CRC1093 People - Ulla Gerling-Driessen

Dr. Ulla Gerling-Driessen

Associated member since December 2020

no picture 

Phone: +49 211 81-14788


Macromolecular Chemistry, HHU Düsseldorf

Research within the CRC1093 Supramolecular ligands for modulating protein interactions of the cytosolic enzyme NGLY1

Research summary follows soon

Professional career


Postdoctoral Researcher / Junior group leader at the Institute of Organic Chemistry and Macromolecular Chemistry, Heinrich-Heine-University Düsseldorf


Postdoctoral Researcher / Project leader at the Department of Biochemistry, Julius-Maximilians-University Würzburg


Postdoctoral Fellow with Prof. Dr. Carolyn Bertozzi (Department of Chemistry) at Stanford University, Palo Alto, CA, USA


Postdoctoral Researcher with Prof. Dr. Beate Koksch (Institute of Organic Chemistry) at Freie Universität Berlin and Prof. Dr. Rainer Haag (Institute of Biomaterial Science) at Helmholtz-Zentrum Geesthacht, Berlin-Teltow



PhD in Chemistry, Freie Universität Berlin


MSc in Chemistry, Freie Universität Berlin

Selected Publications

M. Santos de Freitasa, R. Rezaei Araghi, E. Brandenburg, J. Leitererd, F. Emmerling, K. Folmert, U. I. M. Gerling-Driessen, B. Bardiaux, C. Böttcher, K. Pagel, A. Diehl, H. v. Berlepsch, H. Oschkinat, B. Koksch: The protofilament architecture of a de novo designed coiled coil-based amyloidogenic peptide. J. Struct. Biol. 2018;203:263–272. doi: 10.1016/j.jsb.2018.05.009.

F. M. Tomlin*, U. I. M. Gerling-Driessen*, Y-C. Liu, R. A. Flynn, J. R. Vangala, C. S. Lentz, S Clauder-Muenster, P. Jakob, W. F. Mueller, D. Ordonez, M. Paulsen, N. Matsui, D. Foley, A. Rafalko, T. Suzuki, M. Bogyo, L. M. Steinmetz, S. K. Radhakrishnan, C. R. Bertozzi: Inhibition of NGLY1 inactivates the transcription factor Nrf1 and potentiates proteasome inhibitor cytotoxicity. ACS Cent. Sci. 2017;3(11):1143-1155. doi: 10.1021/acscentsci.7b00224.

J-S. Völler, M. Dulic, U. I. M. Gerling-Driessen, H. Biava, T. Baumann, N. Budisa, I. Gruic-Sovulj, B. Koksch: Discovery and Investigation of Natural Editing Function against Artificial Amino Acids in Protein Translation. ACS Cent. Sci. 2017;3(1):73-80. doi: 10.1021/acscentsci.6b00339.

U. I. M. Gerling-Driessen, N. Mujkic-Ninnemann, D. Ponader, D. Schöne, L. Hartmann, B. Koksch: Exploiting Oligo(amido amine) Backbones for the Multivalent Presentation of Coiled-Coil Peptides. Biomacromolecules 2015; 16(8):2394-2402. doi: 10.1021/acs.biomac.5b00634.

U. I. M. Gerling*, M.S. Miettinen*, B. Koksch: Concluding the amyloid formation pathway from the size of the critical nucleus. ChemPhysChem 2015;16(1):108-114. doi: 10.1002/cphc.201402400.

U. I. M. Gerling, M. Salwiczek, C. D. Cadicamo, H. Erdbrink, C. Czekelius, S. L. Grage, P. Wadhwani, A. S. Ulrich, M. Behrends, G. Haufe, B. Koksch: Fluorinated amino acids in amyloid formation: a symphony of size, hydrophobicity, and α-helix propensity. Chem. Sci. 2014;5:819-830. doi: 10.1039/C3SC52932K.

J. Maity*, U. I. M. Gerling*, S. Vukelić, A. Schäfer, B. Koksch: Proline-glutamate chimera’s side chain conformation directs the type of β-hairpin structure. Amino Acids 2014;46(1):177-186. doi: 10.1007/s00726-013-1610-1.

M. Salwiczek, E. K. Nyakatura, U. I. M. Gerling, S. Ye, B. Koksch: Fluorinated Amino Acids: Compatibility with native protein structures and effects on protein-protein interactions. Chem. Soc Rev. 2012;41(6):2135-2171. doi: 10.1039/c1cs15241f Journal cover.

E. Brandenburg, H. v. Berlepsch, U. I. M. Gerling, C. Böttcher, B. Koksch: Inhibition of Amyloid Aggregation by Formation of Helical Assemblies. Chem. Eur. J. 2011;17(38):10651-10661. doi: 10.1002/chem.201100670.

U. I. M. Gerling, E. Brandenburg, H.v. Berlepsch, K. Pagel, B. Koksch: Structure Analysis of an Amyloid-Forming Model Peptide by a Systematic Glycine and Proline Scan. Biomacromolecules 2011;12(8):2988-96. doi: 10.1021/bm200587m.