Short CV/Education and training

  • 1995
    Wageningen Agricultural University, Netherlands, Erasmus Programme, student research paper

  • 1996 – 1998
    TU Berlin, Institute for the Ecology of Microorganisms, student employee in the project "Bacterial dehalorespiration of chlorinated benzenes"

  • 1998
    TU Berlin, Diplom degree in biotechnology engineering

  • 1999
    TU Berlin, Institute of Biochemistry, student employee in the project "Microbial elimination of dichlordiisopropylether"

  • 1999 – 2003
    Humboldt University of Berlin, Charité, Institute of Biochemistry, Doctor of Natural Science (Dr rer. nat.)

  • 2004 – 2009
    Birkbeck College, London, UK; Postdoc: "Cryo EM studies on Hsp104"

Selected publications

  • Kube, S., N. Kapitein, T. Zimniak, F. Herzog, A. Mogk, P. Wendler (2014). 6Å cryo EM structure of the contractile VipA/B nanomachine in type VI effector secretion. Cell Reports, 8(1):20-30; http://dx.doi.org/10.1016/j.celrep.2014.05.034

  • Carroni, M., E. Kummer, Y. Oguchi, P. Wendler, D. K. Clare, I. Sinning, J. Kopp, A. Mogk, B. Bukau, H. Saibil (2014). Head-to-tail interactions of the coiled-coil domains regulate ClpB cooperation with Hsp70 in protein disaggregation. eLife 2014;10.7554/eLife.02481

  • Desantis, M., E., E.A. Sweeny, D. Snead, E.H. Leung, M.S. Go, K Gupta, P. Wendler, J. Shorter (2013). Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation. J. Biol. Chem. Published on November 26, 2013, doi: 10.1074/jbc.M113.520759

  • Wendler, P., S. Ciniawsky, M. Kock, S. Kube (2012). Structure and function of the AAA+ nucleotide binding pocket. Biochim Biophys Acta 1823(1):2-4.

  • Stotz M et al. (2011). Structure of green-type rubisco activase from tobacco. In: Nat Struc Mol Biol 18(12):1366-70.

  • Mueller-Cajar O. et al. (2011). Structure and function of the AAA+ protein CBBX, a red-type rubisco activase. In: Nature 479(7372):194-9.

  • Wendler P, et al. (2011). Structure and Function of the AAA+ Nucleotide Binding Pocket. In: Biochim Biophys Acta. Jul 28.

  • Wollmann P. et al. (2011). Structure and mechanism of the Swi2/Snf2 remodeller Mot1 in complex with its substrate TBP. In: Nature 475(7356):403-7.

  • Wendler P, Saibil H (2010). Cryo electron microscopy structures of Hsp100 proteins – crowbars in or out? In: Biochem. Cell Biol. 88:89-96.

  • Wendler, P. et al.: Motor mechanism for protein threading through Hsp104. In: Mol Cell 34, 2009. pp. 81-92.

  • Wendler, P. et al.: Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104. In: Cell 131(7), 2007. pp. 1366-1377.

  • Puri, T. et al.: Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex. In: J Mol Biol. 366(1), 2007. pp. 179-192.

  • Wendler, P. et al.: The bipartite nuclear localization sequence of Rpn2 is required for nuclear import of proteasomal base complexes via karyopherin alpha/beta and proteasome functions. In: J Biol Chem 279(36), 2004. pp. 37751-37762.

  • Fehlker, M. et al.: "Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly." In: EMBO Rep 4(10), 2003. pp. 959-963.


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