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× 2024 Post-translational glycosylation diminishes α-synuclein pathology formation M. Pratt ; H. Lashuel
Nature Chemical Biology . 2024-02-14. DOI : 10.1038/s41589-024-01553-0. Author Correction: Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates G. Limorenko ; M. Tatli ; R. Kolla ; S. Nazarov ; M-T. Weil et al.
Nature Communications . 2024. Vol. 15 , num. 1 . DOI : 10.1038/s41467-024-48976-w. Effective Inhibition of TDP-43 Aggregation by Native State Stabilization L. Yang ; Y. Jasiqi ; A. Zettor ; O. Vadas ; J. Chiaravalli et al.
Angewandte Chemie-International Edition . 2024. Vol. 63 , num. 3 , p. e202314587. DOI : 10.1002/anie.202314587. 2023 Recombinant Full-Length TDP-43 Oligomers Retain Their Ability to Bind RNAs, Are Not Toxic, and Do Not Seed TDP-43 Aggregation in Vitro L. Yang ; Y. Jasiqi ; H. Lashuel
Acs Chemical Neuroscience . 2023-12-20. Vol. 15 , num. 1 , p. 193-204. DOI : 10.1021/acschemneuro.3c00691. Development and validation of an expanded antibody toolset that captures alpha-synuclein pathological diversity in Lewy body diseases M. F. Altay ; S. T. Kumar ; J. Burtscher ; S. Jagannath ; C. Strand et al.
Npj Parkinsons Disease . 2023-12-07. Vol. 9 , num. 1 , p. 161. DOI : 10.1038/s41531-023-00604-y. Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates G. Limorenko ; M. Tatli ; R. Kolla ; S. Nazarov ; M-T. Weil et al.
Nature Communications . 2023-07-04. Vol. 14 , num. 1 , p. 3939. DOI : 10.1038/s41467-023-39314-7. Overexpression of human alpha-Synuclein leads to dysregulated microbiome/metabolites with ageing in a rat model of Parkinson disease Y. Singh ; C. Trautwein ; J. Romani ; M. S. S. Salker ; P. H. H. Neckel et al.
Molecular Neurodegeneration . 2023-07-04. Vol. 18 , num. 1 , p. 44. DOI : 10.1186/s13024-023-00628-1. Artificial intelligence-coupled plasmonic infrared sensor for detection of structural protein biomarkers in neurodegenerative diseases D. Kavungal ; P. Magalhaes ; S. T. Kumar ; R. Kolla ; H. A. Lashuel et al.
Science Advances . 2023-07-01. Vol. 9 , num. 28 , p. eadg9644. DOI : 10.1126/sciadv.adg9644. 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. 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. 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. Pathological Relevance of Post-Translationally Modified Alpha-Synuclein (pSer87, pSer129, nTyr39) in Idiopathic Parkinson’s Disease and Multiple System Atrophy B. Sonustun ; M. F. Altay ; C. Strand ; K. Ebanks ; G. Hondhamuni et al.
Cells . 2022-03-01. Vol. 11 , num. 5 , p. 906. DOI : 10.3390/cells11050906. 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. 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. 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. 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. 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. 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. 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. 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. 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 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 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. 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. 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. 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. 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. 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. 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. 2016 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. 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. 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. 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. 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. 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 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. 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. 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. 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. 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. 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 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. 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 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. 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. 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. 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. 2008 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. 2007 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. 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. 2005 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. 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. 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. 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. 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 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. 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. 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.