@phdthesis{Juergens2020,
  author    = {J{\"u}rgens, Lukas Julian Christoph},
  title     = {Spatio-temporale Distribution der Tubuline und Tubulin spezifischen Chaperone im sensorischen Epithel der murinen Cochlea},
  doi       = {10.25972/OPUS-20649},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-206498},
  school      = {Universit{\"a}t W{\"u}rzburg},
  year      = {2020},
  abstract  = {Die f{\"u}nf Tubulin-bindenden Kofaktoren (TBC) sind an der Tubulinsynthese und der Bildung von Mikrotubuli beteiligt. Ihre Bedeutung wird durch verschiedene Krankheiten und Syndrome hervorgehoben, die durch Funktionsst{\"o}rungen oder Mutationen dieser Proteine verursacht werden. Posttranslationale Modifikationen (PTMs) von Tubulin f{\"o}rdern verschiedene Eigenschaften, einschließlich stabilit{\"a}tsf{\"o}rdernder Subpopulationen von Tubulin. Die zell- und zeitspezifische Verteilung der PTMs ist bisher nur im Corti-Organ bei Gerbils untersucht worden. Ziel der vorliegenden Studie war es, die zelltyp- und zeitspezifischen Expressionsmuster von TBC-Proteinen und PTMs erstmals in der murinen Cochlea {\"u}ber mehrere Entwicklungsstadien hinweg zu untersuchen. Dazu wurden murine Cochleae im postnatalen (P) Alter P1, P7 und P14 mittels Immunfluoreszenzanalyse untersucht. Die Untersuchungen zeigten mehrere erhebliche Interspezies-Unterschiede in der Verteilung der PTMs zwischen Gerbil und Maus. Dar{\"u}ber hinaus ist dies die erste Studie, die die r{\"a}umlich-zeitliche Verteilung von TBCs in einem Gewebe beschreibt, das ein volatiles Expressionsmuster aufweist. Die Expressionsanalyse von TBC-Proteinen und PTMs des Tubulins zeigt, dass diese Proteine eine wichtige Rolle bei der physiologischen Entwicklung der Cochlea spielen und f{\"u}r das H{\"o}ren essentiell sein k{\"o}nnten.},
  subject      = {Mikrotubulus},
  language  = {de}
}
@article{JuergensBieniussaVoelkeretal.2020,
  author    = {Juergens, Lukas and Bieniussa, Linda and Voelker, Johannes and Hagen, Rudolf and Rak, Kristen},
  title     = {Spatio-temporal distribution of tubulin-binding cofactors and posttranslational modifications of tubulin in the cochlea of mice},
  series = {Histochemistry and Cell Biology},
  volume    = {154},
  journal   = {Histochemistry and Cell Biology},
  issn      = {0948-6143},
  doi       = {10.1007/s00418-020-01905-6},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-234852},
  pages     = {671-681},
  year      = {2020},
  abstract  = {The five tubulin-binding cofactors (TBC) are involved in tubulin synthesis and the formation of microtubules. Their importance is highlighted by various diseases and syndromes caused by dysfunction or mutation of these proteins. Posttranslational modifications (PTMs) of tubulin promote different characteristics, including stability-creating subpopulations of tubulin. Cell- and time-specific distribution of PTMs has only been investigated in the organ of Corti in gerbils. The aim of the presented study was to investigate the cell type-specific and time-specific expression patterns of TBC proteins and PTMs for the first time in murine cochleae over several developmental stages. For this, murine cochleae were investigated at the postnatal (P) age P1, P7 and P14 by immunofluorescence analysis. The investigations revealed several profound interspecies differences in the distribution of PTMs between gerbil and mouse. Furthermore, this is the first study to describe the spatio-temporal distribution of TBCs in any tissue ever showing a volatile pattern of expression. The expression analysis of TBC proteins and PTMs of tubulin reveals that these proteins play a role in the physiological development of the cochlea and might be essential for hearing.},
  language  = {en}
}
@article{LanglhoferVillmann2016,
  author    = {Langlhofer, Georg and Villmann, Carmen},
  title     = {The Intracellular Loop of the Glycine Receptor: It's not all about the Size},
  series = {Frontiers in Molecular Neuroscience},
  journal   = {Frontiers in Molecular Neuroscience},
  number    = {9},
  doi       = {10.3389/fnmol.2016.00041},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-165394},
  pages     = {41},
  year      = {2016},
  abstract  = {The family of Cys-loop receptors (CLRs) shares a high degree of homology and sequence identity. The overall structural elements are highly conserved with a large extracellular domain (ECD) harboring an α-helix and 10 β-sheets. Following the ECD, four transmembrane domains (TMD) are connected by intracellular and extracellular loop structures. Except the TM3-4 loop, their length comprises 7-14 residues. The TM3-4 loop forms the largest part of the intracellular domain (ICD) and exhibits the most variable region between all CLRs. The ICD is defined by the TM3-4 loop together with the TM1-2 loop preceding the ion channel pore. During the last decade, crystallization approaches were successful for some members of the CLR family. To allow crystallization, the intracellular loop was in most structures replaced by a short linker present in prokaryotic CLRs. Therefore, no structural information about the large TM3-4 loop of CLRs including the glycine receptors (GlyRs) is available except for some basic stretches close to TM3 and TM4. The intracellular loop has been intensively studied with regard to functional aspects including desensitization, modulation of channel physiology by pharmacological substances, posttranslational modifications, and motifs important for trafficking. Furthermore, the ICD interacts with scaffold proteins enabling inhibitory synapse formation. This review focuses on attempts to define structural and functional elements within the ICD of GlyRs discussed with the background of protein-protein interactions and functional channel formation in the absence of the TM3-4 loop.},
  language  = {en}
}