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The elusive tau molecular structures: can we translate the recent breakthroughs into new targets for intervention?

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Fichou, Yann Al-Hilaly, Youssra K Devred, François Smet-Nocca, Caroline Tsvetkov, Philipp O Hanseeuw, Bernard [UCL] Landrieu, Isabelle

Insights into tau molecular structures have advanced significantly in recent years. This field has been the subject of recent breakthroughs, including the first cryo-electron microscopy structures of tau filaments from Alzheimer's and Pick's disease inclusions, as well as the structure of the repeat regions of tau bound to microtubules. Tau structure covers various species as the tau protein itself takes many forms. We will here address a range of studies that help to define the many facets of tau protein structures and how they translate into pathogenic forms. New results shed light on previous data that need now to be revisited in order to up-date our knowledge of tau molecular structure. Finally, we explore how these data can contribute the important medical aspects of this research - diagnosis and therapeutics.

Document type Article de périodique (Journal article) – Synthèse de littérature
Access type Accès libre
Publication date 2019
Language Anglais
Journal information "Acta neuropathologica communications" - Vol. 7, no. 1, p. 31 [1-17] (2019)
Peer reviewed yes
Publisher BioMed Central ((United Kingdom) London)
e-issn 2051-5960
Publication status Publié
Affiliations UCL - SSS/IONS/NEUR - Clinical Neuroscience
UCL - (SLuc) Service de neurologie
Keywords Alzheimer’s disease diagnosis ; Amyloid ; Tauopathies ; Alzheimer’s disease ; Tau structure ; Tau aggregation
Links
  1. Abraha A, Ghoshal N, Gamblin TC, Cryns V, Berry RW, Kuret J, Binder LI (2000) C-terminal inhibition of tau assembly in vitro and in Alzheimer’s disease. J Cell Sci 113(Pt 21):3737–3745
  2. Ait-Bouziad Nadine, Lv Guohua, Mahul-Mellier Anne-Laure, Xiao Shifeng, Zorludemir Gizem, Eliezer David, Walz Thomas, Lashuel Hilal A., Discovery and characterization of stable and toxic Tau/phospholipid oligomeric complexes, 10.1038/s41467-017-01575-4
  3. Al-Hilaly Youssra K., Pollack Saskia J., Rickard Janet E., Simpson Michael, Raulin Ana-Caroline, Baddeley Thomas, Schellenberger Pascale, Storey John M.D., Harrington Charles R., Wischik Claude M., Serpell Louise C., Cysteine-Independent Inhibition of Alzheimer's Disease-like Paired Helical Filament Assembly by Leuco-Methylthioninium (LMT), 10.1016/j.jmb.2018.08.010
  4. Al-Hilaly Youssra K., Pollack Saskia J., Vadukul Devkee M., Citossi Francesca, Rickard Janet E., Simpson Michael, Storey John M.D., Harrington Charles R., Wischik Claude M., Serpell Louise C., Alzheimer's Disease-like Paired Helical Filament Assembly from Truncated Tau Protein Is Independent of Disulfide Crosslinking, 10.1016/j.jmb.2017.09.007
  5. Alonso A. d. C., Zaidi T., Novak M., Grundke-Iqbal I., Iqbal K., Hyperphosphorylation induces self-assembly of   into tangles of paired helical filaments/straight filaments, 10.1073/pnas.121119298
  6. Alonso Alejandra del C., Grundke-Iqbal Inge, Iqbal Khalid, Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules, 10.1038/nm0796-783
  7. Alonso A. C., Zaidi T., Grundke-Iqbal I., Iqbal K., Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease., 10.1073/pnas.91.12.5562
  8. Ambadipudi Susmitha, Biernat Jacek, Riedel Dietmar, Mandelkow Eckhard, Zweckstetter Markus, Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau, 10.1038/s41467-017-00480-0
  9. Ando Kunie, Leroy Karelle, Héraud Céline, Yilmaz Zehra, Authelet Michèle, Suain Valèrie, De Decker Robert, Brion Jean-Pierre, Accelerated Human Mutant Tau Aggregation by Knocking Out Murine Tau in a Transgenic Mouse Model, 10.1016/j.ajpath.2010.10.034
  10. Andorfer Cathy, Kress Yvonne, Espinoza Marisol, De Silva Rohan, Tucker Kerry L., Barde Yves-Alain, Duff Karen, Davies Peter, Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms : Pathology of non-mutant tau in transgenic mice, 10.1046/j.1471-4159.2003.01879.x
  11. Andreasson Ulf, Kuhlmann Julia, Pannee Josef, Umek Robert M., Stoops Erik, Vanderstichele Hugo, Matzen Anja, Vandijck Manu, Dauwe Martine, Leinenbach Andreas, Rutz Sandra, Portelius Erik, Zegers Ingrid, Zetterberg Henrik, Blennow Kaj, Commutability of the certified reference materials for the standardization of β-amyloid 1-42 assay in human cerebrospinal fluid: lessons for tau and β-amyloid 1-40 measurements, 10.1515/cclm-2018-0147
  12. Andronesi Ovidiu C., Bergen Martin von, Biernat Jacek, Seidel Karsten, Griesinger Christian, Mandelkow Eckhard, Baldus Marc, Characterization of Alzheimer’s-like Paired Helical Filaments from the Core Domain of Tau Protein Using Solid-State NMR Spectroscopy, 10.1021/ja7100517
  13. Armstrong Richard A., Lantos Peter L., Cairns Nigel J., What determines the molecular composition of abnormal protein aggregates in neurodegenerative disease?, 10.1111/j.1440-1789.2008.00916.x
  14. Asadollahi Kazem, Riazi Gholamhossein, Rabbani Chadegani Azra, Rafiee Saharnaz, DNA-binding mode transition of tau in the presence of Zinc ions, 10.1080/07391102.2017.1343684
  15. Barghorn Stefan, Davies Peter, Mandelkow Eckhard, Tau Paired Helical Filaments from Alzheimer's Disease Brain and Assembled in Vitro Are Based on β-Structure in the Core Domain†, 10.1021/bi0357006
  16. Barthélemy Nicolas R, Fenaille François, Hirtz Christophe, Sergeant Nicolas, Schraen-Maschke Susanna, Vialaret Jérôme, Buée Luc, Gabelle Audrey, Junot Christophe, Lehmann Sylvain, Becher François, Tau Protein Quantification in Human Cerebrospinal Fluid by Targeted Mass Spectrometry at High Sequence Coverage Provides Insights into Its Primary Structure Heterogeneity, 10.1021/acs.jproteome.5b01001
  17. Benhelli-Mokrani Houda, Mansuroglu Zeyni, Chauderlier Alban, Albaud Benoit, Gentien David, Sommer Sabrina, Schirmer Claire, Laqueuvre Lucie, Josse Thibaut, Buée Luc, Lefebvre Bruno, Galas Marie-Christine, Souès Sylvie, Bonnefoy Eliette, Genome-wide identification of genic and intergenic neuronal DNA regions bound by Tau protein under physiological and stress conditions, 10.1093/nar/gky929
  18. Berriman J., Serpell L. C., Oberg K. A., Fink A. L., Goedert M., Crowther R. A., Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-  structure, 10.1073/pnas.1530287100
  19. Bibow Stefan, Mukrasch Marco D., Chinnathambi Subashchandrabose, Biernat Jacek, Griesinger Christian, Mandelkow Eckhard, Zweckstetter Markus, The Dynamic Structure of Filamentous Tau, 10.1002/anie.201105493
  20. Bourré Gwendoline, Cantrelle François-Xavier, Kamah Amina, Chambraud Béatrice, Landrieu Isabelle, Smet-Nocca Caroline, Direct Crosstalk Between O-GlcNAcylation and Phosphorylation of Tau Protein Investigated by NMR Spectroscopy, 10.3389/fendo.2018.00595
  21. Braak Heiko, Braak Eva, Staging of alzheimer's disease-related neurofibrillary changes, 10.1016/0197-4580(95)00021-6
  22. Braak H, Braak E, Frequency of Stages of Alzheimer-Related Lesions in Different Age Categories, 10.1016/s0197-4580(97)00056-0
  23. Brion Jean-Pierre, Flament-Durand Jacqueline, Dustin Pierre, ALZHEIMER'S DISEASE AND TAU PROTEINS, 10.1016/s0140-6736(86)90495-2
  24. Carmel Gilles, Mager Edward M., Binder Lester I., Kuret Jeff, The Structural Basis of Monoclonal Antibody Alz50's Selectivity for Alzheimer's Disease Pathology, 10.1074/jbc.271.51.32789
  25. Chhatwal Jasmeer P., Schultz Aaron P., Marshall Gad A., Boot Brendon, Gomez-Isla Teresa, Dumurgier Julien, LaPoint Molly, Scherzer Clemens, Roe Allyson D., Hyman Bradley T., Sperling Reisa A., Johnson Keith A., Temporal T807 binding correlates with CSF tau and phospho-tau in normal elderly, 10.1212/wnl.0000000000003050
  26. Chien David T., Szardenings A. Katrin, Bahri Shadfar, Walsh Joseph C., Mu Fanrong, Xia Chunfang, Shankle William R., Lerner Alan J., Su Min-Ying, Elizarov Arkadij, Kolb Hartmuth C., Early Clinical PET Imaging Results with the Novel PHF-Tau Radioligand [F18]-T808, 10.3233/jad-130098
  27. Chukwu Jessica E., Pedersen Jan T., Pedersen Lars Ø., Volbracht Christiane, Sigurdsson Einar M., Kong Xiang-Peng, Tau Antibody Structure Reveals a Molecular Switch Defining a Pathological Conformation of the Tau Protein, 10.1038/s41598-018-24276-4
  28. Craven Kristen M., Kochen William R., Hernandez Carlos M., Flinn Jane M., Zinc Exacerbates Tau Pathology in a Tau Mouse Model, 10.3233/jad-180151
  29. Daebel Venita, Chinnathambi Subashchandrabose, Biernat Jacek, Schwalbe Martin, Habenstein Birgit, Loquet Antoine, Akoury Elias, Tepper Katharina, Müller Henrik, Baldus Marc, Griesinger Christian, Zweckstetter Markus, Mandelkow Eckhard, Vijayan Vinesh, Lange Adam, β-Sheet Core of Tau Paired Helical Filaments Revealed by Solid-State NMR, 10.1021/ja305470p
  30. Dagley Alexander, LaPoint Molly, Huijbers Willem, Hedden Trey, McLaren Donald G., Chatwal Jasmeer P., Papp Kathryn V., Amariglio Rebecca E., Blacker Deborah, Rentz Dorene M., Johnson Keith A., Sperling Reisa A., Schultz Aaron P., Harvard Aging Brain Study: Dataset and accessibility, 10.1016/j.neuroimage.2015.03.069
  31. Dai Chun-ling, Tung Yunn Chyn, Liu Fei, Gong Cheng-Xin, Iqbal Khalid, Tau passive immunization inhibits not only tau but also Aβ pathology, 10.1186/s13195-016-0227-5
  32. de Calignon Alix, Fox Leora M., Pitstick Rose, Carlson George A., Bacskai Brian J., Spires-Jones Tara L., Hyman Bradley T., Caspase activation precedes and leads to tangles, 10.1038/nature08890
  33. de Calignon Alix, Polydoro Manuela, Suárez-Calvet Marc, William Christopher, Adamowicz David H., Kopeikina Kathy J., Pitstick Rose, Sahara Naruhiko, Ashe Karen H., Carlson George A., Spires-Jones Tara L., Hyman Bradley T., Propagation of Tau Pathology in a Model of Early Alzheimer's Disease, 10.1016/j.neuron.2011.11.033
  34. De Vos Ann, Struyfs Hanne, Jacobs Dirk, Fransen Erik, Klewansky Tom, De Roeck Ellen, Robberecht Caroline, Van Broeckhoven Christine, Duyckaerts Charles, Engelborghs Sebastiaan, Vanmechelen Eugeen, The Cerebrospinal Fluid Neurogranin/BACE1 Ratio is a Potential Correlate of Cognitive Decline in Alzheimer’s Disease, 10.3233/jad-160227
  35. Despres Clément, Byrne Cillian, Qi Haoling, Cantrelle François-Xavier, Huvent Isabelle, Chambraud Béatrice, Baulieu Etienne-Emile, Jacquot Yves, Landrieu Isabelle, Lippens Guy, Smet-Nocca Caroline, Identification of the Tau phosphorylation pattern that drives its aggregation, 10.1073/pnas.1708448114
  36. Dominy Stephen S., Lynch Casey, Ermini Florian, Benedyk Malgorzata, Marczyk Agata, Konradi Andrei, Nguyen Mai, Haditsch Ursula, Raha Debasish, Griffin Christina, Holsinger Leslie J., Arastu-Kapur Shirin, Kaba Samer, Lee Alexander, Ryder Mark I., Potempa Barbara, Mydel Piotr, Hellvard Annelie, Adamowicz Karina, Hasturk Hatice, Walker Glenn D., Reynolds Eric C., Faull Richard L. M., Curtis Maurice A., Dragunow Mike, Potempa Jan, Porphyromonas gingivalis in Alzheimer’s disease brains: Evidence for disease causation and treatment with small-molecule inhibitors, 10.1126/sciadv.aau3333
  37. Dujardin Simon, Bégard Séverine, Caillierez Raphaëlle, Lachaud Cédrick, Carrier Sébastien, Lieger Sarah, Gonzalez Jose A., Deramecourt Vincent, Déglon Nicole, Maurage Claude-Alain, Frosch Matthew P., Hyman Bradley T., Colin Morvane, Buée Luc, Different tau species lead to heterogeneous tau pathology propagation and misfolding, 10.1186/s40478-018-0637-7
  38. Eftekharzadeh Bahareh, Daigle J. Gavin, Kapinos Larisa E., Coyne Alyssa, Schiantarelli Julia, Carlomagno Yari, Cook Casey, Miller Sean J., Dujardin Simon, Amaral Ana S., Grima Jonathan C., Bennett Rachel E., Tepper Katharina, DeTure Michael, Vanderburg Charles R., Corjuc Bianca T., DeVos Sarah L., Gonzalez Jose Antonio, Chew Jeannie, Vidensky Svetlana, Gage Fred H., Mertens Jerome, Troncoso Juan, Mandelkow Eckhard, Salvatella Xavier, Lim Roderick Y.H., Petrucelli Leonard, Wegmann Susanne, Rothstein Jeffrey D., Hyman Bradley T., Tau Protein Disrupts Nucleocytoplasmic Transport in Alzheimer’s Disease, 10.1016/j.neuron.2018.07.039
  39. Eschmann Neil A., Georgieva Elka R., Ganguly Pritam, Borbat Peter P., Rappaport Maxime D., Akdogan Yasar, Freed Jack H., Shea Joan-Emma, Han Songi, Signature of an aggregation-prone conformation of tau, 10.1038/srep44739
  40. Falcon Benjamin, Zhang Wenjuan, Murzin Alexey G., Murshudov Garib, Garringer Holly J., Vidal Ruben, Crowther R. Anthony, Ghetti Bernardino, Scheres Sjors H. W., Goedert Michel, Structures of filaments from Pick’s disease reveal a novel tau protein fold, 10.1038/s41586-018-0454-y
  41. Falcon Benjamin, Zhang Wenjuan, Schweighauser Manuel, Murzin Alexey G., Vidal Ruben, Garringer Holly J., Ghetti Bernardino, Scheres Sjors H. W., Goedert Michel, Tau filaments from multiple cases of sporadic and inherited Alzheimer’s disease adopt a common fold, 10.1007/s00401-018-1914-z
  42. Fichou Yann, Lin Yanxian, Rauch Jennifer N., Vigers Michael, Zeng Zhikai, Srivastava Madhur, Keller Timothy J., Freed Jack H., Kosik Kenneth S., Han Songi, Cofactors are essential constituents of stable and seeding-active tau fibrils, 10.1073/pnas.1810058115
  43. Fichou Yann, Vigers Michael, Goring Andrew K., Eschmann Neil A., Han Songi, Heparin-induced tau filaments are structurally heterogeneous and differ from Alzheimer's disease filaments, 10.1039/c8cc01355a
  44. Fitzpatrick Anthony W. P., Falcon Benjamin, He Shaoda, Murzin Alexey G., Murshudov Garib, Garringer Holly J., Crowther R. Anthony, Ghetti Bernardino, Goedert Michel, Scheres Sjors H. W., Cryo-EM structures of tau filaments from Alzheimer’s disease, 10.1038/nature23002
  45. Gamblin T. C., Chen F., Zambrano A., Abraha A., Lagalwar S., Guillozet A. L., Lu M., Fu Y., Garcia-Sierra F., LaPointe N., Miller R., Berry R. W., Binder L. I., Cryns V. L., Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease, 10.1073/pnas.1630428100
  46. Gandhi Neha S., Landrieu Isabelle, Byrne Cillian, Kukic Predrag, Amniai Laziza, Cantrelle François-Xavier, Wieruszeski Jean-Michel, Mancera Ricardo L., Jacquot Yves, Lippens Guy, A Phosphorylation-Induced Turn Defines the Alzheimer’s Disease AT8 Antibody Epitope on the Tau Protein, 10.1002/anie.201501898
  47. Garnier Cyrille, Devred François, Byrne Deborah, Puppo Rémy, Roman Andrei Yu., Malesinski Soazig, Golovin Andrey V., Lebrun Régine, Ninkina Natalia N., Tsvetkov Philipp O., Zinc binding to RNA recognition motif of TDP-43 induces the formation of amyloid-like aggregates, 10.1038/s41598-017-07215-7
  48. Gauthier-Kemper Anne, Suárez Alonso María, Sündermann Frederik, Niewidok Benedikt, Fernandez Maria-Pilar, Bakota Lidia, Heinisch Jürgen Josef, Brandt Roland, Annexins A2 and A6 interact with the extreme N terminus of tau and thereby contribute to tau's axonal localization, 10.1074/jbc.ra117.000490
  49. Gigant Benoît, Landrieu Isabelle, Fauquant Caroline, Barbier Pascale, Huvent Isabelle, Wieruszeski Jean-Michel, Knossow Marcel, Lippens Guy, Mechanism of Tau-Promoted Microtubule Assembly As Probed by NMR Spectroscopy, 10.1021/ja504864m
  50. Ginsberg S. D., Galvin J. E., Chiu T.-S., Lee Virginia M.-Y., Masliah Eliezer, Trojanowski John Q., RNA sequestration to pathological lesions of neurodegenerative diseases, 10.1007/s004010050923
  51. Goedert M., Jakes R., Spillantini M. G., Hasegawa M., Smith M. J., Crowther R. A., Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans, 10.1038/383550a0
  52. Goedert Michel, Spillantini Maria Grazia, Propagation of Tau aggregates, 10.1186/s13041-017-0298-7
  53. Goedert M., Spillantini M.G., Jakes R., Rutherford D., Crowther R.A., Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease, 10.1016/0896-6273(89)90210-9
  54. Grundke-Iqbal I, Iqbal K, Quinlan M, Tung YC, Zaidi MS, Wisniewski HM (1986) Microtubule-associated protein tau. A component of Alzheimer paired helical filaments. J Biol Chem 261:6084–6089
  55. Grundke-Iqbal I., Iqbal K., Tung Y. C., Quinlan M., Wisniewski H. M., Binder L. I., Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology., 10.1073/pnas.83.13.4913
  56. Hanger Diane P., Betts Joanna C., Loviny Thérèse L. F., Blackstock Walter P., Anderton Brian H., New Phosphorylation Sites Identified in Hyperphosphorylated Tau (Paired Helical Filament-Tau) from Alzheimer's Disease Brain Using Nanoelectrospray Mass Spectrometry, 10.1046/j.1471-4159.1998.71062465.x
  57. Hanseeuw Bernard J., Betensky Rebecca A., Schultz Aaron P., Papp Kathryn V., Mormino Elizabeth C., Sepulcre Jorge, Bark John S., Cosio Danielle M., LaPoint Molly, Chhatwal Jasmeer P., Rentz Dorene M., Sperling Reisa A., Johnson Keith A., Fluorodeoxyglucose metabolism associated with tau-amyloid interaction predicts memory decline : Tau, Amyloid, FDG, and Memory in Normal Aging, 10.1002/ana.24910
  58. Hanseeuw Bernard J., Mormino Beth C., Becker Alex, Sepulcre Jorge, Papp Kate V., Schultz Aaron P., Jacobs Heidi IL., Cosio Danielle M., Chhatwal Jasmeer P., Sperling Reisa A., Johnson Keith, LONGITUDINAL TAU ACCUMULATION IS ASSOCIATED WITH COGNITIVE DECLINE IN NORMAL ELDERLY, 10.1016/j.jalz.2017.06.2556
  59. Hansson Oskar, Mormino Elizabeth C, Is longitudinal tau PET ready for use in Alzheimer’s disease clinical trials?, 10.1093/brain/awy065
  60. Harrington C. R., Mukaetova-Ladinska E. B., Hills R., Edwards P. C., Montejo de Garcini E., Novak M., Wischik C. M., Measurement of distinct immunochemical presentations of tau protein in Alzheimer disease., 10.1073/pnas.88.13.5842
  61. Harrison Theresa M., La Joie Renaud, Maass Anne, Baker Suzanne L., Swinnerton Kaitlin, Fenton Laura, Mellinger Taylor J., Edwards Lauren, Pham Julie, Miller Bruce L., Rabinovici Gil D., Jagust William J., Longitudinal tau accumulation and atrophy in aging and alzheimer disease : Tau-PET and Atrophy, 10.1002/ana.25406
  62. Hasegawa Hitomi, Holm Liisa, Advances and pitfalls of protein structural alignment, 10.1016/j.sbi.2009.04.003
  63. Himmler A, Drechsel D, Kirschner M W, Martin D W, Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains., 10.1128/mcb.9.4.1381
  64. Hu Ji-Ying, Zhang De-Lin, Liu Xiao-Ling, Li Xue-Shou, Cheng Xiao-Qing, Chen Jie, Du Hai-Ning, Liang Yi, Pathological concentration of zinc dramatically accelerates abnormal aggregation of full-length human Tau and thereby significantly increases Tau toxicity in neuronal cells, 10.1016/j.bbadis.2016.11.022
  65. Huang Yunpeng, Wu Zhihao, Cao Yu, Lang Minglin, Lu Bingwei, Zhou Bing, Zinc Binding Directly Regulates Tau Toxicity Independent of Tau Hyperphosphorylation, 10.1016/j.celrep.2014.06.047
  66. Huvent Isabelle, Kamah Amina, Cantrelle François-Xavier, Barois Nicolas, Slomianny Christian, Smet-Nocca Caroline, Landrieu Isabelle, Lippens Guy, A functional fragment of Tau forms fibers without the need for an intermolecular cysteine bridge, 10.1016/j.bbrc.2014.01.161
  67. Iqbal Khalid, Alonso Alejandra del C., Gong Cheng-Xin, Khatoon Sabiha, Singh Toolsee J., Grundke-Iqbal Inge, Mechanism of neurofibrillary degeneration in Alzheimer's disease, 10.1007/bf02816111
  68. Jack Clifford R, Wiste Heather J, Schwarz Christopher G, Lowe Val J, Senjem Matthew L, Vemuri Prashanthi, Weigand Stephen D, Therneau Terry M, Knopman Dave S, Gunter Jeffrey L, Jones David T, Graff-Radford Jonathan, Kantarci Kejal, Roberts Rosebud O, Mielke Michelle M, Machulda Mary M, Petersen Ronald C, Longitudinal tau PET in ageing and Alzheimer’s disease, 10.1093/brain/awy059
  69. Jadhav Santosh, Avila Jesus, Schöll Michael, Kovacs Gabor G., Kövari Enikö, Skrabana Rostislav, Evans Lewis D, Kontsekova Eva, Malawska Barbara, de Silva Rohan, Buee Luc, Zilka Norbert, A walk through tau therapeutic strategies, 10.1186/s40478-019-0664-z
  70. Jakes R., Novak M., Davison M., Wischik C.M., Identification of 3- and 4-repeat tau isoforms within the PHF in Alzheimer's disease., 10.1002/j.1460-2075.1991.tb07820.x
  71. Jeganathan Sadasivam, Hascher Antje, Chinnathambi Subashchandrabose, Biernat Jacek, Mandelkow Eva-Maria, Mandelkow Eckhard, Proline-directed Pseudo-phosphorylation at AT8 and PHF1 Epitopes Induces a Compaction of the Paperclip Folding of Tau and Generates a Pathological (MC-1) Conformation, 10.1074/jbc.m805300200
  72. Johnson Keith A., Schultz Aaron, Betensky Rebecca A., Becker J. Alex, Sepulcre Jorge, Rentz Dorene, Mormino Elizabeth, Chhatwal Jasmeer, Amariglio Rebecca, Papp Kate, Marshall Gad, Albers Mark, Mauro Samantha, Pepin Lesley, Alverio Jonathan, Judge Kelly, Philiossaint Marlie, Shoup Timothy, Yokell Daniel, Dickerson Bradford, Gomez-Isla Teresa, Hyman Bradley, Vasdev Neil, Sperling Reisa, Tau positron emission tomographic imaging in aging and early Alzheimer disease : Tau PET in Aging and Early AD, 10.1002/ana.24546
  73. Kadavath Harindranath, Hofele Romina V., Biernat Jacek, Kumar Satish, Tepper Katharina, Urlaub Henning, Mandelkow Eckhard, Zweckstetter Markus, Tau stabilizes microtubules by binding at the interface between tubulin heterodimers, 10.1073/pnas.1504081112
  74. Karch Celeste M., Jeng Amanda T., Goate Alison M., Extracellular Tau Levels Are Influenced by Variability in Tau That Is Associated with Tauopathies, 10.1074/jbc.m112.380642
  75. Kaufman Sarah K., Sanders David W., Thomas Talitha L., Ruchinskas Allison J., Vaquer-Alicea Jaime, Sharma Apurwa M., Miller Timothy M., Diamond Marc I., Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In Vivo, 10.1016/j.neuron.2016.09.055
  76. Kellogg Elizabeth H., Hejab Nisreen M. A., Poepsel Simon, Downing Kenneth H., DiMaio Frank, Nogales Eva, Near-atomic model of microtubule-tau interactions, 10.1126/science.aat1780
  77. Kepe Vladimir, Bordelon Yvette, Boxer Adam, Huang Sung-Cheng, Liu Jie, Thiede Frederick C., Mazziotta John C., Mendez Mario F., Donoghue Natacha, Small Gary W., Barrio Jorge R., PET Imaging of Neuropathology in Tauopathies: Progressive Supranuclear Palsy, 10.3233/jad-130032
  78. La Joie Renaud, Bejanin Alexandre, Fagan Anne M., Ayakta Nagehan, Baker Suzanne L., Bourakova Viktoriya, Boxer Adam L., Cha Jungho, Karydas Anna, Jerome Gina, Maass Anne, Mensing Ashley, Miller Zachary A., O'Neil James P., Pham Julie, Rosen Howard J., Tsai Richard, Visani Adrienne V., Miller Bruce L., Jagust William J., Rabinovici Gil D., Associations between [18F]AV1451 tau PET and CSF measures of tau pathology in a clinical sample, 10.1212/wnl.0000000000004860
  79. Landau Meytal, Sawaya Michael R., Faull Kym F., Laganowsky Arthur, Jiang Lin, Sievers Stuart A., Liu Jie, Barrio Jorge R., Eisenberg David, Towards a Pharmacophore for Amyloid, 10.1371/journal.pbio.1001080
  80. Lee Christopher M., Jacobs Heidi I.L., Marquié Marta, Becker John A., Andrea Nicolas V., Jin David S., Schultz Aaron P., Frosch Matthew P., Gómez-Isla Teresa, Sperling Reisa A., Johnson Keith A., 18F-Flortaucipir Binding in Choroid Plexus: Related to Race and Hippocampus Signal, 10.3233/jad-170840
  81. Lee G, Cowan N, Kirschner M, The primary structure and heterogeneity of tau protein from mouse brain, 10.1126/science.3122323
  82. Li Bin, Chohan Muhammad Omar, Grundke-Iqbal Inge, Iqbal Khalid, Disruption of microtubule network by Alzheimer abnormally hyperphosphorylated tau, 10.1007/s00401-007-0207-8
  83. Li Tong, Braunstein Kerstin E., Zhang Juhong, Lau Ashley, Sibener Leslie, Deeble Christopher, Wong Philip C., The neuritic plaque facilitates pathological conversion of tau in an Alzheimer’s disease mouse model, 10.1038/ncomms12082
  84. Liu Chang, Song Xiaomin, Nisbet Rebecca, Götz Jürgen, Co-immunoprecipitation with Tau Isoform-specific Antibodies Reveals Distinct Protein Interactions and Highlights a Putative Role for 2N Tau in Disease, 10.1074/jbc.m115.641902
  85. Liu F., Iqbal K., Grundke-Iqbal I., Hart G. W., Gong C.-X., O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease, 10.1073/pnas.0400348101
  86. Liu F., Shi J., Tanimukai H., Gu J., Gu J., Grundke-Iqbal I., Iqbal K., Gong C.-X., Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease, 10.1093/brain/awp099
  87. Luk Connie, Compta Yaroslau, Magdalinou Nadia, Martí Maria José, Hondhamuni Geshanthi, Zetterberg Henrik, Blennow Kaj, Constantinescu Radu, Pijnenburg Yolande, Mollenhauer Brit, Trenkwalder Claudia, Van Swieten John, Chiu Wan Zheng, Borroni Barbara, Cámara Ana, Cheshire Perdita, Williams David R., Lees Andrew J., de Silva Rohan, Development and assessment of sensitive immuno-PCR assays for the quantification of cerebrospinal fluid three- and four-repeat tau isoforms in tauopathies, 10.1111/j.1471-4159.2012.07911.x
  88. Mair Waltraud, Muntel Jan, Tepper Katharina, Tang Shaojun, Biernat Jacek, Seeley William W., Kosik Kenneth S., Mandelkow Eckhard, Steen Hanno, Steen Judith A., FLEXITau: Quantifying Post-translational Modifications of Tau Protein in Vitro and in Human Disease, 10.1021/acs.analchem.5b04509
  89. Malia Thomas J., Teplyakov Alexey, Ernst Robin, Wu Sheng-Jiun, Lacy Eilyn R., Liu Xuesong, Vandermeeren Marc, Mercken Marc, Luo Jinquan, Sweet Raymond W., Gilliland Gary L., Epitope mapping and structural basis for the recognition of phosphorylated tau by the anti-tau antibody AT8 : Epitope Mapping and Structure of AT8, 10.1002/prot.24988
  90. Malki Idir, Cantrelle François-Xavier, Sottejeau Yoann, Lippens Guy, Lambert Jean-Charles, Landrieu Isabelle, Regulation of the interaction between the neuronal BIN1 isoform 1 and Tau proteins - role of the SH3 domain, 10.1111/febs.14185
  91. Margittai M., Langen R., Template-assisted filament growth by parallel stacking of tau, 10.1073/pnas.0401911101
  92. Marquié Marta, Normandin Marc D., Vanderburg Charles R., Costantino Isabel M., Bien Elizabeth A., Rycyna Lisa G., Klunk William E., Mathis Chester A., Ikonomovic Milos D., Debnath Manik L., Vasdev Neil, Dickerson Bradford C., Gomperts Stephen N., Growdon John H., Johnson Keith A., Frosch Matthew P., Hyman Bradley T., Gómez-Isla Teresa, Validating novel tau positron emission tomography tracer [F-18]-AV-1451 (T807) on postmortem brain tissue : Validation of PET Tracer, 10.1002/ana.24517
  93. Martinho Marlène, Allegro Diane, Huvent Isabelle, Chabaud Charlotte, Etienne Emilien, Kovacic Hervé, Guigliarelli Bruno, Peyrot Vincent, Landrieu Isabelle, Belle Valérie, Barbier Pascale, Two Tau binding sites on tubulin revealed by thiol-disulfide exchanges, 10.1038/s41598-018-32096-9
  94. Mattsson Niklas, Zetterberg Henrik, Janelidze Shorena, Insel Philip S., Andreasson Ulf, Stomrud Erik, Palmqvist Sebastian, Baker David, Tan Hehir Cristina A., Jeromin Andreas, Hanlon David, Song Linan, Shaw Leslie M., Trojanowski John Q., Weiner Michael W., Hansson Oskar, Blennow Kaj, Plasma tau in Alzheimer disease, 10.1212/wnl.0000000000003246
  95. McMillan Pamela, Korvatska Elena, Poorkaj Parvoneh, Evstafjeva Zana, Robinson Linda, Greenup Lynne, Leverenz James, Schellenberg Gerard D., D'Souza Ian, Tau isoform regulation is region- and cell-specific in mouse brain, 10.1002/cne.21867
  96. Medina Miguel, Avila Jesús, The need for better AD animal models, 10.3389/fphar.2014.00227
  97. Medina Miguel, Hernández Félix, Avila Jesús, New Features about Tau Function and Dysfunction, 10.3390/biom6020021
  98. Mena Ra�l, Edwards Patricia, P�rez-Olvera Ofelia, Wischik Claude M., Monitoring pathological assembly of tau and ?-amyloid proteins in Alzheimer's disease, 10.1007/bf00294259
  99. Meredith Jr. Jere E., Sankaranarayanan Sethu, Guss Valerie, Lanzetti Anthony J., Berisha Flora, Neely Robert J., Slemmon J. Randall, Portelius Erik, Zetterberg Henrik, Blennow Kaj, Soares Holly, Ahlijanian Michael, Albright Charles F., Characterization of Novel CSF Tau and ptau Biomarkers for Alzheimer’s Disease, 10.1371/journal.pone.0076523
  100. Meyer Virginia, Holden Michael R., Weismiller Hilary A., Eaton Gareth R., Eaton Sandra S., Margittai Martin, Fracture and Growth Are Competing Forces Determining the Fate of Conformers in Tau Fibril Populations, 10.1074/jbc.m116.715557
  101. Mirbaha Hilda, Chen Dailu, Morazova Olga A, Ruff Kiersten M, Sharma Apurwa M, Liu Xiaohua, Goodarzi Mohammad, Pappu Rohit V, Colby David W, Mirzaei Hamid, Joachimiak Lukasz A, Diamond Marc I, Inert and seed-competent tau monomers suggest structural origins of aggregation, 10.7554/elife.36584
  102. Mo Zhong-Ying, Zhu Ying-Zhu, Zhu Hai-Li, Fan Jun-Bao, Chen Jie, Liang Yi, Low Micromolar Zinc Accelerates the Fibrillization of Human Tau via Bridging of Cys-291 and Cys-322, 10.1074/jbc.m109.058883
  103. Morishima-Kawashima Maho, Hasegawa Masato, Takio Koji, Suzuki Masami, Yoshida Hirotaka, Watanabe Atsushi, Titani Koiti, Ihara Yasuo, Hyperphosphorylation of Tau in PHF, 10.1016/0197-4580(95)00027-c
  104. Morris Deborah R., Levenson Cathy W., Neurotoxicity of Zinc, Advances in Neurobiology (2017) ISBN:9783319601885 p.303-312, 10.1007/978-3-319-60189-2_15
  105. Morris M, Knudsen GM, Maeda S, Trinidad JC, Ioanoviciu A, Burlingame AL, Mucke L (2015) Tau post-translational modifications in wild-type and human amyloid precursor protein transgenic mice. Nat Neurosci 18:1183–1189. https://doi.org/10.1038/nn.4067nn.4067
  106. Moussaud Simon, Jones Daryl R, Moussaud-Lamodière Elisabeth L, Delenclos Marion, Ross Owen A, McLean Pamela J, Alpha-synuclein and tau: teammates in neurodegeneration?, 10.1186/1750-1326-9-43
  107. Mudher Amrit, Brion Jean-Pierre, Avila Jesus, Medina Miguel, Buée Luc, EuroTau: towing scientists to tau without tautology, 10.1186/s40478-017-0491-z
  108. Nakamura Akinori, Kaneko Naoki, Villemagne Victor L., Kato Takashi, Doecke James, Doré Vincent, Fowler Chris, Li Qiao-Xin, Martins Ralph, Rowe Christopher, Tomita Taisuke, Matsuzaki Katsumi, Ishii Kenji, Ishii Kazunari, Arahata Yutaka, Iwamoto Shinichi, Ito Kengo, Tanaka Koichi, Masters Colin L., Yanagisawa Katsuhiko, High performance plasma amyloid-β biomarkers for Alzheimer’s disease, 10.1038/nature25456
  109. Nelson Peter T., Alafuzoff Irina, Bigio Eileen H., Bouras Constantin, Braak Heiko, Cairns Nigel J., Castellani Rudolph J., Crain Barbara J., Davies Peter, Tredici Kelly Del, Duyckaerts Charles, Frosch Matthew P., Haroutunian Vahram, Hof Patrick R., Hulette Christine M., Hyman Bradley T., Iwatsubo Takeshi, Jellinger Kurt A., Jicha Gregory A., Kövari Enikö, Kukull Walter A., Leverenz James B., Love Seth, Mackenzie Ian R., Mann David M., Masliah Eliezer, McKee Ann C., Montine Thomas J., Morris John C., Schneider Julie A., Sonnen Joshua A., Thal Dietmar R., Trojanowski John Q., Troncoso Juan C., Wisniewski Thomas, Woltjer Randall L., Beach Thomas G., Correlation of Alzheimer Disease Neuropathologic Changes With Cognitive Status: A Review of the Literature, 10.1097/nen.0b013e31825018f7
  110. Ng Kok Pin, Pascoal Tharick A., Mathotaarachchi Sulantha, Therriault Joseph, Kang Min Su, Shin Monica, Guiot Marie-Christine, Guo Qi, Harada Ryuichi, Comley Robert A., Massarweh Gassan, Soucy Jean-Paul, Okamura Nobuyuki, Gauthier Serge, Rosa-Neto Pedro, Monoamine oxidase B inhibitor, selegiline, reduces 18F-THK5351 uptake in the human brain, 10.1186/s13195-017-0253-y
  111. Nizynski Bartosz, Nieznanska Hanna, Dec Robert, Boyko Solomiia, Dzwolak Wojciech, Nieznanski Krzysztof, Amyloidogenic cross-seeding of Tau protein: Transient emergence of structural variants of fibrils, 10.1371/journal.pone.0201182
  112. Novak M., Kabat J., Wischik C.M., Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament., 10.1002/j.1460-2075.1993.tb05665.x
  113. Novak Petr, Cehlar Ondrej, Skrabana Rostislav, Novak Michal, Tau Conformation as a Target for Disease-Modifying Therapy: The Role of Truncation, 10.3233/jad-179942
  114. Ojo Joseph O., Mouzon Benoit C., Crawford Fiona, Repetitive head trauma, chronic traumatic encephalopathy and tau: Challenges in translating from mice to men, 10.1016/j.expneurol.2015.06.003
  115. Oroz Javier, Chang Bliss J., Wysoczanski Piotr, Lee Chung-Tien, Pérez-Lara Ángel, Chakraborty Pijush, Hofele Romina V., Baker Jeremy D., Blair Laura J., Biernat Jacek, Urlaub Henning, Mandelkow Eckhard, Dickey Chad A., Zweckstetter Markus, Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex, 10.1038/s41467-018-06880-0
  116. Ossenkoppele Rik, Schonhaut Daniel R., Schöll Michael, Lockhart Samuel N., Ayakta Nagehan, Baker Suzanne L., O’Neil James P., Janabi Mustafa, Lazaris Andreas, Cantwell Averill, Vogel Jacob, Santos Miguel, Miller Zachary A., Bettcher Brianne M., Vossel Keith A., Kramer Joel H., Gorno-Tempini Maria L., Miller Bruce L., Jagust William J., Rabinovici Gil D., Tau PET patterns mirror clinical and neuroanatomical variability in Alzheimer’s disease, 10.1093/brain/aww027
  117. Ovod Vitaliy, Ramsey Kara N., Mawuenyega Kwasi G., Bollinger Jim G., Hicks Terry, Schneider Theresa, Sullivan Melissa, Paumier Katrina, Holtzman David M., Morris John C., Benzinger Tammie, Fagan Anne M., Patterson Bruce W., Bateman Randall J., Amyloid β concentrations and stable isotope labeling kinetics of human plasma specific to central nervous system amyloidosis, 10.1016/j.jalz.2017.06.2266
  118. Pérez Mar, Medina Miguel, Hernández Félix, Avila Jesús, Secretion of full-length Tau or Tau fragments in cell culture models. Propagation of Tau in vivo and in vitro, 10.1515/bmc-2018-0001
  119. Pérez-Ruiz Elena, Decrop Deborah, Ven Karen, Tripodi Lisa, Leirs Karen, Rosseels Joelle, van de Wouwer Marlies, Geukens Nick, De Vos Ann, Vanmechelen Eugeen, Winderickx Joris, Lammertyn Jeroen, Spasic Dragana, Digital ELISA for the quantification of attomolar concentrations of Alzheimer's disease biomarker protein Tau in biological samples, 10.1016/j.aca.2018.02.011
  120. Pontecorvo Michael J., Devous Michael D., Navitsky Michael, Lu Ming, Salloway Stephen, Schaerf Frederick W., Jennings Danna, Arora Anupa K., McGeehan Anne, Lim Nathaniel C., Xiong Hui, Joshi Abhinay D., Siderowf Andrew, Mintun Mark A., , Relationships between flortaucipir PET tau binding and amyloid burden, clinical diagnosis, age and cognition, 10.1093/brain/aww334
  121. Poorkaj Parvoneh, Kas Arnie, D'Souza Ian, Zhou Yang, Pham Quynh, Stone Mariam, Olson Maynard V., Schellenberg Gerard D., A genomic sequence analysis of the mouse and human microtubule-associated protein tau, 10.1007/s00335-001-2044-8
  122. Qi Haoling, Cantrelle François-Xavier, Benhelli-Mokrani Houda, Smet-Nocca Caroline, Buée Luc, Lippens Guy, Bonnefoy Eliette, Galas Marie-Christine, Landrieu Isabelle, Nuclear Magnetic Resonance Spectroscopy Characterization of Interaction of Tau with DNA and Its Regulation by Phosphorylation, 10.1021/bi5014613
  123. Qi Haoling, Prabakaran Sudhakaran, Cantrelle François-Xavier, Chambraud Béatrice, Gunawardena Jeremy, Lippens Guy, Landrieu Isabelle, Characterization of Neuronal Tau Protein as a Target of Extracellular Signal-regulated Kinase, 10.1074/jbc.m115.700914
  124. Rábano Alberto, Cuadros Raquel, Calero Miguel, Hernández Félix, Avila Jesús, Specific Profile of Tau Isoforms in Argyrophylic Grain Disease, 10.4137/jen.s12202
  125. Rodriguez Jose A., Ivanova Magdalena I., Sawaya Michael R., Cascio Duilio, Reyes Francis E., Shi Dan, Sangwan Smriti, Guenther Elizabeth L., Johnson Lisa M., Zhang Meng, Jiang Lin, Arbing Mark A., Nannenga Brent L., Hattne Johan, Whitelegge Julian, Brewster Aaron S., Messerschmidt Marc, Boutet Sébastien, Sauter Nicholas K., Gonen Tamir, Eisenberg David S., Structure of the toxic core of α-synuclein from invisible crystals, 10.1038/nature15368
  126. Rodríguez-Martín Teresa, Cuchillo-Ibáñez Inmaculada, Noble Wendy, Nyenya Fanon, Anderton Brian H., Hanger Diane P., Tau phosphorylation affects its axonal transport and degradation, 10.1016/j.neurobiolaging.2013.03.015
  127. Roman Andrei Yu., Devred François, Byrne Deborah, La Rocca Romain, Ninkina Natalia N., Peyrot Vincent, Tsvetkov Philipp O., Zinc Induces Temperature-Dependent Reversible Self-Assembly of Tau, 10.1016/j.jmb.2018.12.008
  128. Rosseels Joëlle, Van den Brande Jeff, Violet Marie, Jacobs Dirk, Grognet Pierre, Lopez Juan, Huvent Isabelle, Caldara Marina, Swinnen Erwin, Papegaey Anthony, Caillierez Raphaëlle, Buée-Scherrer Valerie, Engelborghs Sebastiaan, Lippens Guy, Colin Morvane, Buée Luc, Galas Marie-Christine, Vanmechelen Eugeen, Winderickx Joris, Tau Monoclonal Antibody Generation Based on Humanized Yeast Models : IMPACT ON TAU OLIGOMERIZATION AND DIAGNOSTICS, 10.1074/jbc.m114.627919
  129. Sahara Naruhiko, Maeda Sumihiro, Murayama Miyuki, Suzuki Takehiro, Dohmae Naoshi, Yen Shu-Hui, Takashima Akihiko, Assembly of two distinct dimers and higher-order oligomers from full-length tau : Distinct types of tau dimers, 10.1111/j.1460-9568.2007.05555.x
  130. Sato Chihiro, Barthélemy Nicolas R., Mawuenyega Kwasi G., Patterson Bruce W., Gordon Brian A., Jockel-Balsarotti Jennifer, Sullivan Melissa, Crisp Matthew J., Kasten Tom, Kirmess Kristopher M., Kanaan Nicholas M., Yarasheski Kevin E., Baker-Nigh Alaina, Benzinger Tammie L.S., Miller Timothy M., Karch Celeste M., Bateman Randall J., Tau Kinetics in Neurons and the Human Central Nervous System, 10.1016/j.neuron.2018.02.015
  131. Sawaya Michael R., Sambashivan Shilpa, Nelson Rebecca, Ivanova Magdalena I., Sievers Stuart A., Apostol Marcin I., Thompson Michael J., Balbirnie Melinda, Wiltzius Jed J. W., McFarlane Heather T., Madsen Anders Ø., Riekel Christian, Eisenberg David, Atomic structures of amyloid cross-β spines reveal varied steric zippers, 10.1038/nature05695
  132. Sayas C. Laura, Medina Miguel, Cuadros Raquel, Ollá Ivanna, García Esther, Pérez Mar, Ferrer Isidro, Hernández Félix, Avila Jesús, Role of tau N-terminal motif in the secretion of human tau by End Binding proteins, 10.1371/journal.pone.0210864
  133. Schneider A., Biernat J., von Bergen M., Mandelkow E., Mandelkow E.-M., Phosphorylation that Detaches Tau Protein from Microtubules (Ser262, Ser214) Also Protects It against Aggregation into Alzheimer Paired Helical Filaments†, 10.1021/bi981874p
  134. Schöll Michael, Maass Anne, Mattsson Niklas, Ashton Nicholas J., Blennow Kaj, Zetterberg Henrik, Jagust William, Biomarkers for tau pathology, 10.1016/j.mcn.2018.12.001
  135. Seidler P. M., Boyer D. R., Rodriguez J. A., Sawaya M. R., Cascio D., Murray K., Gonen T., Eisenberg D. S., Structure-based inhibitors of tau aggregation, 10.1038/nchem.2889
  136. Shih Heather H., Tu Chao, Cao Wei, Klein Anne, Ramsey Renee, Fennell Brian J., Lambert Matthew, Ní Shúilleabháin Deirdre, Autin Bénédicte, Kouranova Eugenia, Laxmanan Sri, Braithwaite Steven, Wu Leeying, Ait-Zahra Mostafa, Milici Anthony J., Dumin Jo Ann, LaVallie Edward R., Arai Maya, Corcoran Christopher, Paulsen Janet E., Gill Davinder, Cunningham Orla, Bard Joel, Mosyak Lydia, Finlay William J. J., An Ultra-specific Avian Antibody to Phosphorylated Tau Protein Reveals a Unique Mechanism for Phosphoepitope Recognition, 10.1074/jbc.m112.415935
  137. Shimada H, Shinotoh H, Sahara N, Hirano S, Furukawa S, Takahata K, Ito H (2015) Diagnostic utility and clinical significance of tau PET imaging with [11C] PBB3 in diverse tauopathies. 9th Hum Amyloid Imaging Conf 2015 Miami, FL, USA
  138. Siddiqua Ayisha, Luo Yin, Meyer Virginia, Swanson Michael A., Yu Xiang, Wei Guanghong, Zheng Jie, Eaton Gareth R., Ma Buyong, Nussinov Ruth, Eaton Sandra S., Margittai Martin, Conformational Basis for Asymmetric Seeding Barrier in Filaments of Three- and Four-Repeat Tau, 10.1021/ja303498q
  139. Skrabana Rostislav, Kontsek Peter, Mederlyova Anna, Iqbal Khalid, Novak Michal, Folding of Alzheimer's core PHF subunit revealed by monoclonal antibody 423, 10.1016/j.febslet.2004.04.098
  140. Smith Ruben, Wibom Moa, Pawlik Daria, Englund Elisabet, Hansson Oskar, Correlation of In Vivo [18F]Flortaucipir With Postmortem Alzheimer Disease Tau Pathology, 10.1001/jamaneurol.2018.3692
  141. Sotiropoulos Ioannis, Galas Marie-Christine, Silva Joana M., Skoulakis Efthimios, Wegmann Susanne, Maina Mahmoud Bukar, Blum David, Sayas Carmen Laura, Mandelkow Eva-Maria, Mandelkow Eckhard, Spillantini Maria Grazia, Sousa Nuno, Avila Jesus, Medina Miguel, Mudher Amrit, Buee Luc, Atypical, non-standard functions of the microtubule associated Tau protein, 10.1186/s40478-017-0489-6
  142. Spillantini M. G., Crowther R. A., Goedert M., Comparison of the neurofibrillary pathology in Alzheimer's disease and familial presenile dementia with tangles, 10.1007/s004010050487
  143. Spires-Jones Tara L., Kopeikina Katherine J., Koffie Robert M., de Calignon Alix, Hyman Bradley T., Are Tangles as Toxic as They Look?, 10.1007/s12031-011-9566-7
  144. Steen Hanno, Mair Waltraud, Tang Shaojun, Steen Judith A., MAPPING THE TAUOPATHY-SPECIFIC MODIFICATION LANDSCAPE ON TAU, 10.1016/j.jalz.2017.07.426
  145. Stefanoska Kristie, Volkerling Alexander, Bertz Josefine, Poljak Anne, Ke Yazi D., Ittner Lars M., Ittner Arne, An N-terminal motif unique to primate tau enables differential protein–protein interactions, 10.1074/jbc.ra118.001784
  146. Stephens Andrew, Seibyl John, Mueller Andre, Barret Olivier, Berndt Mathias, Madonia Jennifer, Kroth Heiko, Bullich Santiago, Pfeifer Andrea, Muhs Andreas, Tamagnan Gilles, Marek Kenneth, Dinkelborg Ludger, CLINICAL UPDATE: 18F-PI-2620, A NEXT GENERATION TAU PET AGENT EVALUATED IN SUBJECTS WITH ALZHEIMER’S DISEASE AND PROGRESSIVE SUPRANUCLEAR PALSY, 10.1016/j.jalz.2018.06.2287
  147. Sutphen Courtney L., Jasielec Mateusz S., Shah Aarti R., Macy Elizabeth M., Xiong Chengjie, Vlassenko Andrei G., Benzinger Tammie L. S., Stoops Erik E. J., Vanderstichele Hugo M. J., Brix Britta, Darby Heather D., Vandijck Manu L. J., Ladenson Jack H., Morris John C., Holtzman David M., Fagan Anne M., Longitudinal Cerebrospinal Fluid Biomarker Changes in Preclinical Alzheimer Disease During Middle Age, 10.1001/jamaneurol.2015.1285
  148. Taniguchi-Watanabe Sayuri, Arai Tetsuaki, Kametani Fuyuki, Nonaka Takashi, Masuda-Suzukake Masami, Tarutani Airi, Murayama Shigeo, Saito Yuko, Arima Kunimasa, Yoshida Mari, Akiyama Haruhiko, Robinson Andrew, Mann David M. A., Iwatsubo Takeshi, Hasegawa Masato, Biochemical classification of tauopathies by immunoblot, protein sequence and mass spectrometric analyses of sarkosyl-insoluble and trypsin-resistant tau, 10.1007/s00401-015-1503-3
  149. Tepper Katharina, Biernat Jacek, Kumar Satish, Wegmann Susanne, Timm Thomas, Hübschmann Sabrina, Redecke Lars, Mandelkow Eva-Maria, Müller Daniel J., Mandelkow Eckhard, Oligomer Formation of Tau Protein Hyperphosphorylated in Cells, 10.1074/jbc.m114.611368
  150. Tsvetkov Philipp O., Makarov Alexander A., Malesinski Soazig, Peyrot Vincent, Devred Francois, New insights into tau–microtubules interaction revealed by isothermal titration calorimetry, 10.1016/j.biochi.2011.09.011
  151. Tsvetkov Philipp O., Roman Andrei Yu., Baksheeva Viktoriia E., Nazipova Aliya A., Shevelyova Marina P., Vladimirov Vasiliy I., Buyanova Michelle F., Zinchenko Dmitry V., Zamyatnin Andrey A., Devred François, Golovin Andrey V., Permyakov Sergei E., Zernii Evgeni Yu., Functional Status of Neuronal Calcium Sensor-1 Is Modulated by Zinc Binding, 10.3389/fnmol.2018.00459
  152. Tuttle Marcus D, Comellas Gemma, Nieuwkoop Andrew J, Covell Dustin J, Berthold Deborah A, Kloepper Kathryn D, Courtney Joseph M, Kim Jae K, Barclay Alexander M, Kendall Amy, Wan William, Stubbs Gerald, Schwieters Charles D, Lee Virginia M Y, George Julia M, Rienstra Chad M, Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein, 10.1038/nsmb.3194
  153. Vandermeeren Marc, Borgers Marianne, Van Kolen Kristof, Theunis Clara, Vasconcelos Bruno, Bottelbergs Astrid, Wintmolders Cindy, Daneels Guy, Willems Roland, Dockx Koen, Delbroek Lore, Marreiro André, Ver Donck Luc, Sousa Cristiano, Nanjunda Rupesh, Lacy Eilyn, Van De Casteele Tom, Van Dam Debby, De Deyn Peter Paul, Kemp John A., Malia Thomas J., Mercken Marc H., Anti-Tau Monoclonal Antibodies Derived from Soluble and Filamentous Tau Show Diverse Functional Properties in vitro and in vivo, 10.3233/jad-180404
  154. Vanhelmont Thomas, Vandebroek Tom, De Vos Ann, Terwel Dick, Lemaire Katleen, Anandhakumar Jayamani, Franssens Vanessa, Swinnen Erwin, Van Leuven Fred, Winderickx Joris, Serine-409 phosphorylation and oxidative damage define aggregation of human protein tau in yeast : Determinants of tau aggregation in yeast, 10.1111/j.1567-1364.2010.00662.x
  155. Vermeiren Céline, Motte Philippe, Viot Delphine, Mairet-Coello Georges, Courade Jean-Philippe, Citron Martin, Mercier Joël, Hannestad Jonas, Gillard Michel, The tau positron-emission tomography tracer AV-1451 binds with similar affinities to tau fibrils and monoamine oxidases : AV-1451 Tau Pet Tracer Binds Mao-a and -B, 10.1002/mds.27271
  156. von Bergen M., Barghorn S., Jeganathan S., Mandelkow E.-M., Mandelkow E., Spectroscopic Approaches to the Conformation of Tau Protein in Solution and in Paired Helical Filaments, 10.1159/000095257
  157. von Bergen M., Friedhoff P., Biernat J., Heberle J., Mandelkow E.-M., Mandelkow E., Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif (306VQIVYK311) forming beta structure, 10.1073/pnas.97.10.5129
  158. Wang Jian-Zhi, Grundke-Iqbal Inge, Iqbal Khalid, Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration : Kinase/phosphatase/sites involved in tau pathology, 10.1111/j.1460-9568.2006.05226.x
  159. Wasmer C., Lange A., Van Melckebeke H., Siemer A. B., Riek R., Meier B. H., Amyloid Fibrils of the HET-s(218-289) Prion Form a   Solenoid with a Triangular Hydrophobic Core, 10.1126/science.1151839
  160. Watt Nicole T., Whitehouse Isobel J., Hooper Nigel M., The Role of Zinc in Alzheimer's Disease, 10.4061/2011/971021
  161. Wegmann Susanne, Eftekharzadeh Bahareh, Tepper Katharina, Zoltowska Katarzyna M, Bennett Rachel E, Dujardin Simon, Laskowski Pawel R, MacKenzie Danny, Kamath Tarun, Commins Caitlin, Vanderburg Charles, Roe Allyson D, Fan Zhanyun, Molliex Amandine M, Hernandez‐Vega Amayra, Muller Daniel, Hyman Anthony A, Mandelkow Eckhard, Taylor J Paul, Hyman Bradley T, Tau protein liquid–liquid phase separation can initiate tau aggregation, 10.15252/embj.201798049
  162. Weingarten M. D., Lockwood A. H., Hwo S. Y., Kirschner M. W., A protein factor essential for microtubule assembly., 10.1073/pnas.72.5.1858
  163. Weismiller Hilary A., Murphy Rachel, Wei Guanghong, Ma Buyong, Nussinov Ruth, Margittai Martin, Structural disorder in four-repeat Tau fibrils reveals a new mechanism for barriers to cross-seeding of Tau isoforms, 10.1074/jbc.ra118.005316
  164. Wiedemann Christoph, Bellstedt Peter, Görlach Matthias, CAPITO—a web server-based analysis and plotting tool for circular dichroism data, 10.1093/bioinformatics/btt278
  165. Wischik C. M., Novak M., Edwards P. C., Klug A., Tichelaar W., Crowther R. A., Structural characterization of the core of the paired helical filament of Alzheimer disease., 10.1073/pnas.85.13.4884
  166. Wischik C. M., Novak M., Thogersen H. C., Edwards P. C., Runswick M. J., Jakes R., Walker J. E., Milstein C., Roth M., Klug A., Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease., 10.1073/pnas.85.12.4506
  167. Witman G. B., Cleveland D. W., Weingarten M. D., Kirschner M. W., Tubulin requires tau for growth onto microtubule initiating sites., 10.1073/pnas.73.11.4070
  168. Yin Haishan, Kuret Jeff, C-terminal truncation modulates both nucleation and extension phases of τ fibrillization, 10.1016/j.febslet.2005.11.077
  169. Zhang Heng, Zhu Xueyong, Pascual Gabriel, Wadia Jehangir S., Keogh Elissa, Hoozemans Jeroen J., Siregar Berdien, Inganäs Hanna, Stoop Esther J.M., Goudsmit Jaap, Apetri Adrian, Koudstaal Wouter, Wilson Ian A., Structural Basis for Recognition of a Unique Epitope by a Human Anti-tau Antibody, 10.1016/j.str.2018.08.012
  170. Zhang Wenjuan, Falcon Benjamin, Murzin Alexey G, Fan Juan, Crowther R Anthony, Goedert Michel, Scheres Sjors HW, Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer’s and Pick’s diseases, 10.7554/elife.43584
  171. Zhang Zhentao, Song Mingke, Liu Xia, Kang Seong Su, Kwon Il-Sun, Duong Duc M, Seyfried Nicholas T, Hu William T, Liu Zhixue, Wang Jian-Zhi, Cheng Liming, Sun Yi E, Yu Shan Ping, Levey Allan I, Ye Keqiang, Cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in Alzheimer's disease, 10.1038/nm.3700
  172. Zhong Qi, Congdon Erin E., Nagaraja Haikady N., Kuret Jeff, Tau Isoform Composition Influences Rate and Extent of Filament Formation, 10.1074/jbc.m112.364067
  173. Zilka Norbert, Kovacech Branislav, Barath Peter, Kontsekova Eva, Novák Michal, The self-perpetuating tau truncation circle, 10.1042/bst20120015
Bibliographic reference Fichou, Yann ; Al-Hilaly, Youssra K ; Devred, François ; Smet-Nocca, Caroline ; Tsvetkov, Philipp O ; et. al. The elusive tau molecular structures: can we translate the recent breakthroughs into new targets for intervention?. In: Acta neuropathologica communications, Vol. 7, no. 1, p. 31 [1-17] (2019)
Permanent URL http://hdl.handle.net/2078.1/216523