Emily Hank

Department für Pharmazie
Ludwig-Maximilians-Universität München
Butenandtstraße 7
D-81377 München

Zi.Nr.: C1.050A
Tel.: +49 (0)89 2180 77927
Fax.: +49 (0)89 2180 77247
Mail: Emily.Hank@cup.lmu.de

 

Research Interest

TLX (human homologue of Drosophila tailless) is an orphan nuclear receptor that is mainly expressed in neural stem cells. Its link to neurodegenerative diseases and neurological disorders evokes our group’s interest for TLX as a pharmaceutical target. In order to explore the pharmacological potential and the medicinal chemistry of this nuclear receptor, a set of potent and selective tool compounds is needed. My current aim is to perform SAR studies on a recently discovered TLX lead agonist.

Publications

Hank, E. C.; Knümann, L.; López-García, U.; Kardanov, A.; Morozov, V.; Höfner, G.; Merk, D. Systematic optimization of fragment TLX ligands towards agonism and inverse agonism. J. Med. Chem.2026 DOI

Hank, E. C.; D'Arcy-Evans, N. D.; Scaletti, E. R.; Benitez-Buelga, C.; Wallner, O.; Ortis, F.; Zhou, K.; Meng, L.; Del Prado, A.; Calvo, P.; Almlöf, I.; Wiita, E.; Nierlin, K.; Kosenina, S.; Kramer, A.; Eddershaw, A.; Kehler, M.; Long, M.; Jemth, A-S.; Dawson, H.; Stewart, J.; Dickey, A.; Astorga, M. E.; Varga, M.; Homan, E. J.; Scobie, M.; Knapp, S.; Sastre, L.; Stenmark, P.; De Vega, M.; Helleday, T.; Michel, M. Nucleobase catalysts for the enzymatic activation of 8-oxoguanine DNA glycosylase 1. RSC Chem. Biol. 2026 DOI

Hank, E. C.; Sai, M.; Kasch, T.; Meijer, I.; Marschner, J. A.; Merk, D. Development of Tailless Homologue (TLX) Agonist Chemical Tools. J. Med. Chem.2024. DOI

Sai, M.; Hank, E. C.; Lewandowski, M.; Kasch, T.; Marschner, J. A.; Merk, D. Development of Potent and Selective Nurr1 Agonists from Amodiaquine By Scaffold Hopping and Fragment Growing. Commun. Chem., 2024, 7, 149. DOI

Michel, M.; Benítez-Buelga, C.; Calvo, P. A.; Hanna, B. M. F.; Mortusewicz, O.; Masuyer, G.; Davies, J.; Wallner, O.; Sanjiv, K.; Albers, J. J.; Castañeda-Zegarra, S.; Jemth, A.-S.; Visnes, T.; Sastre-Perona, A.; Danda, A. N.; Homan, E. J.; Marimuthu, K.; Zhenjun, Z.; Chi, C. N.; Sarno, A.; Wiita, E.; Nicolai, C. von; Komor, A. J.; Rajagopal, V.; Müller, S.; Hank, E. C.; Varga, M.; Scaletti, E. R.; Pandey, M.; Karsten, S.; Haslene-Hox, H.; Loevenich, S.; Marttila, P.; Rasti, A.; Mamonov, K.; Ortis, F.; Schömberg, F.; Loseva, O.; Stewart, J.; D'Arcy-Evans, N.; Koolmeister, T.; Henriksson, M.; Michel, D.; Ory, A. de; Acero, L.; Calvete, O.; Scobie, M.; Hertweck, C.; Vilotijevic, I.; Kalderén, C.; Osorio, A.; Perona, R.; Stolz, A.; Stenmark, P.; Berglund, U. W.; Vega, M. de; Helleday, T. Small-molecule activation of OGG1 increases oxidative DNA damage repair by gaining a new function. Science, 2022, 376, 1471–1476. DOI

Müller, C.; Hank, E.; Giera, M.; Bracher, F. Dehydrocholesterol Reductase 24 (DHCR24): Medicinal Chemistry, Pharmacology and Novel Therapeutic Options. Curr. Med. Chem., 2022, 29, 4005–4025. DOI