Works matching DE "SULFOLOBUS acidocaldarius"
Results: 32
Sulfolobus acidocaldarius UDG Can Remove dU from the RNA Backbone: Insight into the Specific Recognition of Uracil Linked with Deoxyribose.
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- Genes, 2017, v. 8, n. 1, p. 38, doi. 10.3390/genes8010038
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SacPox from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius is a proficient lactonase.
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- BMC Research Notes, 2014, v. 7, n. 1, p. 1, doi. 10.1186/1756-0500-7-333
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INNOVATIVE BIOCATALYSTS AS TOOLS TO DETECT AND INACTIVATE NERVE AGENTS.
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- Military Medical Science Letters / Vojenské zdravotnické Listy, 2018, v. 87, p. 32
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Insights into the post‐translational modifications of archaeal Sis10b (Alba): lysine‐16 is methylated, not acetylated, and this does not regulate transcription or growth.
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- Molecular Microbiology, 2018, v. 109, n. 2, p. 192, doi. 10.1111/mmi.13973
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Arn S, a kinase involved in starvation-induced archaellum expression.
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- Molecular Microbiology, 2017, v. 103, n. 1, p. 181, doi. 10.1111/mmi.13550
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BarR, an Lrp-type transcription factor in S ulfolobus acidocaldarius, regulates an aminotransferase gene in a β-alanine responsive manner.
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- Molecular Microbiology, 2014, v. 92, n. 3, p. 625, doi. 10.1111/mmi.12583
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The archaellum: a rotating type IV pilus.
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- Molecular Microbiology, 2014, v. 91, n. 4, p. 716, doi. 10.1111/mmi.12486
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The one-component system ArnR: a membrane-bound activator of the crenarchaeal archaellum.
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- Molecular Microbiology, 2013, v. 88, n. 1, p. 125, doi. 10.1111/mmi.12173
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Regulation of archaella expression by the FHA and von Willebrand domain-containing proteins ArnA and ArnB in Sulfolobus acidocaldarius.
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- Molecular Microbiology, 2012, v. 86, n. 1, p. 24, doi. 10.1111/j.1365-2958.2012.08186.x
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Control of archaellation in Sulfolobus acidocaldarius: unravelling of the regulation of surface structure biosynthesis in Archaea begins.
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- Molecular Microbiology, 2012, v. 86, n. 1, p. 1, doi. 10.1111/j.1365-2958.2012.08191.x
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Four chromosome replication origins in the archaeon Pyrobaculum calidifontis.
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- Molecular Microbiology, 2012, v. 85, n. 5, p. 986, doi. 10.1111/j.1365-2958.2012.08155.x
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Towards Reassignment of the Methionine Codon AUG to Two Different Noncanonical Amino Acids in Bacterial Translation.
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- Croatica Chemica Acta, 2016, v. 89, n. 2, p. 243, doi. 10.5562/cca2915
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AglH, a thermophilic UDP- N-acetylglucosamine-1-phosphate:dolichyl phosphate GlcNAc-1-phosphotransferase initiating protein N-glycosylation pathway in Sulfolobus acidocaldarius, is capable of complementing the eukaryal Alg7.
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- Extremophiles, 2017, v. 21, n. 1, p. 121, doi. 10.1007/s00792-016-0890-2
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Characterization of two β-decarboxylating dehydrogenases from Sulfolobus acidocaldarius.
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- Extremophiles, 2016, v. 20, n. 6, p. 843, doi. 10.1007/s00792-016-0872-4
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Disruption of the gene encoding restriction endonuclease SuaI and development of a host-vector system for the thermoacidophilic archaeon Sulfolobus acidocaldarius.
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- Extremophiles, 2016, v. 20, n. 2, p. 139, doi. 10.1007/s00792-016-0807-0
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Membrane-bound amylopullulanase is essential for starch metabolism of Sulfolobus acidocaldarius DSM639.
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- Extremophiles, 2015, v. 19, n. 5, p. 909, doi. 10.1007/s00792-015-0766-x
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UDP-sulfoquinovose formation by Sulfolobus acidocaldarius.
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- Extremophiles, 2015, v. 19, n. 2, p. 451, doi. 10.1007/s00792-015-0730-9
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The saci_2123 gene of the hyperthermoacidophile Sulfolobus acidocaldarius encodes an ATP-binding cassette multidrug transporter.
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- Extremophiles, 2015, v. 19, n. 1, p. 101, doi. 10.1007/s00792-014-0688-z
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Dissection of key determinants of cleavage activity in signal peptidase III (SPaseIII) PibD.
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- Extremophiles, 2014, v. 18, n. 5, p. 905, doi. 10.1007/s00792-014-0675-4
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Deletion of cdvB paralogous genes of Sulfolobus acidocaldarius impairs cell division.
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- Extremophiles, 2014, v. 18, n. 2, p. 331, doi. 10.1007/s00792-013-0618-5
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How hyperthermophiles adapt to change their lives: DNA exchange in extreme conditions.
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- Extremophiles, 2013, v. 17, n. 4, p. 545, doi. 10.1007/s00792-013-0552-6
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ESCRT-III mediated cell division in Sulfolobus acidocaldarius - a reconstitution perspective.
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- Frontiers in Microbiology, 2014, v. 5, p. 1, doi. 10.3389/fmicb.2014.00257
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ESCRT-III mediated cell division in Sulfolobus acidocaldarius – A reconstitution perspective.
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- Frontiers in Microbiology, 2014, v. 5, p. 1, doi. 10.3389/fmicb.2014.00257
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Structured Populations of Sulfolobus acidocaldarius with Susceptibility to Mobile Genetic Elements.
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- Genome Biology & Evolution, 2017, v. 9, n. 6, p. 1699, doi. 10.1093/gbe/evx104
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Evolution of the Thermopsin Peptidase Family (A5).
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- PLoS ONE, 2013, v. 8, n. 11, p. 1, doi. 10.1371/journal.pone.0078998
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Alterations of the Transcriptome of <i>Sulfolobus acidocaldarius</i> by Exoribonuclease aCPSF2.
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- PLoS ONE, 2013, v. 8, n. 10, p. 1, doi. 10.1371/journal.pone.0076569
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Improved conversion of ginsenoside Rb to compound K by semi-rational design of Sulfolobus solfataricus β-glycosidase.
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- AMB Express, 2017, v. 7, n. 1, p. 1, doi. 10.1186/s13568-017-0487-x
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Chalcopyrite bioleaching in the presence of high chloride concentrations.
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- Journal of Chemical Technology & Biotechnology, 2019, v. 94, n. 7, p. 2333, doi. 10.1002/jctb.6028
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Purification, crystallization and preliminary X-ray crystallographic analysis of the flagellar accessory protein FlaH from the methanogenic archaeon Methanocaldococcus jannaschii.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2014, v. 70, n. 11, p. 1543, doi. 10.1107/S2053230X14019980
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Two trehalose-hydrolyzing enzymes from <italic>Crenarchaeon Sulfolobus acidocaldarius</italic> exhibit distinct activities and affinities toward trehalose.
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- Applied Microbiology & Biotechnology, 2018, v. 102, n. 10, p. 4445, doi. 10.1007/s00253-018-8915-7
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Biochemical and structural characterization of recombinant short-chain NAD(H)-dependent dehydrogenase/reductase from Sulfolobus acidocaldarius highly enantioselective on diaryl diketone benzil.
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- Applied Microbiology & Biotechnology, 2013, v. 97, n. 9, p. 3949, doi. 10.1007/s00253-012-4273-z
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Magnetic Au Nanoparticles on Archaeal S-Layer Ghosts as Templates.
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- Nanomaterials & Nanotechnology, 2011, v. 1, n. 2, p. 8
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