Sites of Tau Important for Aggregation Populate β-Structure and Bind to Microtubules and Polyanions

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1. Bimolecular Fluorescence Complementation; Lighting-Up Tau-Tau Interaction in Living Cells
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2. Nuclear Magnetic Resonance Analysis of the Acetylation Pattern of the Neuronal Tau Protein
   Amina Kamah, Isabelle Huvent, François‐Xavier Cantrelle, Haoling Qi, Guy M. Lippens, Isabelle Landrieu, Caroline Smet‐Nocca · 2014 · Biochemistry
3. Intrinsically Disordered Proteins in the Neurodegenerative Processes: Formation of Tau Protein Paired Helical Filaments and Their Analysis
   Rostislav Škrabana, Jozef Ševčı́k, Michal Novák · 2006 · Cellular and Molecular Neurobiology
4. Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences
   Kateřina Melková, Vojtěch Zapletal, Subhash Narasimhan, Séverine Jansen, Jozef Hritz, Rostislav Škrabana, Markus Zweckstetter, Malene Ringkjøbing Jensen, Martin J Blackledge, Lukáš Žı́dek · 2019 · Biomolecules
5. Structural transitions in tau k18 on micelle binding suggest a hierarchy in the efficacy of individual microtubule‐binding repeats in filament nucleation
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6. Oligomer Diversity during the Aggregation of the Repeat Region of Tau
   Magnus Kjærgaard, Alexander J. Dear, Franziska Kundel, Seema Qamar, Georg Meisl, Tuomas P. J. Knowles, David Klenerman · 2018 · ACS Chemical Neuroscience
7. Folding of the Repeat Domain of Tau Upon Binding to Lipid Surfaces
   Barré, Patrick, Eliezer, David · 2006 · Journal of Molecular Biology
8. Spectroscopic Approaches to the Conformation of Tau Protein in Solution and in Paired Helical Filaments
   Martin von Bergen�, Stefan Barghorn, Sadasivam Jeganathan�, Eva‐Maria Mandelkow, Eva‐Maria Mandelkow · 2006 · Neurodegenerative Diseases
9. Cross-seeding and Conformational Selection between Three- and Four-repeat Human Tau Proteins
   Xiang Yu, Yin Luo, Paul D. Dinkel, Jie Zheng, Guanghong Wei, Martin Margittai, Ruth Nussinov, Buyong Ma · 2012 · Journal of Biological Chemistry
10. Hsp40s play complementary roles in the prevention of tau amyloid formation
    Rose Irwin, Ofrah Faust, Ivana M. Petrovic, Sharon G. Wolf, Hagen Hofmann, Rina Rosenzweig · 2021 · eLife
11. Applications of nanomaterials for scavenging reactive oxygen species in the treatment of central nervous system diseases
    Zhen An, Jincong Yan, Ye Zhang, Renjun Pei · 2020 · Journal of Materials Chemistry B
12. Clinical and pathological features of an Alzheimer's disease patient with the MAPT ΔK280 mutation
    Parastoo Momeni, Alan Michael Pittman, Tammaryn Lashley, Jana Vandrovcová, Elke Malzer, Connie Y. Luk, Christine Hulette, Andrew John Lees, Tamás Révész, John Hardy et al. · 2007 · Neurobiology of Aging
13. Prediction of nucleating sequences from amyloidogenic propensities of tau-related peptides.
    Federico A. Rojas Quijano, D. Morrow, B. Wise, F. Brancia, W. Goux · 2006 · Biochemistry
14. The Enigma of Tau Protein Aggregation: Mechanistic Insights and Future Challenges
    Huiting Zheng, Huimin Sun, Qixu Cai, Hwan‐Ching Tai · 2024 · International Journal of Molecular Sciences
15. 13 C Direct Detected NMR for Challenging Systems
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16. Correlation of Amyloid Fibril β‐Structure with the Unfolded State of α‐Synuclein
    Hai‐Young Kim, Henrike Heise, Claudio O. Fernández, Marc Baldus, Markus Zweckstetter · 2007 · ChemBioChem
17. Motional properties of unfolded ubiquitin: a model for a random coil protein
    Julia Wirmer, Wolfgang Peti, Harald Schwalbe · 2006 · Journal of Biomolecular NMR
18. Conformational Dynamics of Intracellular Tau Protein Revealed by CD and SAXS
    Nalini Vijay Gorantla, Alexander V. Shkumatov, Subashchandrabose Chinnathambi · 2016 · Methods in molecular biology
19. Tau Filament Self-Assembly and Structure: Tau as a Therapeutic Target
    Sebastian Scott Oakley, Mahmoud Bukar Maina, Karen E. Marshall, Youssra K. Al‐Hilaly, Charlie Harrington, Claude M. Wischik, Louise C. Serpell · 2020 · Frontiers in Neurology
20. Tangles, Toxicity, and Tau Secretion in AD – New Approaches to a Vexing Problem
    Kerry L. Gendreau, Garth F. Hall · 2013 · Frontiers in Neurology
21. Tau Binds to Multiple Tubulin Dimers with Helical Structure
    Xiaohan Li, Jacob A. Culver, Elizabeth R. Rhoades · 2015 · Journal of the American Chemical Society
22. Frontotemporal lobar degeneration: old knowledge and new insight into the pathogenetic mechanisms of tau mutations
    Giacomina Rossi, Fabrizio Tagliavini · 2015 · Frontiers in Aging Neuroscience
23. Global Conformation of Tau Protein Mapped by Raman Spectroscopy
    Nalini Vijay Gorantla, Puneet Khandelwal, Pankaj Poddar, Subashchandrabose Chinnathambi · 2016 · Methods in molecular biology
24. G-protein coupled purinergic P2Y12 receptor interacts and internalizes TauRD-mediated by membrane-associated actin cytoskeleton remodeling in microglia
    Hariharakrishnan Chidambaram, Rashmi Ranjan Das, Subashchandrabose Chinnathambi · 2022 · European Journal of Cell Biology
25. MAP6-F Is a Temperature Sensor That Directly Binds to and Protects Microtubules from Cold-induced Depolymerization
    Christian Delphin, Denis Bouvier, Maxime Seggio, Emilie Courriol, Yasmina Saoudi, Éric Denarier, Christophe Bosc, Odile Valiron, Mariano Bisbal, Isabelle Arnal et al. · 2012 · Journal of Biological Chemistry
26. The ΔK280 Mutation in MAP tau Favors Exon 10 Skipping In Vivo
    John Cornelis Van Swieten, Iraad F. Bronner, Asma Azmani, Lies-Anne W. F. M. Severijnen, Wouter Kamphorst, Rivka Ravid, Patrizia Rizzu, Rob Willemsen, Peter Heutink · 2007 · Journal of Neuropathology & Experimental Neurology
27. Secondary Metabolites in Ramalina terebrata Detected by UHPLC/ESI/MS/MS and Identification of Parietin as Tau Protein Inhibitor
    Alberto Cornejo, Francisco Salgado, Julio Caballero, Reinaldo Vargas, Mario Juan Simirgiotis, Carlos Areche · 2016 · International Journal of Molecular Sciences
28. Effects of pharmacological modulators of α-synuclein and tau aggregation and internalization
    Antonio Dominguez‐Meijide, Eftychia Vasili, Annekatrin König, Maria‐Sol Cima‐Omori, Alain Ibáñez de Opakua, Andrei Leonov, Sergey Ryazanov, Markus Zweckstetter, Christian Griesinger, Tiago F. Outeiro · 2020 · Scientific Reports
29. Mechanism of Tau-Promoted Microtubule Assembly As Probed by NMR Spectroscopy
    Benoı̂t Gigant, Isabelle Landrieu, Caroline Fauquant, Pascale Barbier, Isabelle Huvent, Jean‐Michel Wieruszeski, M. Knossow, Guy M. Lippens · 2014 · Journal of the American Chemical Society
30. Therapeutic antibody targeting microtubule-binding domain prevents neuronal internalization of extracellular tau via masking neuron surface proteoglycans
    Petronela Weisová, Ondrej Cehlár, Rostislav Škrabana, Monika Žilková, Peter Filipčík, Branislav Kováčech, Michal Prčina, Ľubica Wojčiaková, Ľubica Fialová, Tomáš Smolek et al. · 2019 · Acta Neuropathologica Communications
31. Misfolding and Self-Assembly Dynamics of Microtubule-Binding Repeats of the Alzheimer-Related Protein Tau
    Huan He, Yuying Liu, Yunxiang Sun, Feng Ding · 2021 · Journal of Chemical Information and Modeling
32. Tau Aggregation
    Félix Hernández, Isidró Ferrer, Mar Pérez, Juan Carlos Zabala, José Antonio del Rı́o, Jesús Ávila · 2022 · Neuroscience
33. Interactions between Aβ and Mutated Tau Lead to Polymorphism and Induce Aggregation of Aβ-Mutated Tau Oligomeric Complexes
    Yoav Atsmon‐Raz, Yifat Miller · 2013 · PLoS ONE
34. The Effect of a ΔK280 Mutation on the Unfolded State of a Microtubule-Binding Repeat in Tau
    Austin Huang, Collin M. Stultz · 2008 · PLoS Computational Biology
35. Polyanion Hydrophobicity and Protein Basicity Affect Protein Stability in Protein−Polyanion Complexes
    Erik Sedlák, Diana Fedunová, Věra Veselá, Dagmar Sedláková, Marián Antalı́k · 2009 · Biomacromolecules
36. Key Peptides and Proteins in Alzheimer’s Disease
    Botond Penke, Ferenc Bogár, Gábor Paragi, János Gera, Lívia Fülöp · 2019 · Current Protein and Peptide Science
37. Competing Interactions Stabilize Pro- and Anti-aggregant Conformations of Human Tau
    Susanne Wegmann, Jonas Schöler, Christian A. Bippes, Eckhard Mandelkow�, Daniel J. Müller · 2011 · Journal of Biological Chemistry
38. Acetylation discriminates disease-specific tau deposition
    Pijush Chakraborty, Gwladys Rivière, Alina Hebestreit, Alain Ibáñez de Opakua, Ina Maja Vorberg, Loren B. Andreas, Markus Zweckstetter · 2023 · Nature Communications
39. Monitoring of Intracellular Tau Aggregation Regulated by OGA/OGT Inhibitors
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40. New mutations in MAPT gene causing frontotemporal lobar degeneration: biochemical and structural characterization
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41. Using Intramolecular Disulfide Bonds in Tau Protein to Deduce Structural Features of Aggregation-resistant Conformations
    S. Walker, Orly Ullman, Collin M. Stultz · 2012 · Journal of Biological Chemistry
42. Site-specific dynamic nuclear polarization of hydration water as a generally applicable approach to monitor protein aggregation
    Ànna Pavlova, Evan R. McCarney, Dylan W. Peterson, Frederick W. Dahlquist, John Lew, Songi Han · 2009 · Physical Chemistry Chemical Physics
43. Aggregation of Microtubule Binding Repeats of Tau Protein is Promoted by Cu2+
    Soha Ahmadi, Shaolong Zhu, Renu Sharma, Bing Heng Wu, Ronald Soong, Rudraksha Dutta Majumdar, Derek J. Wilson, André J. Simpson, Heinz‐Bernhard Kraatz · 2019 · ACS Omega
44. The Sulfation Code of Tauopathies: Heparan Sulfate Proteoglycans in the Prion Like Spread of Tau Pathology
    Dylan Mah, Jing Zhao, Xinyue Liu, Fuming Zhang, Jian Liu, Lianchun Wang, Robert J. Linhardt, Chunyu Wang · 2021 · Frontiers in Molecular Biosciences
45. Cytoskeletal Proteins and Alzheimer’s Disease Pathogenesis: Focusing on the Interplay with Tau Pathology
    Gege Jiang, Guanfeng Xie, Xiaoyi Li, Jing Xiong · 2025 · Biomolecules
46. Resonance Raman Spectroscopic Measurements Delineate the Structural Changes that Occur during Tau Fibril Formation
    Gayathri Ramachandran, Erix Alexander Milán‐Garcés, Jayant B. Udgaonkar, Mrinalini Puranik · 2014 · Biochemistry
47. The direct and indirect effects of α-synuclein on microtubule stability in the pathogenesis of Parkinson’s disease
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48. Ubiquitination of Alzheimer's-related tau protein affects liquid-liquid phase separation in a site- and cofactor-dependent manner
    Francesca Parolini, Roberto Tira, Carlo Giorgio Barracchia, Francesca Munari, Stefano Capaldi, Mariapina D’Onofrio, Michael Assfalg · 2022 · International Journal of Biological Macromolecules
49. The structure and phase of tau: from monomer to amyloid filament
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50. 14-3-3/Tau Interaction and Tau Amyloidogenesis
    Yuwen Chen, Xingyu Chen, Zhiyang Yao, Yuqi Shi, Junwen Xiong, Jingjing Zhou, Zhengding Su, Yongqi Huang · 2019 · Journal of Molecular Neuroscience
51. Heparan Sulfate as a Therapeutic Target in Tauopathies: Insights From Zebrafish
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52. Tau Protein and Tauopathies: Exploring Tau Protein–Protein and Microtubule Interactions, Cross‐Interactions and Therapeutic Strategies
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53. Molecular dynamics simulation of the phosphorylation-induced conformational changes of a tau peptide fragment
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54. Molecular Mechanism of Tau Aggregation Induced by Anionic and Cationic Dyes
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55. Structural evaluations of tau protein conformation: methodologies and approaches
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56. Biomolecular condensation of the microtubule-associated protein tau
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57. Sequence-Dependent Backbone Dynamics of Intrinsically Disordered Proteins
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58. N368-Tau fragments generated by legumain are detected only in trace amount in the insoluble Tau aggregates isolated from AD brain
    Schlegel, Kerstin, Awwad, Khader, Heym, Roland G., Holzinger, David, Doell, Annika, Barghorn, Stefan, Jahn, Thomas R., Klein, Corinna, Mordashova, Yulia, Schulz, Michael et al. · 2019 · Acta Neuropathologica Communications
59. Cellular and molecular mechanisms of pathological tau phosphorylation in traumatic brain injury: implications for chronic traumatic encephalopathy
    Neil S. Donison, Jacqueline Palik, Kathryn Volkening, Michael Joseph Strong · 2025 · Molecular Neurodegeneration
60. Post-translational modifications within tau paired helical filament nucleating motifs perturb microtubule interactions and oligomer formation
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61. Molecular insights into the reversible formation of tau protein fibrils
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62. Aggregation of S6 in a quasi-native state by sub-micellar SDS
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63. NMR Meets Tau: Insights into Its Function and Pathology
    Guy M. Lippens, Isabelle Landrieu, Caroline Smet‐Nocca, Isabelle Huvent, Neha S. Gandhi, Benoı̂t Gigant, Clément Despres, Haoling Qi, Juan M. Lopez · 2016 · Biomolecules
64. Inhibition of Tau amyloid fibril formation by folic acid: In-vitro and theoretical studies
    Samin Ghasemzadeh, Gholam Hossein Riazi · 2019 · International Journal of Biological Macromolecules
65. Distance-Based Metrics for Comparing Conformational Ensembles of Intrinsically Disordered Proteins
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66. Increased G3BP2-Tau interaction in tauopathies is a natural defense against Tau aggregation
    Congwei Wang, Marco Terrigno, Juan Li, Tania Distler, Nikhil Janak Pandya, Martin Ebeling, Stefka Tyanova, Jeroen J.M. Hoozemans, Anke A. Dijkstra, Luisa Fuchs et al. · 2023 · Neuron
67. Remodeling of the conformational ensemble of the repeat domain of tau by an aggregation enhancer
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68. Pharmacological Modulators of Tau Aggregation and Spreading
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69. Cytotoxic tau released from lung microvascular endothelial cells upon infection with Pseudomonas aeruginosa promotes neuronal tauopathy
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70. Expanding to fill the gap: A possible role for inert biopolymers in regulating the extent of the ‘macromolecular crowding’ effect
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71. Appraisal of role of the polyanionic inducer length on amyloid formation by 412-residue 1N4R Tau protein: A comparative study
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72. The metamorphic nature of the Tau protein: dynamic flexibility comes at a cost
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73. Removal of Pattern-breaking Sequences in Microtubule Binding Repeats Produces Instantaneous Tau Aggregation and Toxicity
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74. ATP Kinetically Modulates Pathogenic Tau Fibrillations
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75. Therapeutic Strategies for Restoring Tau Homeostasis
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76. Alzheimer’s Disease and Tau Self-Assembly: In the Search of the Missing Link
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77. Revisiting the therapeutic landscape of tauopathies: assessing the current pipeline and clinical trials
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78. Phosphorylation-Induced Structural Reorganization in Tau-Paired Helical Filaments
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79. Tau liquid–liquid phase separation: At the crossroads of tau physiology and tauopathy
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80. Conformations of Microtubule-Associated Protein Tau Mapped by Fluorescence Resonance Energy Transfer
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81. Secondary nucleating sequences affect kinetics and thermodynamics of tau aggregation
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82. Dysregulation of Microtubule Stability Impairs Morphofunctional Connectivity in Primary Neuronal Networks
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83. Kinetic and thermodynamic study of beta-Boswellic acid interaction with Tau protein investigated by surface plasmon resonance and molecular modeling methods
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84. Activating autophagy to eliminate toxic protein aggregates with small molecules in neurodegenerative diseases
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85. Monoclonal antibody Y01 prevents tauopathy progression induced by lysine 280–acetylated tau in cell and mouse models
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86. Tau aggregation and seeding analyses of two novel MAPT variants found in patients with motor neuron disease and progressive parkinsonism
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87. Pyridine-2,3-dicarboxylate, quinolinic acid, induces 1N4R Tau amyloid aggregation in vitro: Another evidence for the detrimental effect of the inescapable endogenous neurotoxin
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88. The Structure Biology of Tau and Clue for Aggregation Inhibitor Design
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89. Alternative Conformations of the Tau Repeat Domain in Complex with an Engineered Binding Protein
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90. Solid-state NMR investigation of the involvement of the P2 region in tau amyloid fibrils
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91. The Role of Disordered Regions in Orchestrating the Properties of Multidomain Proteins: The SARS-CoV-2 Nucleocapsid Protein and Its Interaction with Enoxaparin
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92. Dityrosine cross-linking and its potential roles in Alzheimer’s disease
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93. Finding Order within Disorder: Elucidating the Structure of Proteins Associated with Neurodegenerative Disease
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94. Tau Interacting Proteins: Gaining Insight into the Roles of Tau in Health and Disease
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95. Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression
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96. Upregulated levels and pathological aggregation of abnormally phosphorylated Tau-protein in children with neurodevelopmental disorders
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97. Interactions between Microtubule-Associated Protein Tau (MAPT) and Small Molecules
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98. Stoichiometric 14-3-3ζ binding promotes phospho-Tau microtubule dissociation and reduces aggregation and condensation
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99. Impact of the Hereditary P301L Mutation on the Correlated Conformational Dynamics of Human Tau Protein Revealed by the Paramagnetic Relaxation Enhancement NMR Experiments
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100. Heparin remodels the microtubule-binding repeat R3 of Tau protein towards fibril-prone conformations
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