I. Landrieu

发表

Solution structure of the single-domain prolyl cis/trans isomerase PIN1At from Arabidopsis thaliana.

D. Inzé, I. Landrieu, J. Wieruszeski, 2002, Journal of molecular biology.

Domain 3 of NS5A Protein from the Hepatitis C Virus Has Intrinsic α-Helical Propensity and Is a Substrate of Cyclophilin A*

F. Penin, I. Landrieu, J. Wieruszeski, 2011, The Journal of Biological Chemistry.

1H NMR Study on the Binding of Pin1 Trp-Trp Domain with Phosphothreonine Peptides*

L. Buée, I. Landrieu, J. Wieruszeski, 2001, The Journal of Biological Chemistry.

Cell signaling, post-translational protein modifications and NMR spectroscopy

Philipp Selenko, Richard W. Kriwacki, Isabelle Landrieu, 2012, Journal of biomolecular NMR.

Single domain antibody fragments as new tools for detection of the neuronal tau protein in cells and in mice studies.

L. Buée, J. Rain, I. Landrieu, 2019, ACS chemical neuroscience.

Ranking high affinity ligands of low solubility by NMR spectroscopy.

I. Landrieu, J. Wieruszeski, G. Lippens, 2011, ACS medicinal chemistry letters.

The Talin Rod IBS2 α-Helix Interacts with the β3 Integrin Cytoplasmic Tail Membrane-proximal Helix by Establishing Charge Complementary Salt Bridges*

I. Landrieu, G. Lippens, N. Kieffer, 2008, Journal of Biological Chemistry.

Molecular basis for an ancient partnership between prolyl isomerase Pin1 and phosphatase inhibitor-2.

I. Landrieu, G. Lippens, D. Brautigan, 2011, Biochemistry.

Identification of YHR019 in Saccharomyces cerevisiae chromosome VIII as the gene for the cytosolic asparaginyl‐tRNA synthetase

I. Landrieu, R. Leberman, M. Härtlein, 1998, Yeast.

Structural basis for the non-immunosuppressive character of the cyclosporin A analogue Debio 025.

I. Landrieu, J. Wieruszeski, G. Lippens, 2010, Biochemistry.

Systematic Identification of Tubulin-interacting Fragments of the Microtubule-associated Protein Tau Leads to a Highly Efficient Promoter of Microtubule Assembly*

I. Landrieu, J. Wieruszeski, G. Lippens, 2011, The Journal of Biological Chemistry.

Tanycytes are degraded in Alzheimer Disease, disrupting the brain-to-blood efflux of Tau

F. Pasquier, L. Buée, I. Landrieu, 2022, medRxiv.

Deciphering the Structure and Formation of Amyloids in Neurodegenerative Diseases With Chemical Biology Tools

Davy Sinnaeve, I. Landrieu, E. Dupré, 2022, Frontiers in Chemistry.

BIN1 recovers tauopathy-induced long-term memory deficits in mice and interacts with Tau through Thr348 phosphorylation

Y. Hérault, J. Lambert, P. Amouyel, 2018, bioRxiv.

Direct Crosstalk Between O-GlcNAcylation and Phosphorylation of Tau Protein Investigated by NMR Spectroscopy

I. Landrieu, F. Cantrelle, Caroline Smet-Nocca, 2018, Front. Endocrinol..

Phosphorylated full‐length Tau interacts with 14‐3‐3 proteins via two short phosphorylated sequences, each occupying a binding groove of 14‐3‐3 dimer

I. Landrieu, T. Obsil, F. Cantrelle, 2020, The FEBS journal.

Isomerization and Oligomerization of Truncated and Mutated Tau Forms by FKBP52 are Independent Processes.

I. Landrieu, G. Lippens, E. Baulieu, 2016, Journal of molecular biology.

A functional fragment of Tau forms fibers without the need for an intermolecular cysteine bridge.

I. Landrieu, G. Lippens, F. Cantrelle, 2014, Biochemical and biophysical research communications.

Microinjection of recombinant O-GlcNAc transferase potentiates Xenopus oocytes M-phase entry.

I. Landrieu, G. Lippens, T. Lefebvre, 2008, Biochemical and biophysical research communications.

Structural impact of heparin binding to full-length Tau as studied by NMR spectroscopy.

I. Landrieu, J. Wieruszeski, G. Lippens, 2006, Biochemistry.

H/D exchange of a 15N labelled Tau fragment as measured by a simple Relax-EXSY experiment.

I. Landrieu, G. Lippens, F. Cantrelle, 2014, Journal of magnetic resonance.

Recombinant production of the p10CKS1At protein from Arabidopsis thaliana and 13C and 15N double-isotopic enrichment for NMR studies.

D. Inzé, M. Van Montagu, I. Landrieu, 1999, Protein expression and purification.

Mice lacking phosphatase PP2A subunit PR61/B’δ (Ppp2r5d) develop spatially restricted tauopathy by deregulation of CDK5 and GSK3β

I. Landrieu, G. Lippens, V. Janssens, 2011, Proceedings of the National Academy of Sciences.

NMR investigation of the interaction between the neuronal protein tau and the microtubules.

I. Landrieu, J. Wieruszeski, G. Lippens, 2007, Biochemistry.

Nuclear magnetic resonance analysis of the acetylation pattern of the neuronal Tau protein.

I. Landrieu, G. Lippens, F. Cantrelle, 2014, Biochemistry.

Exploring the molecular function of PIN1 by nuclear magnetic resonance.

L. Buée, I. Landrieu, J. Wieruszeski, 2006, Current protein & peptide science.

Studying the natively unfolded neuronal Tau protein by solution NMR spectroscopy.

L. Buée, I. Landrieu, J. Wieruszeski, 2006, Protein and peptide letters.

NMR analysis of a Tau phosphorylation pattern.

K. Saxena, H. Schwalbe, I. Landrieu, 2006, Journal of the American Chemical Society.

Proline‐Directed Random‐Coil Chemical Shift Values as a Tool for the NMR Assignment of the Tau Phosphorylation Sites

L. Buée, I. Landrieu, J. Wieruszeski, 2004, Chembiochem : a European journal of chemical biology.

Structural analysis of Escherichia coli OpgG, a protein required for the biosynthesis of osmoregulated periplasmic glucans.

B. Clantin, V. Villeret, I. Landrieu, 2004, Journal of molecular biology.

Two Tau binding sites on tubulin revealed by thiol-disulfide exchanges

I. Landrieu, V. Belle, B. Guigliarelli, 2018, Scientific Reports.

Selective intracellular accumulation of the major metabolite issued from the activation of the prodrug ethionamide in mycobacteria.

C. Locht, I. Landrieu, J. Wieruszeski, 2006, The Journal of antimicrobial chemotherapy.

Hepatitis C Virus NS5A Protein Is a Substrate for the Peptidyl-prolyl cis/trans Isomerase Activity of Cyclophilins A and B*

F. Penin, I. Landrieu, J. Wieruszeski, 2009, Journal of Biological Chemistry.

Fragment-based Differential Targeting of PPI Stabilizer Interfaces

C. Ottmann, I. Landrieu, Qing Cao, 2020, Journal of medicinal chemistry.

Set-up and screening of a fragment library targeting the 14-3-3 protein interface.

C. Ottmann, I. Landrieu, T. Obsil, 2019, MedChemComm.

Dynamic interactions and Ca2+-binding modulate the holdase-type chaperone activity of S100B preventing tau aggregation and seeding

A. P. Carapeto, U. Sengupta, I. Landrieu, 2021, Nature Communications.

Plasmodium falciparum Inhibitor-3 Homolog Increases Protein Phosphatase Type 1 Activity and Is Essential for Parasitic Survival*

I. Landrieu, B. Bertin, E. Werkmeister, 2011, The Journal of Biological Chemistry.

Inhibition of Tau seeding by targeting Tau nucleation core within neurons with a single domain antibody fragment.

L. Buée, J. Rain, I. Landrieu, 2022, Molecular therapy : the journal of the American Society of Gene Therapy.

Regions of Tau Implicated in the Paired Helical Fragment Core as Defined by NMR

L. Buée, I. Landrieu, J. Wieruszeski, 2005, Chembiochem : a European journal of chemical biology.

Regulation of Pin1 peptidyl‐prolyl cis/trans isomerase activity by its WW binding module on a multi‐phosphorylated peptide of Tau protein

L. Buée, I. Landrieu, J. Wieruszeski, 2005, FEBS letters.

Proline Conformation in a Functional Tau Fragment.

I. Landrieu, J. Wieruszeski, G. Lippens, 2016, Journal of molecular biology.

Tau pathology modulates Pin1 post-translational modifications and may be relevant as biomarker

L. Buée, I. Landrieu, G. Lippens, 2013, Neurobiology of Aging.

The FK506‐binding protein FKBP52 in vitro induces aggregation of truncated Tau forms with prion‐like behavior

L. Buée, I. Landrieu, G. Lippens, 2015, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Zinc Binding to Tau Influences Aggregation Kinetics and Oligomer Distribution

A. P. Carapeto, I. Landrieu, C. Gomes, 2019, International journal of molecular sciences.

Solution Structure of the N-Terminal Domain of Mediator Subunit MED26 and Molecular Characterization of Its Interaction with EAF1 and TAF7.

V. Villeret, I. Landrieu, D. Monté, 2017, Journal of molecular biology.

Mechanism of Tau-promoted microtubule assembly as probed by NMR spectroscopy.

I. Landrieu, J. Wieruszeski, G. Lippens, 2014, Journal of the American Chemical Society.

Cell signaling, post-translational protein modifications and NMR spectroscopy

I. Landrieu, G. Lippens, R. Kriwacki, 2012, Journal of Biomolecular NMR.

Structural and Functional Characterization of the Interaction between Cyclophilin B and a Heparin-derived Oligosaccharide*

I. Landrieu, J. Wieruszeski, G. Lippens, 2007, Journal of Biological Chemistry.

Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA

I. Landrieu, J. Wieruszeski, G. Lippens, 2013, Journal of Biomolecular NMR.

Phosphorylation and O-GlcNAcylation of the PHF-1 Epitope of Tau Protein Induce Local Conformational Changes of the C-Terminus and Modulate Tau Self-Assembly Into Fibrillar Aggregates

Neha S. Gandhi, I. Landrieu, F. Cantrelle, 2021, Frontiers in Molecular Neuroscience.

A β-Turn Motif in the Steroid Hormone Receptor's Ligand-Binding Domains Interacts with the Peptidyl-prolyl Isomerase (PPIase) Catalytic Site of the Immunophilin FKBP52.

Morkos A. Henen, I. Landrieu, G. Lippens, 2016, Biochemistry.

A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana.

D. Inzé, M. Van Montagu, I. Landrieu, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Microtubule and MAPs: thermodynamics of complex formation by AUC, ITC, fluorescence, and NMR.

I. Landrieu, G. Lippens, P. Barbier, 2010, Methods in cell biology.

NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B

I. Landrieu, G. Lippens, F. Cantrelle, 2017, The Journal of Biological Chemistry.

Tamoxifen inhibits CDK5 kinase activity by interacting with p35/p25 and modulates the pattern of tau phosphorylation.

K. Kosik, I. Landrieu, P. Colas, 2015, Chemistry & biology.

Adoption of a Turn Conformation Drives the Binding Affinity of p53 C-Terminal Domain Peptides to 14-3-3σ.

C. Ottmann, I. Landrieu, M. Ehrmann, 2019, ACS chemical biology.

Arabidopsis PASTICCINO2 Is an Antiphosphatase Involved in Regulation of Cyclin-Dependent Kinase A[W]

D. Inzé, I. Landrieu, G. Lippens, 2006, The Plant Cell Online.

Modulators of 14-3-3 Protein–Protein Interactions

L. M. Stevers, M. Hann, C. Ottmann, 2017, Journal of medicinal chemistry.

Tamoxifen Inhibits CDK 5 Kinase Activity by Interacting with p 35 / p 25 and Modulates the Pattern of Tau Phosphorylation Graphical

K. Kosik, I. Landrieu, P. Colas, 2015 .

Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases

I. Landrieu, P. Ratcliffe, C. Domene, 2016, Nature Communications.

Role of Tau as a Microtubule-Associated Protein: Structural and Functional Aspects

P. Tsvetkov, I. Landrieu, V. Belle, 2019, Front. Aging Neurosci..

Molecular Implication of PP2A and Pin1 in the Alzheimer's Disease Specific Hyperphosphorylation of Tau

I. Landrieu, J. Wieruszeski, G. Lippens, 2011, PloS one.

Supplementary Materials for Identification of the Tau phosphorylation pattern that drives its aggregation

I. Landrieu, G. Lippens, E. Baulieu, 2017 .

Functional Analysis of Cyclin-Dependent Kinase Inhibitors of Arabidopsis

Franky R. G. Terras, D. Inzé, I. Landrieu, 2001, The Plant Cell Online.

1H, 15N and 13C assignments of the N-terminal domain of the Mediator complex subunit MED26

V. Villeret, I. Landrieu, J. Baert, 2016, Biomolecular NMR Assignments.

1H, 15N and 13C assignments of the N-terminal domain of the Mediator complex subunit MED26

V. Villeret, I. Landrieu, J. Baert, 2016, Biomolecular NMR assignments.

Structural Basis of Tau Interaction With BIN1 and Regulation by Tau Phosphorylation

J. Lambert, I. Landrieu, F. Cantrelle, 2018, Front. Mol. Neurosci..

Selectivity via Cooperativity: Preferential Stabilization of the p65/14-3-3 Interaction with Semisynthetic Natural Products

C. Ottmann, I. Landrieu, Andrew J. Wilson, 2020, Journal of the American Chemical Society.

Characterization of ERM transactivation domain binding to the ACID/PTOV domain of the Mediator subunit MED25

V. Villeret, I. Landrieu, D. Monté, 2015, Nucleic acids research.

Molecular mechanisms of the phospho‐dependent prolyl cis/trans isomerase Pin1

I. Landrieu, G. Lippens, C. Smet, 2007, The FEBS journal.

The Arabidopsis thaliana PIN1At Gene Encodes a Single-domain Phosphorylation-dependent Peptidyl Prolylcis/trans Isomerase*

D. Inzé, M. Van Montagu, I. Landrieu, 2000, The Journal of Biological Chemistry.

Exacerbation of C1q dysregulation, synaptic loss and memory deficits in tau pathology linked to neuronal adenosine A2A receptor

L. Buée, I. Landrieu, S. Gras, 2019, Brain : a journal of neurology.

Major Differences between the Self-Assembly and Seeding Behavior of Heparin-Induced and in Vitro Phosphorylated Tau and Their Modulation by Potential Inhibitors

I. Landrieu, G. Lippens, G. Bitan, 2019, ACS chemical biology.

Characterization of Neuronal Tau Protein as a Target of Extracellular Signal-regulated Kinase*

J. Gunawardena, I. Landrieu, G. Lippens, 2016, The Journal of Biological Chemistry.

The elusive tau molecular structures: can we translate the recent breakthroughs into new targets for intervention?

Luc Buée, Caroline Smet-Nocca, Joris Winderickx, 2019, Acta Neuropathologica Communications.

Spectroscopic Studies of GSK3β Phosphorylation of the Neuronal Tau Protein and Its Interaction with the N-terminal Domain of Apolipoprotein E

I. Landrieu, J. Wieruszeski, G. Lippens, 2010, The Journal of Biological Chemistry.

Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA

I. Landrieu, J. Wieruszeski, G. Lippens, 2013, Journal of biomolecular NMR.

The Study of Posttranslational Modifications of Tau Protein by Nuclear Magnetic Resonance Spectroscopy: Phosphorylation of Tau Protein by ERK2 Recombinant Kinase and Rat Brain Extract, and Acetylation by Recombinant Creb-Binding Protein.

J. Gunawardena, I. Landrieu, G. Lippens, 2017, Methods in molecular biology.

Inhibition of Tau seeding by targeting Tau nucleation core within neurons with a single domain antibody fragment

L. Buée, J. Rain, I. Landrieu, 2021, bioRxiv.

Neurofibrillary degeneration of the Alzheimer-type: an alternate pathway to neuronal apoptosis?

Luc Buée, Stéphane Flament, Isabelle Landrieu, 2003, Biochemical pharmacology.

Stabilizer-Guided Inhibition of Protein-Protein Interactions.

Morkos A. Henen, C. Ottmann, I. Landrieu, 2015, Angewandte Chemie.

Immunophilin FKBP52 induces Tau-P301L filamentous assembly in vitro and modulates its activity in a model of tauopathy

I. Landrieu, G. Lippens, E. Baulieu, 2014, Proceedings of the National Academy of Sciences.

Two Tau binding sites on tubulin revealed by thiol-disulfide exchanges

I. Landrieu, V. Belle, B. Guigliarelli, 2018, Scientific Reports.

Prevention of tau seeding and propagation by immunotherapy with a central tau epitope antibody

L. Buée, I. Landrieu, M. Citron, 2019, Brain : a journal of neurology.

Comparative analysis of Erk phosphorylation suggests a mixed strategy for measuring phospho-form distributions

Hanno Steen, Jeremy Gunawardena, Isabelle Landrieu, 2011, Molecular systems biology.

Accepting its Random Coil Nature Allows a Partial NMR Assignment of the Neuronal Tau Protein

I. Landrieu, J. Wieruszeski, G. Lippens, 2004, Chembiochem : a European journal of chemical biology.

NMR observation of Tau in Xenopus oocytes.

I. Landrieu, J. Wieruszeski, G. Lippens, 2008, Journal of magnetic resonance.

Tau Aggregation in Alzheimer's Disease

I. Landrieu, J. Wieruszeski, G. Lippens, 2007, Prion.

Monitoring of the ethionamide pro-drug activation in mycobacteria by (1)H high resolution magic angle spinning NMR.

I. Landrieu, J. Wieruszeski, G. Lippens, 2005, Biochemical and biophysical research communications.

Pin1: a therapeutic target in Alzheimer neurodegeneration.

A. Delacourte, L. Buée, I. Landrieu, 2002, Journal of molecular neuroscience : MN.

NMR Meets Tau: Insights into Its Function and Pathology

Neha S. Gandhi, I. Landrieu, G. Lippens, 2016, Biomolecules.

A Phosphorylation-Induced Turn Defines the Alzheimer's Disease AT8 Antibody Epitope on the Tau Protein.

Neha S. Gandhi, I. Landrieu, J. Wieruszeski, 2015, Angewandte Chemie.

Nuclear magnetic resonance spectroscopy characterization of interaction of Tau with DNA and its regulation by phosphorylation.

L. Buée, I. Landrieu, G. Lippens, 2015, Biochemistry.

Control of protein-protein interactions: structure-based discovery of low molecular weight inhibitors of the interactions between Pin1 WW domain and phosphopeptides.

L. Buée, I. Landrieu, J. Wieruszeski, 2005, Journal of medicinal chemistry.

Solution NMR Study of the Monomeric Form of p13 suc1 Protein Sheds Light on the Hinge Region Determining the Affinity for a Phosphorylated Substrate*

D. Inzé, I. Landrieu, J. Wieruszeski, 2002, The Journal of Biological Chemistry.

p13 SUC1 and the WW Domain of PIN1 Bind to the Same Phosphothreonine-Proline Epitope*

D. Inzé, I. Landrieu, J. Wieruszeski, 2001, The Journal of Biological Chemistry.

Letter to the Editor: Sequence-specific 1H, 13C and 15N chemical shift backbone NMR assignment and secondary structure of the Arabidopsis thaliana PIN1At protein

D. Inzé, S. Grzesiek, I. Landrieu, 2000, Journal of biomolecular NMR.

Inhibition of 14-3-3/Tau by Hybrid Small-Molecule Peptides Operating via Two Different Binding Modes

C. Ottmann, I. Landrieu, L. Brunsveld, 2018, ACS chemical neuroscience.

Phosphorylation in intrinsically disordered regions regulates the activity of Neurogenin2

I. Landrieu, G. Lippens, A. Philpott, 2014, BMC Biochemistry.

Mitochondrial asparaginyl-tRNA synthetase is encoded by the yeast nuclear gene YCR24c.

I. Landrieu, M. Härtlein, D. Portetelle, 1997, European journal of biochemistry.

Identification of a Plasmodium falciparum inhibitor‐2 motif involved in the binding and regulation activity of protein phosphatase type 1

I. Landrieu, A. Martoriati, F. Cantrelle, 2014, The FEBS journal.

The peptidyl-prolyl isomerase and chaperone Par27 of Bordetella pertussis as the prototype for a new group of parvulins.

H. Hodak, C. Locht, F. Jacob-Dubuisson, 2008, Journal of Molecular Biology.

Involvement of 14‐3‐3 in tubulin instability and impaired axon development is mediated by Tau

C. Ottmann, I. Landrieu, Y. Suh, 2015, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Regulation of the interaction between the neuronal BIN1 isoform 1 and Tau proteins – role of the SH3 domain

J. Lambert, I. Landrieu, G. Lippens, 2017, The FEBS journal.

Characterization of the AT180 epitope of phosphorylated Tau protein by a combined nuclear magnetic resonance and fluorescence spectroscopy approach.

I. Landrieu, G. Lippens, Laziza Amniai, 2011, Biochemical and biophysical research communications.

Nuclear Magnetic Resonance Spectroscopy Insights into Tau Structure in Solution: Impact of Post-translational Modifications.

I. Landrieu, E. Dupré, X. Hanoulle, 2019, Advances in experimental medicine and biology.

Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.

I. Landrieu, J. Wieruszeski, G. Lippens, 2011, Molecular bioSystems.

Selective backbone labelling of ILV methyl labelled proteins

I. Landrieu, J. Wieruszeski, G. Lippens, 2009, Journal of biomolecular NMR.

Tau phosphorylation regulates the interaction between BIN1’s SH3 domain and Tau’s proline-rich domain

J. Lambert, P. Amouyel, I. Landrieu, 2015, Acta neuropathologica communications.

Conformation and Affinity Modulations by Multiple Phosphorylation Occurring in the BIN1 SH3 Domain Binding Site of the Tau Protein Proline-Rich Region.

Davy Sinnaeve, I. Landrieu, E. Dupré, 2023, Biochemistry.

Alzheimer disease specific phosphoepitopes of Tau interfere with assembly of tubulin but not binding to microtubules

I. Landrieu, J. Wieruszeski, G. Lippens, 2009, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Characterization of the Arabidopsis thaliana Arath;CDC25 dual-specificity tyrosine phosphatase.

D. Inzé, I. Landrieu, J. Wieruszeski, 2004, Biochemical and biophysical research communications.

NMR Analysis of a Tau Phosphorylation Pattern

K. Saxena, H. Schwalbe, I. Landrieu, 2006 .

NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer's disease.

L. Buée, I. Landrieu, J. Wieruszeski, 2010, Biochemical Society transactions.

The O-β-linked N-acetylglucosaminylation of the Lamin B receptor and its impact on DNA binding and phosphorylation.

I. Landrieu, E. Nikolakaki, F. Cantrelle, 2018, Biochimica et biophysica acta. General subjects.

Strategy of selection and optimization of single domain antibodies targeting the PHF6 linear peptide within the Tau intrinsically disordered protein

J. Rain, I. Landrieu, E. Dupré, 2023, bioRxiv.

The peptidyl prolyl cis/trans-isomerase Pin1 recognizes the phospho-Thr212-Pro213 site on Tau.

L. Buée, I. Landrieu, J. Wieruszeski, 2004, Biochemistry.

Structural characterization by nuclear magnetic resonance of the impact of phosphorylation in the proline‐rich region of the disordered Tau protein

I. Landrieu, J. Wieruszeski, G. Lippens, 2012, Proteins.

ELISE NMR: experimental liquid sealing of NMR samples.

I. Landrieu, J. Wieruszeski, G. Lippens, 2006, Journal of magnetic resonance.

Design Of Drug-Like Protein-Protein Interaction Stabilizers Guided By Chelation-Controlled Bioactive Conformation Stabilization.

C. Ottmann, I. Landrieu, A. Gunnarsson, 2020, Chemistry.

Towards understanding the phosphorylation code of tau.

I. Landrieu, J. Wieruszeski, G. Lippens, 2012, Biochemical Society transactions.

NMR Spectroscopy of the Main Protease of SARS‐CoV‐2 and Fragment‐Based Screening Identify Three Protein Hotspots and an Antiviral Fragment

I. Landrieu, J. Dubuisson, F. Cantrelle, 2021, Angewandte Chemie.

1H, 13C, and 15N chemical shift assignment of human PACSIN1/syndapin I SH3 domain in solution

Davy Sinnaeve, I. Landrieu, F. Cantrelle, 2020, Biomolecular NMR Assignments.