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  1. The figure of Melusine in Fontane’s texts : images, digressions, and lacunae
    Autor*in: Menke, Bettine
    Erschienen: 31.03.2009

    The Melusines that appear in Fontane’s texts [...] must be read as part of history of citations and refigurations, a history that then revives and flourishes in diluted form around the turn of the century with the trivial myth of the femme fatale.... mehr

     

    The Melusines that appear in Fontane’s texts [...] must be read as part of history of citations and refigurations, a history that then revives and flourishes in diluted form around the turn of the century with the trivial myth of the femme fatale. The new context for Fontane’s Melusine is the social construction of the feminine in the context of the conflict over the equality and/or the difference of the sexes, and the currency of certain clichéd versions of this construction. [...] In this essay, I will examine the function that the Melusine figure — as the recasting and rewriting of a myth — assumes in realist texts and, specifically, in the texts of Fontane.

     
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    Quelle: GiNDok
    Sprache: Englisch
    Medientyp: Wissenschaftlicher Artikel
    Format: Online
    DDC Klassifikation: Literaturen germanischer Sprachen; Deutsche Literatur (830)
    Schlagworte: Fontane, Theodor
    Lizenz:

    publikationen.ub.uni-frankfurt.de/home/index/help

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    info:eu-repo/semantics/openAccess
  2. Syntactic annotation of non-canonical linguistic structures
    Autor*in: Hirschmann, Hagen ; Doolittle, Seanna ; Lüdeling, Anke
    Erschienen: 27.10.2009

    This paper deals with the syntactic annotation of corpora that contain both ‘canonical’ and ‘non-canonical’ sentences. mehr

     

    This paper deals with the syntactic annotation of corpora that contain both ‘canonical’ and ‘non-canonical’ sentences.

     
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    Quelle: GiNDok
    Sprache: Englisch
    Medientyp: Konferenzveröffentlichung; conferenceObject
    Format: Online
    DDC Klassifikation: Sprache (400)
    Schlagworte: Korpus <Linguistik>
    Lizenz:

    publikationen.ub.uni-frankfurt.de/home/index/help

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    info:eu-repo/semantics/openAccess
  3. What's hard? : Quantitative evidence for difficult constructions in German learner data
    Autor*in: Zeldes, Amir ; Lüdeling, Anke ; Hirschmann, Hagen
    Erschienen: 27.10.2009

    Our study is concerned with the identification of ‘difficult’ structure s in the acquisition of a foreign language, which will shed light on theoretical considerations of L2 processing. We argue that – compared to simple vocabulary items or abstract... mehr

     

    Our study is concerned with the identification of ‘difficult’ structure s in the acquisition of a foreign language, which will shed light on theoretical considerations of L2 processing. We argue that – compared to simple vocabulary items or abstract syntactic patterns – structures that contain lexical material as well as categorial variables are especially difficult to acquire. The difficulty level for particular patterns is shown to depend on surface invariability but not on the syntactic categories within which target patterns are embedded. As an example we study the distribution of certain structures which are underused by L2 German learners.

     
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    Quelle: GiNDok
    Sprache: Englisch
    Medientyp: Konferenzveröffentlichung; conferenceObject
    Format: Online
    DDC Klassifikation: Germanische Sprachen; Deutsch (430)
    Schlagworte: Fremdsprachenunterricht
    Lizenz:

    publikationen.ub.uni-frankfurt.de/home/index/help

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    info:eu-repo/semantics/restrictedAccess
  4. EFP1 is an ER stress-induced glycoprotein which interacts with the pro-apoptotic protein Par-4
    Autor*in: Appel, Sarah ; Vetterkind, Susanne ; Koplin, Ansgar ; Maertens, Barbara ; Boosen, Meike ; Preuss, Ute
    Erschienen: 08.05.2009

    We have isolated the rat ortholog of EFP1 (EF-hand binding protein 1) as a novel interaction partner of the pro-apoptotic protein Par-4 (prostate apoptosis response-4). Rat EFP1 contains two thioredoxin domains, the COOH-terminal one harboring a CGFC... mehr

     

    We have isolated the rat ortholog of EFP1 (EF-hand binding protein 1) as a novel interaction partner of the pro-apoptotic protein Par-4 (prostate apoptosis response-4). Rat EFP1 contains two thioredoxin domains, the COOH-terminal one harboring a CGFC motif, and has a similar protein domain structure as members of the protein disulfide isomerase (PDI) family. In REF52.2 and CHO cells, EFP1 colocalized with the endoplasmic reticulum (ER) marker PDI. Furthermore, EFP1 possesses catalytic activity as demonstrated by an insulin disulfide reduction assay. Western blot analysis revealed two EFP1 protein bands of approximately 136 and 155 kDa, representing different glycosylation states of the protein. Complex formation between EFP1 and Par-4 was confirmed in vitro and in vivo by co-immunoprecipitation, dot blot overlay and pull-down experiments. In CHO cells, coexpression of EFP1 and Par-4 resulted in enhanced Par-4-mediated apoptosis, which required the catalytic activity of EFP1. Interestingly, EFP1 was specifically upregulated in NIH3T3 cells after induction of ER stress by thapsigargin, tunicamycin, and brefeldin A, but not by agents that induce oxidative stress or ER-independent apoptosis. Furthermore, we could show that the induction of apoptosis by Ca2+ stress-inducing agents was significantly decreased after siRNA oligonucleotide-mediated knockdown of Par-4. Our data suggest that EFP1 might represent a cell-protective enzyme that could play an important role in the decision between survival and initiation of Par-4-mediated apoptosis.

     
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    Quelle: GiNDok
    Sprache: Englisch
    Medientyp: Wissenschaftlicher Artikel
    Format: Online
    DDC Klassifikation: Medizin und Gesundheit (610)
    Lizenz:

    creativecommons.org/licenses/by-nc/3.0/de/deed.de

    ;

    info:eu-repo/semantics/openAccess
  5. Digital Germanic philology? : questions, challenges and obstacles for scholars of german
    Autor*in: Szurawitzki, Michael
    Erschienen: 10.11.2009

    Is the digital future a blessing for philologists, especially those working the vast area of Germanic Languages & Literatures? Or does it rather come with problems that jeopardize philology, in the Germanic and the broader scope? This paper sets out... mehr

     

    Is the digital future a blessing for philologists, especially those working the vast area of Germanic Languages & Literatures? Or does it rather come with problems that jeopardize philology, in the Germanic and the broader scope? This paper sets out to explore the status quo (1.) of digital source material in Germanic philology, ranging from medieval manuscripts to 21st century e-books and their, at times, highly restricted availability to the scientific community. Do we really face a quantum leap in terms of open access, or is this leap rather confined to those only who pay the exorbitant fees specialist libraries charge for the use of their rare manuscript and book collections? How about Google Books (2.)? Are we in danger of neglecting everything that is (still) missing there? And what is in it for the German scholar? Can we believe that in some years’ time we will be able to get our hands on every source text we desire within seconds since it is only a click away? This paper critically assesses the process and progress of the digitization of mankind’s written records (3.), focusing on problems to be overcome by e.g. medievalists wishing to consult certain source material. This is illustrated by means of the example of how it is not yet possible consult certain materials related to the Franciscan preacher Berthold von Regensburg († 1272). A short concluding summary (4.) highlights perspectives for further thinking and discussion.

     
    Export in Literaturverwaltung
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    Quelle: GiNDok
    Sprache: Englisch
    Medientyp: Konferenzveröffentlichung; conferenceObject
    Format: Online
    DDC Klassifikation: Literaturen germanischer Sprachen; Deutsche Literatur (830)
    Schlagworte: Germanistik
    Lizenz:

    publikationen.ub.uni-frankfurt.de/home/index/help

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    info:eu-repo/semantics/openAccess