Selected publications

In our lab we apply a broad range of computational tools to a variety of research projects including small molecule drug discovery, protein modelling, and the design of novel gene therapy approaches.

Teresa Kaserer

Additionally: ORCID.

(1) Austin M, Burschowsky D, Chan DTY, Jenkinson L, Haynes S, Diamandakis A, Seewooruthun C, Addyman A, Fiedler S, Ryman S, Whitehouse J, Slater LH, Hadjinicolaou AV, Gileadi U, Gowans E, Shibata Y, Barnard M, Kaserer T, Sharma P, Luheshi NM, Wilkinson RW, Vaughan TJ, Holt SV, Cerundolo V, Carr MD, Groves MAT. Structural and functional characterization of C0021158, a high-affinity monoclonal antibody that inhibits Arginase 2 function via a novel noncompetitive mechanism of action. mABs 2020;12(1):1801230. doi: 10.1080/19420862.2020.1801230.

This paper reports a novel Arg2 antibody for cancer therapy.

(2) Kostaras E,* Kaserer T,* Lazaro G, Heuss SF, Hussain A, Casado P, Hayes A, Yandim C, Palaskas N, Yu Y, Schwartz B, Raynaud F, Chung YL, Cutillas PR, Vivanco I. A systematic molecular and pharmacologic evaluation of AKT inhibitors reveals new insight into their biological activity. Br. J. Cancer 2020; 23:542-555. doi: 10.1038/s41416-020-0889-4.

In this paper, we systematically characterize clinically relevant AKT1 inhibitors.

(3) Weston M,* Kaserer T,* Wu A, Mouravlev A, Carpenter JC, Snowball A, Knauss S, von Schimmelmann M, During MJ, Lignani G, Schorge S, Young D, Kullmann DM, Lieb A. Olanzapine: a full and potent agonist at the hM4D(Gi) DREADD amenable to clinical translation of chemogenetics. Sci Adv 2019;eaaw1567. doi: 10.1126/sciadv.aaw1567.

In this paper, we identify olanzapine as a suitable drug for DREADD-based gene therapy approaches.

(4) Hagenbuchner J,* Obsilova V,* Kaserer T,* Kaiser N, Rass B, Psenakova K, Docekal V, Alblova M, Kohoutova K, Schuster D, Aneichyk T, Vesely J, Obexer P, Obsil T, Ausserlechner MJ. Modulating FOXO3 transcriptional activity by small, DBD-binding molecules. eLife 2019; e48876. doi: 10.7554/eLife.48876.

In this paper, we report the first FOXO3 inhibitor.

(5) Kaserer T,‡ Blagg J‡. Combining mutational signatures, clonal fitness, and drug affinity to define drug-specific resistance mutations in cancer. Cell Chem Biol 2018;25:1359-1371.e2. doi: 10.1016/j.chembiol.2018.07.013.

This paper reports a computational workflow to prospectively predict drug resistance mutations in cancer patients.

(6) Liu M,‡ Mallinger A, Tortorici M, Newbatt Y, Richards M, Mirza A, van Montfort RLM, Burke R, Blagg J,‡ Kaserer T‡. Evaluation of APOBEC3B recognition motifs by NMR reveals preferred substrates. ACS Chem Biol 2018;13:2427– 2432. doi: 10.1021/acschembio.8b00639.

In this paper, we identify DNA sequences prone to APOBEC-mediated mutation, potentially giving rise to resistance mutations.

(7) Kaserer T, Lantero A, Schmidhammer H, Spetea M, Schuster D. μ Opioid receptor: novel antagonists and structural modeling. Sci Rep 2016;6:21548. doi: 10.1038/srep21548.

This paper reports the identification and characterization of novel μ Opioid receptor antagonists.

(8) Kaserer T, Rigo R, Schuster P, Alcaro S, Sissi C, Schuster D. Optimized virtual screening workflow for the identification of novel G-quadruplex ligands. J Chem Inf Model 2016;53:484–500. doi: 10.1021/acs.jcim.5b00658.

This paper reports the identification and characterization of novel G-quadruplex ligands.

(9) Kaserer T, Höferl M, Müller K, Elmer S, Ganzera M, Jäger W, Schuster D. In silico predictions of drug-drug interactions caused by CYP1A2, 2C9 and 3A4 inhibition – a comparative study of virtual screening performance. Mol Inf 2015;34:431–457. doi: 10.1002/ minf.201400192.

In this paper, we identify compounds causing drug-drug interactions via inhibition of metabolic enzymes.

(10) Kaserer T, Temml V, Kutil Z, Vanek T, Landa P, Schuster D. Prospective performance evaluation of selected common virtual screening tools. Case study: cyclooxygenase (COX) 1 and 2. Eur J Med Chem 2015;96:445-457. doi: 10.1016/j. ejmech.2015.04.017.

In this paper, we report novel inhibitors of cyclooxygenases 1 and 2.