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Dr Christoph Goebl

Postdoctoral Fellow Christoph Goebl image 2019

PhD (Graz)

Email christoph.goebl@otago.ac.nz

Research interests

Dr Christoph Goebl obtained his Bachelor and Master's degrees in Chemistry from the Karl-Franzens-University of Graz in Austria, and then his PhD in molecular biology from the same institute with Prof Klaus Zangger. During his PhD, he was a recipient of a DOC-fellowship of the Austrian Academy of Sciences and performed a one-year research stay with Dr Nico Tjandra at the NIH in Bethesda, USA, focusing on NMR spectroscopy of proteins. After his PhD, Dr Goebl joined Prof Tobias Madl as a PFP Helmholtz Fellow at the Technical University of Munich and the Helmholtz Center Munich, Germany where he became interested in the molecular basis of reactive oxygen species in biology. He then carried out a cell-biology focused post-doctoral position with Prof Tak W. Mak and Dr Chiara Gorrini at the Princess Margaret Cancer Centre in Toronto, Canada, working on cancer-pathways and redox signalling.

Dr Goebl combines expertise in structural biology (using NMR spectroscopy, small-angle X-ray scattering (SAXS) and X-ray crystallography) with experience in biochemical methods in oxidative stress signalling. He is exploring oxidative stress pathways of the Aryl hydrcarbon receptor (AhR) with focus on its metabolomic signalling in cancers. He also discovered redox-mediated amyloid formation of the tumour suppressor protein p16, and is currently investigating its role in melanoma.

Dr Goebll is a current recipient of the HRC's Sir Charles Hercus Health Research Fellowship.

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Publications

Göbl, C., Morris, V. K., van Dam, L., Visscher, M., Polderman, P. E., Hartlmüller, C., … Dansen, T. B. (2020). Cysteine oxidation triggers amyloid fibril formation of the tumor suppressor p16INK4A. Redox Biology, 28, 101316. doi: 10.1016/j.redox.2019.101316

Hartlmüller, C., Spreitzer, E., Göbl, C., Falsone, F., & Madl, T. (2019). NMR characterization of solvent accessibility and transient structure in intrinsically disordered proteins. Journal of Biomolecular NMR, 73(6-7), 305-317. doi: 10.1007/s10858-019-00248-2

Kubli, S. P., Bassin, C., Roux, C., Wakeham, A., Göbl, C., Zhou, W., … Gorrini, C. (2019). AhR controls redox homeostasis and shapes the tumor microenvironment in BRCA1-associated breast cancer. PNAS, 116(9), 3604-3613. doi: 10.1073/pnas.1815126116

Weber, B., Hora, M., Kazman, P., Göbl, C., Camilloni, C., Reif, B., & Buchner, J. (2018). The antibody light-chain linker regulates domain orientation and amyloidogenicity. Journal of Molecular Biology, 430(24), 4925-4940. doi: 10.1016/j.jmb.2018.10.024

Göbl, C., & Madl, T. (2018). Entspannte Moleküle: NMR-Ober- flächen daten zur Strukturbestimmung. Biospektrum, 24(2), 161-163. doi: 10.1007/s12268-018-0898-5

Journal - Research Article

Göbl, C., Morris, V. K., van Dam, L., Visscher, M., Polderman, P. E., Hartlmüller, C., … Dansen, T. B. (2020). Cysteine oxidation triggers amyloid fibril formation of the tumor suppressor p16INK4A. Redox Biology, 28, 101316. doi: 10.1016/j.redox.2019.101316

Hartlmüller, C., Spreitzer, E., Göbl, C., Falsone, F., & Madl, T. (2019). NMR characterization of solvent accessibility and transient structure in intrinsically disordered proteins. Journal of Biomolecular NMR, 73(6-7), 305-317. doi: 10.1007/s10858-019-00248-2

Kubli, S. P., Bassin, C., Roux, C., Wakeham, A., Göbl, C., Zhou, W., … Gorrini, C. (2019). AhR controls redox homeostasis and shapes the tumor microenvironment in BRCA1-associated breast cancer. PNAS, 116(9), 3604-3613. doi: 10.1073/pnas.1815126116

Weber, B., Hora, M., Kazman, P., Göbl, C., Camilloni, C., Reif, B., & Buchner, J. (2018). The antibody light-chain linker regulates domain orientation and amyloidogenicity. Journal of Molecular Biology, 430(24), 4925-4940. doi: 10.1016/j.jmb.2018.10.024

Göbl, C., & Madl, T. (2018). Entspannte Moleküle: NMR-Ober- flächen daten zur Strukturbestimmung. Biospektrum, 24(2), 161-163. doi: 10.1007/s12268-018-0898-5

Cristóvão, J. S., Morris, V. K., Cardoso, I., Leal, S. S., Martínez, J. M., Botelho, H. M., Göbl, C., … Gomes, C. M. (2018). The neuronal S100B protein is a calcium-tuned suppressor of amyloid-β aggregation. Science Advances, 4(6), eaaq1702. doi: 10.1126/sciadv.aaq1702

Gourinchas, G., Etzl, S., Göbl, C., Vide, U., Madl, T., & Winkler, A. (2017). Long-range allosteric signaling in red light–regulated diguanylyl cyclases. Science Advances, 3(3), e1602498. doi: 10.1126/sciadv.1602498

Rodriquez Camargo, D. C., Tripsianes, K., Buday, K., Franko, A., Göbl, C., Hartlmüller, C., … Reif, B. (2017). The redox environment triggers conformational changes and aggregation of hIAPP in Type II Diabetes. Scientific Reports, 7, 44041. doi: 10.1038/srep44041

Suárez-Calvet, M., Neumann, M., Arzberger, T., Abou-Ajram, C., Funk, E., Hartmann, H., … Göbl, C., … Haass, C. (2016). Monomethylated and unmethylated FUS exhibit increased binding to Transportin and distinguish FTLD-FUS from ALS-FUS. Acta Neuropathologica, 131(4), 587-604. doi: 10.1007/s00401-016-1544-2

Strickland, M., Schwieters, C. D., Göbl, C., Opina, A. C. L., Strub, M.-P., Swenson, R. E., … Tjandra, N. (2016). Characterizing the magnetic susceptibility tensor of lanthanide-containing polymethylated-DOTA complexes. Journal of Biomolecular NMR, 66(2), 125-139. doi: 10.1007/s10858-016-0061-x

Gersch, M., Famulla, K., Dahmen, M., Göbl, C., Malik, I., Richter, K., … Sieber, S. A. (2015). AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control. Nature Communications, 6, 6320. doi: 10.1038/ncomms7320

Chromikova, V., Mader, A., Hofbauer, S., Göbl, C., Madl, T., Gach, J. S., … Kunert, R. (2015). Introduction of germline residues improves the stability of anti-HIV mAb 2G12-IgM. Biochimica et Biophysica Acta: Proteins & Proteomics, 1854(10, Pt A), 1536-1544. doi: 10.1016/j.bbapap.2015.02.018

Hacker, C., Christ, N. A., Duchardt-Ferner, E., Korn, S., Göbl, C., Berninger, L., … Wöhnert, J. (2015). The solution structure of the lantibiotic immunity protein NisI and its interactions with nisin. Journal of Biological Chemistry, 290(48), 28869-28886. doi: 10.1074/jbc.M115.679969

Göbl, C., Madl, T., Simon, B., & Sattler, M. (2014). NMR approaches for structural analysis of multidomain proteins and complexes in solution. Progress in Nuclear Medicine Resonance Spectroscopy, 80, 26-63. doi: 10.1016/j.pnmrs.2014.05.003

Kosol, S., Schrank, E., Bukvić Krajačić, M., Wagner, G. E., Meyer, N. H., Göbl, C., … Novak, P. (2012). Probing the interactions of macrolide antibiotics with membrane-mimetics by NMR spectroscopy. Journal of Medicinal Chemistry, 55(11), 5632-5636. doi: 10.1021/jm300647f

Göbl, C., Dulle, M., Hohlweg, W., Grossauer, J., Falsone, S. F., Glatter, O., & Zangger, K. (2010). Influence of phosphocholine alkyl Chain length on peptide—micelle interactions and micellar size and shape. Journal of Physical Chemistry B, 114(13), 4717-4724. doi: 10.1021/jp9114089

Göbl, C., Kosol, S., Stockner, T., Rückert, H. M., & Zangger, K. (2010). Solution structure and membrane binding of the toxin Fst of the par addiction module. Biochemistry, 49(31), 6567-6575. doi: 10.1021/bi1005128

Pieber, B., Schober, S., Goebl, C., & Mittelbach, M. (2010). Novel sensitive determination of steryl glycosides in biodiesel by gas chromatography–mass spectroscopy. Journal of Chromatography A, 1217(42), 6555-6561. doi: 10.1016/j.chroma.2010.08.006

Zangger, K., Respondek, M., Göbl, C., Hohlweg, W., Rasmussen, K., Grampp, G., & Madl, T. (2009). Positioning of micelle-bound peptides by paramagnetic relaxation enhancements. Journal of Physical Chemistry B, 113(13), 4400-4406. doi: 10.1021/jp808501x

Respondek, M., Madl, T., Göbl, C., Golser, R., & Zangger, K. (2007). Mapping the orientation of helices in micelle-bound peptides by paramagnetic relaxation waves. Journal of the American Chemical Society, 129(16), 5228-5234. doi: 10.1021/ja069004f

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Journal - Research Other

Göbl, C., Focke-Teikl, M., Najafi, N., Schrank, E., Madl, T., Kosol, S., … Tjandra, N. (2017). Flexible IgE epitope-containing domains of Phl p 5 cause high allergenic activity. Journal of Allergy & Clinical Immunology, 140(4), 1187-1191. doi: 10.1016/j.jaci.2017.05.005

Göbl, C., & Tjandra, N. (2012). Application of solution NMR spectroscopy to study protein dynamics. Entropy, 14(3), 581-598. doi: 10.3390/e14030581

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Conference Contribution - Published proceedings: Abstract

Cristóvão, J. S., Morris, V., Cardoso, I., Leal, S. S., Botelho, H. M., Göbl, C., … Gomes, C. M. (2017). The neuronal S100B cytokine targeting amyloid-β aggregation in Alzheimer's disease. FEBS Journal, 284(Suppl. 1), (pp. 184). doi: 10.1111/febs.14174

Kosol, S., Göbl, C., Čuljak, K., Hohlweg, W., Novak, P., & Zangger, K. (2011). Determining the orientation of drugs in receptors by solvent paramagnetic relaxation NMR spectroscopy. Proceedings of the Second World Conference on Physico-Chemical Methods in Drug Discovery and Development. Retrieved from https://www.bib.irb.hr/527060?rad=527060

Schrank, E., Kosol, S., Čuljak, K., Göbl, C., Zangger, K., & Novak, P. (2011). Deciphering interactions of macrolide antibiotics with membrane- mimetics by NMR spectroscopy. Proceedings of the Second World Conference on Physico-Chemical Methods in Drug Discovery and Development. Retrieved from https://www.bib.irb.hr/527071?rad=527071

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Awarded Doctoral Degree

Göbl, C. (2012). Paramagnetic relaxation enhancements in structure determination of proteins by NMR spectroscopy (PhD). Universität Graz, Graz, Austria. 97p. Retrieved from http://inis.iaea.org/search/search.aspx?orig_q=RN:44111672

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