Repairing Membranes to Rescue Mitochondria in Degenerative Diseases

Scientific References

Review Papers

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Research Papers

α-Synuclein (αSyn)
  • Herrera M, El Saghir A, Mansueto S, Ghio S, Fusco G, De Simone A, Vassallo N. Aggregation and membrane activity of mutant A30P alpha-synuclein on mitochondrial membranes. Int J Biol Macromol. 2026;355:151491. doi: 10.1016/j.ijbiomac.2026.151491. PMID: 41856188.
  • Bro̷chner BV, Zhang X, Nielsen J, Kjems J, Otzen DE, Malle MG. Single-vesicle Tracking of α-Synuclein Oligomers Reveals Pore Formation by a Three-Stage Model. ACS Nano. 2025;19(36):32108-32122. doi: 10.1021/acsnano.5c04005. PMID: 40794544.
  • Šneiderienė G, Czekalska MA, Xu CK, Jayaram AK, Krainer G, Arter WE, Peter QAE, Castellana-Cruz M, Saar KL, Levin A, Mueller T, Fiedler S, Devenish SRA, Fiegler H, Kumita JR, Knowles TPJ. α-Synuclein Oligomers Displace Monomeric α-Synuclein from Lipid Membranes. ACS Nano. 2024;18(27):17469-17482. doi: 10.1021/acsnano.3c10889. PMID: 38916260.
  • Maurer M, Lazaridis T. Transmembrane β-Barrel Models of α-Synuclein Oligomers. J Chem Inf Model. 2023;63(22):7171-7179. doi: 10.1021/acs.jcim.3c00997. PMID: 37963823.
  • Yang Z, Yao Y, Zhou Y, Li X, Tang Y, Wei G. EGCG attenuates α-synuclein protofibril-membrane interactions and disrupts the protofibril. Int J Biol Macromol. 2023;230:123194. doi: 10.1016/j.ijbiomac.2023.123194. PMID: 36623616.
  • Pirhaghi M, Frank SA, Alam P, Nielsen J, Sereikaite V, Gupta A, Strømgaard K, Andreasen M, Sharma D, Saboury AA, Otzen DE. A penetratin-derived peptide reduces the membrane permeabilization and cell toxicity of α-synuclein oligomers. J Biol Chem. 2022;298(12):102688. doi: 10.1016/j.jbc.2022.102688. PMID: 36370848.
  • Yoo G, An HJ, Yeou S, Lee NK. α-Synuclein Disrupts Vesicle Fusion by Two Mutant-Specific Mechanisms. Mol Cells. 2022;45(11):806-819. doi: 10.14348/molcells.2022.0102. PMID: 36380732.
  • Sanders HM, Kostelic MM, Zak CK, Marty MT. Lipids and EGCG Affect α-Synuclein Association and Disruption of Nanodiscs. Biochemistry. 2022;61(11):1014-1021. doi: 10.1021/acs.biochem.2c00160. PMID: 35616927.
  • Parres-Gold J, Chieng A, Wong Su S, Wang Y. Real-Time Characterization of Cell Membrane Disruption by α-Synuclein Oligomers in Live SH-SY5Y Neuroblastoma Cells. ACS Chem Neurosci. 2020;11(17):2528-2534. doi: 10.1021/acschemneuro.0c00309. PMID: 32786327.
  • Dutta S, Watson BG, Mattoo S, Rochet JC. Calcein Release Assay to Measure Membrane Permeabilization by Recombinant Alpha-Synuclein. Bio Protoc. 2020;10(14). doi: 10.21769/bioprotoc.3690. PMID: 32953942.
  • Hannestad JK, Rocha S, Agnarsson B, Zhdanov VP, Wittung-Stafshede P, Höök F. Single-vesicle imaging reveals lipid-selective and stepwise membrane disruption by monomeric α-synuclein. Proc Natl Acad Sci U S A. 2020;117(25):14178-14186. doi: 10.1073/pnas.1914670117. PMID: 32513706.
  • Ghio S, Camilleri A, Caruana M, Ruf VC, Schmidt F, Leonov A, Ryazanov S, Griesinger C, Cauchi RJ, Kamp F, Giese A, Vassallo N. Cardiolipin Promotes Pore-Forming Activity of Alpha-Synuclein Oligomers in Mitochondrial Membranes. ACS Chem Neurosci. 2019;10(8):3815-3829. doi: 10.1021/acschemneuro.9b00320. PMID: 31356747.
  • Ludtmann MHR, Angelova PR, Horrocks MH, Choi ML, Rodrigues M, Baev AY, Berezhnov AV, Yao Z, Little D, Banushi B, Al-Menhali AS, Ranasinghe RT, Whiten DR, Yapom R, Dolt KS, Devine MJ, Gissen P, Kunath T, Jaganjac M, Pavlov EV, Klenerman D, Abramov AY, Gandhi S. α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson's disease. Nat Commun. 2018;9(1):2293. doi: 10.1038/s41467-018-04422-2. PMID: 29895861.
  • Yang JE, Rhoo KY, Lee S, Lee JT, Park JH, Bhak G, Paik SR. EGCG-mediated Protection of the Membrane Disruption and Cytotoxicity Caused by the 'Active Oligomer' of α-Synuclein. Sci Rep. 2017;7(1):17945. doi: 10.1038/s41598-017-18349-z. PMID: 29263416.
  • 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. Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers. Science. 2017;358(6369):1440-1443. doi: 10.1126/science.aan6160. PMID: 29242346.
  • Chaudhary H, Subramaniam V, Claessens MMAE. Direct Visualization of Model Membrane Remodeling by α-Synuclein Fibrillization. Chemphyschem. 2017;18(12):1620-1626. doi: 10.1002/cphc.201700050. PMID: 28370874.
  • Kaufmann TJ, Harrison PM, Richardson MJ, Pinheiro TJ, Wall MJ. Intracellular soluble α-synuclein oligomers reduce pyramidal cell excitability. J Physiol. 2016;594(10):2751-72. doi: 10.1113/JP271968. PMID: 26915902.
  • Angelova PR, Ludtmann MH, Horrocks MH, Negoda A, Cremades N, Klenerman D, Dobson CM, Wood NW, Pavlov EV, Gandhi S, Abramov AY. Ca2+ is a key factor in α-synuclein-induced neurotoxicity. J Cell Sci. 2016;129(9):1792-801. doi: 10.1242/jcs.180737. PMID: 26989132.
  • Hu R, Diao J, Li J, Tang Z, Li X, Leitz J, Long J, Liu J, Yu D, Zhao Q. Intrinsic and membrane-facilitated α-synuclein oligomerization revealed by label-free detection through solid-state nanopores. Sci Rep. 2016;6:20776. doi: 10.1038/srep20776. PMID: 26865505.
  • Stefanovic AN, Lindhoud S, Semerdzhiev SA, Claessens MM, Subramaniam V. Oligomers of Parkinson's Disease-Related α-Synuclein Mutants Have Similar Structures but Distinctive Membrane Permeabilization Properties. Biochemistry. 2015;54(20):3142-50. doi: 10.1021/bi501369k. PMID: 25909158.
  • Pacheco CR, Morales CN, Ramírez AE, Muñoz FJ, Gallegos SS, Caviedes PA, Aguayo LG, Opazo CM. Extracellular α-synuclein alters synaptic transmission in brain neurons by perforating the neuronal plasma membrane. J Neurochem. 2015;132(6):731-41. doi: 10.1111/jnc.13060. PMID: 25669123.
  • Surguchev A, Surguchov A. Effect of α-synuclein on membrane permeability and synaptic transmission: a clue to neurodegeneration?. J Neurochem. 2015;132(6):619-21. doi: 10.1111/jnc.13045. PMID: 25739983.
  • Mironov SL. α-Synuclein forms non-selective cation channels and stimulates ATP-sensitive potassium channels in hippocampal neurons. J Physiol. 2015;593(1):145-59. doi: 10.1113/jphysiol.2014.280974. PMID: 25556793.
  • Lorenzen N, Nielsen SB, Yoshimura Y, Vad BS, Andersen CB, Betzer C, Kaspersen JD, Christiansen G, Pedersen JS, Jensen PH, Mulder FA, Otzen DE. How epigallocatechin gallate can inhibit α-synuclein oligomer toxicity in vitro. J Biol Chem. 2014;289(31):21299-310. doi: 10.1074/jbc.M114.554667. PMID: 24907278.
  • Luth ES, Stavrovskaya IG, Bartels T, Kristal BS, Selkoe DJ. Soluble, prefibrillar α-synuclein oligomers promote complex I-dependent, Ca2+-induced mitochondrial dysfunction. J Biol Chem. 2014;289(31):21490-507. doi: 10.1074/jbc.M113.545749. PMID: 24942732.
  • Stefanovic AN, Stöckl MT, Claessens MM, Subramaniam V. α-Synuclein oligomers distinctively permeabilize complex model membranes. FEBS J. 2014;281(12):2838-50. doi: 10.1111/febs.12824. PMID: 24767583.
  • Nübling GS, Levin J, Bader B, Lorenzl S, Hillmer A, Högen T, Kamp F, Giese A. Modelling Ser129 phosphorylation inhibits membrane binding of pore-forming alpha-synuclein oligomers. PLoS One. 2014;9(6):e98906. doi: 10.1371/journal.pone.0098906. PMID: 24911099.
  • Fecchio C, De Franceschi G, Relini A, Greggio E, Dalla Serra M, Bubacco L, Polverino de Laureto P. α-Synuclein oligomers induced by docosahexaenoic acid affect membrane integrity. PLoS One. 2013;8(11):e82732. doi: 10.1371/journal.pone.0082732. PMID: 24312431.
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  • Caruana M, Neuner J, Högen T, Schmidt F, Kamp F, Scerri C, Giese A, Vassallo N. Polyphenolic compounds are novel protective agents against lipid membrane damage by α-synuclein aggregates in vitro. Biochim Biophys Acta. 2012;1818(11):2502-10. doi: 10.1016/j.bbamem.2012.05.019. PMID: 22634381.
  • Tosatto L, Andrighetti AO, Plotegher N, Antonini V, Tessari I, Ricci L, Bubacco L, Dalla Serra M. Alpha-synuclein pore forming activity upon membrane association. Biochim Biophys Acta. 2012;1818(11):2876-83. doi: 10.1016/j.bbamem.2012.07.007. PMID: 22820150.
  • Schmidt F, Levin J, Kamp F, Kretzschmar H, Giese A, Bötzel K. Single-channel electrophysiology reveals a distinct and uniform pore complex formed by α-synuclein oligomers in lipid membranes. PLoS One. 2012;7(8):e42545. doi: 10.1371/journal.pone.0042545. PMID: 22880029.
  • Tsigelny IF, Sharikov Y, Wrasidlo W, Gonzalez T, Desplats PA, Crews L, Spencer B, Masliah E. Role of α-synuclein penetration into the membrane in the mechanisms of oligomer pore formation. FEBS J. 2012;279(6):1000-13. doi: 10.1111/j.1742-4658.2012.08489.x. PMID: 22251432.
  • Stöckl M, Claessens MM, Subramaniam V. Kinetic measurements give new insights into lipid membrane permeabilization by α-synuclein oligomers. Mol Biosyst. 2012;8(1):338-45. doi: 10.1039/c1mb05293d. PMID: 22009045.
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β-Amyloid (Aβ)
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  • Limbocker R, Cremades N, Cascella R, Tessier PM, Vendruscolo M, Chiti F. Characterization of Pairs of Toxic and Nontoxic Misfolded Protein Oligomers Elucidates the Structural Determinants of Oligomer Toxicity in Protein Misfolding Diseases. Acc Chem Res. 2023;56(12):1395-1405. doi: 10.1021/acs.accounts.3c00045. PMID: 37071750.
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  • Budvytyte R, Ambrulevičius F, Jankaityte E, Valincius G. Electrochemical assessment of dielectric damage to phospholipid bilayers by amyloid β-Oligomers. Bioelectrochemistry. 2022;145:108091. doi: 10.1016/j.bioelechem.2022.108091. PMID: 35240464.
  • Dai Y, Xie Z, Liang L. Pore Formation Mechanism of A-Beta Peptide on the Fluid Membrane: A Combined Coarse-Grained and All-Atomic Model. Molecules. 2022;27(12). doi: 10.3390/molecules27123924. PMID: 35745043.
  • Nguyen HL, Linh HQ, Krupa P, La Penna G, Li MS. Amyloid β Dodecamer Disrupts the Neuronal Membrane More Strongly than the Mature Fibril: Understanding the Role of Oligomers in Neurotoxicity. J Phys Chem B. 2022;126(20):3659-3672. doi: 10.1021/acs.jpcb.2c01769. PMID: 35580354.
  • Durell SR, Kayed R, Guy HR. The amyloid concentric β-barrel hypothesis: Models of amyloid beta 42 oligomers and annular protofibrils. Proteins. 2022;90(5):1190-1209. doi: 10.1002/prot.26301. PMID: 35038191.
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  • Gu L, Guo Z. Lipid membranes induce structural conversion from amyloid oligomers to fibrils. Biochem Biophys Res Commun. 2021;557:122-126. doi: 10.1016/j.bbrc.2021.03.174. PMID: 33862455.
  • Ngo ST, Nguyen PH, Derreumaux P. Impact of the Rat R5G, Y10F, and H13R Mutations on Tetrameric Aβ42 β-Barrel in a Lipid Bilayer Membrane Model. J Phys Chem B. 2021;125(12):3105-3113. doi: 10.1021/acs.jpcb.1c00030. PMID: 33739113.
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  • Venko K, Novič M, Stoka V, Žerovnik E. Prediction of Transmembrane Regions, Cholesterol, and Ganglioside Binding Sites in Amyloid-Forming Proteins Indicate Potential for Amyloid Pore Formation. Front Mol Neurosci. 2021;14:619496. doi: 10.3389/fnmol.2021.619496. PMID: 33642992.
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  • Diociaiuti M, Bombelli C, Zanetti-Polzi L, Belfiore M, Fioravanti R, Macchia G, Giordani C. The Interaction between Amyloid Prefibrillar Oligomers of Salmon Calcitonin and a Lipid-Raft Model: Molecular Mechanisms Leading to Membrane Damage, Ca2+-Influx and Neurotoxicity. Biomolecules. 2019;10(1). doi: 10.3390/biom10010058. PMID: 31905804.
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Islet Amyloid Polypeptide (IAPP)
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  • Lewis A, Pham T, Nguyen N, Graf A, Cheng KH. Lipid domain boundary triggers membrane damage and protein folding of human islet amyloid polypeptide in the early pathogenesis of amyloid diseases. Biophys Chem. 2023;296:106993. doi: 10.1016/j.bpc.2023.106993. PMID: 36898349.
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  • Sciacca MF, Lolicato F, Tempra C, Scollo F, Sahoo BR, Watson MD, García-Viñuales S, Milardi D, Raudino A, Lee JC, Ramamoorthy A, La Rosa C. Lipid-Chaperone Hypothesis: A Common Molecular Mechanism of Membrane Disruption by Intrinsically Disordered Proteins. ACS Chem Neurosci. 2020;11(24):4336-4350. doi: 10.1021/acschemneuro.0c00588. PMID: 33269918.
  • Qiao Q, Wei G, Yao D, Song Z. Formation of α-helical and β-sheet structures in membrane-bound human IAPP monomer and the resulting membrane deformation. Phys Chem Chem Phys. 2019;21(36):20239-20251. doi: 10.1039/c9cp03151k. PMID: 31490518.
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  • Gurlo T, Ryazantsev S, Huang CJ, Yeh MW, Reber HA, Hines OJ, O'Brien TD, Glabe CG, Butler PC. Evidence for proteotoxicity in beta cells in type 2 diabetes: toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway. Am J Pathol. 2010;176(2):861-9. doi: 10.2353/ajpath.2010.090532. PMID: 20042670.
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Tau Protein (tau)
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  • Sun M, Lin J, Li S. Extracellular tau oligomers exert neurocytotoxicity by triggering mitochondrial dysfunction. J Alzheimers Dis. 2026;110(1):409-425. doi: 10.1177/13872877251414979. PMID: 41631871.
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  • Sadleir KR, Gomez KP, Edwards AE, Patel AJ, Ley ML, Khatri AW, Guo J, Mahesh S, Watkins EA, Popovic J, Karunakaran DKP, Prokopenko D, Tanzi RE, Bustos B, Lubbe SJ, Demonbruen AR, McNally EM, Vassar R. Annexin A6 membrane repair protein protects against amyloid-induced dystrophic neurites and tau phosphorylation in Alzheimer's disease model mice. Acta Neuropathol. 2025;149(1):51. doi: 10.1007/s00401-025-02888-1. PMID: 40411591.
  • Camilleri A, Ghio S, Caruana M, Weckbecker D, Schmidt F, Kamp F, Leonov A, Ryazanov S, Griesinger C, Giese A, Cauchi RJ, Vassallo N. Tau-induced mitochondrial membrane perturbation is dependent upon cardiolipin. Biochim Biophys Acta Biomembr. 2020;1862(2):183064. doi: 10.1016/j.bbamem.2019.183064. PMID: 31521630.
  • Mari SA, Wegmann S, Tepper K, Hyman BT, Mandelkow EM, Mandelkow E, Müller DJ. Reversible Cation-Selective Attachment and Self-Assembly of Human Tau on Supported Brain Lipid Membranes. Nano Lett. 2018;18(5):3271-3281. doi: 10.1021/acs.nanolett.8b01085. PMID: 29644863.
  • Patel N, Ramachandran S, Azimov R, Kagan BL, Lal R. Ion Channel Formation by Tau Protein: Implications for Alzheimer's Disease and Tauopathies. Biochemistry. 2015;54(50):7320-5. doi: 10.1021/acs.biochem.5b00988. PMID: 26575330.
  • Lasagna-Reeves CA, Sengupta U, Castillo-Carranza D, Gerson JE, Guerrero-Munoz M, Troncoso JC, Jackson GR, Kayed R. The formation of tau pore-like structures is prevalent and cell specific: possible implications for the disease phenotypes. Acta Neuropathol Commun. 2014;2:56. doi: 10.1186/2051-5960-2-56. PMID: 24887264.
  • Flach K, Hilbrich I, Schiffmann A, Gärtner U, Krüger M, Leonhardt M, Waschipky H, Wick L, Arendt T, Holzer M. Tau oligomers impair artificial membrane integrity and cellular viability. J Biol Chem. 2012;287(52):43223-33. doi: 10.1074/jbc.M112.396176. PMID: 23129775.
  • Jones EM, Dubey M, Camp PJ, Vernon BC, Biernat J, Mandelkow E, Majewski J, Chi EY. Interaction of tau protein with model lipid membranes induces tau structural compaction and membrane disruption. Biochemistry. 2012;51(12):2539-50. doi: 10.1021/bi201857v. PMID: 22401494.
TDP-43 and SOD1
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  • Latimer CS, Liachko NF. Tau and TDP-43 synergy: a novel therapeutic target for sporadic late-onset Alzheimer's disease. Geroscience. 2021;43(4):1627-1634. doi: 10.1007/s11357-021-00407-0. PMID: 34185246.
  • Dhakal S, Wyant CE, George HE, Morgan SE, Rangachari V. Prion-like C-Terminal Domain of TDP-43 and α-Synuclein Interact Synergistically to Generate Neurotoxic Hybrid Fibrils. J Mol Biol. 2021;433(10):166953. doi: 10.1016/j.jmb.2021.166953. PMID: 33771571.
  • Post J, Kogel V, Schaffrath A, Lohmann P, Shah NJ, Langen KJ, Willbold D, Willuweit A, Kutzsche J. A Novel Anti-Inflammatory d-Peptide Inhibits Disease Phenotype Progression in an ALS Mouse Model. Molecules. 2021;26(6). doi: 10.3390/molecules26061590. PMID: 33805709.
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  • Malik R, Meng H, Wongkongkathep P, Corrales CI, Sepanj N, Atlasi RS, Klärner FG, Schrader T, Spencer MJ, Loo JA, Wiedau M, Bitan G. The molecular tweezer CLR01 inhibits aberrant superoxide dismutase 1 (SOD1) self-assembly in vitro and in the G93A-SOD1 mouse model of ALS. J Biol Chem. 2019;294(10):3501-3513. doi: 10.1074/jbc.RA118.005940. PMID: 30602569.
  • Srinivasan E, Rajasekaran R. Probing the inhibitory activity of epigallocatechin-gallate on toxic aggregates of mutant (L84F) SOD1 protein through geometry based sampling and steered molecular dynamics. J Mol Graph Model. 2017;74:288-295. doi: 10.1016/j.jmgm.2017.04.019. PMID: 28458007.
  • Chen CH, Khan A, Huang JJ, Ulmschneider MB. Mechanisms of Membrane Pore Formation by Amyloidogenic Peptides in Amyotrophic Lateral Sclerosis. Chemistry. 2016;22(29):9958-61. doi: 10.1002/chem.201601765. PMID: 27224887.
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  • Ding X, Ma M, Teng J, Teng RK, Zhou S, Yin J, Fonkem E, Huang JH, Wu E, Wang X. Exposure to ALS-FTD-CSF generates TDP-43 aggregates in glioblastoma cells through exosomes and TNTs-like structure. Oncotarget. 2015;6(27):24178-91. doi: 10.18632/oncotarget.4680. PMID: 26172304.
  • Irvin CW, Kim RB, Mitchell CS. Seeking homeostasis: temporal trends in respiration, oxidation, and calcium in SOD1 G93A Amyotrophic Lateral Sclerosis mice. Front Cell Neurosci. 2015;9:248. doi: 10.3389/fncel.2015.00248. PMID: 26190973.
  • Fang YS, Tsai KJ, Chang YJ, Kao P, Woods R, Kuo PH, Wu CC, Liao JY, Chou SC, Lin V, Jin LW, Yuan HS, Cheng IH, Tu PH, Chen YR. Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients. Nat Commun. 2014;5:4824. doi: 10.1038/ncomms5824. PMID: 25215604.
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  • Allen MJ, Lacroix JJ, Ramachandran S, Capone R, Whitlock JL, Ghadge GD, Arnsdorf MF, Roos RP, Lal R. Mutant SOD1 forms ion channel: implications for ALS pathophysiology. Neurobiol Dis. 2012;45(3):831-8. doi: 10.1016/j.nbd.2011.08.031. PMID: 21930207.
  • Chung J, Yang H, de Beus MD, Ryu CY, Cho K, Colón W. Cu/Zn superoxide dismutase can form pore-like structures. Biochem Biophys Res Commun. 2003;312(4):873-6. doi: 10.1016/j.bbrc.2003.11.008. PMID: 14651952.
Huntingtin (mHtt)
  • Gamage YI, Pan J. Elucidating the Influence of Lipid Composition on Bilayer Perturbations Induced by the N-terminal Region of the Huntingtin Protein. Biophysica. 2023;3(4):582-597. doi: 10.3390/biophysica3040040. PMID: 38737720.
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  • van der Bent ML, Evers MM, Vallès A. Emerging Therapies for Huntington's Disease - Focus on N-Terminal Huntingtin and Huntingtin Exon 1. Biologics. 2022;16:141-160. doi: 10.2147/BTT.S270657. PMID: 36213816.
  • Vöpel T, Bravo-Rodriguez K, Mittal S, Vachharajani S, Gnutt D, Sharma A, Steinhof A, Fatoba O, Ellrichmann G, Nshanian M, Heid C, Loo JA, Klärner FG, Schrader T, Bitan G, Wanker EE, Ebbinghaus S, Sanchez-Garcia E. Inhibition of Huntingtin Exon-1 Aggregation by the Molecular Tweezer CLR01. J Am Chem Soc. 2017;139(16):5640-5643. doi: 10.1021/jacs.6b11039. PMID: 28406616.
  • Takeuchi T, Nagai Y. Protein Misfolding and Aggregation as a Therapeutic Target for Polyglutamine Diseases. Brain Sci. 2017;7(10). doi: 10.3390/brainsci7100128. PMID: 29019918.
  • Kegel-Gleason KB. Huntingtin interactions with membrane phospholipids: strategic targets for therapeutic intervention?. J Huntingtons Dis. 2013;2(3):239-50. doi: 10.3233/JHD-130068. PMID: 25062673.
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  • Marchut AJ, Hall CK. Spontaneous formation of annular structures observed in molecular dynamics simulations of polyglutamine peptides. Comput Biol Chem. 2006;30(3):215-8. doi: 10.1016/j.compbiolchem.2006.01.003. PMID: 16678490.
  • Ignatova Z, Gierasch LM. Extended polyglutamine tracts cause aggregation and structural perturbation of an adjacent beta barrel protein. J Biol Chem. 2006;281(18):12959-67. doi: 10.1074/jbc.M511523200. PMID: 16524881.
  • Kagan BL, Hirakura Y, Azimov R, Azimova R. The channel hypothesis of Huntington's disease. Brain Res Bull. 2001;56(3-4):281-4. doi: 10.1016/s0361-9230(01)00654-2. PMID: 11719262.
  • Monoi H, Futaki S, Kugimiya S, Minakata H, Yoshihara K. Poly-L-glutamine forms cation channels: relevance to the pathogenesis of the polyglutamine diseases. Biophys J. 2000;78(6):2892-9. doi: 10.1016/s0006-3495(00)76830-5. PMID: 10827970.
  • Hirakura Y, Azimov R, Azimova R, Kagan BL. Polyglutamine-induced ion channels: a possible mechanism for the neurotoxicity of Huntington and other CAG repeat diseases. J Neurosci Res. 2000;60(4):490-4. doi: 10.1002/(sici)1097-4547(20000515)60:4<490::aid-jnr7>3.0.co;2-9. PMID: 10797551.
Prion Protein (PrP)
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  • Emendato A, Divisato G, Giannino E, Mansueto S, Zizolfi MC, Peltrini R, Parisi S, De Simone A. Structural and cellular properties of human prion protein oligomers. Commun Biol. 2025;8(1):1704. doi: 10.1038/s42003-025-09105-5. PMID: 41299034.
  • Wu J, Wang X, Lakkaraju A, Sternke-Hoffmann R, Qureshi BM, Aguzzi A, Luo J. Channel Activities of the Full-Length Prion and Truncated Proteins. ACS Chem Neurosci. 2024;15(1):98-107. doi: 10.1021/acschemneuro.3c00412. PMID: 38096481.
  • Rai SK, Khanna R, Avni A, Mukhopadhyay S. Heterotypic electrostatic interactions control complex phase separation of tau and prion into multiphasic condensates and co-aggregates. Proc Natl Acad Sci U S A. 2023;120(2):e2216338120. doi: 10.1073/pnas.2216338120. PMID: 36595668.
  • Admane N, Srivastava A, Jamal S, Sharma R, Kundu B, Grover A. Molecular insights into the critical role of gallate moiety of green tea catechins in modulating prion fibrillation, cellular internalization, and neuronal toxicity. Int J Biol Macromol. 2022;223(Pt A):755-765. doi: 10.1016/j.ijbiomac.2022.11.049. PMID: 36368361.
  • Qin K, Zhao L, Solanki A, Busch C, Mastrianni J. Anle138b prevents PrP plaque accumulation in Tg(PrP-A116V) mice but does not mitigate clinical disease. J Gen Virol. 2019;100(6):1027-1037. doi: 10.1099/jgv.0.001262. PMID: 31045489.
  • Hayward S, Milner-White EJ. Geometrical principles of homomeric β-barrels and β-helices: Application to modeling amyloid protofilaments. Proteins. 2017;85(10):1866-1881. doi: 10.1002/prot.25341. PMID: 28646497.
  • Sabareesan AT, Singh J, Roy S, Udgaonkar JB, Mathew MK. The Pathogenic A116V Mutation Enhances Ion-Selective Channel Formation by Prion Protein in Membranes. Biophys J. 2016;110(8):1766-1776. doi: 10.1016/j.bpj.2016.03.017. PMID: 27119637.
  • Fernández C, Núñez-Ramírez R, Jiménez M, Rivas G, Giraldo R. RepA-WH1, the agent of an amyloid proteinopathy in bacteria, builds oligomeric pores through lipid vesicles. Sci Rep. 2016;6:23144. doi: 10.1038/srep23144. PMID: 26984374.
  • Shi S, Wagner J, Mitteregger-Kretzschmar G, Ryazanov S, Leonov A, Griesinger C, Giese A. Quantitative Real-Time Quaking-Induced Conversion Allows Monitoring of Disease-Modifying Therapy in the Urine of Prion-Infected Mice. J Neuropathol Exp Neurol. 2015;74(9):924-33. doi: 10.1097/NEN.0000000000000233. PMID: 26247395.
  • Andrich K, Bieschke J. The Effect of (-)-Epigallo-catechin-(3)-gallate on Amyloidogenic Proteins Suggests a Common Mechanism. Adv Exp Med Biol. 2015;863:139-61. doi: 10.1007/978-3-319-18365-7_7. PMID: 26092630.
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  • Solomon IH, Biasini E, Harris DA. Ion channels induced by the prion protein: mediators of neurotoxicity. Prion. 2012;6(1):40-5. doi: 10.4161/pri.6.1.18627. PMID: 22453177.
  • Solomon IH, Huettner JE, Harris DA. Neurotoxic mutants of the prion protein induce spontaneous ionic currents in cultured cells. J Biol Chem. 2010;285(34):26719-26. doi: 10.1074/jbc.M110.134619. PMID: 20573963.
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  • Zhong J, Zheng W, Huang L, Hong Y, Wang L, Qiu Y, Sha Y. PrP106-126 amide causes the semi-penetrated poration in the supported lipid bilayers. Biochim Biophys Acta. 2007;1768(6):1420-9. doi: 10.1016/j.bbamem.2007.03.003. PMID: 17451641.
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