6cfh › Citations

Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation.

Guenther EL, Cao Q, Trinh H, Lu J, Sawaya MR, Cascio D, Boyer DR, Rodriguez JA, Hughes MP, Eisenberg DS
Nat Struct Mol Biol 25 463-471 (2018)
Related entries: 5whn, 5whp, 5wia, 5wiq, 5wkb, 5wkd, 6cb9, 6cew, 6cf4

Cited: 104 times
EuropePMC logo PMID: 29786080

Abstract

The normally soluble TAR DNA-binding protein 43 (TDP-43) is found aggregated both in reversible stress granules and in irreversible pathogenic amyloid. In TDP-43, the low-complexity domain (LCD) is believed to be involved in both types of aggregation. To uncover the structural origins of these two modes of β-sheet-rich aggregation, we have determined ten structures of segments of the LCD of human TDP-43. Six of these segments form steric zippers characteristic of the spines of pathogenic amyloid fibrils; four others form LARKS, the labile amyloid-like interactions characteristic of protein hydrogels and proteins found in membraneless organelles, including stress granules. Supporting a hypothetical pathway from reversible to irreversible amyloid aggregation, we found that familial ALS variants of TDP-43 convert LARKS to irreversible aggregates. Our structures suggest how TDP-43 adopts both reversible and irreversible β-sheet aggregates and the role of mutation in the possible transition of reversible to irreversible pathogenic aggregation.

Reviews - 6cfh mentioned but not cited (2)

  1. Structural Insights Into TDP-43 and Effects of Post-translational Modifications. François-Moutal L, Perez-Miller S, Scott DD, Miranda VG, Mollasalehi N, Khanna M. Front Mol Neurosci 12 301 (2019)
  2. Electron Diffraction of 3D Molecular Crystals. Saha A, Nia SS, Rodríguez JA. Chem Rev 122 13883-13914 (2022)

Articles - 6cfh mentioned but not cited (2)

  1. Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation. Guenther EL, Cao Q, Trinh H, Lu J, Sawaya MR, Cascio D, Boyer DR, Rodriguez JA, Hughes MP, Eisenberg DS. Nat Struct Mol Biol 25 463-471 (2018)
  2. Structure-based machine-guided mapping of amyloid sequence space reveals uncharted sequence clusters with higher solubilities. Louros N, Orlando G, De Vleeschouwer M, Rousseau F, Schymkowitz J. Nat Commun 11 3314 (2020)


Reviews citing this publication (32)

  1. The molecular language of membraneless organelles. Gomes E, Shorter J. J Biol Chem 294 7115-7127 (2019)
  2. Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis. Prasad A, Bharathi V, Sivalingam V, Girdhar A, Patel BK. Front Mol Neurosci 12 25 (2019)
  3. Protein transmission in neurodegenerative disease. Peng C, Trojanowski JQ, Lee VM. Nat Rev Neurol 16 199-212 (2020)
  4. Biomolecular Phase Separation: From Molecular Driving Forces to Macroscopic Properties. Dignon GL, Best RB, Mittal J. Annu Rev Phys Chem 71 53-75 (2020)
  5. Friend or foe-Post-translational modifications as regulators of phase separation and RNP granule dynamics. Hofweber M, Dormann D. J Biol Chem 294 7137-7150 (2019)
  6. FUS and TDP-43 Phases in Health and Disease. Portz B, Lee BL, Shorter J. Trends Biochem Sci 46 550-563 (2021)
  7. The expanding amyloid family: Structure, stability, function, and pathogenesis. Sawaya MR, Hughes MP, Rodriguez JA, Riek R, Eisenberg DS. Cell 184 4857-4873 (2021)
  8. The cryo-EM method microcrystal electron diffraction (MicroED). Nannenga BL, Gonen T. Nat Methods 16 369-379 (2019)
  9. Biological phase separation: cell biology meets biophysics. Yoshizawa T, Nozawa RS, Jia TZ, Saio T, Mori E. Biophys Rev 12 519-539 (2020)
  10. Liquid-Liquid Phase Separation and Its Mechanistic Role in Pathological Protein Aggregation. Babinchak WM, Surewicz WK. J Mol Biol 432 1910-1925 (2020)
  11. Methods for Physical Characterization of Phase-Separated Bodies and Membrane-less Organelles. Mitrea DM, Chandra B, Ferrolino MC, Gibbs EB, Tolbert M, White MR, Kriwacki RW. J Mol Biol 430 4773-4805 (2018)
  12. Triad of TDP43 control in neurodegeneration: autoregulation, localization and aggregation. Tziortzouda P, Van Den Bosch L, Hirth F. Nat Rev Neurosci 22 197-208 (2021)
  13. Molecular structure in biomolecular condensates. Peran I, Mittag T. Curr Opin Struct Biol 60 17-26 (2020)
  14. Molecular Mechanisms Underlying TDP-43 Pathology in Cellular and Animal Models of ALS and FTLD. Wood A, Gurfinkel Y, Polain N, Lamont W, Lyn Rea S. Int J Mol Sci 22 4705 (2021)
  15. Liquid-Liquid Phase Separation of TDP-43 and FUS in Physiology and Pathology of Neurodegenerative Diseases. Carey JL, Guo L. Front Mol Biosci 9 826719 (2022)
  16. Karyopherins and condensates. Springhower CE, Rosen MK, Chook YM. Curr Opin Cell Biol 64 112-123 (2020)
  17. Looking Beyond the Core: The Role of Flanking Regions in the Aggregation of Amyloidogenic Peptides and Proteins. Ulamec SM, Brockwell DJ, Radford SE. Front Neurosci 14 611285 (2020)
  18. Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins. Bianchi G, Longhi S, Grandori R, Brocca S. Int J Mol Sci 21 E6208 (2020)
  19. Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils. Chatani E, Yuzu K, Ohhashi Y, Goto Y. Int J Mol Sci 22 4349 (2021)
  20. Molecular Dissection of TDP-43 as a Leading Cause of ALS/FTLD. Tamaki Y, Urushitani M. Int J Mol Sci 23 12508 (2022)
  21. Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective. Daskalov A, El Mammeri N, Lends A, Shenoy J, Lamon G, Fichou Y, Saad A, Martinez D, Morvan E, Berbon M, Grélard A, Kauffmann B, Ferber M, Bardiaux B, Habenstein B, Saupe SJ, Loquet A. Front Mol Neurosci 14 670513 (2021)
  22. Inherited and Sporadic Amyotrophic Lateral Sclerosis and Fronto-Temporal Lobar Degenerations arising from Pathological Condensates of Phase Separating Proteins. Fernandopulle M, Wang G, Nixon-Abell J, Qamar S, Balaji V, Morihara R, St George-Hyslop PH. Hum Mol Genet 28 R187-R196 (2019)
  23. The Cryo-EM Effect: Structural Biology of Neurodegenerative Disease Aggregates. Creekmore BC, Chang YW, Lee EB. J Neuropathol Exp Neurol 80 514-529 (2021)
  24. Preventing Biofilm Formation and Development on Ear, Nose and Throat Medical Devices. Gheorghe DC, Ilie A, Niculescu AG, Grumezescu AM. Biomedicines 9 1025 (2021)
  25. The Different Faces of the TDP-43 Low-Complexity Domain: The Formation of Liquid Droplets and Amyloid Fibrils. Chien HM, Lee CC, Huang JJ. Int J Mol Sci 22 8213 (2021)
  26. The Impact of Dysregulated microRNA Biogenesis Machinery and microRNA Sorting on Neurodegenerative Diseases. Weng YT, Chang YM, Chern Y. Int J Mol Sci 24 3443 (2023)
  27. Direct targeting of TDP-43, from small molecules to biologics: the therapeutic landscape. Francois-Moutal L, Scott DD, Khanna M. RSC Chem Biol 2 1158-1166 (2021)
  28. Disrupting pathologic phase transitions in neurodegeneration. Hurtle BT, Xie L, Donnelly CJ. J Clin Invest 133 e168549 (2023)
  29. TDP43 ribonucleoprotein granules: physiologic function to pathologic aggregates. Corbet GA, Wheeler JR, Parker R, Weskamp K. RNA Biol 18 128-138 (2021)
  30. Advances in mass spectrometry to unravel the structure and function of protein condensates. Sahin C, Leppert A, Landreh M. Nat Protoc 18 3653-3661 (2023)
  31. Mutations in human prion-like domains: pathogenic but not always amyloidogenic. Bartolomé-Nafría A, García-Pardo J, Ventura S. Prion 18 28-39 (2024)
  32. RNA: The Unsuspected Conductor in the Orchestra of Macromolecular Crowding. Zacco E, Broglia L, Kurihara M, Monti M, Gustincich S, Pastore A, Plath K, Nagakawa S, Cerase A, Sanchez de Groot N, Tartaglia GG. Chem Rev 124 4734-4777 (2024)

Articles citing this publication (68)

  1. The role of liquid-liquid phase separation in aggregation of the TDP-43 low-complexity domain. Babinchak WM, Haider R, Dumm BK, Sarkar P, Surewicz K, Choi JK, Surewicz WK. J Biol Chem 294 6306-6317 (2019)
  2. Cryo-EM structures of four polymorphic TDP-43 amyloid cores. Cao Q, Boyer DR, Sawaya MR, Ge P, Eisenberg DS. Nat Struct Mol Biol 26 619-627 (2019)
  3. Widespread occurrence of the droplet state of proteins in the human proteome. Hardenberg M, Horvath A, Ambrus V, Fuxreiter M, Vendruscolo M. Proc Natl Acad Sci U S A 117 33254-33262 (2020)
  4. Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly. Gui X, Luo F, Li Y, Zhou H, Qin Z, Liu Z, Gu J, Xie M, Zhao K, Dai B, Shin WS, He J, He L, Jiang L, Zhao M, Sun B, Li X, Liu C, Li D. Nat Commun 10 2006 (2019)
  5. TDP-43 extracted from frontotemporal lobar degeneration subject brains displays distinct aggregate assemblies and neurotoxic effects reflecting disease progression rates. Laferrière F, Maniecka Z, Pérez-Berlanga M, Hruska-Plochan M, Gilhespy L, Hock EM, Wagner U, Afroz T, Boersema PJ, Barmettler G, Foti SC, Asi YT, Isaacs AM, Al-Amoudi A, Lewis A, Stahlberg H, Ravits J, De Giorgi F, Ichas F, Bezard E, Picotti P, Lashley T, Polymenidou M. Nat Neurosci 22 65-77 (2019)
  6. The mutational landscape of a prion-like domain. Bolognesi B, Faure AJ, Seuma M, Schmiedel JM, Tartaglia GG, Lehner B. Nat Commun 10 4162 (2019)
  7. The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure. Boyer DR, Li B, Sun C, Fan W, Zhou K, Hughes MP, Sawaya MR, Jiang L, Eisenberg DS. Proc Natl Acad Sci U S A 117 3592-3602 (2020)
  8. Phase separation-deficient TDP43 remains functional in splicing. Schmidt HB, Barreau A, Rohatgi R. Nat Commun 10 4890 (2019)
  9. Prion-Like Propagation of Protein Misfolding and Aggregation in Amyotrophic Lateral Sclerosis. McAlary L, Plotkin SS, Yerbury JJ, Cashman NR. Front Mol Neurosci 12 262 (2019)
  10. Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils. Cao Q, Boyer DR, Sawaya MR, Ge P, Eisenberg DS. Nat Struct Mol Biol 27 653-659 (2020)
  11. Extreme amyloid polymorphism in Staphylococcus aureus virulent PSMα peptides. Salinas N, Colletier JP, Moshe A, Landau M. Nat Commun 9 3512 (2018)
  12. CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid. Lu J, Cao Q, Hughes MP, Sawaya MR, Boyer DR, Cascio D, Eisenberg DS. Nat Commun 11 4090 (2020)
  13. TDP-43 and Tau Oligomers in Alzheimer's Disease, Amyotrophic Lateral Sclerosis, and Frontotemporal Dementia. Montalbano M, McAllen S, Cascio FL, Sengupta U, Garcia S, Bhatt N, Ellsworth A, Heidelman EA, Johnson OD, Doskocil S, Kayed R. Neurobiol Dis 146 105130 (2020)
  14. Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS. Lee M, Ghosh U, Thurber KR, Kato M, Tycko R. Nat Commun 11 5735 (2020)
  15. TREM2 interacts with TDP-43 and mediates microglial neuroprotection against TDP-43-related neurodegeneration. Xie M, Liu YU, Zhao S, Zhang L, Bosco DB, Pang YP, Zhong J, Sheth U, Martens YA, Zhao N, Liu CC, Zhuang Y, Wang L, Dickson DW, Mattson MP, Bu G, Wu LJ. Nat Neurosci 25 26-38 (2022)
  16. ATP binds and inhibits the neurodegeneration-associated fibrillization of the FUS RRM domain. Kang J, Lim L, Song J. Commun Biol 2 223 (2019)
  17. Structure-based inhibitors halt prion-like seeding by Alzheimer's disease-and tauopathy-derived brain tissue samples. Seidler PM, Boyer DR, Murray KA, Yang TP, Bentzel M, Sawaya MR, Rosenberg G, Cascio D, Williams CK, Newell KL, Ghetti B, DeTure MA, Dickson DW, Vinters HV, Eisenberg DS. J Biol Chem 294 16451-16464 (2019)
  18. Aging can transform single-component protein condensates into multiphase architectures. Garaizar A, Espinosa JR, Joseph JA, Krainer G, Shen Y, Knowles TPJ, Collepardo-Guevara R. Proc Natl Acad Sci U S A 119 e2119800119 (2022)
  19. Structure of amyloid-β (20-34) with Alzheimer's-associated isomerization at Asp23 reveals a distinct protofilament interface. Warmack RA, Boyer DR, Zee CT, Richards LS, Sawaya MR, Cascio D, Gonen T, Eisenberg DS, Clarke SG. Nat Commun 10 3357 (2019)
  20. A Chemical Chaperone Decouples TDP-43 Disordered Domain Phase Separation from Fibrillation. Choi KJ, Tsoi PS, Moosa MM, Paulucci-Holthauzen A, Liao SJ, Ferreon JC, Ferreon ACM. Biochemistry 57 6822-6826 (2018)
  21. Low-complexity domain of U1-70K modulates phase separation and aggregation through distinctive basic-acidic motifs. Xue S, Gong R, He F, Li Y, Wang Y, Tan T, Luo SZ. Sci Adv 5 eaax5349 (2019)
  22. Gel-like inclusions of C-terminal fragments of TDP-43 sequester stalled proteasomes in neurons. Riemenschneider H, Guo Q, Bader J, Frottin F, Farny D, Kleinberger G, Haass C, Mann M, Hartl FU, Baumeister W, Hipp MS, Meissner F, Fernández-Busnadiego R, Edbauer D. EMBO Rep 23 e53890 (2022)
  23. Amyotrophic Lateral Sclerosis: Proteins, Proteostasis, Prions, and Promises. McAlary L, Chew YL, Lum JS, Geraghty NJ, Yerbury JJ, Cashman NR. Front Cell Neurosci 14 581907 (2020)
  24. MicroED methodology and development. Nannenga BL. Struct Dyn 7 014304 (2020)
  25. The cooperative binding of TDP-43 to GU-rich RNA repeats antagonizes TDP-43 aggregation. Rengifo-Gonzalez JC, El Hage K, Clément MJ, Steiner E, Joshi V, Craveur P, Durand D, Pastré D, Bouhss A. Elife 10 e67605 (2021)
  26. Antibody against TDP-43 phosphorylated at serine 375 suggests conformational differences of TDP-43 aggregates among FTLD-TDP subtypes. Neumann M, Frick P, Paron F, Kosten J, Buratti E, Mackenzie IR. Acta Neuropathol 140 645-658 (2020)
  27. Mutations linked to neurological disease enhance self-association of low-complexity protein sequences. Zhou X, Sumrow L, Tashiro K, Sutherland L, Liu D, Qin T, Kato M, Liszczak G, McKnight SL. Science 377 eabn5582 (2022)
  28. RNA recognition motifs of disease-linked RNA-binding proteins contribute to amyloid formation. Agrawal S, Kuo PH, Chu LY, Golzarroshan B, Jain M, Yuan HS. Sci Rep 9 6171 (2019)
  29. Liquid-Liquid Phase Separation Enhances TDP-43 LCD Aggregation but Delays Seeded Aggregation. Pakravan D, Michiels E, Bratek-Skicki A, De Decker M, Van Lindt J, Alsteens D, Derclaye S, Van Damme P, Schymkowitz J, Rousseau F, Tompa P, Van Den Bosch L. Biomolecules 11 548 (2021)
  30. Protein structural transitions critically transform the network connectivity and viscoelasticity of RNA-binding protein condensates but RNA can prevent it. Tejedor AR, Sanchez-Burgos I, Estevez-Espinosa M, Garaizar A, Collepardo-Guevara R, Ramirez J, Espinosa JR. Nat Commun 13 5717 (2022)
  31. USP7 regulates ALS-associated proteotoxicity and quality control through the NEDD4L-SMAD pathway. Zhang T, Periz G, Lu YN, Wang J. Proc Natl Acad Sci U S A 117 28114-28125 (2020)
  32. High-throughput cryo-EM structure determination of amyloids. Lövestam S, Scheres SHW. Faraday Discuss 240 243-260 (2022)
  33. Kinetic interplay between droplet maturation and coalescence modulates shape of aged protein condensates. Garaizar A, Espinosa JR, Joseph JA, Collepardo-Guevara R. Sci Rep 12 4390 (2022)
  34. Altered Phase Separation and Cellular Impact in C9orf72-Linked ALS/FTD. Solomon DA, Smikle R, Reid MJ, Mizielinska S. Front Cell Neurosci 15 664151 (2021)
  35. Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly. Taş K, Volta BD, Lindner C, El Bounkari O, Hille K, Tian Y, Puig-Bosch X, Ballmann M, Hornung S, Ortner M, Prem S, Meier L, Rammes G, Haslbeck M, Weber C, Megens RTA, Bernhagen J, Kapurniotu A. Nat Commun 13 5004 (2022)
  36. Molecular structure of an amyloid fibril formed by FUS low-complexity domain. Sun Y, Zhang S, Hu J, Tao Y, Xia W, Gu J, Li Y, Cao Q, Li D, Liu C. iScience 25 103701 (2022)
  37. Purification and Structural Characterization of Aggregation-Prone Human TDP-43 Involved in Neurodegenerative Diseases. Wright GSA, Watanabe TF, Amporndanai K, Plotkin SS, Cashman NR, Antonyuk SV, Hasnain SS. iScience 23 101159 (2020)
  38. ALS mutations in the TIA-1 prion-like domain trigger highly condensed pathogenic structures. Sekiyama N, Takaba K, Maki-Yonekura S, Akagi KI, Ohtani Y, Imamura K, Terakawa T, Yamashita K, Inaoka D, Yonekura K, Kodama TS, Tochio H. Proc Natl Acad Sci U S A 119 e2122523119 (2022)
  39. Mass Spectrometry of RNA-Binding Proteins during Liquid-Liquid Phase Separation Reveals Distinct Assembly Mechanisms and Droplet Architectures. Sahin C, Motso A, Gu X, Feyrer H, Lama D, Arndt T, Rising A, Gese GV, Hällberg BM, Marklund EG, Schafer NP, Petzold K, Teilum K, Wolynes PG, Landreh M. J Am Chem Soc 145 10659-10668 (2023)
  40. Micellar TIA1 with folded RNA binding domains as a model for reversible stress granule formation. Fritzsching KJ, Yang Y, Pogue EM, Rayman JB, Kandel ER, McDermott AE. Proc Natl Acad Sci U S A 117 31832-31837 (2020)
  41. Minimalist Design of an Intrinsically Disordered Protein-Mimicking Scaffold for an Artificial Membraneless Organelle. Liu J, Zhorabek F, Dai X, Huang J, Chau Y. ACS Cent Sci 8 493-500 (2022)
  42. Phosphorylated and Phosphonated Low-Complexity Protein Segments for Biomimetic Mineralization and Repair of Tooth Enamel. Chang R, Liu YJ, Zhang YL, Zhang SY, Han BB, Chen F, Chen YX. Adv Sci (Weinh) 9 e2103829 (2022)
  43. Sequence determinants of in cell condensate morphology, dynamics, and oligomerization as measured by number and brightness analysis. Emenecker RJ, Holehouse AS, Strader LC. Cell Commun Signal 19 65 (2021)
  44. Frontotemporal dementia-linked P112H mutation of TDP-43 induces protein structural change and impairs its RNA binding function. Agrawal S, Jain M, Yang WZ, Yuan HS. Protein Sci 30 350-365 (2021)
  45. Interactions between the Intrinsically Disordered Regions of hnRNP-A2 and TDP-43 Accelerate TDP-43's Conformational Transition. Chiang WC, Lee MH, Chen TC, Huang JR. Int J Mol Sci 21 E5930 (2020)
  46. Sequence Determinants of TDP-43 Ribonucleoprotein Condensate Formation and Axonal Transport in Neurons. Vishal SS, Wijegunawardana D, Salaikumaran MR, Gopal PP. Front Cell Dev Biol 10 876893 (2022)
  47. Sequence-based Prediction of the Cellular Toxicity Associated with Amyloid Aggregation within Protein Condensates. Horvath A, Vendruscolo M, Fuxreiter M. Biochemistry 61 2461-2469 (2022)
  48. Time-Dependent Material Properties of Aging Biomolecular Condensates from Different Viscoelasticity Measurements in Molecular Dynamics Simulations. Tejedor AR, Collepardo-Guevara R, Ramírez J, Espinosa JR. J Phys Chem B 127 4441-4459 (2023)
  49. Bioinformatic identification of previously unrecognized amyloidogenic proteins. Rosenberg GM, Murray KA, Salwinski L, Hughes MP, Abskharon R, Eisenberg DS. J Biol Chem 298 101920 (2022)
  50. Location and Concentration of Aromatic-Rich Segments Dictates the Percolating Inter-Molecular Network and Viscoelastic Properties of Ageing Condensates. Blazquez S, Sanchez-Burgos I, Ramirez J, Higginbotham T, Conde MM, Collepardo-Guevara R, Tejedor AR, Espinosa JR. Adv Sci (Weinh) 10 e2207742 (2023)
  51. Modulation of assembly of TDP-43 low-complexity domain by heparin: From droplets to amyloid fibrils. Garg DK, Bhat R. Biophys J 121 2568-2582 (2022)
  52. Ab Initio Determination of Peptide Structures by MicroED. Zee CT, Saha A, Sawaya MR, Rodriguez JA. Methods Mol Biol 2215 329-348 (2021)
  53. Different Intermolecular Interactions Drive Nonpathogenic Liquid-Liquid Phase Separation and Potentially Pathogenic Fibril Formation by TDP-43. Zeng YT, Bi LL, Zhuo XF, Yang LY, Sun B, Lu JX. Int J Mol Sci 23 15227 (2022)
  54. Micro-electron diffraction structure of the aggregation-driving N terminus of Drosophila neuronal protein Orb2A reveals amyloid-like β-sheets. Bowler JT, Sawaya MR, Boyer DR, Cascio D, Bali M, Eisenberg DS. J Biol Chem 298 102396 (2022)
  55. Targeting the glycine-rich domain of TDP-43 with antibodies prevents its aggregation in vitro and reduces neurofilament levels in vivo. Riemenschneider H, Simonetti F, Sheth U, Katona E, Roth S, Hutten S, Farny D, Michaelsen M, Nuscher B, Schmidt MK, Flatley A, Schepers A, Gruijs da Silva LA, Zhou Q, Klopstock T, Liesz A, Arzberger T, Herms J, Feederle R, Gendron TF, Dormann D, Edbauer D. Acta Neuropathol Commun 11 112 (2023)
  56. Tryptophan Probes of TDP-43 C-Terminal Domain Amyloid Formation. Shuster SO, Lee JC. J Phys Chem B 125 3781-3789 (2021)
  57. A crystal-structural study of Pauling-Corey rippled sheets. Kuhn AJ, Ehlke B, Johnstone TC, Oliver SRJ, Raskatov JA. Chem Sci 13 671-680 (2022)
  58. Structure and Conservation of Amyloid Spines From the Candida albicans Als5 Adhesin. Golan N, Schwartz-Perov S, Landau M, Lipke PN. Front Mol Biosci 9 926959 (2022)
  59. The new missense G376V-TDP-43 variant induces late-onset distal myopathy but not amyotrophic lateral sclerosis. Zibold J, Lessard LER, Picard F, da Silva LG, Zadorozhna Y, Streichenberger N, Belotti E, Osseni A, Emerit A, Errazuriz-Cerda E, Michel-Calemard L, Menassa R, Coudert L, Wiessner M, Stucka R, Klopstock T, Simonetti F, Hutten S, Nonaka T, Hasegawa M, Strom TM, Bernard E, Ollagnon E, Urtizberea A, Dormann D, Petiot P, Schaeffer L, Senderek J, Leblanc P. Brain 147 1768-1783 (2024)
  60. Early-Stage Oligomerization of Prion-like Polypeptides Reveals the Molecular Mechanism of Amyloid-Disrupting Capacity by Proline Residues. Lin TY, Ma YW, Tsai MY. J Phys Chem B 127 1074-1088 (2023)
  61. Self-assembled fibrinogen-fibronectin hybrid protein nanofibers with medium-sensitive stability. Scheuer K, Helbing C, Firkowska-Boden I, Jandt KD. RSC Adv 11 14113-14120 (2021)
  62. Structural polymorphism of the low-complexity C-terminal domain of TDP-43 amyloid aggregates revealed by solid-state NMR. Shenoy J, Lends A, Berbon M, Bilal M, El Mammeri N, Bertoni M, Saad A, Morvan E, Grélard A, Lecomte S, Theillet FX, Buell AK, Kauffmann B, Habenstein B, Loquet A. Front Mol Biosci 10 1148302 (2023)
  63. Cryo-EM observation of the amyloid key structure of polymorphic TDP-43 amyloid fibrils. Sharma K, Stockert F, Shenoy J, Berbon M, Abdul-Shukkoor MB, Habenstein B, Loquet A, Schmidt M, Fändrich M. Nat Commun 15 486 (2024)
  64. Halogen doped graphene quantum dots modulate TDP-43 phase separation and aggregation in the nucleus. Zhang H, Guo H, Li D, Zhang Y, Zhang S, Kang W, Liu C, Le W, Wang L, Li D, Dai B. Nat Commun 15 2980 (2024)
  65. Importance of the Q/N-rich segment for protein stability of endogenous mouse TDP-43. Sato T, Oda K, Sakai S, Kato R, Yamamori S, Itakura M, Kodera Y, Nishizawa M, Sasaoka T, Onodera O, Yokoyama M. Sci Rep 12 14923 (2022)
  66. Low complexity domains of the nucleocapsid protein of SARS-CoV-2 form amyloid fibrils. Tayeb-Fligelman E, Bowler JT, Tai CE, Sawaya MR, Jiang YX, Garcia G, Griner SL, Cheng X, Salwinski L, Lutter L, Seidler PM, Lu J, Rosenberg GM, Hou K, Abskharon R, Pan H, Zee CT, Boyer DR, Li Y, Anderson DH, Murray KA, Falcon G, Cascio D, Saelices L, Damoiseaux R, Arumugaswami V, Guo F, Eisenberg DS. Nat Commun 14 2379 (2023)
  67. Targeting amyotrophic lateral sclerosis by neutralizing seeding-competent TDP-43 in CSF. Audrain M, Egesipe AL, Tentillier N, Font L, Ratnam M, Mottier L, Clavel M, Le Roux-Bourdieu M, Fenyi A, Ollier R, Chevalier E, Guilhot F, Fuchs A, Piorkowska K, Carlyle B, Arnold SE, Berry JD, Luthi-Carter R, Adolfsson O, Pfeifer A, Kosco-Vilbois M, Seredenina T, Afroz T. Brain Commun 5 fcad306 (2023)
  68. The Regulatory Mechanism of Transthyretin Irreversible Aggregation through Liquid-to-Solid Phase Transition. Duan G, Li Y, Ye M, Liu H, Wang N, Luo S. Int J Mol Sci 24 3729 (2023)


Quick links