@book{OPUS4-28242,
  title     = {Studies in Modern English},
  editor    = {Lazebna, Nataliia and Kumar, Dinesh},
  publisher = {W{\"u}rzburg University Press},
  address   = {W{\"u}rzburg},
  isbn      = {978-3-95826-198-3},
  doi       = {10.25972/WUP-978-3-95826-199-0},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-282426},
  publisher      = {W{\"u}rzburg University Press},
  pages     = {VIII, 125},
  year      = {2022},
  abstract  = {The book "Studies in Modern English" interprets English-language communication in the humanitarian paradigm of knowledge within the linguistic and psycho-sociocultural study of speech activity prioritizing cognitive and communicative paradigms. Digital discourse as the formation of new semiotic phenomena has crowned the rapid scientific and technological progress. Researchers' scientific achievements represented in the book are systemic and valid in terms of evidence-based narratives, which reflect the transformational horizon of information theory, communication theory, and theory of linguodidactics in modern English verbal, creative and digital environments. The book represents an integrated approach to the study of modern English as an open synergetic system, which requires a description of the relationship between verbal and nonverbal notions in digital space. The book integrates such innovative perspectives as the interaction of natural English and programming languages, cyber aggression as a communicative pattern in English-language digital discourse, ethics, and democratization of modern English language, relevant developments in the field of English language as a Foreign Language, and other related issues. A complex focus of the book in the realm of modern English-language communication concerns verbal and nonverbal notions analyzed in the context of socio-cultural and digital communicative spaces.},
  subject      = {Englischunterricht},
  language  = {en}
}
@book{Halder2022,
  author    = {Halder, Partho},
  title     = {Identification and characterization of synaptic proteins of Drosophila melanogaster using monoclonal antibodies of the Wuerzburg Hybridoma Library},
  doi       = {10.25972/OPUS-27020},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-270205},
  publisher      = {Universit{\"a}t W{\"u}rzburg},
  year      = {2022},
  abstract  = {For a large fraction of the proteins expressed in the human brain only the primary structure is known from the genome project. Proteins conserved in evolution can be studied in genetic models such as Drosophila. In this doctoral thesis monoclonal antibodies (mAbs) from the Wuerzburg Hybridoma library are produced and characterized with the aim to identify the target antigen. The mAb ab52 was found to be an IgM which recognized a cytosolic protein of Mr ~110 kDa on Western blots. The antigen was resolved by two-dimensional gel electrophoresis (2DE) as a single distinct spot. Mass spectrometric analysis of this spot revealed EPS-15 (epidermal growth factor receptor pathway substrate clone 15) to be a strong candidate. Another mAb from the library, aa2, was already found to recognize EPS-15, and comparison of the signal of both mAbs on Western blots of 1D and 2D electrophoretic separations revealed similar patterns, hence indicating that both antigens could represent the same protein. Finally absence of the wild-type signal in homozygous Eps15 mutants in a Western blot with ab52 confirmed the ab52 antigen to be EPS-15. Thus both the mAbs aa2 and ab52 recognize the Drosophila homologue of EPS-15. The mAb aa2, being an IgG, is more suitable for applications like immunoprecipitation (IP). It has already been submitted to the Developmental Studies Hybridoma Bank (DSHB) to be easily available for the entire research community. The mAb na21 was also found to be an IgM. It recognizes a membrane associated antigen of Mr ~10 kDa on Western blots. Due to the membrane associated nature of the protein, it was not possible to resolve it by 2DE and due to the IgM nature of the mAb it was not possible to enrich the antigen by IP. Preliminary attempts to biochemically purify the endogenously expressed protein from the tissue, gave 99 promising results but could not be completed due to lack of time. Thus biochemical purification of the protein seems possible in order to facilitate its identification by mass spectrometry. Several other mAbs were studied for their staining pattern on cryosections and whole mounts of Drosophila brains. However, many of these mAbs stained very few structures in the brain, which indicated that only a very limited amount of protein would be available as starting material. Because these antibodies did not produce signals on Western blots, which made it impossible to enrich the antigens by electrophoretic methods, we did not attempt their purification. However, the specific localization of these proteins makes them highly interesting and calls for their further characterization, as they may play a highly specialized role in the development and/or function of the neural circuits they are present in. The purification and identification of such low expression proteins would need novel methods of enrichment of the stained structures.},
  subject      = {Taufliege},
  language  = {en}
}