Business address

Deutsches Zentrum für Neurodegenerative Erkrankungen e.V. (DZNE)
University of Tübingen
Otfried-Müller-Str. 23
D-72076 Tübingen,
Germany

Phone: +49 (0)7071 9254-400
Fax: +49 (0)7071 9254-153
E-mail: christian-johannes.gloeckner@guest.uni-tuebingen.de

External Website: DZNE [german version] [english version]

• German Society for Proteome Research (DGPF)

1. Balta EA, Schäffner I, Wittmann MT, Sock E, von Zweydorf F, von Wittgenstein J, Steib K, Heim B, Kremmer E, Häberle BM, Ueffing M, Lie DC, Gloeckner CJ (2018) Phosphorylation of the neurogenic transcription factor SOX11 on serine 133 modulates neuronal morphogenesis. Sci Rep. 8, 16196

2. Hans F, Eckert M, von Zweydorf F, Gloeckner CJ, Kahle PJ (2018) Identification and characterization of ubiquitinylation sites in TAR DNA-binding protein of 43 kDa (TDP-43). J Biol Chem. 293, 16083-16099

3. Jonasz J. Weber, Matthias Golla, Giambattista Guaitoli, Pimthanya Wanichawan, Stefanie N. Hayer, Stefan Hauser, Ann-Christin Krahl, Maike Nagel, Sebastian Samer, Eleonora Aronica, Cathrine R. Carlson, Ludger Schöls, Olaf Riess, Christian J. Gloeckner, Huu P. Nguyen, Jeannette Hübener-Schmid (2017) A combinatorial approach to identify calpain cleavage sites in the Machado-Joseph disease protein ataxin-3. Brain. 140, 1280-1299

4. Deyaert E, Wauters L, Guaitoli G, Konijnenberg A, Leemans M, Terheyden S, Petrovic A, Gallardo R, Nederveen-Schippers LM, Athanasopoulos PS, Pots H, Van Haastert PJM, Sobott F, Gloeckner CJ, Efremov R, Kortholt A, and Versees W (2017). A homologue of the Parkinson's disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover. Nat Commun. 8:1008.
5. Guaitoli G, Raimondi F, Gilsbach BK, Gomez-Llorente Y, Deyaert E, Renzi F, Li X, Schaffner A, Jagtap PK, Boldt K, von Zweydorf F, Gotthardt K, Lorimer DD, Yue Z, Burgin A, Janjic N, Sattler M, Versees W, Ueffing M, Ubarretxena-Belandia I, Kortholt A, and Gloeckner CJ (2016). Structural model of the dimeric Parkinson's protein LRRK2 reveals a compact architecture involving distant interdomain contacts. Proc. Natl Acad. Sci. U S A. 113:E4357-66
6. Porras P, Duesbury M, Fabregat A, Ueffing M, Orchard S, Gloeckner CJ, Hermjakob H (2015). A visual review of the interactome of LRRK2: Using deep-curated molecular interactions data to represent biology. Proteomics 15, 1390-1404
7. Waschbüsch D, Michels H, Strassheim S, Ossendorf E, Kessler D, Gloeckner CJ, Barnekow A. (2014). LRRK2 transport is regulated by its novel interacting partner Rab32. PLoS One. 9:e111632.                   
   Piccoli G, Onofri F, Cirnaru MD, Kaiser CJO, Jagtap P, Kastenmüller A, Pischedda F, Marte A, von Zweydorf F, Vogt A, Giesert F, Pan L, Antonucci F, Kiel C, Zhang M, Weinkauf S, Sattler M, Sala C, Matteoli M, Ueffing M and Gloeckner CJ (2014). LRRK2 binds to neuronal vesicles through protein interactions mediated by its C-terminal WD40 domain. Mol. Cell. Biol. 34: 2147-2161.
8. Muda K, Bertinetti D, Gesellchen F, Hermann JS, von Zweydorf F, Geerlof A, Jacob A, Ueffing M, Gloeckner CJ*, Herberg FW (2014). Parkinson-related LRRK2 mutation R1441C/G/H impairs PKA phosphorylation of LRRK2 and disrupts its interaction with 14-3-3. Proc. Natl Acad. Sci. U S A. 111:E34-43.
9. Gillardon, F., Kremmer, E., Froehlich, T., Ueffing, M., Hengerer, B., Gloeckner, C.J. (2013) ATP-competitive LRRK2 inhibitors interfere with monoclonal antibody binding to the kinase domain of LRRK2 under native conditions. A method to directly monitor the active conformation of LRRK2? J. Neurosci. Methods. 214,62-68
10. Piccoli, G., Condliffe, S.B., Bauer, M., Giesert, F., Boldt, K., De Astis, S., Meixner, A., Sarioglu, H., Vogt-Weisenhorn, D.M., Wurst, W., Gloeckner, C.J., Matteoli, M., Sala, C., Ueffing, M. (2011). LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool. J Neurosci 31, 2225-2237.
11. Meixner, A., Boldt, K., Van Troys, M., Askenazi, M., Gloeckner, C.J., Bauer, M., Marto, J.A., Ampe, C., Kinkl, N., and Ueffing, M. (2011). A QUICK screen for Lrrk2 interaction partners--leucine-rich repeat kinase 2 is involved in actin cytoskeleton dynamics. Mol Cell Proteomics 10, M110 001172.
12. Gloeckner, C. J., Boldt, K., von Zweydorf, F., Helm, S., Wiesent, L., Sarioglu, H. and Ueffing, M. (2010). Phosphopeptide analysis reveals two discrete clusters of phosphorylation in the N-terminus and the Roc domain of the Parkinson-disease associated protein kinase LRRK2. J Proteome Res. 9, 1738-1745.
13. Gloeckner, C. J., Schumacher, A., Boldt, K. and Ueffing, M. (2009). The Parkinson disease-associated protein kinase LRRK2 exhibits MAPKKK activity and phosphorylates MKK3/6 and MKK4/7, in vitro. J Neurochem. 109, 959-968.
14. Gloeckner, C. J., Boldt, K., Schumacher, A., Roepman, R. and Ueffing, M. (2007). A novel tandem affinity purification strategy for the efficient isolation and characterisation of native protein complexes. Proteomics  7, 4228-4234.
15. Gloeckner, C. J., Kinkl, N., Schumacher, A., Braun, R. J., O'Neill, E., Meitinger, T., Kolch, W., Prokisch, H. and Ueffing, M. (2006). The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity. Hum Mol Genet. 15, 223-232.

For further publications of Dr. Johannes Gloeckner Lab see PubMed