Pohl, Corinna

[["dc.bibliographiccitation.journal","Annals of the Rheumatic Diseases"],["dc.bibliographiccitation.volume","69"],["dc.contributor.author","Sehnert, B."],["dc.contributor.author","Burkhardt, Harald"],["dc.contributor.author","Nimmerjahn, F."],["dc.contributor.author","Pohle, S."],["dc.contributor.author","Wessels, Johannes Theodor"],["dc.contributor.author","Vestweber, Dietmar"],["dc.contributor.author","Zwerina, Jochen"],["dc.contributor.author","Schett, Georg"],["dc.contributor.author","Duebel, S."],["dc.contributor.author","Voll, R."],["dc.date.accessioned","2018-11-07T08:46:00Z"],["dc.date.available","2018-11-07T08:46:00Z"],["dc.date.issued","2010"],["dc.identifier.doi","10.1136/ard.2010.129635e"],["dc.identifier.isi","000275376600114"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/20585"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","B M J Publishing Group"],["dc.publisher.place","London"],["dc.relation.conference","30th European Workshop for Rheumatology Research"],["dc.relation.eventlocation","Bamberg, GERMANY"],["dc.title","A Tissue-Specific Nf-Kappa B Inhibitor Ameliorates Inflammatory Joint Diseases"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","091112"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Applied Physics Letters"],["dc.bibliographiccitation.volume","102"],["dc.contributor.author","Joly, P."],["dc.contributor.author","Petrarca, M."],["dc.contributor.author","Vogel, A."],["dc.contributor.author","Pohl, T."],["dc.contributor.author","Nagy, T."],["dc.contributor.author","Jusforgues, Q."],["dc.contributor.author","Simon, P."],["dc.contributor.author","Kasparian, J."],["dc.contributor.author","Weber, K."],["dc.contributor.author","Wolf, J.-P."],["dc.date.accessioned","2018-11-07T09:27:10Z"],["dc.date.available","2018-11-07T09:27:10Z"],["dc.date.issued","2013"],["dc.description.abstract","We compare laser-induced condensation by UV laser pulses of femtosecond, sub-picosecond, and nanosecond duration between each other, as well as with respect to near-infrared (NIR) (800 nm) ultrashort laser pulses. Particle nucleation by UV pulses is so efficient that their growth beyond several hundreds of nm is limited by the local concentration of water vapour molecules. Furthermore, we evidence a dual mechanism: While condensation induced by ultrashort UV pulses rely on nitrogen photo-oxidative chemistry like in the NIR, nanosecond laser-induced condensation occurs without NO2 production, evidencing the domination of a mechanism distinct from that previously identified in the femtosecond regime. (C) 2013 American Institute of Physics. [http://dx.doi.org/10.1063/1.4794416]"],["dc.description.sponsorship","European Research Council"],["dc.identifier.doi","10.1063/1.4794416"],["dc.identifier.isi","000316085200012"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/30469"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Inst Physics"],["dc.relation.issn","0003-6951"],["dc.title","Laser-induced condensation by ultrashort laser pulses at 248 nm"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","12"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Infection"],["dc.bibliographiccitation.lastpage","21"],["dc.bibliographiccitation.volume","50"],["dc.contributor.author","Schmidt-Ott, Ruprecht"],["dc.contributor.author","Pohl, S."],["dc.contributor.author","Burghard, S."],["dc.contributor.author","Weig, Michael S."],["dc.contributor.author","Gross, U."],["dc.date.accessioned","2018-11-07T08:41:56Z"],["dc.date.available","2018-11-07T08:41:56Z"],["dc.date.issued","2005"],["dc.description.abstract","Objectives. Enterocyte invasion of Campylobacter jejuni 81-176 has been reported to depend upon the virulence ptasmid pVir. The objective of this study was to determine the prevalence of pVir in clinical C. jejuni isolates, to investigate DNA homologies between C. jejuni plasmids and the significance of plasmids for C. jejuni invasiveness. Methods. DNA homologies between C. jejuni plasmids were studied by southern blot hybridization. C. jejuni invasion into human intestinal Caco-2 cells was assessed in a gentamicin exclusion assay. Results. Twenty-nine percent of C. jejuni isolated from patients with Moody or watery diarrhoea harboured plasmids of various sizes. One plasmid (7%) was a pVir homologue whereas, the majority of the plasmids (53%) belonged to a subgroup distinct from pVir. The plasmids of this novel subgroup share extensive DNA sequence homology with each other, including homologues to so-called invasion-promoting genes. However, conjugative transfer of these plasmids clearly did not increase invasiveness of plasmidless recipient C. jejuni strains. Conclusion. This study indicates that only a small proportion of C. jejuni strains carry the virulence factor pVir and that at least one other distinctive group of plasmids in C. jejuni exists, which does not seem to be associated with invasiveness. (C) 2004 The British Infection Society. Published by Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.jinf.2004.02.013"],["dc.identifier.isi","000226327200003"],["dc.identifier.pmid","15603835"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19580"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","W B Saunders Co Ltd"],["dc.relation.issn","0163-4453"],["dc.title","Identification and characterization of a major subgroup of conjugative Campylobacter jejuni plasmids"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3701"],["dc.bibliographiccitation.issue","21"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","3709"],["dc.bibliographiccitation.volume","29"],["dc.contributor.author","Wohlgemuth, Ingo"],["dc.contributor.author","Pohl, Corinna"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2017-09-07T11:45:13Z"],["dc.date.available","2017-09-07T11:45:13Z"],["dc.date.issued","2010"],["dc.description.abstract","The speed and accuracy of protein synthesis are fundamental parameters for understanding the fitness of living cells, the quality control of translation, and the evolution of ribosomes. In this study, we analyse the speed and accuracy of the decoding step under conditions reproducing the high speed of translation in vivo. We show that error frequency is close to 10(-3), consistent with the values measured in vivo. Selectivity is predominantly due to the differences in k(cat) values for cognate and near-cognate reactions, whereas the intrinsic affinity differences are not used for tRNA discrimination. Thus, the ribosome seems to be optimized towards high speed of translation at the cost of fidelity. Competition with near-and non-cognate ternary complexes reduces the rate of GTP hydrolysis in the cognate ternary complex, but does not appreciably affect the rate-limiting tRNA accommodation step. The GTP hydrolysis step is crucial for the optimization of both the speed and accuracy, which explains the necessity for the trade-off between the two fundamental parameters of translation. The EMBO Journal (2010) 29, 3701-3709. doi:10.1038/emboj.2010.229; Published online 14 September 2010"],["dc.identifier.doi","10.1038/emboj.2010.229"],["dc.identifier.gro","3142832"],["dc.identifier.isi","000285386700010"],["dc.identifier.pmid","20842102"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/279"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0261-4189"],["dc.title","Optimization of speed and accuracy of decoding in translation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Journal of Inherited Metabolic Disease"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Pohl, S."],["dc.contributor.author","Tiede, Stephan"],["dc.contributor.author","Luebke, Torben"],["dc.contributor.author","Grabinski, N."],["dc.contributor.author","Storch, S."],["dc.contributor.author","Braulke, Thomas"],["dc.date.accessioned","2018-11-07T11:00:11Z"],["dc.date.available","2018-11-07T11:00:11Z"],["dc.date.issued","2007"],["dc.format.extent","101"],["dc.identifier.isi","000248860000403"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/50872"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Dordrecht"],["dc.relation.issn","0141-8955"],["dc.title","Molecular analysis of the GlcNac-1-phosphotransferase"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2661"],["dc.bibliographiccitation.journal","Brain"],["dc.bibliographiccitation.lastpage","2675"],["dc.bibliographiccitation.volume","135"],["dc.contributor.author","Kollmann, Katrin"],["dc.contributor.author","Damme, Markus"],["dc.contributor.author","Markmann, S."],["dc.contributor.author","Morelle, Willy"],["dc.contributor.author","Schweizer, M."],["dc.contributor.author","Hermans-Borgmeyer, Irm"],["dc.contributor.author","Roechert, A. K."],["dc.contributor.author","Pohl, S."],["dc.contributor.author","Luebke, Torben"],["dc.contributor.author","Michalski, J-C"],["dc.contributor.author","Kakela, R."],["dc.contributor.author","Walkley, Steven U."],["dc.contributor.author","Braulke, Thomas"],["dc.date.accessioned","2018-11-07T09:06:22Z"],["dc.date.available","2018-11-07T09:06:22Z"],["dc.date.issued","2012"],["dc.description.abstract","Mucolipidosis II is a neurometabolic lysosomal trafficking disorder of infancy caused by loss of mannose 6-phosphate targeting signals on lysosomal proteins, leading to lysosomal dysfunction and accumulation of non-degraded material. However, the identity of storage material and mechanisms of neurodegeneration in mucolipidosis II are unknown. We have generated 'knock-in' mice with a common mucolipidosis II patient mutation that show growth retardation, progressive brain atrophy, skeletal abnormalities, elevated lysosomal enzyme activities in serum, lysosomal storage in fibroblasts and brain and premature death, closely mimicking the mucolipidosis II disease in humans. The examination of affected mouse brains at different ages by immunohistochemistry, ultrastructural analysis, immunoblotting and mass spectrometric analyses of glycans and anionic lipids revealed that the expression and proteolytic processing of distinct lysosomal proteins such as alpha-L-fucosidase, beta-hexosaminidase, alpha-mannosidase or Niemann-Pick C2 protein are more significantly impacted by the loss of mannose 6-phosphate residues than enzymes reaching lysosomes independently of this targeting mechanism. As a consequence, fucosylated N-glycans, GM2 and GM3 gangliosides, cholesterol and bis(monoacylglycero) phosphate accumulate progressively in the brain of mucolipidosis II mice. Prominent astrogliosis and the accumulation of organelles and storage material in focally swollen axons were observed in the cerebellum and were accompanied by a loss of Purkinje cells. Moreover, an increased neuronal level of the microtubule-associated protein 1 light chain 3 and the formation of p62-positive neuronal aggregates indicate an impairment of constitutive autophagy in the mucolipidosis II brain. Our findings demonstrate the essential role of mannose 6-phosphate for selected lysosomal proteins to maintain the capability for degradation of sequestered components in lysosomes and autopha-golysosomes and prevent neurodegeneration. These lysosomal proteins might be a potential target for a valid therapeutic approach for mucolipidosis II disease."],["dc.identifier.doi","10.1093/brain/aws209"],["dc.identifier.isi","000308873600009"],["dc.identifier.pmid","22961545"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25540"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","0006-8950"],["dc.title","Lysosomal dysfunction causes neurodegeneration in mucolipidosis II 'knock-in' mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2979"],["dc.bibliographiccitation.journal","Philosophical Transactions of the Royal Society B: Biological Sciences"],["dc.bibliographiccitation.lastpage","2986"],["dc.contributor.author","Wohlgemuth, Ingo"],["dc.contributor.author","Pohl, Corinna"],["dc.contributor.author","Mittelstaet, Joerg"],["dc.contributor.author","Konevega, Andrey L."],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2018-01-29T13:36:26Z"],["dc.date.available","2018-01-29T13:36:26Z"],["dc.date.issued","2011"],["dc.identifier.doi","10.1098/rstb.2011.0138"],["dc.identifier.eissn","1471-2970"],["dc.identifier.pmid","21930591"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11885"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.title","Evolutionary optimization of speed and accuracy of decoding on the ribosome"],["dc.type","review"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","International Journal of Medical Microbiology"],["dc.bibliographiccitation.volume","296"],["dc.contributor.author","Dasti, Javid Iqbal"],["dc.contributor.author","Schmidt-Ott, Ruprecht"],["dc.contributor.author","Pohl, S."],["dc.contributor.author","Lugert, Raimond"],["dc.contributor.author","Weig, Michael S."],["dc.contributor.author","Grob, U."],["dc.date.accessioned","2018-11-07T09:19:33Z"],["dc.date.available","2018-11-07T09:19:33Z"],["dc.date.issued","2006"],["dc.format.extent","94"],["dc.identifier.isi","000241442600123"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28669"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Gmbh, Urban & Fischer Verlag"],["dc.publisher.place","Jena"],["dc.relation.conference","58th Annual Conference of the German-Society-of-Hygiene-and-Microbiology"],["dc.relation.eventlocation","Wurzburg, GERMANY"],["dc.relation.issn","1438-4221"],["dc.title","Campylobacter coli: Antimicrobial resistance and role of plasmid encoded tet(O) gene in tetracycline resistant clinical isolates."],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","14418"],["dc.bibliographiccitation.issue","40"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","14423"],["dc.bibliographiccitation.volume","111"],["dc.contributor.author","Maracci, Cristina"],["dc.contributor.author","Peske, Frank"],["dc.contributor.author","Dannies, Ev"],["dc.contributor.author","Pohl, Corinna"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2017-09-07T11:45:27Z"],["dc.date.available","2017-09-07T11:45:27Z"],["dc.date.issued","2014"],["dc.description.abstract","GTP hydrolysis by elongation factor Tu (EF-Tu), a translational GTPase that delivers aminoacyl-tRNAs to the ribosome, plays a crucial role in decoding and translational fidelity. The basic reaction mechanism and the way the ribosome contributes to catalysis are a matter of debate. Here we use mutational analysis in combination with measurements of rate/pH profiles, kinetic solvent isotope effects, and ion dependence of GTP hydrolysis by EF-Tu off and on the ribosome to dissect the reaction mechanism. Our data suggest that-contrary to current models-the reaction in free EF-Tu follows a pathway that does not involve the critical residue H84 in the switch II region. Binding to the ribosome without a cognate codon in the A site has little effect on the GTPase mechanism. In contrast, upon cognate codon recognition, the ribosome induces a rearrangement of EF-Tu that renders GTP hydrolysis sensitive to mutations of Asp21 and His84 and insensitive to K+ ions. We suggest that Asp21 and His84 provide a network of interactions that stabilize the positions of the gamma-phosphate and the nucleophilic water, respectively, and thus play an indirect catalytic role in the GTPase mechanism on the ribosome."],["dc.identifier.doi","10.1073/pnas.1412676111"],["dc.identifier.gro","3142034"],["dc.identifier.isi","000342633900039"],["dc.identifier.pmid","25246550"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3812"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [FOR 1805]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0027-8424"],["dc.title","Ribosome-induced tuning of GTP hydrolysis by a translational GTPase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e29525"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","PLOS ONE"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Tzivelekidis, Tina"],["dc.contributor.author","Jank, Thomas"],["dc.contributor.author","Pohl, Corinna"],["dc.contributor.author","Schlosser, Andreas"],["dc.contributor.author","Rospert, Sabine"],["dc.contributor.author","Knudsen, Charlotte R."],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Belyi, Yury"],["dc.contributor.author","Aktories, Klaus"],["dc.contributor.editor","Kwaik, Yousef Abu"],["dc.date.accessioned","2018-01-29T13:06:01Z"],["dc.date.available","2018-01-29T13:06:01Z"],["dc.date.issued","2011"],["dc.description.abstract","Legionella pneumophila, which is the causative organism of Legionnaireś disease, translocates numerous effector proteins into the host cell cytosol by a type IV secretion system during infection. Among the most potent effector proteins of Legionella are glucosyltransferases (lgt's), which selectively modify eukaryotic elongation factor (eEF) 1A at Ser-53 in the GTP binding domain. Glucosylation results in inhibition of protein synthesis. Here we show that in vitro glucosylation of yeast and mouse eEF1A by Lgt3 in the presence of the factors Phe-tRNA(Phe) and GTP was enhanced 150 and 590-fold, respectively. The glucosylation of eEF1A catalyzed by Lgt1 and 2 was increased about 70-fold. By comparison of uncharged tRNA with two distinct aminoacyl-tRNAs (His-tRNA(His) and Phe-tRNA(Phe)) we could show that aminoacylation is crucial for Lgt-catalyzed glucosylation. Aminoacyl-tRNA had no effect on the enzymatic properties of lgt's and did not enhance the glucosylation rate of eEF1A truncation mutants, consisting of the GTPase domain only or of a 5 kDa peptide covering Ser-53 of eEF1A. Furthermore, binding of aminoacyl-tRNA to eEF1A was not altered by glucosylation. Taken together, our data suggest that the ternary complex, consisting of eEF1A, aminoacyl-tRNA and GTP, is the bona fide substrate for lgt's."],["dc.identifier.doi","10.1371/journal.pone.0029525"],["dc.identifier.pmid","22216304"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11884"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.relation.eissn","1932-6203"],["dc.title","Aminoacyl-tRNA-charged eukaryotic elongation factor 1A is the bona fide substrate for Legionella pneumophila effector glucosyltransferases"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]