@article{FuhrmannSeehaferValorietal.2011,
  author    = {Fuhrmann, Marcel and Seehafer, Norbert and Valori, Gherardo and Wiegelmann, Thomas},
  title     = {A comparison of preprocessing methods for solar force-free magnetic field extrapolation},
  issn      = {0004-6361},
  year      = {2011},
  language  = {en}
}
@phdthesis{Kadyamusuma2011,
  author    = {Kadyamusuma, McLoddy R.},
  title     = {The effect of brain damage and linguistic experience on shona lexicaltone processing},
  address   = {Potsdam},
  pages     = {165 S.},
  year      = {2011},
  language  = {en}
}
@misc{Kraemer2011,
  author    = {Kr{\"a}mer, Raimund},
  title     = {Linz, J. J., An Authoritarian Regime, the case of Spain},
  isbn      = {978-3-941880-21-4},
  year      = {2011},
  language  = {en}
}
@misc{Schmaedeke2011,
  author    = {Schm{\"a}deke, Philipp},
  title     = {Schumpeter, J. A., Capitalism, Socialism and Democracy, New York, Harper \& Row, 1942},
  isbn      = {978-3-941880-21-4},
  year      = {2011},
  language  = {en}
}
@article{HundertmarkDimovaLengefeldetal.2011,
  author    = {Hundertmark, Michaela and Dimova, Rumiana and Lengefeld, Jan and Seckler, Robert and Hincha, Dirk K.},
  title     = {The intrinsically disordered late embryogenesis abundant protein LEA18 from Arabidopsis thaliana modulates membrane stability through binding and folding.},
  issn      = {0006-3002},
  year      = {2011},
  abstract  = {Intrinsically disordered proteins (IDPs) constitute a substantial part of cellular proteomes. Late embryogenesis abundant (LEA) proteins are mostly predicted to be IDPs associated with dehydration tolerance in many plant, animal and bacterial species. Their functions, however, are largely unexplored and also their structure and interactions with potential target molecules have only recently been experimentally investigated in a small number of proteins. Here, we report on the structure and interactions with membranes of the Pfam LEA_1 protein LEA18 from the higher plant Arabidopsis thaliana. This functionally uncharacterized positively charged protein specifically aggregated and destabilized negatively charged liposomes. Isothermal titration calorimetry showed binding of the protein to both charged and uncharged membranes. LEA18 alone was largely unstructured in solution. While uncharged membranes had no influence on the secondary structure of LEA18, the protein partially folded into ;-sheet structure in the presence of negatively charged liposomes. These data suggest that LEA18 does not function as a membrane stabilizing protein, as suggested for other LEA proteins. Instead, a possible function of LEA18 could be the composition-dependent modulation of membrane stability, e.g., during signaling or vesicle-mediated transport. Research Highlights},
  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{Kosta2011,
  author    = {Kosta, Peter},
  title     = {Causatives and anti-causatives, unaccusatives and unergatives : or how big is the contribution of the lexicon to syntax?},
  isbn      = {978-3-631-61869-1},
  year      = {2011},
  language  = {en}
}
@phdthesis{Bennecke2011,
  author    = {Bennecke, Gudrun Elisabeth},
  title     = {Turning wind into power : effects of stakeholder networks on renewalbe energy governanace in India},
  series = {European university studies : series XXXI political science},
  volume    = {23},
  journal   = {European university studies : series XXXI political science},
  publisher = {Lang Peter GmbH Internationaler Verlag der Wissenschaften},
  address   = {Frankfurt},
  isbn      = {978-3-631-61570-6},
  issn      = {0721-3654},
  pages     = {278 S.},
  year      = {2011},
  language  = {en}
}
@phdthesis{Athikomrattanakul2011,
  author    = {Athikomrattanakul, Umporn},
  title     = {Development and characterization of molecularly imprinted polymers as binding elements against nitrofurantoin},
  address   = {Potsdam},
  pages     = {97 S.},
  year      = {2011},
  language  = {en}
}
@phdthesis{CuadrosInostroza2011,
  author    = {Cuadros-Inostroza, Alvaro},
  title     = {Integrated analysis of transcriptome and metabolome to understand grapevine development},
  address   = {Potsdam},
  pages     = {136 S.},
  year      = {2011},
  language  = {en}
}