Publikationen 

Prof. Dr. Wolfgang Voos

Originalarbeiten (2007 - 2022)

  • Jaworek, W., Sylvester, M., Cenini, G. & Voos, W. (2022) Elucidation of the interaction proteome of mitochondrial chaperone Hsp78 highlights its role in protein aggregation during heat stress. J. Biol. Chem. 298, 102494. doi:
    10.1016/j.jbc.2022.102494
  • Pollecker, K., Sylvester, M., & Voos, W. (2021). Proteomic analysis demonstrates the role of the quality control protease LONP1 in mitochondrial protein aggregation. J. Biol. Chem. 297, 101134. doi: 10.1016/j.jbc.2021.101134
  • Bogorodskiy ,A., Okhrimenko, I., Maslov, I., Maliar, N., Burkatovskiy, D., von Ameln, F., Schulga, A., Jakobs, P., Altschmied, J., Haendeler, J., Katranidis, A., Sorokin, I., Mishin, A., Gordeliy, V., Büldt, G., Voos, W., Gensch, T. & Borshchevskiy, V. (2021) Accessing mitochondrial protein import in living cells by protein microinjection. Front. Cell. Dev. Biol., 9, 698658
  • Rungranatanawanich, W., Cenini, G., Mastinu, A., Sylverster, M., Wilkening, A., Abate, G., Bonini, S.A., Aria, F., Maccarinelli, G., Memo, M., Voos, W. & Uberti, D. (2019). Gamma-Oryzanol improves congnitive function and modulates hippocampal proteome in mice. Nutrients 11, 753
  • Wilkening, A., Rüb, C., Sylvester, M. & Voos, W. (2018). High aggregation sensitivity of mammalian mitochondrial elongation factor Tu (Tufm) as a sensor for organellar stress. J. Biol. Chem. 293, 11537-11552 (Veröffentlicht in BioRxiv https://doi.org/10.1101/253153)
  • Bruderek, M., Jaworek, W., Wilkening, A., Förtsch, A., Rüb, C., Cenini, G., Sylvester, M. & Voos, W. (2018). IMiQ: a novel protein quality control compartment protecting mitochondrial functional integrity. Mol. Biol. Cell 29, 256-269 (Veröffentlicht in BioRxiv https://doi.org/10.1101/075127)
  • Cenini, C., Rüb, C., Bruderek, M. & Voos, W. (2016). Amyloid β-peptides interfere with mitochondrial preprotein import competence by a co-aggregation process. Mol. Biol. Cell 27, 3257-3272
  • Hallman, K., Kudin, A. P., Zsurka, G., Kornblum, C., Reimann, J., Stüve, B., Waltz, S., Hattingen, E., Thile, H., Nürnberg, P., Rüb, C., Voos, W., Kopatz, J., Neumann, H. & Kunz, W. (2016). Loss of the smallest subunit of cytochrome c oxidase, COX8A, causes Leigh-like syndrome and epilepsy. Brain 139, 338-345
  • 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. 288, 30931-30943
  • Goller, T., Seibold, U., Kremmer, E., Voos, W. & Kolanus, W. (2013). ATAD3 function is essential for early post-implanttion development in the mouse. PLoSOne 8(1), e 54799
  • Becker, D., Richter, J., Tocliescu, M.A., Przedborski, S. & Voos, W. (2012). Pink1 and its membrane potential-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

Übersichtsartikel  (2007 - 2020)

  • Pollecker, K. & Voos, W. (2020) The mitochondrial LON protease: Novel functions off the beaten track? Biomolecules 10, 253
  • Cenini, G. & Voos, W. (2019) Mitochondrial as potential target in Alzheimer disease therapy: An update. Front. Pharmacol. 10, 902
  • Rüb, C., Wilkening, A. & Voos, W. (2017). Mitochondrial quality control by the Pink1/Parkin system. Cell Tissue Res. 367, 111-123
  • Voos, W., Jaworek, W., Wilkening, J. & Bruderek M. (2016). Quality control at the mitochondrion. Essays Biochem. 60, 213-225
  • Cenini, G. & Voos, W. (2016). Role of mitochondrial protein quality control in oxidative stress-induced neurodegenerative diseases. Curr. Alzheimer Res. 13, 164-173
  • Rüb, C., Schröder, N. & Voos, W. (2015). Biochemical properties of the kinase PINK1 as sensor protein for mitochondrial damage signalling. Biochem. Soc. Trans. 43, 287-291
  • Becker, D. & Voos, W. (2015). In vitro analysis of the mitochondrial preprotein import machinery using recombinant precursor polypeptides. In: Membrane Trafficking: Second edition (Ed. Tang, B., L.), Meth. Mol. Biol. 1270, 15-36 (Springer Science+Business Media, New York)
  • Voos, W. (2013). Chaperone-protease networks in mitochondrial protein homeostasis. Biochim. Biophys. Acta 1833, 388-399
  • Becker D., Seibold, U. & Voos W. (2011). Mitochondrial protein import into fungi and animals. In: Adv. in Plant Biol. 1 (Eds. Kempken, F.) Springer, S. 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

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