4rik › Citations

Structure of the toxic core of α-synuclein from invisible crystals.

Rodriguez JA, Ivanova MI, Sawaya MR, Cascio D, Reyes FE, Shi D, Sangwan S, Guenther EL, Johnson LM, Zhang M, Jiang L, Arbing MA, Nannenga BL, Hattne J, Whitelegge J, Brewster AS, Messerschmidt M, Boutet S, Sauter NK, Gonen T, Eisenberg DS
Nature 525 486-90 (2015)
Related entries: 4ril, 4znn

Cited: 313 times
EuropePMC logo PMID: 26352473

Abstract

The protein α-synuclein is the main component of Lewy bodies, the neuron-associated aggregates seen in Parkinson disease and other neurodegenerative pathologies. An 11-residue segment, which we term NACore, appears to be responsible for amyloid formation and cytotoxicity of human α-synuclein. Here we describe crystals of NACore that have dimensions smaller than the wavelength of visible light and thus are invisible by optical microscopy. As the crystals are thousands of times too small for structure determination by synchrotron X-ray diffraction, we use micro-electron diffraction to determine the structure at atomic resolution. The 1.4 Å resolution structure demonstrates that this method can determine previously unknown protein structures and here yields, to our knowledge, the highest resolution achieved by any cryo-electron microscopy method to date. The structure exhibits protofibrils built of pairs of face-to-face β-sheets. X-ray fibre diffraction patterns show the similarity of NACore to toxic fibrils of full-length α-synuclein. The NACore structure, together with that of a second segment, inspires a model for most of the ordered portion of the toxic, full-length α-synuclein fibril, presenting opportunities for the design of inhibitors of α-synuclein fibrils.

Articles - 4rik mentioned but not cited (6)

  1. Structure of the toxic core of α-synuclein from invisible crystals. Rodriguez JA, Ivanova MI, Sawaya MR, Cascio D, Reyes FE, Shi D, Sangwan S, Guenther EL, Johnson LM, Zhang M, Jiang L, Arbing MA, Nannenga BL, Hattne J, Whitelegge J, Brewster AS, Messerschmidt M, Boutet S, Sauter NK, Gonen T, Eisenberg DS. Nature 525 486-490 (2015)
  2. Cryo-EM structure of alpha-synuclein fibrils. Guerrero-Ferreira R, Taylor NM, Mona D, Ringler P, Lauer ME, Riek R, Britschgi M, Stahlberg H. Elife 7 e36402 (2018)
  3. Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy. Guerrero-Ferreira R, Taylor NM, Arteni AA, Kumari P, Mona D, Ringler P, Britschgi M, Lauer ME, Makky A, Verasdonck J, Riek R, Melki R, Meier BH, Böckmann A, Bousset L, Stahlberg H. Elife 8 e48907 (2019)
  4. Evidence for Intramolecular Antiparallel Beta-Sheet Structure in Alpha-Synuclein Fibrils from a Combination of Two-Dimensional Infrared Spectroscopy and Atomic Force Microscopy. Roeters SJ, Iyer A, Pletikapić G, Kogan V, Subramaniam V, Woutersen S. Sci Rep 7 41051 (2017)
  5. Nano-particle mediated inhibition of Parkinson's disease using computational biology approach. Kaushik AC, Bharadwaj S, Kumar S, Wei DQ. Sci Rep 8 9169 (2018)
  6. Conformational Search for the Building Block of Proteins Based on the Gradient Gravitational Search Algorithm (ConfGGS) Using Force Fields: CHARMM, AMBER, and OPLS-AA. Pradhan R, Panigrahi S, Sahu PK. J Chem Inf Model 63 670-690 (2023)


Reviews citing this publication (128)

  1. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. Chiti F, Dobson CM. Annu Rev Biochem 86 27-68 (2017)
  2. α-synuclein toxicity in neurodegeneration: mechanism and therapeutic strategies. Wong YC, Krainc D. Nat Med 23 1-13 (2017)
  3. A new era for understanding amyloid structures and disease. Iadanza MG, Jackson MP, Hewitt EW, Ranson NA, Radford SE. Nat Rev Mol Cell Biol 19 755-773 (2018)
  4. The Synucleinopathies: Twenty Years On. Goedert M, Jakes R, Spillantini MG. J Parkinsons Dis 7 S51-S69 (2017)
  5. Structural Studies of Amyloid Proteins at the Molecular Level. Eisenberg DS, Sawaya MR. Annu Rev Biochem 86 69-95 (2017)
  6. The activities of amyloids from a structural perspective. Riek R, Eisenberg DS. Nature 539 227-235 (2016)
  7. Review: Sporadic Parkinson's disease: development and distribution of α-synuclein pathology. Del Tredici K, Braak H. Neuropathol Appl Neurobiol 42 33-50 (2016)
  8. Like prions: the propagation of aggregated tau and α-synuclein in neurodegeneration. Goedert M, Masuda-Suzukake M, Falcon B. Brain 140 266-278 (2017)
  9. Mechanisms of α-Synuclein Induced Synaptopathy in Parkinson's Disease. Bridi JC, Hirth F. Front Neurosci 12 80 (2018)
  10. Half a century of amyloids: past, present and future. 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. Chem Soc Rev 49 5473-5509 (2020)
  11. Secondary nucleation in amyloid formation. Törnquist M, Michaels TCT, Sanagavarapu K, Yang X, Meisl G, Cohen SIA, Knowles TPJ, Linse S. Chem Commun (Camb) 54 8667-8684 (2018)
  12. Alpha-synuclein structure, functions, and interactions. Emamzadeh FN. J Res Med Sci 21 29 (2016)
  13. Implications of peptide assemblies in amyloid diseases. Ke PC, Sani MA, Ding F, Kakinen A, Javed I, Separovic F, Davis TP, Mezzenga R. Chem Soc Rev 46 6492-6531 (2017)
  14. 3D Electron Diffraction: The Nanocrystallography Revolution. Gemmi M, Mugnaioli E, Gorelik TE, Kolb U, Palatinus L, Boullay P, Hovmöller S, Abrahams JP. ACS Cent Sci 5 1315-1329 (2019)
  15. Cellular and Molecular Basis of Neurodegeneration in Parkinson Disease. Zeng XS, Geng WS, Jia JJ, Chen L, Zhang PP. Front Aging Neurosci 10 109 (2018)
  16. Alpha-Synuclein in Parkinson's Disease: From Pathogenetic Dysfunction to Potential Clinical Application. Xu L, Pu J. Parkinsons Dis 2016 1720621 (2016)
  17. The expanding amyloid family: Structure, stability, function, and pathogenesis. Sawaya MR, Hughes MP, Rodriguez JA, Riek R, Eisenberg DS. Cell 184 4857-4873 (2021)
  18. The cryo-EM method microcrystal electron diffraction (MicroED). Nannenga BL, Gonen T. Nat Methods 16 369-379 (2019)
  19. Amyloid Polymorphism in the Protein Folding and Aggregation Energy Landscape. Adamcik J, Mezzenga R. Angew Chem Int Ed Engl 57 8370-8382 (2018)
  20. Amyloid assembly and disassembly. Chuang E, Hori AM, Hesketh CD, Shorter J. J Cell Sci 131 jcs189928 (2018)
  21. How can rAAV-α-synuclein and the fibril α-synuclein models advance our understanding of Parkinson's disease? Volpicelli-Daley LA, Kirik D, Stoyka LE, Standaert DG, Harms AS. J Neurochem 139 Suppl 1 131-155 (2016)
  22. ɑ-Synuclein strains and seeding in Parkinson's disease, incidental Lewy body disease, dementia with Lewy bodies and multiple system atrophy: similarities and differences. Peelaerts W, Bousset L, Baekelandt V, Melki R. Cell Tissue Res 373 195-212 (2018)
  23. Small-molecule PET Tracers for Imaging Proteinopathies. Mathis CA, Lopresti BJ, Ikonomovic MD, Klunk WE. Semin Nucl Med 47 553-575 (2017)
  24. Neurodegeneration and the ordered assembly of α-synuclein. Spillantini MG, Goedert M. Cell Tissue Res 373 137-148 (2018)
  25. Monomer-dependent secondary nucleation in amyloid formation. Linse S. Biophys Rev 9 329-338 (2017)
  26. Lipids at the Crossroad of α-Synuclein Function and Dysfunction: Biological and Pathological Implications. Alza NP, Iglesias González PA, Conde MA, Uranga RM, Salvador GA. Front Cell Neurosci 13 175 (2019)
  27. Potential Modes of Intercellular α-Synuclein Transmission. Valdinocci D, Radford RA, Siow SM, Chung RS, Pountney DL. Int J Mol Sci 18 E469 (2017)
  28. Versatile Structures of α-Synuclein. Wang C, Zhao C, Li D, Tian Z, Lai Y, Diao J, Liu C. Front Mol Neurosci 9 48 (2016)
  29. α-synuclein aggregation and its modulation. Ghosh D, Mehra S, Sahay S, Singh PK, Maji SK. Int J Biol Macromol 100 37-54 (2017)
  30. Designer protein disaggregases to counter neurodegenerative disease. Shorter J. Curr Opin Genet Dev 44 1-8 (2017)
  31. Review: Spreading the word: precise animal models and validated methods are vital when evaluating prion-like behaviour of alpha-synuclein. Rey NL, George S, Brundin P. Neuropathol Appl Neurobiol 42 51-76 (2016)
  32. New Perspectives on Roles of Alpha-Synuclein in Parkinson's Disease. Zhang G, Xia Y, Wan F, Ma K, Guo X, Kou L, Yin S, Han C, Liu L, Huang J, Xiong N, Wang T. Front Aging Neurosci 10 370 (2018)
  33. Prion-like propagation of pathology in Parkinson disease. Volpicelli-Daley L, Brundin P. Handb Clin Neurol 153 321-335 (2018)
  34. Evidence of distinct α-synuclein strains underlying disease heterogeneity. Holec SAM, Woerman AL. Acta Neuropathol 142 73-86 (2021)
  35. Towards correlative super-resolution fluorescence and electron cryo-microscopy. Wolff G, Hagen C, Grünewald K, Kaufmann R. Biol Cell 108 245-258 (2016)
  36. Biophysical processes underlying cross-seeding in amyloid aggregation and implications in amyloid pathology. Ivanova MI, Lin Y, Lee YH, Zheng J, Ramamoorthy A. Biophys Chem 269 106507 (2021)
  37. Proteopathic Strains and the Heterogeneity of Neurodegenerative Diseases. Walker LC. Annu Rev Genet 50 329-346 (2016)
  38. Alpha Synuclein Connects the Gut-Brain Axis in Parkinson's Disease Patients - A View on Clinical Aspects, Cellular Pathology and Analytical Methodology. Schaeffer E, Kluge A, Böttner M, Zunke F, Cossais F, Berg D, Arnold P. Front Cell Dev Biol 8 573696 (2020)
  39. Dynamic structural flexibility of α-synuclein. Mor DE, Ugras SE, Daniels MJ, Ischiropoulos H. Neurobiol Dis 88 66-74 (2016)
  40. Genetics of Parkinson's disease and related disorders. Zhang PL, Chen Y, Zhang CH, Wang YX, Fernandez-Funez P. J Med Genet 55 73-80 (2018)
  41. The elusive tau molecular structures: can we translate the recent breakthroughs into new targets for intervention? Fichou Y, Al-Hilaly YK, Devred F, Smet-Nocca C, Tsvetkov PO, Verelst J, Winderickx J, Geukens N, Vanmechelen E, Perrotin A, Serpell L, Hanseeuw BJ, Medina M, Buée L, Landrieu I. Acta Neuropathol Commun 7 31 (2019)
  42. Effects of oligomer toxicity, fibril toxicity and fibril spreading in synucleinopathies. Cascella R, Bigi A, Cremades N, Cecchi C. Cell Mol Life Sci 79 174 (2022)
  43. The Promise and Challenges of Developing miRNA-Based Therapeutics for Parkinson's Disease. Titze-de-Almeida SS, Soto-Sánchez C, Fernandez E, Koprich JB, Brotchie JM, Titze-de-Almeida R. Cells 9 E841 (2020)
  44. The formation, function and regulation of amyloids: insights from structural biology. Landreh M, Sawaya MR, Hipp MS, Eisenberg DS, Wüthrich K, Hartl FU. J Intern Med 280 164-176 (2016)
  45. Is Lewy pathology in the human nervous system chiefly an indicator of neuronal protection or of toxicity? Chartier S, Duyckaerts C. Cell Tissue Res 373 149-160 (2018)
  46. 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)
  47. Molecular Mechanisms and Regulation of Mammalian Mitophagy. Choubey V, Zeb A, Kaasik A. Cells 11 38 (2021)
  48. Protein aggregation, misfolding and consequential human neurodegenerative diseases. Sami N, Rahman S, Kumar V, Zaidi S, Islam A, Ali S, Ahmad F, Hassan MI. Int J Neurosci 127 1047-1057 (2017)
  49. Ecology and Biogenesis of Functional Amyloids in Pseudomonas. Rouse SL, Matthews SJ, Dueholm MS. J Mol Biol 430 3685-3695 (2018)
  50. MicroED opens a new era for biological structure determination. Nannenga BL, Gonen T. Curr Opin Struct Biol 40 128-135 (2016)
  51. A critical review of the prion hypothesis of human synucleinopathies. Tamgüney G, Korczyn AD. Cell Tissue Res 373 213-220 (2018)
  52. Databases and Archiving for CryoEM. Patwardhan A, Lawson CL. Methods Enzymol 579 393-412 (2016)
  53. Interaction of Alpha-Synuclein With Lipids: Mitochondrial Cardiolipin as a Critical Player in the Pathogenesis of Parkinson's Disease. Gilmozzi V, Gentile G, Castelo Rueda MP, Hicks AA, Pramstaller PP, Zanon A, Lévesque M, Pichler I. Front Neurosci 14 578993 (2020)
  54. Alpha-Synuclein Aggregation Pathway in Parkinson's Disease: Current Status and Novel Therapeutic Approaches. Vidović M, Rikalovic MG. Cells 11 1732 (2022)
  55. Extracellular Interactions of Alpha-Synuclein in Multiple System Atrophy. Valdinocci D, Radford RAW, Goulding M, Hayashi J, Chung RS, Pountney DL. Int J Mol Sci 19 E4129 (2018)
  56. Membrane interactions of intrinsically disordered proteins: The example of alpha-synuclein. Das T, Eliezer D. Biochim Biophys Acta Proteins Proteom 1867 879-889 (2019)
  57. Alpha-synuclein and iron: two keys unlocking Parkinson's disease. Lingor P, Carboni E, Koch JC. J Neural Transm (Vienna) 124 973-981 (2017)
  58. Membranes as modulators of amyloid protein misfolding and target of toxicity. Rawat A, Langen R, Varkey J. Biochim Biophys Acta Biomembr 1860 1863-1875 (2018)
  59. MicroED in natural product and small molecule research. Danelius E, Halaby S, van der Donk WA, Gonen T. Nat Prod Rep 38 423-431 (2021)
  60. Neurons and Glia Interplay in α-Synucleinopathies. Mavroeidi P, Xilouri M. Int J Mol Sci 22 4994 (2021)
  61. Amyloid-Like Aggregation in Diseases and Biomaterials: Osmosis of Structural Information. Balasco N, Diaferia C, Morelli G, Vitagliano L, Accardo A. Front Bioeng Biotechnol 9 641372 (2021)
  62. Circular RNAs in Embryogenesis and Cell Differentiation With a Focus on Cancer Development. Di Agostino S, Riccioli A, De Cesaris P, Fontemaggi G, Blandino G, Filippini A, Fazi F. Front Cell Dev Biol 8 389 (2020)
  63. Mechanisms of Neurodegeneration in Various Forms of Parkinsonism-Similarities and Differences. Koziorowski D, Figura M, Milanowski ŁM, Szlufik S, Alster P, Madetko N, Friedman A. Cells 10 656 (2021)
  64. An Update on the Critical Role of α-Synuclein in Parkinson's Disease and Other Synucleinopathies: from Tissue to Cellular and Molecular Levels. Serratos IN, Hernández-Pérez E, Campos C, Aschner M, Santamaría A. Mol Neurobiol 59 620-642 (2022)
  65. Protein Quality Control Pathways at the Crossroad of Synucleinopathies. De Mattos EP, Wentink A, Nussbaum-Krammer C, Hansen C, Bergink S, Melki R, Kampinga HH. J Parkinsons Dis 10 369-382 (2020)
  66. Taking the measure of MicroED. Rodriguez JA, Eisenberg DS, Gonen T. Curr Opin Struct Biol 46 79-86 (2017)
  67. Understanding amyloid fibril formation using protein fragments: structural investigations via vibrational spectroscopy and solid-state NMR. Martial B, Lefèvre T, Auger M. Biophys Rev 10 1133-1149 (2018)
  68. Vertebrate food products as a potential source of prion-like α-synuclein. Killinger BA, Labrie V. NPJ Parkinsons Dis 3 33 (2017)
  69. The Proteome Folding Problem and Cellular Proteostasis. Powers ET, Gierasch LM. J Mol Biol 433 167197 (2021)
  70. Lipids as Trans-Acting Effectors for α-Synuclein in the Pathogenesis of Parkinson's Disease. Ikenaka K, Suzuki M, Mochizuki H, Nagai Y. Front Neurosci 13 693 (2019)
  71. Toward the Atomic Structure of PrPSc. Rodriguez JA, Jiang L, Eisenberg DS. Cold Spring Harb Perspect Biol 9 a031336 (2017)
  72. Navigating the dynamic landscape of alpha-synuclein morphology: a review of the physiologically relevant tetrameric conformation. Lucas HR, Fernández RD. Neural Regen Res 15 407-415 (2020)
  73. Targeting alpha-synuclein via the immune system in Parkinson's disease: Current vaccine therapies. Fleming SM, Davis A, Simons E. Neuropharmacology 202 108870 (2022)
  74. The complementarity of serial femtosecond crystallography and MicroED for structure determination from microcrystals. Zatsepin NA, Li C, Colasurd P, Nannenga BL. Curr Opin Struct Biol 58 286-293 (2019)
  75. Advances in methods for atomic resolution macromolecular structure determination. Thompson MC, Yeates TO, Rodriguez JA. F1000Res 9 F1000 Faculty Rev-667 (2020)
  76. Atomic resolution structure determination by the cryo-EM method MicroED. Liu S, Hattne J, Reyes FE, Sanchez-Martinez S, Jason de la Cruz M, Shi D, Gonen T. Protein Sci 26 8-15 (2017)
  77. Beyond protein structure determination with MicroED. Nguyen C, Gonen T. Curr Opin Struct Biol 64 51-58 (2020)
  78. Delivering the Promise of Gene Therapy with Nanomedicines in Treating Central Nervous System Diseases. Luo M, Lee LKC, Peng B, Choi CHJ, Tong WY, Voelcker NH. Adv Sci (Weinh) 9 e2201740 (2022)
  79. In Search of Effective Treatments Targeting α-Synuclein Toxicity in Synucleinopathies: Pros and Cons. Fouka M, Mavroeidi P, Tsaka G, Xilouri M. Front Cell Dev Biol 8 559791 (2020)
  80. The Neuroprotective Role of Protein Quality Control in Halting the Development of Alpha-Synuclein Pathology. Manecka DL, Vanderperre B, Fon EA, Durcan TM. Front Mol Neurosci 10 311 (2017)
  81. Alpha-Synuclein and Cognitive Decline in Parkinson Disease. Fan TS, Liu SC, Wu RM. Life (Basel) 11 1239 (2021)
  82. Consequences of variability in α-synuclein fibril structure on strain biology. Holec SAM, Liu SL, Woerman AL. Acta Neuropathol 143 311-330 (2022)
  83. Electron Diffraction of 3D Molecular Crystals. Saha A, Nia SS, Rodríguez JA. Chem Rev 122 13883-13914 (2022)
  84. Formation of Heterotypic Amyloids: α-Synuclein in Co-Aggregation. Bhasne K, Mukhopadhyay S. Proteomics 18 e1800059 (2018)
  85. Molecular pathology of neurodegenerative diseases by cryo-EM of amyloids. Scheres SHW, Ryskeldi-Falcon B, Goedert M. Nature 621 701-710 (2023)
  86. Understanding and controlling amyloid aggregation with chirality. Foley AR, Raskatov JA. Curr Opin Chem Biol 64 1-9 (2021)
  87. Adeno-Associated Virus Expression of α-Synuclein as a Tool to Model Parkinson's Disease: Current Understanding and Knowledge Gaps. Huntington TE, Srinivasan R. Aging Dis 12 1120-1137 (2021)
  88. Alpha-synuclein Immunization Strategies for Synucleinopathies in Clinical Studies: A Biological Perspective. Knecht L, Folke J, Dodel R, Ross JA, Albus A. Neurotherapeutics 19 1489-1502 (2022)
  89. Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A Minireview. Lermyte F. Life (Basel) 10 E320 (2020)
  90. Comparing the Folds of Prions and Other Pathogenic Amyloids. Flores-Fernández JM, Rathod V, Wille H. Pathogens 7 E50 (2018)
  91. High-Resolution Macromolecular Structure Determination by MicroED, a cryo-EM Method. Rodriguez JA, Gonen T. Methods Enzymol 579 369-392 (2016)
  92. α-Synuclein-mediated neurodegeneration in Dementia with Lewy bodies: the pathobiology of a paradox. Simon C, Soga T, Okano HJ, Parhar I. Cell Biosci 11 196 (2021)
  93. An Overview of Microcrystal Electron Diffraction (MicroED). Mu X, Gillman C, Nguyen C, Gonen T. Annu Rev Biochem 90 431-450 (2021)
  94. MicroED: conception, practice and future opportunities. Clabbers MTB, Shiriaeva A, Gonen T. IUCrJ 9 169-179 (2022)
  95. Monitoring α-synuclein aggregation. Estaun-Panzano J, Arotcarena ML, Bezard E. Neurobiol Dis 176 105966 (2023)
  96. Bacterial Protein Homeostasis Disruption as a Therapeutic Intervention. Khodaparast L, Wu G, Khodaparast L, Schmidt BZ, Rousseau F, Schymkowitz J. Front Mol Biosci 8 681855 (2021)
  97. Electron cryomicroscopy as a powerful tool in biomedical research. Quentin D, Raunser S. J Mol Med (Berl) 96 483-493 (2018)
  98. Macromolecular crystallography using microcrystal electron diffraction. Clabbers MTB, Xu H. Acta Crystallogr D Struct Biol 77 313-324 (2021)
  99. Mechanisms Underlying Neurodegenerative Disorders and Potential Neuroprotective Activity of Agrifood By-Products. Angeloni C, Malaguti M, Prata C, Freschi M, Barbalace MC, Hrelia S. Antioxidants (Basel) 12 94 (2022)
  100. Target Enzymes Considered for the Treatment of Alzheimer's Disease and Parkinson's Disease. Kim N, Lee HJ. Biomed Res Int 2020 2010728 (2020)
  101. The Evolution and the Advantages of MicroED. Nannenga BL, Bu G, Shi D. Front Mol Biosci 5 114 (2018)
  102. Development of Small Molecules Targeting α-Synuclein Aggregation: A Promising Strategy to Treat Parkinson's Disease. Peña-Díaz S, García-Pardo J, Ventura S. Pharmaceutics 15 839 (2023)
  103. Diffraction Techniques in Structural Biology. Egli M. Curr Protoc Nucleic Acid Chem 65 7.13.1-7.13.41 (2016)
  104. Examining the Toxicity of α-Synuclein in Neurodegenerative Disorders. Shan FY, Fung KM, Zieneldien T, Kim J, Cao C, Huang JH. Life (Basel) 11 1126 (2021)
  105. Growing and making nano- and microcrystals. Shoeman RL, Hartmann E, Schlichting I. Nat Protoc 18 854-882 (2023)
  106. Macromolecular Nanocrystal Structural Analysis with Electron and X-Rays: A Comparative Review. Khakurel KP, Angelov B, Andreasson J. Molecules 24 E3490 (2019)
  107. MicroED for the study of protein-ligand interactions and the potential for drug discovery. Clark LJ, Bu G, Nannenga BL, Gonen T. Nat Rev Chem 5 853-858 (2021)
  108. MicroED in drug discovery. Danelius E, Patel K, Gonzalez B, Gonen T. Curr Opin Struct Biol 79 102549 (2023)
  109. Pre-structured hydrophobic peptide β-strands: A universal amyloid trap? Sivanesam K, Andersen N. Arch Biochem Biophys 664 51-61 (2019)
  110. Advances in protein misfolding, amyloidosis and its correlation with human diseases. Kundu D, Prerna K, Chaurasia R, Bharty MK, Dubey VK. 3 Biotech 10 193 (2020)
  111. Amyloidogenicity at a Distance: How Distal Protein Regions Modulate Aggregation in Disease. Lucato CM, Lupton CJ, Halls ML, Ellisdon AM. J Mol Biol 429 1289-1304 (2017)
  112. Challenges with osmolytes as inhibitors of protein aggregation: Can nucleic acid aptamers provide an answer? Patel KA, Sethi R, Dhara AR, Roy I. Int J Biol Macromol 100 75-88 (2017)
  113. Current status and future prospects for enabling chemistry technology in the drug discovery process. Djuric SW, Hutchins CW, Talaty NN. F1000Res 5 2426 (2016)
  114. The young person's guide to the PDB. Minor W, Dauter Z, Jaskolski M. Postepy Biochem 62 242-249 (2016)
  115. Analysis and comparison of electron radiation damage assessments in Cryo-EM by single particle analysis and micro-crystal electron diffraction. Shi D, Huang R. Front Mol Biosci 9 988928 (2022)
  116. Light, Water, and Melatonin: The Synergistic Regulation of Phase Separation in Dementia. Loh D, Reiter RJ. Int J Mol Sci 24 5835 (2023)
  117. Multifaceted interactions mediated by intrinsically disordered regions play key roles in alpha synuclein aggregation. Khare SD, Chinchilla P, Baum J. Curr Opin Struct Biol 80 102579 (2023)
  118. Peptide-based approaches to directly target alpha-synuclein in Parkinson's disease. Allen SG, Meade RM, White Stenner LL, Mason JM. Mol Neurodegener 18 80 (2023)
  119. Targeting α-Synuclein in Parkinson's Disease by Induced Pluripotent Stem Cell Models. Spathopoulou A, Edenhofer F, Fellner L. Front Neurol 12 786835 (2021)
  120. The Synucleins and the Astrocyte. Myers AJ, Brahimi A, Jenkins IJ, Koob AO. Biology (Basel) 12 155 (2023)
  121. Advancements in Genetic and Biochemical Insights: Unraveling the Etiopathogenesis of Neurodegeneration in Parkinson's Disease. Ratan Y, Rajput A, Pareek A, Pareek A, Jain V, Sonia S, Farooqui Z, Kaur R, Singh G. Biomolecules 14 73 (2024)
  122. Alpha-Synuclein Contribution to Neuronal and Glial Damage in Parkinson's Disease. Saramowicz K, Siwecka N, Galita G, Kucharska-Lusina A, Rozpędek-Kamińska W, Majsterek I. Int J Mol Sci 25 360 (2023)
  123. Brain clearance of protein aggregates: a close-up on astrocytes. Giusti V, Kaur G, Giusto E, Civiero L. Mol Neurodegener 19 5 (2024)
  124. Energetics of cosolvent effect on peptide aggregation. Matubayasi N, Masutani K. Biophys Physicobiol 16 185-195 (2019)
  125. Extension of research data repository system to support direct compute access to biomedical datasets: enhancing Dataverse to support large datasets. McKinney B, Meyer PA, Crosas M, Sliz P. Ann N Y Acad Sci 1387 95-104 (2017)
  126. Interactions of amyloidogenic proteins with mitochondrial protein import machinery in aging-related neurodegenerative diseases. Reed AL, Mitchell W, Alexandrescu AT, Alder NN. Front Physiol 14 1263420 (2023)
  127. The Bidirectional Interplay of α-Synuclein with Lipids in the Central Nervous System and Its Implications for the Pathogenesis of Parkinson's Disease. Battis K, Xiang W, Winkler J. Int J Mol Sci 24 13270 (2023)
  128. Update on Nonhuman Primate Models of Brain Disease and Related Research Tools. Qiao N, Ma L, Zhang Y, Wang L. Biomedicines 11 2516 (2023)

Articles citing this publication (179)

  1. Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein. Tuttle MD, Comellas G, Nieuwkoop AJ, Covell DJ, Berthold DA, Kloepper KD, Courtney JM, Kim JK, Barclay AM, Kendall A, Wan W, Stubbs G, Schwieters CD, Lee VM, George JM, Rienstra CM. Nat Struct Mol Biol 23 409-415 (2016)
  2. Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers. Fusco G, Chen SW, Williamson PTF, Cascella R, Perni M, Jarvis JA, Cecchi C, Vendruscolo M, Chiti F, Cremades N, Ying L, Dobson CM, De Simone A. Science 358 1440-1443 (2017)
  3. Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel. Li B, Ge P, Murray KA, Sheth P, Zhang M, Nair G, Sawaya MR, Shin WS, Boyer DR, Ye S, Eisenberg DS, Zhou ZH, Jiang L. Nat Commun 9 3609 (2018)
  4. Amyloid fibril structure of α-synuclein determined by cryo-electron microscopy. Li Y, Zhao C, Luo F, Liu Z, Gui X, Luo Z, Zhang X, Li D, Liu C, Li X. Cell Res 28 897-903 (2018)
  5. EMDataBank unified data resource for 3DEM. Lawson CL, Patwardhan A, Baker ML, Hryc C, Garcia ES, Hudson BP, Lagerstedt I, Ludtke SJ, Pintilie G, Sala R, Westbrook JD, Berman HM, Kleywegt GJ, Chiu W. Nucleic Acids Res 44 D396-403 (2016)
  6. The CryoEM Method MicroED as a Powerful Tool for Small Molecule Structure Determination. Jones CG, Martynowycz MW, Hattne J, Fulton TJ, Stoltz BM, Rodriguez JA, Nelson HM, Gonen T. ACS Cent Sci 4 1587-1592 (2018)
  7. The cytotoxic Staphylococcus aureus PSMα3 reveals a cross-α amyloid-like fibril. Tayeb-Fligelman E, Tabachnikov O, Moshe A, Goldshmidt-Tran O, Sawaya MR, Coquelle N, Colletier JP, Landau M. Science 355 831-833 (2017)
  8. Structure-based inhibitors of tau aggregation. Seidler PM, Boyer DR, Rodriguez JA, Sawaya MR, Cascio D, Murray K, Gonen T, Eisenberg DS. Nat Chem 10 170-176 (2018)
  9. Structural basis of synaptic vesicle assembly promoted by α-synuclein. Fusco G, Pape T, Stephens AD, Mahou P, Costa AR, Kaminski CF, Kaminski Schierle GS, Vendruscolo M, Veglia G, Dobson CM, De Simone A. Nat Commun 7 12563 (2016)
  10. Structure insight of GSDMD reveals the basis of GSDMD autoinhibition in cell pyroptosis. Kuang S, Zheng J, Yang H, Li S, Duan S, Shen Y, Ji C, Gan J, Xu XW, Li J. Proc Natl Acad Sci U S A 114 10642-10647 (2017)
  11. 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)
  12. Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts. Strohäker T, Jung BC, Liou SH, Fernandez CO, Riedel D, Becker S, Halliday GM, Bennati M, Kim WS, Lee SJ, Zweckstetter M. Nat Commun 10 5535 (2019)
  13. 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)
  14. Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED. de la Cruz MJ, Hattne J, Shi D, Seidler P, Rodriguez J, Reyes FE, Sawaya MR, Cascio D, Weiss SC, Kim SK, Hinck CS, Hinck AP, Calero G, Eisenberg D, Gonen T. Nat Methods 14 399-402 (2017)
  15. Structures of fibrils formed by α-synuclein hereditary disease mutant H50Q reveal new polymorphs. Boyer DR, Li B, Sun C, Fan W, Sawaya MR, Jiang L, Eisenberg DS. Nat Struct Mol Biol 26 1044-1052 (2019)
  16. 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)
  17. Hydrogen positions in single nanocrystals revealed by electron diffraction. Palatinus L, Brázda P, Boullay P, Perez O, Klementová M, Petit S, Eigner V, Zaarour M, Mintova S. Science 355 166-169 (2017)
  18. The collection of MicroED data for macromolecular crystallography. Shi D, Nannenga BL, de la Cruz MJ, Liu J, Sawtelle S, Calero G, Reyes FE, Hattne J, Gonen T. Nat Protoc 11 895-904 (2016)
  19. Seeded assembly in vitro does not replicate the structures of α-synuclein filaments from multiple system atrophy. Lövestam S, Schweighauser M, Matsubara T, Murayama S, Tomita T, Ando T, Hasegawa K, Yoshida M, Tarutani A, Hasegawa M, Goedert M, Scheres SHW. FEBS Open Bio 11 999-1013 (2021)
  20. A short motif in the N-terminal region of α-synuclein is critical for both aggregation and function. Doherty CPA, Ulamec SM, Maya-Martinez R, Good SC, Makepeace J, Khan GN, van Oosten-Hawle P, Radford SE, Brockwell DJ. Nat Struct Mol Biol 27 249-259 (2020)
  21. Ab initio structure determination from prion nanocrystals at atomic resolution by MicroED. Sawaya MR, Rodriguez J, Cascio D, Collazo MJ, Shi D, Reyes FE, Hattne J, Gonen T, Eisenberg DS. Proc Natl Acad Sci U S A 113 11232-11236 (2016)
  22. Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity. Krotee P, Rodriguez JA, Sawaya MR, Cascio D, Reyes FE, Shi D, Hattne J, Nannenga BL, Oskarsson ME, Philipp S, Griner S, Jiang L, Glabe CG, Westermark GT, Gonen T, Eisenberg DS. Elife 6 e19273 (2017)
  23. Structural Ensembles of Membrane-bound α-Synuclein Reveal the Molecular Determinants of Synaptic Vesicle Affinity. Fusco G, De Simone A, Arosio P, Vendruscolo M, Veglia G, Dobson CM. Sci Rep 6 27125 (2016)
  24. O-GlcNAcylation of α-Synuclein at Serine 87 Reduces Aggregation without Affecting Membrane Binding. Lewis YE, Galesic A, Levine PM, De Leon CA, Lamiri N, Brennan CK, Pratt MR. ACS Chem Biol 12 1020-1027 (2017)
  25. Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp. Gallagher-Jones M, Glynn C, Boyer DR, Martynowycz MW, Hernandez E, Miao J, Zee CT, Novikova IV, Goldschmidt L, McFarlane HT, Helguera GF, Evans JE, Sawaya MR, Cascio D, Eisenberg DS, Gonen T, Rodriguez JA. Nat Struct Mol Biol 25 131-134 (2018)
  26. MicroED structures of HIV-1 Gag CTD-SP1 reveal binding interactions with the maturation inhibitor bevirimat. Purdy MD, Shi D, Chrustowicz J, Hattne J, Gonen T, Yeager M. Proc Natl Acad Sci U S A 115 13258-13263 (2018)
  27. Structural features of α-synuclein amyloid fibrils revealed by Raman spectroscopy. Flynn JD, McGlinchey RP, Walker RL, Lee JC. J Biol Chem 293 767-776 (2018)
  28. Solving a new R2lox protein structure by microcrystal electron diffraction. Xu H, Lebrette H, Clabbers MTB, Zhao J, Griese JJ, Zou X, Högbom M. Sci Adv 5 eaax4621 (2019)
  29. Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2. Guenther EL, Ge P, Trinh H, Sawaya MR, Cascio D, Boyer DR, Gonen T, Zhou ZH, Eisenberg DS. Nat Struct Mol Biol 25 311-319 (2018)
  30. Differential Membrane Binding and Seeding of Distinct α-Synuclein Fibrillar Polymorphs. Shrivastava AN, Bousset L, Renner M, Redeker V, Savistchenko J, Triller A, Melki R. Biophys J 118 1301-1320 (2020)
  31. Machining protein microcrystals for structure determination by electron diffraction. Duyvesteyn HME, Kotecha A, Ginn HM, Hecksel CW, Beale EV, de Haas F, Evans G, Zhang P, Chiu W, Stuart DI. Proc Natl Acad Sci U S A 115 9569-9573 (2018)
  32. 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)
  33. α-Synuclein Oligomers Induce Glutamate Release from Astrocytes and Excessive Extrasynaptic NMDAR Activity in Neurons, Thus Contributing to Synapse Loss. Trudler D, Sanz-Blasco S, Eisele YS, Ghatak S, Bodhinathan K, Akhtar MW, Lynch WP, Piña-Crespo JC, Talantova M, Kelly JW, Lipton SA. J Neurosci 41 2264-2273 (2021)
  34. The Impact of N-terminal Acetylation of α-Synuclein on Phospholipid Membrane Binding and Fibril Structure. Iyer A, Roeters SJ, Schilderink N, Hommersom B, Heeren RM, Woutersen S, Claessens MM, Subramaniam V. J Biol Chem 291 21110-21122 (2016)
  35. C-terminal truncation of α-synuclein promotes amyloid fibril amplification at physiological pH. van der Wateren IM, Knowles TPJ, Knowles TPJ, Buell AK, Dobson CM, Galvagnion C. Chem Sci 9 5506-5516 (2018)
  36. MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography. Clabbers MTB, Holmes S, Muusse TW, Vajjhala PR, Thygesen SJ, Malde AK, Hunter DJB, Croll TI, Flueckiger L, Nanson JD, Rahaman MH, Aquila A, Hunter MS, Liang M, Yoon CH, Zhao J, Zatsepin NA, Abbey B, Sierecki E, Gambin Y, Stacey KJ, Darmanin C, Kobe B, Xu H, Ve T. Nat Commun 12 2578 (2021)
  37. Native Top-Down Mass Spectrometry and Ion Mobility MS for Characterizing the Cobalt and Manganese Metal Binding of α-Synuclein Protein. Wongkongkathep P, Han JY, Choi TS, Yin S, Kim HI, Loo JA. J Am Soc Mass Spectrom 29 1870-1880 (2018)
  38. β-barrel Oligomers as Common Intermediates of Peptides Self-Assembling into Cross-β Aggregates. Sun Y, Ge X, Xing Y, Wang B, Ding F. Sci Rep 8 10353 (2018)
  39. X-ray Crystallographic Structure of Oligomers Formed by a Toxic β-Hairpin Derived from α-Synuclein: Trimers and Higher-Order Oligomers. Salveson PJ, Spencer RK, Nowick JS. J Am Chem Soc 138 4458-4467 (2016)
  40. Amyloid seeding of transthyretin by ex vivo cardiac fibrils and its inhibition. Saelices L, Chung K, Lee JH, Cohn W, Whitelegge JP, Benson MD, Eisenberg DS. Proc Natl Acad Sci U S A 115 E6741-E6750 (2018)
  41. A comprehensive analysis of SNCA-related genetic risk in sporadic parkinson disease. Pihlstrøm L, Blauwendraat C, Cappelletti C, Berge-Seidl V, Langmyhr M, Henriksen SP, van de Berg WDJ, Gibbs JR, Cookson MR, International Parkinson Disease Genomics Consortium, North American Brain Expression Consortium, Singleton AB, Nalls MA, Toft M. Ann Neurol 84 117-129 (2018)
  42. Common fibrillar spines of amyloid-β and human islet amyloid polypeptide revealed by microelectron diffraction and structure-based inhibitors. Krotee P, Griner SL, Sawaya MR, Cascio D, Rodriguez JA, Shi D, Philipp S, Murray K, Saelices L, Lee J, Seidler P, Glabe CG, Jiang L, Gonen T, Eisenberg DS. J Biol Chem 293 2888-2902 (2018)
  43. Structural insights into α-synuclein monomer-fibril interactions. Kumari P, Ghosh D, Vanas A, Fleischmann Y, Wiegand T, Jeschke G, Riek R, Eichmann C. Proc Natl Acad Sci U S A 118 e2012171118 (2021)
  44. MicroED structure of the NaK ion channel reveals a Na+ partition process into the selectivity filter. Liu S, Gonen T. Commun Biol 1 38 (2018)
  45. Skin hydration: interplay between molecular dynamics, structure and water uptake in the stratum corneum. Mojumdar EH, Pham QD, Topgaard D, Sparr E. Sci Rep 7 15712 (2017)
  46. Comparison of strategies for non-perturbing labeling of α-synuclein to study amyloidogenesis. Haney CM, Wissner RF, Warner JB, Wang YJ, Ferrie JJ, J Covell D, Karpowicz RJ, Lee VM, Petersson EJ. Org Biomol Chem 14 1584-1592 (2016)
  47. Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies. Lo CH, Lim CK, Ding Z, Wickramasinghe SP, Braun AR, Ashe KH, Rhoades E, Thomas DD, Sachs JN. Alzheimers Dement 15 1489-1502 (2019)
  48. 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)
  49. 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)
  50. Distinct C9orf72-Associated Dipeptide Repeat Structures Correlate with Neuronal Toxicity. Flores BN, Dulchavsky ME, Krans A, Sawaya MR, Paulson HL, Todd PK, Barmada SJ, Ivanova MI. PLoS One 11 e0165084 (2016)
  51. Familial Parkinson's point mutation abolishes multiple system atrophy prion replication. Woerman AL, Kazmi SA, Patel S, Aoyagi A, Oehler A, Widjaja K, Mordes DA, Olson SH, Prusiner SB. Proc Natl Acad Sci U S A 115 409-414 (2018)
  52. Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides. Reynolds NP, Adamcik J, Berryman JT, Handschin S, Zanjani AAH, Li W, Liu K, Zhang A, Mezzenga R. Nat Commun 8 1338 (2017)
  53. Inhibition of synucleinopathic seeding by rationally designed inhibitors. Sangwan S, Sahay S, Murray KA, Morgan S, Guenther EL, Jiang L, Williams CK, Vinters HV, Goedert M, Eisenberg DS. Elife 9 e46775 (2020)
  54. In situ protein micro-crystal fabrication by cryo-FIB for electron diffraction. Li X, Zhang S, Zhang J, Sun F. Biophys Rep 4 339-347 (2018)
  55. Getting the chemistry right: protonation, tautomers and the importance of H atoms in biological chemistry. Bax B, Chung CW, Edge C. Acta Crystallogr D Struct Biol 73 131-140 (2017)
  56. Optical Structural Analysis of Individual α-Synuclein Oligomers. Varela JA, Rodrigues M, De S, Flagmeier P, Gandhi S, Dobson CM, Klenerman D, Lee SF. Angew Chem Int Ed Engl 57 4886-4890 (2018)
  57. Probing the Origin of the Toxicity of Oligomeric Aggregates of α-Synuclein with Antibodies. Cascella R, Perni M, Chen SW, Fusco G, Cecchi C, Vendruscolo M, Chiti F, Dobson CM, De Simone A. ACS Chem Biol 14 1352-1362 (2019)
  58. Amphiphilic surface chemistry of fullerenols is necessary for inhibiting the amyloid aggregation of alpha-synuclein NACore. Sun Y, Kakinen A, Zhang C, Yang Y, Faridi A, Davis TP, Cao W, Ke PC, Ding F. Nanoscale 11 11933-11945 (2019)
  59. Identification of distinct pathological signatures induced by patient-derived α-synuclein structures in nonhuman primates. Bourdenx M, Nioche A, Dovero S, Arotcarena ML, Camus S, Porras G, Thiolat ML, Rougier NP, Prigent A, Aubert P, Bohic S, Sandt C, Laferrière F, Doudnikoff E, Kruse N, Mollenhauer B, Novello S, Morari M, Leste-Lasserre T, Damas IT, Goillandeau M, Perier C, Estrada C, Garcia-Carrillo N, Recasens A, Vaikath NN, El-Agnaf OMA, Herrero MT, Derkinderen P, Vila M, Obeso JA, Dehay B, Bezard E. Sci Adv 6 eaaz9165 (2020)
  60. Molecular determinants of the interaction of EGCG with ordered and disordered proteins. Fusco G, Sanz-Hernandez M, Ruggeri FS, Vendruscolo M, Dobson CM, De Simone A. Biopolymers 109 e23117 (2018)
  61. A Role of Cholesterol in Modulating the Binding of α-Synuclein to Synaptic-Like Vesicles. Man WK, De Simone A, Barritt JD, Vendruscolo M, Dobson CM, Fusco G. Front Neurosci 14 18 (2020)
  62. Inhibition of tau aggregation using a naturally-occurring cyclic peptide scaffold. Wang CK, Northfield SE, Huang YH, Ramos MC, Craik DJ. Eur J Med Chem 109 342-349 (2016)
  63. MicroED methodology and development. Nannenga BL. Struct Dyn 7 014304 (2020)
  64. Taking a Bite Out of Amyloid: Mechanistic Insights into α-Synuclein Degradation by Cathepsin L. McGlinchey RP, Dominah GA, Lee JC. Biochemistry 56 3881-3884 (2017)
  65. A cullin-RING ubiquitin ligase targets exogenous α-synuclein and inhibits Lewy body-like pathology. Gerez JA, Prymaczok NC, Rockenstein E, Herrmann US, Schwarz P, Adame A, Enchev RI, Courtheoux T, Boersema PJ, Riek R, Peter M, Aguzzi A, Masliah E, Picotti P. Sci Transl Med 11 eaau6722 (2019)
  66. Site-Specific Fluorescence Polarization for Studying the Disaggregation of α-Synuclein Fibrils by Small Molecules. Haney CM, Cleveland CL, Wissner RF, Owei L, Robustelli J, Daniels MJ, Canyurt M, Rodriguez P, Ischiropoulos H, Baumgart T, Petersson EJ. Biochemistry 56 683-691 (2017)
  67. Combustion-derived nanoparticles, the neuroenteric system, cervical vagus, hyperphosphorylated alpha synuclein and tau in young Mexico City residents. Calderón-Garcidueñas L, Reynoso-Robles R, Pérez-Guillé B, Mukherjee PS, Gónzalez-Maciel A. Environ Res 159 186-201 (2017)
  68. Prospecting for natural products by genome mining and microcrystal electron diffraction. Kim LJ, Ohashi M, Zhang Z, Tan D, Asay M, Cascio D, Rodriguez JA, Tang Y, Nelson HM. Nat Chem Biol 17 872-877 (2021)
  69. Comparing serial X-ray crystallography and microcrystal electron diffraction (MicroED) as methods for routine structure determination from small macromolecular crystals. Wolff AM, Young ID, Sierra RG, Brewster AS, Martynowycz MW, Nango E, Sugahara M, Nakane T, Ito K, Aquila A, Bhowmick A, Biel JT, Carbajo S, Cohen AE, Cortez S, Gonzalez A, Hino T, Im D, Koralek JD, Kubo M, Lazarou TS, Nomura T, Owada S, Samelson AJ, Tanaka T, Tanaka R, Thompson EM, van den Bedem H, Woldeyes RA, Yumoto F, Zhao W, Tono K, Boutet S, Iwata S, Gonen T, Sauter NK, Fraser JS, Thompson MC. IUCrJ 7 306-323 (2020)
  70. Computational insights into the role of α-strand/sheet in aggregation of α-synuclein. Balupuri A, Choi KE, Kang NS. Sci Rep 9 59 (2019)
  71. Nanoscale mosaicity revealed in peptide microcrystals by scanning electron nanodiffraction. Gallagher-Jones M, Ophus C, Bustillo KC, Boyer DR, Panova O, Glynn C, Zee CT, Ciston J, Mancia KC, Minor AM, Rodriguez JA. Commun Biol 2 26 (2019)
  72. On the appearance of carboxylates in electrostatic potential maps. Wang J. Protein Sci 26 396-402 (2017)
  73. Chiral recognition in amyloid fiber growth. Torbeev V, Grogg M, Ruiz J, Boehringer R, Schirer A, Hellwig P, Jeschke G, Hilvert D. J Pept Sci 22 290-304 (2016)
  74. De novo designed protein inhibitors of amyloid aggregation and seeding. Murray KA, Hu CJ, Griner SL, Pan H, Bowler JT, Abskharon R, Rosenberg GM, Cheng X, Seidler PM, Eisenberg DS. Proc Natl Acad Sci U S A 119 e2206240119 (2022)
  75. Ligand Incorporation into Protein Microcrystals for MicroED by On-Grid Soaking. Martynowycz MW, Gonen T. Structure 29 88-95.e2 (2021)
  76. Modulation of the extent of structural heterogeneity in α-synuclein fibrils by the small molecule thioflavin T. Kumar H, Singh J, Kumari P, Udgaonkar JB. J Biol Chem 292 16891-16903 (2017)
  77. Near-Infrared Emitting PbS Quantum Dots for in Vivo Fluorescence Imaging of the Thrombotic State in Septic Mouse Brain. Imamura Y, Yamada S, Tsuboi S, Nakane Y, Tsukasaki Y, Komatsuzaki A, Jin T. Molecules 21 E1080 (2016)
  78. Potent inhibitors of toxic alpha-synuclein identified via cellular time-resolved FRET biosensors. Braun AR, Liao EE, Horvath M, Kalra P, Acosta K, Young MC, Kochen NN, Lo CH, Brown R, Evans MD, Pomerantz WCK, Rhoades E, Luk K, Cornea RL, Thomas DD, Sachs JN. NPJ Parkinsons Dis 7 52 (2021)
  79. An enhanced recombinant amino-terminal acetylation system and novel in vivo high-throughput screen for molecules affecting α-synuclein oligomerisation. Eastwood TA, Baker K, Brooker HR, Frank S, Mulvihill DP. FEBS Lett 591 833-841 (2017)
  80. Demonstration of electron diffraction from membrane protein crystals grown in a lipidic mesophase after lamella preparation by focused ion beam milling at cryogenic temperatures. Polovinkin V, Khakurel K, Babiak M, Angelov B, Schneider B, Dohnalek J, Andreasson J, Hajdu J. J Appl Crystallogr 53 1416-1424 (2020)
  81. Experimental Phasing of MicroED Data Using Radiation Damage. Martynowycz MW, Hattne J, Gonen T. Structure 28 458-464.e2 (2020)
  82. Physical and Toxicological Profiles of Human IAPP Amyloids and Plaques. Kakinen A, Sun Y, Javed I, Faridi A, Pilkington EH, Faridi P, Purcell AW, Zhou R, Ding F, Lin S, Chun Ke P, Davis TP. Sci Bull (Beijing) 64 26-35 (2019)
  83. Femtosecond Hydration Map of Intrinsically Disordered α-Synuclein. Arya S, Singh AK, Bhasne K, Dogra P, Datta A, Das P, Mukhopadhyay S. Biophys J 114 2540-2551 (2018)
  84. Immunoglobulin Light Chains Form an Extensive and Highly Ordered Fibril Involving the N- and C-Termini. Piehl DW, Blancas-Mejía LM, Wall JS, Kennel SJ, Ramirez-Alvarado M, Rienstra CM. ACS Omega 2 712-720 (2017)
  85. The differential solvent exposure of N-terminal residues provides "fingerprints" of alpha-synuclein fibrillar polymorphs. Landureau M, Redeker V, Bellande T, Eyquem S, Melki R. J Biol Chem 296 100737 (2021)
  86. Time, space, and disorder in the expanding proteome universe. Minde DP, Dunker AK, Lilley KS. Proteomics 17 (2017)
  87. CGG repeats trigger translational frameshifts that generate aggregation-prone chimeric proteins. Wright SE, Rodriguez CM, Monroe J, Xing J, Krans A, Flores BN, Barsur V, Ivanova MI, Koutmou KS, Barmada SJ, Todd PK. Nucleic Acids Res 50 8674-8689 (2022)
  88. Curcumin Interacts with α-Synuclein Condensates To Inhibit Amyloid Aggregation under Phase Separation. Xu B, Chen J, Liu Y. ACS Omega 7 30281-30290 (2022)
  89. From electron crystallography of 2D crystals to MicroED of 3D crystals. Martynowycz MW, Gonen T. Curr Opin Colloid Interface Sci 34 9-16 (2018)
  90. MicroED: a versatile cryoEM method for structure determination. Nannenga BL, Gonen T. Emerg Top Life Sci 2 1-8 (2018)
  91. Molecular Insights into the Misfolding and Dimerization Dynamics of the Full-Length α-Synuclein from Atomistic Discrete Molecular Dynamics Simulations. Zhang Y, Wang Y, Liu Y, Wei G, Ding F, Sun Y. ACS Chem Neurosci 13 3126-3137 (2022)
  92. article-commentary Neurodegeneration: Taming tangled tau. Eisenberg DS, Sawaya MR. Nature 547 170-171 (2017)
  93. Self-Assembled Cyclic d,l-α-Peptides as Generic Conformational Inhibitors of the α-Synuclein Aggregation and Toxicity: In Vitro and Mechanistic Studies. Chemerovski-Glikman M, Rozentur-Shkop E, Richman M, Grupi A, Getler A, Cohen HY, Shaked H, Wallin C, Wärmländer SK, Haas E, Gräslund A, Chill JH, Rahimipour S. Chemistry 22 14236-14246 (2016)
  94. Single residue modulators of amyloid formation in the N-terminal P1-region of α-synuclein. Ulamec SM, Maya-Martinez R, Byrd EJ, Dewison KM, Xu Y, Willis LF, Sobott F, Heath GR, van Oosten Hawle P, Buchman VL, Radford SE, Brockwell DJ. Nat Commun 13 4986 (2022)
  95. C-terminal truncation modulates α-Synuclein's cytotoxicity and aggregation by promoting the interactions with membrane and chaperone. Zhang C, Pei Y, Zhang Z, Xu L, Liu X, Jiang L, Pielak GJ, Zhou X, Liu M, Li C. Commun Biol 5 798 (2022)
  96. Conformational Ensembles of α-Synuclein Derived Peptide with Different Osmolytes from Temperature Replica Exchange Sampling. Jamal S, Kumari A, Singh A, Goyal S, Grover A. Front Neurosci 11 684 (2017)
  97. Cross-seeding of alpha-synuclein aggregation by amyloid fibrils of food proteins. Vaneyck J, Segers-Nolten I, Broersen K, Claessens MMAE. J Biol Chem 296 100358 (2021)
  98. Dynamical Behavior of Human α-Synuclein Studied by Quasielastic Neutron Scattering. Fujiwara S, Araki K, Matsuo T, Yagi H, Yamada T, Shibata K, Mochizuki H. PLoS One 11 e0151447 (2016)
  99. Structure-Based Discovery of Small-Molecule Inhibitors of the Autocatalytic Proliferation of α-Synuclein Aggregates. Chia S, Faidon Brotzakis Z, Horne RI, Possenti A, Mannini B, Cataldi R, Nowinska M, Staats R, Linse S, Knowles TPJ, Habchi J, Vendruscolo M. Mol Pharm 20 183-193 (2023)
  100. The Route from the Folded to the Amyloid State: Exploring the Potential Energy Surface of a Drug-Like Miniprotein. Taricska N, Horváth D, Menyhárd DK, Ákontz-Kiss H, Noji M, So M, Goto Y, Fujiwara T, Perczel A. Chemistry 26 1968-1978 (2020)
  101. BetaSerpentine: a bioinformatics tool for reconstruction of amyloid structures. Bondarev SA, Bondareva OV, Zhouravleva GA, Kajava AV. Bioinformatics 34 599-608 (2018)
  102. Fluorescence spectroscopy reveals N-terminal order in fibrillar forms of α-synuclein. Haney CM, Petersson EJ. Chem Commun (Camb) 54 833-836 (2018)
  103. High-Pressure-Driven Reversible Dissociation of α-Synuclein Fibrils Reveals Structural Hierarchy. Piccirilli F, Plotegher N, Ortore MG, Tessari I, Brucale M, Spinozzi F, Beltramini M, Mariani P, Militello V, Lupi S, Perucchi A, Bubacco L. Biophys J 113 1685-1696 (2017)
  104. Intestine-derived α-synuclein initiates and aggravates pathogenesis of Parkinson's disease in Drosophila. Liu W, Lim KL, Tan EK. Transl Neurodegener 11 44 (2022)
  105. The Effect of (-)-Epigallocatechin-3-Gallate on the Amyloid-β Secondary Structure. Acharya A, Stockmann J, Beyer L, Rudack T, Nabers A, Gumbart JC, Gerwert K, Batista VS. Biophys J 119 349-359 (2020)
  106. The fold preference and thermodynamic stability of α-synuclein fibrils is encoded in the non-amyloid-β component region. Xu L, Bhattacharya S, Thompson D. Phys Chem Chem Phys 20 4502-4512 (2018)
  107. Effect of Osmolytes on Conformational Behavior of Intrinsically Disordered Protein α-Synuclein. Jahan I, Nayeem SM. Biophys J 117 1922-1934 (2019)
  108. Hydrogens and hydrogen-bond networks in macromolecular MicroED data. Clabbers MTB, Martynowycz MW, Hattne J, Gonen T. J Struct Biol X 6 100078 (2022)
  109. Understanding the dynamics of monomeric, dimeric, and tetrameric α-synuclein structures in water. Mane JY, Stepanova M. FEBS Open Bio 6 666-686 (2016)
  110. V63 and N65 of overexpressed α-synuclein are involved in mitochondrial dysfunction. Zhang H, Liu J, Wang X, Duan C, Wang X, Yang H. Brain Res 1642 308-318 (2016)
  111. Amyloid-like oligomerization of AIMP2 contributes to α-synuclein interaction and Lewy-like inclusion. Ham S, Yun SP, Kim H, Kim D, Seo BA, Kim H, Shin JY, Dar MA, Lee GH, Lee YI, Kim D, Kim S, Kweon HS, Shin JH, Ko HS, Lee Y. Sci Transl Med 12 eaax0091 (2020)
  112. Beam-sensitive metal-organic framework structure determination by microcrystal electron diffraction. Banihashemi F, Bu G, Thaker A, Williams D, Lin JYS, Nannenga BL. Ultramicroscopy 216 113048 (2020)
  113. Cathepsin K is a potent disaggregase of α-synuclein fibrils. McGlinchey RP, Lacy SM, Walker RL, Lee JC. Biochem Biophys Res Commun 529 1106-1111 (2020)
  114. Effects of sedimentation, microgravity, hydrodynamic mixing and air-water interface on α-synuclein amyloid formation. Zhou J, Ruggeri FS, Zimmermann MR, Meisl G, Longo G, Sekatskii SK, Knowles TPJ, Knowles TPJ, Dietler G. Chem Sci 11 3687-3693 (2020)
  115. Fragment-based determination of a proteinase K structure from MicroED data using ARCIMBOLDO_SHREDDER. Richards LS, Millán C, Miao J, Martynowycz MW, Sawaya MR, Gonen T, Borges RJ, Usón I, Rodriguez JA. Acta Crystallogr D Struct Biol 76 703-712 (2020)
  116. Mechanisms of enhanced aggregation and fibril formation of Parkinson's disease-related variants of α-synuclein. Ohgita T, Namba N, Kono H, Shimanouchi T, Saito H. Sci Rep 12 6770 (2022)
  117. Minimal Nucleation State of α-Synuclein Is Stabilized by Dynamic Threonine-Water Networks. Romo TD, Lewis AK, Braun AR, Grossfield A, Sachs JN. ACS Chem Neurosci 8 1859-1864 (2017)
  118. Small-Molecule-Induced Soluble Oligomers of α-Synuclein with Helical Structure. Fonseca-Ornelas L, Schmidt C, Camacho-Zarco AR, Fernandez CO, Becker S, Zweckstetter M. Chemistry 23 13010-13014 (2017)
  119. Synthesis and evaluation of temperature- and glucose-sensitive nanoparticles based on phenylboronic acid and N-vinylcaprolactam for insulin delivery. Wu JZ, Bremner DH, Li HY, Sun XZ, Zhu LM. Mater Sci Eng C Mater Biol Appl 69 1026-1035 (2016)
  120. α-Synuclein-Confocal Nanoscanning (ASYN-CONA), a Bead-Based Assay for Detecting Early-Stage α-Synuclein Aggregation. Pérez-Pi I, Evans DA, Horrocks MH, Pham NT, Dolt KS, Koszela J, Kunath T, Auer M. Anal Chem 91 5582-5590 (2019)
  121. Detergent-insoluble inclusion constitutes the first pathology in PFN1 transgenic rats. Yuan G, Cui S, Chen X, Song H, Huang C, Tong J, Yuan Z, Yu L, Xiong X, Zhao J, Huang B, Wu Q, Zhou Y, Chen G, Zhou H, Xia XG. J Neurochem 157 1244-1252 (2021)
  122. Neuronal identity defines α-synuclein and tau toxicity. Praschberger R, Kuenen S, Schoovaerts N, Kaempf N, Singh J, Janssens J, Swerts J, Nachman E, Calatayud C, Aerts S, Poovathingal S, Verstreken P. Neuron 111 1577-1590.e11 (2023)
  123. Novel engineered nanobodies specific for N-terminal region of alpha-synuclein recognize Lewy-body pathology and inhibit in-vitro seeded aggregation and toxicity. Hmila I, Vaikath NN, Majbour NK, Erskine D, Sudhakaran IP, Gupta V, Ghanem SS, Islam Z, Emara MM, Abdesselem HB, Kolatkar PR, Achappa DK, Vinardell T, El-Agnaf OMA. FEBS J 289 4657-4673 (2022)
  124. Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions. Cieplak AS. PLoS One 12 e0180905 (2017)
  125. Real-Time 3D Imaging and Inhibition Analysis of Various Amyloid Aggregations Using Quantum Dots. Lin X, Galaqin N, Tainaka R, Shimamori K, Kuragano M, Noguchi TQP, Tokuraku K. Int J Mol Sci 21 E1978 (2020)
  126. Supramolecular Assembly and Chirality of Synthetic Carbohydrate Materials. Gim S, Fittolani G, Nishiyama Y, Seeberger PH, Ogawa Y, Delbianco M. Angew Chem Int Ed Engl 59 22577-22583 (2020)
  127. WT and A53T α-Synuclein Systems: Melting Diagram and Its New Interpretation. Bokor M, Tantos Á, Tompa P, Han KH, Tompa K. Int J Mol Sci 21 E3997 (2020)
  128. Avidity-Based Method for the Efficient Generation of Monoubiquitinated Recombinant Proteins. Nelson SL, Li Y, Chen Y, Deshmukh L. J Am Chem Soc 145 7748-7752 (2023)
  129. Dimer crystallization of chiral proteoids. Wang PY, Mason TG. Phys Chem Chem Phys 19 7167-7175 (2017)
  130. Dissecting the Self-assembly Dynamics of Imperfect Repeats in α-Synuclein. Huang F, Wang Y, Zhang Y, Wang C, Lian J, Ding F, Sun Y. J Chem Inf Model 63 3591-3600 (2023)
  131. Long-range Regulation of Partially Folded Amyloidogenic Peptides. Bhattacharya S, Xu L, Thompson D. Sci Rep 10 7597 (2020)
  132. MicroED Structure of a Protoglobin Reactive Carbene Intermediate. Danelius E, Porter NJ, Unge J, Arnold FH, Gonen T. J Am Chem Soc 145 7159-7165 (2023)
  133. Rapid Structural Analysis of a Synthetic Non-canonical Amino Acid by Microcrystal Electron Diffraction. Gleason PR, Nannenga BL, Mills JH. Front Mol Biosci 7 609999 (2020)
  134. Recent Developments Toward Integrated Metabolomics Technologies (UHPLC-MS-SPE-NMR and MicroED) for Higher-Throughput Confident Metabolite Identifications. Ghosh R, Bu G, Nannenga BL, Sumner LW. Front Mol Biosci 8 720955 (2021)
  135. Threonine Cavities Are Targetable Motifs That Control Alpha-Synuclein Fibril Growth. Nathan Kochen N, Vasandani V, Seaney D, Pandey AK, Walters MA, Braun AR, Sachs JN. ACS Chem Neurosci 13 2646-2657 (2022)
  136. α-synuclein folds: the cards are on the table. Peelaerts W, Baekelandt V. Nat Struct Mol Biol 23 359-360 (2016)
  137. Ab Initio Determination of Peptide Structures by MicroED. Zee CT, Saha A, Sawaya MR, Rodriguez JA. Methods Mol Biol 2215 329-348 (2021)
  138. Aggregation of a Parkinson's Disease-Related Peptide: When Does Urea Weaken Hydrophobic Interactions? Galamba N. ACS Chem Neurosci 13 1769-1781 (2022)
  139. Foldamers reveal and validate therapeutic targets associated with toxic α-synuclein self-assembly. Ahmed J, Fitch TC, Donnelly CM, Joseph JA, Ball TD, Bassil MM, Son A, Zhang C, Ledreux A, Horowitz S, Qin Y, Paredes D, Kumar S. Nat Commun 13 2273 (2022)
  140. 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)
  141. MicroED Sample Preparation and Data Collection For Protein Crystals. Bu G, Nannenga BL. Methods Mol Biol 2215 287-297 (2021)
  142. NACore Amyloid Formation in the Presence of Phospholipids. Pallbo J, Imai M, Gentile L, Takata SI, Olsson U, Sparr E. Front Physiol 11 592117 (2020)
  143. Protein and Small Molecule Structure Determination by the Cryo-EM Method MicroED. Danelius E, Gonen T. Methods Mol Biol 2305 323-342 (2021)
  144. Strong inhibition of peptide amyloid formation by a fatty acid. Pallbo J, Olsson U, Sparr E. Biophys J 120 4536-4546 (2021)
  145. Two Dimensional Oblique Molecular Packing within a Model Peptide Ribbon Aggregate. Kuczera S, Rüter A, Roger K, Olsson U. Chemphyschem 21 1519-1523 (2020)
  146. 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)
  147. Adsorption and decontamination of α-synuclein from medically and environmentally-relevant surfaces. Phan HTM, Bartz JC, Ayers J, Giasson BI, Schubert M, Rodenhausen KB, Kananizadeh N, Li Y, Bartelt-Hunt SL. Colloids Surf B Biointerfaces 166 98-107 (2018)
  148. Amyloid fibrils prepared using an acetylated and methyl amidated peptide model of the α-Synuclein NAC 71-82 amino acid stretch contain an additional cross-β structure also found in prion proteins. Näsström T, Andersson PO, Lejon C, Karlsson BCG. Sci Rep 9 15949 (2019)
  149. Assessment of Amyloid Forming Tendency of Peptide Sequences from Amyloid Beta and Tau Proteins Using Force-Field, Semi-Empirical, and Density Functional Theory Calculations. Muvva C, Murugan NA, Subramanian V. Int J Mol Sci 22 3244 (2021)
  150. Fragment-Based Ab Initio Phasing of Peptidic Nanocrystals by MicroED. Richards LS, Flores MD, Millán C, Glynn C, Zee CT, Sawaya MR, Gallagher-Jones M, Borges RJ, Usón I, Rodriguez JA. ACS Bio Med Chem Au 3 201-210 (2023)
  151. Geometrical principles of homomeric β-barrels and β-helices: Application to modeling amyloid protofilaments. Hayward S, Milner-White EJ. Proteins 85 1866-1881 (2017)
  152. Getting in charge of β-synuclein fibrillation. Landau M. J Biol Chem 292 16380-16381 (2017)
  153. Microcrystal Electron Diffraction for Molecular Design of Functional Non-Fullerene Acceptor Structures. Halaby S, Martynowycz M, Zhu Z, Tretiak S, Zhugayevych A, Gonen T, Seifrid M. Chem Mater 33 966-977 (2021)
  154. Morphological Determinants of Carbon Nanomaterial-Induced Amyloid Peptide Self-Assembly. Xing Y, Sun Y, Wang B, Ding F. Front Chem 8 160 (2020)
  155. Studying membrane proteins with MicroED. Gallenito MJ, Gonen T. Biochem Soc Trans 50 231-239 (2022)
  156. The "speed limit" for macromolecular crystal growth. Arias RJ, Kaiser JT, Rees DC. Protein Sci 27 1837-1841 (2018)
  157. Toward a Soluble Model System for the Amyloid State. Thomas NC, Bartlett GJ, Woolfson DN, Gellman SH. J Am Chem Soc 139 16434-16437 (2017)
  158. Atomic structures determined from digitally defined nanocrystalline regions. Gallagher-Jones M, Bustillo KC, Ophus C, Richards LS, Ciston J, Lee S, Minor AM, Rodriguez JA. IUCrJ 7 490-499 (2020)
  159. Beta-Barrel Detection for Medium Resolution Cryo-Electron Microscopy Density Maps Using Genetic Algorithms and Ray Tracing. Ng A, Si D. J Comput Biol 25 326-336 (2018)
  160. Determining the Location of the α-Synuclein Dimer Interface Using Native Top-Down Fragmentation and Isotope Depletion-Mass Spectrometry. Jeacock K, Chappard A, Gallagher KJ, Mackay CL, Kilgour DPA, Horrocks MH, Kunath T, Clarke DJ. J Am Soc Mass Spectrom 34 847-856 (2023)
  161. Improving data quality for three-dimensional electron diffraction by a post-column energy filter and a new crystal tracking method. Yang T, Xu H, Zou X. J Appl Crystallogr 55 1583-1591 (2022)
  162. In-vitro and in-silico investigation of protective mechanisms of crocin against E46K α-synuclein amyloid formation. Ghasemi Tigan M, Ghahghaei A, Lagzian M. Mol Biol Rep 46 4279-4292 (2019)
  163. Intramolecular interaction kinetically regulates fibril formation by human and mouse α-synuclein. Ohgita T, Kono H, Morita I, Oyama H, Shimanouchi T, Kobayashi N, Saito H. Sci Rep 13 10885 (2023)
  164. Invisible Killers. Volpicelli-Daley LA, Standaert DG. Mov Disord 31 44 (2016)
  165. Lipid-induced polymorphic amyloid fibril formation by α-synuclein. Singh BP, Morris RJ, Kunath T, MacPhee CE, Horrocks MH. Protein Sci 32 e4736 (2023)
  166. Parkinson's disease: Crystals of a toxic core. Goedert M, Cheng Y. Nature 525 458-459 (2015)
  167. Probing Skin Barrier Recovery on Molecular Level Following Acute Wounds: An In Vivo/Ex Vivo Study on Pigs. Mojumdar EH, Madsen LB, Hansson H, Taavoniku I, Kristensen K, Persson C, Morén AK, Mokso R, Schmidtchen A, Ruzgas T, Engblom J. Biomedicines 9 360 (2021)
  168. Rapid Scan Electron Paramagnetic Resonance Spectroscopy Is a Suitable Tool to Study Intermolecular Interactions of Intrinsically Disordered Protein. Dröden J, Drescher M. Biology (Basel) 12 79 (2023)
  169. Substitution of Met-38 to Ile in γ-synuclein found in two patients with amyotrophic lateral sclerosis induces aggregation into amyloid. Aubrey LD, Ninkina N, Ulamec SM, Abramycheva NY, Vasili E, Devine OM, Wilkinson M, Mackinnon E, Limorenko G, Walko M, Muwanga S, Amadio L, Peters OM, Illarioshkin SN, Outeiro TF, Ranson NA, Brockwell DJ, Buchman VL, Radford SE. Proc Natl Acad Sci U S A 121 e2309700120 (2024)
  170. Challenges in solving structures from radiation-damaged tomograms of protein nanocrystals assessed by simulation. Peck A, Yao Q, Brewster AS, Zwart PH, Heumann JM, Sauter NK, Jensen GJ. Acta Crystallogr D Struct Biol 77 572-586 (2021)
  171. Co-aggregation of α-synuclein with amyloid-β stabilizes β-sheet-rich oligomers and enhances the formation of β-barrels. Huang F, Liu Y, Wang Y, Xu J, Lian J, Zou Y, Wang C, Ding F, Sun Y. Phys Chem Chem Phys 25 31604-31614 (2023)
  172. Detergent-insoluble PFN1 inoculation expedites disease onset and progression in PFN1 transgenic rats. Cui S, Zhang T, Xiong X, Zhao J, Cao Q, Zhou H, Xia XG. Front Neurosci 17 1279259 (2023)
  173. Elucidation of Secondary Structure and Toxicity of α-Synuclein Oligomers and Fibrils Grown in the Presence of Phosphatidylcholine and Phosphatidylserine. Dou T, Matveyenka M, Kurouski D. ACS Chem Neurosci 14 3183-3191 (2023)
  174. Lighting Up Alpha-synuclein Oligomers. Richter F. EBioMedicine 29 3-4 (2018)
  175. Mechanistic Insights into Polyphenols' Aggregation Inhibition of α-Synuclein and Related Peptides. Martins GF, Nascimento C, Galamba N. ACS Chem Neurosci 14 1905-1920 (2023)
  176. Non-steric-zipper models for pathogenic α-synuclein conformers. Schuman B, Won A, Brand-Arzamendi K, Koprich JB, Wen XY, Howson PA, Brotchie JM, Yip CM. APL Bioeng 2 026105 (2018)
  177. SPEADI: Accelerated Analysis of IDP-Ion Interactions from MD-Trajectories. de Bruyn E, Dorn AE, Zimmermann O, Rossetti G. Biology (Basel) 12 581 (2023)
  178. Visualizing the Entire Range of Noncovalent Interactions in Nanocrystalline Hybrid Materials Using 3D Electron Diffraction. Luo Y, Clabbers MTB, Qiao J, Yuan Z, Yang W, Zou X. J Am Chem Soc 144 10817-10824 (2022)
  179. α-Synuclein pathology from the body to the brain: so many seeds so close to the central soil. Yang Y, Zhang Z. Neural Regen Res 19 1463-1472 (2024)


Quick links