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• Journal article
  Filloux A, 2011,

  Protein secretion systems in Pseudomonas aeruginosa: an essay on diversity, evolution, and function

  , Frontiers in Microbiology, Vol: 2, ISSN: 1664-302X

  Protein secretion systems are molecular nanomachines used by Gram-negative bacteria to thrive within their environment. They are used to release enzymes that hydrolyze complex carbon sources into usable compounds, or to release proteins that capture essential ions such as iron. They are also used to colonize and survive within eukaryotic hosts, causing acute or chronic infections, subverting the host cell response and escaping the immune system. In this article, the opportunistic human pathogen Pseudomonas aeruginosa is used as a model to review the diversity of secretion systems that bacteria have evolved to achieve these goals. This diversity may result from a progressive transformation of cell envelope complexes that initially may not have been dedicated to secretion. The striking similarities between secretion systems and type IV pili, flagella, bacteriophage tail, or efflux pumps is a nice illustration of this evolution. Differences are also needed since various secretion configurations call for diversity. For example, some proteins are released in the extracellular medium while others are directly injected into the cytosol of eukaryotic cells. Some proteins are folded before being released and transit into the periplasm. Other proteins cross the whole cell envelope at once in an unfolded state. However, the secretion system requires conserved basic elements or features. For example, there is a need for an energy source or for an outer membrane channel. The structure of this review is thus quite unconventional. Instead of listing secretion types one after each other, it presents a melting pot of concepts indicating that secretion types are in constant evolution and use basic principles. In other words, emergence of new secretion systems could be predicted the way Mendeleïev had anticipated characteristics of yet unknown elements.

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• Journal article
  Luther PK, Winkler H, Taylor K, Zoghbi ME, Craig R, Padron R, Squire JM, Liu Jet al., 2011,

  Direct visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle

  , PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 108, Pages: 11423-11428, ISSN: 0027-8424
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  • Citations: 138
• Journal article
  Sedoud A, Cox N, Sugiura M, Lubitz W, Boussac A, Rutherford AWet al., 2011,

  Semiquinone-iron complex of photosystem II: EPR signals assigned to the low-field edge of the ground state doublet of QA•-Fe2+ and QB•-Fe2+.

  , Biochemistry, Vol: 50, Pages: 6012-6021

  The quinone-iron complex of the electron acceptor complex of Photosystem II was studied by EPR spectroscopy in Thermosynechococcus elongatus. New g ∼ 2 features belonging to the EPR signal of the semiquinone forms of the primary and secondary quinone, i.e., Q(A)(•-)Fe(2+) and Q(B)(•-)Fe(2+), respectively, are reported. In previous studies, these signals were missed because they were obscured by the EPR signal arising from the stable tyrosyl radical, TyrD(•). When the TyrD(•) signal was removed, either by chemical reduction or by the use of a mutant lacking TyrD, the new signals dominated the spectrum. For Q(A)(•-)Fe(2+), the signal was formed by illumination at 77 K or by sodium dithionite reduction in the dark. For Q(B)(•-)Fe(2+), the signal showed the characteristic period-of-two variations in its intensity when generated by a series of laser flashes. The new features showed relaxation characteristics comparable to those of the well-known features of the semiquinone-iron complexes and showed a temperature dependence consistent with an assignment to the low-field edge of the ground state doublet of the spin system. Spectral simulations are consistent with this assignment and with the current model of the spin system. The signal was also present in Q(B)(•-)Fe(2+) in plant Photosystem II, but in plants, the signal was not detected in the Q(A)(•-)Fe(2+) state.

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• Journal article
  Saridakis E, Khurshid S, Govada L, Phan Q, Hawkins D, Crichlow GV, Lolis E, Reddy SM, Chayen NEet al., 2011,

  Protein crystallization facilitated by molecularly imprinted polymers

  , PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 108, Pages: 11081-11086, ISSN: 0027-8424
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  • Citations: 117
• Journal article
  Chen S, Beeby M, Murphy GE, Leadbetter JR, Hendrixson DR, Briegel A, Li Z, Shi J, Tocheva EI, Muller A, Dobro MJ, Jensen GJet al., 2011,

  Structural diversity of bacterial flagellar motors

  , EMBO J., Vol: 30, Pages: 2972-2981
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• Journal article
  Su J-H, Cox N, Ames W, Pantazis DA, Rapatskiy L, Lohmiller T, Kulik LV, Dorlet P, Rutherford AW, Neese F, Boussac A, Lubitz W, Messinger Jet al., 2011,

  The electronic structures of the <i>S</i>₂ states of the oxygen-evolving complexes of photosystem II in plants and cyanobacteria in the presence and absence of methanol

  , BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, Vol: 1807, Pages: 829-840, ISSN: 0005-2728
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  • Citations: 72
• Journal article
  Mikkelsen H, Sivaneson M, Filloux A, 2011,

  Key two-component regulatory systems that control biofilm formation in <i>Pseudomonas aeruginosa</i>

  , ENVIRONMENTAL MICROBIOLOGY, Vol: 13, Pages: 1666-1681, ISSN: 1462-2912
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  • Citations: 180
• Journal article
  Herrero C, Quaranta A, Leibl W, Rutherford AW, Aukauloo Aet al., 2011,

  Artificial photosynthetic systems. Using light and water to provide electrons and protons for the synthesis of a fuel

  , ENERGY & ENVIRONMENTAL SCIENCE, Vol: 4, Pages: 2353-2365, ISSN: 1754-5692
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  • Citations: 93
• Journal article
  Ramachandran PL, Lovett JE, Carl PJ, Cammarata M, Lee JH, Jung YO, Ihee H, Timmel CR, van Thor JJet al., 2011,

  The Short-Lived Signaling State of the Photoactive Yellow Protein Photoreceptor Revealed by Combined Structural Probes

  , JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, Vol: 133, Pages: 9395-9404, ISSN: 0002-7863
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  • Citations: 73
• Journal article
  Herrero C, Quaranta A, Protti S, Leibl W, Rutherford AW, Fallahpour R, Charlot M-F, Aukauloo Aet al., 2011,

  Light-Driven Activation of the [H₂O(terpy)Mn<SUP>III</SUP>-μ-(O₂)-Mn<SUP>IV</SUP>(terpy)OH₂] Unit in a Chromophore-Catalyst Complex

  , CHEMISTRY-AN ASIAN JOURNAL, Vol: 6, Pages: 1335-1339, ISSN: 1861-4728
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  • Citations: 21
• Journal article
  Sage JT, Zhang Y, McGeehan J, Ravelli RBG, Weik M, Thor JJVet al., 2011,

  Infrared protein crystallography

  , Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics, Vol: 1841, Pages: 760-777

  We consider the application of infrared spectroscopy to protein crystals, with particular emphasis on exploiting molecular orientation through polarization measurements on oriented single crystals. Infrared microscopes enable transmission measurements on individual crystals using either thermal or nonthermal sources, and can accommodate flow cells, used to measure spectral changes induced by exposure to soluble ligands, and cryostreams, used for measurements of flash-cooled crystals. Comparison of unpolarized infrared measurements on crystals and solutions probes the effects of crystallization and can enhance the value of the structural models refined from X-ray diffraction data by establishing solution conditions under which they are most relevant. Results on several proteins are consistent with similar equilibrium conformational distributions in crystal and solutions. However, the rates of conformational change are often perturbed. Infrared measurements also detect products generated by X-ray exposure, including CO2. Crystals with favorable symmetry exhibit infrared dichroism that enhances the synergy with X-ray crystallography. Polarized infrared measurements on crystals can distinguish spectral contributions from chemically similar sites, identify hydrogen bonding partners, and, in opportune situations, determine three-dimensional orientations of molecular groups. This article is part of a Special Issue entitled: Protein Structure and Function in the Crystalline State.

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• Journal article
  Garcia-Caballero A, Gavira JA, Pineda-Molina E, Chayen NE, Govada L, Khurshid S, Saridakis E, Boudjemline A, Swann MJ, Stewart PS, Briggs RA, Kolek SA, Oberthuer D, Dierks K, Betzel C, Santana M, Hobbs JR, Thaw P, Savill TJ, Mesters JR, Hilgenfeld R, Bonander N, Bill RMet al., 2011,

  Optimization of Protein Crystallization: The OptiCryst Project

  , CRYSTAL GROWTH & DESIGN, Vol: 11, Pages: 2112-2121, ISSN: 1528-7483
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  • Citations: 12
• Conference paper
  Choudhury HG, Cameron AD, Iwata S, Beis Ket al., 2011,

  <i>Escherichia coli</i> detoxification of chalcolgens by TehAB

  , 36th FEBS Congress of the Biochemistry for Tomorrows Medicine, Publisher: WILEY-BLACKWELL, Pages: 101-101, ISSN: 1742-464X
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• Journal article
  Michoux F, Ahmad N, McCarthy J, Nixon PJet al., 2011,

  Contained and high-level production of recombinant protein in plant chloroplasts using a temporary immersion bioreactor

  , PLANT BIOTECHNOLOGY JOURNAL, Vol: 9, Pages: 575-584, ISSN: 1467-7644
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  • Citations: 32
• Journal article
  Wong ARC, Pearson JS, Bright MD, Munera D, Robinson KS, Lee SF, Frankel G, Hartland ELet al., 2011,

  Enteropathogenic and enterohaemorrhagic <i>Escherichia coli</i>: even more subversive elements

  , MOLECULAR MICROBIOLOGY, Vol: 80, Pages: 1420-1438, ISSN: 0950-382X
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  • Citations: 273
• Journal article
  Reichmann NT, Gruendling A, 2011,

  Location, synthesis and function of glycolipids and polyglycerolphosphate lipoteichoic acid in Gram-positive bacteria of the phylum <i>Firmicutes</i>

  , FEMS MICROBIOLOGY LETTERS, Vol: 319, Pages: 97-105, ISSN: 0378-1097
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  • Citations: 147
• Journal article
  Kafasla P, Lin H, Curry S, Jackson RJet al., 2011,

  Activation of picornaviral IRESs by PTB shows differential dependence on each PTB RNA-binding domain

  , RNA, Vol: 17, Pages: 1120-1131, ISSN: 1355-8382
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  • Citations: 30
• Journal article
  Machuca-Tzili LE, Buxton S, Thorpe A, Timson CM, Wigmore P, Luther PK, Brook JDet al., 2011,

  Zebrafish deficient for Muscleblind-like 2 exhibit features of myotonic dystrophy

  , DISEASE MODELS & MECHANISMS, Vol: 4, Pages: 381-392, ISSN: 1754-8403
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  • Citations: 25
• Journal article
  Robinson KS, Clements A, Williams AC, Berger CN, Frankel Get al., 2011,

  Bax Inhibitor 1 in apoptosis and disease

  , ONCOGENE, Vol: 30, Pages: 2391-2400, ISSN: 0950-9232
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  • Citations: 61
• Journal article
  Boehm M, Romero E, Reisinger V, Yu J, Komenda J, Eichacker LA, Dekker JP, Nixon PJet al., 2011,

  Investigating the Early Stages of Photosystem II Assembly in Synechocystis sp PCC 6803 <i>ISOLATION OF CP47 AND CP43 COMPLEXES</i>

  , JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 286, Pages: 14812-14819
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  • Citations: 92
• Journal article
  Nishi K, Ono T, Nakamura T, Fukunaga N, Izumi M, Watanabe H, Suenaga A, Maruyama T, Yamagata Y, Curry S, Otagiri Met al., 2011,

  Structural Insights into Differences in Drug-binding Selectivity between Two Forms of Human α1-Acid Glycoprotein Genetic Variants, the A and F1*S Forms

  , Journal of Biological Chemistry, Vol: 286, Pages: 14427-14434, ISSN: 1083-351X

  Human α(1)-acid glycoprotein (hAGP) in serum functions as a carrier of basic drugs. In most individuals, hAGP exists as a mixture of two genetic variants, the F1*S and A variants, which bind drugs with different selectivities. We prepared a mutant of the A variant, C149R, and showed that its drug-binding properties were indistinguishable from those of the wild type. In this study, we determined the crystal structures of this mutant hAGP alone and complexed with disopyramide (DSP), amitriptyline (AMT), and the nonspecific drug chlorpromazine (CPZ). The crystal structures revealed that the drug-binding pocket on the A variant is located within an eight-stranded β-barrel, similar to that found in the F1*S variant and other lipocalin family proteins. However, the binding region of the A variant is narrower than that of the F1*S variant. In the crystal structures of complexes with DSP and AMT, the two aromatic rings of each drug interact with Phe-49 and Phe-112 at the bottom of the binding pocket. Although the structure of CPZ is similar to those of DSP and AMT, its fused aromatic ring system, which is extended in length by the addition of a chlorine atom, appears to dictate an alternative mode of binding, which explains its nonselective binding to the F1*S and A variant hAGPs. Modeling experiments based on the co-crystal structures suggest that, in complexes of DSP, AMT, or CPZ with the F1*S variant, Phe-114 sterically hinders interactions with DSP and AMT, but not CPZ.

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• Journal article
  Masino L, Nicastro G, De Simone A, Calder L, Molloy J, Pastore Aet al., 2011,

  The Josephin Domain Determines the Morphological and Mechanical Properties of Ataxin-3 Fibrils

  , BIOPHYSICAL JOURNAL, Vol: 100, Pages: 2033-2042, ISSN: 0006-3495
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  • Citations: 42
• Journal article
  Ryan AJ, Chung C-W, Curry S, 2011,

  Crystallographic analysis reveals the structural basis of the high-affinity binding of iophenoxic acid to human serum albumin

  , BMC STRUCTURAL BIOLOGY, Vol: 11
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  • Citations: 30
• Journal article
  Sheppard C, Camara B, Shadrin A, Akulenko N, Lu M, Baldwin G, Severinov K, Cota E, Matthews S, Wigneshweraraj SRet al., 2011,

  Inhibition of <i>Escherichia coli</i> RNAp by T7 Gp2 Protein: Role of Negatively Charged Strip of Amino Acid Residues in Gp2

  , JOURNAL OF MOLECULAR BIOLOGY, Vol: 407, Pages: 623-632, ISSN: 0022-2836
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  • Citations: 10
• Journal article
  Attia M, Foerster A, Rachez C, Freemont P, Avner P, Rogner UCet al., 2011,

  Interaction between Nucleosome Assembly Protein 1-like Family Members

  , JOURNAL OF MOLECULAR BIOLOGY, Vol: 407, Pages: 647-660, ISSN: 0022-2836
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  • Citations: 35
• Journal article
  Grippon S, Zhao Q, Robinson T, Marshall JJT, O'Neill RJ, Manning H, Kennedy G, Dunsby C, Neil M, Halford SE, French PMW, Baldwin GSet al., 2011,

  Differential modes of DNA binding by mismatch uracil DNA glycosylase from Escherichia coli: implications for abasic lesion processing and enzyme communication in the base excision repair pathway

  , Nucleic Acids Research, Vol: 39, Pages: 2593-2603, ISSN: 1362-4962

  Mismatch uracil DNA glycosylase (Mug) fromEscherichia coli is an initiating enzyme in thebase-excision repair pathway. As with other DNAglycosylases, the abasic product is potentiallymore harmful than the initial lesion. Since Mug isknown to bind its product tightly, inhibitingenzyme turnover, understanding how Mug bindsDNA is of significance when considering how Muginteracts with downstream enzymes in the baseexcisionrepair pathway. We have demonstrateddifferential binding modes of Mug between its substrateand abasic DNA product using both band shiftand fluorescence anisotropy assays. Mug binds itsproduct cooperatively, and a stoichiometric analysisof DNA binding, catalytic activity and saltdependenceindicates that dimer formation is offunctional significance in both catalytic activity andproduct binding. This is the first report ofcooperativity in the uracil DNA glycosylase superfamilyof enzymes, and forms the basis of productinhibition in Mug. It therefore provides a new perspectiveon abasic site protection and the findingsare discussed in the context of downstream lesionprocessing and enzyme communication in the baseexcision repair pathway.

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• Journal article
  Choudhury HG, Cameron AD, Iwata S, Beis Ket al., 2011,

  Structure and mechanism of the chalcogen-detoxifying protein TehB from <i>Escherichia coli</i>

  , BIOCHEMICAL JOURNAL, Vol: 435, Pages: 85-91, ISSN: 0264-6021
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  • Citations: 12
• Journal article
  Salgado PS, Yan R, Rowan F, Cota Eet al., 2011,

  Expression, crystallization and preliminary X-ray data analysis of NT-Als9-2, a fungal adhesin from <i>Candida albicans</i>

  , ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, Vol: 67, Pages: 467-470
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  • Citations: 3
• Journal article
  Petit SJ, Wise EL, Chambers JC, Sehmi J, Chayen NE, Kooner JS, Pease JEet al., 2011,

  The CXCL16 A181V Mutation Selectively Inhibits Monocyte Adhesion to CXCR6 but Is Not Associated With Human Coronary Heart Disease

  , ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY, Vol: 31, Pages: 914-920, ISSN: 1079-5642
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  • Citations: 16
• Journal article
  Pearson JS, Riedmaier P, Marches O, Frankel G, Hartland ELet al., 2011,

  A type III effector protease NleC from enteropathogenic <i>Escherichia coli</i> targets NF-κB for degradation

  , MOLECULAR MICROBIOLOGY, Vol: 80, Pages: 219-230, ISSN: 0950-382X
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  • Citations: 102

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