en Experimental Neurobiology

Cited by CrossRef (159)

  1. P. Gubellini, P. Kachidian. Animal models of Parkinson's disease: An updated overview. Revue Neurologique 2015;171:750
    https://doi.org/10.1016/j.neurol.2015.07.011
  2. E. Caggiu, K. Paulus, G. Galleri, G. Arru, R. Manetti, G.P. Sechi, L.A. Sechi. Homologous HSV1 and alpha-synuclein peptides stimulate a T cell response in Parkinson's disease. Journal of Neuroimmunology 2017;310:26
    https://doi.org/10.1016/j.jneuroim.2017.06.004
  3. Mohammad A. A. Fakhree, Sjoerd A. J. Engelbertink, Kirsten A. van Leijenhorst-Groener, Christian Blum, Mireille M. A. E. Claessens. Cooperation of Helix Insertion and Lateral Pressure to Remodel Membranes. Biomacromolecules 2019;20:1217
    https://doi.org/10.1021/acs.biomac.8b01606
  4. Kurt A. Jellinger. Neuropathology and pathogenesis of extrapyramidal movement disorders: a critical update—I. Hypokinetic-rigid movement disorders. J Neural Transm 2019;126:933
    https://doi.org/10.1007/s00702-019-02028-6
  5. Chiara Fecchio, Luana Palazzi, Patrizia Polverino de Laureto. α-Synuclein and Polyunsaturated Fatty Acids: Molecular Basis of the Interaction and Implication in Neurodegeneration. Molecules 2018;23:1531
    https://doi.org/10.3390/molecules23071531
  6. Sindhu Menon, Rikke H Kofoed, Fadl Nabbouh, Kristiana Xhima, Yasmeen Al-Fahoum, Tammy Langman, Howard T J Mount, Lamya S Shihabuddin, S Pablo Sardi, Paul E Fraser, Joel C Watts, Isabelle Aubert, Anurag Tandon. Viral alpha-synuclein knockdown prevents spreading synucleinopathy. 2021;3
    https://doi.org/10.1093/braincomms/fcab247
  7. Emelie E. Aspholm, Irena Matečko-Burmann, Björn M. Burmann. Keeping α-Synuclein at Bay: A More Active Role of Molecular Chaperones in Preventing Mitochondrial Interactions and Transition to Pathological States?. Life 2020;10:289
    https://doi.org/10.3390/life10110289
  8. Andreas Beier, Thomas C. Schwarz, Dennis Kurzbach, Gerald Platzer, Francesca Tribuzio, Robert Konrat. Modulation of Correlated Segment Fluctuations in IDPs upon Complex Formation as an Allosteric Regulatory Mechanism. Journal of Molecular Biology 2018;430:2439
    https://doi.org/10.1016/j.jmb.2018.04.035
  9. Rosie Bell, Michele Vendruscolo. Modulation of the Interactions Between α-Synuclein and Lipid Membranes by Post-translational Modifications. Front. Neurol. 2021;12
    https://doi.org/10.3389/fneur.2021.661117
  10. Himanshu Chaudhary, Vinod Subramaniam, Mireille M. A. E. Claessens. Direct Visualization of Model Membrane Remodeling by α‐Synuclein Fibrillization. ChemPhysChem 2017;18:1620
    https://doi.org/10.1002/cphc.201700050
  11. Mayu S. Terakawa, Yuxi Lin, Misaki Kinoshita, Shingo Kanemura, Dai Itoh, Toshihiko Sugiki, Masaki Okumura, Ayyalusamy Ramamoorthy, Young-Ho Lee. Impact of membrane curvature on amyloid aggregation. Biochimica et Biophysica Acta (BBA) - Biomembranes 2018;1860:1741
    https://doi.org/10.1016/j.bbamem.2018.04.012
  12. Elma Aflaki, Wendy Westbroek, Ellen Sidransky. The Complicated Relationship between Gaucher Disease and Parkinsonism: Insights from a Rare Disease. Neuron 2017;93:737
    https://doi.org/10.1016/j.neuron.2017.01.018
  13. Orkid Coskuner, Vladimir N. Uversky. Dancing protein clouds: Intrinsically disordered proteins in health and disease, Part A. 2017.
    https://doi.org/10.1016/bs.pmbts.2019.05.007
  14. Siyuan Zhang, Samantha A. Glukhova, Kim A. Caldwell, Guy A. Caldwell. NCEH-1 modulates cholesterol metabolism and protects against α-synuclein toxicity in a C. elegans model of Parkinson’s disease. 2017;26:3823
    https://doi.org/10.1093/hmg/ddx269
  15. Nisha Rani, Mohammad Mumtaz Alam, Azfar Jamal, Usama Bin Ghaffar, Suhel Parvez. Caenorhabditis elegans: A transgenic model for studying age-associated neurodegenerative diseases. Ageing Research Reviews 2023;91:102036
    https://doi.org/10.1016/j.arr.2023.102036
  16. Jobin Varkey, Ralf Langen. Membrane remodeling by amyloidogenic and non-amyloidogenic proteins studied by EPR. Journal of Magnetic Resonance 2017;280:127
    https://doi.org/10.1016/j.jmr.2017.02.014
  17. Yutaka Nakagawa, Shizuo Yamada. Metal homeostasis disturbances in neurodegenerative disorders, with special emphasis on Creutzfeldt-Jakob disease – Potential pathogenetic mechanism and therapeutic implications. Pharmacology & Therapeutics 2020;207:107455
    https://doi.org/10.1016/j.pharmthera.2019.107455
  18. Giorgia De Franceschi, Chiara Fecchio, Ronit Sharon, Anthony H.V. Schapira, Christos Proukakis, Vittorio Bellotti, Patrizia Polverino de Laureto. α-Synuclein structural features inhibit harmful polyunsaturated fatty acid oxidation, suggesting roles in neuroprotection. Journal of Biological Chemistry 2017;292:6927
    https://doi.org/10.1074/jbc.M116.765149
  19. Peter J. Chung, Hyeondo Luke Hwang, Benjamin R. Slaw, Alessandra Leong, Erin J. Adams, Ka Yee C. Lee. The C‐Terminal Domain of α‐Synuclein Confers Steric Stabilization on Synaptic Vesicle‐Like Surfaces. Adv Materials Inter 2020;7
    https://doi.org/10.1002/admi.201902151
  20. A.R. Carta, L. Boi, A. Pisanu, M.F. Palmas, E. Carboni, A. De Simone. Advances in modelling alpha-synuclein-induced Parkinson’s diseases in rodents: Virus-based models versus inoculation of exogenous preformed toxic species. Journal of Neuroscience Methods 2020;338:108685
    https://doi.org/10.1016/j.jneumeth.2020.108685
  21. Daniel Jacobs, David P. Hoogerheide, Amandine Rovini, Zhiping Jiang, Jennifer C. Lee, Tatiana K. Rostovtseva, Sergey M. Bezrukov. Probing Membrane Association of α-Synuclein Domains with VDAC Nanopore Reveals Unexpected Binding Pattern. Sci Rep 2019;9
    https://doi.org/10.1038/s41598-019-40979-8
  22. Yong Qi Leong, Rhun Yian Koh, Soi Moi Chye, Khuen Yen Ng. Unravelling the genetic links between Parkinson’s disease and lung cancer. 2023;404:551
    https://doi.org/10.1515/hsz-2022-0228
  23. Elka R. Georgieva. Nanoscale lipid membrane mimetics in spin-labeling and electron paramagnetic resonance spectroscopy studies of protein structure and function. 2017;6:75
    https://doi.org/10.1515/ntrev-2016-0080
  24. Shruti Arya, Avinash K. Singh, Karishma Bhasne, Priyanka Dogra, Anindya Datta, Payel Das, Samrat Mukhopadhyay. Femtosecond Hydration Map of Intrinsically Disordered α-Synuclein. Biophysical Journal 2018;114:2540
    https://doi.org/10.1016/j.bpj.2018.04.028
  25. Mario Gonzalez-Garcia, Giuliana Fusco, Alfonso De Simone. Metal interactions of α-synuclein probed by NMR amide-proton exchange. Front. Chem. 2023;11
    https://doi.org/10.3389/fchem.2023.1167766
  26. Jason Candreva, Edward Chau, Margaret E. Rice, Jin Ryoun Kim. Interactions between Soluble Species of β-Amyloid and α-Synuclein Promote Oligomerization while Inhibiting Fibrillization. Biochemistry 2020;59:425
    https://doi.org/10.1021/acs.biochem.9b00655
  27. Carlos Navarro-Paya, Maximo Sanz-Hernandez, Alfonso De Simone. Plasticity of Membrane Binding by the Central Region of α-Synuclein. Front. Mol. Biosci. 2022;9
    https://doi.org/10.3389/fmolb.2022.857217
  28. Simona Daniele, Deborah Pietrobono, Jonathan Fusi, Annalisa Lo Gerfo, Eugenio Cerri, Lucia Chico, Caterina Iofrida, Lucia Petrozzi, Filippo Baldacci, Chiara Giacomelli, Fabio Galetta, Gabriele Siciliano, Ubaldo Bonuccelli, Maria L. Trincavelli, Ferdinando Franzoni, Claudia Martini. α-Synuclein Aggregated with Tau and β-Amyloid in Human Platelets from Healthy Subjects: Correlation with Physical Exercise. Front. Aging Neurosci. 2018;10
    https://doi.org/10.3389/fnagi.2018.00017
  29. Gina M. Moriarty, Michael P. Olson, Tamr B. Atieh, Maria K. Janowska, Sagar D. Khare, Jean Baum. A pH-dependent switch promotes β-synuclein fibril formation via glutamate residues. Journal of Biological Chemistry 2017;292:16368
    https://doi.org/10.1074/jbc.M117.780528
  30. Niloofar Rezaeian, Niloofar Shirvanizadeh, Soheila Mohammadi, Maryam Nikkhah, Seyed Shahriar Arab. The inhibitory effects of biomimetically designed peptides on α-synuclein aggregation. Archives of Biochemistry and Biophysics 2017;634:96
    https://doi.org/10.1016/j.abb.2017.09.015
  31. Gerald H. Lushington, Frances E. S. Parker, Thomas H. W. Lushington, Nora M. Wallace. Computational Modeling of Drugs Against Alzheimer’s Disease. 2017.
    https://doi.org/10.1007/978-1-4939-7404-7_20
  32. Rosemary B. Cornell, Neale D. Ridgway. CTP:phosphocholine cytidylyltransferase: Function, regulation, and structure of an amphitropic enzyme required for membrane biogenesis. Progress in Lipid Research 2015;59:147
    https://doi.org/10.1016/j.plipres.2015.07.001
  33. Meraj Ramezani, Marcus M. Wilkes, Tapojyoti Das, David Holowka, David Eliezer, Barbara Baird. Regulation of exocytosis and mitochondrial relocalization by Alpha-synuclein in a mammalian cell model. npj Parkinsons Dis. 2019;5
    https://doi.org/10.1038/s41531-019-0084-6
  34. Damilare D. Akintade, Bhabatosh Chaudhuri. The effect of copy number on α-synuclein’s toxicity and its protective role in Bax-induced apoptosis, in yeast. 2020;40
    https://doi.org/10.1042/BSR20201912
  35. Manuel Menéndez-González, Huber Padilla-Zambrano, Cristina Tomás-Zapico, Benjamin García. Clearing Extracellular Alpha-Synuclein from Cerebrospinal Fluid: A New Therapeutic Strategy in Parkinson’s Disease. Brain Sciences 2018;8:52
    https://doi.org/10.3390/brainsci8040052
  36. Katsuya Araki, Kotomi Sugawara, Eri H. Hayakawa, Kumi Ubukawa, Isuzu Kobayashi, Hideki Wakui, Naoto Takahashi, Kenichi Sawada, Hideki Mochizuki, Wataru Nunomura. The localization of α-synuclein in the process of differentiation of human erythroid cells. Int J Hematol 2018;108:130
    https://doi.org/10.1007/s12185-018-2457-8
  37. Angelo Gallo, Silvia Mansueto, Alessandro Emendato, Giuliana Fusco, Alfonso De Simone. α-Synuclein and Mitochondria: Probing the Dynamics of Disordered Membrane-protein Regions Using Solid-State Nuclear Magnetic Resonance. JACS Au 2024
    https://doi.org/10.1021/jacsau.4c00323
  38. Ricardo Gaspar, Jon Pallbo, Ulrich Weininger, Sara Linse, Emma Sparr. Reprint of “Ganglioside lipids accelerate α-synuclein amyloid formation”. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2019;1867:508
    https://doi.org/10.1016/j.bbapap.2019.02.003
  39. Julie K. Andersen, Shankar Chinta. Advances in Geroscience. 2019.
    https://doi.org/10.1007/978-3-319-23246-1_8
  40. David Snead, David Eliezer. Intrinsically Disordered Proteins. 2019.
    https://doi.org/10.1016/bs.mie.2018.08.005
  41. Alysia Ross, Viktoria Xing, Ting Ting Wang, Samantha C. Bureau, Giovana A. Link, Teresa Fortin, Hui Zhang, Shawn Hayley, Hongyu Sun. Alleviating toxic α-Synuclein accumulation by membrane depolarization: evidence from an in vitro model of Parkinson’s disease. Mol Brain 2020;13
    https://doi.org/10.1186/s13041-020-00648-8
  42. Peter J. Chung, Qingteng Zhang, Hyeondo Luke Hwang, Alessandra Leong, Piotr Maj, Robert Szczygiel, Eric M. Dufresne, Suresh Narayanan, Erin J. Adams, Ka Yee C. Lee. α-Synuclein Sterically Stabilizes Spherical Nanoparticle-Supported Lipid Bilayers. ACS Appl. Bio Mater. 2019;2:1413
    https://doi.org/10.1021/acsabm.8b00774
  43. Kseniia Afitska, Anna Fucikova, Volodymyr V. Shvadchak, Dmytro A. Yushchenko. α-Synuclein aggregation at low concentrations. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2019;1867:701
    https://doi.org/10.1016/j.bbapap.2019.05.003
  44. Timothy S. Jarvela, Hoa A. Lam, Michael Helwig, Nikolai Lorenzen, Daniel E. Otzen, Pamela J. McLean, Nigel T. Maidment, Iris Lindberg. The neural chaperone proSAAS blocks α-synuclein fibrillation and neurotoxicity. Proc. Natl. Acad. Sci. U.S.A. 2016;113
    https://doi.org/10.1073/pnas.1601091113
  45. Giuliana Fusco, Maximo Sanz-Hernandez, Alfonso De Simone. Order and disorder in the physiological membrane binding of α-synuclein. Current Opinion in Structural Biology 2018;48:49
    https://doi.org/10.1016/j.sbi.2017.09.004
  46. Roberta Cascella, Michele Perni, Serene W. Chen, Giuliana Fusco, Cristina Cecchi, Michele Vendruscolo, Fabrizio Chiti, Christopher M. Dobson, Alfonso De Simone. Probing the Origin of the Toxicity of Oligomeric Aggregates of α-Synuclein with Antibodies. ACS Chem. Biol. 2019;14:1352
    https://doi.org/10.1021/acschembio.9b00312
  47. Katarzyna Makasewicz, Sara Linse, Emma Sparr. Interplay of α-synuclein with Lipid Membranes: Cooperative Adsorption, Membrane Remodeling and Coaggregation. JACS Au 2024;4:1250
    https://doi.org/10.1021/jacsau.3c00579
  48. Martin Kiechle, Veselin Grozdanov, Karin M. Danzer. The Role of Lipids in the Initiation of α-Synuclein Misfolding. Front. Cell Dev. Biol. 2020;8
    https://doi.org/10.3389/fcell.2020.562241
  49. Mark R. Cookson. Disease-Modifying Targets in Neurodegenerative Disorders. 2020.
    https://doi.org/10.1016/B978-0-12-805120-7.00007-5
  50. Catherine Xu, Marta Castellana-Cruz, Serene Chen, Zhen Du, Georg Meisl, Aviad Levin, Benedetta Mannini, Laura Itzhaki, Tuomas Knowles, Christopher Dobson, Nunilo Cremades, Janet Kumita. The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity. Molecules 2022;27:1293
    https://doi.org/10.3390/molecules27041293
  51. Tae Su Choi, Jong Yoon Han, Chae Eun Heo, Sun Woo Lee, Hugh I. Kim. Electrostatic and hydrophobic interactions of lipid-associated α-synuclein: The role of a water-limited interfaces in amyloid fibrillation. Biochimica et Biophysica Acta (BBA) - Biomembranes 2018;1860:1854
    https://doi.org/10.1016/j.bbamem.2018.02.007
  52. I. Golomidov, O. Bolshakova, A. Komissarov, V. Sharoyko, Е. Slepneva, A. Slobodina, E. Latypova, O. Zherebyateva, T. Tennikova, S. Sarantseva. The neuroprotective effect of fullerenols on a model of Parkinson’s disease in Drosophila melanogaster. Biochemical and Biophysical Research Communications 2020;523:446
    https://doi.org/10.1016/j.bbrc.2019.12.075
  53. Magdalena I. Ivanova, Yuxi Lin, Young-Ho Lee, Jie Zheng, Ayyalusamy Ramamoorthy. Biophysical processes underlying cross-seeding in amyloid aggregation and implications in amyloid pathology. Biophysical Chemistry 2021;269:106507
    https://doi.org/10.1016/j.bpc.2020.106507
  54. Ranit Pariary, Dipita Bhattacharyya, Anirban Bhunia. Mitochondrial-membrane association of α-synuclein: Pros and cons in consequence of Parkinson's disease pathophysiology. Gene Reports 2019;16:100423
    https://doi.org/10.1016/j.genrep.2019.100423
  55. Ge Gao, Zhipeng Wang, Lingling Lu, Chunli Duan, Xiaomin Wang, Hui Yang. Morphological analysis of mitochondria for evaluating the toxicity of α-synuclein in transgenic mice and isolated preparations by atomic force microscopy. Biomedicine & Pharmacotherapy 2017;96:1380
    https://doi.org/10.1016/j.biopha.2017.11.057
  56. Neda Valian, Mansooreh Heravi, Abolhassan Ahmadiani, Leila Dargahi. Effect of methamphetamine on rat primary midbrain cells; mitochondrial biogenesis as a compensatory response. Neuroscience 2019;406:278
    https://doi.org/10.1016/j.neuroscience.2019.03.016
  57. Tapojyoti Das, David Eliezer. Membrane interactions of intrinsically disordered proteins: The example of alpha-synuclein. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2019;1867:879
    https://doi.org/10.1016/j.bbapap.2019.05.001
  58. Laura Boi, Augusta Pisanu, Maria Francesca Palmas, Giuliana Fusco, Ezio Carboni, Maria Antonietta Casu, Valentina Satta, Maria Scherma, Elzbieta Janda, Ignazia Mocci, Giovanna Mulas, Anna Ena, Saturnino Spiga, Paola Fadda, Alfonso De Simone, Anna R. Carta. Modeling Parkinson’s Disease Neuropathology and Symptoms by Intranigral Inoculation of Preformed Human α-Synuclein Oligomers. IJMS 2020;21:8535
    https://doi.org/10.3390/ijms21228535
  59. E. Srinivasan, G. Chandrasekhar, P. Chandrasekar, K. Anbarasu, A. S. Vickram, Rohini Karunakaran, R. Rajasekaran, P. S. Srikumar. Alpha-Synuclein Aggregation in Parkinson's Disease. Front. Med. 2021;8
    https://doi.org/10.3389/fmed.2021.736978
  60. Martin Soste, Konstantina Charmpi, Fabienne Lampert, Juan Atilio Gerez, Marc van Oostrum, Liliana Malinovska, Paul Jonathan Boersema, Natalia Cecilia Prymaczok, Roland Riek, Matthias Peter, Stefano Vanni, Andreas Beyer, Paola Picotti. Proteomics-Based Monitoring of Pathway Activity Reveals that Blocking Diacylglycerol Biosynthesis Rescues from Alpha-Synuclein Toxicity. Cell Systems 2019;9:309
    https://doi.org/10.1016/j.cels.2019.07.010
  61. Guohua Lv, Myung Soo Ko, Tapojyoti Das, David Eliezer. Molecular and functional interactions of alpha-synuclein with Rab3a. Journal of Biological Chemistry 2022;298:102239
    https://doi.org/10.1016/j.jbc.2022.102239
  62. Wing K. Man, Alfonso De Simone, Joseph D. Barritt, Michele Vendruscolo, Christopher M. Dobson, Giuliana Fusco. A Role of Cholesterol in Modulating the Binding of α-Synuclein to Synaptic-Like Vesicles. Front. Neurosci. 2020;14
    https://doi.org/10.3389/fnins.2020.00018
  63. Wojciech Bobela, Patrick Aebischer, Bernard Schneider. Αlpha-Synuclein as a Mediator in the Interplay between Aging and Parkinson’s Disease. Biomolecules 2015;5:2675
    https://doi.org/10.3390/biom5042675
  64. Marcia Cristina Teixeira dos Santos, Rosie Bell, Andre Nogueira da Costa. Recent Developments in Circulating Biomarkers in Parkinson’s Disease: The Potential Use of Mirnas in A Clinical Setting. Bioanalysis 2016;8:2497
    https://doi.org/10.4155/bio-2016-0166
  65. Yoon‐Hui Sung, David Eliezer. Structure and dynamics of the extended‐helix state of alpha‐synuclein: Intrinsic lability of the linker region. Protein Science 2018;27:1314
    https://doi.org/10.1002/pro.3426
  66. Irem Nasir, Paulo L. Onuchic, Sergio R. Labra, Ashok A. Deniz. Single-molecule fluorescence studies of intrinsically disordered proteins and liquid phase separation. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2019;1867:980
    https://doi.org/10.1016/j.bbapap.2019.04.007
  67. Rosie Bell, Marta Castellana-Cruz, Aishwarya Nene, Rebecca J. Thrush, Catherine K. Xu, Janet R. Kumita, Michele Vendruscolo. Effects of N-terminal Acetylation on the Aggregation of Disease-related α-synuclein Variants. Journal of Molecular Biology 2023;435:167825
    https://doi.org/10.1016/j.jmb.2022.167825
  68. Ting Wang, Jesse C. Hay. Alpha-synuclein Toxicity in the Early Secretory Pathway: How It Drives Neurodegeneration in Parkinsons Disease. Front. Neurosci. 2015;9
    https://doi.org/10.3389/fnins.2015.00433
  69. Carlos Navarro-Paya, Maximo Sanz-Hernandez, Alfonso De Simone. In Silico Study of the Mechanism of Binding of the N-Terminal Region of α Synuclein to Synaptic-Like Membranes. Life 2020;10:98
    https://doi.org/10.3390/life10060098
  70. Daniel R. Whiten, Yukun Zuo, Laura Calo, Minee‐Liane Choi, Suman De, Patrick Flagmeier, David C. Wirthensohn, Franziska Kundel, Rohan T. Ranasinghe, Santiago E. Sanchez, Dilan Athauda, Steven F. Lee, Christopher M. Dobson, Sonia Gandhi, Maria‐Grazia Spillantini, David Klenerman, Mathew H. Horrocks. Nanoscopic Characterisation of Individual Endogenous Protein Aggregates in Human Neuronal Cells. ChemBioChem 2018;19:2033
    https://doi.org/10.1002/cbic.201800209
  71. Meredith E Jackrel, James Shorter. Engineering enhanced protein disaggregases for neurodegenerative disease. Prion 2015;9:90
    https://doi.org/10.1080/19336896.2015.1020277
  72. Enrico Zurlo, Pravin Kumar, Georg Meisl, Alexander J. Dear, Dipro Mondal, Mireille M. A. E. Claessens, Tuomas P. J. Knowles, Martina Huber, Dariush Hinderberger. In situ kinetic measurements of α-synuclein aggregation reveal large population of short-lived oligomers. PLoS ONE 2021;16:e0245548
    https://doi.org/10.1371/journal.pone.0245548
  73. Bani Kumar Pathak, Sandip Dey, Sukanya Mozumder, Jayati Sengupta. Membrane Proteins. 2021.
    https://doi.org/10.1016/bs.apcsb.2021.08.001
  74. Victorio Martin Pozo Devoto, Nicolas Dimopoulos, Matías Alloatti, María Belén Pardi, Trinidad M. Saez, María Gabriela Otero, Lucas Eneas Cromberg, Antonia Marín-Burgin, Maria Elida Scassa, Gorazd B. Stokin, Alejandro F. Schinder, Gustavo Sevlever, Tomás Luis Falzone. αSynuclein control of mitochondrial homeostasis in human-derived neurons is disrupted by mutations associated with Parkinson’s disease. Sci Rep 2017;7
    https://doi.org/10.1038/s41598-017-05334-9
  75. Daniele Colombo, Paraskevi Pnevmatikou, Elsa Melloni, Charlotte Keywood. Therapeutic innovation in Parkinson’s disease: a 2020 update on disease-modifying approaches. Expert Review of Neurotherapeutics 2020;20:1047
    https://doi.org/10.1080/14737175.2020.1800454
  76. Masoomeh Dadkhah, Milad Baziar, Nima Rezaei. The regulatory role of BDNF in neuroimmune axis function and neuroinflammation induced by chronic stress: A new therapeutic strategies for neurodegenerative disorders. Cytokine 2024;174:156477
    https://doi.org/10.1016/j.cyto.2023.156477
  77. Phuong H. Nguyen, Ayyalusamy Ramamoorthy, Bikash R. Sahoo, Jie Zheng, Peter Faller, John E. Straub, Laura Dominguez, Joan-Emma Shea, Nikolay V. Dokholyan, Alfonso De Simone, Buyong Ma, Ruth Nussinov, Saeed Najafi, Son Tung Ngo, Antoine Loquet, Mara Chiricotto, Pritam Ganguly, James McCarty, Mai Suan Li, Carol Hall, Yiming Wang, Yifat Miller, Simone Melchionna, Birgit Habenstein, Stepan Timr, Jiaxing Chen, Brianna Hnath, Birgit Strodel, Rakez Kayed, Sylvain Lesné, Guanghong Wei, Fabio Sterpone, Andrew J. Doig, Philippe Derreumaux. Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer’s Disease, Parkinson’s Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis. Chem. Rev. 2021;121:2545
    https://doi.org/10.1021/acs.chemrev.0c01122
  78. Nasir Uddin Mahbub, Md Minarul Islam, Seong-Tshool Hong, Hea-Jong Chung. Dysbiosis of the gut microbiota and its effect on α-synuclein and prion protein misfolding: consequences for neurodegeneration. Front. Cell. Infect. Microbiol. 2024;14
    https://doi.org/10.3389/fcimb.2024.1348279
  79. Suaad Abd-Elhadi, Misericordia Basora, Dolores Vilas, Eduardo Tolosa, Ronit Sharon. Total α-synuclein levels in human blood cells, CSF, and saliva determined by a lipid-ELISA. Anal Bioanal Chem 2016;408:7669
    https://doi.org/10.1007/s00216-016-9863-7
  80. Bryan A. Killinger, Ronald Melki, Patrik Brundin, Jeffrey H. Kordower. Endogenous alpha-synuclein monomers, oligomers and resulting pathology: let’s talk about the lipids in the room. npj Parkinsons Dis. 2019;5
    https://doi.org/10.1038/s41531-019-0095-3
  81. Atena Pakzadiyan, Seifollah Jalili. Computational Modeling of the Effect of Trifluoroethanol on the Conformation of α-Synuclein Peptide. J. Comput. Biophys. Chem. 2022;21:695
    https://doi.org/10.1142/S2737416522500296
  82. Caterina Masaracchia, Marilena Hnida, Ellen Gerhardt, Tomás Lopes da Fonseca, Anna Villar-Pique, Tiago Branco, Markus A. Stahlberg, Camin Dean, Claudio O. Fernández, Ira Milosevic, Tiago F. Outeiro. Membrane binding, internalization, and sorting of alpha-synuclein in the cell. acta neuropathol commun 2018;6
    https://doi.org/10.1186/s40478-018-0578-1
  83. Bruna Martins, Mónica Vieira, Cristina Delerue-Matos, Clara Grosso, Cristina Soares. Biological Potential, Gastrointestinal Digestion, Absorption, and Bioavailability of Algae-Derived Compounds with Neuroprotective Activity: A Comprehensive Review. Marine Drugs 2022;20:362
    https://doi.org/10.3390/md20060362
  84. Amber Tariq, JiaBei Lin, Megan M Noll, Mariana P Torrente, Korrie L Mack, Oscar Hernandez Murillo, Meredith E Jackrel, James Shorter. Potentiating Hsp104 activity via phosphomimetic mutations in the middle domain. 2018;18
    https://doi.org/10.1093/femsyr/foy042
  85. Lingjia Xu, Jiali Pu. Alpha-Synuclein in Parkinson’s Disease: From Pathogenetic Dysfunction to Potential Clinical Application. Parkinson's Disease 2016;2016:1
    https://doi.org/10.1155/2016/1720621
  86. Tatsunori Maekawa, Toshikuni Sasaoka, Sadahiro Azuma, Takafumi Ichikawa, Heather L. Melrose, Matthew J. Farrer, Fumiya Obata. Leucine-rich repeat kinase 2 (LRRK2) regulates α-synuclein clearance in microglia. BMC Neurosci 2016;17
    https://doi.org/10.1186/s12868-016-0315-2
  87. Xiaochu Lou, Jaewook Kim, Brenden J. Hawk, Yeon-Kyun Shin. α-Synuclein may cross-bridge v-SNARE and acidic phospholipids to facilitate SNARE-dependent vesicle docking. 2017;474:2039
    https://doi.org/10.1042/BCJ20170200
  88. David H. Johnson, Orianna H. Kou, Nicoletta Bouzos, Wade F. Zeno. Protein–membrane interactions: sensing and generating curvature. Trends in Biochemical Sciences 2024;49:401
    https://doi.org/10.1016/j.tibs.2024.02.005
  89. Brian Bicknell, Ann Liebert, Geoffrey Herkes. Parkinson’s Disease and Photobiomodulation: Potential for Treatment. JPM 2024;14:112
    https://doi.org/10.3390/jpm14010112
  90. Mohammad A. A. Fakhree, Ine Segers Nolten, Christian Blum, Mireille M. A. E. Claessens. Different Conformational Subensembles of the Intrinsically Disordered Protein α-Synuclein in Cells. J. Phys. Chem. Lett. 2018;9:1249
    https://doi.org/10.1021/acs.jpclett.8b00092
  91. Marco Emanuele, Evelina Chieregatti. Mechanisms of Alpha-Synuclein Action on Neurotransmission: Cell-Autonomous and Non-Cell Autonomous Role. Biomolecules 2015;5:865
    https://doi.org/10.3390/biom5020865
  92. Zachary M March, Katelyn Sweeney, Hanna Kim, Xiaohui Yan, Laura M Castellano, Meredith E Jackrel, JiaBei Lin, Edward Chuang, Edward Gomes, Corey W Willicott, Karolina Michalska, Robert P Jedrzejczak, Andrzej Joachimiak, Kim A Caldwell, Guy A Caldwell, Ophir Shalem, James Shorter. Therapeutic genetic variation revealed in diverse Hsp104 homologs. 2020;9
    https://doi.org/10.7554/eLife.57457
  93. Greta Musteikytė, Akhila K. Jayaram, Catherine K. Xu, Michele Vendruscolo, Georg Krainer, Tuomas P.J. Knowles. Interactions of α-synuclein oligomers with lipid membranes. Biochimica et Biophysica Acta (BBA) - Biomembranes 2021;1863:183536
    https://doi.org/10.1016/j.bbamem.2020.183536
  94. Pravin Hivare, Kratika Mujmer, Gitanjali Swarup, Sharad Gupta, Dhiraj Bhatia. Endocytic pathways of pathogenic protein aggregates in neurodegenerative diseases. Traffic 2023;24:434
    https://doi.org/10.1111/tra.12906
  95. Sima Shahraki, Saeed Shojaei, Siroos Shojaei. Inhibitory Role of β-Casein on the α-Synuclein Aggregation Associated with Parkinson’s Disease In Vitro. Int J Pept Res Ther 2018;24:179
    https://doi.org/10.1007/s10989-017-9600-x
  96. Mayu S. Terakawa, Young-Ho Lee, Misaki Kinoshita, Yuxi Lin, Toshihiko Sugiki, Naoya Fukui, Tatsuya Ikenoue, Yasushi Kawata, Yuji Goto. Membrane-induced initial structure of α-synuclein control its amyloidogenesis on model membranes. Biochimica et Biophysica Acta (BBA) - Biomembranes 2018;1860:757
    https://doi.org/10.1016/j.bbamem.2017.12.011
  97. Takahiro Watanabe-Nakayama, Maika Nawa, Hiroki Konno, Noriyuki Kodera, Toshio Ando, David B. Teplow, Kenjiro Ono. Self- and Cross-Seeding on α-Synuclein Fibril Growth Kinetics and Structure Observed by High-Speed Atomic Force Microscopy. ACS Nano 2020;14:9979
    https://doi.org/10.1021/acsnano.0c03074
  98. Shariq I. Sherwani, Haseeb A. Khan. Role of 5-hydroxymethylcytosine in neurodegeneration. Gene 2015;570:17
    https://doi.org/10.1016/j.gene.2015.06.052
  99. Malabika Maulik, Swarup Mitra, Abel Bult-Ito, Barbara E. Taylor, Elena M. Vayndorf. Behavioral Phenotyping and Pathological Indicators of Parkinson's Disease in C. elegans Models. Front. Genet. 2017;8
    https://doi.org/10.3389/fgene.2017.00077
  100. Zachary M. March, Korrie L. Mack, James Shorter. AAA+ Protein-Based Technologies to Counter Neurodegenerative Disease. Biophysical Journal 2019;116:1380
    https://doi.org/10.1016/j.bpj.2019.03.007
  101. Giuliana Fusco, Alfonso De Simone, Paolo Arosio, Michele Vendruscolo, Gianluigi Veglia, Christopher M. Dobson. Structural Ensembles of Membrane-bound α-Synuclein Reveal the Molecular Determinants of Synaptic Vesicle Affinity. Sci Rep 2016;6
    https://doi.org/10.1038/srep27125
  102. Hisae Sumi-Akamaru, Goichi Beck, Koei Shinzawa, Shinsuke Kato, Yuichi Riku, Mari Yoshida, Harutoshi Fujimura, Yoshihide Tsujimoto, Saburo Sakoda, Hideki Mochizuki. High expression of α-synuclein in damaged mitochondria with PLA2G6 dysfunction. acta neuropathol commun 2016;4
    https://doi.org/10.1186/s40478-016-0298-3
  103. Ivan A. Kuznetsov, Andrey V. Kuznetsov. Can the lack of fibrillar form of alpha-synuclein in Lewy bodies be explained by its catalytic activity?. Mathematical Biosciences 2022;344:108754
    https://doi.org/10.1016/j.mbs.2021.108754
  104. Lilit Gabrielyan, Honghui Liang, Artem Minalyan, Asa Hatami, Varghese John, Lixin Wang. Behavioral Deficits and Brain α-Synuclein and Phosphorylated Serine-129 α-Synuclein in Male and Female Mice Overexpressing Human α-Synuclein. JAD 2021;79:875
    https://doi.org/10.3233/JAD-200983
  105. Sung Yun Jung, Jong Min Choi, Maxime W.C. Rousseaux, Anna Malovannaya, Jean J. Kim, Joachim Kutzera, Yi Wang, Yin Huang, Weimin Zhu, Suman Maity, Huda Yahya Zoghbi, Jun Qin. An Anatomically Resolved Mouse Brain Proteome Reveals Parkinson Disease-relevant Pathways. Molecular & Cellular Proteomics 2017;16:581
    https://doi.org/10.1074/mcp.M116.061440
  106. Dale W. Prebble, Mingming Xu, George D. Mellick, Anthony R. Carroll. Sycosterol A, an α-Synuclein Inhibitory Sterol from the Australian Ascidian Sycozoa cerebriformis. J. Nat. Prod. 2021;84:3039
    https://doi.org/10.1021/acs.jnatprod.1c00768
  107. Rosemary B. Cornell. Membrane lipid compositional sensing by the inducible amphipathic helix of CCT. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 2016;1861:847
    https://doi.org/10.1016/j.bbalip.2015.12.022
  108. Elisa Caggiu, Kai Paulus, Giannina Arru, Rosanna Piredda, Gian Pietro Sechi, Leonardo A. Sechi. Humoral cross reactivity between α-synuclein and herpes simplex-1 epitope in Parkinson's disease, a triggering role in the disease?. Journal of Neuroimmunology 2016;291:110
    https://doi.org/10.1016/j.jneuroim.2016.01.007
  109. Cristian Follmer, Eduardo Coelho-Cerqueira, Danilo Y. Yatabe-Franco, Gabriel D.T. Araujo, Anderson S. Pinheiro, Gilberto B. Domont, David Eliezer. Oligomerization and Membrane-binding Properties of Covalent Adducts Formed by the Interaction of α-Synuclein with the Toxic Dopamine Metabolite 3,4-Dihydroxyphenylacetaldehyde (DOPAL). Journal of Biological Chemistry 2015;290:27660
    https://doi.org/10.1074/jbc.M115.686584
  110. Andrei Surguchov. . 2015.
    https://doi.org/10.1016/bs.ircmb.2015.07.007
  111. Timothy J. Collier, Kinshuk R. Srivastava, Craig Justman, Tom Grammatopoulous, Birgit Hutter-Paier, Manuela Prokesch, Daniel Havas, Jean-Christophe Rochet, Fang Liu, Kevin Jock, Patrícia de Oliveira, Georgia L. Stirtz, Ulf Dettmer, Caryl E. Sortwell, Mel B. Feany, Peter Lansbury, Lisa Lapidus, Katrina L. Paumier. Nortriptyline inhibits aggregation and neurotoxicity of alpha-synuclein by enhancing reconfiguration of the monomeric form. Neurobiology of Disease 2017;106:191
    https://doi.org/10.1016/j.nbd.2017.07.007
  112. Anne Baumann, Ana Jorge-Finnigan, Kunwar Jung-KC, Alexander Sauter, Istvan Horvath, Ludmilla A. Morozova-Roche, Aurora Martinez. Tyrosine Hydroxylase Binding to Phospholipid Membranes Prompts Its Amyloid Aggregation and Compromises Bilayer Integrity. Sci Rep 2016;6
    https://doi.org/10.1038/srep39488
  113. Ricardo Gaspar, Jon Pallbo, Ulrich Weininger, Sara Linse, Emma Sparr. Ganglioside lipids accelerate α-synuclein amyloid formation. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2018;1866:1062
    https://doi.org/10.1016/j.bbapap.2018.07.004
  114. Melissa Birol, Ana M. Melo. Untangling the Conformational Polymorphism of Disordered Proteins Associated With Neurodegeneration at the Single-Molecule Level. Front. Mol. Neurosci. 2020;12
    https://doi.org/10.3389/fnmol.2019.00309
  115. Silvia Mansueto, Giuliana Fusco, Alfonso De Simone. α-Synuclein and biological membranes: the danger of loving too much. Chem. Commun. 2023;59:8769
    https://doi.org/10.1039/D3CC01682J
  116. Giuliana Fusco, Tillmann Pape, Amberley D. Stephens, Pierre Mahou, Ana Rita Costa, Clemens F. Kaminski, Gabriele S. Kaminski Schierle, Michele Vendruscolo, Gianluigi Veglia, Christopher M. Dobson, Alfonso De Simone. Structural basis of synaptic vesicle assembly promoted by α-synuclein. Nat Commun 2016;7
    https://doi.org/10.1038/ncomms12563
  117. Orkid Coskuner-Weber, Vladimir Uversky. Insights into the Molecular Mechanisms of Alzheimer’s and Parkinson’s Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology. IJMS 2018;19:336
    https://doi.org/10.3390/ijms19020336
  118. Igor Dikiy, Bruno Fauvet, Ana Jovičić, Anne-Laure Mahul-Mellier, Carole Desobry, Farah El-Turk, Aaron D. Gitler, Hilal A. Lashuel, David Eliezer. Semisynthetic and in Vitro Phosphorylation of Alpha-Synuclein at Y39 Promotes Functional Partly Helical Membrane-Bound States Resembling Those Induced by PD Mutations. ACS Chem. Biol. 2016;11:2428
    https://doi.org/10.1021/acschembio.6b00539
  119. Luana Palazzi, Elena Bruzzone, Giovanni Bisello, Manuela Leri, Massimo Stefani, Monica Bucciantini, Patrizia Polverino de Laureto. Oleuropein aglycone stabilizes the monomeric α-synuclein and favours the growth of non-toxic aggregates. Sci Rep 2018;8
    https://doi.org/10.1038/s41598-018-26645-5
  120. Z. A. Goncharova, T. S. Kolmakova, M. A. Gelpei. Alpha-synuclein and oxidative stress enzymes as biomarkers of Parkinson’s disease. Neurochem. J. 2017;11:121
    https://doi.org/10.1134/S1819712417020052
  121. Tim E. Moors, Dragomir Milovanovic. Defining a Lewy Body: Running Up the Hill of Shifting Definitions and Evolving Concepts. JPD 2024;14:17
    https://doi.org/10.3233/JPD-230183
  122. Volodymyr V. Shvadchak, Oleksandr Kucherak, Kseniia Afitska, Dmytro Dziuba, Dmytro A. Yushchenko. Environmentally sensitive probes for monitoring protein-membrane interactions at nanomolar concentrations. Biochimica et Biophysica Acta (BBA) - Biomembranes 2017;1859:852
    https://doi.org/10.1016/j.bbamem.2017.01.021
  123. José Raphael Monteiro Neto, Vanderlei de Araújo Lima, Cristian Follmer. Fibrillation of α‐synuclein triggered by bacterial endotoxin and lipid vesicles is modulated by N‐terminal acetylation and familial Parkinson's disease mutations. The FEBS Journal 2024;291:1151
    https://doi.org/10.1111/febs.17027
  124. Mamatha Nagamadhu Murthy, Baragur Venkatanarayanasetty Shyamala. Ashwagandha- Withania somnifera (L.) Dunal as a multipotent neuroprotective remedy for genetically induced motor dysfunction and cellular toxicity in human neurodegenerative disease models of Drosophila. Journal of Ethnopharmacology 2024;318:116897
    https://doi.org/10.1016/j.jep.2023.116897
  125. Jet Shee Teng, Yin Yin Ooi, Soi Moi Chye, Anna Pick Kiong Ling, Rhun Yian Koh. Immunotherapies for Parkinson’s Disease: Progression of Clinical Development. CNSNDDT 2021;20:802
    https://doi.org/10.2174/1871527320666210526160926
  126. Cencen Liu, Yunfei Zhao, Huan Xi, Jie Jiang, Yang Yu, Wei Dong. The Membrane Interaction of Alpha-Synuclein. Front. Cell. Neurosci. 2021;15
    https://doi.org/10.3389/fncel.2021.633727
  127. Ana Belén Uceda, Rafael Ramis, Kris Pauwels, Miquel Adrover, Laura Mariño, Juan Frau, Bartolomé Vilanova. Understanding the effect of the membrane-mimetic micelles on the interplay between α-synuclein and Cu(II)/Cu(I) cations. Journal of Inorganic Biochemistry 2023;247:112344
    https://doi.org/10.1016/j.jinorgbio.2023.112344
  128. Meraj Ramezani, Alice Wagenknecht-Wiesner, Tong Wang, David A. Holowka, David Eliezer, Barbara A. Baird. Alpha synuclein modulates mitochondrial Ca2+ uptake from ER during cell stimulation and under stress conditions. npj Parkinsons Dis. 2023;9
    https://doi.org/10.1038/s41531-023-00578-x
  129. Ersoy Cholak, Saskia Bucciarelli, Katrine Bugge, Nicolai Tidemand Johansen, Bente Vestergaard, Lise Arleth, Birthe B. Kragelund, Annette E. Langkilde. Distinct α-Synuclein:Lipid Co-Structure Complexes Affect Amyloid Nucleation through Fibril Mimetic Behavior. Biochemistry 2019;58:5052
    https://doi.org/10.1021/acs.biochem.9b00925
  130. Liang Xu, Ruth Nussinov, Buyong Ma. Coupling of the non-amyloid-component (NAC) domain and the KTK(E/Q)GV repeats stabilize the α-synuclein fibrils. European Journal of Medicinal Chemistry 2016;121:841
    https://doi.org/10.1016/j.ejmech.2016.01.044
  131. Danail Minchev, Maria Kazakova, Victoria Sarafian. Neuroinflammation and Autophagy in Parkinson’s Disease—Novel Perspectives. IJMS 2022;23:14997
    https://doi.org/10.3390/ijms232314997
  132. Neha Jain, Dominic Narang, Karishma Bhasne, Vijit Dalal, Shruti Arya, Mily Bhattacharya, Samrat Mukhopadhyay. Direct Observation of the Intrinsic Backbone Torsional Mobility of Disordered Proteins. Biophysical Journal 2016;111:768
    https://doi.org/10.1016/j.bpj.2016.07.023
  133. Jessica Dröden, Malte Drescher. Rapid Scan Electron Paramagnetic Resonance Spectroscopy Is a Suitable Tool to Study Intermolecular Interactions of Intrinsically Disordered Protein. Biology 2023;12:79
    https://doi.org/10.3390/biology12010079
  134. Matteo Runfola, Alfonso De Simone, Michele Vendruscolo, Christopher M. Dobson, Giuliana Fusco. The N-terminal Acetylation of α-Synuclein Changes the Affinity for Lipid Membranes but not the Structural Properties of the Bound State. Sci Rep 2020;10
    https://doi.org/10.1038/s41598-019-57023-4
  135. André Pineda, Jacqueline Burré. Modulating membrane binding of α-synuclein as a therapeutic strategy. Proc. Natl. Acad. Sci. U.S.A. 2017;114:1223
    https://doi.org/10.1073/pnas.1620159114
  136. Velmarini Vasquez, Joy Mitra, Pavana M. Hegde, Arvind Pandey, Shiladitya Sengupta, Sankar Mitra, K.S. Rao, Muralidhar L. Hegde. Chromatin-Bound Oxidized α-Synuclein Causes Strand Breaks in Neuronal Genomes in in vitro Models of Parkinson’s Disease. JAD 2017;60:S133
    https://doi.org/10.3233/JAD-170342
  137. Ana West, Benjamin E. Brummel, Anthony R. Braun, Elizabeth Rhoades, Jonathan N. Sachs. Membrane remodeling and mechanics: Experiments and simulations of α-Synuclein. Biochimica et Biophysica Acta (BBA) - Biomembranes 2016;1858:1594
    https://doi.org/10.1016/j.bbamem.2016.03.012
  138. Tapojyoti Das, Meraj Ramezani, David Snead, Cristian Follmer, Peter Chung, Ka Yee Lee, David A. Holowka, Barbara A. Baird, David Eliezer. The Role of Membrane Affinity and Binding Modes in Alpha-Synuclein Regulation of Vesicle Release and Trafficking. Biomolecules 2022;12:1816
    https://doi.org/10.3390/biom12121816
  139. David Snead, David Eliezer. Intrinsically disordered proteins in synaptic vesicle trafficking and release. Journal of Biological Chemistry 2019;294:3325
    https://doi.org/10.1074/jbc.REV118.006493
  140. Wing K. Man, Bogachan Tahirbegi, Michail D. Vrettas, Swapan Preet, Liming Ying, Michele Vendruscolo, Alfonso De Simone, Giuliana Fusco. The docking of synaptic vesicles on the presynaptic membrane induced by α-synuclein is modulated by lipid composition. Nat Commun 2021;12
    https://doi.org/10.1038/s41467-021-21027-4
  141. Claire Hoenen, Audrey Gustin, Cindy Birck, Mélanie Kirchmeyer, Nicolas Beaume, Paul Felten, Luc Grandbarbe, Paul Heuschling, Tony Heurtaux, Serge Nataf. Alpha-Synuclein Proteins Promote Pro-Inflammatory Cascades in Microglia: Stronger Effects of the A53T Mutant. PLoS ONE 2016;11:e0162717
    https://doi.org/10.1371/journal.pone.0162717
  142. Khalid Bashir Dar, Aashiq Hussain Bhat, Shajrul Amin, Bilal Ahmad Reshi, Mohammad Afzal Zargar, Akbar Masood, Showkat Ahmad Ganie. Elucidating Critical Proteinopathic Mechanisms and Potential Drug Targets in Neurodegeneration. Cell Mol Neurobiol 2020;40:313
    https://doi.org/10.1007/s10571-019-00741-0
  143. Ryan Khounlo, Brenden J. D. Hawk, Tung-Mei Khu, Gyeongji Yoo, Nam Ki Lee, Josh Pierson, Yeon-Kyun Shin. Membrane Binding of α-Synuclein Stimulates Expansion of SNARE-Dependent Fusion Pore. Front. Cell Dev. Biol. 2021;9
    https://doi.org/10.3389/fcell.2021.663431
  144. Ersoy Cholak, Katrine Bugge, Adree Khondker, Kimmie Gauger, Elena Pedraz‐Cuesta, Morten Enghave Pedersen, Saskia Bucciarelli, Bente Vestergaard, Stine F. Pedersen, Maikel C. Rheinstädter, Annette Eva Langkilde, Birthe B. Kragelund. Avidity within the N‐terminal anchor drives α‐synuclein membrane interaction and insertion. FASEB j. 2020;34:7462
    https://doi.org/10.1096/fj.202000107R
  145. Saly Charles-Achille, Jean-Marc Janot, Bastien Cayrol, Sébastien Balme. Influence of Seed structure on Volume distribution of α‐Synuclein Oligomer at Early Stages of Aggregation using nanopipette. ChemBioChem 2024
    https://doi.org/10.1002/cbic.202300748
  146. Boris Zhang, Feng Li, Zhengyao Chen, Indira Shrivastava, Edward Gasanoff, Ruben Dagda. Naja mossambica mossambica Cobra Cardiotoxin Targets Mitochondria to Disrupt Mitochondrial Membrane Structure and Function. Toxins 2019;11:152
    https://doi.org/10.3390/toxins11030152
  147. Larisa Ryskalin, Francesca Biagioni, Gabriele Morucci, Carla L. Busceti, Alessandro Frati, Stefano Puglisi-Allegra, Michela Ferrucci, Francesco Fornai. Spreading of Alpha Synuclein from Glioblastoma Cells towards Astrocytes Correlates with Stem-like Properties. Cancers 2022;14:1417
    https://doi.org/10.3390/cancers14061417
  148. Meir Schechter, Ronit Sharon. An Emerging Role for Phosphoinositides in the Pathophysiology of Parkinson’s Disease. JPD 2021;11:1725
    https://doi.org/10.3233/JPD-212684
  149. Moutusi Manna, Rajesh K. Murarka. Polyunsaturated Fatty Acid Modulates Membrane-Bound Monomeric α-Synuclein by Modulating Membrane Microenvironment through Preferential Interactions. ACS Chem. Neurosci. 2021;12:675
    https://doi.org/10.1021/acschemneuro.0c00694
  150. L. Aerts, V.A. Morais. Parkinson's Disease. 2021.
    https://doi.org/10.1016/B978-0-12-803783-6.00002-X
  151. Stephanie Ghio, Angelique Camilleri, Mario Caruana, Viktoria C. Ruf, Felix Schmidt, Andrei Leonov, Sergey Ryazanov, Christian Griesinger, Ruben J. Cauchi, Frits Kamp, Armin Giese, Neville Vassallo. Cardiolipin Promotes Pore-Forming Activity of Alpha-Synuclein Oligomers in Mitochondrial Membranes. ACS Chem. Neurosci. 2019;10:3815
    https://doi.org/10.1021/acschemneuro.9b00320
  152. Brenden J. D. Hawk, Ryan Khounlo, Yeon-Kyun Shin. Alpha-Synuclein Continues to Enhance SNARE-Dependent Vesicle Docking at Exorbitant Concentrations. Front. Neurosci. 2019;13
    https://doi.org/10.3389/fnins.2019.00216
  153. Jaka Kragelj, Rania Dumarieh, Yiling Xiao, Kendra K. Frederick. Conformational ensembles explain NMR spectra of frozen intrinsically disordered proteins. Protein Science 2023;32
    https://doi.org/10.1002/pro.4628
  154. Andre Melnik, Valentina Cappelletti, Federico Vaggi, Ilaria Piazza, Marco Tognetti, Carmen Schwarz, Gea Cereghetti, Mennat Allah Ahmed, Martin Soste, Kent Matlack, Natalie de Souza, Attila Csikasz-Nagy, Paola Picotti. Comparative analysis of the intracellular responses to disease-related aggregation-prone proteins. Journal of Proteomics 2020;225:103862
    https://doi.org/10.1016/j.jprot.2020.103862
  155. Michele Vendruscolo, Marta Castellana-Cruz, Aishwarya Nene, Rebecca J. Thrush, Catherine K. Xu, Janet R. Kumita, Michele Vendruscolo. Effects of N-Terminal Acetylation on the Aggregationof Disease-Related a Lpha-Synuclein Variants. SSRN Journal 2022
    https://doi.org/10.2139/ssrn.4194537
  156. Ana Belén Uceda, Juan Frau, Bartolomé Vilanova, Miquel Adrover. On the effect of methionine oxidation on the interplay between α-synuclein and synaptic-like vesicles. International Journal of Biological Macromolecules 2023;229:92
    https://doi.org/10.1016/j.ijbiomac.2022.12.262
  157. Slav A. Semerdzhiev, Ine Segers-Nolten, Paul van der Schoot, Christian Blum, Mireille M. A. E. Claessens. SARS-CoV-2 N-protein induces the formation of composite α-synuclein/N-protein fibrils that transform into a strain of α-synuclein fibrils. Nanoscale 2023;15:18337
    https://doi.org/10.1039/D3NR03556E
  158. Abid Oueslati. Implication of Alpha-Synuclein Phosphorylation at S129 in Synucleinopathies: What Have We Learned in the Last Decade?. JPD 2016;6:39
    https://doi.org/10.3233/JPD-160779
  159. Saranna Fanning, Aftabul Haque, Thibaut Imberdis, Valeriya Baru, M. Inmaculada Barrasa, Silke Nuber, Daniel Termine, Nagendran Ramalingam, Gary P.H. Ho, Tallie Noble, Jackson Sandoe, Yali Lou, Dirk Landgraf, Yelena Freyzon, Gregory Newby, Frank Soldner, Elizabeth Terry-Kantor, Tae-Eun Kim, Harald F. Hofbauer, Michel Becuwe, Rudolf Jaenisch, David Pincus, Clary B. Clish, Tobias C. Walther, Robert V. Farese, Supriya Srinivasan, Michael A. Welte, Sepp D. Kohlwein, Ulf Dettmer, Susan Lindquist, Dennis Selkoe. Lipidomic Analysis of α-Synuclein Neurotoxicity Identifies Stearoyl CoA Desaturase as a Target for Parkinson Treatment. Molecular Cell 2019;73:1001
    https://doi.org/10.1016/j.molcel.2018.11.028