Funktionelle Neuroproteomik und Translationale Biomarker in neurodegenerativen Erkrankungen
Priv.-Doz. Dr. Christian Johannes Gloeckner
Gruppenleiter
Otfried-Müller-Str. 23
72076 Tübingen

johannes.gloeckner@dzne.de
 +49 7071 9254-400

Publikationen

Die vollständige Publikaitonsliste findet man hier.

Maria Dolores Perez Carrion, Silvia Marsicano, Federica Daniele, Antonella Marte, Francesca Pischedda, Eliana Di Cairano, Ester Piovesana, Felix Von Zweydorf, Elisabeth Kremmer, Christian Johannes Gloeckner, Franco Onofri, Carla Perego, Giovanni Piccoli. The LRRK2 G2385R variant is a partial loss-of-function mutation that affects synaptic vesicle trafficking through altered protein interactions. Scientific Reports. 2017 Nov 30; 7 doi: 10.1038/s41598-017-05760-9
Egon Deyaert, Lina Wauters, Giambattista Guaitoli, Albert Konijnenberg, Margaux Leemans, Susanne Terheyden, Arsen Petrovic, Rodrigo Gallardo, Laura M. Nederveen-Schippers, Panagiotis S. Athanasopoulos, Henderikus Pots, Peter J. M. Van Haastert, Frank Sobott, Christian Johannes Gloeckner, Rouslan Efremov, Arjan Kortholt, Wim Versées. A homologue of the Parkinson's disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover. Nature Communications. 2017 Nov 30; 8 doi: 10.1038/s41467-017-01103-4
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. A combinatorial approach to identify calpain cleavage sites in the Machado-Joseph disease protein ataxin-3. Brain. 2017 Apr 30; 140:1280-1299. doi: 10.1093/brain/awx039
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, Gloeckner CJ. Structural model of the dimeric Parkinson's protein LRRK2 reveals a compact architecture involving distant interdomain contacts. Proceedings of the National Academy of Sciences of the United States of America. 2016 Jan 01; 113:E4357-66. doi: 10.1073/pnas.1523708113
Giambattista Guaitoli, Bernd K. Gilsbach, Francesco Raimondi, Christian Johannes Gloeckner. First model of dimeric LRRK2: The challenge of unrevealing the structure of a multidomain Parkinson's-associated protein. Biochemical Society Transactions. 2016 Dec 14; 44:1635-1641. doi: 10.1042/BST20160226
Porras P, Duesbury M, Fabregat A, Ueffing M, Orchard S, Gloeckner CJ, Hermjakob H. A visual review of the interactome of LRRK2: Using deep-curated molecular interaction data to represent biology. Proteomics. 2015 Jan 01; 15:1390-404. doi: 10.1002/pmic.201400390
Piccoli G, Onofri F, Cirnaru MD, Kaiser CJ, Jagtap P, Kastenmuller 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, Gloeckner CJ. Leucine-rich repeat kinase 2 binds to neuronal vesicles through protein interactions mediated by its C-terminal WD40 domain. Mol Cell Biol. 2004 Jan 01; 34:2147-61. doi: 10.1128/MCB.00914-13
Muda K, Bertinetti D, Gesellchen F, Hermann JS, von Zweydorf F, Geerlof A, Jacob A, Ueffing M, Gloeckner CJ, Herberg FW. Parkinson-related LRRK2 mutation R1441C/G/H impairs PKA phosphorylation of LRRK2 and disrupts its interaction with 14-3-3. Proceedings of the National Academy of Sciences of the United States of America. 2014 Jan 01; 111:E34-43. doi: 10.1073/pnas.1312701111
Waschbusch D, Michels H, Strassheim S, Ossendorf E, Kessler D, Gloeckner CJ, Barnekow A. LRRK2 transport is regulated by its novel interacting partner Rab32. PloS one. 2014 Jan 01; 9:e111632. doi: 10.1371/journal.pone.0111632
Gillardon F, Kremmer E, Froehlich T, Ueffing M, Hengerer B, Gloeckner CJ. 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? Journal of neuroscience methods. . 2013 Jan 01; 214:62-8. doi: 10.1016/j.jneumeth.2012.12.015
Meixner A, Boldt K, Van Troys M, Askenazi M, Gloeckner CJ, Bauer M, Marto JA, Ampe C, Kinkl N, Ueffing M. QUICK screen for Lrrk2 interaction partners--leucine-rich repeat kinase 2 is involved in actin cytoskeleton dynamics. Molecular & cellular proteomics. 2001 Jan 01; 10:M110 001172. doi: 10.1074/mcp.M110.001172
Gloeckner CJ, Boldt K, von Zweydorf F, Helm S, Wiesent L, Sarioglu H, Ueffing M. Phosphopeptide analysis reveals two discrete clusters of phosphorylation in the N-terminus and the Roc domain of the Parkinson-disease associated protein kinase LRRK2. Journal of proteome research. 2010 Jan 01; 9:1738-45. doi: 10.1021/pr9008578
Gloeckner CJ, Boldt K, Schumacher A, Roepman R, Ueffing M. A novel tandem affinity purification strategy for the efficient isolation and characterisation of native protein complexes. Proteomics. 2007 Jan 01; 7:4228-34. doi: 10.1002/pmic.200700038
Gloeckner CJ, Kinkl N, Schumacher A, Braun RJ, O'Neill E, Meitinger T, Kolch W, Prokisch H, Ueffing M. The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity. Human molecular genetics. 2006 Jan 01; 15:223-32. doi: 10.1093/hmg/ddi439

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