@article{Prelog2012,
  author    = {Prelog, Martina},
  title     = {Differential Approaches for Vaccination from Childhood to Old Age},
  series = {Gerontology},
  volume    = {59},
  journal   = {Gerontology},
  number    = {3},
  issn      = {0304-324X},
  doi       = {10.1159/000343475},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-196602},
  pages     = {230-239},
  year      = {2012},
  abstract  = {Primary prevention strategies, such as vaccinations at the age extremes, in neonates and elderly individuals, demonstrate a challenge to health professionals and public health specialists. The aspects of the differentiation and maturation of the adaptive immune system, the functional implications of immunological immaturity or immunosenescence and its impact on vaccine immunogenicity and efficacy will be highlighted in this review. Several approaches have been undertaken to promote Th1 responses in neonates and to enhance immune functions in elderly, such as conjugation to carrier proteins, addition of adjuvants, concomitant vaccination with other vaccines, change in antigen concentrations or dose intervals or use of different administration routes. Also, early protection by maternal vaccination seems to be beneficial in neonates. However, it also appears necessary to think of other end points than antibody concentrations to assess vaccine efficacy in neonates or elderly, as also the cellular immune response may be impaired by the mechanisms of immaturity, underlying health conditions, immunosuppressive treatments or immunosenescence. Thus, lifespan vaccine programs should be implemented to all individuals on a population level not only to improve herd protection and to maintain protective antibody levels and immune memory, but also to cover all age groups, to protect unvaccinated elderly persons and to provide indirect protection for neonates and small infants.},
  language  = {en}
}
@article{Wajant2019,
  author    = {Wajant, Harald},
  title     = {Molecular mode of action of TRAIL receptor agonists—common principles and their translational exploitation},
  series = {Cancers},
  volume    = {11},
  journal   = {Cancers},
  number    = {7},
  doi       = {10.3390/cancers11070954},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-202416},
  pages     = {954},
  year      = {2019},
  abstract  = {Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) and its death receptors TRAILR1/death receptor 4 (DR4) and TRAILR2/DR5 trigger cell death in many cancer cells but rarely exert cytotoxic activity on non-transformed cells. Against this background, a variety of recombinant TRAIL variants and anti-TRAIL death receptor antibodies have been developed and tested in preclinical and clinical studies. Despite promising results from mice tumor models, TRAIL death receptor targeting has failed so far in clinical studies to show satisfying anti-tumor efficacy. These disappointing results can largely be explained by two issues: First, tumor cells can acquire TRAIL resistance by several mechanisms defining a need for combination therapies with appropriate sensitizing drugs. Second, there is now growing preclinical evidence that soluble TRAIL variants but also bivalent anti-TRAIL death receptor antibodies typically require oligomerization or plasma membrane anchoring to achieve maximum activity. This review discusses the need for oligomerization and plasma membrane attachment for the activity of TRAIL death receptor agonists in view of what is known about the molecular mechanisms of how TRAIL death receptors trigger intracellular cell death signaling. In particular, it will be highlighted which consequences this has for the development of next generation TRAIL death receptor agonists and their potential clinical application.},
  language  = {en}
}
@article{Wajant2019,
  author    = {Wajant, Harald},
  title     = {Molecular mode of action of TRAIL receptor agonists—common principles and their translational exploitation},
  series = {Cancers},
  volume    = {11},
  journal   = {Cancers},
  number    = {7},
  doi       = {10.3390/cancers11070954},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-201833},
  pages     = {954},
  year      = {2019},
  abstract  = {Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) and its death receptors TRAILR1/death receptor 4 (DR4) and TRAILR2/DR5 trigger cell death in many cancer cells but rarely exert cytotoxic activity on non-transformed cells. Against this background, a variety of recombinant TRAIL variants and anti-TRAIL death receptor antibodies have been developed and tested in preclinical and clinical studies. Despite promising results from mice tumor models, TRAIL death receptor targeting has failed so far in clinical studies to show satisfying anti-tumor efficacy. These disappointing results can largely be explained by two issues: First, tumor cells can acquire TRAIL resistance by several mechanisms defining a need for combination therapies with appropriate sensitizing drugs. Second, there is now growing preclinical evidence that soluble TRAIL variants but also bivalent anti-TRAIL death receptor antibodies typically require oligomerization or plasma membrane anchoring to achieve maximum activity. This review discusses the need for oligomerization and plasma membrane attachment for the activity of TRAIL death receptor agonists in view of what is known about the molecular mechanisms of how TRAIL death receptors trigger intracellular cell death signaling. In particular, it will be highlighted which consequences this has for the development of next generation TRAIL death receptor agonists and their potential clinical application.},
  language  = {en}
}
@article{WeberOsbornFrankeetal.1977,
  author    = {Weber, Klaus and Osborn, Mary and Franke, Werner W. and Seib, Erinita and Scheer, Ulrich and Herth, Werner},
  title     = {Identification of microtubular structures in diverse plant and animal cells by immunological cross-reaction revealed in immunofluorescence microscopy using antibodies against tubulin from porcine brain},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-41383},
  year      = {1977},
  abstract  = {Antibody against tubulin from porcine brain was used to evaluate the immunological cross reactivity of tubulin from a variety of animal and plant cells. Indirect immunofluorescence microscopy revealed microtubule-containing structures including cytoplasmic microtubules, spindle microtubules, cilia and fIagella. Thus tubulin from diverse species of both mammals and plants show immunological cross-reactivity with tubulin from porcine brain. Results obtained by immunofluorescence microscopy are whenever possible compared with previously known ultrastructural results obtained by electron microscopy.},
  subject      = {Cytologie},
  language  = {en}
}