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Featured Publications

Mechanisms and pathology of protein misfolding and aggregation.

Louros N, Schymkowitz J, Rousseau F. Nature Rev. Mol. Cell Biol. 24(12): 912-933. (2023)

 

Medin promotes vascular amyloid-β aggregation in Alzheimer’s disease. 

Wagner J, Degenhardt K, Veit M, Louros N, et al. Nature 612, 123-131

(2022)

 

Mapping the sequence specificity of heterotypic amyloid interactions enables the identification of aggregation modifiers. 

Louros N, et al. Nature Communications 13, 1351 (2022)

Thermodynamic analysis of amyloid fibril structures reveals a common framework for stability in amyloid polymorphs. 

#van der Kant R, #Louros N, et al. Structure 30(8): 1178-89 #equal contribution (2022)

 

Structure-based machine-guided mapping of amyloid sequence space reveals uncharted sequence clusters with higher solubilities. 

Louros N, et al. Nature Communications 11, 3314. (2020) 

 

LRRC37B is a species-specific regulator of voltage-gated channels and excitability in human cortical neurons.

Libé-Philippot B, Lejeune A, Wierda K, Louros N, et al. Cell 186(26): 5766-5783 (2023)

Full list of Publications (sorted by year)

    Pharmacological modulation of septins restores calcium homeostasis and is neuroprotective in models of Alzheimer’s disease.

    Princen K, Van Dooren T, Van Gorsel M, Louros N, Yang X, Dumbacher M, Bastiens I, Coupet K, Dupont S, Cuveliers E, Lauwers A, Laghmouchi M, Vanwelden T, Carmans S, Van Damme N, Duhamel H, Vansteenkiste S, Prepad J, Pipeleers K, Rodiers O, De Ridder L, Claes S, Busschots Y, Pringels L, Verhelst V, Debroux E, Brouwer M, Lievens S, Tavernier J, Farinelli M, Hughes-Asceri S, Voets M, Winderickx J, Wera S, De Wit J, Schymkowitz J, Rousseau F, Zetterberg H, Cummings J, Annaert W, Cornelissen T, De Winter H, De Witte K, Fivaz M, Griffioen G. Science, 384(6699), eadd6260. (2024) 

     

    CORDAX web server: An online platform for the prediction and 3D visualization of aggregation motifs in protein sequences.

    Louros N, Rousseau F, Schymkowitz J. Bioinformatics, 40(5), btae279. (2024) 

     

    An end-to-end approach for single-cell infrared absorption spectroscopy of bacterial inclusion bodies:from AFM-IR measurement to interpretation of large sample sets.

    Duverger W, Tsaka G, Khodoparast L, Khodoparast L, Louros N, Rousseau F, Schymkowitz J. J. Nanobiotechnol. 22, 406. (2024)

     

    Local structural preferences in shaping tau amyloid polymorphism.

    Louros N, Wilkinson M, Tsaka G, Ramakers M, Morelli C, Garcia T, Gallardo R, D’Haeyer S, Goossens V, Audenaert D, Thal D, Mackenzie IR, Rademakers R, Ranson N, Radford S, Rousseau F, Schymkowitz J. Nature Commun 15, 1028. (2024)

     

    N-glycosylation as a eukaryotic protective mechanism against protein aggregation.

    Duran-Romaña R, Houben B, Louros N, De Vleeschouwer M, Wilson M, Matthijs G, Schymkowitz J, Rousseau F. Science Adv. 10, eadk8173. (2024) 

     

    LRRC37B is a species-specific regulator of voltage-gated channels and excitability in human cortical neurons.

    Libé-Philippot B, Lejeune A, Wierda K, Louros N, Erkol E, Vlaeminck I, Beckers S, Gaspariunaite V, Bilheu A, Konstantoulea K, Nyitrai H, Vennekens KM, Vidal N, Bird TW, Soto D, Dennis MY, Rousseau F, Comoletti D, Schymkowitz J, Theys T, de Wit J, Vanderhaeghen P.  Cell 186(26): 5766-5783.e25. (2023)

     

    Mechanisms and pathology of protein misfolding and aggregation.

    Louros N, Schymkowitz J, Rousseau F. Nature Rev. Mol. Cell Biol. 24(12): 912-933. (2023)

     

    Sequence-targeted Peptides Divert Functional Bacterial Amyloid Towards Destabilized Aggregates and Reduce Biofilm Formation. 

    Sønderby T, Louros N, Khodaparast L, Khodaparast L, Madsen D, Olsen W, Nagaraj M, Strømgaard K, Rousseau F, Schymkowitz J, Otzen D. J. Mol. Biol. 435 (11): 168039. (2023)

     

    Exploiting the intrinsic misfolding propensity of the KRAS oncoprotein. 

    Janssen K, Claes F, Van de Velde D, Wehbi V, Houben B, Lampi Y, Louros N, Nys M, Khodoparast L, Khodoparast L, van der Kant R, Verniers J, Garcia T, Ramakers M, Konstantoulea K, Maragkou K, Musteanu M, Barbacid M, Scorneaux B, Beinaert E, Schymkowitz J, Rousseau F. Proc. Nat. Acad. Sci. USA 120(9):e2214921120. (2023)

     

    Enhanced therapeutic window for antimicrobial Pept-ins by investigating their structure-activity relationship.

    Wu G, Khodoparast L, Khodoparast L, De Vleeschouwer M, Louros N, Gallardo R, Yi P, Rousseau F, Schymkowitz J. PLOS ONE 18(3): e0283674. (2023) 

     

    EndophilinA-dependent coupling between activity-dependent calcium influx and synaptic autophagy is disrupted by a Parkinson-risk mutation. 

    Bademosi A, Decet M, Kuenen S, Catalayud C, Swerts J, Gallego S, Schoovaerts N, Louros N, Martin E, Karamanou S, Sibarita J-B, Vints K, Gounko N, Meunier F, Economou A, Versees, W, Rousseau F, Schymkowitz J, Soukup S, Verstreken P. Neuron 119(9): 1402-22. (2023)

    Exploiting ligand binding domain dimerization for development of novel androgen receptor inhibitors. 

    Helsen C, Nguyen TT, Lee XY, Eerlings R, Louros N, Schymkowitz J, Rousseau F, Claessens F, Voet A (2022) Mol. Cancer Ther. 21(12): 1823-34. (2022)

     

    Medin promotes vascular amyloid-β aggregation in Alzheimer’s disease. 

    Wagner J, Degenhardt K, Veit M, Louros N, Konstantoulea K, Skodras A, Obermüller U, Wild K, Bansal V, Dalmia A, Häsler L, Lambert M, Liu P, Davies H, Madine J, Kronenberg-Versteeg D, Feederle R, Del Turco D, Nilsson P, Lashley T, Deller T, Gearing M, Walker L, Heutink P, Rousseau F, Schymkowitz J, Jucker M, Neher J. Nature 612, 123-131. (2022)

     

    Investigating the Sequence Determinants of the Curling of Amyloid Fibrils Using Ovalbumin as a Case Study. 

    Housmans J, Houben B, Monge-Morera M, Asvestas D, Nguyen H, Tsaka G, Louros N, Carpentier S, Delcour J, Rousseau F, Schymkowitz J. Biomacromolecules, 23(9): 3779-97. (2022)

     

    Thermodynamic analysis of amyloid fibril structures reveals a common framework for stability in amyloid polymorphs. 

    #van der Kant R, #Louros N, Schymkowitz J, Rousseau F. Structure 30(8): 1178-89 #equal contribution (2022)

     

    StAmP-DB: A platform for structures of polymorphic amyloid fibril cores. 

    #Louros N, #van der Kant R, Rousseau F, Schymkowitz J. Bioinformatics, 38(9):2636-8. #equal contribution (2022) 

     

    Mapping the sequence specificity of heterotypic amyloid interactions enables the identification of aggregation modifiers. 

    Louros N, Ramakers M, Michiels E, Konstantoulea K, Morelli C, Garcia T, Moonen N, D’Haeyer S, Goossens V, Thal D, Audenaert D, Rousseau F, Schymkowitz J. Nature Commun 13, 1351 (2022)

     

    Heterotypic amyloid interactions: clues to polymorphic bias and selective cellular vulnerability? 

    Louros N, Schymkowitz J, Rousseau F. Curr. Opinion Struct. Biol. 72:176-186. (2021)

     

    Arabidopsis thaliana plant natriuretic peptide active domain forms amyloid-like fibrils in a pH-dependent manner. 

    Nasi G, Aktipi F, Spatharas P, Louros N, Tsiolaki P, Magafa V, Trougakos I, Iconomidou V. Plants 11(1):9. (2021) 

     

    Bcl-xL acts as an inhibitor of IP3R channels, thereby antagonizing Ca2+-driven apoptosis. 

    Rosa N, Ivanova H, Wagner L, Kale J, Lemmens I, Karamanou S, Louros N, Shabardina V, Welkenhuyzen K, La Rovere R, Vandermarliere E, Hamada K, Ando H, Rousseau F, Schymkowitz J, Mikoshiba K, Economou A, Tavernier J, Andrews DW, Parys JB, Yule DI, Bultynck G. Nature Cell Death Differ. 29: 788-805. (2021) 

     

    Heterotypic Aβ interactions facilitate amyloid assembly and modify amyloid structure. 

    Konstantoulea K, Guerreiro P, Ramakers M, Louros N, Aubrey L, Houben B, Michiels E, De Vleeschouwer M, Lampi Y, Ribeiro L, De Wit J, Xue W-F, Rousseau F, Schymkowitz J. EMBO Journal, 41(2):e108591. (2021)

     

    Heating wheat gluten promotes the formation of amyloid-like fibrils. 

    Monge-Morera M, Lambrecht M, Deleu L, Louros N, Rousseau F, Schymkowitz J, Delcour J. ACS Omega 6(3):1823. (2021)

     

    Heterotypic interactions in amyloid function and disease.

    #Konstantoulea K, #Louros N, Rousseau F., Schymkowitz J. FEBS J 289: 2025-2046. #equal contribution (2021)

     

    Repurposing the Antidepressant Sertraline as SHMT Inhibitor to Suppress Serine/Glycine Synthesis–Addicted Breast Tumor Growth. 

    Geeraerts S, Kampen KR, Rinaldi G, Gupta P, Planque M, Louros N, Heylen E, De Cremer K, De Brucker K, Vereecke S, Verbelen B, Vermeersch P, Schymkowitz J, Rousseau F, Cassiman D, Fendt SM, Voet A, Cammue BPA, Thevissen K, De Keersmaecker K. Mol. Cancer Ther. 20(1): 50-63. (2021)

     

    The structural basis for an on-off switch controlling Gβγ-mediated inhibition of TRPM3 channels. 

    Behrendt M, Gruss F, Enzeroth R, Dembla S, Zhao S, Crassous P-A, Mohr F, Nys M, Louros N, Gallardo R, Zorzini V, Wagner D, Economou A, Rousseau F, Schymkowitz J, Philipp S, Rohacs T, Ulens C, Oberwinkler J. Proc. Natl. Acad. Sci. USA 117(46): 29090-0. (2020) 

     

    Processing induced changes in food proteins: amyloid formation during boiling of hen egg white.

    Monge-Morera M, Lambrecht M, Deleu L, Gallardo R, Louros N, De Vleeschouwer M, Rousseau F, Schymkowitz J, Delcour J. Biomacromolecules 21(6), 2218-28. (2020)

     

    Structure-based machine-guided mapping of amyloid sequence space reveals uncharted sequence clusters with higher solubilities. 

    Louros N, Orlando G, De Vleeschouwer M, Rousseau F, Schymkowitz J. Nature Commun 11, 3314. (2020) 

     

    Autonomous versus chaperone-dependent control of aggregation is differentiated by aggregation gatekeeper charge. 

    Houben B, Michiels E, Ramakers M, Konstantoulea K, Louros N, Verniers J, De Vleeschouwer M, Chicoria N, Vanpoucke T, Gallardo R, Schymkowitz J, Rousseau F. EMBO Journal, e102864. (2020) 

     

    Reverse engineering synthetic antiviral amyloids. 

    Michiels E, Roose K, Gallardo R, Khodoparast L, Khodoparast L, van der Kant R, Siemons M, Houben B, Ramakers M, Wilkinson H, Guerrero P, Louros N, Kaptein S, Ibañez L, Smet A, Baatsen P, Liu S, Vorberg I, Bormans G, Neyts J, Saelens X, Schymkowitz J, Rousseau F. Nature Commun 11, 2832. (2020) 

     

    Thermodynamic and Evolutionary Coupling between the Native and Amyloid State of Globular Proteins. 

    Langenberg T, Gallardo R, van der Kant R, Louros N, Michiels E, Duran-Romaña R, Houben B, Cassio R, Wilkinson H, Garcia T, Ulens C, Van Durme J, Rousseau F, Schymkowitz J. Cell Reports 31(2), 107512. (2020) 

     

    Entropic bristles tune the seeding efficiency of prion-nucleating fragments.

    Michiels E, Liu S, Gallardo R, Louros N, Mathelié-Guinlet M, Dufrêne Y, Schymkowitz J, Vorberg I, Rousseau F. Cell Reports 30, 2834-45. (2020) 

    Exposure of a cryptic HSP70 binding site determines the cytotoxicity of the ALS-associated SOD1 mutant A4V. 

    Claes F, Rudyak S, Laird A, Louros N, Beerten J, Debulpaep M, Van Durme J, De Baets G, Houben B, Ramakers M, Yuan K, Gwee S, Hernandez S, Broersen K, Oliveberg M, Moahamed B, Kirstein J, Robberecht W, Rousseau F, Schymkowitz J. Prot. Eng. Des. and Selection (PEDS). 32(10):443‐457. (2019) 

     

    WALTZ-DB 2.0: an updated database containing structural information of experimentally determined amyloid-forming peptides. 

    Louros N, Konstantoulea K, De Vleeschouwer M, Ramakers M, Schymkowitz J, Rousseau F. Nucleic Acids Res. 48: D389-93. (2019)

     

    Hidden aggregation hot-spots on human apolipoprotein E: a structural study.

    Tsiolaki P, Katsafana A, Baltoumas F, Louros N, Iconomidou V. Inter. J. Mol. Sciences, 20(9): 2274. (2019) 

    Hexapeptide tandem repeats dictate the formation of silkmoth chorion, a natural protective amyloid. 

    #Tsiolaki P, #Louros N, Iconomidou V. J. Mol. Biol., 430: 3774-3783. #equal contribution (2018)

     

    Aggregating sequences that occur in many proteins constitute weak spots of bacterial proteostasis. 

    Khodaparast L, Khodaparast L, Gallardo R, Louros N, Michiels E, Ramakrishnan R, Ramakers M, Claes F, Young L, Shahrooei M, Wilkinson H, Desager M, Mengistu W, Nilsson PR, Hammarström P, Aertsen A, Carpentier S, Van Eldere J, Rousseau F, Schymkowitz J. Nature Commun, 9(1): 866. (2018) 

     

    αCGRP, another amyloidogenic member of the CGRP family. 

    Tsiolaki P, Nasi GI, Baltoumas FA, Louros N, Magafa V, Hamodrakas SJ, Iconomidou VA. J. Struct. Biol., 203(1): 27-36. (2018)

     

     

    Tracking the amyloidogenic core of IAPP amyloid fibrils: Insights from micro-Raman spectroscopy. 

    Louros N, Tsiolaki PL, Baltoumas FA, Chryssikos GD, Gionis V, Hamodrakas SJ, Iconomidou VA. J. Struct. Biol., 199(2): 140-152. (2017) 

     

    Unraveling the aggregation propensity of human insulin C-peptide. 

    Tsiolaki P, Louros N, Zompra AA, Hamodrakas SJ, Iconomidou VA. Biopolymers, 108 (2). (2017)

     

    --- Book Chapter ----

    Exploring amyloidogenicity of Clusterin: a structural and bioinformatics analysis. 

    Tsiolaki P, Nastou K, Louros N, Hamodrakas S, Iconomidou V. Adv. Exp. Med. and Biol., 989:93-107. (2017) 

     

     

    Intrinsic aggregation propensity of the CsgB nucleator protein is crucial for curli fiber formation.

    Louros N, Bolas GM, Tsiolaki PL, Hamodrakas SJ, Iconomidou VA. J. Struct. Biol., 195(2): 179-189. (2016)

     

    A common "aggregation-prone" interface possibly participates in the self-assembly of human zona pellucida proteins.

    Louros N, Chrysina ED, Baltatzis GE, Patsouris ES, Hamodrakas SJ, Iconomidou VA. FEBSLetters, 590: 619–630. (2016)

     

    A β-solenoid model of the Pmel17 repeat domain: insights to the formation of functional amyloid fibrils.

    Louros N, Baltoumas FA, Hamodrakas SJ, Iconomidou VA. J. Comp. Aid Mol. Des., 30(2): 153-164. (2016)

     

    Identification of an amyloid fibril forming segment of human Pmel17 repeat domain (RPT domain).

    Louros N and Iconomidou V. Biopolymers, 106(1):133-139. (2016)

     

    Exploring the 'aggregation-prone' core of human Cystatin C: A structural study. 

    Tsiolaki P, Louros N, Hamodrakas SJ, Iconomidou VA. J. Struct. Biol., 191(3): 272. (2015)

     

    Chameleon ‘aggregation-prone’ segments of apoA-I: A model of amyloid fibrils formed in apoA-I amyloidosis.

    Louros N, Tsiolaki PL, Griffin MD, Howlett GJ, Hamodrakas SJ, Iconomidou VA. Int. J. Biol. Macromol., 79: 711-718.  (2015)

     

    Structural studies and cytotoxicity assays of "aggregation-prone" IAPP8-16& its non-amyloidogenic variants suggest its important role in fibrillogenesis and cytotoxicity of human amylin.

    Louros N, Tsiolaki P, Zompra A, Pappa E, Magafa V, Pairas G, Cordopatis P, Cheimonidou C, Trougakos I, Iconomidou V, Hamodrakas S. Biopolymers, 104(3): 196–5. (2015)  

     

    Structural studies of 'aggregation-prone' peptide-analogues of teleostean egg chorion ZPB proteins.

    Louros N, Petronikolou N, Karamanos T, Cordopatis P, Iconomidou VA, Hamodrakas SJ. Biopolymers, 102(6): 427-236. (2014)

     

    An N-terminal pro-atrial natriuretic peptide aggregation-prone segment involved in isolated atrial amyloidosis.

    Louros N, Iconomidou V, Tsiolaki P, Chrysina E, Baltatzis G, Patsouris E, Hamodrakas S. FEBS Letters, 588:52-7. (2014)

     

    Structural analysis of peptide-analogues of human zona pellucida ZP1 protein with amyloidogenic properties: Insights into mammalian zona pellucida formation.

    Louros N, Iconomidou V, Giannelou P, Hamodrakas S. PLoS ONE, 8(9): e73258. (2013)

     

    ---- Conference Proceedings ----

    An ‘aggregation prone’ segments of human amylin (IAPP) and non-amyloidogenic variants. 

    Louros N, Tsiolaki P, Zompra A, Pappa E, Magafa V, Pairas G, Iconomidou V, Cordopatis P, Hamodrakas S. (2014) J. Pept. Sci. 20: S208-209.

     

    Structural analysis of peptide-analogues of human zona pellucida ZP1 protein with amyloidogenic properties: Insights into mammalian zona pellucida formation. 

    Louros N, Iconomodou V, Hamodrakas S. (2012) J. Pept. Sci. 18: S168-168.