R. Hilgenfeld, J. Lei & L. Zhang:
The Structure of the Zika Virus Protease, NS2B/NS3pro.
Adv. Exp. Med. Biol. 1062, 131-145 (2018).

J. Lei, Y. Kusov & R. Hilgenfeld:
Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein.
Antiviral Res. 149, 58-74 (2018).

T. Schöne, L.L. Grimm, N. Sakai, L. Zhang, R. Hilgenfeld & T. Peters:
STD-NMR experiments identify a structural motif with novel second-site activity against West Nile virus NS2B-NS3 protease.
Antiviral Res. 146,174-183 (2017).

J. Lei & R. Hilgenfeld:
RNA-virus proteases counteracting host innate immunity.
FEBS Lett. 591, 3190-3210 (2017).

J. Kouretova, M.Z. Hammamy, A. Epp, K. Hardes, S. Kallis, L. Zhang, R. Hilgenfeld, R. Bartenschlager & T. Steinmetzer:
Effects of NS2B-NS3 protease and furin inhibition on West Nile and Dengue virus replication.
J. Enzyme Inhib. Med. Chem. 32, 712-721 (2017).

W. Rut, L. Zhang, P. Kasperkiewicz, M. Poreba, R. Hilgenfeld & M. Drąg:
Extended substrate specificity and first potent irreversible inhibitor/activity-based probe design for Zika virus NS2B-NS3 protease.
Antiviral Res. 139, 88-94 (2017).

C. Nitsche, L. Zhang, L.F. Weigel, J. Schilz, D. Graf, R. Bartenschlager, R. Hilgenfeld & C.D. Klein:
Peptide-Boronic Acid Inhibitors of Flaviviral Proteases: Medicinal Chemistry and Structural Biology.
J. Med. Chem. 60, 511-516 (2017).

R. Hilgenfeld:
Zika virus NS1, a pathogenicity factor with many faces.
EMBO J. 35, 2631-2633 (2016).

D. Becker, Z. Kaczmarska, C. Arkona, R. Schulz, C. Tauber, G. Wolber, R. Hilgenfeld, M. Coll & J. Rademann:
Irreversible inhibitors of the 3C protease of Coxsackie virus through templated assembly of protein-binding fragments.
Nat. Commun. 7,12761 (2016).

Y. Ma-Lauer, J. Carbajo-Lozoya, M.Y. Hein, M.A. Müller, W. Deng, J. Lei, B. Meyer, Y. Kusov, B. von Brunn, D.R. Bairad, S. Hünten, C. Drosten C, H. Hermeking, H. Leonhardt, M. Mann, R. Hilgenfeld & A. von Brunn:
p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PLpro via E3 ubiquitin ligase RCHY1.
Proc. Natl. Acad. Sci. USA, 113, 5192-5201 (2016).

J. Lei, G. Hansen, C. Nitsche, C. Klein, L. Zhang & R. Hilgenfeld:
Crystal structure of Zika virus NS2B-NS3 protease in complex with a boronate inhibitor.
Science, 353, 503-505 (2016).

J. Lei & R. Hilgenfeld:
Structural and mutational analysis of the interaction between the Middle-East respiratory syndrome coronavirus (MERS-CoV) papain-like protease and human ubiquitin.
Virol. Sin., 4, 288-299 (2016).

L. Sun, A. Meijer, M. Froeyen, L. Zhang, H.J. Thibaut, J. Baggen, S. George, J. Vernachio, F.J. van Kuppeveld, P. Leyssen, R. Hilgenfeld, J. Neyts & L. Delang:
Antiviral activity of broad-spectrum and enterovirus-specific inhibitors against clinical isolates of enterovirus D68.
Antimicrob. Agents Chemother. 59, 7782-7785 (2015).

Y. Kusov, J. Tan, E. Alvarez, L. Enjuanes & R. Hilgenfeld:
A G-quadruplex-binding macrodomain within the "SARS-unique domain" is essential for the activity of the SARS-coronavirus replication-transcription complex.
Virology 484, 313-322 (2015).

C. Lacroix, S. George, P. Leyssen, R. Hilgenfeld & J. Neyts:
The enterovirus 3C protease inhibitor SG85 efficiently blocks rhinovirus replication and is not cross-resistant with rupintrivir.
Antimicrob. Agents Chemother. 59, 5814-5818 (2015).

Z. Han, N. Sakai, L.H. Böttger, S. Klinke, J. Hauber, A.X. Trautwein & R. Hilgenfeld:
Crystal Structure of the Peroxo-diiron(III) Intermediate of Deoxyhypusine Hydroxylase, an Oxygenase Involved in Hypusination.
Structure 23, 882-892 (2015).

S.S. Jadav, B.N. Sinha, R. Hilgenfeld, B. Pastorino, X. de Lamballerie & V. Jayaprakash:
Thiazolidone derivatives as inhibitors of chikungunya virus.
Eur. J. Med. Chem. 89,172-178 (2015).

A. Shukla & R. Hilgenfeld:
Acquisition of new protein domains by coronaviruses: analysis of overlapping genes coding for proteins N and 9b in SARS coronavirus.
Virus Genes 50, 29-38 (2015).

J. Lei, J.R. Mesters, C. Drosten, S. Anemüller, Q. Ma & R. Hilgenfeld:
Crystal structure of the papain-like protease of MERS coronavirus reveals unusual, potentially druggable active-site features.
Antiviral Res. 109, 72-82 (2014).

L. van der Linden, R. Ulferts, S.B. Nabuurs, Y. Kusov, H. Liu, S. George, C. Lacroix, N. Goris, D. Lefebvre, K.H. Lanke, K. De Clercq, R. Hilgenfeld, J. Neyts & F.J. van Kuppeveld:
Application of a cell-based protease assay for testing inhibitors of picornavirus 3C proteases.
Antiviral Res. 103, 17-24 (2014).

J. Rocha-Pereira, M.S. Nascimento, Q. Ma, R. Hilgenfeld, J. Neyts & D. Jochmans:
The enterovirus protease inhibitor rupintrivir exerts broad-spectrum anti-norovirus activity and clears cells from the norovirus replicon.
Antimicrob. Agents Chemother. 58, 4675-4681 (2014).

D.X. Liu, T.S. Fung, K.K. Chong, A. Shukla & R. Hilgenfeld:
Accessory proteins of SARS-CoV and other coronaviruses.
Antiviral Res. 109, 97-109 (2014).

R. Hilgenfeld:
From SARS to MERS: Crystallographic studies on coronaviral proteases enable antiviral drug design.
FEBS J. 281, 4085-4096 (2014).

J. Tan, S. George, Y. Kusov, M. Perbandt, S. Anemüller, J.R. Mesters, H. Norder, B. Coutard, C. Lacroix, P. Leyssen, J. Neyts & R. Hilgenfeld:
3C protease of enterovirus 68: Structure-based design of Michael acceptor inhibitors and their broad-spectrum antiviral effects against picornaviruses.
J. Virol. 87, 4339-4351 (2013).

R. Hilgenfeld & M. Peiris:
From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses.
Antiviral Res. 100, 286–295 (2013).