Publications


Pre-print and latest publications

Sergey Nazarov, Anass Chiki, Driss Boudeffa and Hilal A. Lashuel. The structural basis of huntingtin (Htt) fibril polymorphism, revealed by cryo-EM of exon 1 Htt fibrils.        https://doi.org/10.1101/2021.09.23.461534


2022

Prominent astrocytic alpha-synuclein pathology with unique post-translational modification signatures unveiled across Lewy body disorders

M. F. Altay; A. K. L. Liu; J. L. Holton; L. Parkkinen; H. A. Lashuel 

Acta Neuropathologica Communications. 2022-11-12. Vol. 10, num. 1, p. 163. DOI : 10.1186/s40478-022-01468-8.

Revisiting the specificity and ability of phospho-S129 antibodies to capture alpha-synuclein biochemical and pathological diversity

H. A. Lashuel; A-L. Mahul-Mellier; S. Novello; R. N. Hegde; Y. Jasiqi et al. 

Npj Parkinsons Disease. 2022-10-20. Vol. 8, num. 1, p. 136. DOI : 10.1038/s41531-022-00388-7.

N-terminal mutant huntingtin deposition correlates with CAG repeat length and symptom onset, but not neuronal loss in Huntington’s disease

F. E. Layburn; A. Y. S. Tan; N. F. Mehrabi; M. A. Curtis; L. J. Tippett et al. 

Neurobiology Of Disease. 2022-10-11. Vol. 174, p. 105884. DOI : 10.1016/j.nbd.2022.105884.

Pathological substrate of memory impairment in multiple system atrophy

Y. Miki; K. Tanji; K. Shinnai; M. T. Tanaka; F. Altay et al. 

Neuropathology And Applied Neurobiology. 2022-08-12.  p. e12844. DOI : 10.1111/nan.12844.

Opportunities and challenges of alpha-synuclein as a potential biomarker for Parkinson’s disease and other synucleinopathies

P. Magalhaes; H. A. Lashuel 

Npj Parkinsons Disease. 2022-07-22. Vol. 8, num. 1, p. 93. DOI : 10.1038/s41531-022-00357-0.

On-Demand Nanoliter Sampling Probe for the Collection of Brain Fluid

J. Teixidor; S. Novello; D. Ortiz; L. Menin; H. A. Lashuel et al. 

Analytical Chemistry. 2022-07-05. Vol. 94, num. 29, p. 10415-10426. DOI : 10.1021/acs.analchem.2c01577.

Structural Basis of Huntingtin Fibril Polymorphism Revealed by Cryogenic Electron Microscopy of Exon 1 HTT Fibrils

S. Nazarov; A. Chiki; D. Boudeffa; H. A. Lashuel 

Journal Of The American Chemical Society. 2022-06-22. Vol. 144, num. 24, p. 10723-10735. DOI : 10.1021/jacs.2c00509.

Remembering John Q Trojanowski, in his own words: A life dedicated to discovering building blocks and using them to build bridges of knowledge, collaboration, and discovery

H. A. Lashuel 

Npj Parkinsons Disease. 2022-04-12. Vol. 8, num. 1, p. 43. DOI : 10.1038/s41531-022-00310-1.

A NAC domain mutation (E83Q) unlocks the pathogenicity of human alpha-synuclein and recapitulates its pathological diversity

S. T. Kumar; A-L. Mahul-Mellier; R. N. Hegde; G. Riviere; R. Moons et al. 

Science Advances. 2022-04-01. Vol. 8, num. 17, p. eabn0044. DOI : 10.1126/sciadv.abn0044.

Alpha-synuclein as a Potential Biomarker for Parkinson’s Disease and Other Synucleinopathies: Gaps, Challenges, and Opportunities

P. Santana Magalhães; H. A. Lashuel 

2022-03-12. 

Comparative Analysis of Total Alpha-Synuclein (alpha SYN) Immunoassays Reveals That They Do Not Capture the Diversity of Modified alpha SYN Proteoforms

L. Petricca; N. Chiki; L. Hanna-El-Daher; L. Aeschbach; R. Burai et al. 

Journal Of Parkinsons Disease. 2022-01-01. Vol. 12, num. 5, p. 1449-1462. DOI : 10.3233/JPD-223285.

Non-monotonic fibril surface occlusion by GFP tags from coarse-grained molecular simulations

J. C. Shillcock; J. Hastings; N. Riguet; H. A. Lashuel 

Computational and Structural Biotechnology Journal. 2022. Vol. 20, p. 309-321. DOI : 10.1016/j.csbj.2021.12.017.

Revisiting the grammar of Tau aggregation and pathology formation: how new insights from brain pathology are shaping how we study and target Tauopathies

G. Limorenko; H. A. Lashuel 

Chemical Society Reviews. 2022. Vol. 51, num. 2, p. 513-565. DOI : 10.1039/d1cs00127b.

2021

To target Tau pathologies, we must embrace and reconstruct their complexities

G. Limorenko; H. A. Lashuel 

Neurobiology Of Disease. 2021-12-01. Vol. 161, p. 105536. DOI : 10.1016/j.nbd.2021.105536.

Nuclear and cytoplasmic huntingtin inclusions exhibit distinct biochemical composition, interactome and ultrastructural properties

N. Riguet; A-L. Mahul-Mellier; N. Maharjan; J. Burtscher; M. Croisier et al. 

Nature Communications. 2021-11-12. Vol. 12, num. 1, p. 6579. DOI : 10.1038/s41467-021-26684-z.

Fatal attraction-The role of hypoxia when alpha-synuclein gets intimate with mitochondria

J. Burtscher; M. M. K. Syed; M. A. Keller; H. A. Lashuel; G. P. Millet 

Neurobiology Of Aging. 2021-11-01. Vol. 107, p. 128-141. DOI : 10.1016/j.neurobiolaging.2021.07.017.

The Nt17 Domain and its Helical Conformation Regulate the Aggregation, Cellular Properties and Neurotoxicity of Mutant Huntingtin Exon 1

S. Vieweg; A-L. Mahul Mellier; F. S. Ruggeri; N. Riguet; S. M. Deguire et al. 

Journal of Molecular Biology. 2021-10-15. Vol. 433, num. 21, p. 167222. DOI : 10.1016/j.jmb.2021.167222.

Pharmacological characterization of mutant huntingtin aggregate-directed PET imaging tracer candidates

F. Herrmann; M. Hessmann; S. Schaertl; K. Berg-Rosseburg; C. J. Brown et al. 

Scientific Reports. 2021-09-09. Vol. 11, num. 1, p. 17977. DOI : 10.1038/s41598-021-97334-z.

Alpha-synuclein research: defining strategic moves in the battle against Parkinson’s disease

L. M. A. Oliveira; T. Gasser; R. Edwards; M. Zweckstetter; R. Melki et al. 

Npj Parkinsons Disease. 2021-07-26. Vol. 7, num. 1, p. 65. DOI : 10.1038/s41531-021-00203-9.

Investigating Crosstalk Among PTMs Provides Novel Insight Into the Structural Basis Underlying the Differential Effects of Nt17 PTMs on Mutant Httex1 Aggregation

A. Chiki; Z. Zhang; K. Rajasekhar; L. A. Abriata; I. Rostami et al. 

Frontiers in Molecular Biosciences. 2021-07-26. Vol. 8. DOI : 10.3389/fmolb.2021.686086.

A New Chemoenzymatic Semisynthetic Approach Provides Insight into the Role of Phosphorylation beyond Exon1 of Huntingtin and Reveals N-Terminal Fragment Length-Dependent Distinct Mechanisms of Aggregation

R. Kolla; G. Pushparathinam; J. Ricci; A. Reif; I. Rostami et al. 

Journal of the American Chemical Society. 2021-06-23. Vol. 143, num. 26, p. 9798-9812. DOI : 10.1021/jacs.1c03108.

Rethinking protein aggregation and drug discovery in neurodegenerative diseases: Why we need to embrace complexity?

H. Lashuel 

Current Opinion in Chemical Biology. 2021-06-23. Vol. 64, p. 67-75. DOI : 10.1016/j.cbpa.2021.05.006.

Lewy body-associated proteins: Victims, instigators, or innocent bystanders? The case of AIMP2 and alpha-synuclein

H. A. Lashuel; S. Novello 

Neurobiology of Disease. 2021-06-06.  p. 105417. DOI : 10.1016/j.nbd.2021.105417.

Parkinson mice show functional and molecular changes in the gut long before motoric disease onset

M. Gries; A. Christmann; S. Schulte; M. Weyland; S. Rommel et al. 

Molecular Neurodegeneration. 2021-06-02. Vol. 16, num. 1, p. 34. DOI : 10.1186/s13024-021-00439-2.

Enforced dimerization between XBP1s and ATF6f enhances the protective effects of the UPR in models of neurodegeneration

R. L. Vidal; D. Sepulveda; P. Troncoso-Escudero; P. Garcia-Huerta; C. Gonzalez et al. 

Molecular Therapy. 2021-05-05. Vol. 29, num. 5, p. 1862-1882. DOI : 10.1016/j.ymthe.2021.01.033.

Correlative light and electron microscopy suggests that mutant huntingtin dysregulates the endolysosomal pathway in presymptomatic Huntington’s disease

Y. Zhou; T. R. Peskett; C. Landles; J. B. Warner; K. Sathasivam et al. 

Acta Neuropathologica Communications. 2021-04-14. Vol. 9, num. 1, p. 70. DOI : 10.1186/s40478-021-01172-z.

Alpha-Synuclein oligomerization and aggregation: All models are useful but only if we know what they model This is the reply to a comment “Alpha-synuclein oligomerization and aggregation: A model will always be a model” on the original article “Monitoring alpha-synuclein oligomerization and aggregation using bimolecular fluorescence complementation assays: What you see is not always what you get”. The articles are accompanied by a Preface “How good are cellular models?”.

H. A. Lashuel 

Journal Of Neurochemistry. 2021-03-22. Vol. 157, num. 4, p. 891-898. DOI : 10.1111/jnc.15275.

Hypoxia Conditioning as a Promising Therapeutic Target in Parkinson’s Disease?

J. Burtscher; M. M. K. Syed; H. A. Lashuel; G. P. Millet 

Movement Disorders. 2021-02-27. Vol. 36, num. 4, p. 857-861. DOI : 10.1002/mds.28544.

Reverse engineering Lewy bodies: how far have we come and how far can we go?

M. B. Fares; S. Jagannath; H. Lashuel 

Nature Reviews Neuroscience. 2021-01-11. Vol. 22, num. 2, p. 111-131. DOI : 10.1038/s41583-020-00416-6.

Monitoring alpha-synuclein oligomerization and aggregation using bimolecular fluorescence complementation assays: What you see is not always what you get

B. Frey; A. AlOkda; M. P. Jackson; N. Riguet; J. A. Duce et al. 

Journal of Neurochemistry. 2021. Vol. 157, num. 4, p. 872-888. DOI : 10.1111/jnc.15147.

2020

Site-Specific Phosphorylation of Huntingtin Exon 1 Recombinant Proteins Enabled by the Discovery of Novel Kinases

A. Chiki; J. Ricci; R. Hegde; L. A. Abriata; A. Reif et al. 

Chembiochem. 2020-10-13.  p. 1-16. DOI : 10.1002/cbic.202000508.

How specific are the conformation-specific α-synuclein antibodies? Characterization and validation of 16 α-synuclein conformation-specific antibodies using well-characterized preparations of α-synuclein monomers, fibrils and oligomers with distinct structures and morphology

S. K. Thangaraj; S. Jagannath; C. Francois; H. Vanderstichele; E. Stoops et al. 

Neurobiology of Disease. 2020-09-22. Vol. 146, p. 105086. DOI : 10.1016/j.nbd.2020.105086.

TBK1 phosphorylates mutant Huntingtin and suppresses its aggregation and toxicity in Huntington’s disease models

R. N. Hegde; A. Chiki; L. Petricca; P. Martufi; N. Arbez et al. 

The EMBO Journal. 2020-08-05.  p. e104671. DOI : 10.15252/embj.2020104671.

Half a century of amyloids: past, present and future

P. C. Ke; R. Zhou; L. C. Serpell; R. Riek; T. P. J. Knowles et al. 

Chemical Society Reviews. 2020-07-07. Vol. 49, num. 15, p. 5473-5509. DOI : 10.1039/C9CS00199A.

Do Lewy bodies contain alpha-synuclein fibrils? and Does it matter? A brief history and critical analysis of recent reports

H. A. Lashuel 

Neurobiology Of Disease. 2020-07-01. Vol. 141, p. 104876. DOI : 10.1016/j.nbd.2020.104876.

Phosphorylation of the overlooked tyrosine 310 regulates the structure, aggregation, and microtubule- and lipid-binding properties of Tau

N. Ait-Bouziad; A. Chiki; G. Limorenko; S. Xiao; D. Eliezer et al. 

Journal Of Biological Chemistry. 2020-06-05. Vol. 295, num. 23, p. 7905-7922. DOI : 10.1074/jbc.RA119.012517.

Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity

A. D. Stephens; M. Zacharopoulou; R. Moons; G. Fusco; N. Seetaloo et al. 

Nature Communications. 2020-06-04. Vol. 11, num. 1, p. 2820. DOI : 10.1038/s41467-020-16564-3.

Education and research are essential for lasting peace in Yemen

F. Zakham; O. Vapalahti; H. A. Lashual 

Lancet. 2020-04-04. Vol. 395, num. 10230, p. 1114-1114. DOI : 10.1016/S0140-6736(20)30162-8.

Unraveling the complexity of amyloid polymorphism using gold nanoparticles and cryo-EM

U. Cendrowska; P. J. Silva; N. Ait-Bouziad; M. Mueller; Z. P. Guven et al. 

Proceedings Of The National Academy Of Sciences Of The United States Of America. 2020-03-24. Vol. 117, num. 12, p. 6866-6874. DOI : 10.1073/pnas.1916176117.

The busy lives of academics have hidden costs — and universities must take better care of their faculty members

H. Lashuel 

Nature Careers Community. 2020-03-05. DOI : 10.1038/d41586-020-00661-w.

A simple, versatile and robust centrifugation-based filtration protocol for the isolation and quantification of alpha-synuclein monomers, oligomers and fibrils: Towards improving experimental reproducibility in alpha-synuclein research

S. T. Kumar; S. Donzelli; A. Chiki; M. M. K. Syed; H. A. Lashuel 

Journal Of Neurochemistry. 2020-02-25.  p. e14955. DOI : 10.1111/jnc.14955.

The process of Lewy body formation, rather than simply α-synuclein fibrillization, is one of the major drivers of neurodegeneration

A-L. Mahul-Mellier; J. Burtscher; N. Maharjan; L. Weerens; M. Croisier et al. 

Proceedings of the National Academy of Sciences of United States of America. 2020-02-19.  p. 201913904. DOI : 10.1073/pnas.1913904117.

Site-Specific Hyperphosphorylation Inhibits, Rather than Promotes, Tau Fibrillization, Seeding Capacity, and Its Microtubule Binding

M. Haj-Yahya; P. Gopinath; K. Rajasekhar; H. Mirbaha; M. I. Diamond et al. 

Angewandte Chemie-International Edition. 2020-01-28. Vol. 59, num. 10, p. 4059-4067. DOI : 10.1002/anie.201913001.

Ultrasensitive quantitative measurement of huntingtin phosphorylation at residue S13

C. Cariulo; M. Verani; P. Martufi; R. Ingenito; M. Finotto et al. 

Biochemical And Biophysical Research Communications. 2020-01-15. Vol. 521, num. 3, p. 549-554. DOI : 10.1016/j.bbrc.2019.09.097.

What about faculty?

H. A. Lashuel 

Elife. 2020-01-08. Vol. 9, p. e54551. DOI : 10.7554/eLife.54551.

Pronounced α-synuclein pathology in a seeding-based mouse model is not sufficient to induce mitochondrial respiration deficits in the striatum and amygdala

J. Burtscher; J-C. Copin; C. Sandi; H. Lashuel 

eNeuro. 2020. Vol. 7, num. 4, p. ENEURO.0110-20.2020. DOI : 10.1523/ENEURO.0110-20.2020.

2019

The Role of Post-translational Modifications on the Energy Landscape of Huntingtin N-Terminus

H. Yalinca; C. J. C. Gehin; V. Oleinikovas; H. A. Lashuel; F. L. Gervasio et al. 

Frontiers in Molecular Biosciences. 2019-10-01. Vol. 6, p. 95. DOI : 10.3389/fmolb.2019.00095.

Phospho-S129 Alpha-Synuclein Is Present in Human Plasma but Not in Cerebrospinal Fluid as Determined by an Ultrasensitive Immunoassay

C. Cariulo; P. Martufi; M. Verani; L. Azzollini; G. Bruni et al. 

Frontiers in Neuroscience. 2019-08-22. Vol. 13, p. 889. DOI : 10.3389/fnins.2019.00889.

Single Posttranslational Modifications in the Central Repeat Domains of Tau4 Impact its Aggregation and Tubulin Binding

D. Ellmer; M. Brehs; M. Haj-Yahya; H. A. Lashuel; C. F. W. Becker 

Angewandte Chemie-International Edition. 2019-02-04. Vol. 58, num. 6, p. 1616-1620. DOI : 10.1002/anie.201805238.

alpha-Synuclein O-GlcNAcylation alters aggregation and toxicity, revealing certain residues as potential inhibitors of Parkinson’s disease

P. M. Levine; A. Galesic; A. T. Balana; A-L. Mahul-Mellier; M. X. Navarro et al. 

Proceedings Of The National Academy Of Sciences Of The United States Of America. 2019-01-29. Vol. 116, num. 5, p. 1511-1519. DOI : 10.1073/pnas.1808845116.

Chronic corticosterone aggravates behavioral and neuronal symptomatology in a mouse model of alpha-synuclein pathology

J. Burtscher; J-C. Copin; J. Rodrigues; S. T. Kumar; A. Chiki et al. 

Neurobiol Aging. 2019. Vol. 83, p. 11-20. DOI : 10.1016/j.neurobiolaging.2019.08.007.

Antibody-based methods for the measurement of α-synuclein concentration in human cerebrospinal fluid – method comparison and round robin study

B. Mollenhauer; B. F. DuBois; D. Drake; J. Duong; K. Blennow et al. 

Journal of Neurochemistry. 2019. Vol. 149, num. 1, p. 126-138. DOI : 10.1111/jnc.14569.

2018

N-terminal Huntingtin (Htt) phosphorylation is a molecular switch regulating Htt aggregation, helical conformation, internalization, and nuclear targeting

S. M. Deguire; F. S. Ruggeri; M-B. Fares; A. Chiki; U. Cendrowska et al. 

Journal of Biological Chemistry. 2018-09-05.  p. jbc.RA118.004621. DOI : 10.1074/jbc.RA118.004621.

Identification and nanomechanical characterization of the fundamental single-strand protofilaments of amyloid α-synuclein fibrils

F. S. Ruggeri; F. Benedetti; T. P. J. Knowles; H. A. Lashuel; S. Sekatskii et al. 

Proceedings of the National Academy of Sciences. 2018-06-25.  p. 201721220. DOI : 10.1073/pnas.1721220115.

Resolving molecule-specific information in dynamic lipid membrane processes with multi-resonant infrared metasurfaces

D. Rodrigo; A. Tittl; N. Ait-Bouziad; A. John-Herpin; O. Limaj et al. 

Nature Communications. 2018-06-04. Vol. 9, num. 1, p. 2160. DOI : 10.1038/s41467-018-04594-x.

Real-time in-situ secondary structure analysis of protein monolayer with mid-infrared plasmonic nanoantennas

D. Etezadi; J. B. Warner; H. A. Lashuel; H. Altug 

ACS Sensors. 2018-05-30. Vol. 3, num. 6, p. 1109-1117. DOI : 10.1021/acssensors.8b00115.

Protein Semisynthesis Provides Access to Tau Disease-Associated Post-translational Modifications (PTMs) and Paves the Way to Deciphering the Tau PTM Code in Health and Diseased States

M. Haj-Yahya; H. A. Lashuel 

Journal of the American Chemical Society. 2018-04-24. Vol. 140, num. 21, p. 6611-6621. DOI : 10.1021/jacs.8b02668.

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy

A. Reif; A. Chiki; J. Ricci; H. Lashuel 

Journal of Visualized Experiments. 2018-03-29. num. 136, p. e57506. DOI : 10.3791/57506.

Exploring the role of post-translational modifications in regulating α-synuclein interactions by studying the effects of phosphorylation on nanobody binding

F. El Turk; E. De Genst; T. Guilliams; B. C. D. Fauvet; J. Kiwi et al. 

Proteins Science. 2018-03-29. Vol. 27, num. 7, p. 1262-1274. DOI : 10.1002/pro.3412.

Combined Multi-Plane Tomographic Phase Retrieval and Stochastic Optical Fluctuation Imaging for 4D Cell Microscopy

A. Descloux; K. Grußmayer; E. Bostan; T. Lukes; A. Bouwens et al. 

Nature Photonics. 2018. Vol. 12, num. 3, p. 165-172. DOI : 10.1038/s41566-018-0109-4.

2017

Activation of the STING-dependent type I interferon response reduces microglial reactivity and neuroinflammation

V. Mathus; R. Burai; R. Vest; L. Bonanno; B. Lehallier et al. 

Neuron. 2017. Vol. 96, num. 6, p. 1290-1302.e6. DOI : 10.1016/j.neuron.2017.11.032.

Phosphorylation of huntingtin at residue T3 is decreased in Huntington’s disease and modulates mutant huntingtin protein conformation

C. Cariulo; L. Azzollini; M. Verani; P. Martufi; R. Boggio et al. 

Proceedings of the National Academy of Sciences. 2017. Vol. 114, num. 50, p. E10809-E10818. DOI : 10.1073/pnas.1705372114.

Monomeric Huntingtin Exon 1 Has Similar Overall Structural Features for Wild-Type and Pathological Polyglutamine Lengths

J. B. Warner IV; K. Ruff; P. Siong Tan; E. A. Lemke; R. V. Pappu et al. 

Journal of the American Chemical Society. 2017. Vol. 139, num. 41, p. 14456-14469. DOI : 10.1021/jacs.7b06659.

Membrane scission driven by the PROPPIN Atg18

N. Gopaldass; B. Fauvet; H. Lashuel; A. Roux; A. Mayer 

Embo Journal. 2017. Vol. 36, num. 22, p. 3274-3291. DOI : 10.15252/embj.201796859.

Amyloid Single Cell Cytotoxicity Assays by Nanomotion Detection

F. Ruggeri; A-L. Mahul; S. Kasas; H. Lashuel; G. Longo et al. 

Cell Death Discovery. 2017. Vol. 3, num. 1, p. 17053-17060. DOI : 10.1038/cddiscovery.2017.53.

Discovery and characterization of novel stable tau oligomeric complexes: Implications for the role of Tau/phospholipid interactions in regulating its functions in health and disease

N. Ait-Bouziad; G. Lv; A. L. Mahul-Mellier; S. Xiao; G. Zorludemir et al. 

Nature Communications. 2017. Vol. 8, num. 1, p. 1678. DOI : 10.1038/s41467-017-01575-4.

A user’s guide for α-synuclein biomarker studies in biological fluids: Perianalytical considerations

B. Mollenhauer; R. Batrla; O. El-Agnaf; D. R. Galasko; H. A. Lashuel et al. 

Movement Disorders. 2017. Vol. 32, num. 8, p. 1117-1130. DOI : 10.1002/mds.27090.

Polyglutamine expansion affects huntingtin conformation in multiple Huntington’s disease models

M. Daldin; V. Fodale; C. Cariulo; L. Azzollini; M. Verani et al. 

Scientific Reports. 2017. Vol. 7, num. 1, p. 5070. DOI : 10.1038/s41598-017-05336-7.

Glycation potentiates α-synuclein-associated neurodegeneration in synucleinopathies

H. Vicente Miranda; É. M. Szego; L. M. A. Oliveira; C. Breda; E. Darendelioglu et al. 

Brain : a journal of neurology. 2017. Vol. 140, num. 5, p. 1399-1419. DOI : 10.1093/brain/awx056.

Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation-Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6

A. Chiki; S. M. DeGuire; F. S. Ruggeri; D. Sanfelice; A. Ansaloni et al. 

Angewandte Chemie (International ed. in English). 2017. Vol. 56, num. 19, p. 5202-5207. DOI : 10.1002/anie.201611750.

Nanoplasmonic mid-infrared biosensor for in vitro protein secondary structure detection

D. Etezadi; J. B. Warner IV; F. S. Ruggeri; G. Dietler; H. A. Lashuel et al. 

Light: Science and Applications. 2017. Vol. 6, num. 8, p. e17029. DOI : 10.1038/lsa.2017.29.

The America I believe in

H. A. Lashuel 

Science (New York, N.Y.). 2017. Vol. 355, num. 6326, p. 766. DOI : 10.1126/science.355.6326.766.

The mechanism of sirtuin 2-mediated exacerbation of alpha-synuclein toxicity in models of Parkinson disease

R. M. de Oliveira; H. Vicente Miranda; L. Francelle; R. Pinho; É. M. Szegö et al. 

PLoS Biology. 2017. Vol. 15, num. 3, p. e2000374. DOI : 10.1371/journal.pbio.2000374.

2016

Nanoscale studies link amyloid maturity with polyglutamine diseases onset

F. S. Ruggeri; S. Vieweg; U. Cendrowska; G. Longo; A. Chiki et al. 

Scientific Reports. 2016-08-01. Vol. 6, p. 31155. DOI : 10.1038/srep31155.

A New Caged-Glutamine Derivative as a Tool To Control the Assembly of Glutamine-Containing Amyloidogenic Peptides

L. Awad; N. Jejelava; R. Burai; H. A. Lashuel 

Chembiochem : a European journal of chemical biology. 2016. Vol. 17, num. 24, p. 2353-2360. DOI : 10.1002/cbic.201600474.

Semisynthetic and in Vitro Phosphorylation of Alpha-Synuclein at Y39 Promotes Functional Partly Helical Membrane-Bound States Resembling Those Induced by PD Mutations

I. Dikiy; B. Fauvet; A. Jovicic; A-L. Mahul-Mellier; C. Desobry et al. 

Acs Chemical Biology. 2016. Vol. 11, num. 9, p. 2428-2437. DOI : 10.1021/acschembio.6b00539.

An Intein-based Strategy for the Production of Tag-free Huntingtin Exon 1 Proteins Enables New Insights into the Polyglutamine Dependence of Httex1 Aggregation and Fibril Formation

S. Vieweg; A. Ansaloni; Z-M. Wang; J. B. Warner; H. A. Lashuel 

Journal Of Biological Chemistry. 2016. Vol. 291, num. 23, p. 12074-12086. DOI : 10.1074/jbc.M116.713982.

Health hazards of methylammonium lead iodide based perovskites: cytotoxicity studies

I. R. Benmessaoud; A-L. Mahul-Mellier; E. Horváth; B. Maco; M. Spina et al. 

Toxicol. Res.. 2016. Vol. 5, num. 2, p. 407-419. DOI : 10.1039/C5TX00303B.

Induction of de novo α-synuclein fibrillization in a neuronal model for Parkinson’s disease

M-B. Fares; B. Maco; A. Oueslati; E. Rockenstein; N. Ninkina et al. 

Proceedings of the National Academy of Sciences of the United States of America. 2016. Vol. 113, num. 7, p. E912-21. DOI : 10.1073/pnas.1512876113.

Microtubule-Binding R3 Fragment from Tau Self-Assembles into Giant Multistranded Amyloid Ribbons

J. Adamcik; A. Sanchez-Ferrer; N. Ait-Bouziad; N. P. Reynolds; H. A. Lashuel et al. 

Angewandte Chemie-International Edition. 2016. Vol. 55, num. 2, p. 618-622. DOI : 10.1002/anie.201508968.

2015

Detection of huntingtin exon 1 phosphorylation by Phos-Tag SDS-PAGE: Predominant phosphorylation on threonine 3 and regulation by IKKβ

M. B. Bustamante; A. Ansaloni; J. F. Pedersen; L. Azzollini; C. Cariulo et al. 

Biochemical and Biophysical Research Communications. 2015-08-07. Vol. 463, num. 4, p. 1317-1322. DOI : 10.1016/j.bbrc.2015.06.116.

Semisynthesis and Enzymatic Preparation of Post-translationally Modified α-Synuclein

B. Fauvet; H. A. Lashuel 

Methods in molecular biology (Clifton, N.J.). 2015. Vol. 1345, p. 3-20. DOI : 10.1007/978-1-4939-2978-8_1.

Photobiomodulation Suppresses Alpha-Synuclein-Induced Toxicity in an AAV-Based Rat Genetic Model of Parkinson’s Disease

A. Oueslati; B. Lovisa; J. Perrin; G. Wagnières; H. van den Bergh et al. 

PloS One. 2015. Vol. 10, num. 10, p. e0140880. DOI : 10.1371/journal.pone.0140880.

Fibril growth and seeding capacity play key roles in α-synuclein-mediated apoptotic cell death

Mahul-Mellier; F. Vercruysse; B. Maco; N. Ait-Bouziad; M. De Roo et al. 

Cell death and differentiation. 2015. Vol. 22, num. 12, p. 2107-22. DOI : 10.1038/cdd.2015.79.

Influence of the β-sheet content on the mechanical properties of aggregates during amyloid fibrillization

F. S. Ruggeri; J. Adamcik; J. S. Jeong; H. A. Lashuel; R. Mezzenga et al. 

Angewandte Chemie (International ed. in English). 2015. Vol. 54, num. 8, p. 2462-2466. DOI : 10.1002/anie.201409050.

Structural differences of amyloid-beta fibrils revealed by antibodies from phage display

P. Droste; A. Frenzel; M. Steinwand; T. Pelat; P. Thullier et al. 

Bmc Biotechnology. 2015. Vol. 15, p. 57. DOI : 10.1186/s12896-015-0146-8.

Elucidating the Role of Site-Specific Nitration of alpha-Synuclein in the Pathogenesis of Parkinson’s Disease via Protein Semisynthesis and Mutagenesis

R. Burai; N. Ait-Bouziad; A. Chiki; H. A. Lashuel 

Journal Of The American Chemical Society. 2015. Vol. 137, num. 15, p. 5041-5052. DOI : 10.1021/ja5131726.

Parkinson disease mutant E46K enhances α-synuclein phosphorylation in mammalian cell lines, in yeast, and in vivo

M. K. Mbefo; M-B. Fares; K. Paleologou; A. Oueslati; G. Yin et al. 

The Journal of biological chemistry. 2015. Vol. 290, num. 15, p. 9412-27. DOI : 10.1074/jbc.M114.610774.

Parkinson’s Disease Genes VPS35 and EIF4G1 Interact Genetically and Converge on α-Synuclein

N. Dhungel; S. Eleuteri; L-B. Li; N. J. Kramer; J. W. Chartron et al. 

Neuron. 2015. Vol. 85, num. 1, p. 76-87. DOI : 10.1016/j.neuron.2014.11.027.

Novel therapeutic strategy for neurodegeneration by blocking Aβ seeding mediated aggregation in models of Alzheimer’s disease

S. Eleuteri; S. Di Giovanni; E. Rockenstein; M. Mante; A. Adame et al. 

Neurobiology of disease. 2015. Vol. 74, p. 144-57. DOI : 10.1016/j.nbd.2014.08.017.

2014

The H50Q Mutation Enhances alpha-Synuclein Aggregation, Secretion, and Toxicity

O. Khalaf; B. Fauvet; A. Oueslati; I. Dikiy; A-L. Mahul-Mellier et al. 

Journal Of Biological Chemistry. 2014. Vol. 289, num. 32, p. 21856-21876. DOI : 10.1074/jbc.M114.553297.

The novel Parkinson’s disease linked mutation G51D attenuates in vitro aggregation and membrane binding of alpha-synuclein, and enhances its secretion and nuclear localization in cells

M-B. Fares; N. Ait-Bouziad; I. Dikiy; M. K. Mbefo; A. Jovicic et al. 

Human Molecular Genetics. 2014. Vol. 23, num. 17, p. 4491-4509. DOI : 10.1093/hmg/ddu165.

One-Pot Semisynthesis of Exon 1 of the Huntingtin Protein: New Tools for Elucidating the Role of Posttranslational Modifications in the Pathogenesis of Huntington’s Disease

A. Ansaloni; Z-M. Wang; J. S. Jeong; F. S. Ruggeri; G. Dietler et al. 

Angewandte Chemie-International Edition. 2014. Vol. 53, num. 7, p. 1928-1933. DOI : 10.1002/anie.201307510.

c-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson’s disease

A-L. Mahul-Mellier; B. Fauvet; A. Gysbers; I. Dikiy; A. Oueslati et al. 

Human molecular genetics. 2014. Vol. 23, num. 11, p. 2858-79. DOI : 10.1093/hmg/ddt674.

2013

Alpha-synuclein Post-translational Modifications as Potential Biomarkers for Parkinson Disease and Other Synucleinopathies

A. W. Schmid; B. Fauvet; M. Moniatte; H. A. Lashuel 

Molecular & Cellular Proteomics. 2013. Vol. 12, num. 12, p. 3543-3558. DOI : 10.1074/mcp.R113.032730.

Parkin depletion delays motor decline dose-dependently without overtly affecting neuropathology in alpha-synuclein transgenic mice

M. Fournier; A. Roux; J. Garrigue; M-P. Muriel; P. Blanche et al. 

BMC neuroscience. 2013. Vol. 14, num. 1, p. 135. DOI : 10.1186/1471-2202-14-135.

Real-time Amyloid Aggregation Monitoring with a Photonic Crystal-based Approach

S. Santi; V. Musi; E. Descrovi; V. Paeder; J. Di Francesco et al. 

ChemPhysChem. 2013. Vol. 14, num. 15, p. 3476-3482. DOI : 10.1002/cphc.201300633.

Synthetic polyubiquitinated α-Synuclein reveals important insights into the roles of the ubiquitin chain in regulating its pathophysiology

M. Haj-Yahya; B. Fauvet; Y. Herman-Bachinsky; M. Hejjaoui; S. N. Bavikar et al. 

Proceedings of the National Academy of Sciences of the United States of America. 2013. Vol. 110, num. 44, p. 17726-31. DOI : 10.1073/pnas.1315654110.

One-pot total chemical synthesis of human α-synuclein

B. Fauvet; S. M. Butterfield; J. Fuks; A. Brik; H. A. Lashuel 

Chemical communications (Cambridge, England). 2013. Vol. 49, num. 81, p. 9254-6. DOI : 10.1039/c3cc45353g.

Polo-like kinase 2 regulates selective autophagic α-synuclein clearance and suppresses its toxicity in vivo

A. Oueslati; B. L. Schneider; P. Aebischer; H. A. Lashuel 

Proceedings of the National Academy of Sciences of the United States of America. 2013. Vol. 110, num. 41, p. E3945-54. DOI : 10.1073/pnas.1309991110.

Oxidative and nitrative alpha-synuclein modifications and proteostatic stress: implications for disease mechanisms and interventions in synucleinopathies

S. Schildknecht; H. R. Gerding; C. Karreman; M. Drescher; H. A. Lashuel et al. 

Journal of neurochemistry. 2013. Vol. 125, num. 4, p. 491-511. DOI : 10.1111/jnc.12226.

Novel Mechanistic Insight into the Molecular Basis of Amyloid Polymorphism and Secondary Nucleation during Amyloid Formation

J. S. Jeong; A. Ansaloni; R. Mezzenga; H. A. Lashuel; G. Dietler 

Journal of molecular biology. 2013. Vol. 425, num. 10, p. 1765-81. DOI : 10.1016/j.jmb.2013.02.005.

The many faces of α-synuclein: from structure and toxicity to therapeutic target

H. A. Lashuel; C. R. Overk; A. Oueslati; E. Masliah 

Nature reviews. Neuroscience. 2013. Vol. 14, num. 1, p. 38-48. DOI : 10.1038/nrn3406.

2012

Characterization of Molecular Determinants of the Conformational Stability of Macrophage Migration Inhibitory Factor: Leucine 46 Hydrophobic Pocket

F. El-Turk; B. Fauvet; A. Ashrafi; H. Ouertatani-Sakouhi; M-K. Cho et al. 

PLoS ONE. 2012. Vol. 7, num. 9, p. e45024. DOI : 10.1371/journal.pone.0045024.

Discovery of a novel aggregation domain in the huntingtin protein: implications for the mechanisms of Htt aggregation and toxicity

Z-M. Wang; H. A. Lashuel 

Angewandte Chemie (International ed. in English). 2012. Vol. 52, num. 2, p. 562-7. DOI : 10.1002/anie.201206561.

The Size of the Proteasomal Substrate Determines Whether Its Degradation Will Be Mediated by Mono- or Polyubiquitylation

N. Shabek; Y. Herman-Bachinsky; S. Buchsbaum; O. Lewinson; M. Haj-Yahya et al. 

Molecular cell. 2012. Vol. 48, num. 1, p. 87-97. DOI : 10.1016/j.molcel.2012.07.011.

Discovery and Structure Activity Relationship of Small Molecule Inhibitors of Toxic β-Amyloid-42 Fibril Formation

H. Kroth; A. Ansaloni; Y. Varisco; A. Jan; N. Sreenivasachary et al. 

The Journal of biological chemistry. 2012. Vol. 287, num. 41, p. 34786-800. DOI : 10.1074/jbc.M112.357665.

Characterization of semisynthetic and naturally Nα-acetylated α-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of α-synuclein

B. Fauvet; M-B. Fares; F. Samuel; I. Dikiy; A. Tandon et al. 

The Journal of biological chemistry. 2012. Vol. 287, num. 34, p. 28243-62. DOI : 10.1074/jbc.M112.383711.

Measurement of intrinsic properties of amyloid fibrils by the peak force QNM method

J. Adamcik; C. Lara; I. Usov; J. S. Jeong; F. S. Ruggeri et al. 

Nanoscale. 2012. Vol. 4, num. 15, p. 4426-9. DOI : 10.1039/c2nr30768e.

Phosphorylation of α-synuclein is crucial in compensating for proteasomal dysfunction

H. S. Choi; H. Liew; A. Jang; Y-M. Kim; H. Lashuel et al. 

Biochemical and biophysical research communications. 2012. Vol. 424, num. 3, p. 597-603. DOI : 10.1016/j.bbrc.2012.06.159.

Reactive oxidative species enhance amyloid toxicity in APP/PS1 mouse neurons

B. Yang; X. Sun; H. Lashuel; Y. Zhang 

Neuroscience Bulletin. 2012. Vol. 28, p. 233-239. DOI : 10.1007/s12264-012-1239-1.

Establishing the links between Aβ aggregation and cytotoxicity in vitro using biophysical approaches

A. Jan; H. A. Lashuel 

Methods in molecular biology (Clifton, N.J.). 2012. Vol. 849, p. 227-43. DOI : 10.1007/978-1-61779-551-0_16.

α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer

B. Fauvet; M. K. Mbefo; M-B. Fares; C. Desobry; S. Michael et al. 

The Journal of biological chemistry. 2012. Vol. 287, num. 19, p. 15345-64. DOI : 10.1074/jbc.M111.318949.

Elucidating the role of C-terminal post-translational modifications using protein semisynthesis strategies: α-synuclein phosphorylation at tyrosine 125

M. Hejjaoui; S. Butterfield; B. Fauvet; F. Vercruysse; J. Cui et al. 

Journal of the American Chemical Society. 2012. Vol. 134, num. 11, p. 5196-210. DOI : 10.1021/ja210866j.

Chemical strategies for controlling protein folding and elucidating the molecular mechanisms of amyloid formation and toxicity

S. Butterfield; M. Hejjaoui; B. Fauvet; L. Awad; H. A. Lashuel 

Journal of molecular biology. 2012. Vol. 421, num. 2-3, p. 204-36. DOI : 10.1016/j.jmb.2012.01.051.

Mimicking Phosphorylation at Serine 87 Inhibits the Aggregation of Human α-Synuclein and Protects against Its Toxicity in a Rat Model of Parkinson’s Disease

A. Oueslati; K. E. Paleologou; B. L. Schneider; P. Aebischer; H. A. Lashuel 

The Journal of neuroscience : the official journal of the Society for Neuroscience. 2012. Vol. 32, num. 5, p. 1536-44. DOI : 10.1523/JNEUROSCI.3784-11.2012.

2011

Arab world needs its science diaspora

H. A. Lashuel; W. K. Al-Delaimy 

Nature. 2011. Vol. 472, p. 418-418. DOI : 10.1038/472418d.

Phosphorylation of alpha-Synuclein at Y125 and S129 Alters Its Metal Binding Properties: Implications for Understanding the Role of alpha-Synuclein in the Pathogenesis of Parkinson’s Disease and Related Disorders

Y. Lu; M. Prudent; B. Fauvet; H. A. Lashuel; H. H. Girault 

Acs Chemical Neuroscience. 2011. Vol. 2, num. 11, p. 667-675. DOI : 10.1021/cn200074d.

Chemical Synthesis and Expression of the HIV-1 Rev Protein

P. Siman; O. Blatt; T. Moyal; T. Danieli; M. Lebendiker et al. 

ChemBioChem. 2011. Vol. 12, num. 7, p. 1097-1104. DOI : 10.1002/cbic.201100033.

Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species

A. Jan; O. Adolfsson; I. Allaman; B. AL; M. PJ et al. 

The journal of biological chemistry. 2011. Vol. 286, num. 10, p. 8585-96. DOI : 10.1074/jbc.M110.172411.

Towards elucidation of the role of ubiquitination in the pathogenesis of Parkinson’s disease with semisynthetic ubiquitinated α-synuclein

M. Hejjaoui; M. Haj-Yahya; K. KS; A. Brik; H. Lashuel 

Angewandte Chemie International Edition. 2011. Vol. 50, num. 2, p. 405-409. DOI : 10.1002/anie.201005546.

Macrophage migration inhibitory factor is critically involved in basal and fluoxetine-stimulated adult hippocampal cell proliferation and in anxiety, depression, and memory-related behaviors

L. Conboy; E. Varea; J. E. Castro; H. Sakouhi-Ouertatani; T. Calandra et al. 

Molecular Psychiatry. 2011. Vol. 16, num. 5, p. 533-47. DOI : 10.1038/mp.2010.15.

2010

Parkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer model

P. J. Khandelwal; S. B. Dumanis; L. R. Feng; K. Maguire-Zeiss; G. Rebeck et al. 

Molecular neurodegeneration. 2010. Vol. 5, p. 47. DOI : 10.1186/1750-1326-5-47.

Stable  -Synuclein Oligomers Strongly Inhibit Chaperone Activity of the Hsp70 System by Weak Interactions with J-domain Co-chaperones

M-P. Hinault; A. F. H. Cuendet; R. U. H. Mattoo; M. Mensi; G. Dietler et al. 

Journal of Biological Chemistry. 2010. Vol. 285, num. 49, p. 38173-38182. DOI : 10.1074/jbc.M110.127753.

The anti-Parkinsonian drug selegiline delays the nucleation phase of α-synuclein aggregation leading to the formation of nontoxic species

C. A. Braga; C. Follmer; F. L. Palhano; E. Khattar; M. S. Freitas et al. 

Journal of molecular biology. 2010. Vol. 405, num. 1, p. 254-73. DOI : 10.1016/j.jmb.2010.10.027.

Identification and characterization of novel classes of macrophage migration inhibitory factor (MIF) inhibitors with distinct mechanisms of action

H. Ouertatani-Sakouhi; F. El-Turk; B. Fauvet; M-K. Cho; D. Pinar Karpinar et al. 

The Journal of biological chemistry. 2010. Vol. 285, num. 34, p. 26581-98. DOI : 10.1074/jbc.M110.113951.

Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: implications for Parkinson’s disease pathogenesis and therapies

A. Oueslati; M. Fournier; H. A. Lashuel 

Progress in brain research. 2010. Vol. 183, p. 115-45. DOI : 10.1016/S0079-6123(10)83007-9.

An integrative in silico methodology for the identification of modulators of macrophage migration inhibitory factor (MIF) tautomerase activity

F. El Turk; B. Fauvet; H. Ouertatani-Sakouhi; A. Lugari; S. Betzi et al. 

Bioorganic & medicinal chemistry. 2010. Vol. 18, num. 14, p. 5425-40. DOI : 10.1016/j.bmc.2010.05.010.

Amyloidogenic protein-membrane interactions: mechanistic insight from model systems

S. M. Butterfield; H. A. Lashuel 

Angewandte Chemie (International ed. in English). 2010. Vol. 49, num. 33, p. 5628-54. DOI : 10.1002/anie.200906670.

Preparation and characterization of toxic Abeta aggregates for structural and functional studies in Alzheimer’s disease research

A. Jan; D. M. Hartley; H. A. Lashuel 

Nature protocols. 2010. Vol. 5, num. 6, p. 1186-209. DOI : 10.1038/nprot.2010.72.

Kinetic-based high-throughput screening assay to discover novel classes of macrophage migration inhibitory factor inhibitors

H. Ouertatani-Sakouhi; M. Liu; F. El-Turk; G. D. Cuny; M. A. Glicksman et al. 

Journal of biomolecular screening. 2010. Vol. 15, num. 4, p. 347-58. DOI : 10.1177/1087057110363825.

Entacapone and tolcapone, two catechol O-methyltransferase inhibitors, block fibril formation of alpha-synuclein and beta-amyloid and protect against amyloid-induced toxicity

S. Di Giovanni; S. Eleuteri; K. E. Paleologou; G. Yin; M. Zweckstetter et al. 

The Journal of biological chemistry. 2010. Vol. 285, num. 20, p. 14941-54. DOI : 10.1074/jbc.M109.080390.

Amyloid-beta aggregates cause alterations of astrocytic metabolic phenotype: impact on neuronal viability

I. Allaman; M. Gavillet; M. Bélanger; T. Laroche; D. Viertl et al. 

The Journal of neuroscience : the official journal of the Society for Neuroscience. 2010. Vol. 30, num. 9, p. 3326-3338. DOI : 10.1523/JNEUROSCI.5098-09.2010.

Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions

K. E. Paleologou; A. Oueslati; G. Shakked; C. C. Rospigliosi; H-Y. Kim et al. 

The Journal of neuroscience : the official journal of the Society for Neuroscience. 2010. Vol. 30, num. 9, p. 3184-98. DOI : 10.1523/JNEUROSCI.5922-09.2010.

Phosphorylation of synucleins by members of the Polo-like kinase family

M. Mbefo; K. Paleologou; A. Boucharaba; A. Oueslati; H. Schell et al. 

The Journal of biological chemistry. 2010. Vol. 285, num. 4, p. 2807-2822. DOI : 10.1074/jbc.M109.081950.

2009

Structural properties of pore-forming oligomers of alpha-synuclein

H. Y. Kim; M. K. Cho; A. Kumar; E. Maier; C. Siebenharr et al. 

Journal of the American Chemical Society. 2009. Vol. 131, num. 47, p. 17482-17489. DOI : 10.1021/ja9077599.

Dissecting the mechanisms of tissue transglutaminase-induced cross-linking of alpha-synuclein: implications for the pathogenesis of Parkinson disease

A. W. Schmid; D. Chiappe; V. Pignat; V. Grimminger; I. Hang et al. 

The Journal of biological chemistry. 2009. Vol. 284, num. 19, p. 13128-42. DOI : 10.1074/jbc.M809067200.

E46K Parkinson’s-linked mutation enhances C-terminal-to-N-terminal contacts in alpha-synuclein

C. C. Rospigliosi; S. McClendon; A. W. Schmid; T. F. Ramlall; P. Barré et al. 

Journal of molecular biology. 2009. Vol. 388, num. 5, p. 1022-32. DOI : 10.1016/j.jmb.2009.03.065.

Switch-peptides as folding precursors in self-assembling peptides and amyloid fibrillogenesis

M. S. Camus; R. Mimna; A. Schmid; A. Chandravarkar; G. Tuchscherer et al. 

Advances in experimental medicine and biology. 2009. Vol. 611, p. 281-2. DOI : 10.1007/978-0-387-73657-0_126.

Amyloids go genomic: insights regarding the sequence determinants of prion formation from genome-wide studies

H. A. Lashuel; R. V. Pappu 

Chembiochem : a European journal of chemical biology. 2009. Vol. 10, num. 12, p. 1951-4. DOI : 10.1002/cbic.200900373.

Parkin deficiency delays motor decline and disease manifestation in a mouse model of synucleinopathy

M. Fournier; J. Vitte; J. Garrigue; D. Langui; J-P. Dullin et al. 

PloS One. 2009. Vol. 4, num. 8, p. e6629. DOI : 10.1371/journal.pone.0006629.

A new class of isothiocyanate-based irreversible inhibitors of macrophage migration inhibitory factor

H. Ouertatani-Sakouhi; F. El-Turk; B. Fauvet; T. Roger; D. Le Roy et al. 

Biochemistry. 2009. Vol. 48, num. 41, p. 9858-70. DOI : 10.1021/bi900957e.

Structure and function of the molecular chaperone Hsp104 from yeast

V. Grimminger-Marquardt; H. A. Lashuel 

Biopolymers. 2009. Vol. 93, num. 3, p. 252-76. DOI : 10.1002/bip.21301.

Highly efficient and chemoselective peptide ubiquitylation

K. S. Ajish Kumar; M. Haj-Yahya; D. Olschewski; H. A. Lashuel; A. Brik 

Angewandte Chemie (International ed. in English). 2009. Vol. 48, num. 43, p. 8090-4. DOI : 10.1002/anie.200902936.

2008

Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein

K. E. Paleologou; A. W. Schmid; C. C. Rospigliosi; H-Y. Kim; G. R. Lamberto et al. 

The Journal of biological chemistry. 2008. Vol. 283, num. 24, p. 16895-905. DOI : 10.1074/jbc.M800747200.

Switch-peptides: design and characterization of controllable super-amyloid-forming host-guest peptides as tools for identifying anti-amyloid agents

M-S. Camus; S. Dos Santos; A. Chandravarkar; B. Mandal; A. W. Schmid et al. 

Chembiochem : a European journal of chemical biology. 2008. Vol. 9, num. 13, p. 2104-12. DOI : 10.1002/cbic.200800245.

The ratio of monomeric to aggregated forms of Abeta40 and Abeta42 is an important determinant of amyloid-beta aggregation, fibrillogenesis, and toxicity

A. Jan; O. Gokce; R. Luthi-Carter; H. A. Lashuel 

The Journal of biological chemistry. 2008. Vol. 283, num. 42, p. 28176-89. DOI : 10.1074/jbc.M803159200.

Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease

C. Lo Bianco; J. Shorter; E. Régulier; H. Lashuel; T. Iwatsubo et al. 

The Journal of clinical investigation. 2008. Vol. 118, num. 9, p. 3087-97. DOI : 10.1172/JCI35781.

The conformational flexibility of the carboxy terminal residues 105-114 is a key modulator of the catalytic activity and stability of macrophage migration inhibitory factor

F. El-Turk; M. Cascella; H. Ouertatani-Sakouhi; R. L. Narayanan; L. Leng et al. 

Biochemistry. 2008. Vol. 47, num. 40, p. 10740-56. DOI : 10.1021/bi800603x.

Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of Abeta fibrils and protofibrils

M. Arimon; V. Grimminger; F. Sanz; H. A. Lashuel 

Journal of molecular biology. 2008. Vol. 384, num. 5, p. 1157-73. DOI : 10.1016/j.jmb.2008.09.063.

Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC region

F. E. Herrera; A. Chesi; K. E. Paleologou; A. Schmid; A. Munoz et al. 

PloS One. 2008. Vol. 3, num. 10, p. e3394. DOI : 10.1371/journal.pone.0003394.

Switch peptide via Staudinger reaction

N. Nepomniaschiy; V. Grimminger; A. Cohen; S. DiGiovanni; H. A. Lashuel et al. 

Organic letters. 2008. Vol. 10, num. 22, p. 5243-6. DOI : 10.1021/ol802268e.

2007

Dopamine affects the stability, hydration, and packing of protofibrils and fibrils of the wild type and variants of alpha-synuclein

C. Follmer; L. Romão; C. M. Einsiedler; T. C. R. Porto; F. A. Lara et al. 

Biochemistry. 2007. Vol. 46, num. 2, p. 472-82. DOI : 10.1021/bi061871+.

The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric states

R. A. Fredenburg; C. Rospigliosi; R. K. Meray; J. C. Kessler; H. A. Lashuel et al. 

Biochemistry. 2007. Vol. 46, num. 24, p. 7107-18. DOI : 10.1021/bi7000246.

Branched KLVFF tetramers strongly potentiate inhibition of beta-amyloid aggregation

S. M. Chafekar; H. Malda; M. Merkx; E. W. Meijer; D. Viertl et al. 

Chembiochem : a European journal of chemical biology. 2007. Vol. 8, num. 15, p. 1857-64. DOI : 10.1002/cbic.200700338.

Switch-peptides as folding precursors in self-assembling peptides and amyloid fibrillogenesis

G. Tuchscherer; A. Chandravarkar; M-S. Camus; J. Berard; K. Murat et al. 

Biopolymers. 2007. Vol. 88, num. 2, p. 239-252. DOI : 10.1002/bip.20663.

Disruption of amyloid-derived peptide assemblies through the controlled induction of a beta-sheet to alpha-helix transformation: application of the switch concept

R. Mimna; M-S. Camus; A. Schmid; G. Tuchscherer; H. A. Lashuel et al. 

Angewandte Chemie, International Edition. 2007. Vol. 46, num. 15, p. 2681-2684. DOI : 10.1002/anie.200603681.

2006

Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?

H. A. Lashuel; P. T. Lansbury 

Quarterly reviews of biophysics. 2006. Vol. 39, num. 2, p. 167-201. DOI : 10.1017/S0033583506004422.

A century-old debate on protein aggregation and neurodegeneration enters the clinic

P. T. Lansbury; H. A. Lashuel 

Nature. 2006. Vol. 443, num. 7113, p. 774-9. DOI : 10.1038/nature05290.

Islam: governments need to reform education and build a scientific culture

H. A. Lashuel; N. Zawia 

Nature. 2006. Vol. 444, num. 7119, p. 545. DOI : 10.1038/444545a.

Rescuing defective vesicular trafficking protects against alpha-synuclein toxicity in cellular and animal models of Parkinson’s disease

H. A. Lashuel; H. Hirling 

ACS chemical biology. 2006. Vol. 1, num. 7, p. 420-4. DOI : 10.1021/cb600331e.

Switch-peptides: from conformational studies to Alzheimer’s disease

L. Saucede; S. Dos Santos; A. Chandravarkar; B. Mandal; R. Mimna et al. 

Chimia. 2006. Vol. 60, num. 4, p. 199-202. DOI : 10.2533/000942906777674921.

2005

The materials science of protein aggregation

D. L. Cox; H. A. Lashuel; K. Y. C. Lee; R. R. R. Singh 

MRS Bulletin. 2005. Vol. 30, num. 6, p. 452-457. DOI : 10.1557/mrs2005.123.

Production and characterization of astrocyte-derived human apolipoprotein E isoforms from immortalized astrocytes and their interactions with amyloid-beta

M. Morikawa; J. D. Fryer; P. M. Sullivan; E. A. Christopher; S. E. Wahrle et al. 

Neurobiology of disease. 2005. Vol. 19, num. 1-2, p. 66-76. DOI : 10.1016/j.nbd.2004.11.005.

In vitro preparation of prefibrillar intermediates of amyloid-beta and alpha-synuclein

H. A. Lashuel; D. Grillo-Bosch 

Methods in molecular biology (Clifton, N.J.). 2005. Vol. 299, p. 19-33. DOI : 10.1385/1-59259-874-9:019.

Molecular electron microscopy approaches to elucidating the mechanisms of protein fibrillogenesis

H. A. Lashuel; J. S. Wall 

Methods in molecular biology (Clifton, N.J.). 2005. Vol. 299, p. 81-101. DOI : 10.1385/1-59259-874-9:081.

Membrane permeabilization: a common mechanism in protein-misfolding diseases

H. A. Lashuel 

Science of aging knowledge environment : SAGE KE. 2005. Vol. 2005, num. 38, p. pe28. DOI : 10.1126/sageke.2005.38.pe28.

From hexamer to amyloid: marginal stability of apolipoprotein SAA2.2 leads to in vitro fibril formation at physiological temperature

L. Wang; H. A. Lashuel; W. Colón 

Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis. 2005. Vol. 12, num. 3, p. 139-48. DOI : 10.1080/13506120500223084.

Lead (Pb) exposure and its effect on APP proteolysis and Abeta aggregation

M. R. Basha; M. Murali; H. K. Siddiqi; K. Ghosal; O. K. Siddiqi et al. 

The FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 2005. Vol. 19, num. 14, p. 2083-4. DOI : 10.1096/fj.05-4375fje.

Amyloid fibril formation by macrophage migration inhibitory factor

H. A. Lashuel; B. Aljabari; E. M. Sigurdsson; C. N. Metz; L. Leng et al. 

Biochemical and biophysical research communications. 2005. Vol. 338, num. 2, p. 973-80. DOI : 10.1016/j.bbrc.2005.10.040.

2004

Interactions among alpha-synuclein, dopamine, and biomembranes: some clues for understanding neurodegeneration in Parkinson’s disease

J-C. Rochet; T. F. Outeiro; K. A. Conway; T. T. Ding; M. J. Volles et al. 

Journal of molecular neuroscience : MN. 2004. Vol. 23, num. 1-2, p. 23-34. DOI : 10.1385/JMN:23:1-2:023.

Quaternary structure, protein dynamics, and synaptic function of SAP97 controlled by L27 domain interactions

T. Nakagawa; K. Futai; H. A. Lashuel; I. Lo; K. Okamoto et al. 

Neuron. 2004. Vol. 44, num. 3, p. 453-67. DOI : 10.1016/j.neuron.2004.10.012.

2003

Hydration and packing are crucial to amyloidogenesis as revealed by pressure studies on transthyretin variants that either protect or worsen amyloid disease

A. D. Ferrão-Gonzales; L. Palmieri; M. Valory; J. L. Silva; H. Lashuel et al. 

Journal of molecular biology. 2003. Vol. 328, num. 4, p. 963-74. DOI : 10.1016/S0022-2836(03)00368-1.

Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities

D. Foguel; M. C. Suarez; A. D. Ferrão-Gonzales; T. C. R. Porto; L. Palmieri et al. 

Proceedings of the National Academy of Sciences of the United States of America. 2003. Vol. 100, num. 17, p. 9831-6. DOI : 10.1073/pnas.1734009100.

Mixtures of wild-type and a pathogenic (E22G) form of Abeta40 in vitro accumulate protofibrils, including amyloid pores

H. A. Lashuel; D. M. Hartley; B. M. Petre; J. S. Wall; M. N. Simon et al. 

Journal of molecular biology. 2003. Vol. 332, num. 4, p. 795-808. DOI : 10.1016/S0022-2836(03)00927-6.

Discovery of inhibitors that elucidate the role of UCH-L1 activity in the H1299 lung cancer cell line

Y. Liu; H. A. Lashuel; S. Choi; X. Xing; A. Case et al. 

Chemistry & biology. 2003. Vol. 10, num. 9, p. 837-46. DOI : 10.1016/j.chembiol.2003.08.010.

Abeta protofibrils possess a stable core structure resistant to hydrogen exchange

I. Kheterpal; H. A. Lashuel; D. M. Hartley; T. Walz; P. T. Lansbury et al. 

Biochemistry. 2003. Vol. 42, num. 48, p. 14092-8. DOI : 10.1021/bi0357816.

hA molecular switch in amyloid assembly: Met35 and amyloid beta-protein oligomerization

G. Bitan; B. Tarus; S. S. Vollers; H. A. Lashuel; M. M. Condron et al. 

Journal of the American Chemical Society. 2003. Vol. 125, num. 50, p. 15359-65. DOI : 10.1021/ja0349296.

2002

Synthesis, structure, and activity of diclofenac analogues as transthyretin amyloid fibril formation inhibitors

V. B. Oza; C. Smith; P. Raman; E. K. Koepf; H. A. Lashuel et al. 

Journal of medicinal chemistry. 2002. Vol. 45, num. 2, p. 321-32. DOI : 10.1021/jm010257n.

Neurodegenerative disease: amyloid pores from pathogenic mutations

H. A. Lashuel; D. Hartley; B. M. Petre; T. Walz; P. T. Lansbury 

Nature. 2002. Vol. 418, num. 6895, p. 291. DOI : 10.1038/418291a.

New class of inhibitors of amyloid-beta fibril formation. Implications for the mechanism of pathogenesis in Alzheimer’s disease

H. A. Lashuel; D. M. Hartley; D. Balakhaneh; A. Aggarwal; S. Teichberg et al. 

The Journal of biological chemistry. 2002. Vol. 277, num. 45, p. 42881-90. DOI : 10.1074/jbc.M206593200.

Alpha-synuclein, especially the Parkinson’s disease-associated mutants, forms pore-like annular and tubular protofibrils

H. A. Lashuel; B. M. Petre; J. Wall; M. Simon; R. J. Nowak et al. 

Journal of molecular biology. 2002. Vol. 322, num. 5, p. 1089-102. DOI : 10.1016/S0022-2836(02)00735-0.

The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson’s disease susceptibility

Y. Liu; L. Fallon; H. A. Lashuel; Z. Liu; P. T. Lansbury 

Cell. 2002. Vol. 111, num. 2, p. 209-18. DOI : 10.1016/S0092-8674(02)01012-7.

Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channel

L. Wang; H. A. Lashuel; T. Walz; W. Colon 

Proceedings of the National Academy of Sciences of the United States of America. 2002. Vol. 99, num. 25, p. 15947-52. DOI : 10.1073/pnas.252508399.

2000

Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly: Implications for amyloid fibril formation and materials science

H. A. Lashuel; S. R. LaBrenz; L. Woo; L. C. Serpell; J. W. Kelly 

Journal of the American Chemical Society. 2000. Vol. 122, num. 22, p. 5262-5277. DOI : 10.1021/ja9937831.

A glimpse of a possible amyloidogenic intermediate of transthyretin

K. Liu; H. S. Cho; H. A. Lashuel; J. W. Kelly; D. E. Wemmer 

Nature structural biology. 2000. Vol. 7, num. 9, p. 754-7. DOI : 10.1038/78980.

Nuclear import factors importin alpha and importin beta undergo mutually induced conformational changes upon association

G. Cingolani; H. A. Lashuel; L. Gerace; C. W. Müller 

FEBS letters. 2000. Vol. 484, num. 3, p. 291-8. DOI : 10.1016/S0014-5793(00)02154-2.

1999

Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30M, and L55P amyloid fibril formation

H. A. Lashuel; Z. Lai; J. W. Kelly 

Biochemistry. 1999. Vol. 37, num. 51, p. 17851-64. DOI : 10.1021/bi981876+.

The nucleation of monomeric parallel beta-sheet-like structures and their self-assembly in aqueous solution

P. Chitnumsub; W. R. Fiori; H. A. Lashuel; H. Diaz; J. W. Kelly 

Bioorganic & medicinal chemistry. 1999. Vol. 7, num. 1, p. 39-59. DOI : 10.1016/S0968-0896(98)00222-3.

Association between the first two immunoglobulin-like domains of the neural cell adhesion molecule N-CAM

A. R. Atkins; M. J. Osborne; H. A. Lashuel; G. M. Edelman; P. E. Wright et al. 

FEBS letters. 1999. Vol. 451, num. 2, p. 162-8. DOI : 10.1016/S0014-5793(99)00554-2.

The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions

H. A. Lashuel; C. Wurth; L. Woo; J. W. Kelly 

Biochemistry. 1999. Vol. 38, num. 41, p. 13560-73. DOI : 10.1021/bi991021c.

1998

Recombinant human retinol-binding protein refolding, native disulfide formation, and characterization

Y. Xie; H. A. Lashuel; G. J. Miroy; S. Dikler; J. W. Kelly 

Protein expression and purification. 1998. Vol. 14, num. 1, p. 31-7. DOI : 10.1006/prep.1998.0944.

Inhibiting transthyretin conformational changes that lead to amyloid fibril formation

S. A. Peterson; T. Klabunde; H. A. Lashuel; H. Purkey; J. C. Sacchettini et al. 

Proceedings of the National Academy of Sciences of the United States of America. 1998. Vol. 95, num. 22, p. 12956-60. DOI : 10.1073/pnas.95.22.12956.

Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: identification of the transmembrane domain as a site for oligomerization

M. P. Patricelli; H. A. Lashuel; D. K. Giang; J. W. Kelly; B. F. Cravatt 

Biochemistry. 1998. Vol. 37, num. 43, p. 15177-87. DOI : 10.1021/bi981733n.

Complete inhibition of Cdk/cyclin by one molecule of p21(Cip1)

L. Hengst; U. Göpfert; H. A. Lashuel; S. I. Reed 

Genes & development. 1998. Vol. 12, num. 24, p. 3882-8. DOI : 10.1101/gad.12.24.3882.

1997

Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid

J. W. Kelly; W. Colon; Z. Lai; H. A. Lashuel; J. McCulloch et al. 

Advances in protein chemistry. 1997. Vol. 50, p. 161-81. DOI : 10.1016/S0065-3233(08)60321-6.

Guanidine hydrochloride-induced denaturation and refolding of transthyretin exhibits a marked hysteresis: equilibria with high kinetic barriers

Z. Lai; J. McCulloch; H. A. Lashuel; J. W. Kelly 

Biochemistry. 1997. Vol. 36, num. 33, p. 10230-9. DOI : 10.1021/bi963195p.

Oligomerization properties of GCN4 leucine zipper e and g position mutants

X. Zeng; H. Zhu; H. A. Lashuel; J. C. Hu 

Protein science : a publication of the Protein Society. 1997. Vol. 6, num. 10, p. 2218-26. DOI : 10.1002/pro.5560061016.

1996

Inhibiting transthyretin amyloid fibril formation via protein stabilization

G. J. Miroy; Z. Lai; H. A. Lashuel; S. A. Peterson; C. Strang et al. 

Proceedings of the National Academy of Sciences of the United States of America. 1996. Vol. 93, num. 26, p. 15051-6. DOI : 10.1073/pnas.93.26.15051.