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The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.
ISME J. 2009 Sep;3(9):1012-35. doi: 10.1038/ismej.2009.45. Epub 2009 Apr 30.
ISME J. 2009.
PMID: 19404327
Free article.
Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii. Part I: the effect of growth temperature.
Williams TJ, Burg DW, Raftery MJ, Poljak A, Guilhaus M, Pilak O, Cavicchioli R.
Williams TJ, et al. Among authors: pilak o.
J Proteome Res. 2010 Feb 5;9(2):640-52. doi: 10.1021/pr900509n.
J Proteome Res. 2010.
PMID: 20039705
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The RNA polymerase subunits E/F from the Antarctic archaeon Methanococcoides burtonii bind to specific species of mRNA.
De Francisci D, Campanaro S, Kornfeld G, Siddiqui KS, Williams TJ, Ertan H, Treu L, Pilak O, Lauro FM, Harrop SJ, Curmi PM, Cavicchioli R.
De Francisci D, et al. Among authors: pilak o.
Environ Microbiol. 2011 Aug;13(8):2039-55. doi: 10.1111/j.1462-2920.2010.02385.x. Epub 2010 Nov 25.
Environ Microbiol. 2011.
PMID: 21108724
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Chaperonins from an Antarctic archaeon are predominantly monomeric: crystal structure of an open state monomer.
Pilak O, Harrop SJ, Siddiqui KS, Chong K, De Francisci D, Burg D, Williams TJ, Cavicchioli R, Curmi PM.
Pilak O, et al.
Environ Microbiol. 2011 Aug;13(8):2232-49. doi: 10.1111/j.1462-2920.2011.02477.x. Epub 2011 Apr 7.
Environ Microbiol. 2011.
PMID: 21477108
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A chemically modified alpha-amylase with a molten-globule state has entropically driven enhanced thermal stability.
Siddiqui KS, Poljak A, De Francisci D, Guerriero G, Pilak O, Burg D, Raftery MJ, Parkin DM, Trewhella J, Cavicchioli R.
Siddiqui KS, et al. Among authors: pilak o.
Protein Eng Des Sel. 2010 Oct;23(10):769-80. doi: 10.1093/protein/gzq051. Epub 2010 Aug 9.
Protein Eng Des Sel. 2010.
PMID: 20696745
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The crystal structure of the apoenzyme of the iron-sulphur cluster-free hydrogenase.
Pilak O, Mamat B, Vogt S, Hagemeier CH, Thauer RK, Shima S, Vonrhein C, Warkentin E, Ermler U.
Pilak O, et al.
J Mol Biol. 2006 May 5;358(3):798-809. doi: 10.1016/j.jmb.2006.02.035. Epub 2006 Mar 2.
J Mol Biol. 2006.
PMID: 16540118
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The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site.
Shima S, Pilak O, Vogt S, Schick M, Stagni MS, Meyer-Klaucke W, Warkentin E, Thauer RK, Ermler U.
Shima S, et al. Among authors: pilak o.
Science. 2008 Jul 25;321(5888):572-5. doi: 10.1126/science.1158978.
Science. 2008.
PMID: 18653896
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The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex.
Hiromoto T, Ataka K, Pilak O, Vogt S, Stagni MS, Meyer-Klaucke W, Warkentin E, Thauer RK, Shima S, Ermler U.
Hiromoto T, et al. Among authors: pilak o.
FEBS Lett. 2009 Feb 4;583(3):585-90. doi: 10.1016/j.febslet.2009.01.017. Epub 2009 Jan 20.
FEBS Lett. 2009.
PMID: 19162018
Free article.
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