Chair of Biochemistry

    Gerling-Driessen, Ulla, Dr.

    Dr. Ulla Gerling-Driessen    

    Group: Molecular Oncology
    Phone: +49 931 - 31-84163
    E-mail: ulla.gerling-driessen@uni-wuerzburg.de
    Room: B110b








    Curriculum vitae


    Dr. Ulla Gerling-Driessen



    Project leader



    Chair of Biochemistry, Theodor-Boveri-Institute at the Biocentre
    University of Würzburg
    Am Hubland
    97074 Würzburg
    Phone +49 931 - 31 84163





    B.Sc. in Chemistry, Institute of Chemistry and Biochemistry,

    Freie Universität Berlin, Berlin, Germany



    M.Sc. in Chemistry, Institute of Chemistry and Biochemistry,

    Freie Universität Berlin, Berlin, Germany



    PhD in Bioorganic Chemistry, Institute of Chemistry and Biochemistry,

    Freie Universität Berlin, Berlin, Germany



    Postdoc in Biopolymer Chemistry at the Institute of Chemistry and Biochemistry, Freie Universität Berlin and the Institute of Biomaterial Science, Helmholtz-Zentrum Geesthacht, Berlin, Germany



    Postdoc in Chemical Glycobiology at the Department of Chemistry, Stanford University, Stanford, CA, USA


    Since 2019

    Project leader at the Department of Biochemistry,

    University of Würzburg, Würzburg, Germany


    Research Fields

    Chemical Glycobiology, Glycosylation in cancer immunotherapy, Congenital Disorders of Glycosylation


    2013: Student Travel Award for the 21st Winter Fluorine Conference 2013: PhD grade: summa cum laude

    2016: Postdoctoral Fellowship of the Deutsche Forschungsgemeinschaft (DFG)


    Selected Publications


    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, 1143-1155. § Contributed equally

    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, 73-80.

    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, 2394-2402.

    U. I. M. Gerling§, M.S. Miettinen§, B. Koksch; “Concluding the amyloid formation pathway from the size of the critical nucleus” ChemPhysChem, 2015, 16, 108-114.

    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.

    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, 177-186. § Contributed equally

    P. D. Rakowska, H. Jiang, S. Ray, A. Pyne, B. Lamarre, M. Carr, P. J. Judge, J. Ravi, U. I. M. Gerling, B. Koksch, G. J. Martyna, B. W. Hoogenboom, A. Watts, J. Crain, C. R. M. Grovenor, M. G. Ryadnov; “Nanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers” Proc. Natl. Acad. Sci. U.S.A. 2013, 110, 8918-8923.

    H. Erdbrink, I. Peuser, U. I. M. Gerling, D. Lentz, B. Koksch, C. Czekelius; “Conjugate hydrotrifluoromethylation of α, β -unsaturated acyl-oxazolidinones: synthesis of chiral fluorinated amino acids” Org. Biomol. Chem. 2012, 10, 8583-8586.

    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, 2135-2171. * Journal cover article

    R. Rezaei Araghi, C. Baldauf, U. I. M. Gerling, C. D. Cadicamo, B. Koksch; “A systematic study of fundamentals in a-helical coiled coil mimicry by alternating sequences of β- und γ-amino acids” Amino Acids, 2011, 41, 733-742.

    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, 10651-10661.

    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, 2988-96.

    A.Botev, L.M. Munter, R. Wenzel, L. Richter, V. Althoff, J. Ismer, U. Gerling, C. Weise, B. Koksch, P.W. Hildebrand, R. Bittl, G. Multhaup; “The Amyloid Precursor Protein C-Terminal Fragment C100 Occurs in Monomeric and Dimeric Stable Conformations and Binds γ-Secretase Modulators” Biochemistry, 2011, 50, 828-825.

    J.A. Falenski, U. Gerling, B. Koksch; “Multiple glycosylation of de novo designed alpha-helical coiled coil peptides” Bioorg. Med. Chem. 2010, 18, 3703-3706.


    Full list: https://scholar.google.de/citations?user=daHoyMAAAAAJ&hl=de&oi=ao

    Research profile

    Glycans are key players in many cellular processes. As abundant components on the cell surface, glycans are exposed to the environment, act as mediators of intercellular interactions and participate in the pathogen recognition by components of the immune system. Due to their crucial role in many important processes, abnormal glycosylation has been linked to the pathology of many diseases, such as the malignant transformation of cancer cells, certain neurodegenerative diseases and inflammation. As a non-templated, posttranslational modification, glycans are not amenable to investigations by traditional genetic techniques. Given their heterogenic nature, glycoprotein analysis faces technical challenges that require the development of new tools and strategies for a better investigation of these molecules. As a chemical biologist, I use chemical tools to address complex biological questions. I am particularly interested in elucidating the role of glycans in the pathology of diseases, such as cancer or certain genetic disorders of glycosylation that have been associated with abnormal glycosylation pattern.


    Glycosylation in Cancer

    Altered protein glycosylation has long been identified as a hallmark of cancer. Tumor immune evasion, tumor progression, metastatic spread and poor clinical prognosis have been linked to abnormal glycosylation pattern. However, the functional significance with respect to tumor progression and immune cell modulation are not well understood.

    The new established Cancer Therapy Research Center, integrated in the department of Biochemistry, is focusing on projects in molecular oncology with the goal of developing new technologies for cancer therapy. One concept is the use of tumor killing oncolytic viruses, which is based on tumor lysis by the virus followed by activation of the body’s own immune system to attack the tumor cells. Recent studies revealed that hiding the virus from the immune system by using certain cell carriers, significantly prolonged the life time of the virus and resulted in increased oncolysis and immune stimulation.

    Our goal is to understand the role of glycosylation in this process. In this context, we aim to elucidate glycosylation profiles in different stem, cancer and immune cells. Identifying the key players that support successful virus replication in cells and better understanding how altered surface glycosylation modulates the interaction with immune cells, will be the basis to improve the efficacy of stem cell-mediated delivery of oncolytic viruses and the successful development of cancer specific vaccines.


    Congenital Disorders of Glycosylation (CDGs)

    Congenital disorders of glycosylation (CDGs), are rare genetic diseases affecting enzymes involved in the assembly and processing of glycans. The clinical spectrum is broad, ranging from severe multisystemic phenotypes to symptoms restricted to specific organs. Today more than 100 district CDGs have been identified in humans, most of which affect the N-glycan biosynthesis, an essential process for the survival of all eukaryotes. However, little is known about the glycobiology underlying the pathology of CDGs, such as proteins and pathways that are impaired due to altered or truncated glycosylation.

    We aim to understand cause and consequences of altered protein glycosylation on a molecular level. Our goal is to explain the diverse clinical phenotypes in CDGs by linking aberrantly glycosylated proteins to impaired biological functions and pathways. We are investigating patient cells and generated knock out cell lines with a combination of multi-omics approaches and biochemical methods to identify proteins with impaired functions due to altered glycan structures. Thereby, we are elucidating new crucial functions of glycoproteins and unravel their role in essential biological pathways. The gain in this fundamental knowledge will contribute to better understand altered glycosylation pattern in other, more common diseases, such as cancer, neurodegenerative diseases and inflammation.


    Bioothogonal tool development for glycan analysis

    The analysis of glycans and glycoproteins is still very challenging. Bioorthogonal chemistry alleviates some of these problems by incorporating chemical handles into biomolecules and utilizing them to attach probes in a way that does not exhibit cross reactivity with the natural environment. To better analyze glycans and glycoproteins in our research, we constantly develop new bioorthogonal probes with a broad application spectrum. Our probes can be used for qualitative and quantitative analysis of glycoproteins and other biomolecules in multiple applications such as imaging, mass spectrometry, isolation and purification.