Publications of the Steyaert Lab

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2017

Manglik, A., Kobilka, B.K., & Steyaert, J. (2016) Nanobodies to study G protein-coupled receptor structure and function. Annu Rev Pharmacol Toxicol 57, 19-37 

 

2016

Zhan, YA., Abskharon, R., Li, Y., Yuan, J., Zeng, L., Dang, J., Martinez, MC., Wang, Z.,Mikol, J., Lehmann, S., Bu, S., Steyaert, J., Cui, L., Petersen, RB., Kong, Q., Wang, GX., Wohlkonig, A., Zou, WQ. (2016) Quiescin-sulfhydryl oxidase inhibits prion formation in vitro. Aging, advance publication on line.

 

Jianga, X., Smirnovab, I., Kashob, V., Wua, J., Hiratae, K., Kea, M., Pardon, E, Steyaert, J., Yan, N.,& Kaback, R.H. (2016) Crystal Structure of a LacY/Nanobody Complex: the periplasmic-open conformation, Proc Natl Acad Sci USA 133, 12420-12425.

 

Ismail, S., Gherardi, M.-J., Zanoun, M., Gigoux, V., Clerc, P., Gaits-Iacovoni, F., Steyaert, J., O Nikolaev, V., & Fourmy, D. (2016) Internalized Receptor for Glucose-dependent Insulinotropic Peptide stimulates adenylyl cyclase on early endosomes. Biochemical Pharmacology 120, 33-45.

 

Claes, K., Vandewalle, K., Laukens, B., Laeremans, T., Vosters, O., Langer, I., Parmentier, M., Steyaert, J. & Callewaert, N. (2016) Modular integrated secretory system engineering in Pichia pastoris to enhance integral G-protein coupled receptor expression. ACS Synthetic Biology 5, 1070-1075.

 

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., Steyaert, J., Rudolph M.G., Thoma, R. & Ruf, A. (2016) Crystal Structures of the Human Doublecortin C- and N-terminal Domains in Complex with Specific Antibodies. JBC 291, 16292-16306.

 

Staus, D.P., Stracha, 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. (2016) Allosteric Nanobodies Reveal the Dynamic Range and Diverse Mechanisms of GPCR Activation, Nature  535, 182-186.

 

DeVree, B., Mahoney, J., Velez-Ruiz, G., Rasmussen, S., Kuszak, A., Edwald, E., Fung, J. J. , Manglik, A., Masureel, M., Du , Y., Matt, R., Pardon, E., Steyaert, J., Kobilka, B. & Sunahara, R. (2016) Allosteric coupling from G protein to the agonist binding pocket in GPCRs, Nature 535, 182-186

 

Massa, S., Vikani, N.; Betti, C., Ballet, S., Vanderhaegen, S., Steyaert, J., Descamps, B., Vanhove, C., Bunschoten, A., van Leeuwen, F., Hernot, S., Caveliers, V., Lahoutte, T., Muyldermans, S., Xavier, C., & Devoogdt, N. (2016) Sortase A-mediated site-specific labeling of camelid single-domain antibody-fragments: a versatile strategy for multiple molecular imaging modalities. Contrast Media and Molecular Imaging 11, 328-339

 

Figueroa, M., Sleutel, M., Vandevenne, M., Parvizi, G., Attout, S., Jacquin, O., Vandenameele, J., Fischer, A., Damblon, C., Goormaghtigh, E., Valerio-Lepiniec, M., Urvoas, A., Durand, D., Pardon, E., Steyaert, J., Minard, P., Maes, D., Matagne, A., Martial, J., Van de Weerdt, C. (2016) The unexpected structure of the designed protein octarellin V. 1 forms a challenge for protein structure prediction tools.  Journal of Structural Biology  195, 19-30

 

Wijckmans, E., Nys, M., Debaveye, S., Brams, M., Pardon, E., Bertrand, D., Steyaert, J. & Ulens, C. (2016) Functional and Biochemical characterization of Alvinella pompejana Cys-loop receptor homologues. Plos One 11, e0151183

 

Peyrassol, X., Laeremans, T., Lahura, V., Steyaert, J., Parmentier, M. & Langer, I. (2016) Development by genetic immunization of monovalent antibodies (nanobodies) behaving as antagonists of the human ChemR23 receptor. Journal of immunology 196, 2893-2901.

 

2015

Rostislavleva, K., Soler, N., Ohashi, Y., Zhang, L., Pardon, E., Burke, J., Masson, G.R., Johnson, C., Steyaert, J., Ktistakis, N.T., & Williams, R.L. (2015) Structure and flexibility equip the endosomal Vps34 complex to phosphorylate membranes. Science 350, aac7365

 

Geertsma, E.R., Chang, Y.-N., Shaik, F.R., Neldner, Y., Pardon, E., Steyaert, J. & Dutzler, R. (2015) Structure of a prokaryotic Prestin homolog reveals the architecture of the SLC26 family. Nature Struct Mol Biol 22, 803-808.

News & views: Reithmeier, R. & Moreas, T. (2015) Solute carriers keep on rockin’. Nature Struct Mol Biol 22, 752-754

 

Huang, W, Manglik, A., Venkatakrishnan, A.J., Laeremans, T., Feinberg, E., Sanborn, A., kato, H., Livingston, K., Thorsen, T., Kling, R., Granier, G., Gmeiner, P, Traynor, J., Weis, W., Steyaert, J., Dror, R. & Kobilka, B. (2015) Structural Insights into μ-Opioid Receptor Activation. Nature 524, 315–32.

 

Sounier, R., Mas, C., Steyaert, J., Laeremans, T., Manglik, A., Huang, W., Kobilka, B., Demene, H. & Granier, G. (2015) Propagation of conformational changes during μ-opioid receptor activation. Nature 524, 375–378.

 

Newman, J., Savitsky, P., Allerston, C., Bizard, A. H., Özer, Ö., Sarlós, K., Liu, Y., Pardon, E., Steyaert, J., Hickson, I., & Gileadi, O. (2015) Crystal structure of the Bloom’s syndrome helicase indicates a role for the HRDC domain in conformational changes. Nucleic Acids Research 43, 5221-5235.

 

Lan, T-H, Qiuju Liu, Q., Li, C., Wu, C., Steyaert, J. & Lambert, N. A. (2015) BRET evidence that β 2 adrenergic receptors do not oligomerize in cells, Scientific Reports, e10166.

 

2014

Smirnova, I., Kasho, V., Jiang, X., Pardon, E., Steyaert, J., & Kaback, R.H. (2014). Outward-facing conformers of LacY stabilized by nanobodies. Proc Natl Acad Sci U S A 111, 18548-18553
 

Ehrnstorfer, I.A., Geertsma, E.R., Pardon, E., Steyaert, J. & Dutzler, R. (2014) The structural basis for transition metal ion selectivity in transporters of the SLC11/NRAMP family. Nature Struct Mol Biol 21, 990–996.  

 

Somme, J., Van Laer, B., M Roovers,, B., M., Steyaert, J., Versées, W. & Droogmans, L. (2014) Characterization of two homologous 2′-O-methyltransferases showing different specificities for their tRNA substrates. RNA 20, 1257-1271

 

Nunes-Silva, S., Gangnard, S., Vidal, M., Vuchelen, A., Dechavanne, S., Chan, S., Pardon, E., Steyaert, J., Ramboarina, S., Chêne, A., & Gamain, B. (2014) Llama immunization with full-length VAR2CSA generates cross-reactive and inhibitory single-domain antibodies against the DBL1X domain. Scientific Reports 4, Article number: 7373.

 

Triest, S., Wohlkönig, A., Pardon, E., Steyaert, J. (2014) Production, crystallization and preliminary X-ray diffraction of the Gαs α-helical domain in complex with a nanobody. Acta Crystallographica. Section F, Structural Biology Communications 70, 1504-1507.

 

Oyen, D., Steyaert, J., &  Barlow, J. (2014) Inhibition of ligand exchange kinetics via active-site trapping with an antibody fragment. Biochemistry 53, 1879–1881

 

Fislage, M., Brosens, E., Deyaert, Egon., Spilotros, A., Pardon, E., Loris, R., Steyaert, J., Garcia-Pino, A., & Versees, W. (2014) SAXS analysis of the tRNA-modifying enzyme complex MnmE/MnmG reveals a novel interaction mode and GTP-induced oligomerization, Nucleic acids res 42, 5978-5992.

 

Pathare, G.R., Nagy, I., Śledź, P.,  Anderson, D.J., Zhou, H.-J., Pardon, E., Steyaert, J., Förster, F., Bracher, A. & Baumeister, W. (2014) Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11. Proc Natl Acad Sci U S A 111, 2984-2989.

      

Pardon, E., Laeremans, T., Triest, S., Rasmussen, S. G. F., Wohlkönig, A., Ruf, A., Muyldermans, S., Hol, W.J.G.,  Kobilka, B.K. & Steyaert, J. (2014) A general protocol for the generation of Nanobodies for structural biology. Nature protocols 9, 674-693.

 

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. (2014) Regulation of Beta-2-Adrenergic Receptor Function by Conformationally Selective Single-domain Intrabodies, Mol Pharm 85, 472-481.

 

Abskharon, R.N.N., Giachin, G., Wohlkonig, A., Soror, S.H., Pardon, E., Legname, G. & Steyaert, J. (2014) Probing the N-terminal β-sheet conversion in the crystal structure of the full-length human prion protein bound to a Nanobody, J Am Chem Soc 136, 937-944.
 

2013

Kruse, A.C.,  Ring, A.M., Manglik, A., Hu, J., Hu, K., Eitel, K., Hübner, H., Pardon, E., Valant, V., Sexton, P.M. , Christopoulos, A., Felder, C., Gmeiner, P., Steyaert, J., Weis, W.I., K., Garcia, K., Wess, J., & Kobilka, B.K. (2013) Activation and allosteric modulation of a muscarinic acetylcholine receptor. Nature 504, 101-106.

 

Oyen, D., Wechselberger, R., Srinivasan, V., Steyaert, J., & Barlow, J. N. (2013). Mechanistic analysis of allosteric and non-allosteric effects arising from nanobody binding to two epitopes of the dihydrofolate reductase of Escherichia coli. BBA-Proteins and Proteomics 1834, 2147-2157.

 

Löw, C., Yau, Y. H., Pardon, E., Jegerschöld, C., Wåhlin, L., Quistgaard, E. M., Moberg, P., Geifman-Shochat, S., Steyaert, J. & Nordlund, P. (2013). Nanobody Mediated Crystallization of an Archeal Mechanosensitive Channel. PloS one 8, e77984.

 

Yuan, J., Zhan, Y.-A., Abskharon, R., Xiao, X., Martinez, M. C., Zhou, X., Kneale, G., Mikol, J., Lehmann, S., Surewicz, W.K., Castilla, J., Steyaert, J., Zhang, Z., Kong, Q., Petersen, R.B., Wohlkonig, A. & Zou, W-Q (2013) Recombinant Human Prion Protein Inhibits Prion Propagation in vitro. Nature Scientific Reports 3, 2911.

 

De Genst, E. J., Chan, P. H., Pardon, E., Hsu, S. T., Kumita, J. R., Christodoulou, J., Menzer, L., Chirgadze, D. Y., Robinson, C. V., Muyldermans, S., Matagne, A., Wyns, L., Dobson, C. M., Dumoulin, M. (2013). A Nanobody Binding to Non-amyloidogenic Regions of the Protein Human Lysozyme Enhances Partial Unfolding but Inhibits Amyloid Fibril Formation. The journal of physical chemistry B 117, 13245-13258.

 

Saskia Vanderhaegen, S.,  Fislage, M.,  Katarzyna Domanska,  K., Versées, W., Pardon, E., Bellotti, V., & Steyaert, J. (2013) Structure of an early native-like intermediate of β2-microglobulin amyloidogenesis. Protein Science 22, 1349-1357.

 

Ward, A., Szewczyk, P., Grimar, V., Lee, C.-W., Matrinez, L.,  Cay, A., Villaluz, M., Pardon, E., Cregger, C., Falsone, P.,  Urbatsch, I., Govaerts, C.,  Steyaert, J., and Chang, G. (2013) Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain, Proc. Natl. Acad. Sci. USA 110, 13386-13391.

 

Khamrui, S., Hol, W., Turley, S., Pardon, E.,Steyaert, J., Fan, E., Verlinde, C., Bergman, L.W. (2013) The structure of the D3 domain of Plasmodium falciparum myosin tail interacting protein MTIP in complex with a Nanobody, Molecular & Biochemical Parasitology 190, 87-91.  

 

Vercruysse,T., Boons, E., Venken, T., Vanstreels, E., Voet, A., Steyaert, J., De Maeyer, M., Daelemans, D. (2013) Mapping the Binding Interface between an HIV-1 Inhibiting Intrabody and the Viral Protein Rev. PLoS one 8, e60259

 

Sohier, J.S., Laurent C., Chevigne A., Pardon E., Srinivasan V., Wernery U., Steyaert J., Galleni M. (2013) Allosteric inhibition of VIM metallo-beta-lactamases by a camelid nanobody. Biochemical Journal 15, 477-86

 

Vuchelen, A., Pardon, E., Steyaert, J., Gamain, B., Loris, R., van Nuland, N.A. J., Ramboarina, S. (2013) Production, crystallization and X-ray diffraction analysis of two nanobodies against the Duffy binding-like (DBL) domain DBL6∊-FCR3 of the Plasmodium falciparum VAR2CSA protein. Acta Crystallographica Section F 69, 270-274. 

 

Banner, D. W., Gsell, B., Benz, J., Bertschinger, J., Burger, D., Brack, S., Cuppuleri, S., Debulpaep, M., Gast, A., Grabulovski, D., Hennig, M., Hilpert, H., Huber, W., Kuglstatter, A., Kusznir, E., Laeremans, T., Matile, H., Miscenic, C., Rufer, A. C., Schlatter, D., Steyaert, J., Stihle, M., Thoma, R., Weber, M. & Ruf, A. (2013) Mapping the conformational space accessible to BACE2 using surface mutants and cocrystals with Fab fragments, Fynomers and Xaperones. Acta Crystallographica Section D 69, 1124-1137

 

Rivera-Calzada, A., Fronzes , R., Savva C.  G., Chandran, V., Lian, P. W. , Laeremans, T., Pardon, E., Steyaert, J., Remaut, H., Waksman, G., & Orlova E. V. (2013) Structure of a bacterial type IV secretion core complex at subnanometer resolution. EMBO J. 32, 1195 - 1204

 

Guilliams, T., T., El-Turk, F., Buell, A.K., O'Day, E.M. Aprile, F.A.,  Esbjörner, E.K.,  Vendruscolo, M., Cremades, N., Pardon, E., Wyns, L., Welland, M.E., Steyaert, J., Christodoulou, J., Dobson, C.M. & De Genst, E. (2013) Nanobodies raised against monomeric b-synuclein distinguish between fibrils at different maturation stages. J Mol Biol 425, 2397–2411  

 

JMB commentary: The Mysterious C-Terminal Tail of Alpha-Synuclein: Nanobody's Guess. JMB 4252393-2396

 

Irannejad, R., Tomshine, J.C., Tomshine, J.R., Steyaert, J., Rasmussen, S., Sunahara, R., Chevalier, M., El-Samad, H., Huang, B., & von Zastrow, M. (2013) Conformational biosensors reveal adrenoceptor signaling from endosomes. Nature 495, 534-538.

 

News & views: Lohse, M.J. & Calebiro, D. (2013) Cell biology: Receptor signals come in waves. Nature 495, 457-458.
 

Van Laer, K., Dziewulska, A. M., Fislage, M., Wahni, K., Hbeddou, A. A., Collet, J.-F., Versées, W., Mateos, L. M., Tamu Dufe, V., Messens, J. (2013) NrdH-redoxin of Mycobacterium tuberculosis and Corynebacterium glutamicum Dimerizes at High Protein Concentration and Exclusively Receives Electrons from Thioredoxin Reductase. Journal of Biological Chemistry 288, 7942-7955.

 

2012

Park, Y.-J.,   Budiarto, T., Wu, M., Pardon, E., Steyaert, J., & Hol, W.G.J. (2012) 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, Nucleic acids res 406966-6977.

 

Baranova, E., Fronzes, R., Garcia-Pino, A., Van Gerven, N, Papapostolou, D., Péhau-Arnaudet, Pardon, E., Steyaert, J., Howorka, S. & Remaut, H. (2012) SbsB structure and lattice reconstruction unveil Ca2+ triggered S-layer assembly, Nature 487, 119-122.

 

Park, Y.J., Pardon, E., Wu, M., Steyaert, J. & Hol, W.G.J (2012) Crystal structure of a heterodimer of editosome interaction proteins in complex with two copies of a cross-reacting nanobody. Nucleic acids res 40, 1828-1840

 

Fislage, M., Roovers, M., Tuszynska, I., Bujnicki, J. M., Droogmans, L., & Versees, W. (2012) Crystal structures of the tRNA:m2G6 methyltransferase Trm14/TrmN from two domains of life. Nucleic Acids Res 40, 5149-5161.

 

Roovers, M., Oudjama, Y., Fislage, M., Bujnicki, J. M., Versees, W., & Droogmans, L. (2012). The open reading frame TTC1157 of Thermus thermophilus HB27 encodes the methyltransferase forming N(2)-methylguanosine at position 6 in tRNA. RNA 18, 815-824.

 

Kint, C. I., Verstraeten, N., Wens, I., Liebens, V. R., Hofkens, J., Versees, W., Fauvart, M., Michiels, J. (2012). The Escherichia coli GTPase ObgE modulates hydroxyl radical levels in response to DNA replication fork arrest. FEBS J. 279, 3692-3704

 

2011

Abskharon, R.N.N., Soror, S.H., Pardon, E, El Hassan, H., Legname, G., Steyaert, J., Wohlkonig, A. (2011) Combining in-situ proteolysis and microseed matrix screening to promote crystallization of PrP(c)-nanobody complexes. Protein Engineering Design & Selection 24, 737-741.

 

Miśkiewicz, K., Jose, L.E., Bento, A.A., Fislage, M., Taes, I., Kasprowicz, J., Swerts, J., Sigrist, S., Versées, W., Robberecht, W., Verstreken, P. (2011) Elp3 controls active zone morphology by acetylating the ELKS family member Bruchpilot. Neuron 72(5), 776-788.

 

Westfield, G., Rasmussen, S.G.F,  Su M., Dutta, S, DeVree, B.T., Chung, K.Y., Calinski, D., Velez-Ruiz, G., Oleskie, A.N., Pardon, E., Chae, P.S., Liu, T., Li, S., Woods Jr., V.L., Steyaert, J., Kobilka, B.K., Sunahara, R.K. & Skiniotis, G. (2011) Structural flexibility of the Gαs α-helical domain in the β2-adrenoceptor Gs Complex. Proc. Natl. Acad. Sci. USA 108, 16086-16091.  

 

Korotkov K.V., Johnson T.L., Jobling M.G., Pruneda J., Pardon E., Héroux, A., Turley, S., Steyaert, J., Holmes, R.K., Sandkvist, M., & Hol, W.G.J. (2011) Structural and Functional Studies on the Interaction of GspC and GspD in the Type II Secretion System. PLoS Pathog 7(9): e1002228. doi:10.1371/journal.ppat.1002228. 

 

Rasmussen, S.G.F, DeVree, B.T., Zou, Y, Kruse, A.C., Chung, K.Y.,Thian, T.S., Thian, F.S., Chae, P.S., Pardon, E., Calinski, D., Mathiesen, J.M., Shah, S.T.A., Lyons, J.A., Caffrey, M., Gellman, S.H., Steyaert, J., Skiniotis, G., Weis, W., Sunahara, R.K., Kobilka, B.K. (2011) Crystal Structure of the b2 Adrenergic Receptor-Gs protein complex. Nature 477, 549–555.

 

News in Focus: Buchen L (2011) Cell signaling caught in the act. Nature 475, 273-274

News & Views: Schwartz, T.W. & Sakmar, T.P. (2011) Structural biology: Snapshot of a signalling complex. Nature 477, 540-541

365 days: Interactive timeline: Van Noorden R. (2011) A clickable calendar. Nature doi:10.1038/nature.2011.9686

Cell-signalling work nets chemistry Nobel: Van Noorden R. (2012) Kobilka and Lefkowitz win award for decades of research on G-protein-coupled receptors. Nature doi:10.1038/nature.2012.11557
 

Steyaert, J. & Kobilka, B.K. (2011) Nanobody stabilization of G protein coupled receptor conformational states. Current Opinion in Structural Biology 21, 567-572

 

Vercruysse, T., Pawar, S., De Borggraeve, W., Pardon, E., Pavlakis, G.N., Pannecouque, C.,  Steyaert, J., Balzarini, J. & Daelemans, D. (2011) Measuring cooperative Rev protein-protein interactions on Rev Responsive RNA by fluorescence resonance energy transfer. RNA Biology 8, 316-324.

 

Domanska, K., Vanderhaegen, S, Srinivasan , V.,  Pardon, E., Dupeux, F., Marquez,J.A., Gorgetti, S., Stoppini, M., Wyns, L., Bellotti, V. & Steyaert, J. (2011) Atomic structure of a nanobody trapped intermediate of β2m amyloidogenesis, Proc. Natl. Acad. Sci. USA 108, 1314-1319

 

Verstraeten, N., Fauvart, M., Versées, W., Michiels, J. (2011) The universally conserved prokaryotic GTPases. Microbiol Mol Biol Rev. 75 (3), 507-42.

 

Oyen, D., Srinivasan, V., Steyaert, J., & Barlow, JN. (2011) Constraining enzyme conformational change by an antibody leads to hyperbolic inhibition. J. Mol. Biol. 407, 138-48

 

Rasmussen, S.G.F., Choi, H.-J., Fung, J.-J., Pardon, E., Casarosa, P., Seok Chae, P. , 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. (2011) Structure of a nanobody-stabilized active state of the β2 adrenoceptor. Nature 469, 175-80.

 

News and Views: Sprang, S.R. (2011) Cell signalling: Binding the receptor at both ends. Nature 469, 172-173.
 

Wu, M., Park, Y.-U., Pardon, E., Guo, X., Turley, S., Stuart, K. S., Hayhurst, A., Deng, J., Steyaert, J. and Hol, W.G.J. (2011) Structures of a key interaction protein from the trypanosoma brucei editosome in complex with single domain antibodies, J. Struct. Biol. 174, 124-136

 

Miśkiewicz, K., Jose, Liya E., Bento-Abreu, A., Fislage, M., Taes, I., Kasprowicz, J., Swerts, J., Sigrist, S., Versées, W., Robberecht, W., Verstreken, P. (2011). ELP3 Controls Active Zone Morphology by Acetylating the ELKS Family Member Bruchpilot. Neuron 72, 776-788. 

 

Fislage, M., Roovers, M., Munnich, S., Droogmans, L., & Versées, W. (2011). Crystallization and preliminary X-ray crystallographic analysis of putative tRNA-modification enzymes from Pyrococcus furiosus and Thermus thermophilus. Acta Crystallographica Section F 67, 1432-1435. 
 
Verstraeten, N., Fauvart, M., Versees, W., & Michiels, J. (2011). The universally conserved prokaryotic GTPases. Microbiol Mol Biol Rev 75, 507-542
 

2010

Abskharon R.N., Soror S.H., Pardon E., El Hassan H., Legname G., Steyaert J. & Wohlkonig A. (2010) Crystallization and preliminary X-ray diffraction analysis of a specific VHH domain against mouse prion protein. Acta Crystallogr Sect F Struct Biol Cryst Commun. 66, 1644-1646. 

 

De Genst, E., Guilliams, T., Wellens, J., O' Day, E., Waudby, C., Meehan, C., Dumoulin, M., Hsu, S.T-D., Cremades, N., Verschueren, K., Pardon, E., Wyns, L., Steyaert, J., Christodoulou, J. & Dobson, C. (2010) Structure and properties of a complex of α-synuclein and a single domain camelid antibody,  J. mol. Biol  402,  326-343. 

 

Vandemeulebroucke, A., Minici, C., Bruno, I., Muzzolini, L., Tornaghi, P., Parkin, D., Schramm, V.L., Versées, W.,  Steyaert, J., & Degano, M.  (2010) Structure, function, and inhibition of the principal nucleotide catabolic enzyme in the purine-auxotrophic Trypanosoma brucei brucei. Biochemistry 49, 8999-9010.

 

Berg, M., Kohl, L., Van der Veken, P., Joossens, J., Al-Salabi, MI., Castagna, V., Giannese, F., Cos, P., Versées, W., Steyaert, J., Grellier, P., Haemers, A., Degano, M., Maes, L., de Koning, H.P. & Augustyns, K.  (2010) Evaluation of nucleoside hydrolase inhibitors for treatment of African trypanosomiasis. Antimicrobial agents and chemotherapy 54, 1900-8. 

 

Vercruysse, T., Pardon, E., Vanstreels, E., Steyaert, J., & Daelemans, D. (2010). An intrabody based on a llama single-domain antibody targeting the N-terminal alpha-helical multimerization domain of HIV-1 rev prevents viral production. J.biol. chem. 285, 21768-80. 

 

Van den Abbeele,  A., De Clercq, S. , De Ganck, A., De Corte, V,  Van Loo, B., Soror, S. H., Srinivasan, V., Steyaert, J., Vandekerckhove, J., and Gettemans, J. (2010) A llama-derived gelsolin single domain antibody blocks gelsolin–G-actin interaction. Cellular and Molecular Life Sciences 67, 1519-1535. 

 

Ryckaert, S., Pardon, E., Steyaert, J., & Callewaert, N. (2010) Isolation of antigen-binding camelid heavy chain antibody fragments (nanobodies) from an immune library displayed on the surface of Pichia pastoris. J. of Biotechnology 145, 93-98. 

 

Versees, W., De Groeve, S., & Van Lijsebettens, M. (2010). Elongator, a conserved multitasking complex? Molecular Microbiology 76, 1065-1069. 

 

Berg, M., Kohl, L., Van der Veken, P., Joossens, J., Al-Salabi, M. I., Castagna, V., Giannese, F., Cos, P., Versees, W., Steyaert, J., Grellier, P., Haemers, A., Degano, M., Maes, L., de Koning, H. P., Augustyns, K. (2010). Evaluation of nucleoside hydrolase inhibitors for treatment of African trypanosomiasis. Antimicrob Agents Chemother 54, 1900-1908.

 

2009

De Vocht, C., Ranquin, A., Willaert, R., Van Ginderachter, J., Vanhaecke, T., Rogiers, V., Versées, W., Van Gelder, P. & Steyaert, J. (2009) Assessment of stability, toxicity and immunogenicity of new polymeric nanoreactors for use in enzyme replacement therapy of MNGIE. J. of Contr. Rel. 137, 246-254. 

 

Barlow, J., Conrath, K., & Steyaert, J. (2009) Substrate-dependent modulation of enzyme activity by allosteric effector antibodies. Biochim. Biophys. Acta 1794, 1259-1268. 

 

Versées, W., Goeminne, A., Berg, M., Vandemeulebroucke, A., Haemers, A., Augustyns, K., & Steyaert,  J. (2009) Crystal structures of T. vivax nucleoside hydrolase in complex with new potent and specific inhibitors Biochim. Biophys. Acta 1794, 953-960. 

 

Berg, M., Bal, G., Goeminne, A., Van Der Veken, P., Versées, W., Steyaert, J., Haemers, A., Augustyns, K.  (2009) Synthesis of bicyclic N-arylmethyl-substituted iminoribitol derivatives as selective nucleoside hydrolase inhibitors. Chem. Med. Chem  4, 249-260. 

 

Korotkov K. V., Pardon E., Steyaert J. &  Hol W. (2009) Crystal Structure of the N-Terminal Domain of the Secretin GspD from ETEC Determined with the Assistance of a Nanobody. Structure 17, 255-265

 

Lam, A. Y., Pardon, E., Korotkov K. V., Hol, W.G.J & Steyaert, J. (2009) Crystal structure of the EpsI:EpsJ pseudopilin heterodimer from Vibrio vulnificus in complex with a nanobody, J. Struct. Biol. 166, 8-15. 

 

Meyer, S., Wittinghofer, A., & Versees, W. (2009). G-domain dimerization orchestrates the tRNA wobble modification reaction in the MnmE/GidA complex. J Mol Biol 392, 910-922.

 

2008

Vandemeulebroucke, A., De Vos, S., Van Holsbeke, E., Steyaert, J. & Versées, W. (2008) A flexible loop as a functional element in the catalytic mechanism of Nucleoside hydrolase from Trypanosoma vivax. J. Biol. Chem. 283, 22272-82. 

 

Goeminne, A., Berg, M., Mcnaughton, M., Bal, G., Surpateanu, G., Van Der Veken, P., De Prol, S., Versées, W., Steyaert, J., Haemers, A. & Augustyns, K. (2008) N-Arylmethyl substituted iminoribitol derivatives as inhibitors of a purine specific nucleoside hydrolase Bioorg. & Med. Chem. 16, 6752-6763.

 

Goeminne,  A., Mcnaughton, M., Bal, G., Surpateanu, G., Van Der Veken, P., De Prol, S., Versees, W., Steyaert, J., Haemers, A., Augustyns, K. (2008) Synthesis and biochemical evaluation of guanidino-alkyl-ribitol derivatives as nucleoside hydrolase inhibitors. Eur. J. Med. Chem. 43, 315-326. 

 

Meyer, S., Scrima, A., Versees, W., & Wittinghofer, A. (2008) Crystal structures of the conserved tRNA-modifying enzyme GidA: implications for its interaction with MnmE and substrate. J Mol Biol 380, 532-547.

 

2007

Barlow, J. N. & Steyaert, J (2007) Examination of the mechanism and energetic contribution of leaving group activation in the purine-specific nucleoside hydrolase from Trypanosoma vivax, BBA 1774, 1451–1461. 

 

Spaepen, S., Versées, W., Gocke, D., Pohl, M., Steyaert, J., & Vanderleyden, J (2007) Characterization of Phenylpyruvate Decarboxylase, Involved in Auxin Production of Azospirillum brasilense. J. of Bacteriology 189, 7626-7633. 

 

Versees, W., Spaepen, S., Wood, M., Leeper, F., Vanderleyden, J., & Steyaert, J. (2007) Molecular Mechanism of allosteric substrate activation in a thiamine diphosphate-dependent decarboxylase, J.Biol. Chem. 282, 35269-35278. 

 

Goeminne, A., McNaughton, M., Bal, G., Surpateanu, G., Van Der Veken, P., De Prol, S., Versées, W., Steyaert, J., Haemers, A., Augustyns, K. (2007) 1,2,3-Triazolylalkylribitol derivatives as nucleoside hydrolase inhibitors. Bioorg. & Med. Chem. Lett. 17, 2523-2526. 

 

Versees, W., Spaepen, S., Vanderleyden, J., Steyaert J. (2007) The crystal structure of phenylpyruvate decarboxylase from Azospirillum brasilense at 1.5 A resolution. FEBS J. 274, 2363-75.

 

2006

Vandemeulebroucke, A., Versées, W., Steyaert, J. & Barlow, J. (2006) Multiple transients in the pre-steady-state of nucleoside hydrolase reveal complex substrate binding, product base release, and two apparent rates of chemistry. Biochemistry 45, 9307-7318.

 

Versees, W., Barlow, J., & Steyaert, J. (2006) Transition-state complex of the purine-specific nucleoside hydrolase of T. vivax: enzyme conformational changes and implications for catalysis, J. Mol. Biol. 359, 331-346.

 

Muzzolini, L., Versees, W., Tornaghi, P., Van Holsbeke, E., Steyaert, J. & Degano, M. (2006) New insights into the mechanism of nucleoside hydrolases from the crystal structure of the Escherichia coli YbeK protein bound to the reaction product. Biochemistry 24, 773-82. 

 

Loverix, S., Versees, W., Steyaert, J. & Geerlings, P. (2006) Quantum Chemical Study of Leaving Group Activation in T. vivax Nucleoside Hydrolase. Int. J. Quantum Chem. 106, 565-570. 

 

2005

Ranquin, A., Wim Versées, W., Meier, W., Steyaert, J, and Van Gelder, P. (2005) Therapeutic Nanoreactors: Combining Chemistry and Biology in a Novel Triblock Copolymer Drug Delivery System. Nanoletters 5, 2220-4. 

 

Huysmans G., Ranquin A., Wyns L., Steyaert J. & Van Gelder P. (2005) Encapsulation of therapeutic nucleoside hydrolase in functionalised nanocapsules. J Control Release.  102, 171-179.

 

Mignon, P., Loverix, S., Steyaert, J. & Geerlings, P. (2005) Influence of the p–p interaction on the hydrogen bonding capacity of stacked DNA/RNA bases. Nucleic Acids Research 33, 1779–1789.

 

Loverix, S., Geerlings, P., McNaughton, P., Augustyns, K., Vandemeulebroucke, A., Steyaert, J. & Versées, W. (2005) Substrate-assisted Leaving Group Activation in Enzyme-catalyzed N-Glycosidic Bond Cleavage, J. Biol. Chem 280, 14799–14802.

 

2004

Versées, W, Loverix, S., Vandemeulebroucke, A., Geerlings, P., & Steyaert, J. (2004) Leaving group activation by aromatic stacking: an alternative to general acid catalysis. J. Mol. Biol. 338, 1-6.

 

Mignon, P., Loverix, S., Steyaert, J. & Geerlings, P. (2004) Functional assesment of “in vivo” and “in silico” mutations in the Guanie Binding Site of RNase T1: A DFT Study, Int J Quantum Chem. 99, 53-58

 

2003

Vandemeulebroucke, A., Versées, W., De Vos, S., Van Holsbeke, E., & Steyaert, J. (2003) Pre-Steady State Analysis of the Nucleoside Hydrolase of Trypanosoma vivax. Evidence for half-of- the-sites reactivity and rate limiting product release. Biochemistry 44, 12902-12908.

 

Versées, W. & Steyaert, J. (2003) Catalysis by inosine-adenosine-guanosine-preferring nucleoside hydrolases. Current opinion in structural biology 13, 731-738.

 

Versées, W., Van Holsbeke, E., De Vos, S., Decanniere, K., Zegers, I. & Steyaert, J. (2003) Cloning, preliminary characterization, and crystallization of nucleoside hydrolases from Caenorhabditis elegans and Campylobacter jejuni. Acta Crystallographica D59, 1087–1089.

 

Loverix, S. & Steyaert, J. (2003) Ribonucleases: from prototypes to therapeutic targets ? Current Medicinal Chemistry 10, 1241-1253.

 

2002

Mignon, P., Steyaert, J., Loris, R., Geerlings, P. & Loverix, S. (2002) A nucleophyle activation dyad in ribonucleases: a combined X-ray crystallographic/ ab initio quantum chemical study. Journal Bioogical Chemistry 277, 36770-36774.

 

Versées, W., Decanniere, K., Van Holsbeke E., Devroede, N. & Steyaert, J. (2002) Enzyme-Substrate Interactions in the Purine-Specific Nucleoside Hydrolase from Trypanosoma vivax. Journal Biological Chemistry 277, 15938-15946.

 

2001

De Vos, S., Backmann, J., Steyaert, J., & Loris, R. (2001) Hydrophobic core manipulations in RNase T1, Biochemistry 40, 10140-10149.

 

Deswarte, J., De Vos, S., Langhorst, U., Steyaert, J., & Loris, R. (2001) The contribution of metal ions to the conformational stability of RNase T1: crystal vs. solution. European Journal of Biochemistry 268, 3993-4000.

 

Versées, W., Decanniere, K., Pellé, R., Depoorter, J., Parkin, D.W., & Steyaert, J. (2001) Structure and Function of a novel Purine-Specific Nucleoside Hydrolase from Trypanosoma vivax. Journal Molecular Biology 307, 1363-1379.

 

Loverix, S., & Steyaert, J. (2001) Mechanistic analyses of RNase T1. Methods in Enzymology 341, 305-323.

 

2000

Loverix, S., Winquist, A., Strömberg, R., & Steyaert, J. (2000) Mechanism of RNase T1: concerted triester-like phosphoryl transfer via a catalytic three-centered hydrogen bond. Chemistry & Biology 7, 651-658.

 

Langhorst, U., Backmann, J., Loris, R., & Steyaert, J. (2000) Water mediated interactions in proteins: thermodynamic analysis of a hydration site in RNase T1, Biochemistry 39, 6586-6593.

 

1999

Huyghues-Despointes, B.M., Langhorst, U., Steyaert, J.,  Pace, C.N., & Scholtz, J.M. (1999) Hydrogen-exchange stabilities of RNase T1 and variants with buried and solvent-exposed Ala>Gly mutations in the helix. Biochemistry 38, 16481-16490.

 

Loris, R., De Vos, S., Langhorst, U., Decanniere, K., Bouckaert, J., Maes, D., Transue, T.R., & Steyaert, J. (1999) Conserved Water Molecules in a Large Family of Microbial Ribonucleases, Proteins 36, 117-134.

 

Langhorst, U., Loris, R., Denisov, V.P., Doumen, J., Roose, P., Maes, D., Halle, B., & Steyaert, J. (1999) Dissection of the structural and functional role of a conserved hydration site in RNase T1, Protein science 8,  722-730.

 

1998

Loverix, S., Laus, G., Martins, J., Wyns, L., & Steyaert, J. (1998) Reconsidering the energetics of Ribonuclease Catalyzed RNA hydrolysis. European Journal of Biochemistry 257, 286-290.

 

Dao-Thi, T.R. Transue, Pellé, R., Murphy, N.B., Poortmans, F., & Steyaert, J. (1998) Expression, Purification, Crystallization and preliminary X-ray analysis of cyclophylin of the bovine parasite Trypanosoma bucei brucei. Acta Crystallographica D54, 1046-1048.

 

Loverix, S., Winquist, A., Strömberg, R., & Steyaert, J. (1998) An engineered Ribonuclease specific for thiophosphate RNA. Nature Structural Biology 5, 365-368.

 

Zegers,I., Loris, R., Dehollander,G., Haikal, A., F., Poortmans, F., Steyaert, J., & Wyns, L. (1998) The hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analysed by time-resolved crystallography. Nature Structural Biology 5, 280-283.

 

De Vos, S., Doumen, J.,  Langhorst, U., & Steyaert, J. (1998) Dissecting Histidine Interactions of Ribonuclease T1 with Asparagine and Glutamine Replacements: Analysis of Double Mutant Cycles at one Position. Journal Molecular Biology 275, 541-661.

 

1997

Steyaert, J. (1997) Review. A decade of protein engineering on Ribonuclease T1. European Journal of Biochemistry 247, 1-11.

 

Loverix, S., Doumen, J., & Steyaert, J. (1997) Additivity of Protein-Guanine Interactions in Ribonucleases T1. The Journal of Biological Chemistry 272, 9635-9639.

 

1996

Doumen, J., Gonciarz, M., Zegers, I., Loris, R. Wyns, L., & Steyaert, J. (1996) A catalytic function for the structurally conserved residue Phe100 of ribonuclease T1. Protein Science 5, 1523-1530.

 

1995

Steyaert, J., & Engelborghs, Y. (1995) A two binding site kinetic model for the ribonuclease catalysed depolymerisation of dinucleoside phosphate substrates.  European Journal of Biochemistry 233, 140-144.

 

Fish, W., R., Nkhungulu, Z., M., Muriuki, C., W., Ndegwa, D., M., Londsdale-Eccles, J., D., & Steyaert, J. (1995) Primary structure and partial characterization of a life-cycle-regulated cysteine protease from Trypanosoma (Nannomonas) congolense. Gene 161, 125-128.

 

1994

Steyaert, J., Haikal, A. F., and Wyns, L. (1994) Investigation of the functional interplay between the primary site and the subsite of RNase T1: Kinetic analysis of single and double mutants for modified substrates  Proteins: Structure, Function and Genetics 18, 318-323.

 

Pletinckx J., Steyaert J., Hui-Woog Choe, Heinemann, U., & Wyns, L. (1994) Crystallographic study of Glu58 RNase T1*2'-guanosine monophosphate at 1.9 A resolution. Biochemistry 33, 1654-1662.

 

1993

Loris, R., Steyaert, J., Maes, D., Lisgarten J., Pickersgill, R., & Wyns, L. (1993) Crystal structure determination and refinement at 2.3 A resolution of the lentil lectin. Biochemistry 32, 8772-8781. Bernard, P., Kezdi, K., E., Van Melderen, L., Steyaert, J., Wyns, L., Pato, M. L., Higgins, P., N., and Couturier, M. (1993) The F plasmid ccdB protein induces efficient ATP-dependent DNA cleavage by gyrase. Journal Molecular Biology 234, 534-541.

 

Steyaert, J., Van Melderen, L., Bernard, P., Dao Thi, M. H., Loris, R., Wyns, L., & Couturier, M. (1993) Purification, Circular dichroism analysis, crystallization and primary X-ray diffraction analysis of the F plasmid CcdB killer protein. Journal Molecular Biolology. 203, 513-515.

 

Steyaert, J., & Wyns, L. (1993) Functional interactions among the His40, Glu58 and His92 catalysts of Ribonuclease T1 as studied by double and triple mutants. Journal Molecular Biology 229, 770-781.

 

1992

Zegers, I., Verhelst, P., Choe, H.-W., Steyaert, J., Heinemann, U., Saenger, W., & Wyns, L. (1992) Role of Histidine-40 in Ribonuclease T1 Catalysis: Three-Dimensional Structures of the Partially Active His40Lys Mutant. Biochemistry 31, 11317-11325.

 

Steyaert, J., Haikal, A. F., Stanssens, P., & Wyns, L. (1992) Dissection of the Ribonuclease T1 subsite: the transesterification kinetics of Asn36Ala and Asn98Ala RNase T1 for minimal dinucleoside phosphates. European Journal Biochemistry 203, 551-555.

 

1991

Steyaert, J., Haikel A. F., Wyns, L., & Stanssens, P. (1991) Subsite Interactions of Ribonuclease T1: Asn36 and Asn98 Accelerate GpN Transesterification through Interactions with the Leaving Nucleoside N. Biochemistry 30, 8666-8670.

 

Steyaert, J., Wyns, L., & Stanssens, P. (1991) Subsite Interations of Ribonuclease T1: Viscosity Effects Indicate That the Rate-Limiting Step of GpN Transesterification Depends on the Nature of N. Biochemistry 30, 8661-8665.

 

Steyaert, J., Opsomer, C., Wyns, L., & Stanssens, P. (1991) Quantitative Analysis of the Contribution of Glu46 and Asn98 to the Guanosine Specificity of Ribonuclease T1. Biochemistry 30, 494-499.

 

1990

Steyaert, J., Hallenga, K., Wyns, L., & Stanssens, P. (1990) Histidine-40 of Ribonuclease T1 Acts as Base Catalyst When the True Catalytic Base, Glutamic Acid-58, Is Replaced by Alanine. Biochemistry 29, 9064-9072.

 

1989

Shirley, B., A., Stanssens, P., Steyaert, J., & Pace, N. (1989) Conformational Stability and Activity of Ribonuclease T1 and Mutants. J. Biol. Chem. 264, 11621-11625.