Journal articles on the topic 'Tau seeding'
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Andrés-Benito, Pol, Margarita Carmona, Mónica Jordán, Joaquín Fernández-Irigoyen, Enrique Santamaría, José Antoni del Rio, and Isidro Ferrer. "Host Tau Genotype Specifically Designs and Regulates Tau Seeding and Spreading and Host Tau Transformation Following Intrahippocampal Injection of Identical Tau AD Inoculum." International Journal of Molecular Sciences 23, no. 2 (January 10, 2022): 718. http://dx.doi.org/10.3390/ijms23020718.
Full textWu, Ruozhen, Jianlan Gu, Dingwei Zhou, Yunn Chyn Tung, Nana Jin, Dandan Chu, Wen Hu, et al. "Seeding-Competent Tau in Gray Matter Versus White Matter of Alzheimer’s Disease Brain." Journal of Alzheimer's Disease 79, no. 4 (February 16, 2021): 1647–59. http://dx.doi.org/10.3233/jad-201290.
Full textFerrer, Isidro, Maria Victoria Zelaya, Meritxell Aguiló García, Margarita Carmona, Irene López‐González, Pol Andrés‐Benito, Laia Lidón, Rosalina Gavín, Paula Garcia‐Esparcia, and José Antonio Rio. "Relevance of host tau in tau seeding and spreading in tauopathies." Brain Pathology 30, no. 2 (August 27, 2019): 298–318. http://dx.doi.org/10.1111/bpa.12778.
Full textHolmes, B. B., J. L. Furman, T. E. Mahan, T. R. Yamasaki, H. Mirbaha, W. C. Eades, L. Belaygorod, N. J. Cairns, D. M. Holtzman, and M. I. Diamond. "Proteopathic tau seeding predicts tauopathy in vivo." Proceedings of the National Academy of Sciences 111, no. 41 (September 26, 2014): E4376—E4385. http://dx.doi.org/10.1073/pnas.1411649111.
Full textHolth, Jerrah K., Sarah K. Fritschi, Chanung Wang, Nigel P. Pedersen, John R. Cirrito, Thomas E. Mahan, Mary Beth Finn, et al. "The sleep-wake cycle regulates brain interstitial fluid tau in mice and CSF tau in humans." Science 363, no. 6429 (January 24, 2019): 880–84. http://dx.doi.org/10.1126/science.aav2546.
Full textRobert, Aiko, Michael Schöll, and Thomas Vogels. "Tau Seeding Mouse Models with Patient Brain-Derived Aggregates." International Journal of Molecular Sciences 22, no. 11 (June 7, 2021): 6132. http://dx.doi.org/10.3390/ijms22116132.
Full textPolanco, Juan Carlos, Yevhen Akimov, Avinash Fernandes, Adam Briner, Gabriel Rhys Hand, Marloes van Roijen, Giuseppe Balistreri, and Jürgen Götz. "CRISPRi screening reveals regulators of tau pathology shared between exosomal and vesicle-free tau." Life Science Alliance 6, no. 1 (October 31, 2022): e202201689. http://dx.doi.org/10.26508/lsa.202201689.
Full textAbskharon, Romany, Paul M. Seidler, Michael R. Sawaya, Duilio Cascio, Tianxiao P. Yang, Stephan Philipp, Christopher Kazu Williams, et al. "Crystal structure of a conformational antibody that binds tau oligomers and inhibits pathological seeding by extracts from donors with Alzheimer's disease." Journal of Biological Chemistry 295, no. 31 (June 3, 2020): 10662–76. http://dx.doi.org/10.1074/jbc.ra120.013638.
Full textLeyns, Cheryl E. G., Maud Gratuze, Sneha Narasimhan, Nimansha Jain, Lauren J. Koscal, Hong Jiang, Melissa Manis, et al. "TREM2 function impedes tau seeding in neuritic plaques." Nature Neuroscience 22, no. 8 (June 24, 2019): 1217–22. http://dx.doi.org/10.1038/s41593-019-0433-0.
Full textRidler, Charlotte. "Tau seeding starts early in the entorhinal cortex." Nature Reviews Neurology 14, no. 7 (May 24, 2018): 380. http://dx.doi.org/10.1038/s41582-018-0016-9.
Full textVigers, Michael, and Songi Han. "Proteolytic Fragments of tau Produce Seeding-Competent Fibrils." Biophysical Journal 118, no. 3 (February 2020): 541a. http://dx.doi.org/10.1016/j.bpj.2019.11.2963.
Full textFurman, Jennifer L., Jaime Vaquer-Alicea, Charles L. White, Nigel J. Cairns, Peter T. Nelson, and Marc I. Diamond. "Widespread tau seeding activity at early Braak stages." Acta Neuropathologica 133, no. 1 (November 22, 2016): 91–100. http://dx.doi.org/10.1007/s00401-016-1644-z.
Full textTarutani, Airi, Haruka Miyata, Takashi Nonaka, Kazuko Hasegawa, Mari Yoshida, Yuko Saito, Shigeo Murayama, et al. "Human tauopathy-derived tau strains determine the substrates recruited for templated amplification." Brain 144, no. 8 (March 9, 2021): 2333–48. http://dx.doi.org/10.1093/brain/awab091.
Full textSoares, Alberto Carpinteiro, Andreia Ferreira, Jonas Mariën, Charlotte Delay, Edward Lee, John Q. Trojanowski, Dieder Moechars, Wim Annaert, and Louis De Muynck. "PIKfyve activity is required for lysosomal trafficking of tau aggregates and tau seeding." Journal of Biological Chemistry 296 (January 2021): 100636. http://dx.doi.org/10.1016/j.jbc.2021.100636.
Full textRosenqvist, Nina, Ayodeji A. Asuni, Christian R. Andersson, Søren Christensen, Justus A. Daechsel, Jan Egebjerg, Jeppe Falsig, et al. "Highly specific and selective anti‐pS396‐tau antibody C10.2 targets seeding‐competent tau." Alzheimer's & Dementia: Translational Research & Clinical Interventions 4, no. 1 (January 2018): 521–34. http://dx.doi.org/10.1016/j.trci.2018.09.005.
Full textManos, Justine D., Christina N. Preiss, Nandini Venkat, Joseph Tamm, Peter Reinhardt, Taekyung Kwon, Jessica Wu, et al. "Uncovering specificity of endogenous TAU aggregation in a human iPSC-neuron TAU seeding model." iScience 25, no. 1 (January 2022): 103658. http://dx.doi.org/10.1016/j.isci.2021.103658.
Full textAlbert, Marie, Georges Mairet-Coello, Clément Danis, Sarah Lieger, Raphaëlle Caillierez, Sébastien Carrier, Emilie Skrobala, et al. "Prevention of tau seeding and propagation by immunotherapy with a central tau epitope antibody." Brain 142, no. 6 (April 30, 2019): 1736–50. http://dx.doi.org/10.1093/brain/awz100.
Full textGuo, Jing L., and Virginia M. Y. Lee. "Seeding of Normal Tau by Pathological Tau Conformers Drives Pathogenesis of Alzheimer-like Tangles." Journal of Biological Chemistry 286, no. 17 (March 3, 2011): 15317–31. http://dx.doi.org/10.1074/jbc.m110.209296.
Full textSigurdsson, Einar M., Erin Elizabeth Congdon, Jiaping Gu, and Suhail Rasool. "P4-229: TAU ANTIBODY-MEDIATED PREVENTION OF SEEDING OF TAU PATHOLOGY AND ASSOCIATED TOXICITY." Alzheimer's & Dementia 10 (July 2014): P871. http://dx.doi.org/10.1016/j.jalz.2014.05.1747.
Full textStopschinski, Barbara E., Talitha L. Thomas, Sourena Nadji, Eric Darvish, Linfeng Fan, Brandon B. Holmes, Anuja R. Modi, et al. "A synthetic heparinoid blocks Tau aggregate cell uptake and amplification." Journal of Biological Chemistry 295, no. 10 (January 23, 2020): 2974–83. http://dx.doi.org/10.1074/jbc.ra119.010353.
Full textKaufman, Sarah K., Sarah Svirsky, Jonathan D. Cherry, Ann C. McKee, and Marc I. Diamond. "Tau seeding in chronic traumatic encephalopathy parallels disease severity." Acta Neuropathologica 142, no. 6 (October 9, 2021): 951–60. http://dx.doi.org/10.1007/s00401-021-02373-5.
Full textMcEwan, William A., Benjamin Falcon, Marina Vaysburd, Dean Clift, Adrian L. Oblak, Bernardino Ghetti, Michel Goedert, and Leo C. James. "Cytosolic Fc receptor TRIM21 inhibits seeded tau aggregation." Proceedings of the National Academy of Sciences 114, no. 3 (January 3, 2017): 574–79. http://dx.doi.org/10.1073/pnas.1607215114.
Full textSong, Liqing, Daniel E. Oseid, Evan A. Wells, and Anne Skaja Robinson. "The Interplay between GSK3β and Tau Ser262 Phosphorylation during the Progression of Tau Pathology." International Journal of Molecular Sciences 23, no. 19 (October 1, 2022): 11610. http://dx.doi.org/10.3390/ijms231911610.
Full textFichou, Yann, Yanxian Lin, Jennifer N. Rauch, Michael Vigers, Zhikai Zeng, Madhur Srivastava, Timothy J. Keller, Jack H. Freed, Kenneth S. Kosik, and Songi Han. "Cofactors are essential constituents of stable and seeding-active tau fibrils." Proceedings of the National Academy of Sciences 115, no. 52 (December 11, 2018): 13234–39. http://dx.doi.org/10.1073/pnas.1810058115.
Full textCooper, Joanna M., Aurelien Lathuiliere, Mary Migliorini, Allison L. Arai, Mashhood M. Wani, Simon Dujardin, Selen C. Muratoglu, Bradley T. Hyman, and Dudley K. Strickland. "Regulation of tau internalization, degradation, and seeding by LRP1 reveals multiple pathways for tau catabolism." Journal of Biological Chemistry 296 (January 2021): 100715. http://dx.doi.org/10.1016/j.jbc.2021.100715.
Full textVan Kolen, Kristof, Thomas J. Malia, Clara Theunis, Rupesh Nanjunda, Alexey Teplyakov, Robin Ernst, Sheng-Jiun Wu, et al. "Discovery and Functional Characterization of hPT3, a Humanized Anti-Phospho Tau Selective Monoclonal Antibody." Journal of Alzheimer's Disease 77, no. 4 (October 13, 2020): 1397–416. http://dx.doi.org/10.3233/jad-200544.
Full textVasconcelos, Bruno, Ilie-Cosmin Stancu, Arjan Buist, Matthew Bird, Peng Wang, Alexandre Vanoosthuyse, Kristof Van Kolen, et al. "Heterotypic seeding of Tau fibrillization by pre-aggregated Abeta provides potent seeds for prion-like seeding and propagation of Tau-pathology in vivo." Acta Neuropathologica 131, no. 4 (January 6, 2016): 549–69. http://dx.doi.org/10.1007/s00401-015-1525-x.
Full textPérez, Mar, Miguel Medina, Félix Hernández, and Jesús Avila. "Secretion of full-length Tau or Tau fragments in cell culture models. Propagation of Tau in vivo and in vitro." Biomolecular Concepts 9, no. 1 (March 5, 2018): 1–11. http://dx.doi.org/10.1515/bmc-2018-0001.
Full textFerrer, Isidro, Pol Andrés-Benito, Paula Garcia-Esparcia, Irene López-Gonzalez, Diego Valiente, Mónica Jordán-Pirla, Margarita Carmona, Julia Sala-Jarque, Vanessa Gil, and José Antonio del Rio. "Differences in Tau Seeding in Newborn and Adult Wild-Type Mice." International Journal of Molecular Sciences 23, no. 9 (April 26, 2022): 4789. http://dx.doi.org/10.3390/ijms23094789.
Full textGuo, Jing L., Sneha Narasimhan, Lakshmi Changolkar, Zhuohao He, Anna Stieber, Bin Zhang, Ronald J. Gathagan, et al. "Unique pathological tau conformers from Alzheimer’s brains transmit tau pathology in nontransgenic mice." Journal of Experimental Medicine 213, no. 12 (October 17, 2016): 2635–54. http://dx.doi.org/10.1084/jem.20160833.
Full textHeinsen, Helmut, and Lea T. Grinberg. "On the origin of tau seeding activity in Alzheimer’s disease." Acta Neuropathologica 136, no. 5 (July 23, 2018): 815–17. http://dx.doi.org/10.1007/s00401-018-1890-3.
Full textNachman, Eliana, Anne S. Wentink, Karine Madiona, Luc Bousset, Taxiarchis Katsinelos, Kieren Allinson, Harm Kampinga, et al. "Disassembly of Tau fibrils by the human Hsp70 disaggregation machinery generates small seeding-competent species." Journal of Biological Chemistry 295, no. 28 (May 28, 2020): 9676–90. http://dx.doi.org/10.1074/jbc.ra120.013478.
Full textLedreux, Aurélie, Sarah Thomas, Eric D. Hamlett, Camille Trautman, Anah Gilmore, Emily Rickman Hager, Daniel A. Paredes, Martin Margittai, Juan Fortea, and Ann-Charlotte Granholm. "Small Neuron-Derived Extracellular Vesicles from Individuals with Down Syndrome Propagate Tau Pathology in the Wildtype Mouse Brain." Journal of Clinical Medicine 10, no. 17 (August 31, 2021): 3931. http://dx.doi.org/10.3390/jcm10173931.
Full textDeVos, Sarah L., Rebecca L. Miller, Kathleen M. Schoch, Brandon B. Holmes, Carey S. Kebodeaux, Amy J. Wegener, Guo Chen, et al. "Tau reduction prevents neuronal loss and reverses pathological tau deposition and seeding in mice with tauopathy." Science Translational Medicine 9, no. 374 (January 25, 2017): eaag0481. http://dx.doi.org/10.1126/scitranslmed.aag0481.
Full textFerrer, Isidro, Pol Andrés-Benito, Margarita Carmona, and José Antonio del Rio. "Common and Specific Marks of Different Tau Strains Following Intra-Hippocampal Injection of AD, PiD, and GGT Inoculum in hTau Transgenic Mice." International Journal of Molecular Sciences 23, no. 24 (December 14, 2022): 15940. http://dx.doi.org/10.3390/ijms232415940.
Full textGhag, Gaurav, Nemil Bhatt, Daniel V. Cantu, Marcos J. Guerrero-Munoz, Anna Ellsworth, Urmi Sengupta, and Rakez Kayed. "Soluble tau aggregates, not large fibrils, are the toxic species that display seeding and cross-seeding behavior." Protein Science 27, no. 11 (October 19, 2018): 1901–9. http://dx.doi.org/10.1002/pro.3499.
Full textAnnadurai, Narendran, Lukáš Malina, Mario Salmona, Luisa Diomede, Antonio Bastone, Alfredo Cagnotto, Margherita Romeo, et al. "Antitumour drugs targeting tau R3 VQIVYK and Cys322 prevent seeding of endogenous tau aggregates by exogenous seeds." FEBS Journal 289, no. 7 (November 18, 2021): 1929–49. http://dx.doi.org/10.1111/febs.16270.
Full textDanis, Clément, Elian Dupré, Orgeta Zejneli, Raphaëlle Caillierez, Alexis Arrial, Séverine Bégard, Justine Mortelecque, et al. "Inhibition of Tau seeding by targeting Tau nucleation core within neurons with a single domain antibody fragment." Molecular Therapy 30, no. 4 (April 2022): 1484–99. http://dx.doi.org/10.1016/j.ymthe.2022.01.009.
Full textBajracharya, Rinie, David Brici, Jürgen Götz, and Rebecca M. Nisbet. "P4-036: NOVEL TAU-SPECIFIC MONOCLONAL ANTIBODY REDUCES TAU SEEDING AND ENHANCES PHAGOCYTIC ACTIVITY OF MICROGLIAL CELLS." Alzheimer's & Dementia 15 (July 2019): P1288. http://dx.doi.org/10.1016/j.jalz.2019.06.3695.
Full textFalcon, Benjamin, Annalisa Cavallini, Rachel Angers, Sarah Glover, Tracey K. Murray, Luanda Barnham, Samuel Jackson, et al. "Conformation Determines the Seeding Potencies of Native and Recombinant Tau Aggregates." Journal of Biological Chemistry 290, no. 2 (November 18, 2014): 1049–65. http://dx.doi.org/10.1074/jbc.m114.589309.
Full textYanamandra, Kiran, Najla Kfoury, Hong Jiang, Thomas E. Mahan, Shengmei Ma, Susan E. Maloney, David F. Wozniak, Marc I. Diamond, and David M. Holtzman. "Anti-Tau Antibodies that Block Tau Aggregate Seeding In Vitro Markedly Decrease Pathology and Improve Cognition In Vivo." Neuron 80, no. 2 (October 2013): 402–14. http://dx.doi.org/10.1016/j.neuron.2013.07.046.
Full textYanamandra, Kiran, Najla Kfoury, Hong Jiang, Thomas E. Mahan, Shengmei Ma, Susan E. Maloney, David F. Wozniak, Marc I. Diamond, and David M. Holtzman. "Anti-Tau Antibodies that Block Tau Aggregate Seeding In Vitro Markedly Decrease Pathology and Improve Cognition In Vivo." Neuron 80, no. 6 (December 2013): 1572. http://dx.doi.org/10.1016/j.neuron.2013.12.007.
Full textFalcon, Benjamin, Annalisa Cavallini, Suchira Bose, and Michel Goedert. "P1-004: IDENTIFICATION OF TAU SPECIES REQUIRED FOR SEEDING IN A CELL-BASED MODEL OF PATHOLOGICAL TAU PROPAGATION." Alzheimer's & Dementia 10 (July 2014): P305—P306. http://dx.doi.org/10.1016/j.jalz.2014.05.239.
Full textBose, Suchira, Annalisa Cavallini, Caroline Kerridge, Jane Cooper, Samuel J. Jackson, Alessia Landi, Claire V. Cella, et al. "O4-04-02: Characterisation of Tau Species Involved in Tau Seeding and Spread in Cellular and Animal Models." Alzheimer's & Dementia 12 (July 2016): P340. http://dx.doi.org/10.1016/j.jalz.2016.06.625.
Full textAtsmon-Raz, Yoav, and Yifat Miller. "Insight into Atomic Resolution of the Cross-Seeding between Tau/Mutated Tau and Amyloid-β in Neurodegenerative Diseases." Israel Journal of Chemistry 55, no. 6-7 (April 15, 2015): 628–36. http://dx.doi.org/10.1002/ijch.201400162.
Full textMakwana, Kamlesh M., Matthew P. Sarnowski, Jiayuan Miao, Yu-Shan Lin, and Juan R. Del Valle. "N-Amination Converts Amyloidogenic Tau Peptides into Soluble Antagonists of Cellular Seeding." ACS Chemical Neuroscience 12, no. 20 (October 5, 2021): 3928–38. http://dx.doi.org/10.1021/acschemneuro.1c00528.
Full textQi, Ruxi, Yin Luo, Guanghong Wei, Ruth Nussinov, and Buyong Ma. "Aβ “Stretching-and-Packing” Cross-Seeding Mechanism Can Trigger Tau Protein Aggregation." Journal of Physical Chemistry Letters 6, no. 16 (August 7, 2015): 3276–82. http://dx.doi.org/10.1021/acs.jpclett.5b01447.
Full textKraus, Allison, Eri Saijo, Michael A. Metrick, Kathy Newell, Christina J. Sigurdson, Gianluigi Zanusso, Bernardino Ghetti, and Byron Caughey. "Seeding selectivity and ultrasensitive detection of tau aggregate conformers of Alzheimer disease." Acta Neuropathologica 137, no. 4 (December 20, 2018): 585–98. http://dx.doi.org/10.1007/s00401-018-1947-3.
Full textManca, Matteo, and Allison Kraus. "Defining the Protein Seeds of Neurodegeneration using Real-Time Quaking-Induced Conversion Assays." Biomolecules 10, no. 9 (August 25, 2020): 1233. http://dx.doi.org/10.3390/biom10091233.
Full textStopschinski, Barbara E., Kelly Del Tredici, Sandi-Jo Estill-Terpack, Estifanos Ghebremdehin, Fang F. Yu, Heiko Braak, and Marc I. Diamond. "Anatomic survey of seeding in Alzheimer’s disease brains reveals unexpected patterns." Acta Neuropathologica Communications 9, no. 1 (October 11, 2021). http://dx.doi.org/10.1186/s40478-021-01255-x.
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