Search Results - "Pilak, Oliver"

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  1. 1

    Crystal Structure of [Fe]-Hydrogenase Reveals the Geometry of the Active Site by Shima, Seigo, Pilak, Oliver, Vogt, Sonja, Schick, Michael, Stagni, Marco S, Meyer-Klaucke, Wolfram, Warkentin, Eberhard, Thauer, Rudolf K, Ermler, Ulrich

    “…Biological formation and consumption of molecular hydrogen (H₂) are catalyzed by hydrogenases, of which three phylogenetically unrelated types are known:…”
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    Journal Article
  2. 2

    The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex by Hiromoto, Takeshi, Ataka, Kenichi, Pilak, Oliver, Vogt, Sonja, Stagni, Marco Salomone, Meyer-Klaucke, Wolfram, Warkentin, Eberhard, Thauer, Rudolf K., Shima, Seigo, Ermler, Ulrich

    Published in FEBS letters (04-02-2009)
    “…[Fe]-hydrogenase is one of three types of enzymes known to activate H 2. Crystal structure analysis recently revealed that its active site iron is ligated…”
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    Journal Article
  3. 3
  4. 4

    Chaperonins from an Antarctic archaeon are predominantly monomeric: crystal structure of an open state monomer by Pilak, Oliver, Harrop, Stephen J., Siddiqui, Khawar S., Chong, Kevin, De Francisci, Davide, Burg, Dominic, Williams, Timothy J., Cavicchioli, Ricardo, Curmi, Paul M. G.

    Published in Environmental microbiology (01-08-2011)
    “…Summary Archaea are abundant in permanently cold environments. The Antarctic methanogen, Methanococcoides burtonii, has proven an excellent model for studying…”
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  5. 5

    Global Proteomic Analysis of the Insoluble, Soluble, and Supernatant Fractions of the Psychrophilic Archaeon Methanococcoides burtonii Part I: The Effect of Growth Temperature by Williams, Timothy J, Burg, Dominic W, Raftery, Mark J, Poljak, Anne, Guilhaus, Michael, Pilak, Oliver, Cavicchioli, Ricardo

    Published in Journal of proteome research (05-02-2010)
    “…The response of the cold-adapted (psychrophilic) methanogenic archaeon Methanococcoides burtonii to growth temperature was investigated using differential…”
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    Journal Article
  6. 6

    The Crystal Structure of the Apoenzyme of the Iron–Sulphur Cluster-free Hydrogenase by Pilak, Oliver, Mamat, Björn, Vogt, Sonja, Hagemeier, Christoph H., Thauer, Rudolf K., Shima, Seigo, Vonrhein, Clemens, Warkentin, Eberhard, Ermler, Ulrich

    Published in Journal of molecular biology (05-05-2006)
    “…The iron–sulphur cluster-free hydrogenase (Hmd, EC 1.12.98.2) from methanogenic archaea is a novel type of hydrogenase that tightly binds an iron-containing…”
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    Journal Article
  7. 7

    A chemically modified α-amylase with a molten-globule state has entropically driven enhanced thermal stability by Siddiqui, Khawar Sohail, Poljak, Anne, De Francisci, Davide, Guerriero, Gea, Pilak, Oliver, Burg, Dominic, Raftery, Mark J., Parkin, Don M., Trewhella, Jill, Cavicchioli, Ricardo

    Published in Protein engineering, design and selection (01-10-2010)
    “…The thermostability properties of TAA were investigated by chemically modifying carboxyl groups on the surface of the enzyme with AMEs. The TAAMOD exhibited a…”
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    Journal Article
  8. 8

    The RNA polymerase subunits E/F from the Antarctic archaeon Methanococcoides burtonii bind to specific species of mRNA by De Francisci, Davide, Campanaro, Stefano, Kornfeld, Geoff, Siddiqui, Khawar S., Williams, Timothy J., Ertan, Haluk, Treu, Laura, Pilak, Oliver, Lauro, Federico M., Harrop, Stephen J., Curmi, Paul M. G., Cavicchioli, Ricardo

    Published in Environmental microbiology (01-08-2011)
    “…Summary RNA polymerase in Archaea is composed of 11 or 12 subunits – 9 or 10 that form the core, and a heterodimer formed from subunits E and F that associates…”
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    Journal Article
  9. 9

    A chemically modified a-amylase with a molten-globule state has entropically driven enhanced thermal stability by Siddiqui, Khawar Sohail, Poljak, Anne, De Francisci, Davide, Guerriero, Gea, Pilak, Oliver, Burg, Dominic, Raftery, Mark J, Parkin, Don M, Trewhella, Jill, Cavicchioli, Ricardo

    Published in Protein engineering (01-10-2010)
    “…The thermostability properties of TAA were investigated by chemically modifying carboxyl groups on the surface of the enzyme with AMEs. The TAAMOD exhibited a…”
    Get full text
    Journal Article