J. Steyaert

发表

Crystal Structure of the β2Adrenergic Receptor-Gs protein complex

S. Rasmussen, Brian T DeVree, Y. Zou, 2011, Nature.

Structure of a nanobody-stabilized active state of the β2 adrenoceptor

S. Rasmussen, Brian T DeVree, T. S. Kobilka, 2010, Nature.

Structure of an endosomal signaling GPCR–G protein–β-arrestin megacomplex

Yong Zi Tan, J. Steyaert, R. Lefkowitz, 2019, Nature Structural & Molecular Biology.

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

E. Pardon, J. Steyaert, I. Lax, 2018, Nature.

Structural insights into μ-opioid receptor activation

Stephen M. Husbands, A. J. Venkatakrishnan, Ron O. Dror, 2015, Nature.

Structure and properties of a complex of α-synuclein and a single-domain camelid antibody.

C. Dobson, L. Wyns, E. Pardon, 2010, Journal of molecular biology.

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

D. Banner, A. Kuglstatter, J. Steyaert, 2013, Acta crystallographica. Section D, Biological crystallography.

A genetically encoded biosensor reveals location bias of opioid drug action

J. Steyaert, M. von Zastrow, A. Manglik, 2018, bioRxiv.

A Genetically Encoded Biosensor Reveals Location Bias of Opioid Drug Action

J. Steyaert, A. Manglik, M. Stoeber, 2018, Neuron.

Activation and allosteric modulation of a muscarinic acetylcholine receptor

J. Wess, K. Garcia, P. Sexton, 2013, Nature.

Structural Insights into Metabotropic Glutamate Receptor Activation

M. J. Robertson, T. S. Kobilka, E. Pardon, 2018, Nature.

Author Correction: Structural insights into the activation of metabotropic glutamate receptors

M. J. Robertson, T. S. Kobilka, J. M. Mathiesen, 2019, Nature.

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

Tong Liu, Georgios Skiniotis, Min Su, 2011, Proceedings of the National Academy of Sciences.

Probing the N-terminal β-sheet conversion in the crystal structure of the human prion protein bound to a nanobody.

Giuseppe Legname, Jan Steyaert, Els Pardon, 2014, Journal of the American Chemical Society.

Propagation of conformational changes during μ-opioid receptor activation

Aashish Manglik, Brian K. Kobilka, Sébastien Granier, 2015, Nature.

Allosteric Nanobodies Reveal the Dynamic Range and Diverse Mechanisms of GPCR Activation

Aashish Manglik, Jan Steyaert, Ryan T. Strachan, 2016, Nature.

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

E. Vanstreels, J. Steyaert, Tom Venken, 2013, PloS one.

Nanobodies to Study G Protein-Coupled Receptor Structure and Function.

J. Steyaert, B. Kobilka, A. Manglik, 2017, Annual review of pharmacology and toxicology.

Conserved water molecules in a large family of microbial ribonucleases

K. Decanniere, T. Transue, D. Maes, 1999, Proteins.

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

Benjamin Bishop, Mark S. P. Sansom, Tomas Malinauskas, 2019, Nature Chemical Biology.

Heteromeric GABAA receptor structures in positively-modulated active states

F. Dimaio, M. Babu, R. Esnouf, 2018, bioRxiv.

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

D. Bertrand, E. Pardon, J. Steyaert, 2020, eLife.

A Functionally Conserved Mechanism of Modulation via a Vestibule Site in Pentameric Ligand-Gated Ion Channels

D. Bertrand, E. Pardon, J. Steyaert, 2019, bioRxiv.

Crystal and cryo-EM structures of the cytosolic G protein alpha chaperone and guanine nucleotide exchange factor Ric-8A bound to Gαi1

S. Sprang, W. Chiu, J. Steyaert, 2020, bioRxiv.

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

S. Sprang, W. Chiu, J. Steyaert, 2020, Nature Communications.

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

C. Vanhove, S. Muyldermans, J. Steyaert, 2016, Contrast media & molecular imaging.

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

J. Steyaert, D. Fourmy, V. Nikolaev, 2016, Biochemical pharmacology.

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

J. Martial, D. Maes, J. Meiler, 2016, Journal of structural biology.

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

L. Wyns, J. Steyaert, P. Stanssens, 1990, Biochemistry.

Encapsulation of therapeutic nucleoside hydrolase in functionalised nanocapsules.

L. Wyns, J. Steyaert, P. van Gelder, 2005, Journal of controlled release : official journal of the Controlled Release Society.

Functional assessment of “in vivo” and “in silico” mutations in the guanine binding site of RNase T1: A DFT study

J. Steyaert, P. Geerlings, P. Mignon, 2004 .

A Nucleophile Activation Dyad in Ribonucleases

J. Steyaert, P. Geerlings, R. Loris, 2002, The Journal of Biological Chemistry.

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

W. Stec, E. Pardon, J. Steyaert, 2019, Nature.

Megabodies expand the nanobody toolkit for protein structure determination by single-particle cryo-EM

E. Pardon, J. Steyaert, W. Vranken, 2019, Nature Methods.

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

J. Steyaert, N. Triballeau, K. Conrath, 2017, Journal of medicinal chemistry.

Structure of autoinhibited Akt1 reveals mechanism of PIP3-mediated activation

T. Leonard, E. Pardon, J. Steyaert, 2021, Proceedings of the National Academy of Sciences.

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

F. Buckner, C. Verlinde, W. Hol, 2017, Biochimie.

Nanobody-enabled monitoring of kappa opioid receptor states

Reid H. J. Olsen, B. Roth, E. Pardon, 2020, Nature Communications.

Structure of autoinhibited Akt1 reveals mechanism of PIP3-mediated activation

T. Leonard, E. Pardon, J. Steyaert, 2021, Proceedings of the National Academy of Sciences.

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

N. Callewaert, E. Pardon, J. Steyaert, 2010, Journal of biotechnology.

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

E. Pardon, J. Steyaert, G. Legname, 2011, Protein engineering, design & selection : PEDS.

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

P. Tompa, E. Pardon, J. Steyaert, 2018, Methods in enzymology.

Structural basis of sodium-dependent bile salt uptake into the liver

E. Pardon, J. Steyaert, N. Reyes, 2022, Nature.

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

J. Steyaert, J. Hanson, M. Meyrath, 2018, Biochemical pharmacology.

Influenza A virus RNA polymerase structures provide insights into viral genome replication

E. Pardon, J. Steyaert, J. Grimes, 2019, Nature.

Dissecting lipid contents in the distinct regions of native retinal rod disk membranes

Elliot H. Choi, A. Saghatelian, K. Palczewski, 2021, bioRxiv.

Investigation of the functional interplay between the primary site and the subsite of RNase T1: Kinetic analysis of single and multiple mutants for modified substrates

L. Wyns, J. Steyaert, A. Haikal, 1994, Proteins.

Structure of the human alpha1beta3gamma2 GABA-A receptor in a lipid bilayer

E. Pardon, J. Steyaert, K. Miller, 2019 .

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

L. Wyns, J. Steyaert, P. Stanssens, 1991, Biochemistry.

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

J. Steyaert, W. Versées, P. Van der Veken, 2008, European journal of medicinal chemistry.

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

J. Fernández-Recio, E. Pardon, J. Steyaert, 2019, Nature Communications.

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

Ryan T. Strachan, G. Pasternak, R. Stevens, 2018, Cell.

Nanobodies targeting LexA autocleavage disclose a novel suppression strategy of SOS-response pathway.

L. Van Melderen, E. Pardon, J. Steyaert, 2022, Structure.

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

S. Rasmussen, Brian T DeVree, E. Pardon, 2016, Nature.

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

E. Pardon, J. Steyaert, G. Legname, 2014 .

Quantum chemical study of leaving group activation in T. vivax nucleoside hydrolase

J. Steyaert, P. Geerlings, W. Versées, 2006 .

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

R. Wintjens, J. Steyaert, A. Baulard, 2017, Biochemical and biophysical research communications.

Production, crystallization and X-ray diffraction analysis of two nanobodies against the Duffy binding-like (DBL) domain DBL6ℇ-FCR3 of the Plasmodium falciparum VAR2CSA protein.

B. Gamain, E. Pardon, J. Steyaert, 2013, Acta crystallographica. Section F, Structural biology and crystallization communications.

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

K. Decanniere, J. Steyaert, I. Zegers, 2003, Acta crystallographica. Section D, Biological crystallography.

Influenza A virus RNA polymerase structures provide insights into viral genome replication

E. Pardon, J. Steyaert, J. Grimes, 2019, Nature.

Conformational biosensors reveal GPCR signalling from endosomes

Jonathan R. Tomshine, H. El-Samad, S. Rasmussen, 2013, Nature.

Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallograph

L. Wyns, J. Steyaert, R. Loris, 1998, Nature Structural Biology.

Dissecting histidine interactions of ribonuclease T1 with asparagine and glutamine replacements: analysis of double mutant cycles at one position.

J. Steyaert, U. Langhorst, S. De Vos, 1998, Journal of molecular biology.

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

L. Wyns, J. Steyaert, P. Stanssens, 1992, European journal of biochemistry.

Subsite interactions of ribonuclease T1: Asn36 and Asn98 accelerate GpN transesterification through interactions with the leaving nucleoside N.

L. Wyns, J. Steyaert, P. Stanssens, 1991, Biochemistry.

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

C. Pace, J. M. Scholtz, J. Steyaert, 1999, Biochemistry.

ChILL & DisCO to discover competitive, connective and allosteric Nanobodies that modulate the SOS1•RAS protein-protein interactions and tune the nucleotide exchange rate

E. Pardon, J. Steyaert, A. Sablina, 2022, bioRxiv.

Synthesis of Bicyclic N‐Arylmethyl‐Substituted Iminoribitol Derivatives as Selective Nucleoside Hydrolase Inhibitors

J. Steyaert, W. Versées, M. Berg, 2009, ChemMedChem.

Evaluation of Nucleoside Hydrolase Inhibitors for Treatment of African Trypanosomiasis

H. D. de Koning, J. Steyaert, M. Degano, 2010, Antimicrobial Agents and Chemotherapy.

Evaluation of nucleoside hydrolase inhibitors for the treatment of 1 African trypanosomiasis

J. Steyaert, M. Degano, W. Versées, 2010 .

Vrije Universiteit Brussel Structure and mechanism of the 6-oxopurine nucleosidase from Trypanosoma brucei

J. Steyaert, M. Degano, I. Bruno, 2010 .

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

J. Steyaert, W. Versées, M. Berg, 2009, Biochimica et biophysica acta.

N-Arylmethyl substituted iminoribitol derivatives as inhibitors of a purine specific nucleoside hydrolase.

J. Steyaert, W. Versées, M. Berg, 2008, Bioorganic & medicinal chemistry.

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

J. Steyaert, W. Versées, S. Apers, 2007, Bioorganic & medicinal chemistry letters.

Transition-state complex of the purine-specific nucleoside hydrolase of T. vivax: enzyme conformational changes and implications for catalysis.

J. Steyaert, W. Versées, J. Barlow, 2006, Journal of molecular biology.

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

J. Steyaert, M. Degano, W. Versées, 2006, Biochemistry.

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

Jan Steyaert, K. Decanniere, J. Steyaert, 2002, The Journal of Biological Chemistry.

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

K. Decanniere, J. Steyaert, W. Versées, 2022 .

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

J. Steyaert, W. Versées, R. Singh, 2017, Protein science : a publication of the Protein Society.

Catalysis by nucleoside hydrolases.

J. Steyaert, W. Versées, 2003, Current opinion in structural biology.

Influence of the π–π interaction on the hydrogen bonding capacity of stacked DNA/RNA bases

J. Steyaert, P. Geerlings, P. Mignon, 2005, Nucleic acids research.

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

R. Dutzler, E. Pardon, J. Steyaert, 2015, Nature Structural &Molecular Biology.

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

J. Steyaert, T. Laeremans, C. Blanchetot, 2016, mAbs.

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

M. Parmentier, J. Steyaert, J. Van Damme, 2016, The Journal of Immunology.

Regulation of Beta-2-Adrenergic Receptor Function by Conformationally Selective Single-domain Intrabodies

Ryan T. Strachan, S. Rasmussen, E. Pardon, 2013 .

In vitro reconstitution of dynamically interacting integral membrane subunits of energy-coupling factor transporters

E. Pardon, J. Steyaert, I. Setyawati, 2020, eLife.

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

G. Goodhill, E. Pardon, J. Steyaert, 2020, Proceedings of the National Academy of Sciences.

Vrije Universiteit Brussel Development by Genetic Immunization of Monovalent Antibodies ( Nanobodies ) Behaving as Antagonists of the Human ChemR 23 Receptor

M. Parmentier, J. Steyaert, T. Laeremans, 2017 .

Constraining enzyme conformational change by an antibody leads to hyperbolic inhibition.

J. Steyaert, D. Oyen, V. Srinivasan, 2011, Journal of molecular biology.

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

W. Hol, E. Pardon, J. Steyaert, 2011, PLoS pathogens.

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

J. Steyaert, R. Strömberg, S. Loverix, 2000, Chemistry & biology.

Substrate-assisted Leaving Group Activation in Enzyme-catalyzed N-Glycosidic Bond Cleavage*

J. Steyaert, P. Geerlings, W. Versées, 2005, Journal of Biological Chemistry.

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

B. Gamain, E. Pardon, J. Steyaert, 2014, Scientific Reports.

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

K. Decanniere, J. Steyaert, E. Brosens, 2022 .

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

E. Pardon, J. Steyaert, J. Kosiński, 2019, Journal of the American Chemical Society.

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

D. Bertrand, E. Pardon, J. Steyaert, 2016, PloS one.

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

Jan Steyaert, John E. Burke, Yohei Ohashi, 2015, Science.

Molecular Mechanism of Allosteric Substrate Activation in a Thiamine Diphosphate-dependent Decarboxylase*

J. Steyaert, J. Vanderleyden, W. Versées, 2007, Journal of Biological Chemistry.

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

E. Pardon, J. Steyaert, B. Kobilka, 2019, Scientific Reports.

Nanobodies as allosteric modulators of Parkinson’s disease–associated LRRK2

S. Knapp, E. Pardon, J. Steyaert, 2021, bioRxiv.

Nanobodies to study protein conformational states.

E. Pardon, J. Steyaert, T. Uchański, 2020, Current opinion in structural biology.

Nanobodies raised against monomeric α-synuclein distinguish between fibrils at different maturation stages.

Alexander K. Buell, C. Dobson, L. Wyns, 2013, Journal of molecular biology.

Nanobody CDR3 mimetics enhance SOS1-catalyzed nucleotide exchange on RAS

J. Steyaert, W. Versées, Alexandre Wohlkönig, 2022, bioRxiv.

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

Ronnie Willaert, Vera Rogiers, Tamara Vanhaecke, 2009, Journal of controlled release : official journal of the Controlled Release Society.

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

A. Schlessinger, E. Pardon, J. Steyaert, 2019, Proceedings of the National Academy of Sciences.

Domain-interface dynamics of CFTR revealed by stabilizing nanobodies

J. Riordan, E. Pardon, J. Steyaert, 2019, Nature Communications.

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

Y. Liu, E. Pardon, J. Steyaert, 2015, Nucleic acids research.

Snapshots of actin and tubulin folding inside the TRiC chaperonin

E. Pardon, J. Steyaert, W. Yue, 2021, Nature Structural & Molecular Biology.

Structure of the phosphoinositide 3-kinase p110γ-p101 complex reveals molecular mechanism of GPCR activation

Scott D. Hansen, E. Pardon, J. Steyaert, 2021, bioRxiv.

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

C. Pannecouque, E. Pardon, J. Steyaert, 2011, RNA biology.

Structure of the phosphoinositide 3-kinase (PI3K) p110γ-p101 complex reveals molecular mechanism of GPCR activation

Scott D. Hansen, E. Pardon, J. Steyaert, 2021, Science advances.

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

E. Pardon, J. Steyaert, G. Chang, 2013, Proceedings of the National Academy of Sciences.

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

R. Dutzler, E. Pardon, J. Steyaert, 2016, Nature Structural &Molecular Biology.

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

R. Dutzler, E. Pardon, J. Steyaert, 2014, Nature Structural &Molecular Biology.

A general protocol for the generation of Nanobodies for structural biology

S. Muyldermans, W. Hol, S. Rasmussen, 2014, Nature Protocols.

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

E. Pardon, J. Steyaert, K. Locher, 2017, Scientific Reports.

Structural insights into the activation of metabotropic glutamate receptors

M. J. Robertson, T. S. Kobilka, E. Pardon, 2019, Nature.

Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11

F. Förster, W. Baumeister, A. Bracher, 2014, Proceedings of the National Academy of Sciences.

Structure of PINK1 in complex with its substrate ubiquitin

E. Pardon, J. Steyaert, S. Freund, 2017, Nature.

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

J. Steyaert, R. Loris, J. Backmann, 2000, Biochemistry.

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

D. Maes, J. Steyaert, R. Loris, 2008, Protein science : a publication of the Protein Society.

Development of a universal nanobody-binding Fab module for fiducial-assisted cryo-EM studies of membrane proteins

J. Kowal, E. Pardon, J. Steyaert, 2021, Proceedings of the National Academy of Sciences.

Nanobody stabilization of G protein-coupled receptor conformational states.

Jan Steyaert, J. Steyaert, B. Kobilka, 2011, Current opinion in structural biology.

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

E. Pardon, J. Steyaert, J. Grimes, 2019, Nature.

GABAA receptor signalling mechanisms revealed by structural pharmacology

Jasenko Zivanov, Tomas Malinauskas, Jan Steyaert, 2019, Nature.

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

E. Orlova, G. Waksman, E. Pardon, 2013, The EMBO journal.

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

S. Howorka, E. Pardon, J. Steyaert, 2012, Nature.

Megabodies expand the nanobody toolkit for protein structure determination by single-particle cryo-EM

E. Pardon, J. Steyaert, J. Naismith, 2021, Nature Methods.

GABAA receptor signalling mechanisms revealed by structural pharmacology

Jasenko Zivanov, Tomas Malinauskas, Jan Steyaert, 2019, Nature.

Leaving group activation by aromatic stacking: an alternative to general acid catalysis.

Paul Geerlings, Jan Steyaert, J. Steyaert, 2004, Journal of molecular biology.

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

M. Parmentier, J. Steyaert, J. Pin, 2017, mAbs.

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

E. Pardon, J. Steyaert, G. Legname, 2019, PLoS pathogens.

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

E. Pardon, J. Steyaert, Young-Jun Park, 2012, Nucleic acids research.

A structure of substrate-bound Synaptojanin1 provides new insights in its mechanism and the effect of disease mutations

P. Verstreken, E. Pardon, J. Steyaert, 2020, eLife.

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

E. Vanstreels, E. Pardon, J. Steyaert, 2010, The Journal of Biological Chemistry.

A topological switch in CFTR modulates channel activity and sensitivity to unfolding

E. Pardon, J. Steyaert, A. Garcia-Pino, 2021, Nature Chemical Biology.

Nano-scale resolution of native retinal rod disk membranes reveals differences in lipid composition

Elliot H. Choi, A. Saghatelian, K. Palczewski, 2021, The Journal of cell biology.

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

E. Pardon, J. Steyaert, M. Galleni, 2013, The Biochemical journal.

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

Jan Steyaert, J. Steyaert, W. Versées, 2005, Nano letters.

Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody.

Jan Steyaert, Wim G J Hol, Els Pardon, 2009, Structure.

Recombinant Human Prion Protein Inhibits Prion Propagation in vitro

J. Steyaert, J. Castilla, W. Surewicz, 2013, Scientific Reports.

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

J. Steyaert, J. Castilla, W. Surewicz, 2017, Microbial Cell Factories.

Structure, mechanism, and inhibition of Hedgehog acyltransferase

Edward W. Tate, E. Pardon, J. Steyaert, 2021, Molecular cell.

Structure and Mechanism of Hedgehog Acyl Transferase

Edward W. Tate, E. Pardon, J. Steyaert, 2021, bioRxiv.

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

P. Stewart, K. Palczewski, E. Pardon, 2018, Nature Communications.

Structural basis for GABAA receptor potentiation by neurosteroids

E. Pardon, J. Steyaert, L. De Colibus, 2017, Nature Structural & Molecular Biology.

Quiescin-sulfhydryl oxidase inhibits prion formation in vitro

J. Steyaert, R. Petersen, S. Lehmann, 2016, Aging.

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

E. Pardon, J. Steyaert, A. Fish, 2018, Acta crystallographica. Section F, Structural biology communications.

Deciphering the mechanism of RNase T1.

J. Steyaert, S. Loverix, 2001, Methods in enzymology.

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

J. Steyaert, G. Legname, J. Messens, 2012, Microbial Cell Factories.

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

Alexander K. Buell, C. Dobson, L. Wyns, 2017 .

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

J. Steyaert, L. Droogmans, M. Roovers, 2014, RNA.

Crystal structure determination and refinement at 2.3-A resolution of the lentil lectin.

R. Pickersgill, L. Wyns, D. Maes, 1993, Biochemistry.

The F plasmid CcdB protein induces efficient ATP-dependent DNA cleavage by gyrase.

L. Wyns, M. Couturier, L. Van Melderen, 1993, Journal of molecular biology.

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

J. Steyaert, D. Oyen, R. Wechselberger, 2013, Biochimica et biophysica acta.

Anomaly in α-scattering from 6Li between 35 and 45 MeV

J. Steyaert, M. Zisman, M. Bernas, 1975 .

An engineered ribonuclease preferring phosphorothioate RNA

J. Steyaert, R. Strömberg, S. Loverix, 1998, Nature Structural Biology.

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

R. Dror, D. Shaw, Y. Zou, 2018, Nature Chemical Biology.

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

M. Steinmetz, M. Rudolph, J. Steyaert, 2016, The Journal of Biological Chemistry.

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

E. Pardon, J. Steyaert, Young-Jun Park, 2011, Nucleic acids research.

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

W. Hol, E. Pardon, J. Steyaert, 2010, Journal of structural biology.

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

J. Steyaert, R. Custers, 2020, EMBO reports.

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

U. Baumann, E. Pardon, J. Steyaert, 2017, Biochimica et biophysica acta. Biomembranes.

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

C. Verlinde, W. Hol, L. Bergman, 2013, Molecular and biochemical parasitology.

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

W. Hol, E. Pardon, J. Steyaert, 2009, Journal of structural biology.

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

Antoniya A. Aleksandrova, E. Pardon, J. Steyaert, 2019, Cell.

Structure, substrate recognition and initiation of hyaluronan synthase

E. Pardon, J. Steyaert, P. Stansfeld, 2022, Nature.

Mapping inhibitory sites on the RNA polymerase of the 1918 pandemic influenza virus using nanobodies

E. Pardon, J. Steyaert, J. Grimes, 2022, Nature communications.

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

J. Lamerdin, J. Steyaert, G. Skiniotis, 2017, Proceedings of the National Academy of Sciences.

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

J. Fernández-Recio, E. Pardon, J. Steyaert, 2019, Nature Communications.

The contribution of metal ions to the conformational stability of ribonuclease T1: crystal versus solution.

J. Steyaert, R. Loris, U. Langhorst, 2001, European journal of biochemistry.

Polymeric nanoreactors for enzyme replacement therapy of MNGIE.

T. Vanhaecke, V. Rogiers, J. Steyaert, 2010, Journal of controlled release : official journal of the Controlled Release Society.

Vrije Universiteit Brussel Polymeric nanoreactors for enzyme replacement therapy by MNGIE

T. Vanhaecke, V. Rogiers, J. Steyaert, 2010 .

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

E. Pardon, J. Steyaert, W. Jonckheere, 2019, Nature Microbiology.

Substrate-dependent modulation of enzyme activity by allosteric effector antibodies.

J. Steyaert, K. Conrath, J. Barlow, 2009, Biochimica et biophysica acta.

HDX-MS-optimized approach to characterize nanobodies as tools for biochemical and structural studies of class IB phosphoinositide 3-kinases.

E. Pardon, J. Steyaert, M. Rathinaswamy, 2021, Structure.

HDX-MS optimized approach to characterize nanobodies as tools for biochemical and structural studies of class IB phosphoinositide 3-kinases

E. Pardon, J. Steyaert, M. Rathinaswamy, 2021, bioRxiv.

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

R. Dutzler, E. Pardon, J. Steyaert, 2017, Biochemistry.

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

E. Pardon, J. Steyaert, A. Fish, 2018, bioRxiv.

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

L. Wyns, J. Steyaert, U. Heinemann, 1994, Biochemistry.

Regulation of b 2 -Adrenergic Receptor Function by Conformationally Selective Single-Domain Intrabodies s

Ryan T. Strachan, S. Rasmussen, E. Pardon, 2014 .

Crystal structure of active mu-opioid receptor bound to the agonist BU72

Kathryn E. Livingston, Evan N. Feinberg, R. Dror, 2015 .

A Flexible Loop as a Functional Element in the Catalytic Mechanism of Nucleoside Hydrolase from Trypanosoma vivax*

J. Steyaert, W. Versées, S. De Vos, 2008, Journal of Biological Chemistry.

The crystal structure of phenylpyruvate decarboxylase from Azospirillum brasilense at 1.5 Å resolution

J. Steyaert, J. Vanderleyden, W. Versées, 2007, The FEBS journal.

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

D. Bertrand, E. Pardon, J. Steyaert, 2019, Nature Chemical Biology.

Cryo-EM Structure of an Atypical Proton-Coupled Peptide Transporter: Di- and Tripeptide Permease C

E. Pardon, J. Steyaert, D. Svergun, 2022, bioRxiv.

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

E. Pardon, J. Steyaert, Jianping Wu, 2016, Proceedings of the National Academy of Sciences.

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

A. Kruse, E. Pardon, J. Steyaert, 2016 .

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

J. Vandekerckhove, J. Steyaert, J. Gettemans, 2010, Cellular and Molecular Life Sciences.

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

Roger L. Williams, E. Pardon, J. Steyaert, 2020, Biophysical Journal.

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

Alessandro Spilotros, Remy Loris, Marcus Fislage, 2014, Nucleic acids research.

Hydrophobic core manipulations in ribonuclease T1.

J. Steyaert, R. Loris, M. Prévost, 2001, Biochemistry.

Prion biology

S. Prusiner, E. Pardon, J. Steyaert, 2011 .

Structure of an Endosomal Signaling GPCR–G Protein–β-arrestin Mega-Complex

Yong Zi Tan, J. Steyaert, R. Lefkowitz, 2019, Nature Structural & Molecular Biology.

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

J. Steyaert, R. Gallardo, W. Versées, 2019, The Biochemical journal.

BRET evidence that β2 adrenergic receptors do not oligomerize in cells

T. Lan, J. Steyaert, N. Lambert, 2015, Scientific Reports.

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

S. Sprang, W. Chiu, J. Steyaert, 2020, Nature Communications.

Author Correction: Structural insights into μ-opioid receptor activation

Kathryn E. Livingston, Evan N. Feinberg, R. Dror, 2020, Nature.

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

E. Pardon, J. Steyaert, W. Versées, 2020, The Biochemical journal.

A Topological Switch in the Cystic Fibrosis Transmembrane Conductance Regulator Modulates Channel Activity and Sensitivity to Disease-Causing Mutation

E. Pardon, J. Steyaert, A. Garcia-Pino, 2020 .

A Topological Switch Enables Misfolding of the Cystic Fibrosis Transmembrane Conductance Regulator

E. Pardon, J. Steyaert, A. Garcia-Pino, 2020, bioRxiv.

human NBD1 of CFTR in complex with nanobodies T2a and T4

J. Riordan, E. Pardon, J. Steyaert, 2019 .

Structure of Nanobody Nb23

J. Steyaert, F. Fogolari, G. Esposito, 2021, Molecules.

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

C. Robinson, M. Bucciantini, M. Stefani, 2017, Scientific Reports.

Structural insights into the activation of metabotropic glutamate receptors

M. J. Robertson, T. S. Kobilka, J. M. Mathiesen, 2019, Nature.

A decade of protein engineering on ribonuclease T1--atomic dissection of the enzyme-substrate interactions.

J. Steyaert, 1997, European journal of biochemistry.

A catalytic function for the structurally conserved residue Phe 100 of ribonuclease T1

L. Wyns, J. Steyaert, R. Loris, 1996, Protein science : a publication of the Protein Society.

Crystal Structure of a ligand-bound LacY–Nanobody Complex

R. Stroud, J. Finer-Moore, E. Pardon, 2018, Proceedings of the National Academy of Sciences.

Plasticity of the binding pocket in peptide transporters underpins promiscuous substrate recognition

E. Pardon, J. Steyaert, Jan Strauss, 2023, bioRxiv.

Primary structure and partial characterization of a life-cycle-regulated cysteine protease from Trypanosoma (Nannomonas) congolense.

J. Steyaert, C. Muriuki, J. Lonsdale-Eccles, 1995, Gene.

Conformational transitions and ligand-binding to a muscle-type nicotinic acetylcholine receptor

C. Chipot, J. Steyaert, J. Baenziger, 2022, Neuron.

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

J. Steyaert, J. Barlow, 2007, Biochimica et biophysica acta.

Additivity of Protein-Guanine Interactions in Ribonuclease T1*

J. Steyaert, S. Loverix, Jan Doumen, 1997, The Journal of Biological Chemistry.

A two-binding-site kinetic model for the ribonuclease-T1-catalysed transesterification of dinucleoside phosphate substrates.

J. Steyaert, Y. Engelborghs, 1995, European journal of biochemistry.

Crystallographic study of Glu58Ala RNase T1 x 2'-guanosine monophosphate at 1.9-A resolution.

L. Wyns, J. Steyaert, U. Heinemann, 1994, Biochemistry.

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

L. Wyns, J. Steyaert, P. Stanssens, 1991, Biochemistry.

Conformational Stability and Activity of Ribonuclease T1 and Mutants

C. Pace, B. Shirley, J. Steyaert, 1989 .

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

P. Kolb, E. Pardon, J. Steyaert, 2018, Angewandte Chemie.

Bypassing the Need for Cell Permeabilization: Nanobody CDR3 Peptide Improves Binding on Living Bacteria

E. Pardon, J. Steyaert, H. Remaut, 2023, Bioconjugate chemistry.

Structural basis of purine nucleotide inhibition of human uncoupling protein 1

E. Pardon, J. Steyaert, V. Moiseenkova-Bell, 2023, Science advances.

In vivo and in vitro characterizations of melibiose permease (MelB) conformation-dependent nanobodies reveal sugar-binding mechanisms

E. Pardon, J. Steyaert, H. Kaback, 2023, The Journal of biological chemistry.

Competitive, connective and allosteric Nanobodies that modulate the SOS1•RAS protein-protein interactions and tune the nucleotide exchange rate as a starting point for drug design

E. Pardon, J. Steyaert, A. Sablina, 2023, bioRxiv.

Structure, substrate recognition and initiation of hyaluronan synthase

E. Pardon, J. Steyaert, P. Stansfeld, 2022, Nature.

Nanobody-aided crystallization of the transcription regulator PaaR2 from Escherichia coli O157:H7.

E. Pardon, J. Steyaert, R. Loris, 2021, Acta crystallographica. Section F, Structural biology communications.

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

E. Pardon, J. Steyaert, G. Legname, 2019 .

Crystal structure of human Mediator subunit MED23

B. Clantin, V. Villeret, E. Pardon, 2018, Nature Communications.

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

M. Parmentier, J. Steyaert, T. Laeremans, 2018, Front. Endocrinol..

Rational Design of Nanobody80 Loop Peptidomimetics: Towards Biased β2 Adrenergic Receptor Ligands.

Samuel L. C. Moors, E. Pardon, J. Steyaert, 2017, Chemistry.

Thermodynamics of Nanobody Binding to Lactose Permease.

E. Pardon, J. Steyaert, H. Kaback, 2016, Biochemistry.

Modular Integrated Secretory System Engineering in Pichia pastoris To Enhance G-Protein Coupled Receptor Expression.

N. Callewaert, M. Parmentier, J. Steyaert, 2016, ACS synthetic biology.

Transient conformers of LacY are trapped by nanobodies

E. Pardon, J. Steyaert, H. Kaback, 2015, Proceedings of the National Academy of Sciences.

Outward-facing conformers of LacY stabilized by nanobodies

E. Pardon, J. Steyaert, H. Kaback, 2014, Proceedings of the National Academy of Sciences.

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

E. Pardon, J. Steyaert, Sarah Triest, 2014, Acta crystallographica. Section F, Structural biology communications.

Nanobody Mediated Crystallization of an Archeal Mechanosensitive Channel

P. Nordlund, E. Pardon, J. Steyaert, 2013, PloS one.

Structure of an early native‐like intermediate of β2‐microglobulin amyloidogenesis

E. Pardon, J. Steyaert, M. Fislage, 2013, Protein science : a publication of the Protein Society.

Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic β2-microglobulin variant

L. Wyns, E. Pardon, J. Steyaert, 2011, Proceedings of the National Academy of Sciences of the United States of America.

Interrogating dense ligand chemical space with a forward-synthetic library

P. Kolb, E. Pardon, J. Steyaert, 2019, Proceedings of the National Academy of Sciences.

Characterization of Phenylpyruvate Decarboxylase, Involved in Auxin Production of Azospirillum brasilense

J. Steyaert, J. Vanderleyden, W. Versées, 2007, Journal of bacteriology.

Functional interactions among the His40, Glu58 and His92 catalysts of ribonuclease T1 as studied by double and triple mutants.

L. Wyns, J. Steyaert, 1993, Journal of molecular biology.

Brussel Structure and nucleotide-induced conformational dynamics of the Chlorobium tepidum

J. Steyaert, R. Gallardo, W. Versées, 2019 .

Purification, circular dichroism analysis, crystallization and preliminary X-ray diffraction analysis of the F plasmid CcdB killer protein.

L. Wyns, M. Couturier, L. Van Melderen, 1993, Journal of molecular biology.

Structural basis of the allosteric inhibition of human ABCG2 by nanobodies.

E. Pardon, J. Steyaert, K. Locher, 2023, Journal of molecular biology.

Structural basis for the allosteric modulation of rhodopsin by nanobody binding to its extracellular domain

E. Pardon, J. Steyaert, K. Katayama, 2023, Nature communications.

Metabotropic Glutamate Receptor 5 Extracellular Domain in Complex with Nb43 and L-quisqualic acid

M. J. Robertson, T. S. Kobilka, J. M. Mathiesen, 2019 .

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

Ryan T. Strachan, A. Kruse, E. Pardon, 2016 .

Domain-interface dynamics of CFTR revealed by stabilizing nanobodies

J. Riordan, E. Pardon, J. Steyaert, 2019, Nature Communications.

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

J. Steyaert, M. Degano, W. Versées, 2010, Biochemistry.

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

R. Stroud, J. Finer-Moore, E. Pardon, 2020, PloS one.

Nanobody-enabled monitoring of kappa opioid receptor states

Reid H. J. Olsen, B. Roth, E. Pardon, 2020, Nature Communications.

Mimicking the regulatory state of a major facilitator superfamily sugar transporter

E. Pardon, J. Steyaert, H. Kaback, 2023 .

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

L. Wyns, E. Pardon, J. Steyaert, 2010 .

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

M. Parmentier, J. Steyaert, J. Van Damme, 2016, Journal of Immunology.

Transient conformers of LacY are trapped by nanobodies

E. Pardon, J. Steyaert, H. Kaback, 2015, Proceedings of the National Academy of Sciences of the United States of America.

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

J. Steyaert, D. Oyen, J. Barlow, 2014, Biochemistry.

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

P. Tompa, E. Pardon, J. Steyaert, 2018, Methods in enzymology.

Substrate-dependent modulation of enzyme activity by allosteric effector antibodies.

J. Steyaert, K. Conrath, J. Barlow, 2009, Biochimica et Biophysica Acta.

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

J. Steyaert, W. Versées, S. De Vos, 2003, Biochemistry.

Structure of PINK1 in complex with its substrate ubiquitin

E. Pardon, J. Steyaert, S. Freund, 2017, Nature.

Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic β2-microglobulin variant

L. Wyns, E. Pardon, J. Steyaert, 2011, Proceedings of the National Academy of Sciences.

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

J. Steyaert, R. Gallardo, W. Versées, 2019, The Biochemical journal.

Thermodynamics of Nanobody Binding to Lactose Permease.

E. Pardon, J. Steyaert, H. Kaback, 2016, Biochemistry.

Evaluation of Nucleoside Hydrolase Inhibitors for Treatment of African Trypanosomiasis

H. D. de Koning, J. Steyaert, M. Degano, 2010, Antimicrobial Agents and Chemotherapy.

Structural basis of membrane targeting and coatomer assembly by human GBP1

S. Tans, E. Pardon, J. Steyaert, 2023, bioRxiv.

Structure-based design of nanobodies that inhibit seeding of Alzheimer’s patient–extracted tau fibrils

M. Sawaya, E. Pardon, J. Steyaert, 2023, Proceedings of the National Academy of Sciences of the United States of America.

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

J. Steyaert, T. Laeremans, C. Blanchetot, 2016, mAbs.

CryoEM structure of human full-length alpha1beta3gamma2L GABA(A)R in complex with picrotoxin and megabody Mb38.

E. Pardon, J. Steyaert, K. Miller, 2019 .

Reconsidering the energetics of ribonuclease catalysed RNA hydrolysis.

L. Wyns, J. Steyaert, J. Martins, 1998, European journal of biochemistry.

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

D. Bertrand, E. Pardon, J. Steyaert, 2016, PloS one.

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

F. Buckner, C. Verlinde, W. Hol, 2017, Biochimie.

Synthesis of Bicyclic N‐Arylmethyl‐Substituted Iminoribitol Derivatives as Selective Nucleoside Hydrolase Inhibitors

J. Steyaert, W. Versées, M. Berg, 2009, ChemMedChem.

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

W. Hol, E. Pardon, J. Steyaert, 2010, Journal of structural biology.

Structural basis of purine nucleotide inhibition of human uncoupling protein 1

E. Pardon, J. Steyaert, V. Moiseenkova-Bell, 2023, Science advances.

Structural basis of substrate transport and drug recognition by the human thiamine transporter SLC19A3

E. Pardon, J. Steyaert, K. Jungnickel, 2024, bioRxiv.

Extracellular modulation of TREK-2 activity with nanobodies provides insight into the mechanisms of K2P channel regulation

E. Pardon, J. Steyaert, E. Carpenter, 2023, bioRxiv.

Structural insights into Pseudomonas aeruginosa lysine-specific uptake mechanism for extremely low pH regulation

Aurélien F. A. Moumbock, E. Pardon, J. Steyaert, 2024, bioRxiv.

Receptor-recognition and antiviral mechanisms of retrovirus-derived human proteins.

E. Pardon, J. Steyaert, M. Backovic, 2024, Nature structural & molecular biology.

Rapid small-scale nanobody-assisted purification of ryanodine receptors for cryo-EM

E. Pardon, J. Steyaert, R. Efremov, 2024, bioRxiv.

Structure and function of the EA1 surface layer of Bacillus anthracis

E. Pardon, J. Steyaert, H. Remaut, 2023, Nature communications.

Regulation of a Class III PI3K Lipid Kinase (VPS34 Complex II) by the Small G Protein Rab5A: Single Molecule Analysis Reveals a Dual Regulatory Mechanism.

Roger L. Williams, E. Pardon, J. Steyaert, 2020, Biophysical journal.

Mouse Prion Protein in complex with Nanobody 484

E. Pardon, J. Steyaert, G. Legname, 2019 .

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

E. Pardon, J. Steyaert, W. Jonckheere, 2019, Nature Microbiology.

Influenza A virus RNA polymerase structures provide insights into viral genome 2 replication 3

E. Pardon, J. Steyaert, J. Grimes, 2019 .

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. Corrigendum

B. Gamain, E. Pardon, J. Steyaert, 2013, Acta Crystallographica. Section F : Structural Biology and Crystallization Communications.

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

L. Wyns, M. Vendruscolo, E. Pardon, 2022 .

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

J. Steyaert, R. Loris, J. Backmann, 2000, Biochemistry.

Multiple transients in the pre-steady-state of nucleoside hydrolase reveal complex substrate binding, product base release, and two apparent rates of chemistry.

J. Steyaert, W. Versées, An Vandemeulebroucke, 2006, Biochemistry.