@article{Kraft2011, author = {Kraft, Tobias}, title = {?'100 a{\~n}os de recepc{\´i}on? el ensayo politico sobre la Isla de Cuba de Alexander von Humboldt en la recepci{\´o}n cubana entre 1826 y 1930}, isbn = {978-3-938944-54-7}, year = {2011}, language = {de} } @article{Riedel2011, author = {Riedel, Peter}, title = {Zwischen bisch{\"o}flicher Kurie und pr{\"a}monstratensischem Kapitel : zur Vergabe bisch{\"o}flicher {\"A}mter als Spiegel der Beziehungen zwischen Bischof und Domstift im sp{\"a}tmittelalterlichen Bistum Brandenburg}, isbn = {978-3-942411-36-3}, year = {2011}, language = {de} } @article{LindeckeScheffler2011, author = {Lindecke, Oliver and Scheffler, Ingo}, title = {Zur Ektoparasitenfauna der Flederm{\"a}use in Sachsen Anhalt : Ectoparasites of bats in Saxony-Anhalt}, issn = {0018-0637}, year = {2011}, abstract = {During the summer 2010 several mist nettings for the monitoring of bat species were performed in Saxony-Anhalt. Captured individuals were tested for ectoparasitic infestation. The aim was to update the fauna of ectoparasites of this state and to collect data on the distribution of individual species. Regarding this, results of previous surveys are summarised. In the present study nine out of thirteen bat species were found to be infested with a total of one flea species, one species of bat flies and eight species of mites. The infestation with fleas was below the expectations. Six spinturnicid mite species out of those occurring in Germany could be ascertained for Saxony-Anhalt. These are Spinturnix acuminatus (Koch, 1836), S. andegavinus (Kolenati, 1857), S. helvetiae Deunff, Keller \& Aellen, 1986, S. mystacinus (Kolenati, 1857), S. plecotinus (Koch, 1839) and S. puncata (Sundevall, 1833). Details about the infestation with parasites (abundances) of the respective bat species are presented. Further information on the biology of spinturnicid mites are given and infestation characteristics are compared with those of other surveys. Keywords: ectoparasites, bats, Chiroptera, gamasine mite, Acari, Spinturnix, Ischnopsyllidae, Nycteribiidae, Saxony-Anhalt, Germany}, language = {de} } @article{HeimannNeitmann2011, author = {Heimann, Heinz-Dieter and Neitmann, Klaus}, title = {Zur Einleitung : was Papst und Kaiser durch ihr Wort besch{\"u}tzen}, isbn = {978-3-9810642-8-5}, year = {2011}, language = {de} } @article{BankKashgar2011, author = {Bank, Roland and Kashgar, Maral}, title = {Zur Arbeit des Committee against Torture and other Cruel, Inhuman or Degrading Treatment or Punishment und des Subcommittee on Prevention of Torture}, isbn = {978-3-86956-104-2}, year = {2011}, language = {de} } @article{Stillmark2011, author = {Stillmark, Hans-Christian}, title = {Zu Kleists theatralischer Transformation der K{\"o}rper}, isbn = {978- 3-939888-93-2}, year = {2011}, abstract = {Der Beitrag untersucht Kleists Dramentexte vor allem im Hinblick auf den "Skandal" des Koerpers und versucht dafuer eine Erklaerung zu finden. Diese besteht zunaechst im Herausfall aus dem Paradigma des aesthetischem Koerpers als einem schoenen Koerper. Zum zweiten aber auch darin, das Kleist mit seinen literarischen Mitteln eine drastische Performation des Koerpers fuer das Buehnenstueck vornahm ohne dafuer eine theatralische Praxis zu haben. Der Einsatz des Koerpers als ein Zeichen im Buehnenspiel ist daher strategisch vom Autor Kleist zu einer Aussage performiert worden, die neben den Aussagen des sprachlichen Textes eine weitere koerpersprachliche Textur konstruiert.}, language = {de} } @article{LilieBaerKettneretal.2011, author = {Lilie, Hauke and Baer, Dorit and Kettner, Karina and Weininger, Ulrich and Balbach, Jochen and Naumann, Manfred and Mueller, Eva-Christina and Otto, Albrecht and Gast, Klaus and Golbik, Ralph and Kriegel, Thomas}, title = {Yeast hexokinase isoenzyme ScHxk2 stability of a two-domain protein with discontinuous domains}, series = {Protein engineering design \& selection}, volume = {24}, journal = {Protein engineering design \& selection}, number = {1-2}, publisher = {Oxford Univ. Press}, address = {Oxford}, issn = {1741-0126}, doi = {10.1093/protein/gzq098}, pages = {79 -- 87}, year = {2011}, abstract = {The hexokinase isoenzyme 2 of Saccharomyces cerevisiae (ScHxk2) represents an archetype of a two-domain protein with the active site located in a cleft between the two domains. Binding of the substrate glucose results in a rigid body movement of the two domains leading to a cleft closure of the active site. Both domains of this enzyme are composed of discontinuous peptide sequences. This structural feature is reflected in the stability and folding of the ScHxk2 protein. Structural transitions induced by urea treatment resulted in the population of a thermodynamically stable folding intermediate, which, however, does not correspond to a molecule with one domain folded and the other unfolded. As demonstrated by different spectroscopic techniques, both domains are structurally affected by the partial denaturation. The intermediate possesses only 40\% of the native secondary structural content and a substantial increase in the Stokes radius as judged by circular dichroism and dynamic light scattering analyses. One-dimensional H-1 NMR data prove that all tryptophan residues are in a non-native environment in the intermediate, indicating substantial changes in the tertiary structure. Still, the intermediate possesses quite a high stability for a transition intermediate of about Delta G = -22 kJ mol(-1).}, language = {en} } @article{LilieBaerKettneretal.2011, author = {Lilie, Hauke and B{\"a}r, Dorit and Kettner, Karina and Weininger, Ulrich and Balbach, Jochen and Naumann, Manfred and M{\"u}ller, Eva-Christina and Otto, Albrecht and Gast, Klaus and Golbik, Ralph}, title = {Yeast hexokinase isoenzyme ScHxk2 : stability of a two-domain protein with discontinuous domains}, issn = {0269-2139}, year = {2011}, abstract = {The hexokinase isoenzyme 2 of Saccharomyces cerevisiae (ScHxk2) represents an archetype of a two-domain protein with the active site located in a cleft between the two domains. Binding of the substrate glucose results in a rigid body movement of the two domains leading to a cleft closure of the active site. Both domains of this enzyme are composed of discontinuous peptide sequences. This structural feature is reflected in the stability and folding of the ScHxk2 protein. Structural transitions induced by urea treatment resulted in the population of a thermodynamically stable folding intermediate, which, however, does not correspond to a molecule with one domain folded and the other unfolded. As demonstrated by different spectroscopic techniques, both domains are structurally affected by the partial denaturation. The intermediate possesses only 40\% of the native secondary structural content and a substantial increase in the Stokes radius as judged by circular dichroism and dynamic light scattering analyses. One-dimensional 1H NMR data prove that all tryptophan residues are in a non-native environment in the intermediate, indicating substantial changes in the tertiary structure. Still, the intermediate possesses quite a high stability for a transition intermediate of about ;G = ;22 kJ mol;1.}, language = {en} } @article{RedelbergerSedukGenestetal.2011, author = {Redelberger, David and Seduk, Farida and Genest, Olivier and Mejean, Vincent and Leimk{\"u}hler, Silke and Iobbi-Nivol, Chantal}, title = {YcdY Protein of Escherichia coli, an Atypical Member of the TorD Chaperone Family}, series = {Journal of bacteriology}, volume = {193}, journal = {Journal of bacteriology}, number = {23}, publisher = {American Society for Microbiology}, address = {Washington}, issn = {0021-9193}, doi = {10.1128/JB.05927-11}, pages = {6512 -- 6516}, year = {2011}, abstract = {The TorD family of specific chaperones is divided into four subfamilies dedicated to molybdoenzyme biogenesis and a fifth one, exemplified by YcdY of Escherichia coli, for which no defined partner has been identified so far. We propose that YcdY is the chaperone of YcdX, a zinc protein involved in the swarming motility process of E. coli, since YcdY interacts with YcdX and increases its activity in vitro.}, language = {en} } @article{KalimuthuLeimkuehlerBernhardt2011, author = {Kalimuthu, Palraj and Leimk{\"u}hler, Silke and Bernhardt, Paul V.}, title = {Xanthine dehydrogenase electrocatalysis autocatalysis and novel activity}, series = {The journal of physical chemistry : B, Condensed matter, materials, surfaces, interfaces \& biophysical chemistry}, volume = {115}, journal = {The journal of physical chemistry : B, Condensed matter, materials, surfaces, interfaces \& biophysical chemistry}, number = {11}, publisher = {American Chemical Society}, address = {Washington}, issn = {1520-6106}, doi = {10.1021/jp111809f}, pages = {2655 -- 2662}, year = {2011}, abstract = {The enzyme xanthine dehydrogenase (XDH) from the purple photosynthetic bacterium Rhodobacter capsulatus catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid as part of purine metabolism. The native electron acceptor is NAD(+) but herein we show that uric acid in its 2-electron oxidized form is able to act as an artificial electron acceptor from XDH in an electrochemically driven catalytic system. Hypoxanthine oxidation is also observed with the novel production of uric acid in a series of two consecutive 2-electron oxidation reactions via xanthine. XDH exhibits native activity in terms of its pH optimum and inhibition by allopurinol.}, language = {en} }