol: 6
  • Journal article
    Lu D, Wörmann ME, Zhang X, Schneewind O, Gründling A, Freemont PS, co-corresponding authorset al., 2009,

  • Journal article
    Saridakis E, Chayen NE, 2009,

    , TRENDS IN BIOTECHNOLOGY, Vol: 27, Pages: 99-106, ISSN: 0167-7799
  • Journal article
    Hwang Y-S, Cho J, Tay F, Heng JYY, Ho R, Kazarian SG, Williams DR, Boccaccini AR, Polak JM, Mantalaris Aet al., 2009,

    , BIOMATERIALS, Vol: 30, Pages: 499-507, ISSN: 0142-9612
  • Journal article
    Goodman AL, Merighi M, Hyodo M, Ventre I, Filloux A, Lory Set al., 2009,

    , GENES & DEVELOPMENT, Vol: 23, Pages: 249-259, ISSN: 0890-9369
  • Journal article
    Emami K, Topakas E, Nagy T, Henshaw J, Jackson KA, Nelson KE, Mongodin EF, Murray JW, Lewis RJ, Gilbert HJet al., 2009,

    , JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 284, Pages: 1086-1096
  • Journal article
    Valkov E, Gupta SS, Hare S, Helander A, Roversi P, McClure M, Cherepanov Pet al., 2009,

    , NUCLEIC ACIDS RESEARCH, Vol: 37, Pages: 243-255, ISSN: 0305-1048

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