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You are here: Home Research Group Voos Publications


Publications of Voos group since 2004


Peer-reviewed research articles (2004-2014): 

  • Federowicz, M. A., de Vries-Schneider, R. L. A., Rüb, C., Becker, D., Huang, Y., Zhou, C., Alessi-Wolken, D. M., Voos, W., Liu, Y. & Przedborski, S. (2014). Cytosolic cleaved Pink1 represses Parkin translocation to mitochondrial and mitophagy. EMBO Rep. 15, 86-93.
  • Guardia-Laguarta, C., Area-Gomez, E. Rüb, C., Liu, Y., Magrane, J., Becker, D., Voos, W., Schon E. A. & Przedborski, S. (2014). alpha-Synuclein is localized to mitochondria-associated ER membranes. J. Neurosci. 34, 249-259.
  • Lewrenz I., Guiard, B., Rietzschel, N. Lill, R., van der Laan, M. & Voos, W. (2013). The functional interaction of mitochondrial Hsp70s with the escort protein Zim17 is critical for mitochondrial Fe/S biogenesis and mtHsp70 substrate interaction at the inner membrane preprotein translocase. J. Biol. Chem. , in press.
  • Goller, T., Seibold, U., Kremmer, E., Voos, W. & Kolanus, W. (2013). ATAD3 function is essential for early post-implantion development in the mouse. PLoSOne 8(1), e 54799.

  • Becker, D., Richter, J., Tocliescu, M.A., Przedborski, S. & Voos. W. (2012). Pink1 and its Dy-dependent cleavage product both localize to the outer mitochondrial membrane by a unique targeting mode. J. Biol. Chem. 287, 22969-22987.
  • Bender, T., Lewrenz, I., Franken, S., Baitzel, C. & Voos, W. (2011). Mitochondrial enzymes are protected from stress-induced aggregation by mitochondrial Hsp70 and the Pim1/LON protease. Mol. Biol. Cell 22, 541-554.
  • Bender, T., Leidhold, C., Ruppert, T., Franken, S. & Voos, W. (2010). Mitochondrial protein homeostasis under oxidative stress requires the ATP-dependent protease Pim1/LON. Proteomics 10, 1426-1443. 
  •  Vögtle, F.-N., Wortelkamp, S., Zahedi, R. P., Becker, D., Leidhold, C., Kris Gevaert, K., Josef Kellermann, J., Voos, W., Sickmann, A., Nikolaus Pfanner, N. & Chris Meisinger, C. (2009). Global analysis of the mitochondrial N-proteome reveals a critical role of processing peptidases for protein stability. Cell 139, 428-439. 
  • Gispert, S., Ricciardi, F., Kurz, A., Azizov, M., Hoepken, H., Becker, D., Voos, W., Leuner, K., Müller, W. E., Kudin, A. P., Kunz, W. S., Zimmermann, A., Roeper, J., Wenzel, D., Jendrach, M., Garcia-Arenciba, M., Fernandez-Ruiz, J., Huber, L., Rohrer, H., Barrera M., Reichert, A., Rüb, U., Chen, A., Nussbaum, R. L., Steinmetz, H. & Auburger, G. (2009). Parkinson phenotype in aged PINK1-deficient mice is accompanied by progressive mitochondrial dysfunction in absence of neurodegeneration. PLoS ONE 4(6), e5777. 
  • Becker, D., Krayl, M., Strub, A., Li, Y., Mayer, M. P. & Voos, W. (2009). The active, ATP-driven membrane translocation of mitochondrial preproteins by mtHsp70 is dependent on a functional inter-domain communication. J. Biol. Chem.284, 2934-2946. 
  • Krayl, M., Lim, J. H., Martin, F., Guiard, B. & Voos, W. (2007). A cooperative action of the ATP-dependent import motor complex and the inner membrane potential drives mitochondrial preprotein import. Mol. Cell. Biol.27, 411-425. 
  • Porras, P., Padilla, C. A., Krayl, M., Voos, W. & Bárcena, J. A. (2006). One single in frame AUG codon is responsible for a diversity of subcellular localizations of Glutaredoxin 2 in Saccharomyces cerevisiae. J. Biol. Chem. 281, 16551-16562. 
  • Meinecke, M., Wagner, R., Kovermann, P., Guiard, B., Mick, D. U., Hutu, D.P., Voos, W., Truscott, K.N., Chacinska, A., Pfanner, N. & Rehling, P. (2006). Tim50 maintains the permeability barrier of the mitochondrial inner membrane. Science 312, 1523-1536. 
  • Krayl, M., Guiard, B., Paal, K. & Voos, W. (2006). Fluorescence-mediated analysis of mitochondrial preprotein import in vitro. Anal. Biochem. 355, 81-89. 
  • Leidhold, C., von Janowsky, B., Becker, D., Bender, T. & Voos, W. (2006). Structure and function of Hsp78, the mitochondrial ClpB homolog. J. Struct. Biol. 156, 149-164. 
  •  Von Janowsky, B., Major, T., Knapp K. & Voos, W. (2006). The disaggregation activity of the mitochondrial ClpB homolog Hsp78 maintains Hsp70 function under heat stress. J. Mol. Biol. 357, 793-807. 
  • Major, T., von Janowsky, B., Ruppert, T., Mogk, A. & Voos, W. (2006). Proteomic analysis of mitochondrial protein turnover: identification of novel substrate proteins of the matrix protease Pim1. Mol. Cell. Biol. 26, 762-776. 
  • Von Janowsky, B., Knapp, K., Major, T., Krayl, M., Guiard, B. & Voos, W. (2005). Structural properties of substrate proteins determine the degradation by the mitochondrial AAA+ protease Pim1. Biol. Chem. 386, 1307-1317. 
  • Li, Y., Dudek, J., Guiard, B., Pfanner, N., Rehling, P. & Voos, W. (2004). The presequence translocase-associated protein import motor of mitochondria: Pam16 functions in an antagonistic manner to Pam18. J. Biol. Chem. 279, 38047-38054. 
  • Frazier, A., Dudek, J., Guiard, B., Voos, W., Li, Y., Lind, M., Meisinger, C., Geissler, A., Sickmann, A., Meyer, H. E., Bilanchone, V., Cumsky, M. G., Truscott, K. N., Pfanner, N. & Rehling, P. (2004). Pam16 plays an essential role in the mitochondrial protein import motor. Nat. Struct. Mol. Biol. 11, 226-233. 



  • Voos, W. (2013). Chaperone-protease networks in mitochondrial protein homeostasis. Biochim. Biophys. Acta 1833, 388-399. 
  • Becker D., Seibold, U. & Voos W. (2010). Mitochondrial protein import into fungi and animals. In: Adv. in Plant Biol. 1 (Eds. Kempken, F.) Springer, 289-324.
  • Voos, W. (2009). Mitochondrial protein homeostasis: the cooperative roles of chaperones and proteases. Res. Mic. 160, 718-725. 
  • Becker, D., Krayl, M. & Voos, W. (2008). In vitro analysis of the mitochondrial preprotein import machinery using recombinant precursor polypeptides. In: Meth. Mol. Biol., (Ed. Vacura A.) Humana Press, S. 59-84. 
  • Leidhold, C. & Voos. W. (2007). Chaperones and proteases: Guardians of protein integrity in eukaryotic organelles.Ann. NY Acad. Sci. 1113, 72-86. 
  • Voos, W. & Pfanner, N. (2005). The chaperone system of mitochondria. Handbook of Protein Folding II (Eds.: Buchner, J. & Kiefhaber T.), Weinheim, Whiley-VCH, S. 1020-1046. 


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