Year |
Citation |
Score |
2024 |
Balana AT, Mahul-Mellier AL, Nguyen BA, Horvath M, Javed A, Hard ER, Jasiqi Y, Singh P, Afrin S, Pedretti R, Singh V, Lee VM, Luk KC, Saelices L, Lashuel HA, et al. O-GlcNAc forces an α-synuclein amyloid strain with notably diminished seeding and pathology. Nature Chemical Biology. PMID 38347213 DOI: 10.1038/s41589-024-01551-2 |
0.316 |
|
2023 |
Yang L, Jasiqi Y, Lashuel H. Recombinant Full-Length TDP-43 Oligomers Retain Their Ability to Bind RNAs, Are Not Toxic, and Do Not Seed TDP-43 Aggregation in Vitro. Acs Chemical Neuroscience. 15: 193-204. PMID 38116987 DOI: 10.1021/acschemneuro.3c00691 |
0.336 |
|
2023 |
Yang L, Jasiqi Y, Zettor A, Vadas O, Chiaravalli J, Agou F, Lashuel HA. Effective Inhibition of TDP-43 Aggregation by Native State Stabilization. Angewandte Chemie (International Ed. in English). 63: e202314587. PMID 37949836 DOI: 10.1002/anie.202314587 |
0.309 |
|
2023 |
Limorenko G, Tatli M, Kolla R, Nazarov S, Weil MT, Schöndorf DC, Geist D, Reinhardt P, Ehrnhoefer DE, Stahlberg H, Gasparini L, Lashuel HA. Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates. Nature Communications. 14: 3939. PMID 37402718 DOI: 10.1038/s41467-023-39314-7 |
0.359 |
|
2023 |
Kumar ST, Nazarov S, Porta S, Maharjan N, Cendrowska U, Kabani M, Finamore F, Xu Y, Lee VM, Lashuel HA. Seeding the aggregation of TDP-43 requires post-fibrillization proteolytic cleavage. Nature Neuroscience. PMID 37248338 DOI: 10.1038/s41593-023-01341-4 |
0.387 |
|
2023 |
Balana AT, Mahul-Mellier AL, Nguyen BA, Horvath M, Javed A, Hard ER, Jasiqi Y, Singh P, Afrin S, Pedretti R, Singh V, Lee VM, Luk KC, Saelices L, Lashuel HA, et al. O-GlcNAc modification forces the formation of an α-Synuclein amyloid-strain with notably diminished seeding activity and pathology. Biorxiv : the Preprint Server For Biology. PMID 36945566 DOI: 10.1101/2023.03.07.531573 |
0.349 |
|
2022 |
Altay MF, Liu AKL, Holton JL, Parkkinen L, Lashuel HA. Prominent astrocytic alpha-synuclein pathology with unique post-translational modification signatures unveiled across Lewy body disorders. Acta Neuropathologica Communications. 10: 163. PMID 36371251 DOI: 10.1186/s40478-022-01468-8 |
0.318 |
|
2022 |
Lashuel HA, Mahul-Mellier AL, Novello S, Hegde RN, Jasiqi Y, Altay MF, Donzelli S, DeGuire SM, Burai R, Magalhães P, Chiki A, Ricci J, Boussouf M, Sadek A, Stoops E, et al. Revisiting the specificity and ability of phospho-S129 antibodies to capture alpha-synuclein biochemical and pathological diversity. Npj Parkinson's Disease. 8: 136. PMID 36266318 DOI: 10.1038/s41531-022-00388-7 |
0.729 |
|
2022 |
Teixidor J, Novello S, Ortiz D, Menin L, Lashuel HA, Bertsch A, Renaud P. On-Demand Nanoliter Sampling Probe for the Collection of Brain Fluid. Analytical Chemistry. PMID 35786947 DOI: 10.1021/acs.analchem.2c01577 |
0.688 |
|
2022 |
Nazarov S, Chiki A, Boudeffa D, Lashuel HA. Structural Basis of Huntingtin Fibril Polymorphism Revealed by Cryogenic Electron Microscopy of Exon 1 HTT Fibrils. Journal of the American Chemical Society. 144: 10723-10735. PMID 35679155 DOI: 10.1021/jacs.2c00509 |
0.372 |
|
2021 |
Shillcock JC, Hastings J, Riguet N, Lashuel HA. Non-monotonic fibril surface occlusion by GFP tags from coarse-grained molecular simulations. Computational and Structural Biotechnology Journal. 20: 309-321. PMID 35070162 DOI: 10.1016/j.csbj.2021.12.017 |
0.329 |
|
2021 |
Limorenko G, Lashuel HA. Revisiting the grammar of Tau aggregation and pathology formation: how new insights from brain pathology are shaping how we study and target Tauopathies. Chemical Society Reviews. PMID 34889934 DOI: 10.1039/d1cs00127b |
0.35 |
|
2021 |
Riguet N, Mahul-Mellier AL, Maharjan N, Burtscher J, Croisier M, Knott G, Hastings J, Patin A, Reiterer V, Farhan H, Nasarov S, Lashuel HA. Nuclear and cytoplasmic huntingtin inclusions exhibit distinct biochemical composition, interactome and ultrastructural properties. Nature Communications. 12: 6579. PMID 34772920 DOI: 10.1038/s41467-021-26684-z |
0.316 |
|
2021 |
Limorenko G, Lashuel HA. To target Tau pathologies, we must embrace and reconstruct their complexities. Neurobiology of Disease. 161: 105536. PMID 34718129 DOI: 10.1016/j.nbd.2021.105536 |
0.337 |
|
2021 |
Herrmann F, Hessmann M, Schaertl S, Berg-Rosseburg K, Brown CJ, Bursow G, Chiki A, Ebneth A, Gehrmann M, Hoeschen N, Hotze M, Jahn S, Johnson PD, Khetarpal V, Kiselyov A, ... ... Lashuel H, et al. Pharmacological characterization of mutant huntingtin aggregate-directed PET imaging tracer candidates. Scientific Reports. 11: 17977. PMID 34504195 DOI: 10.1038/s41598-021-97334-z |
0.317 |
|
2021 |
Vieweg S, Mahul-Mellier AL, Ruggeri FS, Riguet N, DeGuire SM, Chiki A, Cendrowska U, Dietler G, Lashuel HA. The Nt17 domain and its helical conformation regulate the aggregation, cellular properties and neurotoxicity of mutant huntingtin exon 1. Journal of Molecular Biology. 167222. PMID 34492254 DOI: 10.1016/j.jmb.2021.167222 |
0.308 |
|
2021 |
Chiki A, Zhang Z, Rajasekhar K, Abriata LA, Rostami I, Krapp LF, Boudeffa D, Dal Peraro M, Lashuel HA. Investigating Crosstalk Among PTMs Provides Novel Insight Into the Structural Basis Underlying the Differential Effects of Nt17 PTMs on Mutant Httex1 Aggregation. Frontiers in Molecular Biosciences. 8: 686086. PMID 34381813 DOI: 10.3389/fmolb.2021.686086 |
0.348 |
|
2021 |
Lashuel HA. Rethinking protein aggregation and drug discovery in neurodegenerative diseases: Why we need to embrace complexity? Current Opinion in Chemical Biology. 64: 67-75. PMID 34174698 DOI: 10.1016/j.cbpa.2021.05.006 |
0.304 |
|
2021 |
Kolla R, Gopinath P, Ricci J, Reif A, Rostami I, Lashuel HA. 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. Journal of the American Chemical Society. 143: 9798-9812. PMID 34161085 DOI: 10.1021/jacs.1c03108 |
0.334 |
|
2021 |
Lashuel HA, Novello S. Lewy body-associated proteins: Victims, instigators, or innocent bystanders? The case of AIMP2 and alpha-synuclein. Neurobiology of Disease. 105417. PMID 34102275 DOI: 10.1016/j.nbd.2021.105417 |
0.765 |
|
2021 |
Vidal RL, Sepulveda D, Troncoso-Escudero P, Garcia-Huerta P, Gonzalez C, Plate L, Jerez C, Canovas J, Rivera CA, Castillo V, Cisternas M, Leal S, Martinez A, Grandjean J, Lashuel HA, et al. Enforced dimerization between XBP1s and ATF6f enhances the protective effects of the unfolded protein response (UPR) in models of neurodegeneration. Molecular Therapy : the Journal of the American Society of Gene Therapy. PMID 33545358 DOI: 10.1016/j.ymthe.2021.01.033 |
0.688 |
|
2021 |
Fares MB, Jagannath S, Lashuel HA. Reverse engineering Lewy bodies: how far have we come and how far can we go? Nature Reviews. Neuroscience. PMID 33432241 DOI: 10.1038/s41583-020-00416-6 |
0.31 |
|
2020 |
Chiki A, Ricci J, Hegde RN, Abriata LA, Reif A, Boudeffa D, Lashuel HA. Site-specific phosphorylation of Huntingtin exon 1 recombinant proteins enabled by the discovery of novel kinases. Chembiochem : a European Journal of Chemical Biology. PMID 32805086 DOI: 10.1002/Cbic.202000508 |
0.371 |
|
2020 |
Frey B, AlOkda A, Jackson MP, Riguet N, Duce JA, Lashuel HA. Monitoring alpha-synuclein oligomerization and aggregation using bimolecular fluorescence complementation assays: what you see is not always what you get. Journal of Neurochemistry. PMID 32772367 DOI: 10.1111/Jnc.15147 |
0.377 |
|
2020 |
Hegde RN, Chiki A, Petricca L, Martufi P, Arbez N, Mouchiroud L, Auwerx J, Landles C, Bates GP, Singh-Bains MK, Dragunow M, Curtis MA, Faull RL, Ross CA, Caricasole A, ... Lashuel HA, et al. TBK1 phosphorylates mutant Huntingtin and suppresses its aggregation and toxicity in Huntington's disease models. The Embo Journal. e104671. PMID 32757223 DOI: 10.15252/Embj.2020104671 |
0.39 |
|
2020 |
Ke PC, Zhou R, Serpell LC, Riek R, Knowles TPJ, Lashuel HA, Gazit E, Hamley IW, Davis TP, Fändrich M, Otzen DE, Chapman MR, Dobson CM, Eisenberg DS, Mezzenga R. Half a century of amyloids: past, present and future. Chemical Society Reviews. PMID 32632432 DOI: 10.1039/C9Cs00199A |
0.402 |
|
2020 |
Stephens AD, Zacharopoulou M, Moons R, Fusco G, Seetaloo N, Chiki A, Woodhams PJ, Mela I, Lashuel HA, Phillips JJ, De Simone A, Sobott F, Schierle GSK. Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity. Nature Communications. 11: 2820. PMID 32499486 DOI: 10.1038/S41467-020-16564-3 |
0.423 |
|
2020 |
Ait-Bouziad N, Chiki A, Limorenko G, Xiao S, Eliezer D, Lashuel HA. Phosphorylation of the overlooked tyrosine 310 regulates the structure, aggregation, and microtubule- and lipid-binding properties of Tau. The Journal of Biological Chemistry. PMID 32341125 DOI: 10.1074/Jbc.Ra119.012517 |
0.392 |
|
2020 |
Lashuel HA. Do Lewy bodies contain alpha-synuclein fibrils? and Does it matter? A brief history and critical analysis of recent reports. Neurobiology of Disease. 104876. PMID 32339655 DOI: 10.1016/J.Nbd.2020.104876 |
0.438 |
|
2020 |
Cendrowska U, Silva PJ, Ait-Bouziad N, Müller M, Guven ZP, Vieweg S, Chiki A, Radamaker L, Kumar ST, Fändrich M, Tavanti F, Menziani MC, Alexander-Katz A, Stellacci F, Lashuel HA. Unraveling the complexity of amyloid polymorphism using gold nanoparticles and cryo-EM. Proceedings of the National Academy of Sciences of the United States of America. PMID 32161130 DOI: 10.1073/Pnas.1916176117 |
0.425 |
|
2020 |
Mahul-Mellier AL, Burtscher J, Maharjan N, Weerens L, Croisier M, Kuttler F, Leleu M, Knott GW, Lashuel HA. The process of Lewy body formation, rather than simply α-synuclein fibrillization, is one of the major drivers of neurodegeneration. Proceedings of the National Academy of Sciences of the United States of America. PMID 32075919 DOI: 10.1073/Pnas.1913904117 |
0.427 |
|
2020 |
Kumar ST, Donzelli S, Chiki A, Syed MMK, Lashuel HA. A simple, versatile and robust centrifugation-based filtration protocol for the isolation and quantification of α-synuclein monomers, oligomers and fibrils: Towards improving experimental reproducibility in α-synuclein research. Journal of Neurochemistry. PMID 31925956 DOI: 10.1111/Jnc.14955 |
0.467 |
|
2019 |
Haj-Yahya M, Gopinath P, Rajasekhar K, Mirbaha H, Diamond MI, Lashuel HA. Site-specific hyperphosphorylation inhibits, rather than promotes, tau fibrillization, seeding capacity and its microtubule binding. Angewandte Chemie (International Ed. in English). PMID 31863676 DOI: 10.1002/Anie.201913001 |
0.381 |
|
2019 |
Cariulo C, Verani M, Martufi P, Ingenito R, Finotto M, Deguire SM, Lavery DJ, Toledo-Sherman L, Lee R, Doherty EM, Vogt TF, Dominguez C, Lashuel HA, Petricca L, Caricasole A. Ultrasensitive quantitative measurement of huntingtin phosphorylation at residue S13. Biochemical and Biophysical Research Communications. PMID 31677786 DOI: 10.1016/J.Bbrc.2019.09.097 |
0.391 |
|
2019 |
Yalinca H, Gehin CJC, Oleinikovas V, Lashuel HA, Gervasio FL, Pastore A. The Role of Post-translational Modifications on the Energy Landscape of Huntingtin N-Terminus. Frontiers in Molecular Biosciences. 6: 95. PMID 31632982 DOI: 10.3389/Fmolb.2019.00095 |
0.418 |
|
2019 |
Burtscher J, Copin JC, Rodrigues J, Kumar ST, Chiki A, Guillot de Suduiraut I, Sandi C, Lashuel HA. Chronic corticosterone aggravates behavioral and neuronal symptomatology in a mouse model of alpha-synuclein pathology. Neurobiology of Aging. 83: 11-20. PMID 31585362 DOI: 10.1016/J.Neurobiolaging.2019.08.007 |
0.339 |
|
2019 |
Cariulo C, Martufi P, Verani M, Azzollini L, Bruni G, Weiss A, Deguire SM, Lashuel HA, Scaricamazza E, Sancesario GM, Schirinzi T, Mercuri NB, Sancesario G, Caricasole A, Petricca L. Phospho-S129 Alpha-Synuclein Is Present in Human Plasma but Not in Cerebrospinal Fluid as Determined by an Ultrasensitive Immunoassay. Frontiers in Neuroscience. 13: 889. PMID 31507364 DOI: 10.3389/Fnins.2019.00889 |
0.339 |
|
2019 |
Levine PM, Galesic A, Balana AT, Mahul-Mellier AL, Navarro MX, De Leon CA, Lashuel HA, Pratt MR. α-Synuclein O-GlcNAcylation alters aggregation and toxicity, revealing certain residues as potential inhibitors of Parkinson's disease. Proceedings of the National Academy of Sciences of the United States of America. PMID 30651314 DOI: 10.1073/Pnas.1808845116 |
0.392 |
|
2018 |
Ellmer D, Brehs M, Haj-Yahya M, Lashuel HA, Becker CFW. Single posttranslational modifications in the central repeat domains of Tau4 impact its aggregation and tubulin binding. Angewandte Chemie (International Ed. in English). PMID 30549369 DOI: 10.1002/Anie.201805238 |
0.427 |
|
2018 |
Deguire SM, Ruggeri FS, Fares MB, Chiki A, Cendrowska U, Dietler G, Lashuel HA. N-terminal Huntingtin (Htt) phosphorylation is a molecular switch regulating Htt aggregation, helical conformation, internalization, and nuclear targeting. The Journal of Biological Chemistry. PMID 30185623 DOI: 10.1074/Jbc.Ra118.004621 |
0.391 |
|
2018 |
Mollenhauer B, DuBois BF, Drake D, Duong J, Blennow K, El-Agnaf O, Shaw LM, Masucci J, Taylor P, Umek RM, Dunty IM, Smith CL, Stoops E, Vanderstichele H, Schmid AW, ... ... Lashuel HA, et al. Antibody-based methods for the measurement of α-synuclein concentration in human cerebrospinal fluid - method comparison and round robin study. Journal of Neurochemistry. PMID 30125936 DOI: 10.1111/Jnc.14569 |
0.325 |
|
2018 |
Reif A, Chiki A, Ricci J, Lashuel HA. Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy. Journal of Visualized Experiments : Jove. PMID 30010666 DOI: 10.3791/57506 |
0.399 |
|
2018 |
Ruggeri FS, Benedetti F, Knowles TPJ, Lashuel HA, Sekatskii S, Dietler G. Identification and nanomechanical characterization of the fundamental single-strand protofilaments of amyloid α-synuclein fibrils. Proceedings of the National Academy of Sciences of the United States of America. PMID 29941606 DOI: 10.1073/Pnas.1721220115 |
0.443 |
|
2018 |
Etezadi D, Warner JB, Lashuel HA, Altug H. Real-time in-situ secondary structure analysis of protein monolayer with mid-infrared plasmonic nanoantennas. Acs Sensors. PMID 29845861 DOI: 10.1021/Acssensors.8B00115 |
0.386 |
|
2018 |
Haj-Yahya M, Lashuel HA. 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. Journal of the American Chemical Society. PMID 29684271 DOI: 10.1021/Jacs.8B02668 |
0.449 |
|
2018 |
El Turk F, De Genst E, Guilliams T, Fauvet B, Hejjaoui M, Di Trani J, Chiki A, Mittermaier A, Vendruscolo M, Lashuel HA, Dobson CM. Exploring the role of post-translational modifications in regulating α-synuclein interactions by studying the effects of phosphorylation on nanobody binding. Protein Science : a Publication of the Protein Society. PMID 29603451 DOI: 10.1002/Pro.3412 |
0.387 |
|
2017 |
Etezadi D, Warner Iv JB, Ruggeri FS, Dietler G, Lashuel HA, Altug H. Nanoplasmonic mid-infrared biosensor for protein secondary structure detection. Light, Science & Applications. 6: e17029. PMID 30167280 DOI: 10.1038/Lsa.2017.29 |
0.385 |
|
2017 |
Ait-Bouziad N, Lv G, Mahul-Mellier AL, Xiao S, Zorludemir G, Eliezer D, Walz T, Lashuel HA. Discovery and characterization of stable and toxic Tau/phospholipid oligomeric complexes. Nature Communications. 8: 1678. PMID 29162800 DOI: 10.1038/S41467-017-01575-4 |
0.426 |
|
2017 |
Cariulo C, Azzollini L, Verani M, Martufi P, Boggio R, Chiki A, Deguire SM, Cherubini M, Gines S, Marsh JL, Conforti P, Cattaneo E, Santimone I, Squitieri F, Lashuel HA, et al. Phosphorylation of huntingtin at residue T3 is decreased in Huntington's disease and modulates mutant huntingtin protein conformation. Proceedings of the National Academy of Sciences of the United States of America. PMID 29162692 DOI: 10.1073/Pnas.1705372114 |
0.413 |
|
2017 |
Warner JB, Ruff K, Tan PS, Lemke EA, Pappu RV, Lashuel HA. Monomeric huntingtin exon 1 has similar overall structural features for wild type and pathological polyglutamine lengths. Journal of the American Chemical Society. PMID 28937758 DOI: 10.1021/Jacs.7B06659 |
0.38 |
|
2017 |
Ruggeri FS, Mahul-Mellier AL, Kasas S, Lashuel HA, Longo G, Dietler G. Amyloid single-cell cytotoxicity assays by nanomotion detection. Cell Death Discovery. 3: 17053. PMID 28845298 DOI: 10.1038/Cddiscovery.2017.53 |
0.41 |
|
2017 |
Mollenhauer B, Batrla R, El-Agnaf O, Galasko DR, Lashuel HA, Merchant KM, Shaw LM, Selkoe DJ, Umek R, Vanderstichele H, Zetterberg H, Zhang J, Caspell-Garcia C, Coffey C, Hutten SJ, et al. A user's guide for α-synuclein biomarker studies in biological fluids: Perianalytical considerations. Movement Disorders : Official Journal of the Movement Disorder Society. PMID 28734051 DOI: 10.1002/Mds.27090 |
0.353 |
|
2017 |
Daldin M, Fodale V, Cariulo C, Azzollini L, Verani M, Martufi P, Spiezia MC, Deguire SM, Cherubini M, Macdonald D, Weiss A, Bresciani A, Vonsattel JG, Petricca L, Marsh JL, ... ... Lashuel HA, et al. Polyglutamine expansion affects huntingtin conformation in multiple Huntington's disease models. Scientific Reports. 7: 5070. PMID 28698602 DOI: 10.1038/S41598-017-05336-7 |
0.399 |
|
2017 |
Vicente Miranda H, Szego ÉM, Oliveira LM, Breda C, Darendelioglu E, de Oliveira RM, Ferreira DG, Gomes MA, Rott R, Oliveira M, Munari F, Enguita FJ, Simões T, Rodrigues EF, Heinrich M, ... ... Lashuel HA, et al. Glycation potentiates α-synuclein-associated neurodegeneration in synucleinopathies. Brain : a Journal of Neurology. PMID 28398476 DOI: 10.1093/Brain/Awx056 |
0.404 |
|
2017 |
Chiki A, DeGuire SM, Ruggeri FS, Sanfelice D, Ansaloni A, Wang ZM, Cendrowska U, Burai R, Vieweg S, Pastore A, Dietler G, Lashuel HA. Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation-Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6. Angewandte Chemie (International Ed. in English). PMID 28334491 DOI: 10.1002/Anie.201611750 |
0.354 |
|
2017 |
de Oliveira RM, Vicente Miranda H, Francelle L, Pinho R, Szegö ÉM, Martinho R, Munari F, Lázaro DF, Moniot S, Guerreiro P, Fonseca L, Marijanovic Z, Antas P, Gerhardt E, Enguita FJ, ... ... Lashuel HA, et al. The mechanism of sirtuin 2-mediated exacerbation of alpha-synuclein toxicity in models of Parkinson disease. Plos Biology. 15: e2000374. PMID 28257421 DOI: 10.1371/Journal.Pbio.2000374 |
0.415 |
|
2016 |
Awad L, Jejelava N, Burai R, Lashuel HA. A novel caged-glutamine derivative as a tool to control the assembly of glutamine-containing amyloidogenic peptides. Chembiochem : a European Journal of Chemical Biology. PMID 27788286 DOI: 10.1002/Cbic.201600474 |
0.301 |
|
2016 |
Ruggeri FS, Vieweg S, Cendrowska U, Longo G, Chiki A, Lashuel HA, Dietler G. Nanoscale studies link amyloid maturity with polyglutamine diseases onset. Scientific Reports. 6: 31155. PMID 27499269 DOI: 10.1038/Srep31155 |
0.471 |
|
2016 |
Dikiy I, Fauvet B, Jovičić A, Mahul-Mellier AL, Desobry C, El-Turk F, Gitler AD, Lashuel HA, Eliezer D. Semisynthetic and in vitro phosphorylation of alpha-synuclein at Y39 promotes functional partly-helical membrane-bound states resembling those induced by PD mutations. Acs Chemical Biology. PMID 27356045 DOI: 10.1021/Acschembio.6B00539 |
0.362 |
|
2016 |
Vieweg S, Ansaloni A, Wang ZM, Warner JB, Lashuel HA. An Intein-based Strategy for the Production of Tag-free Huntingtin Exon 1 Proteins enables New Insights into the PolyQ Dependence of Httex1 Aggregation and Fibril Formation. The Journal of Biological Chemistry. PMID 27002149 DOI: 10.1074/Jbc.M116.713982 |
0.432 |
|
2016 |
Fares MB, Maco B, Oueslati A, Rockenstein E, Ninkina N, Buchman VL, Masliah E, Lashuel HA. Induction of de novo α-synuclein fibrillization in a neuronal model for Parkinson's disease. Proceedings of the National Academy of Sciences of the United States of America. PMID 26839406 DOI: 10.1073/Pnas.1512876113 |
0.407 |
|
2016 |
Fauvet B, Lashuel HA. Semisynthesis and Enzymatic Preparation of Post-translationally Modified α-Synuclein. Methods in Molecular Biology (Clifton, N.J.). 1345: 3-20. PMID 26453202 DOI: 10.1007/978-1-4939-2978-8_1 |
0.419 |
|
2015 |
Adamcik J, Sánchez-Ferrer A, Ait-Bouziad N, Reynolds NP, Lashuel HA, Mezzenga R. Microtubule-Binding R3 Fragment from Tau Self-Assembles into Giant Multistranded Amyloid Ribbons. Angewandte Chemie (International Ed. in English). PMID 26636567 DOI: 10.1002/Anie.201508968 |
0.44 |
|
2015 |
Oueslati A, Lovisa B, Perrin J, Wagnières G, van den Bergh H, Tardy Y, Lashuel HA. Photobiomodulation Suppresses Alpha-Synuclein-Induced Toxicity in an AAV-Based Rat Genetic Model of Parkinson's Disease. Plos One. 10: e0140880. PMID 26484876 DOI: 10.1371/Journal.Pone.0140880 |
0.325 |
|
2015 |
Mahul-Mellier AL, Vercruysse F, Maco B, Ait-Bouziad N, De Roo M, Muller D, Lashuel HA. Fibril growth and seeding capacity play key roles in α-synuclein-mediated apoptotic cell death. Cell Death and Differentiation. PMID 26138444 DOI: 10.1038/Cdd.2015.79 |
0.39 |
|
2015 |
Bustamante MB, Ansaloni A, Pedersen JF, Azzollini L, Cariulo C, Wang ZM, Petricca L, Verani M, Puglisi F, Park H, Lashuel H, Caricasole A. Detection of huntingtin exon 1 phosphorylation by Phos-Tag SDS-PAGE: Predominant phosphorylation on Threonine 3 and regulation by IKKβ. Biochemical and Biophysical Research Communications. PMID 26106822 DOI: 10.1016/J.Bbrc.2015.06.116 |
0.381 |
|
2015 |
Droste P, Frenzel A, Steinwand M, Pelat T, Thullier P, Hust M, Lashuel H, Dübel S. Structural differences of amyloid-β fibrils revealed by antibodies from phage display. Bmc Biotechnology. 15: 57. PMID 26084577 DOI: 10.1186/s12896-015-0146-8 |
0.341 |
|
2015 |
Burai R, Ait-Bouziad N, Chiki A, Lashuel HA. Elucidating the Role of Site-Specific Nitration of α-Synuclein in the Pathogenesis of Parkinson's Disease via Protein Semisynthesis and Mutagenesis. Journal of the American Chemical Society. 137: 5041-52. PMID 25768729 DOI: 10.1021/Ja5131726 |
0.423 |
|
2015 |
Mbefo MK, Fares MB, Paleologou K, Oueslati A, Yin G, Tenreiro S, Pinto M, Outeiro T, Zweckstetter M, Masliah E, Lashuel HA. Parkinson disease mutant E46K enhances α-synuclein phosphorylation in mammalian cell lines, in yeast, and in vivo. The Journal of Biological Chemistry. 290: 9412-27. PMID 25657004 DOI: 10.1074/Jbc.M114.610774 |
0.332 |
|
2015 |
Ruggeri FS, Adamcik J, Jeong JS, Lashuel HA, Mezzenga R, Dietler G. Influence of the β-sheet content on the mechanical properties of aggregates during amyloid fibrillization. Angewandte Chemie (International Ed. in English). 54: 2462-6. PMID 25588987 DOI: 10.1002/Anie.201409050 |
0.452 |
|
2015 |
Dhungel N, Eleuteri S, Li LB, Kramer NJ, Chartron JW, Spencer B, Kosberg K, Fields JA, Stafa K, Adame A, Lashuel H, Frydman J, Shen K, Masliah E, Gitler AD. Parkinson's disease genes VPS35 and EIF4G1 interact genetically and converge on α-synuclein. Neuron. 85: 76-87. PMID 25533483 DOI: 10.1016/J.Neuron.2014.11.027 |
0.324 |
|
2015 |
Eleuteri S, Di Giovanni S, Rockenstein E, Mante M, Adame A, Trejo M, Wrasidlo W, Wu F, Fraering PC, Masliah E, Lashuel HA. Novel therapeutic strategy for neurodegeneration by blocking Aβ seeding mediated aggregation in models of Alzheimer's disease. Neurobiology of Disease. 74: 144-57. PMID 25173807 DOI: 10.1016/J.Nbd.2014.08.017 |
0.424 |
|
2015 |
Droste P, Frenzel A, Steinwand M, Pelat T, Thullier P, Hust M, Lashuel H, Dübel S. Structural differences of amyloid-β fibrils revealed by antibodies from phage display Bmc Biotechnology. 15. DOI: 10.1186/S12896-015-0146-8 |
0.434 |
|
2015 |
Dhungel N, Eleuteri S, Li LB, Kramer NJ, Chartron JW, Spencer B, Kosberg K, Fields JA, Stafa K, Adame A, Lashuel H, Frydman J, Shen K, Masliah E, Gitler AD. Erratum to Parkinson's Disease Genes VPS35 and EIF4G1 Interact Genetically and Converge on α-Synuclein [(Neuron 85, (2015) 76-87] Neuron. 85. DOI: 10.1016/J.Neuron.2015.01.022 |
0.311 |
|
2014 |
Khalaf O, Fauvet B, Oueslati A, Dikiy I, Mahul-Mellier AL, Ruggeri FS, Mbefo MK, Vercruysse F, Dietler G, Lee SJ, Eliezer D, Lashuel HA. The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity. The Journal of Biological Chemistry. 289: 21856-76. PMID 24936070 DOI: 10.1074/Jbc.M114.553297 |
0.365 |
|
2014 |
Fares MB, Ait-Bouziad N, Dikiy I, Mbefo MK, JoviÄić A, Kiely A, Holton JL, Lee SJ, Gitler AD, Eliezer D, Lashuel HA. The novel Parkinson's disease linked mutation G51D attenuates in vitro aggregation and membrane binding of α-synuclein, and enhances its secretion and nuclear localization in cells. Human Molecular Genetics. 23: 4491-509. PMID 24728187 DOI: 10.1093/Hmg/Ddu165 |
0.387 |
|
2014 |
Ansaloni A, Wang ZM, Jeong JS, Ruggeri FS, Dietler G, Lashuel HA. 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. Angewandte Chemie (International Ed. in English). 53: 1928-33. PMID 24446188 DOI: 10.1002/Anie.201307510 |
0.423 |
|
2014 |
Mahul-Mellier AL, Fauvet B, Gysbers A, Dikiy I, Oueslati A, Georgeon S, Lamontanara AJ, Bisquertt A, Eliezer D, Masliah E, Halliday G, Hantschel O, Lashuel HA. c-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson's disease. Human Molecular Genetics. 23: 2858-79. PMID 24412932 DOI: 10.1093/Hmg/Ddt674 |
0.357 |
|
2014 |
Lashuel HA, Eleuteri S, Di Giovanni S, Rockenstein E, Mante M, Adame A, Trejo M, Wu F, Fraering PC, Masliah E. Novel Mechanism-Based Inhibitors of Aβ Aggregation and Toxicity Neurobiology of Aging. 35: 720-721. DOI: 10.1016/J.Neurobiolaging.2013.10.057 |
0.378 |
|
2013 |
Fournier M, Roux A, Garrigue J, Muriel MP, Blanche P, Lashuel HA, Anderson JP, Barbour R, Huang J, du Montcel ST, Brice A, Corti O. Parkin depletion delays motor decline dose-dependently without overtly affecting neuropathology in α-synuclein transgenic mice. Bmc Neuroscience. 14: 135. PMID 24192137 DOI: 10.1186/1471-2202-14-135 |
0.385 |
|
2013 |
Santi S, Musi V, Descrovi E, Paeder V, Di Francesco J, Hvozdara L, van der Wal P, Lashuel HA, Pastore A, Neier R, Herzig HP. Real-time amyloid aggregation monitoring with a photonic crystal-based approach. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 14: 3476-82. PMID 24105966 DOI: 10.1002/Cphc.201300633 |
0.427 |
|
2013 |
Haj-Yahya M, Fauvet B, Herman-Bachinsky Y, Hejjaoui M, Bavikar SN, Karthikeyan SV, Ciechanover A, Lashuel HA, Brik A. Synthetic polyubiquitinated α-Synuclein reveals important insights into the roles of the ubiquitin chain in regulating its pathophysiology. Proceedings of the National Academy of Sciences of the United States of America. 110: 17726-31. PMID 24043770 DOI: 10.1073/Pnas.1315654110 |
0.373 |
|
2013 |
Fauvet B, Butterfield SM, Fuks J, Brik A, Lashuel HA. One-pot total chemical synthesis of human α-synuclein. Chemical Communications (Cambridge, England). 49: 9254-6. PMID 23995579 DOI: 10.1039/C3Cc45353G |
0.37 |
|
2013 |
Oueslati A, Schneider BL, Aebischer P, Lashuel HA. Polo-like kinase 2 regulates selective autophagic α-synuclein clearance and suppresses its toxicity in vivo. Proceedings of the National Academy of Sciences of the United States of America. 110: E3945-54. PMID 23983262 DOI: 10.1073/Pnas.1309991110 |
0.359 |
|
2013 |
Schmid AW, Fauvet B, Moniatte M, Lashuel HA. Alpha-synuclein post-translational modifications as potential biomarkers for Parkinson disease and other synucleinopathies. Molecular & Cellular Proteomics : McP. 12: 3543-58. PMID 23966418 DOI: 10.1074/Mcp.R113.032730 |
0.4 |
|
2013 |
Schildknecht S, Gerding HR, Karreman C, Drescher M, Lashuel HA, Outeiro TF, Di Monte DA, Leist M. Oxidative and nitrative alpha-synuclein modifications and proteostatic stress: implications for disease mechanisms and interventions in synucleinopathies. Journal of Neurochemistry. 125: 491-511. PMID 23452040 DOI: 10.1111/Jnc.12226 |
0.386 |
|
2013 |
Jeong JS, Ansaloni A, Mezzenga R, Lashuel HA, Dietler G. Novel mechanistic insight into the molecular basis of amyloid polymorphism and secondary nucleation during amyloid formation. Journal of Molecular Biology. 425: 1765-81. PMID 23415897 DOI: 10.1016/J.Jmb.2013.02.005 |
0.474 |
|
2013 |
Lashuel HA, Overk CR, Oueslati A, Masliah E. The many faces of α-synuclein: from structure and toxicity to therapeutic target. Nature Reviews. Neuroscience. 14: 38-48. PMID 23254192 DOI: 10.1038/Nrn3406 |
0.427 |
|
2013 |
Wang ZM, Lashuel HA. Discovery of a novel aggregation domain in the huntingtin protein: implications for the mechanisms of Htt aggregation and toxicity. Angewandte Chemie (International Ed. in English). 52: 562-7. PMID 23148019 DOI: 10.1002/Anie.201206561 |
0.384 |
|
2013 |
Santi S, Musi V, Descrovi E, Paeder V, Di Francesco J, Hvozdara L, van der Wal P, Lashuel HA, Pastore A, Neier R, Herzig HP. Cover Picture: Real-time Amyloid Aggregation Monitoring with a Photonic Crystal-based Approach (ChemPhysChem 15/2013) Chemphyschem. 14: 3421-3421. DOI: 10.1002/Cphc.201390071 |
0.327 |
|
2012 |
El-Turk F, Fauvet B, Ashrafi A, Ouertatani-Sakouhi H, Cho MK, Neri M, Cascella M, Rothlisberger U, Pojer F, Zweckstetter M, Lashuel H. Characterization of Molecular Determinants of the Conformational Stability of Macrophage Migration Inhibitory Factor: Leucine 46 Hydrophobic Pocket Plos One. 7. PMID 23028743 DOI: 10.1371/Journal.Pone.0045024 |
0.358 |
|
2012 |
Kroth H, Ansaloni A, Varisco Y, Jan A, Sreenivasachary N, Rezaei-Ghaleh N, Giriens V, Lohmann S, López-Deber MP, Adolfsson O, Pihlgren M, Paganetti P, Froestl W, Nagel-Steger L, Willbold D, ... ... Lashuel HA, et al. Discovery and structure activity relationship of small molecule inhibitors of toxic β-amyloid-42 fibril formation. The Journal of Biological Chemistry. 287: 34786-800. PMID 22891248 DOI: 10.1074/Jbc.M112.357665 |
0.42 |
|
2012 |
Choi HS, Liew H, Jang A, Kim YM, Lashuel H, Suh YH. Phosphorylation of α-synuclein is crucial in compensating for proteasomal dysfunction. Biochemical and Biophysical Research Communications. 424: 597-603. PMID 22776201 DOI: 10.1016/J.Bbrc.2012.06.159 |
0.361 |
|
2012 |
Fauvet B, Fares MB, Samuel F, Dikiy I, Tandon A, Eliezer D, Lashuel HA. Characterization of semisynthetic and naturally Nα-acetylated α-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of α-synuclein. The Journal of Biological Chemistry. 287: 28243-62. PMID 22718772 DOI: 10.1074/Jbc.M112.383711 |
0.382 |
|
2012 |
Adamcik J, Lara C, Usov I, Jeong JS, Ruggeri FS, Dietler G, Lashuel HA, Hamley IW, Mezzenga R. Measurement of intrinsic properties of amyloid fibrils by the peak force QNM method. Nanoscale. 4: 4426-9. PMID 22688679 DOI: 10.1039/C2Nr30768E |
0.398 |
|
2012 |
Yang B, Sun X, Lashuel H, Zhang Y. Reactive oxidative species enhance amyloid toxicity in APP/PS1 mouse neurons Neuroscience Bulletin. 28: 233-239. PMID 22622822 DOI: 10.1007/S12264-012-1239-1 |
0.378 |
|
2012 |
Jan A, Lashuel HA. Establishing the links between Aβ aggregation and cytotoxicity in vitro using biophysical approaches. Methods in Molecular Biology (Clifton, N.J.). 849: 227-43. PMID 22528094 DOI: 10.1007/978-1-61779-551-0_16 |
0.435 |
|
2012 |
Butterfield S, Hejjaoui M, Fauvet B, Awad L, Lashuel HA. Chemical strategies for controlling protein folding and elucidating the molecular mechanisms of amyloid formation and toxicity. Journal of Molecular Biology. 421: 204-36. PMID 22342932 DOI: 10.1016/J.Jmb.2012.01.051 |
0.46 |
|
2012 |
Hejjaoui M, Butterfield S, Fauvet B, Vercruysse F, Cui J, Dikiy I, Prudent M, Olschewski D, Zhang Y, Eliezer D, Lashuel HA. Elucidating the role of C-terminal post-translational modifications using protein semisynthesis strategies: α-synuclein phosphorylation at tyrosine 125. Journal of the American Chemical Society. 134: 5196-210. PMID 22339654 DOI: 10.1021/Ja210866J |
0.404 |
|
2012 |
Fauvet B, Mbefo MK, Fares MB, Desobry C, Michael S, Ardah MT, Tsika E, Coune P, Prudent M, Lion N, Eliezer D, Moore DJ, Schneider B, Aebischer P, El-Agnaf OM, ... ... Lashuel HA, et al. α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer. The Journal of Biological Chemistry. 287: 15345-64. PMID 22315227 DOI: 10.1074/Jbc.M111.318949 |
0.35 |
|
2012 |
Oueslati A, Paleologou KE, Schneider BL, Aebischer P, Lashuel HA. 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. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 32: 1536-44. PMID 22302797 DOI: 10.1523/Jneurosci.3784-11.2012 |
0.426 |
|
2011 |
Lu Y, Prudent M, Fauvet B, Lashuel HA, Girault HH. Phosphorylation of α-Synuclein at Y125 and S129 alters its metal binding properties: implications for understanding the role of α-Synuclein in the pathogenesis of Parkinson's Disease and related disorders. Acs Chemical Neuroscience. 2: 667-75. PMID 22860160 DOI: 10.1021/Cn200074D |
0.318 |
|
2011 |
Siman P, Blatt O, Moyal T, Danieli T, Lebendiker M, Lashuel HA, Friedler A, Brik A. Chemical synthesis and expression of the HIV-1 Rev protein. Chembiochem : a European Journal of Chemical Biology. 12: 1097-104. PMID 21488138 DOI: 10.1002/Cbic.201100033 |
0.312 |
|
2011 |
Jan A, Adolfsson O, Allaman I, Buccarello AL, Magistretti PJ, Pfeifer A, Muhs A, Lashuel HA. Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species. The Journal of Biological Chemistry. 286: 8585-96. PMID 21156804 DOI: 10.1074/Jbc.M110.172411 |
0.453 |
|
2011 |
Hejjaoui M, Haj-Yahya M, Kumar KS, Brik A, Lashuel HA. Towards elucidation of the role of ubiquitination in the pathogenesis of Parkinson's disease with semisynthetic ubiquitinated α-synuclein. Angewandte Chemie (International Ed. in English). 50: 405-9. PMID 21154793 DOI: 10.1002/Anie.201005546 |
0.404 |
|
2011 |
Braga CA, Follmer C, Palhano FL, Khattar E, Freitas MS, Romão L, Di Giovanni S, Lashuel HA, Silva JL, Foguel D. The anti-Parkinsonian drug selegiline delays the nucleation phase of α-synuclein aggregation leading to the formation of nontoxic species. Journal of Molecular Biology. 405: 254-73. PMID 21050861 DOI: 10.1016/J.Jmb.2010.10.027 |
0.717 |
|
2010 |
Khandelwal PJ, Dumanis SB, Feng LR, Maguire-Zeiss K, Rebeck G, Lashuel HA, Moussa CE. Parkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer model. Molecular Neurodegeneration. 5: 47. PMID 21050448 DOI: 10.1186/1750-1326-5-47 |
0.374 |
|
2010 |
Hinault MP, Cuendet AF, Mattoo RU, Mensi M, Dietler G, Lashuel HA, Goloubinoff P. Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones. The Journal of Biological Chemistry. 285: 38173-82. PMID 20847048 DOI: 10.1074/Jbc.M110.127753 |
0.427 |
|
2010 |
Oueslati A, Fournier M, Lashuel HA. Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: implications for Parkinson's disease pathogenesis and therapies. Progress in Brain Research. 183: 115-45. PMID 20696318 DOI: 10.1016/S0079-6123(10)83007-9 |
0.424 |
|
2010 |
El Turk F, Fauvet B, Ouertatani-Sakouhi H, Lugari A, Betzi S, Roche P, Morelli X, Lashuel HA. An integrative in silico methodology for the identification of modulators of macrophage migration inhibitory factor (MIF) tautomerase activity. Bioorganic & Medicinal Chemistry. 18: 5425-40. PMID 20639113 DOI: 10.1016/J.Bmc.2010.05.010 |
0.301 |
|
2010 |
Butterfield SM, Lashuel HA. Amyloidogenic protein-membrane interactions: mechanistic insight from model systems. Angewandte Chemie (International Ed. in English). 49: 5628-54. PMID 20623810 DOI: 10.1002/Anie.200906670 |
0.361 |
|
2010 |
Jan A, Hartley DM, Lashuel HA. Preparation and characterization of toxic Abeta aggregates for structural and functional studies in Alzheimer's disease research. Nature Protocols. 5: 1186-209. PMID 20539293 DOI: 10.1038/Nprot.2010.72 |
0.453 |
|
2010 |
Ouertatani-Sakouhi H, El-Turk F, Fauvet B, Cho MK, Pinar Karpinar D, Le Roy D, Dewor M, Roger T, Bernhagen J, Calandra T, Zweckstetter M, Lashuel HA. Identification and characterization of novel classes of macrophage migration inhibitory factor (MIF) inhibitors with distinct mechanisms of action. The Journal of Biological Chemistry. 285: 26581-98. PMID 20516071 DOI: 10.1074/Jbc.M110.113951 |
0.31 |
|
2010 |
Allaman I, Gavillet M, Bélanger M, Laroche T, Viertl D, Lashuel HA, Magistretti PJ. Amyloid-beta aggregates cause alterations of astrocytic metabolic phenotype: impact on neuronal viability. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 30: 3326-38. PMID 20203192 DOI: 10.1523/Jneurosci.5098-09.2010 |
0.358 |
|
2010 |
Paleologou KE, Oueslati A, Shakked G, Rospigliosi CC, Kim HY, Lamberto GR, Fernandez CO, Schmid A, Chegini F, Gai WP, Chiappe D, Moniatte M, Schneider BL, Aebischer P, Eliezer D, ... ... Lashuel HA, et al. Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 30: 3184-98. PMID 20203178 DOI: 10.1523/Jneurosci.5922-09.2010 |
0.379 |
|
2010 |
Di Giovanni S, Eleuteri S, Paleologou KE, Yin G, Zweckstetter M, Carrupt PA, Lashuel HA. Entacapone and tolcapone, two catechol O-methyltransferase inhibitors, block fibril formation of alpha-synuclein and beta-amyloid and protect against amyloid-induced toxicity. The Journal of Biological Chemistry. 285: 14941-54. PMID 20150427 DOI: 10.1074/Jbc.M109.080390 |
0.446 |
|
2010 |
Mbefo MK, Paleologou KE, Boucharaba A, Oueslati A, Schell H, Fournier M, Olschewski D, Yin G, Zweckstetter M, Masliah E, Kahle PJ, Hirling H, Lashuel HA. Phosphorylation of synucleins by members of the Polo-like kinase family. The Journal of Biological Chemistry. 285: 2807-22. PMID 19889641 DOI: 10.1074/Jbc.M109.081950 |
0.352 |
|
2010 |
Grimminger-Marquardt V, Lashuel HA. Structure and function of the molecular chaperone Hsp104 from yeast. Biopolymers. 93: 252-76. PMID 19768774 DOI: 10.1002/Bip.21301 |
0.436 |
|
2010 |
Butterfield S, Lashuel H. Wechselwirkungen zwischen amyloidogenen Proteinen und Membranen: Modellsysteme liefern mechanistische Einblicke Angewandte Chemie. 122: 5760-5788. DOI: 10.1002/Ange.200906670 |
0.328 |
|
2009 |
Kim HY, Cho MK, Kumar A, Maier E, Siebenhaar C, Becker S, Fernandez CO, Lashuel HA, Benz R, Lange A, Zweckstetter M. Structural properties of pore-forming oligomers of alpha-synuclein. Journal of the American Chemical Society. 131: 17482-9. PMID 19888725 DOI: 10.1021/Ja9077599 |
0.443 |
|
2009 |
Ajish Kumar KS, Haj-Yahya M, Olschewski D, Lashuel HA, Brik A. Highly efficient and chemoselective peptide ubiquitylation. Angewandte Chemie (International Ed. in English). 48: 8090-4. PMID 19780082 DOI: 10.1002/Anie.200902936 |
0.322 |
|
2009 |
Ouertatani-Sakouhi H, El-Turk F, Fauvet B, Roger T, Le Roy D, Karpinar DP, Leng L, Bucala R, Zweckstetter M, Calandra T, Lashuel HA. A new class of isothiocyanate-based irreversible inhibitors of macrophage migration inhibitory factor. Biochemistry. 48: 9858-70. PMID 19737008 DOI: 10.1021/Bi900957E |
0.328 |
|
2009 |
Fournier M, Vitte J, Garrigue J, Langui D, Dullin JP, Saurini F, Hanoun N, Perez-Diaz F, Cornilleau F, Joubert C, Ardila-Osorio H, Traver S, Duchateau R, Goujet-Zalc C, Paleologou K, ... Lashuel HA, et al. Parkin deficiency delays motor decline and disease manifestation in a mouse model of synucleinopathy. Plos One. 4: e6629. PMID 19680561 DOI: 10.1371/Journal.Pone.0006629 |
0.355 |
|
2009 |
Lashuel HA, Pappu RV. Amyloids go genomic: insights regarding the sequence determinants of prion formation from genome-wide studies. Chembiochem : a European Journal of Chemical Biology. 10: 1951-4. PMID 19598186 DOI: 10.1002/Cbic.200900373 |
0.325 |
|
2009 |
Camus MS, Mimna R, Schmid A, Chandravarkar A, Tuchscherer G, Lashuel HA, Mutter M. Switch-peptides as folding precursors in self-assembling peptides and amyloid fibrillogenesis. Advances in Experimental Medicine and Biology. 611: 281-2. PMID 19400193 DOI: 10.1007/978-0-387-73657-0_126 |
0.303 |
|
2009 |
Rospigliosi CC, McClendon S, Schmid AW, Ramlall TF, Barré P, Lashuel HA, Eliezer D. E46K Parkinson's-linked mutation enhances C-terminal-to-N-terminal contacts in alpha-synuclein. Journal of Molecular Biology. 388: 1022-32. PMID 19345692 DOI: 10.1016/J.Jmb.2009.03.065 |
0.382 |
|
2009 |
Schmid AW, Chiappe D, Pignat V, Grimminger V, Hang I, Moniatte M, Lashuel HA. Dissecting the mechanisms of tissue transglutaminase-induced cross-linking of alpha-synuclein: implications for the pathogenesis of Parkinson disease. The Journal of Biological Chemistry. 284: 13128-42. PMID 19164286 DOI: 10.1074/Jbc.M809067200 |
0.359 |
|
2009 |
Lashuel HA. F3-02-05: The Role of post-translational modification (phosphorylation) in modulating alpha-synuclein, structure, aggregation and toxicity Alzheimer's & Dementia. 5: P124-P125. DOI: 10.1016/J.Jalz.2009.05.419 |
0.356 |
|
2008 |
Herrera FE, Chesi A, Paleologou KE, Schmid A, Munoz A, Vendruscolo M, Gustincich S, Lashuel HA, Carloni P. Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC region. Plos One. 3: e3394. PMID 18852892 DOI: 10.1371/Journal.Pone.0003394 |
0.385 |
|
2008 |
Arimon M, Grimminger V, Sanz F, Lashuel HA. Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of Abeta fibrils and protofibrils. Journal of Molecular Biology. 384: 1157-73. PMID 18851977 DOI: 10.1016/J.Jmb.2008.09.063 |
0.443 |
|
2008 |
El-Turk F, Cascella M, Ouertatani-Sakouhi H, Narayanan RL, Leng L, Bucala R, Zweckstetter M, Rothlisberger U, Lashuel HA. 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. Biochemistry. 47: 10740-56. PMID 18795803 DOI: 10.1021/Bi800603X |
0.335 |
|
2008 |
Lo Bianco C, Shorter J, Régulier E, Lashuel H, Iwatsubo T, Lindquist S, Aebischer P. Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease. The Journal of Clinical Investigation. 118: 3087-97. PMID 18704197 DOI: 10.1172/Jci35781 |
0.397 |
|
2008 |
Jan A, Gokce O, Luthi-Carter R, Lashuel HA. The ratio of monomeric to aggregated forms of Abeta40 and Abeta42 is an important determinant of amyloid-beta aggregation, fibrillogenesis, and toxicity. The Journal of Biological Chemistry. 283: 28176-89. PMID 18694930 DOI: 10.1074/Jbc.M803159200 |
0.384 |
|
2008 |
Camus MS, Dos Santos S, Chandravarkar A, Mandal B, Schmid AW, Tuchscherer G, Mutter M, Lashuel HA. Switch-peptides: design and characterization of controllable super-amyloid-forming host-guest peptides as tools for identifying anti-amyloid agents. Chembiochem : a European Journal of Chemical Biology. 9: 2104-12. PMID 18683159 DOI: 10.1002/Cbic.200800245 |
0.387 |
|
2008 |
Paleologou KE, Schmid AW, Rospigliosi CC, Kim HY, Lamberto GR, Fredenburg RA, Lansbury PT, Fernandez CO, Eliezer D, Zweckstetter M, Lashuel HA. Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein. The Journal of Biological Chemistry. 283: 16895-905. PMID 18343814 DOI: 10.1074/Jbc.M800747200 |
0.374 |
|
2007 |
Chafekar SM, Malda H, Merkx M, Meijer EW, Viertl D, Lashuel HA, Baas F, Scheper W. Branched KLVFF tetramers strongly potentiate inhibition of beta-amyloid aggregation. Chembiochem : a European Journal of Chemical Biology. 8: 1857-64. PMID 17763487 DOI: 10.1002/Cbic.200700338 |
0.418 |
|
2007 |
Fredenburg RA, Rospigliosi C, Meray RK, Kessler JC, Lashuel HA, Eliezer D, Lansbury PT. The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric states. Biochemistry. 46: 7107-18. PMID 17530780 DOI: 10.1021/Bi7000246 |
0.411 |
|
2007 |
Mimna R, Camus MS, Schmid A, Tuchscherer G, Lashuel HA, Mutter M. Disruption of amyloid-derived peptide assemblies through the controlled induction of a beta-sheet to alpha-helix transformation: application of the switch concept. Angewandte Chemie (International Ed. in English). 46: 2681-4. PMID 17330907 DOI: 10.1002/Anie.200603681 |
0.378 |
|
2007 |
Follmer C, Romão L, Einsiedler CM, Porto TC, Lara FA, Moncores M, Weissmüller G, Lashuel HA, Lansbury P, Neto VM, Silva JL, Foguel D. Dopamine affects the stability, hydration, and packing of protofibrils and fibrils of the wild type and variants of alpha-synuclein. Biochemistry. 46: 472-82. PMID 17209557 DOI: 10.1021/Bi061871+ |
0.372 |
|
2007 |
Tuchscherer G, Chandravarkar A, Camus MS, Bérard J, Murat K, Schmid A, Mimna R, Lashuel HA, Mutter M. Switch-peptides as folding precursors in self-assembling peptides and amyloid fibrillogenesis. Biopolymers. 88: 239-52. PMID 17206626 DOI: 10.1002/Bip.20663 |
0.362 |
|
2006 |
Lashuel HA, Hirling H. Rescuing defective vesicular trafficking protects against alpha-synuclein toxicity in cellular and animal models of Parkinson's disease. Acs Chemical Biology. 1: 420-4. PMID 17168518 DOI: 10.1021/Cb600331E |
0.386 |
|
2006 |
Lansbury PT, Lashuel HA. A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature. 443: 774-9. PMID 17051203 DOI: 10.1038/Nature05290 |
0.433 |
|
2006 |
Lashuel HA, Lansbury PT. Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? Quarterly Reviews of Biophysics. 39: 167-201. PMID 16978447 DOI: 10.1017/S0033583506004422 |
0.451 |
|
2006 |
Saucède L, Dos Santos S, Chandravarkar A, Mandal B, Mimna R, Murat K, Camus MS, Bérard J, Grouzmann E, Adrian M, Dubochet J, Lopez J, Lashuel H, Tuchscherer G, Mutter M. Switch-peptides: From conformational studies to Alzheimer's disease Chimia. 60: 199-202. DOI: 10.2533/000942906777674921 |
0.415 |
|
2005 |
Lashuel HA, Aljabari B, Sigurdsson EM, Metz CN, Leng L, Callaway DJ, Bucala R. Amyloid fibril formation by macrophage migration inhibitory factor. Biochemical and Biophysical Research Communications. 338: 973-80. PMID 16286092 DOI: 10.1016/J.Bbrc.2005.10.040 |
0.491 |
|
2005 |
Basha MR, Murali M, Siddiqi HK, Ghosal K, Siddiqi OK, Lashuel HA, Ge YW, Lahiri DK, Zawia NH. Lead (Pb) exposure and its effect on APP proteolysis and Abeta aggregation. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 19: 2083-4. PMID 16230335 DOI: 10.1096/Fj.05-4375Fje |
0.397 |
|
2005 |
Wang L, Lashuel HA, Colón W. From hexamer to amyloid: marginal stability of apolipoprotein SAA2.2 leads to in vitro fibril formation at physiological temperature. Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 12: 139-48. PMID 16194868 DOI: 10.1080/13506120500223084 |
0.715 |
|
2005 |
Lashuel HA. Membrane permeabilization: a common mechanism in protein-misfolding diseases. Science of Aging Knowledge Environment : Sage Ke. 2005: pe28. PMID 16186179 DOI: 10.1126/Sageke.2005.38.Pe28 |
0.459 |
|
2005 |
Lashuel HA, Wall JS. Molecular electron microscopy approaches to elucidating the mechanisms of protein fibrillogenesis. Methods in Molecular Biology (Clifton, N.J.). 299: 81-101. PMID 15980597 DOI: 10.1385/1-59259-874-9:081 |
0.416 |
|
2005 |
Lashuel HA, Grillo-Bosch D. In vitro preparation of prefibrillar intermediates of amyloid-beta and alpha-synuclein. Methods in Molecular Biology (Clifton, N.J.). 299: 19-33. PMID 15980593 DOI: 10.1385/1-59259-874-9:019 |
0.468 |
|
2005 |
Morikawa M, Fryer JD, Sullivan PM, Christopher EA, Wahrle SE, DeMattos RB, O'Dell MA, Fagan AM, Lashuel HA, Walz T, Asai K, Holtzman DM. Production and characterization of astrocyte-derived human apolipoprotein E isoforms from immortalized astrocytes and their interactions with amyloid-beta. Neurobiology of Disease. 19: 66-76. PMID 15837562 DOI: 10.1016/J.Nbd.2004.11.005 |
0.314 |
|
2005 |
Cox DL, Lashuel H, Lee KYC, Singh RRR. The materials science of protein aggregation Mrs Bulletin. 30: 452-457. DOI: 10.1557/Mrs2005.123 |
0.453 |
|
2004 |
Rochet JC, Outeiro TF, Conway KA, Ding TT, Volles MJ, Lashuel HA, Bieganski RM, Lindquist SL, Lansbury PT. Interactions among alpha-synuclein, dopamine, and biomembranes: some clues for understanding neurodegeneration in Parkinson's disease. Journal of Molecular Neuroscience : Mn. 23: 23-34. PMID 15126689 DOI: 10.1385/Jmn:23:1-2:023 |
0.386 |
|
2003 |
Bitan G, Tarus B, Vollers SS, Lashuel HA, Condron MM, Straub JE, Teplow DB. A molecular switch in amyloid assembly: Met35 and amyloid beta-protein oligomerization. Journal of the American Chemical Society. 125: 15359-65. PMID 14664580 DOI: 10.1021/Ja0349296 |
0.411 |
|
2003 |
Kheterpal I, Lashuel HA, Hartley DM, Walz T, Lansbury PT, Wetzel R. Abeta protofibrils possess a stable core structure resistant to hydrogen exchange. Biochemistry. 42: 14092-8. PMID 14640676 DOI: 10.1021/Bi0357816 |
0.46 |
|
2003 |
Lashuel HA, Hartley DM, Petre BM, Wall JS, Simon MN, Walz T, Lansbury PT. Mixtures of wild-type and a pathogenic (E22G) form of Abeta40 in vitro accumulate protofibrils, including amyloid pores. Journal of Molecular Biology. 332: 795-808. PMID 12972252 DOI: 10.1016/S0022-2836(03)00927-6 |
0.401 |
|
2003 |
Foguel D, Suarez MC, Ferrão-Gonzales AD, Porto TC, Palmieri L, Einsiedler CM, Andrade LR, Lashuel HA, Lansbury PT, Kelly JW, Silva JL. Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities. Proceedings of the National Academy of Sciences of the United States of America. 100: 9831-6. PMID 12900507 DOI: 10.1073/Pnas.1734009100 |
0.618 |
|
2003 |
Ferrão-Gonzales AD, Palmieri L, Valory M, Silva JL, Lashuel H, Kelly JW, Foguel D. Hydration and packing are crucial to amyloidogenesis as revealed by pressure studies on transthyretin variants that either protect or worsen amyloid disease. Journal of Molecular Biology. 328: 963-74. PMID 12729768 DOI: 10.1016/S0022-2836(03)00368-1 |
0.548 |
|
2002 |
Wang L, Lashuel HA, Walz T, Colon W. Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channel. Proceedings of the National Academy of Sciences of the United States of America. 99: 15947-52. PMID 12456883 DOI: 10.1073/Pnas.252508399 |
0.676 |
|
2002 |
Liu Y, Fallon L, Lashuel HA, Liu Z, Lansbury PT. The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility. Cell. 111: 209-18. PMID 12408865 DOI: 10.1016/S0092-8674(02)01012-7 |
0.318 |
|
2002 |
Lashuel HA, Petre BM, Wall J, Simon M, Nowak RJ, Walz T, Lansbury PT. Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. Journal of Molecular Biology. 322: 1089-102. PMID 12367530 DOI: 10.1016/S0022-2836(02)00735-0 |
0.388 |
|
2002 |
Lashuel HA, Hartley DM, Balakhaneh D, Aggarwal A, Teichberg S, Callaway DJ. New class of inhibitors of amyloid-beta fibril formation. Implications for the mechanism of pathogenesis in Alzheimer's disease. The Journal of Biological Chemistry. 277: 42881-90. PMID 12167652 DOI: 10.1074/Jbc.M206593200 |
0.337 |
|
2002 |
Lashuel HA, Hartley D, Petre BM, Walz T, Lansbury PT. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature. 418: 291. PMID 12124613 DOI: 10.1038/418291A |
0.482 |
|
2002 |
Oza VB, Smith C, Raman P, Koepf EK, Lashuel HA, Petrassi HM, Chiang KP, Powers ET, Sachettinni J, Kelly JW. Synthesis, structure, and activity of diclofenac analogues as transthyretin amyloid fibril formation inhibitors. Journal of Medicinal Chemistry. 45: 321-32. PMID 11784137 DOI: 10.1021/Jm010257N |
0.757 |
|
2000 |
Lashuel HA, Labrenz SR, Woo L, Serpell LC, Kelly JW. Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly: implications for amyloid fibril formation and materials science. Journal of the American Chemical Society. 122: 5262-77. PMID 22339465 DOI: 10.1021/Ja9937831 |
0.544 |
|
2000 |
Cingolani G, Lashuel HA, Gerace L, Müller CW. Nuclear import factors importin alpha and importin beta undergo mutually induced conformational changes upon association. Febs Letters. 484: 291-8. PMID 11078895 DOI: 10.1016/S0014-5793(00)02154-2 |
0.319 |
|
2000 |
Liu K, Cho HS, Lashuel HA, Kelly JW, Wemmer DE. A glimpse of a possible amyloidogenic intermediate of transthyretin. Nature Structural Biology. 7: 754-7. PMID 10966644 DOI: 10.1038/78980 |
0.558 |
|
1999 |
Lashuel HA, Wurth C, Woo L, Kelly JW. The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions. Biochemistry. 38: 13560-73. PMID 10521263 DOI: 10.1021/Bi991021C |
0.557 |
|
1999 |
Chitnumsub P, Fiori WR, Lashuel HA, Diaz H, Kelly JW. The nucleation of monomeric parallel beta-sheet-like structures and their self-assembly in aqueous solution. Bioorganic & Medicinal Chemistry. 7: 39-59. PMID 10199655 DOI: 10.1016/S0968-0896(98)00222-3 |
0.501 |
|
1998 |
Lashuel HA, Lai Z, Kelly JW. Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30M, and L55P amyloid fibril formation. Biochemistry. 37: 17851-64. PMID 9922152 DOI: 10.1021/Bi981876+ |
0.573 |
|
1998 |
Patricelli MP, Lashuel HA, Giang DK, Kelly JW, Cravatt BF. Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: identification of the transmembrane domain as a site for oligomerization. Biochemistry. 37: 15177-87. PMID 9790682 DOI: 10.1021/Bi981733N |
0.498 |
|
1998 |
Peterson SA, Klabunde T, Lashuel HA, Purkey H, Sacchettini JC, Kelly JW. Inhibiting transthyretin conformational changes that lead to amyloid fibril formation. Proceedings of the National Academy of Sciences of the United States of America. 95: 12956-60. PMID 9789022 DOI: 10.1073/Pnas.95.22.12956 |
0.77 |
|
1998 |
Xie Y, Lashuel HA, Miroy GJ, Dikler S, Kelly JW. Recombinant human retinol-binding protein refolding, native disulfide formation, and characterization. Protein Expression and Purification. 14: 31-7. PMID 9758748 DOI: 10.1006/Prep.1998.0944 |
0.503 |
|
1997 |
Kelly JW, Colon W, Lai Z, Lashuel HA, McCulloch J, McCutchen SL, Miroy GJ, Peterson SA. Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid. Advances in Protein Chemistry. 50: 161-81. PMID 9338081 DOI: 10.1016/S0065-3233(08)60321-6 |
0.75 |
|
1997 |
Lai Z, McCulloch J, Lashuel HA, Kelly JW. Guanidine hydrochloride-induced denaturation and refolding of transthyretin exhibits a marked hysteresis: equilibria with high kinetic barriers. Biochemistry. 36: 10230-9. PMID 9254621 DOI: 10.1021/Bi963195P |
0.511 |
|
1996 |
Miroy GJ, Lai Z, Lashuel HA, Peterson SA, Strang C, Kelly JW. Inhibiting transthyretin amyloid fibril formation via protein stabilization. Proceedings of the National Academy of Sciences of the United States of America. 93: 15051-6. PMID 8986762 DOI: 10.1073/Pnas.93.26.15051 |
0.609 |
|
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