Ciliary protein function: roles in DNA damage repair and gene regulation

Positions held

  • 2006: Visiting Professor, University of Florida, Gainesville, FL
  • Since 1999: Professor, Faculty of Biology, JGU University of Mainz
  • 1994-1998: Assistant Professor, Cell & Neurobiology, Technical University of Karlsruhe
  • 1993-1994: Postdoc, Mayo Clinic Foundation, Rochester, MN
  • 1991-1993: Research Fellow, Cell & Neurobiology, Technical University of Karlsruhe


  • 1998: Habilitation and venia legendi in Zoology, Technical University of Karlsruhe
  • 1993-1994: Postdoc with Dr. J.L. Salisbury, Mayo Clinic Foundation, Rochester, MN
  • 1991-1993: Postdoc with Prof. R. Paulsen, Cell and Neurobiology, TU Karlsruhe
  • 1988-1991: Dr. rer. nat. with Prof. H. Altner, University of Regensburg
  • 1988: Diploma in Biology, University of Bayreuth

Most relevant publications by Uwe Wolfrum

Goldmann T, Overlack N, van Wyk M, Möller F, Nudelman I, Belakhov V, Baasov T, Wolfrum U* and Nagel-Wolfrum K* (2012). A comparative evaluation of NB30, NB54 and PTC124 in translational read-through efficacy for treatment of an USH1C nonsense mutation. EMBO Mol Med, 4, 1186-1199 *Equal contributions

Sedmak T and Wolfrum U (2010). Intraflagellar transport molecules in ciliary and non-ciliary cells of the retina. J Cell Biol, 189, 171-186

Maerker T, van Wijk E, Overlack N, Kersten FFJ, McGee J, Goldmann T, Sehn E, Roepman R, Walsh EJ, Kremer H and Wolfrum U (2008). A novel Usher protein network at the periciliary reloading point between molecular transport machineries in vertebrate photoreceptor cells. Hum Mol Genet, 17, 71-86

Reiners J, van Wijk E, Märker T, Zimmermann U, Jürgens K, te Brinke H, Overlack, N, Roepman R, Knipper M, Kremer H and Wolfrum U (2005). Scaffold protein harmonin (USH1C) provides molecular links between Usher syndrome type 1 and type 2. Hum Mol Genet, 14, 3933-3943

Tai AW, Chuang J-Z, Bode C, Wolfrum U and Sung C-H (1999). Rhodopsin´s carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding the dynein light chain Tctex-1. Cell, 97, 877-887


  Research website