Profile photoJan Steyaert, PhD
Full Professor & Francqui Research Professor, Faculty of Sciences and Bioengineering Sciences, VUB
Director, Department of Structural Biology Brussels, VUB
Acting Director, Structural Biology Research Center, VIB
Founder & CSO, ConFotherapeutics NV, www.ConFotherapeutics.com

Expertise

Last years, the Steyaert lab pioneered the use of nanobodies for chaperone-assisted X-ray crystallography (www.steyaertlab.eu), aiming at the highest hanging fruits of structural biology including membrane proteins, amyloidogenic proteins, and now also (transient) multiprotein complexes. The elucidation of the first GPCR structures in the agonist-bound active state demonstrate the power of Nanobodies to stabilize G protein coupled receptor conformational states including transmembrane signalling complexes. Recent work focusses on exploiting the conformational complexity of therapeutic targets for Nanobody-enabled drug discovery.

Research output

Modular transient nanoclustering of activated β2-adrenergic receptors revealed by single-molecule tracking of conformation-specific nanobodies

Gormal, R. S., Padmanabhan, P., Kasula, R., Bademosi, A. T., Coakley, S., Giacomotto, J., Blum, A., Joensuu, M., Wallis, T. P., Lo, H. P., Budnar, S., Rae, J., Ferguson, C., Bastiani, M., Thomas, W. G., Pardon, E., Steyaert, J., Yap, A. S., Goodhill, G. J., Hilliard, M. A. & 2 others, Parton, R. G. & Meunier, F. A., 19 Nov 2020, In : Proceedings of the National Academy of Sciences of the United States of America.

Allosteric modulation of the GTPase activity of a bacterial LRRK2 homolog by conformation-specific Nanobodies

Leemans, M., Galicia, C., Deyaert, E., Daems, E., Krause, L., Paesmans, J., Pardon, E., Steyaert, J., Kortholt, A., Sobott, F., Klostermeier, D. & Versees, W., Apr 2020, In : Biochemical Journal. 477, 7, p. 1203-1218 16 p.

Nanobody-enabled monitoring of kappa opioid receptor states

Che, T., English, J., Krumm, B. E., Kim, K., Pardon, E., Olsen, R. H. J., Wang, S., Zhang, S., Diberto, J. F., Sciaky, N., Carroll, F. I., Steyaert, J., Wacker, D. & Roth, B. L., 2 Mar 2020, In : Nature Communications. 11, 1, 12 p., 1145.

Structure of the G protein chaperone and guanine nucleotide exchange factor Ric-8A bound to Gαi1

McClelland, L. J., Zhang, K., Mou, T-C., Johnston, J., Yates-Hansen, C., Li, S., Thomas, C. J., Doukov, T. I., Triest, S., Wohlkonig, A., Tall, G. G., Steyaert, J., Chiu, W. & Sprang, S. R., 26 Feb 2020, In : Nature Communications. 11, 1, 1077.

A Lipid Recognition Site at a Transmembrane Helix Kink Shapes the Agonist Response of a Pentameric Ligand-gated Ion Channel

Baenziger, J. E., Henault, C. M., Govaerts, C., Estrada, A., Lynch, J., Bertrand, D., Pardons, E., Evans, G., Woods, K. N., Elberson, B. W., Cuello, L. G., Brannigan, G. H., Nury, H., Steyaert, J. & Ulens, C., 7 Feb 2020, In : Biophysical Journal. 118, 3, p. 191A-191A

Ric8A-G alpha, a Complex Structure of a Guanine Nucleotide Exchange Factor

McClelland, L. J., Zhang, K., Mou, T-C., Johnston, J., Yates-Hansen, C., Steyaert, J., Chiu, W. & Sprang, S., 7 Feb 2020, In : Biophysical Journal. 118, 3, p. 335A-335A

Editorial overview: Engineered proteins as tools in structural biology

Steyaert, J. & Yeates, T. O., Feb 2020, In : Current Opinion in Structural Biology. 60, p. V-VI

Nanobodies to study protein conformational states

Uchański, T., Pardon, E. & Steyaert, J., Feb 2020, In : Current Opinion in Structural Biology. 60, p. 117-123 7 p.

Modulation of the Erwinia ligand-gated ion channel (ELIC) and the 5-HT3 receptor via a common vestibule site

Brams, M., Govaerts, C., Kambara, K., Price, K. L., Spurny, R., Gharpure, A., Pardon, E., Evans, G. L., Bertrand, D., Lummis, S. C., Hibbs, R. E., Steyaert, J. & Ulens, C., 28 Jan 2020, In : eLife. 9, e51511.

Discussions on the quality of antibodies are no reason to ban animal immunization

Custers, R. & Steyaert, J., 2020, In : EMBO Reports. p. e51761

Diversity in kinetics correlated with structure in nano body-stabilized LacY

Kumar, H., Finer-Moore, J., Smirnova, I., Kasho, V., Pardon, E., Steyaert, J., Kaback, H. R. & Stroud, R. M., 2020, In : PLOS ONE. 15, 5, 14 p., e0232846.

The G-Protein Rab5A Activates VPS34 Complex II, a Class III PI3K, by a Dual Regulatory Mechanism

Buckles, T. C., Ohashi, Y., Tremel, S., McLaughlin, S. H., Pardon, E., Steyaert, J., Gordon, M. T., Williams, R. L. & Falke, J. J., 2020, In : Biophysical Journal.

Structural evidence for the critical role of the prion protein hydrophobic region in forming an infectious prion

Abskharon, R., Wang, F., Wohlkonig, A., Ruan, J., Soror, S., Giachin, G., Pardon, E., Zou, W., Legname, G., Ma, J. & Steyaert, J., 9 Dec 2019, In : PLoS Pathogens. 15, 12, p. e1008139 e1008139.

Structure of an endosomal signaling GPCR-G protein-beta-arrestin megacomplex

Steyaert, J., 18 Nov 2019, In : Nature Structural and Molecular Biology. 26, 12, p. 1123-+ 23 p.

Structure of S-layer protein Sap reveals a mechanism for therapeutic intervention in anthrax

Fioravanti, A., Van Hauwermeiren, F., Van der Verren, S. E., Jonckheere, W., Goncalves, A., Pardon, E., Steyaert, J., De Greve, H., Lamkanfi, M. & Remaut, H., Nov 2019, In : Nature Microbiology. 4, p. 1805–1814 10 p.

A lipid site shapes the agonist response of a pentameric ligand-gated ion channel

Hénault, C. M., Govaerts, C., Spurny, R., Brams, M., Estrada-Mondragon, A., Lynch, J., Bertrand, D., Pardon, E., Evans, G. L., Woods, K., Elberson, B. W., Cuello, L. G., Brannigan, G., Nury, H., Steyaert, J., Baenziger, J. E. & Ulens, C., 7 Oct 2019, In : Nature Chemical Biology. 15, p. 1156–1164 8 p.

Structures of influenza A virus RNA polymerase offer insight into viral genome replication

Fan, H., Walker, A. P., Carrique, L., Keown, J. R., Serna Martin, I., Karia, D., Sharps, J., Hengrung, N., Pardon, E., Steyaert, J., Grimes, J. M. & Fodor, E., 12 Sep 2019, In : Nature. 537, p. 287-290 4 p.

The morphogen Sonic hedgehog inhibits its receptor Patched by a pincer grasp mechanism

Rudolf, A. F., Kinnebrew, M., Kowatsch, C., Ansell, T. B., El Omari, K., Bishop, B., Pardon, E., Schwab, R. A., Malinauskas, T., Qian, M., Duman, R., Covey, D. F., Steyaert, J., Wagner, A., Sansom, M. S. P., Rohatgi, R. & Siebold, C., 4 Sep 2019, In : Nature Chemical Biology. 15, 10, p. 975-982 8 p.

Mechanims of activation of the mu-opoid and the vasopressin V2 receptors seen by liquid NMR

Demene, H., Sounier, R., Laeremans, T., Orcel, H., Steyaert, J., Manglik, A., Kobilka, B., Mouillac, B. & Granier, S., Jul 2019, In : European Biophysics Journal. 48, p. S125-S125

Domain-interface dynamics of CFTR revealed by stabilizing nanobodies

Sigoillot, M., Overtus, M., Grodecka, M., Scholl, D., Garcia-Pino, A., Laeremans, T., He, L., Pardon, E., Hildebrandt, E., Urbatsch, I., Steyaert, J., Riordan, J. R. & Govaerts, C., 14 Jun 2019, In : Nature Communications. 10, 1, 12 p., 2636.

Interrogating dense ligand chemical space with a forward-synthetic library

Chevillard, F., Stotani, S., Karawajczyk, A., Hristeva, S., Pardon, E., Steyaert, J., Tzalis, D. & Kolb, P., 4 Jun 2019, In : Proceedings of the National Academy of Sciences of the United States of America. 166, 23, p. 11496-11501 6 p.

L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction

Errasti-Murugarren, E., Fort, J., Bartoccioni, P., Díaz, L., Pardon, E., Carpena, X., Espino-Guarch, M., Zorzano, A., Ziegler, C., Steyaert, J., Fernández-Recio, J., Fita, I. & Palacín, M., 18 Apr 2019, In : Nature Communications. 10, 1, 12 p., 1807.

Structures of ligand-occupied β-Klotho complexes reveal a molecular mechanism underlying endocrine FGF specificity and activity

Kuzina, E. S., Ung, P. M-U., Mohanty, J., Tome, F., Choi, J., Pardon, E., Steyaert, J., Lax, I., Schlessinger, A., Schlessinger, J. & Lee, S., 16 Apr 2019, In : Proceedings of the National Academy of Sciences of the United States of America. 116, 16, p. 7819-7824 6 p.

Structural insights into the activation of metabotropic glutamate receptors

Koehl, A., Hu, H., Feng, D., Sun, B., Zhang, Y., Robertson, M. J., Chu, M., Kobilka, T. S., Laermans, T., Steyaert, J., Tarrasch, J., Dutta, S., Fonseca, R., Weis, W. I., Mathiesen, J. M., Skiniotis, G. & Kobilka, B. K., 7 Feb 2019, In : Nature. 566, 7742, p. 79–84 6 p.

Cryo-EM structure of the human α1β3γ2 GABAA receptor in a lipid bilayer

Laverty, D., Desai, R., Uchański, T., Masiulis, S., Stec, W. J., Malinauskas, T., Zivanov, J., Pardon, E., Steyaert, J., Miller, K. W. & Aricescu, A. R., 24 Jan 2019, In : Nature. 565, 7740, p. 516-520 5 p.

Cryo-EM structure of the human α1β3γ2 GABAA receptor in a lipid bilayer

Laverty, D., Desai, R., Uchanski, T., Masiulis, S., Stec, W. J., Malinauskas, T., Zivanov, J., Pardon, E., Steyaert, J., Miller, K. W. & Aricescu, A. R., 24 Jan 2019, In : Nature. 565, 7740, p. 516-520 5 p.

GABAA receptor signalling mechanisms revealed by structural pharmacology

Masiulis, S., Desai, R., Uchański, T., Serna Martin, I., Laverty, D., Karia, D., Malinauskas, T., Zivanov, J., Pardon, E., Kotecha, A., Steyaert, J., Miller, K. W. & Aricescu, A. R., 24 Jan 2019, In : Nature. 565, 7740, p. 454-459 6 p.

The Molecular Mechanism of Transport by the Mitochondrial ADP/ATP Carrier

Ruprecht, J. J., King, M. S., Zögg, T., Aleksandrova, A. A., Pardon, E., Crichton, P. G., Steyaert, J. & Kunji, E. R. S., 24 Jan 2019, In : Cell. 176, 3, p. 435-447.e15 13 p.

An improved yeast surface display platform for the screening of nanobody immune libraries

Uchański, T., Zögg, T., Yin, J., Yuan, D., Wohlkönig, A., Fischer, B., Rosenbaum, D. M., Kobilka, B. K., Pardon, E. & Steyaert, J., 23 Jan 2019, In : Scientific Reports - Nature. 9, 1, 12 p., 382.

An improved yeast surface display platform for the screening of nanobody immune libraries

Uchański, T., Zögg, T., Yin, J., Yuan, D., Wohlkönig, A., Fischer, B., Rosenbaum, D. M., Kobilka, B. K., Pardon, E. & Steyaert, J., 23 Jan 2019, In : Scientific Reports - Nature. 9, 1, p. 1-12 12 p., 382.

Structure and nucleotide-induced conformational dynamics of the Chlorobium tepidum Roco protein

Deyaert, E., Leemans, M., Singh, R. K., Gallardo, R., Steyaert, J., Kortholt, A., Lauer, J. & Versées, W., 15 Jan 2019, In : Biochemical Journal. 476, 1, p. 51-66 16 p.

Structure of Prototypic Peptide Transporter DtpA from E. coli in Complex with Valganciclovir Provides Insights into Drug Binding of Human PepT1

Ural-Blimke, Y., Flayhan, A., Strauss, J., Rantos, V., Bartels, K., Nielsen, R., Pardon, E., Steyaert, J., Kosinski, J., Quistgaard, E. M. & Löw, C., 15 Jan 2019, In : Journal of the American Chemical Society. 141, 6, p. 2404–2412 9 p.

GABAA receptor signalling mechanisms revealed by structural pharmacology

Masiulis, S., Desai, R., Uchanski, T., Serna Martin, I., Laverty, D., Karia, D., Malinauskas, T., Zivanov, J., Pardon, E., Kotecha, A., Steyaert, J., Miller, K. W. & Aricescu, A. R., 2 Jan 2019, In : Nature. 565, 7740, p. 454-459 6 p.

Characterization and structure determination of a llama-derived nanobody targeting the J-base binding protein 1

van Beusekom, B., Heidebrecht, T., Adamopoulos, A., Fish, A., Pardon, E., Steyaert, J., Joosten, R. P. & Perrakis, A., 1 Nov 2018, In : Acta Crystallographica Section F - Structural Biology Communications. 74, Pt 11, p. 690-695 6 p.

Structural insights into binding specificity, efficacy and bias of a β 2AR partial agonist

Masureel, M., Zou, Y., Picard, L-P., van der Westhuizen, E., Mahoney, J. P., Rodrigues, J. P. G. L. M., Mildorf, T. J., Dror, R. O., Shaw, D. E., Bouvier, M., Pardon, E., Steyaert, J., Sunahara, R. K., Weis, W. I., Zhang, C. & Kobilka, B. K., Nov 2018, In : Nature Chemical Biology. 14, 11, p. 1059-1066 8 p.

Structural insights into binding specificity, efficacy and bias of a β2AR partial agonist.

Masureel, M., Zou, Y., Picard, LP., van, D. W. E., Mahoney, JP., Rodrigues, JPGLM., Mildorf, TJ., Dror, RO., Shaw, DE., Bouvier, M., Pardon, E., Steyaert, J. & Kobilka, BK., Oct 2018, In : Nature Chemical Biology. 14, p. 1059–1066 8 p.

Use of conformation and domain specific nanobodies to elucidate the working mechanism and structure of LRRK2 and homologous Roco proteins.

Leemans, M., Singh, R. K., Deyaert, E., Steyaert, J., Pardon, E., Gloeckner, C. J., Kortholt, A. & Versees, W., 3 Sep 2018.

Crystal Structure of a ligand-bound LacY-Nanobody Complex

Kumar, H., Finer-Moore, J. S., Jiang, X., Smirnova, I., Kasho, V., Pardon, E., Steyaert, J., Kaback, H. R. & Stroud, R. M., 28 Aug 2018, In : Proceedings of the National Academy of Sciences of the United States of America. 115, 35, p. 8769-8774 6 p.

Crystal structure of human Mediator subunit MED23

Monté, D., Clantin, B., Dewitte, F., Lens, Z., Rucktooa, P., Pardon, E., Steyaert, J., Verger, A. & Villeret, V., 23 Aug 2018, In : Nature Communications. 9, 1, p. 3389-3389 3389.

Mutational analysis of the extracellular disulphide bridges of the atypical chemokine receptor ACKR3/CXCR7 uncovers multiple binding and activation modes for its chemokine and endogenous non-chemokine agonists

Szpakowska, M., Meyrath, M., Reynders, N., Counson, M., Hanson, J., Steyaert, J. & Chevigné, A., Jul 2018, In : Biochemical Pharmacology. 153, p. 299-309 11 p.

Characterisation and structure determination of a llama-derived nanobody targeting the J-base binding protein 1

Beusekom, B. V., Heidebrecht, T., Adamopoulos, A., Fish, A., Pardon, E., Steyaert, J., Joosten, R. P. & Perrakis, A., 7 Jun 2018

A Genetically Encoded Biosensor Reveals Location Bias of Opioid Drug Action

Stoeber, M., Jullié, D., Lobingier, B. T., Laeremans, T., Steyaert, J., Schiller, P. W., Manglik, A. & von Zastrow, M., 6 Jun 2018, In : Neuron. 98, 5, p. 963-976.e5 14 p.

Targeting G protein-coupled receptor signaling at the G protein level with a selective nanobody inhibitor

Gulati, S., Jin, H., Masuho, I., Orban, T., Cai, Y., Pardon, E., Martemyanov, K. A., Kiser, P. D., Stewart, P. L., Ford, C. P., Steyaert, J. & Palczewski, K., 18 May 2018, In : Nature Communications. 9, 1, p. 1996 15 p., 1996.

Nanobody-Enabled Reverse Pharmacology on G-Protein-Coupled Receptors

Pardon, E., Betti, C., Laeremans, T., Chevillard, F., Guillemyn, K., Kolb, P., Ballet, S. & Steyaert, J., 4 May 2018, In : Angewandte Chemie International Edition. 57 , 19, p. 5292-5295 4 p.

Binding Specificities of Nanobody•Membrane Protein Complexes obtained from Chemical Cross-linking and High-Mass MALDI Mass Spectrometry

Köhler, M., Neff, C., Perez, C., Brunner, C., Pardon, E., Steyaert, J., Schneider, G., Locher, K. P. & Zenobi, R., 17 Apr 2018, In : Analytical Chemistry. 90 , 8, p. 5306–5313 8 p.

Development by Genetic Immunization of Monovalent Antibodies Against Human Vasoactive Intestinal Peptide Receptor 1 (VPAC1), New Innovative, and Versatile Tools to Study VPAC1 Receptor Function

Peyrassol, X., Laeremans, T., Lahura, V., Debulpaep, M., El Hassan, H., Steyaert, J., Parmentier, M. & Langer, I., 5 Apr 2018, In : Frontiers in Endocrinology. 9, APR, 13 p., 153.

ALLOSTERIC MODULATION OF THE PENTAMERIC LIGAND-GATED ION CHANNEL ELIC BY FUNCTIONALLY ACTIVE NANOBODIES

Ulens, C., Brains, M., De Peuter, H., Spurny, R., Pardon, E., Bertrand, D., Steyaert, J. & Govaerts, C., Apr 2018, In : The FASEB Journal. 32, 1, issue 1 supplement.

Binding-Site Compatible Fragment Growing Applied to the Design of β2-Adrenergic Receptor Ligands

Chevillard, F., Rimmer, H., Betti, C., Pardon, E., Ballet, S., van Hilten, N., Steyaert, J., Diederich, W. E. & Kolb, P., 8 Feb 2018, In : Journal of Medicinal Chemistry. 61, 3, p. 1118-1129 12 p.

Allosteric Modulation of the Pentameric Ligand-Gated Ion Channel ELIC by Functionally Active Nanobodies

Brams, M., De Peuter, H., Spurny, R., Pardon, E., Bertrand, D., Steyaert, J., Govaerts, C. & Ulens, C., 2 Feb 2018, In : Biophysical Journal. 114, 3, p. 298A-298A 1 p.

Structures of β-klotho reveal a 'zip code'-like mechanism for endocrine FGF signalling

Lee, S., Choi, J., Mohanty, J., Sousa, L. P., Tome, F., Pardon, E., Steyaert, J., Lemmon, M. A., Lax, I. & Schlessinger, J., 25 Jan 2018, In : Nature. 553, 7689, p. 501–505 5 p.

Structure of the Nanobody-Stabilized Active State of the Kappa Opioid Receptor

Che, T., Majumdar, S., Zaidi, S. A., Ondachi, P., McCorvy, J. D., Wang, S., Mosier, P. D., Uprety, R., Vardy, E., Krumm, B. E., Han, G. W., Lee, M-Y., Pardon, E., Steyaert, J., Huang, X-P., Strachan, R. T., Tribo, A. R., Pasternak, G. W., Carroll, F. I., Stevens, R. C. & 4 others, Cherezov, V., Katritch, V., Wacker, D. & Roth, B. L., 11 Jan 2018, In : Cell. 172, 1-2, p. 55-67 12 p., 55-67.e15.

Challenges in the Structural-Functional Characterization of Multidomain, Partially Disordered Proteins CBP and p300: Preparing Native Proteins and Developing Nanobody Tools

Bekesi, A., Abdellaoui, S., Holroyd, N., Van Delm, W., Pardon, E., Pauwels, J., Gevaert, K., Steyaert, J., Derveaux, S., Borysik, A. & Tompa, P., 2018, In : Methods in Enzymology. 611, p. 607-675 69 p.

Structure of PINK1 in complex with its substrate ubiquitin

Schubert, A. F., Gladkova, C., Pardon, E., Wagstaff, J. L., Freund, S. M. V., Steyaert, J., Maslen, S. L. & Komander, D., 7 Dec 2017, In : Nature. 552, 7683, p. 51-56 6 p.

Structural basis for GABAA receptor potentiation by neurosteroids

Miller, P. S., Scott, S., Masiulis, S., De Colibus, L., Pardon, E., Steyaert, J. & Aricescu, A. R., Nov 2017, In : Nature Structural and Molecular Biology. 24, 11, p. 986-992 7 p.

Soluble polymorphic bank vole prion proteins induced by co-expression of quiescin sulfhydryl oxidase in E. coli and their aggregation behaviors

Abskharon, R., Dang, J., Elfarash, A., Wang, Z., Shen, P., Zou, L. S., Hassan, S., Wang, F., Fujioka, H., Steyaert, J., Mulaj, M., Surewicz, W. K., Castilla, J., Wohlkonig, A. & Zou, W-Q., 4 Oct 2017, In : Microbial Cell Factories. 16, 1, 11 p., 170.

Crystallographic and biochemical characterization of the dimeric architecture of site-2 protease

Schacherl, M., Gompert, M., Pardon, E., Lamkemeyer, T., Steyaert, J. & Baumann, U., Oct 2017, In : Biochimica et Biophysica Acta. 1859, 10, p. 1859-1871 13 p.

Discovery, Structure-Activity Relationship, and Binding Mode of an Imidazo[1,2-a]pyridine Series of Autotaxin Inhibitors

Joncour, A., Desroy, N., Housseman, C., Bock, X., Bienvenu, N., Cherel, L., Labeguere, V., Peixoto, C., Annoot, D., Lepissier, L., Heiermann, J., Hengeveld, W. J., Pilzak, G., Monjardet, A., Wakselman, E., Roncoroni, V., Le Tallec, S., Gallen, R., David, C., Vandervoort, N. & 14 others, Christophe, T., Conrath, K., Jans, M., Wohlkonig, A., Soror, S., Steyaert, J., Touitou, R., Fleury, D., Vercheval, L., Mollat, P., Triballeau, N., van der Aar, E., Brys, R. & Heckmann, B., 14 Sep 2017, In : Journal of Medicinal Chemistry. 60, 17, p. 7371-7392 22 p.

Crystal structure of the pentameric ligand-gated ion channel ELIC in complex with a nanobody active as an allosteric modulator

Brams, M., Spurny, R., Price, K., Pardon, E., Bertrand, D., Lummis, S., Steyaert, J., Govaerts, C. & Ulens, C., Sep 2017, In : FEBS Journal. 284, p. 23-23

Generation and Characterization of Anti-VGLUT Nanobodies Acting as Inhibitors of Transport

Schenck, S., Kunz, L., Sahlender, D., Pardon, E., Geertsma, E. R., Savtchouk, I., Suzuki, T., Neldner, Y., Štefanić, S., Steyaert, J., Volterra, A. & Dutzler, R., 1 Aug 2017, In : Biochemistry. 56, 30, p. 3962-3971 10 p.

Leishmania donovani tyrosyl-tRNA synthetase structure in complex with a tyrosyl adenylate analog and comparisons with human and protozoan counterparts

Barros-Álvarez, X., Kerchner, K. M., Koh, C. Y., Turley, S., Pardon, E., Steyaert, J., Ranade, R. M., Gillespie, J. R., Zhang, Z., Verlinde, C. L. M. J., Fan, E., Buckner, F. S. & Hol, W. G. J., 31 Jul 2017, In : Biochimie. 138, p. 124-136 13 p.

Rational Design of Nanobody80 Loop Peptidomimetics: Towards Biased β 2 Adrenergic Receptor Ligands

Martin, C., Moors, S. L. C., Danielsen, M., Betti, C., Fabris, C., Pedersen, D. S., Pardon, E., Peyressatre, M., Feher, K., Martins, J. C., Mathiesen, J. M., Morris, M. C., Devoogdt, N., Caveliers, V., De Proft, F., Steyaert, J. & Ballet, S., 18 Jul 2017, In : Chemistry - a European Journal. 23, 40, p. 9632-9640 9 p.

Antibodies targeting G protein-coupled receptors: Recent advances and therapeutic challenges

Ayoub, M. A., Crépieux, P., Koglin, M., Parmentier, M., Pin, J-P., Poupon, A., Reiter, E., Smit, M., Steyaert, J., Watier, H. & Wilkinson, T., Jul 2017, In : mAbs. 9, 5, p. 735-741 7 p.

Structural analysis of the interaction between spiroisoxazoline SMARt-420 and the Mycobacterium tuberculosis repressor EthR2

Wohlkönig, A., Remaut, H., Moune, M., Tanina, A., Meyer, F., Desroses, M., Steyaert, J., Willand, N., Baulard, A. R. & Wintjens, R., 27 May 2017, In : Biochemical and Biophysical Research Communications. 487, 2, p. 403-408 6 p.

A specific nanobody prevents amyloidogenesis of D76N β2-microglobulin in vitro and modifies its tissue distribution in vivo

Raimondi, S., Porcari, R., Mangione, P. P., Verona, G., Marcoux, J., Giorgetti, S., Taylor, G. W., Ellmerich, S., Ballico, M., Zanini, S., Pardon, E., Al-Shawi, R., Simons, J. P., Corazza, A., Fogolari, F., Leri, M., Stefani, M., Bucciantini, M., Gillmore, J. D., Hawkins, P. N. & 6 others, Valli, M., Stoppini, M., Robinson, C. V., Steyaert, J., Esposito, G. & Bellotti, V., 21 Apr 2017, In : Scientific Reports - Nature. 7, p. 46711 46711.

Structural basis of inhibition of lipid-linked oligosaccharide flippase PglK by a conformational nanobody

Perez, C., Köhler, M., Janser, D., Pardon, E., Steyaert, J., Zenobi, R. & Locher, K. P., 19 Apr 2017, In : Scientific Reports - Nature. 7, p. 46641 46641.

Distinct conformations of GPCR-β-arrestin complexes mediate desensitization, signaling, and endocytosis

Cahill, T. J., Thomsen, A. R. B., Tarrasch, J. T., Plouffe, B., Nguyen, A. H., Yang, F., Huang, L-Y., Kahsai, A. W., Bassoni, D. L., Gavino, B. J., Lamerdin, J. E., Triest, S., Shukla, A. K., Berger, B., Little, J., Antar, A., Blanc, A., Qu, C-X., Chen, X., Kawakami, K. & 7 others, Inoue, A., Aoki, J., Steyaert, J., Sun, J-P., Bouvier, M., Skiniotis, G. & Lefkowitz, R. J., 7 Mar 2017, In : Proceedings of the National Academy of Sciences of the United States of America. 114, 10, p. 2562-2567 6 p.

Structural and biochemical characterization of the nucleoside hydrolase from C. elegans reveals the role of two active site cysteine residues in catalysis

Singh, R. K., Steyaert, J. & Versées, W., 6 Mar 2017, In : Protein Science. 26, 5, p. 985-996 12 p.

Nanobodies to Study G Protein-Coupled Receptor Structure and Function

Manglik, A., Kobilka, B. K. & Steyaert, J., 5 Jan 2017, In : Annual Review of Pharmacology and Toxicology. 57, p. 19-37 19 p.

Quiescin-sulfhydryl oxidase inhibits prion formation in vitro

Zhan, Y-A., Abskharon, R., Li, Y., Yuan, J., Zeng, L., Dang, J., Martinez, M. C., Wang, Z., Mikol, J., Lehmann, S., Bu, S., Steyaert, J., Cui, L., Petersen, R. B., Kong, Q., Wang, G-X., Wohlkonig, A. & Zou, W-Q., 11 Dec 2016, In : Aging (Albany NY). 8, 12, p. 3419-3429 10 p.

Internalized Receptor for Glucose-dependent Insulinotropic Peptide stimulates adenylyl cyclase on early endosomes

Ismail, S., Gherardi, M-J., Froese, A., Zanoun, M., Gigoux, V., Clerc, P., Gaits-Iacovoni, F., Steyaert, J., Nikolaev, V. O. & Fourmy, D., 15 Nov 2016, In : Biochemical Pharmacology. 120, p. 33-45 12 p.

Crystal structure of a LacY-nanobody complex in a periplasmic-open conformation

Jiang, X., Smirnova, I., Kasho, V., Wu, J., Hirata, K., Ke, M., Pardon, E., Steyaert, J., Yan, N. & Kaback, H. R., 1 Nov 2016, In : Proceedings of the National Academy of Sciences of the United States of America. 113, 44, p. 12420-12425 6 p.

Thermodynamics of Nanobody Binding to Lactose Permease

Hariharan, P., Andersson, M., Jiang, X., Pardon, E., Steyaert, J., Kaback, H. R. & Guan, L., 26 Oct 2016, In : Biochemistry. 55, 42, p. 5917-5926 9 p.

ASSESSMENT OF CFTR THERMAL STABILITY BEFORE AND AFTER PURIFICATION

He, L., Aleksandrov, L., Jensen, T., Sigoillot, M., Kousouros, J., Cui, L., Overtus, M., Grodecka, M., Laeremans, T., Pardon, E., Steyaert, J., Govaerts, C. & Riordan, J. R., Oct 2016, In : Pediatric Pulmonology. 51, p. 197-197

Sortase A-mediated site-specific labeling of camelid single-domain antibody-fragments: a versatile strategy for multiple molecular imaging modalities

Massa, S., Vikani, N., Betti, C., Ballet, S., Vanderhaegen, S., Steyaert, J., Descamps, B., Vanhove, C., Bunschoten, A., van Leeuwen, F. W. B., Hernot, S., Caveliers, V., Lahoutte, T., Muyldermans, S., Xavier, C. & Devoogdt, N., Sep 2016, In : Contrast Media & Molecular Imaging. 11, 5, p. 328-339

TOWARDS B-ARRESTIN BIASED B2AR LIGANDS: RATIONAL DESIGN OF NANOBODY LOOP MIMETICS

Martin, C., Betti, C., Fabris, C., Mathiesen, J. M., Pardon, E., Peyressatre, M., Moors, S., De Proft, F., Feher, K., Martins, J., Morris, M. C., Devoogdt, N., Caveliers, V., Steyaert, J. & Ballet, S., Sep 2016, In : Journal of Peptide Science. 22, p. S134-S134

DNA immunization combined with scFv phage display identifies antagonistic GCGR specific antibodies and reveals new epitopes on the small extracellular loops

van der Woning, B., De Boeck, G., Blanchetot, C., Bobkov, V., Klarenbeek, A., Saunders, M., Waelbroeck, M., Laeremans, T., Steyaert, J., Hultberg, A. & De Haard, H., 17 Aug 2016, In : mAbs. 8, 6, p. 1126-1135 9 p.

Crystal Structures of the Human Doublecortin C- and N-terminal Domains in Complex with Specific Antibodies

Burger, D., Stihle, M., Sharma, A., Di Lello, P., Benz, J., D'Arcy, B., Debulpaep, M., Fry, D., Huber, W., Kremer, T., Laeremans, T., Matile, H., Ross, A., Rufer, A. C., Schoch, G., Steinmetz, M. O., Steyaert, J., Rudolph, M. G., Thoma, R. & Ruf, A., 29 Jul 2016, In : Journal of Biological Chemistry. 291, 31, p. 16292-16306 14 p., M116.726547.

Allosteric nanobodies reveal the dynamic range and diverse mechanisms of G-protein-coupled receptor activation

Staus, D. P., Strachan, R. T., Manglik, A., Pani, B., Kahsai, A. W., Kim, T. H., Wingler, L. M., Ahn, S., Chatterjee, A., Masoudi, A., Kruse, A. C., Pardon, E., Steyaert, J., Weis, W. I., Prosser, R. S., Kobilka, B. K., Costa, T. & Lefkowitz, R. J., 21 Jul 2016, In : Nature. 535, 7612, p. 448-452 5 p.

Conformational specific nanobodies for Chlorobium tepidum Roco protein.

Leemans, M., Deyaert, E., Pardon, E., Steyaert, J., Kortholt, A. & Versees, W., 18 Jul 2016.

Conformational specific nanobodies for Chlorobium tepidum Roco protein.

Deyaert, E., Leemans, M., Pardon, E., Steyaert, J., Kortholt, A. & Versees, W., 11 Jul 2016.

Allosteric coupling from G protein to the agonist-binding pocket in GPCRs

DeVree, B. T., Mahoney, J. P., Vélez-Ruiz, G. A., Rasmussen, S. G. F., Kuszak, A. J., Edwald, E., Fung, J-J., Manglik, A., Masureel, M., Du, Y., Matt, R. A., Pardon, E., Steyaert, J., Kobilka, B. K. & Sunahara, R. K., 7 Jul 2016, In : Nature. 535, 7610, p. 182-186 5 p.

The unexpected structure of the designed protein Octarellin V.1 forms a challenge for protein structure prediction tools

Figueroa, M., Sleutel, M., Vandevenne, M., Parvizi, G., Attout, S., Jacquin, O., Vandenameele, J., Fischer, A. W., Damblon, C., Goormaghtigh, E., Valerio-Lepiniec, M., Urvoas, A., Durand, D., Pardon, E., Steyaert, J., Minard, P., Maes, D., Meiler, J., Matagne, A., Martial, J. A. & 1 others, Van de Weerdt, C., Jul 2016, In : Journal of Structural Biology. 195, 1, p. 19-30

Structural Basis for Allosteric Coupling Between G Protein and the Agonist-Binding Pocket in GPCRs

Mahoney, J., DeVree, B., Velez-Ruiz, G., Rasmussen, S., Kuszak, A., Edwald, E., Manglik, A., Masureel, M., Du, Y., Matt, R., Pardon, E., Steyaert, J., Kobilka, B. & Sunahara, R., Apr 2016, Faseb Journal. Vol. 30.

Functional and Biochemical Characterization of Alvinella pompejana Cys-Loop Receptor Homologues

Wijckmans, E., Nys, M., Debaveye, S., Brams, M., Pardon, E., Willegems, K., Bertrand, D., Steyaert, J., Efremov, R. & Ulens, C., 21 Mar 2016, In : PLoS ONE. 11, 3, 23 p., e0151183.

Development by Genetic Immunization of Monovalent Antibodies (Nanobodies) Behaving as Antagonists of the Human ChemR23 Receptor

Peyrassol, X., Laeremans, T., Gouwy, M., Lahura, V., Debulpaep, M., Van Damme, J., Steyaert, J., Parmentier, M. & Langer, I., 15 Mar 2016, In : Journal of Immunology. 196, 6, p. 2893-2901 9 p.

Thermodynamic Insights into Conformational Dynamics of Sugar Transporters

Parameswaran, H., Jiang, X., Pardon, E., Steyaert, J., Kaback, H. R. & Guan, L., 16 Feb 2016, In : Biophysical Journal. 110, 3, p. 137A-137A 1 p.

Modular integrated secretory system engineering in Pichia pastoris to enhance G-protein coupled receptor expression

Claes, K., Vandewalle, K., Laukens, B., Laeremans, T., Vosters, O., Langer, I., Parmentier, M., Steyaert, J. & Callewaert, N., 2016, In : ACS Synthetic Biology. 5, 10, p. 1070-1075 5 p.

Novel Chimeric Polypeptides For Screening and Drug Discovery Puroposes

Steyaert, J., Laeremans, T. & Pardon, E., 31 Dec 2015, IPC No. C07K14/72; C07K16/28; G01N33/566, Patent No. 20150376261, Priority date 30 Jan 2014

MUSCARINIC ACETYLCHOLINE RECEPTOR BINDING AGENTS AND USES THEREOF

Steyaert, J., Pardon, E., Kobilka, B. K., Ring, A., Kruse, A. & Manglik, A., 24 Dec 2015, IPC No. C07K16/28, Patent No. 20150368339, Priority date 5 Feb 2014

Transient conformers of LacY are trapped by nanobodies

Smirnova, I., Kasho, V., Jiang, X., Pardon, E., Steyaert, J. & Kaback, H. R., 10 Nov 2015, In : Proceedings of the National Academy of Sciences of the United States of America. 112, 45, p. 13839-13844 5 p.

Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes

Rostislavleva, K., Soler, N., Ohashi, Y., Zhang, L., Pardon, E., Burke, J. E., Masson, G. R., Johnson, C., Steyaert, J., Ktistakis, N. T. & Williams, R. L., 9 Oct 2015, In : Science. 350, 6257, 11 p., aac7365.

Structure of a prokaryotic fumarate transporter reveals the architecture of the SLC26 family

Geertsma, E. R., Chang, Y-N., Shaik, F. R., Neldner, Y., Pardon, E., Steyaert, J. & Dutzler, R., 6 Oct 2015, In : Nature Structural and Molecular Biology. 22, 10, p. 803-808 8 p.

DEVELOPMENT OF NANOBODIES AGAINST CFTR

Sigoillot, M., Grodecka, M., Franois, D., Overtus, M., He, L., Laeremans, T., Steyaert, J., Riordan, J. & Govaerts, C., Oct 2015, In : Pediatric Pulmonology. 50, p. 218-218

Sortase-mediated site-specific labeling of nanobodies: A generic method for multiple imaging modalities

Massa, S. M., Vikani, N. A., Gorsen, S., Vanderhaegen, S., Steyaert, J., Bartz, C., Betti, C., Ballet, S., Bunschoten, A., Van Leeuwen, F., Descamps, B., Vanhove, C., Caveliers, V., Lahoutte, T., Hernot, S., Muyldermans, S., Xavier, C. & Devoogdt, N., 2 Sep 2015.

Propagation of conformational changes during μ-opioid receptor activation

Sounier, R., Mas, C., Steyaert, J., Laeremans, T., Manglik, A., Huang, W., Kobilka, B. K., Déméné, H. & Granier, S., 5 Aug 2015, In : Nature. 524, 7565, p. 375–378 4 p., 14680.

Structural insights into µ-opioid receptor activation

Huang, W., Manglik, A., Venkatakrishnan, A. J., Laeremans, T., Feinberg, E. N., Sanborn, A. L., Kato, H. E., Livingston, K. E., Thorsen, T. S., Kling, R. C., Granier, S., Gmeiner, P., Husbands, S. M., Traynor, J. R., Weis, W. I., Steyaert, J., Dror, R. O. & Kobilka, B. K., 5 Aug 2015, In : Nature. 524, 7565, p. 315–321 7 p., 14886.

Characterization of two homologous 2 '-O-methyltransferases showing different specificities for their tRNA substrates.

Somme, J., Van Laer, B., Roovers, M., Steyaert, J., Versees, W. & Droogmans, L., 17 Jul 2015.

Structure/function of two homologous tRNA methyltransferases with different substrate specificity

Somme, J., van Laer, B., Roovers, M., Steyaert, J., Versees, W. & Droogmans, L., Jul 2015, In : European Biophysics Journal. 44, S1, p. S142-S142 1 p.

Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes

Newman, J. A., Savitsky, P., Allerston, C. K., Bizard, A. H., Özer, Ö., Sarlós, K., Liu, Y., Pardon, E., Steyaert, J., Hickson, I. D. & Gileadi, O., 26 May 2015, In : Nucleic Acids Res. 43, p. 5221-5235 15 p.

BRET evidence that β2 adrenergic receptors do not oligomerize in cells

Lan, T-H., Liu, Q., Li, C., Wu, G., Steyaert, J. & Lambert, N. A., 8 May 2015, In : Scientific Reports - Nature. 5, 12 p., 10166.

Structural Basis for Allosteric Enhancement of Agonist Affinity by G Proteins

Mahoney, J., DeVree, B., Velez-Ruiz, G., Rasmussen, S., Kuszak, A., Pardon, E., Steyaert, J., Kobilka, B. & Sunahara, R., 1 Apr 2015, In : The FASEB Journal. 29, 1 Supplement

BRET evidence that beta(2) adrenergic receptors do not oligomerize in cells

Lan, T-H., Liu, Q., Li, C., Wu, G., Steyaert, J. & Lambert, N. A., 2015, In : Scientific Reports. 5, 12 p., 10166.

Outward-facing conformers of LacY stabilized by nanobodies

Smirnova, I., Kasho, V., Jiang, X., Pardon, E., Steyaert, J. & Kaback, R., 30 Dec 2014, In : Proc Natl Acad Sci USA. 111, p. 18548-18553 6 p.

Llama immunization with full-length VAR2CSA generates cross-reactive and inhibitory single-domain antibodies against the DBL1X domain

Nunes-Silva, S., Gangnard, S., Vidal, M., Vuchelen, A., Dechavanne, S., Chan, S., Pardon, E., Steyaert, J., Ramboarina, S., Chene, A. & Gamain, B., 9 Dec 2014, In : Scientific Reports - Nature. 4, 9 p., 7373.

TOOLS AND METHODS FOR EXPRESSION OF MEMBRANE PROTEINS

Steyaert, J., Callewaert, N., Laeremans, T., Pardon, E., Kristof, V. & Katrien, C., 4 Dec 2014, IPC No. 14/373329, Patent No. 20140357521

Production, crystallization and preliminary X-ray diffraction of the G[alpha]s [alpha]-helical domain in complex with a nanobody

Triest, S., Wohlkönig, A., Pardon, E. & Steyaert, J., 1 Nov 2014, In : Acta Crystallographica Section F - Structural Biology Communications. 70, 11, p. 1504-1507 4 p.

Production, crystallization and preliminary X-ray diffraction of the Gαs α-helical domain in complex with a nanobody

Triest, S., Wohlkönig, A., Pardon, E. & Steyaert, J., 1 Nov 2014, In : Acta Crystallographica Section F - Structural Biology Communications. 70, p. 1504-1507 4 p.

Crystal structure of a SLC11 (NRAMP) transporter reveals the basis for transition-metal ion transport

Ehrnstorfer, I. A., Geerstma, E., Pardon, E., Steyaert, J. & Dutzler, R., 19 Oct 2014, In : Nature Structural and Molecular Biology. 21, 11, p. 990-996 7 p.

Characterization of two homologous 2 '-O-methyltransferases showing different specificities for their tRNA substrates.

Somme, J., Van Laer, B., Roovers, M., Steyaert, J., Versees, W. & Droogmans, L., 21 Sep 2014.

Binding domains directed against gpcr:g protein complexes and uses derived thereof

Steyaert, J., Pardon, E., Laeremans, T., Kobilka, B. K., Rasmussen, S. G. F., Granier, S. & Sunahara, R. K., 18 Sep 2014, IPC No. US 14/129,100, Patent No. US20140275487 A1, Priority date 21 Jun 2011, Priority No. PCT/EP2012/062036

Characterization of two homologous 2 '-O-methyltransferases showing different specificities for their tRNA substrates

Somme, J., Van Laer, B., Roovers, M., Steyaert, J., Versees, W. & Droogmans, L., 1 Aug 2014, In : RNA. 20, p. 1257-1271 15 p.

Poster: Supertertiary structures of two partially disordered transcriptional co-activators, CBP and p300.

BEKESI, A., Abdellaoui, S., PANCSA, R., VÁRADI, M., Guha Roy, M., Sallam, M., Kosol, S., Contreras Martos, S., Chaves, R., EFREMOV, R., Pardon, E., Steyaert, J., Ando, T. & Kodera, N., 6 Jul 2014, Gordon Research Conference.

Characterization of two homologous 2 '-O-methyltransferases showing different specificities for their tRNA substrates.

Somme, J., Van Laer, B., Roovers, M., Steyaert, J., Versees, W. & Droogmans, L., 19 May 2014.

SAXS analysis of the tRNA-modifying enzyme complex MnmE/MnmG reveals a novel interaction mode and GTP-induced oligomerization

Fislage, M., Brosens, E., Deyaert, E., Spilotros, A., Pardon, E., Loris, R., Steyaert, J., Garcia Pino, A. & Versees, W., 14 May 2014, In : Nucleic Acids Res. 42, p. 5978-5992 15 p.

Inhibition of ligand exchange kinetics via active-site trapping with an antibody fragment

Oyen, D., Steyaert, J. & BARLOW, J., 1 Apr 2014, In : Biochemistry. 53, 12, p. 1879-1881 3 p.

Regulation of beta2-Adrenergic Receptor Function by Conformationally Selective Single-Domain Intrabodies

Staus, D. P., Wingler, L. M., Strachan, R. T., Rasmussen, S. G. F., Pardon, E., Ahn, S., Steyaert, J., Kobilka, B. K. & Lefkowitz, R. J., 1 Mar 2014, In : Molecular Pharmacology. 85, p. 472-481 10 p.

A general protocol for the generation of Nanobodies for structural Biology

Pardon, E., Laeremans, T., Triest, S., Rasmussen, S. G. F., Ruf, A., Muyldermans, S., Hol, W. G. J., Kobilka, B. K. & Steyaert, J., 27 Feb 2014, In : Nature Protocols. 9, p. 674-693 20 p.

Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11

Pathare, G., Nagy, I., Sledz, P., Anderson, D., Zhou, H-J., Pardon, E., Steyaert, J., Forster, F., Bracher, A. & Baumeister, W., 25 Feb 2014, In : Proc Natl Acad Sci USA. 111, 8, p. 2984-2989 6 p.

Probing the N-Terminal beta-Sheet Conversion in the Crystal Structure of the Human Prion Protein Bound to a Nanobody

Abskharon, R., Giachin, G., Soror, S., Pardon, E., Legname, G. & Steyaert, J., 22 Jan 2014, In : J. Am. Chem. Soc.. 136, p. 937-944 8 p.

Activation and allosteric modulation of a muscarinic acetylcholine receptor

Kruse, A., Ring, A., Manglik, A., Pardon, E., Steyaert, J., Wess, J. & Kobilka, B. K., 5 Dec 2013, In : Nature. 504, 7478, p. 101-106 6 p.

Nanobody Mediated Crystallization of an Archeal Mechanosensitive Channel

Low, C., Yau, Y. H., Pardon, E., Jegerschold, C., Steyaert, J. & Nordlund, P., 21 Oct 2013, In : PLoS ONE. 8, 10, 14 p., e77984.

Recombinant Human Prion Protein Inhibits Prion Propagation in vitro

Yuan, J., Abskharon, R., Steyaert, J. & Zou, W., 9 Oct 2013, In : Scientific Reports - Nature. 3, 8 p., 2911.

Mechanistic analysis of allosteric and non-allosteric effects arising from nanobody binding to two epitopes of the dihydrofolate reductase of Escherichia coli

Oyen, D., Wechselberger, R., SRINIVASAN, V., Steyaert, J. & BARLOW, J., 1 Oct 2013, In : Biochim Biophys Acta. 1834, 10, p. 2147-2157 11 p.

Structure of an early native-like intermediate of beta2-microglobulin amyloidogenesis

Vanderhaegen, S., Fislage, M., Domanska, K., Versees, W., Pardon, E., Bellotti, V. & Steyaert, J., 1 Oct 2013, In : Protein Science. 22, 10, p. 1349-1357 9 p.

The structure of the D3 domain of Plasmodium falciparum myosin tail interacting protein MTIP in complex with a nanobody

Khamrui, S., Turley, S., Pardon, E., Steyaert, J., Fan, E., Verlinde, C. & Hol, W. G. J., 31 Aug 2013, In : Mol Biochem Parasitol. 190, 2, p. 87-91 5 p.

Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain

Ward, A. B., Szewczyk, P., Grimard, V., Lee, C-W., Martinez, L., Doshi, R., Caya, A., Villaluz, M., Pardon, E., Cregger, C., Swartz, D. J., Falson, P. G., Urbatsch, I. L., Govaerts, C., Steyaert, J. & Chang, G., 13 Aug 2013, In : Proceedings of the National Academy of Sciences of the United States of America. 110, 33, p. 13386-13391 6 p.

Nanobodies Raised against Monomeric alpha-Synuclein Distinguish between Fibrils at Different Maturation Stages

Guilliams, T., El-Turk, F., Buell, A. K., O'Day, E. M., Aprile, F. A., Esbjoerner, E. K., Vendruscolo, M., Cremades, N., Pardon, E., Wyns, L., Welland, M. E., Steyaert, J., Christodoulou, J., Dobson, C. M. & De Genst, E., 24 Jul 2013, In : Journal of Molecular Biology. 425, 14, p. 2397-2411 15 p.

Mapping the conformational space accessible to BACE2 using surface mutants and cocrystals with Fab fragments, Fynomers and Xaperones

Banner, D., Gsell, B., Debulpaep, M., Laeremans, T., Steyaert, J. & Ruf, A., 1 Jun 2013, In : Acta Cryst D. 69, p. 1124-1137 14 p.

Protein binding domains stabilizing functional conformational states of gpcrs and uses thereof

Steyaert, J., Pardon, E., Laeremans, T., Rasmussen, S. G. F., Kobilka, B. K. & Fung, J. J., 30 May 2013, IPC No. US 13/810,657, Patent No. US20130137856 A1, Priority date 16 Jul 2010, Priority No. PCT/EP2011/062288

Epitope tag for affinity-based applications

Pardon, E., Steyaert, J. & Wyns, L., 9 May 2013, IPC No. US 13/698,624, Patent No. US20130115635 A1, Priority date 25 May 2010, Priority No. PCT/EP2011/058591

Role of quiescin-sulfhydryl oxidase in prion formation

Zhan, Y-A., Abskharon, R., Steyaert, J. & Zou, W., 1 May 2013, In : Prion. 7, S, p. 93-93 1 p.

Unglycosylated recombinant prion protein inhibits homologous prion propagation in vitro: A glycoform barrier?

Yuan, J., Abskharon, R., Steyaert, J. & Zou, W., 1 May 2013, In : Prion. 7, S, p. 93-93 1 p.

Mapping the Binding Interface between an HIV-1 Inhibiting Intrabody and the Viral Protein Rev

Vercruysse, T., Boons, E., Venken, T., Vanstreels, E., Steyaert, J. & Daelemans, D., 2 Apr 2013, In : PLoS ONE. 8, 4, p. 60259 1 p.

Conformational biosensors reveal GPCR signalling from endosomes

Irannejad, R., Tomshine, J. C., Tomshine, J. R., Chevalier, M., Mahoney, J. P., Steyaert, J., Rasmussen, S. G. F., Sunahara, R. K., El-Samad, H., Huang, B. & Von Zastrow, M., 28 Mar 2013, In : Nature. 495, 7442, p. 534-538 5 p.

Structure of a bacterial type IV secretion core complex at subnanometre resolution

Rivera-Calzada, A., Fronzes, R., Savva, C. G., Chandran, V., Lian, P. W., Laeremans, T., Pardon, E., Steyaert, J., Remaut, H. K., Waksman, G. & Orlova, E. V., 19 Mar 2013, In : EMBO Journal. 32, p. 1195–1204 10 p.

Allosteric inhibition of VIM metallo-β-lactamases by a camelid nanobody

Sohier, J. S., Laurent, C., Chevigné, A., Pardon, E., Srinivasan, V., Wernery, U., Lassaux, P., Steyaert, J. & Galleni, M., 2013, In : Biochemical Journal. 450, 3, p. 477-486 10 p.

Production, crystallisation and X-ray diffraction analysis of two nanobodies against the Duffy Binding like domain DBL6e-FCR3 of the Plasmodium falciparum VAR2CSA protein

Vuchelen, A., Pardon, E., Steyaert, J., Gamain, B., Loris, R., Van Nuland, N. & Ramboarina, S., 2013, In : Acta Crystallogr F Struct Biol Commun. 69, p. 270-274 5 p.

Crystal structure of a heterodimer of editosome interaction proteins in complex with two copies of a cross-reacting nanobody

Park, Y-J., Pardon, E., Wu, M., Steyaert, J. & Hol, W. G. J., 27 Oct 2012, In : Nucleic Acids Research. 40, p. 1828-1840 13 p.

Evaluation of protein binders as crystallization facilitators

Thoma, R., Steyaert, J., Laeremans, T. & Weber, M., 5 Aug 2012, In : Protein Science. 21, SI, p. 216-217 2 p.

Investigation of the aggregation mechanism of polyQ proteins using chimeras of BlaP

Pain, C., Willibal, K., Steyaert, J., Pardon, E. & Dumoulin, M., 1 Aug 2012, In : Protein Science. 21, SI, p. 107-108 2 p.

SbsB structure and lattice reconstruction unveil Ca2+ triggered S-layer assembly

BARANOVA, E., Fronzes, R., Garcia Pino, A., Van Gerven, N., Papapostolou, D., Péhau-Arnaudet, G., Pardon, E., Steyaert, J., Howorka, S. & Remaut, H. K., 10 Jun 2012, In : Nature. 487, p. 119-122 4 p.

Nanobody-stabilize the crystal structure of full-length human PrP

Abskharon, R., Soror, S., Giachin, G., Pardon, E., El Hassan, H., Legname, G. & Steyaert, J., 1 Apr 2012, In : Prion. 6, S, p. 115-115 1 p.

A novel expression system for production of soluble prion proteins in E.coli

Abskharon, R., Ramboarina, S., El Hassan, H., Apostol, M., Giachin, G., Legname, G., Mohamed, W., Steyaert, J., Messens, J., Soror, S. & Wohlkonig, A., 10 Jan 2012, In : Microb Cell Fact. 11, p. 6 11 p.

A novel expression system for production of soluble prion proteins in E. coli

Abskharon, R. N. N., Ramboarina, S., El Hassan, H., Mohamed Gad, W., Apostol, M. I., Giachin, G., Legname, G., Steyaert, J., Messens, J., Soror, S. H. & Wohlkonig, A., 2012, In : Microbial Cell Factories. 11, 6, 11 p.

The structure of the C-terminal domain of the largest editosome interaction protein and its role in promoting RNA binding by RNA editing ligase L2

Park, Y-J., Budiarto, T., Wu, M., Pardon, E., Steyaert, J. & Hol, W. G. J., 2012, In : Nucleic Acids Research. 40, p. 6966-6977 12 p.

Crystal structure of the β2 adrenergic receptor–Gs protein complex

Rasmussen, S. G. F., Devree, B. T., Zou, Y., Kruse, A., Chung, K. Y., Kobilka, T. S., Thian, F. S., Chae, P. S., Pardon, E., Calinski, D., Mathiesen, J. M., Shah, S. T. A., Lyons, J. A., Martin, C., Steyaert, J., Skiniotis, G., Weis, W. I., Sunahara, R. K. & Kobilka, B. K., 29 Sep 2011, In : Nature. 477, p. 549-555 6 p.

Structural flexibility of the Gαs α-helical domain in the β2-adrenoceptor Gs complex

Westfield, G. H., Rasmussen, S. G. F., Min, S., Somnath, D., Devree, B. T., Chung, K. Y., Calinski, D., Gisselle, V-R., Oleskie, A. N., Pardon, E., Chae, P. S., Liu, T., Li, S., Woods, V. L., Steyaert, J., Kobilka, B. K., Sunahara, R. K. & Skiniotis, G., 13 Sep 2011, In : Proceedings of the National Academy of Sciences of the United States of America. 108, p. 16086-16091 6 p.

Structural and Functional Studies on the Interaction of GspC and GspD in the Type II Secretion System

Korotkov, K. V., Johnson, T. L., Jobling, M. G., Pruneda, J., Pardon, E., Heroux, A., Turley, S., Steyaert, J., Holmes, R. K., Sandkvist, M. & Hol, W. G. J., 8 Sep 2011, In : PLoS Pathogens. 7, 9, 14 p., e1002228.

Combining in-situ proteolysis and microseed matrix screening to promote crystallization of PrPc-nanobody complexes

Abskharon, R. N. N., Soror, S. H., Pardon, E., El Hassan, H., Legname, G., Steyaert, J. & Wohlkonig, A., Sep 2011, In : Protein Engineering, Design and Selection. 24, 9, p. 737-741 5 p.

Nanobody stabilization of G protein-coupled receptor conformational states

Steyaert, J. & Kobilka, B. K., 31 Aug 2011, In : Current Opinion in Structural Biology. 21, 4, p. 567-572 5 p.

Structural investigation of GPCR transmembrane signaling by use of nanobodies

Steyaert, J., Aug 2011, In : European Biophysics Journal. 40, s1, p. 223-223 1 p.

Structures of a key interaction protein from the Trypanosoma brucei editosome in complex with single domain antibodies

Wu, M., Park, Y-J., Pardon, E., Turley, S., Hayhurst, A., Deng, J., Steyaert, J. & Hol, W. G. J., 30 Apr 2011, In : Journal of Structural Biology. 174, p. 124-136 13 p.

Structure of a nanobody-stabilized active state of the b2 adrenoceptor

Rasmussen, S. G. F., Choi, H-J., Fung, J. J., Pardon, E., Casarosa, P., Chae, P. S., Devree, B. T., Rosenbaum, D. M., Thian, F. S., Kobilka, T. S., Schnapp, A., Konetzki, I., Sunahara, R. K., Gellman, S. H., Pautsch, A., Steyaert, J., Weis, W. I. & Kobilka, B. K., 13 Apr 2011, In : Nature. 469, 7329, p. 175-180 5 p.

Constraining Enzyme Conformational Change by an Antibody Leads to Hyperbolic Inhibition

Oyen, D., SRINIVASAN, VASUNDARA., Steyaert, J. & BARLOW, J., 18 Mar 2011, In : Journal of Molecular Biology. 407, p. 138-148 11 p.

Measuring cooperative Rev protein-protein interactions on Rev responsive RNA by fluorescence resonance energy transfer

Vercruysse, T., Pawar, S., De Borggraeve, W. M., Pardon, E., Pavlakis, G. N., Pannecouque, C., Steyaert, J., Balzarini, J. & Daelemans, D., 1 Mar 2011, In : RNA Biology. 8, p. 316-324 9 p.

Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic beta 2-microglobulin variant

Domanska, K., Vanderhaegen, S., SRINIVASAN, VASUNDARA., Pardon, E., Dupeux, F., Marquez, J. A., Giorgetti, S., Stoppini, M., Wyns, L., Bellotti, V. & Steyaert, J., 25 Jan 2011, In : Proceedings of the National Academy of Sciences of the United States of America. 108, p. 1314-1319 6 p.

Crystallization and preliminary X-ray diffraction analysis of a specific VHH domain against mouse prion protein

Abskharon, R., Soror, S., Pardon, E., El Hassan, H. & Steyaert, J., 1 Dec 2010, In : Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 66, p. 1644-1646 3 p.

Polymeric nanoreactors for enzyme replacement therapy by MNGIE

De Vocht, C., Ranquin, A., Van Ginderachter, J., Vanhaecke, T., Rogiers, V., Van Gelder, P., Versees, W. & Steyaert, J., 20 Nov 2010, In : Journal of Controlled Release. 148, 1, p. E19-E20 2 p.

Polymeric nanoreactors for enzyme replacement therapy of MNGIE

De Vocht, C., Ranquin, A., Van Ginderachter, J., Vanhaecke, T., Rogiers, V., Van Gelder, P., Versées, W. & Steyaert, J., 20 Nov 2010, In : Journal of Controlled Release. 148, 1, p. e19-20 2 p.

Structure and mechanism of the 6-oxopurine nucleosidase from Trypanosoma brucei brucei.

Vandemeulebroucke, A., Minici, C., Bruno, I., Muzzolini, L., Tornaghi, P., Parkin, D., Versees, W., Steyaert, J. & Degano, M., 19 Oct 2010, In : Biochemistry. 49, p. 8999-9010 12 p.

Structure and Properties of a Complex of alpha-Synuclein and a Single-Domain Camelid Antibody

De Genst, E., Guilliams, T., Wellens, J., O'day, E. M., Waudby, C. A., Meehan, S., Dumoulin, M., Hsu, S-T. D., Cremades, N., Verschueren, K., Pardon, E., Wyns, L., Steyaert, J., Christodoulou, J. & Dobson, C. M., 17 Sep 2010, In : Journal of Molecular Biology. 402, p. 326-343 18 p.

An Intrabody Based on a Llama Single-domain Antibody Targeting the N-terminal alpha-Helical Multimerization Domain of HIV-1 Rev Prevents Viral Production

Vercruysse, T., Pardon, E., Vanstreels, E., Steyaert, J. & Daelemans, D., 9 Jul 2010, In : Journal of Biological Chemistry. 285, p. 21768-21780 13 p.

cAbVIM4, a nanobody inhibiting the metallo-beta lactamase VIM-4

Sohier, J. -S., Pardon, E., Laurent, C., Lassaux, P., Buys, N., Willibal, K., Wyns, L., Steyaert, J. & Galleni, M., Jun 2010, In : FEBS Journal. 277, p. 241-241

Influence of Nanobodies on the aggregation properties of Alpha-synuclein

Guilliams, T., De Genst, E., Pardon, E., Cremades, N., Steyaert, J., Wyns, L. & Dobson, C., Jun 2010, In : FEBS Journal. 277, p. 84-84

A llama-derived gelsolin single-domain antibody blocks gelsolin-G-actin interaction

Van Den Abbeele, A., De Clercq, S., De Ganck, A., De Corte, V., Van Loo, B., Soror, S., SRINIVASAN, VASUNDARA., Steyaert, J., Vandekerckhove, J. & Gettemans, J., 1 May 2010, In : Cellular and Molecular Life Sciences. 67, 9, p. 1519-1535 17 p.

Evaluation of nucleoside hydrolase inhibitors for the treatment of African trypanosomiasis.

Berg, M., Kohl, L., Van Der Veken, P., Joossens, J., Al-Salabi, M., Castagna, V. C., Giannese, F., Cos, P., Versees, W., Steyaert, J., Grellier, P., Haemers, A., Degano, M., Maes, L., Harry, D. K. & Augustyns, K., 1 May 2010, In : Antimicrob Agents Chemother. 54, p. 1900-1908 9 p.

An Intrabody based on a Llama Single-domain Antibody Targeting the N-terminal alpha-Helical Multimerization Domain of HIV-1 Rev Inhibits Viral Replication

Daelemans, D., Vercruysse, T., Pardon, E., Vanstreels, E. & Steyaert, J., Apr 2010, In : Antiviral Research. 86, 1, p. A22-A22

Small molecules and macromolecules for the inhibition of beta 2 microglobulin fibrillogenesis

Giorgetti, S., Porcari, R., Raimondi, S., Steyaert, J., Domanska, K., Vanderhaegen, S., Relini, A., Parrini, C., Gliozzi, S., Salmona, M., Bucciantini, M., Stefani, M., Gallanti, A., Zorzoli, I., Esposito, G., Stoppini, M. & Bellotti, V., Apr 2010, In : Amyloid. The Journal of Protein Folding Disorders. 17, p. 50-50

Isolation of antigen-binding camelid heavy chain antibody fragments (nanobodies) from an immune library displayed on the surface of Pichia pastoris

Ryckaert, S., Pardon, E., Steyaert, J. & Callewaert, N., 15 Jan 2010, In : Journal of Biotechnology. 145, p. 93-98 6 p.

Substrate-dependent modulation of enzyme activity by allosteric effector antibodies

Barlow, J. N., Conrath, K. & Steyaert, J., Aug 2009, In : Biochimica et Biophysica Acta. 1794, 8, p. 1259-1268 10 p.

Crystal structures of T.vivax nucleoside hydrolase in complex with new potent and specific inhibitors

Versees, W., Goeminne, A., Berg, M., Vandemeulebroucke, A., Haemers, A., Augustyns, K. & Steyaert, J., Jun 2009, In : Biochimica et Biophysica Acta - Proteins and Proteomics. 1794, p. 953-960 8 p.

A Small Llama Antibody Fragment Efficiently Inhibits the HIV Rev Multimerization In Vitro

Vercruysse, T., Pardon, E., Steyaert, J. & Daelemans, D., May 2009, In : Antiviral Research. 82, 2, p. A27-A27

Nanobody-aided structure determination of the EpsI:EpsJ pseudopilin heterodimer from Vibrio vulnificus

Lam, A. Y., Pardon, E., Korotkov, K. V., Hol, W. G. J. & Steyaert, J., 1 Apr 2009, In : Journal of Structural Biology. 166, p. 8-15 8 p.

Assessment of stability, toxicity and immunogenicity of new polymeric nanoreactors for use in enzyme replacement therapy of MNGIE

De Vocht, C., Ranquin, A., Willaert, R., Van Ginderachter, J., Vanhaecke, T., Rogiers, V., Versees, W., Van Gelder, P. & Steyaert, J., 30 Mar 2009, In : Journal of Controlled Release. 137, p. 246-254 9 p.

Crystal Structure of the N-Terminal Domain of the Secretin GspD from ETEC Determined with the Assistance of a Nanobody

Korotkov, K. V., Pardon, E., Steyaert, J. & Hol, W. G. J., 13 Feb 2009, In : Structure. 17, 2, p. 255-265 11 p.

Synthesis of bicyclic N-arylmethyl substituted iminoribitol derivatives as selective nucleoside hydrolase inhibitors.

Berg, M., Bal, G., Goeminne, A., Van Der Veken, P., Versees, W., Steyaert, J., Haemers, A. & Augustyns, K., Feb 2009, In : ChemMedChem. 4, p. 249-260 12 p.

A flexible loop as a functional element in the catalytic mechanism of nucleoside hydrolase from Trypanosoma vivax

Vandemeulebroucke, A., De Vos, S., Van Holsbeke, E., Steyaert, J. & Versees, W., 8 Aug 2008, In : Journal of Biological Chemistry. 283, p. 22272-22282 11 p.

N-Arylmethyl Substituted Iminoribitol Derivatives as Inhibitors of a Purine Specific Nucleoside Hydrolase.

Goeminne, A., Berg, M., Mcnaughton, M., Bal, G., Surpateanu, G., Van Der Veken, P., De Prol, S., Versees, W., Steyaert, J., Haemers, A. & Augustyns, K., 15 Jul 2008, In : Bioorganic & Medicinal Chemistry. 16, p. 6752-6763 12 p.

Synthesis and biochemical evaluation of guanidino-alkyl-ribitol derivatives as nucleoside hydrolase inhibitors

Goeminne, A., Mcnaughton, M., Bal, G., Surpateanu, G., Van Der Veken, P., De Prol, S., Versees, W., Steyaert, J., Haemers, A. & Augustyns, K., Feb 2008, In : European Journal of Medicinal Chemistry. 43, p. 315-326 12 p.

Waarom Mieke Van Hecke de VUB niet mag uitsluiten

Danckaert, J., Gutwirth, S., Van Bendegem, J., Christiaens, J., Corijn, E. & Steyaert, J., 6 Dec 2007, De Morgen, 6 december 2007, p. 14 1 p.

Molecular mechanism of allosteric substrate activation in a thiamine diphosphate-dependent decarboxylase.

Versees, W., Spaepen, E., Wood, D., Leeper, J., Vanderleyden, J. & Steyaert, J., 30 Nov 2007, In : J. Biol. Chem.. 282, p. 35269-35278 10 p.

Characterization of phenylpyruvate decarboxylase, involved in auxin production of Azospirillum brasilense.

Spaepen, E., Versees, W., Gocke, D., Pohl, M., Steyaert, J. & Vanderleyden, J., Nov 2007, In : Journal of Bacteriology. 189, p. 7626-7633 8 p.

Examination of the mechanism and energetic contribution of leaving group activation in the purine-specific nucleoside hydrolase from Trypanosoma vivax

Barlow, J. N. & Steyaert, J., Nov 2007, In : Biochimica et Biophysica Acta. 1774, 11, p. 1451-1461 11 p.

The crystal structure of phenylpyruvate decarboxylase from Azospirillum brasilense at 1.5 Å resolution. Implications for its catalytic and regulatory mechanism.

Versees, W., Spaepen, S., Vanderleyden, J. & Steyaert, J., 1 May 2007, In : FEBS Journal. 274, p. 2363-2375 13 p.

1,2,3-Triazolylalkylribitol derivatives as nucleoside hydrolase inhibitors.

Goeminne, A., Mcnaughton, M., Bal, G., Surpateanu, G., Van Der Veken, P., De Prol, S., Versees, W., Steyaert, J., Apers, S., Haemers, A. & Augustyns, K., 1 May 2007, In : Bioorganic & Medicinal Chemistry Letters. 17, p. 2523-2526 4 p.

Multiple Transients in the Pre-Steady State of Nucleoside Hydrolase Reveal Complex Substrate Binding, Product Base Release and Two Apparent Rates of Chemistry.

Vandemeulebroucke, A., Versees, W., Steyaert, J. & BARLOW, J., 1 Aug 2006, In : Biochemistry. 45, p. 9307-9318 12 p.

New insights into the mechanism of nucleoside hydrolases from the crystal structure of the Escherichia Coli YbeK protein bound to the reastion product.

Muzzolini, L., Versees, W., Tornaghi, P., Van Holsbeke, E., Steyaert, J. & Degano, M., 24 Jan 2006, In : Biochemistry. 45, p. 773-782 10 p.

New Catalytic Strategies for Leaving Group Activation in Nucleosidehydrolases

Versees, W., Loverix, S., Vandemeulebroucke, A., BARLOW, J., Geerlings, P. & Steyaert, J., 2006, In : Acta Cryst.A.. 62, p. 156 1 p.

Quantum Chemical Study of Leaving Group Activation in T-vivax Nucleoside Hydrolase

Loverix, S., Versees, W., Steyaert, J. & Geerlings, P., 2006, In : International Journal of Quantum Chemistry. 106, p. 565-570 6 p.

Transition-state Complex of the Purine-specific Nucleoside Hydrolase of T. vivax: Enzyme Conformational Changes and Implications for Catalysis.

Versees, W., BARLOW, J. & Steyaert, J., 2006, In : J Mol Biol. 359, 2, p. 331-346 16 p.

Education Assessment - Master in Biomolecular Sciences

Steyaert, J., Van Driessche, E. & Beeckmans, S., Dec 2005, Education assessment Master in biomolecular sciences (with anne ed. Unknown.

Therapeutic nanoreactors: combining chemistry and biology in a novel triblock copolymer drug delivery system

Ranquin, A., Versees, W., Meier, W., Steyaert, J. & Van Gelder, P., Nov 2005, In : Nano Letters. 5, p. 2220-2224 5 p.

Substrate-assisted Leaving Group Activation in Enzyme Catalyzed N-glycosidic Bond Cleavage

Loverix, S., Geerlings, P., Mcnaughton, M., Augustyns, K., Vandemeulebroucke, A., Steyaert, J. & Versees, W., 15 Apr 2005, In : Journal of Biological Chemistry. 280, p. 14799-14802 4 p.

Encapsulation of therapeutic nucleoside hydrolase in functionalised nanocapsules.

Huysmans, G., Ranquin, A., Wyns, L., Steyaert, J. & Van Gelder, P., 2005, In : J Control Release. 102, p. 171-179 9 p.

Influence of the p-p Interactions on the Hydrogen Bonding Capacity of Stacked DNA/RNA Bases

Mignon, P., Loverix, S., Steyaert, J. & Geerlings, P., 2005, In : Nucleic Acids Research. 33, 6, p. 1779-1789 11 p.

Pre-steady state analysis of the nucleoside hydrolase of Trypanosoma vivax. Evidence for rate-limiting product release.

Vandemeulebroucke, A., Versees, W. & Steyaert, J., 2005, FEBS Journal. S1 ed. Vol. 272. p. 101-101 1 p.

Functional Assessment of 'In Vivo' and 'In Silico' Mutations in the Guanine Binding Site of RNAse T1 : a DFT Study

Mignon, P., Loverix, S., Steyaert, J. & Geerlings, P., 15 Jul 2004, In : International Journal of Quantum Chemistry. 99, p. 53-58 6 p.

Leaving Group Activation by Aromatic Stacking : an Alternative to General Acid Catalysis

Versees, W., Loverix, S., Vandemeulebroucke, A., Geerlings, P. & Steyaert, J., 2004, In : J Mol Biol. 338, 1, p. 1-6 6 p.

Catalysis by nucleoside hydrolases

Versees, W. & Steyaert, J., 2003, In : Current Opinion in Structural Biology. 13, 6, p. 731-738 8 p.

Cloning, preliminary characterization, and crystallization of nucleoside hydrolases from Caenorhabditis elegans and Campylobacter jejuni

Versees, W., Van Holsbeke, E., De Vos, S., Decanniere, K., Zegers, I. & Steyaert, J., 2003, In : Acta Cryst D. 59, p. 1087-1089 3 p.

Pre-Steady State Analysis of the Nucleoside Hydrolase of Trypanosoma vivax. Evidence for half-of- the-sites reactivity and rate limiting product release

Vandemeulebroucke, A., Versees, W., De Vos, S., Van Holsbeke, E. & Steyaert, J., 2003, In : Biochemistry. 42, 44, p. 12902-12908 7 p.

Ribonucleases: from prototypes to therapeutic targets ?

Loverix, S. & Steyaert, J., 2003, In : Current Medicinal Chemistry. 10, 8, p. 779-785 7 p.

A nucleophile Activation Diad in Ribonucleases : a Combined X-Ray Crystallographic and Ab Initio Quantum Chemical Approach

Mignon, P., Steyaert, J., Loris, R., Geerlings, P. & Loverix, S., 2002, In : J. Biol. Chem.. 277, 39, p. 36770-36774 5 p.

De Vakgroep Toegepaste Biologische Wetenschappen

De Vuyst, L., Van Driessche, E. & Steyaert, J., 2002, Unknown Journal.

Enzyme-Substrate Interactions in the Purine-Specific Nucleoside Hydrolase from Trypanosoma vivax

Versees, W., Decanniere, K., Van Holsbeke, E., Devroede, N. & Steyaert, J., 2002, In : J. Biol. Chem.. 277, 18, p. 15938-15946 9 p.

Structure and function of a novel purine specific nucleoside hydrolase from Trypanosoma vivax

Versées, W., Decanniere, K., Pellé, R., Depoorter, J., Brosens, E., Parkin, D. W. & Steyaert, J., 13 Apr 2001, In : Journal of Molecular Biology. 307, 5, p. 1363-1379 17 p.

Deciphering the mechanism of RNase T1

Loverix, S. & Steyaert, J., 2001, In : Methods in Enzymology. 341, p. 305-323 19 p.

Hydrophobic core manipulations in RNase T1

De Vos, S., Backmann, J., Steyaert, J. & Loris, R., 2001, In : Biochemistry. 40, 34, p. 10140-10149 9 p.

The contribution of metal ions to the conformational stability of RNase T1: crystal vs. solution

Deswarte, J., De Vos, S., Langhorst, U., Steyaert, J. & Loris, R., 2001, In : European Journal of Biochemistry. 268, 14, p. 3993-4000 8 p.

Analysis of a water mediated protein-protein interactions within RNase T1.

Langhorst, U., Backmann, J., Loris, R. & Steyaert, J., 2000, In : Biochemistry. 39, p. 6586-6593 8 p.

Mechanism of RNase T1: concerted triester-like phosphoryl transfer via a catalytic three-centered hydrogen bond.

Loverix, S., Winquist, A., Stormberg, R. & Steyaert, J., 2000, In : Chem. Biol.. 7, 8

Conserved water molecules in a large family of microbial ribonucleases.

Loris, R., Langhorst, U., De Vos, S., Decanniere, K., Bouckaert, J., Maes, D., Transue, T. & Steyaert, J., 1 Jul 1999, In : Proteins. 36, 1, p. 117-134 18 p.

Dissection of the structural and functional role of a conserved hydration site in RNase T1

Langhorst, U., Loris, R., Denisov, V., Doumen, J., Roose, P., Maes, D., Halle, B. & Steyaert, J., 1999, In : Protein Sci. 8, 4, p. 722–730 9 p.

Hydrogen-exchange stabilities of RNase T1 and variants with buried and solvent-exposed Ala Gly mutations in the helix.

Huyghes-Despointes, B. M. P., Langhorst, U., Steyaert, J., Pace, N. C. & Scholz, J. M., 1999, In : Biochemistry. 38, 50, p. 16481-16490 9 p.

Reconsidering the Energetics of Ribonuclease Catalysed RNA hydrolysis

Loverix, S., Laus, G., Martins, J., Wyns, L. & Steyaert, J., 1 Oct 1998, In : European Journal of Biochemistry. 257, 1, p. 286-290 5 p.

An engineered Ribonuclease specific for thiophosphate RNA.

Loverix, S., Winquist, A., Steyaert, J. & Strömberg, R., May 1998, In : Nature Structural and Molecular Biology. 5, 5, p. 365-368 4 p.

Dissecting Histidine Interactions of Ribonuclease T1 with Asparagine and Glutamine Replacements:Analysis of Double Mutant Cycles at one Position

De Vos, S., Doumen, J., Langhorst, U. & Steyaert, J., 1998, In : Journal of Molecular Biology. 275, p. 651-661 11 p.

Expression, Purification, Crystalization and preliminary X-ray analysis of cyclophyn of the bovine parasite Trypanosoma bucei brucei.

Dao-Thi Minh, H., Transue, T. R., Pelle, R., Murphy, N., Poortmans, F. & Steyaert, J., 1998, In : Acta Cryst D. 54, 5, p. 1946-1948 3 p.

The hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analysed by time-resolved crystallography

Zegers, I., Loris, R., Dehollander, G., Haikal, A., Poortmans, F., Steyaert, J. & Wyns, L., 1998, In : Nature Structural and Molecular Biology. 5, 3, p. 280-283 4 p.

A decade of protein engineering on ribonuclease T-1 - Atomic dissection of the enzyme-substrate interactions

Steyaert, J., 1 Jul 1997, In : European Journal of Biochemistry. 247, 1, p. 1-11 11 p.

Additivity of protein-guanine interactions in ribonuclease T1

Loverix, S., Doumen, J. & Steyaert, J., 11 Apr 1997, In : Journal of Biological Chemistry. 272, 15, p. 9635-9639 5 p.

The contribution of a structurally conserved water molecule to the conformational stability of RNAse T1

Langhorst, U. & Steyaert, J., 1997, In : Protein Engineering. 10, p. 29-29 1 p.

A catalytic function of the structurally conserved Phe100 in ribonuclease T1

Doumen, J., Gonciarz, M., Zegers, I., Loris, R., Wyns, L. & Steyaert, J., 1996, In : Protein Science. 5, p. 1523-1530 8 p.

A 2-BINDING-SITE KINETIC-MODEL FOR THE RIBONUCLEASE-T-1-CATALYZED TRANSESTERIFICATION OF DINUCLEOSIDE PHOSPHATE SUBSTRATES

STEYAERT, J. & ENGELBORGHS, Y., 1 Oct 1995, In : European Journal of Biochemistry. 233, 1, p. 140-144 5 p.

PRIMARY STRUCTURE AND PARTIAL CHARACTERIZATION OF A LIFE-CYCLE-REGULATED CYSTEINE PROTEASE FROM TRYPANOSOMA (NANNOMONAS) CONGOLENSE

FISH, WR., NKHUNGULU, ZM., MURIUKI, CW., NDEGWA, DM., LONSDALEECCLES, JD. & STEYAERT, J., 8 Aug 1995, In : Gene. 161, 1, p. 125-128 3 p.

INVESTIGATION OF THE FUNCTIONAL INTERPLAY BETWEEN THE PRIMARY SITE AND THE SUBSITE OF RNASE-T(1) - KINETIC-ANALYSIS OF SINGLE AND MULTIPLE MUTANTS FOR MODIFIED SUBSTRATES

STEYAERT, J., HAIKAL, AF. & WYNS, L., Apr 1994, In : Proteins. 18, 4, p. 318-323 6 p.

CRYSTALLOGRAPHIC STUDY OF GLU58ALA RNASE T1-CENTER-DOT-2'-GUANOSINE MONOPHOSPHATE AT 1.9-ANGSTROM RESOLUTION

PLETINCKX, J., STEYAERT, J., ZEGERS, I., CHOE, HW., HEINEMANN, U. & WYNS, L., 22 Feb 1994, In : Biochemistry. 33, 7, p. 1654-1662 9 p.

THE F-PLASMID CCDB PROTEIN INDUCES EFFICIENT ATP-DEPENDENT DNA CLEAVAGE BY GYRASE

BERNARD, P., KEZDY, KE., VANMELDEREN, L., STEYAERT, J., WYNS, L., PATO, ML., HIGGINS, PN. & COUTURIER, M., 5 Dec 1993, In : Journal of Molecular Biology. 234, 3, p. 534-541 8 p.

PURIFICATION, CIRCULAR-DICHROISM ANALYSIS, CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION ANALYSIS OF THE F-PLASMID CCDB KILLER PROTEIN

STEYAERT, J., VANMELDEREN, L., BERNARD, P., THI, MHD., LORIS, R., WYNS, L. & COUTURIER, M., 20 May 1993, In : Journal of Molecular Biology. 231, 2, p. 513-515 3 p.

FUNCTIONAL INTERACTIONS AMONG THE HIS40, GLU58 AND HIS92 CATALYSTS OF RIBONUCLEASE-T(1) AS STUDIED BY DOUBLE AND TRIPLE MUTANTS

STEYAERT, J. & WYNS, L., 5 Feb 1993, In : Journal of Molecular Biology. 229, 3, p. 770-781 12 p.

THE METAL AND SACCHARIDE BINDING-SITES OF THE LENTIL LECTIN - AN X-RAY STUDY

LORIS, R., STEYAERT, J. & WYNS, L., 9 Jan 1993, In : Journal of Cellular Biochemistry. p. 368-368 1 p.

Crystal Structure determination and refinement at 2.3-Å resolution of the lentil lectin.

Loris, R., Steyaert, J., Maes, D., Lisgarten, J., Pickersgill, R. & Wyns, L., 1993, In : Biochemistry. 32, p. 8772-8781 10 p.

Role of histidine-40 in ribonuclease T1 catalysis: three-dimensionalstructures of the partially active His40Lys mutant

Zegers, I., Verhelst, P., Choe, H. W., Steyaert, J., Heinemann, U., Saenger, W. & Wyns, L., 24 Nov 1992, In : Biochemistry. 31, 46, p. 11317-11325 9 p.

Dissection of the ribonuclease T1 subsite. The transesterification kinetics of Asn36Ala and Asn98Ala ribonuclease T1 for minimal dinucleoside phosphates

Steyaert, J., Haikal, A. F., Stanssens, P. & Wyns, L., 1 Feb 1992, In : European Journal of Biochemistry. 203, 3, p. 551-555 5 p.

Subsite interactions of ribonuclease T1: viscosity effects indicate that the rate-limiting step of GpN transesterification depends on the nature of N

Steyaert, J., Wyns, L. & Stanssens, P., 3 Sep 1991, In : Biochemistry. 30, 35, p. 8661-8865 5 p.

Quantitative analysis of the contribution of Glu46 and Asn98 to the guanosine specificity of ribonuclease T1

Steyaert, J., Opsomer, C., Wyns, L. & Stanssens, P., 15 Jan 1991, In : Biochemistry. 30, 2, p. 494-499 6 p.

Histidine-40 of ribonuclease T1 acts as base catalyst when the true catalytic base, glutamic acid-58, is replaced by alanine

Steyaert, J., Hallenga, K., Wyns, L. & Stanssens, P., 25 Sep 1990, In : Biochemistry. 29, 38, p. 9064-9072 9 p.

Conformational stability and activity of ribonuclease T1 and mutants. Gln25----Lys, Glu58----Ala, and the double mutant

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