@phdthesis{Mueller2012,
  author    = {M{\"u}ller, J{\"u}rgen J.},
  title     = {A real-time in-memory discovery service},
  address   = {Potsdam},
  pages     = {XXV, 172 S.},
  year      = {2012},
  language  = {en}
}
@article{MuellerBarbirzHeinleetal.2008,
  author    = {M{\"u}ller, J{\"u}rgen J. and Barbirz, Stefanie and Heinle, Karolin and Freiberg, Alexander and Seckler, Robert and Heinemann, Udo},
  title     = {An intersubunit active site between supercoiled parallel beta helices in the trimeric tailspike endorhamnosidase of Shigella flexneri phage Sf6},
  doi       = {10.1016/j.str.2008.01.019},
  year      = {2008},
  abstract  = {Sf6 belongs to the Podoviridae family of temperate bacteriophages that infect gram-negative bacteria by insertion of their double-stranded DNA. They attach to their hosts specifically via their tailspike proteins. The 1.25 {\AA} crystal structure of Shigella phage Sf6 tailspike protein (Sf6 TSP) reveals a conserved architecture with a central, right-handed ; helix. In the trimer of Sf6 TSP, the parallel ; helices form a left-handed, coiled;; coil with a pitch of 340 {\AA}. The C-terminal domain consists of a ; sandwich reminiscent of viral capsid proteins. Further crystallographic and biochemical analyses show a Shigella cell wall O-antigen fragment to bind to an endorhamnosidase active site located between two ;-helix subunits each anchoring one catalytic carboxylate. The functionally and structurally related bacteriophage, P22 TSP, lacks sequence identity with Sf6 TSP and has its active sites on single subunits. Sf6 TSP may serve as an example for the evolution of different host specificities on a similar general architecture.},
  language  = {en}
}
@article{KleinDarvinMeinkeetal.2013,
  author    = {Klein, Julia and Darvin, Maxim E. and Meinke, Martina C. and Schweigert, Florian J. and M{\"u}ller, Kerstin E. and Lademann, J{\"u}rgen},
  title     = {Analyses of the correlation between dermal and blood carotenoids in female cattle by optical methods},
  series = {Journal of biomedical optics},
  volume    = {18},
  journal   = {Journal of biomedical optics},
  number    = {6},
  publisher = {SPIE},
  address   = {Bellingham},
  issn      = {1083-3668},
  doi       = {10.1117/1.JBO.18.6.061219},
  pages     = {6},
  year      = {2013},
  abstract  = {Herd health programs for the maintenance of welfare and productivity in cattle need efficient tools for monitoring the health of individual animals. Recent reports demonstrate that the oxidative status is related to various stress conditions in dairy cows. Biomarkers, among other carotenoids, could serve as indicators of stress originating from the environment (e.g., heat stress or sun radiation) or from the animal itself (e.g., disease). To date, only invasive in vitro tests are available to assess the oxidative status in cattle. The present study compares the results of optical noninvasive in vivo measurements of dermal carotenoids in cattle udder skin using an LED-based miniaturized spectroscopic system (MSS) with those obtained by photometric analysis of beta carotene in whole blood samples using a portable device. Correlations between the concentrations of dermal and blood carotenoids were calculated under consideration of the nutritional status of the animals. Significant correlation (R = 0.86) was found for cattle with a moderate to obese body condition. Thus, the blood and skin concentrations of the marker substance beta carotene are comparable under stable stress conditions of the cattle. This demonstrates that the MSS is suitable for noninvasive assessment of dermal carotenoid concentrations in cattle.},
  language  = {en}
}
@article{SeulMuellerAndresetal.2014,
  author    = {Seul, Anait and M{\"u}ller, J{\"u}rgen J. and Andres, Dorothee and Stettner, Eva and Heinemann, Udo and Seckler, Robert},
  title     = {Bacteriophage P22 tailspike: structure of the complete protein and function of the interdomain linker},
  series = {Acta crystallographica : Section D, Biological crystallography},
  volume    = {70},
  journal   = {Acta crystallographica : Section D, Biological crystallography},
  publisher = {Wiley-Blackwell},
  address   = {Hoboken},
  issn      = {1399-0047},
  doi       = {10.1107/S1399004714002685},
  pages     = {1336 -- 1345},
  year      = {2014},
  abstract  = {Attachment of phages to host cells, followed by phage DNA ejection, represents the first stage of viral infection of bacteria. Salmonella phage P22 has been extensively studied, serving as an experimental model for bacterial infection by phages. P22 engages bacteria by binding to the sugar moiety of lipopolysaccharides using the viral tailspike protein for attachment. While the structures of the N-terminal particle-binding domain and the major receptor-binding domain of the tailspike have been analyzed individually, the three-dimensional organization of the intact protein, including the highly conserved linker region between the two domains, remained unknown. A single amino-acid exchange in the linker sequence made it possible to crystallize the full-length protein. Two crystal structures of the linker region are presented: one attached to the N-terminal domain and the other present within the complete tailspike protein. Both retain their biological function, but the mutated full-length tailspike displays a retarded folding pathway. Fitting of the full-length tailspike into a published cryo-electron microscopy map of the P22 virion requires an elastic distortion of the crystal structure. The conservation of the linker suggests a role in signal transmission from the distal tip of the molecule to the phage head, eventually leading to DNA ejection.},
  language  = {en}
}
@article{DamaschunDamaschunGastetal.1993,
  author    = {Damaschun, Gregor and Damaschun, Hilde and Gast, Klaus and Misselwitz, Rolf and M{\"u}ller, J{\"u}rgen J. and Pfeil, Wolfgang and Zirwer, Dietrich},
  title     = {Cold denaturation-induced conformational changes in phosphoglycerate kinase from yeast},
  year      = {1993},
  language  = {en}
}
@article{BarbirzMuellerUetrechtetal.2008,
  author    = {Barbirz, Stefanie and M{\"u}ller, J{\"u}rgen J. and Uetrecht, Charlotte and Clark, Alvin J. and Heinemann, Udo and Seckler, Robert},
  title     = {Crystal structure of Escherichia coli phage HK620 tailspike : podoviral tailspike endoglycosidase modules are evolutionarily related},
  issn      = {0950-382X},
  year      = {2008},
  abstract  = {Bacteriophage HK620 infects Escherichia coli H and is closely related to Shigella phage Sf6 and Salmonella phage P22. All three Podoviridae recognize and cleave their respective host cell receptor polysaccharide by homotrimeric tailspike proteins. The three proteins exhibit high sequence identity in the 110 residues of their N-terminal particle- binding domains, but no apparent sequence similarity in their major, receptor-binding parts. We have biochemically characterized the receptor-binding part of HK620 tailspike and determined its crystal structure to 1.38 {\AA} resolution. Its major domain is a right-handed parallel ;-helix, as in Sf6 and P22 tailspikes. HK620 tailspike has endo-N- acetylglucosaminidase activity and produces hexasaccharides of an O18A1-type O-antigen. As indicated by the structure of a hexasaccharide complex determined at 1.6 {\AA} resolution, the endoglycosidase-active sites are located intramolecularly, as in P22, and not between subunits, as in Sf6 tailspike. In contrast, the extreme C-terminal domain of HK620 tailspike forms a ;-sandwich, as in Sf6 and unlike P22 tailspike. Despite the different folds, structure-based sequence alignments of the C-termini reveal motifs conserved between the three proteins. We propose that the tailspike genes of P22, Sf6 and HK620 have a common precursor and are not mosaics of unrelated gene fragments.},
  language  = {en}
}
@inproceedings{KurbelNowakAzodietal.2015,
  author    = {Kurbel, Karl and Nowak, Dawid and Azodi, Amir and Jaeger, David and Meinel, Christoph and Cheng, Feng and Sapegin, Andrey and Gawron, Marian and Morelli, Frank and Stahl, Lukas and Kerl, Stefan and Janz, Mariska and Hadaya, Abdulmasih and Ivanov, Ivaylo and Wiese, Lena and Neves, Mariana and Schapranow, Matthieu-Patrick and F{\"a}hnrich, Cindy and Feinbube, Frank and Eberhardt, Felix and Hagen, Wieland and Plauth, Max and Herscheid, Lena and Polze, Andreas and Barkowsky, Matthias and Dinger, Henriette and Faber, Lukas and Montenegro, Felix and Czach{\´o}rski, Tadeusz and Nycz, Monika and Nycz, Tomasz and Baader, Galina and Besner, Veronika and Hecht, Sonja and Schermann, Michael and Krcmar, Helmut and Wiradarma, Timur Pratama and Hentschel, Christian and Sack, Harald and Abramowicz, Witold and Sokolowska, Wioletta and Hossa, Tymoteusz and Opalka, Jakub and Fabisz, Karol and Kubaczyk, Mateusz and Cmil, Milena and Meng, Tianhui and Dadashnia, Sharam and Niesen, Tim and Fettke, Peter and Loos, Peter and Perscheid, Cindy and Schwarz, Christian and Schmidt, Christopher and Scholz, Matthias and Bock, Nikolai and Piller, Gunther and B{\"o}hm, Klaus and Norkus, Oliver and Clark, Brian and Friedrich, Bj{\"o}rn and Izadpanah, Babak and Merkel, Florian and Schweer, Ilias and Zimak, Alexander and Sauer, J{\"u}rgen and Fabian, Benjamin and Tilch, Georg and M{\"u}ller, David and Pl{\"o}ger, Sabrina and Friedrich, Christoph M. and Engels, Christoph and Amirkhanyan, Aragats and van der Walt, Est{\´e}e and Eloff, J. H. P. and Scheuermann, Bernd and Weinknecht, Elisa},
  title     = {HPI Future SOC Lab},
  editor    = {Meinel, Christoph and Polze, Andreas and Oswald, Gerhard and Strotmann, Rolf and Seibold, Ulrich and Schulzki, Bernhard},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-102516},
  pages     = {iii, 154},
  year      = {2015},
  abstract  = {Das Future SOC Lab am HPI ist eine Kooperation des Hasso-Plattner-Instituts mit verschiedenen Industriepartnern. Seine Aufgabe ist die Erm{\"o}glichung und F{\"o}rderung des Austausches zwischen Forschungsgemeinschaft und Industrie. Am Lab wird interessierten Wissenschaftlern eine Infrastruktur von neuester Hard- und Software kostenfrei f{\"u}r Forschungszwecke zur Verf{\"u}gung gestellt. Dazu z{\"a}hlen teilweise noch nicht am Markt verf{\"u}gbare Technologien, die im normalen Hochschulbereich in der Regel nicht zu finanzieren w{\"a}ren, bspw. Server mit bis zu 64 Cores und 2 TB Hauptspeicher. Diese Angebote richten sich insbesondere an Wissenschaftler in den Gebieten Informatik und Wirtschaftsinformatik. Einige der Schwerpunkte sind Cloud Computing, Parallelisierung und In-Memory Technologien. In diesem Technischen Bericht werden die Ergebnisse der Forschungsprojekte des Jahres 2015 vorgestellt. Ausgew{\"a}hlte Projekte stellten ihre Ergebnisse am 15. April 2015 und 4. November 2015 im Rahmen der Future SOC Lab Tag Veranstaltungen vor.},
  language  = {en}
}
@article{BroekerGohlkeMuelleretal.2013,
  author    = {Br{\"o}ker, Nina Kristin and Gohlke, Ulrich and M{\"u}ller, J{\"u}rgen J. and Uetrecht, Charlotte and Heinemann, Udo and Seckler, Robert and Barbirz, Stefanie},
  title     = {Single amino acid exchange in bacteriophage HK620 tailspike protein results in thousand-fold increase of its oligosaccharide affinity},
  series = {Glycobiology},
  volume    = {23},
  journal   = {Glycobiology},
  number    = {1},
  publisher = {Oxford Univ. Press},
  address   = {Cary},
  issn      = {0959-6658},
  doi       = {10.1093/glycob/cws126},
  pages     = {59 -- 68},
  year      = {2013},
  abstract  = {Bacteriophage HK620 recognizes and cleaves the O-antigen polysaccharide of Escherichia coli serogroup O18A1 with its tailspike protein (TSP). HK620TSP binds hexasaccharide fragments with low affinity, but single amino acid exchanges generated a set of high-affinity mutants with submicromolar dissociation constants. Isothermal titration calorimetry showed that only small amounts of heat were released upon complex formation via a large number of direct and solvent-mediated hydrogen bonds between carbohydrate and protein. At room temperature, association was both enthalpy- and entropy-driven emphasizing major solvent rearrangements upon complex formation. Crystal structure analysis showed identical protein and sugar conformers in the TSP complexes regardless of their hexasaccharide affinity. Only in one case, a TSP mutant bound a different hexasaccharide conformer. The extended sugar binding site could be dissected in two regions: first, a hydrophobic pocket at the reducing end with minor affinity contributions. Access to this site could be blocked by a single aspartate to asparagine exchange without major loss in hexasaccharide affinity. Second, a region where the specific exchange of glutamate for glutamine created a site for an additional water molecule. Side-chain rearrangements upon sugar binding led to desolvation and additional hydrogen bonding which define this region of the binding site as the high-affinity scaffold.},
  language  = {en}
}