Статті в журналах з теми "Soluble tau protein"
Оформте джерело за APA, MLA, Chicago, Harvard та іншими стилями
Ознайомтеся з топ-50 статей у журналах для дослідження на тему "Soluble tau protein".
Біля кожної праці в переліку літератури доступна кнопка «Додати до бібліографії». Скористайтеся нею – і ми автоматично оформимо бібліографічне посилання на обрану працю в потрібному вам стилі цитування: APA, MLA, «Гарвард», «Чикаго», «Ванкувер» тощо.
Також ви можете завантажити повний текст наукової публікації у форматі «.pdf» та прочитати онлайн анотацію до роботи, якщо відповідні параметри наявні в метаданих.
Переглядайте статті в журналах для різних дисциплін та оформлюйте правильно вашу бібліографію.
Webster, Jack M., April L. Darling, Taylor A. Sanders, Danielle M. Blazier, Yamile Vidal-Aguiar, David Beaulieu-Abdelahad, Drew G. Plemmons, et al. "Hsp22 with an N-Terminal Domain Truncation Mediates a Reduction in Tau Protein Levels." International Journal of Molecular Sciences 21, no. 15 (July 30, 2020): 5442. http://dx.doi.org/10.3390/ijms21155442.
Повний текст джерелаRank, Kenneth B., Adele M. Pauley, Keshab Bhattacharya, Zhigang Wang, David B. Evans, Timothy J. Fleck, Jennifer A. Johnston та Satish K. Sharma. "Direct interaction of soluble human recombinant tau protein with Aβ 1-42 results in tau aggregation and hyperphosphorylation by tau protein kinase II". FEBS Letters 514, № 2-3 (13 березня 2002): 263–68. http://dx.doi.org/10.1016/s0014-5793(02)02376-1.
Повний текст джерелаZhao, Yanyan, Ole Tietz, Wei-Li Kuan, Abdul K. Haji-Dheere, Stephen Thompson, Benjamin Vallin, Elisabetta Ronchi, Gergely Tóth, David Klenerman, and Franklin I. Aigbirhio. "A fluorescent molecular imaging probe with selectivity for soluble tau aggregated protein." Chemical Science 11, no. 18 (2020): 4773–78. http://dx.doi.org/10.1039/c9sc05620c.
Повний текст джерелаChatterjee, Shreyasi, Megan Sealey, Eva Ruiz, Chrysia M. Pegasiou, Keeley Brookes, Sam Green, Anna Crisford, et al. "Age-related changes in tau and autophagy in human brain in the absence of neurodegeneration." PLOS ONE 18, no. 1 (January 26, 2023): e0262792. http://dx.doi.org/10.1371/journal.pone.0262792.
Повний текст джерелаMroczko, Groblewska, and Litman-Zawadzka. "The Role of Protein Misfolding and Tau Oligomers (TauOs) in Alzheimer′s Disease (AD)." International Journal of Molecular Sciences 20, no. 19 (September 20, 2019): 4661. http://dx.doi.org/10.3390/ijms20194661.
Повний текст джерелаGyparaki, Melina Theoni, Arian Arab, Elena M. Sorokina, Adriana N. Santiago-Ruiz, Christopher H. Bohrer, Jie Xiao, and Melike Lakadamyali. "Tau forms oligomeric complexes on microtubules that are distinct from tau aggregates." Proceedings of the National Academy of Sciences 118, no. 19 (May 5, 2021): e2021461118. http://dx.doi.org/10.1073/pnas.2021461118.
Повний текст джерелаCowan, Catherine M., Shmma Quraishe, and Amritpal Mudher. "What is the pathological significance of tau oligomers?" Biochemical Society Transactions 40, no. 4 (July 20, 2012): 693–97. http://dx.doi.org/10.1042/bst20120135.
Повний текст джерелаYu, Hai-Yang, Dong-Mei Gao, Wei Zhou, Bing-Bing Xia, Zhi-Yuan He, Bo Wu, Min-Zhi Jiang, Ming-Li Wang, and Jun Zhao. "Expression, purification, and bioactivity of a soluble recombinant ovine interferon-tau in Escherichia coli." Journal of Veterinary Research 65, no. 1 (January 29, 2021): 101–8. http://dx.doi.org/10.2478/jvetres-2021-0011.
Повний текст джерелаLin, Gaoping, Feiyan Zhu, Nicholas M. Kanaan, Rei Asano, Norimichi Shirafuji, Hirohito Sasaki, Tomohisa Yamaguchi, et al. "Clioquinol Decreases Levels of Phosphorylated, Truncated, and Oligomerized Tau Protein." International Journal of Molecular Sciences 22, no. 21 (November 8, 2021): 12063. http://dx.doi.org/10.3390/ijms222112063.
Повний текст джерелаVitali, Antonella, Alessandra Piccini, Roberta Borghi, Pantaleo Fornaro, Sandra L. Siedlak, Mark A. Smith, Pierluigi Gambetti, Bernardino Ghetti та Massimo Tabaton. "Soluble amyloid β-protein is increased in frontotemporal dementia with tau gene mutations". Journal of Alzheimer's Disease 6, № 1 (20 лютого 2004): 45–51. http://dx.doi.org/10.3233/jad-2004-6106.
Повний текст джерелаCorbett, Grant T., Zemin Wang, Wei Hong, Marti Colom-Cadena, Jamie Rose, Meichen Liao, Adhana Asfaw, et al. "PrP is a central player in toxicity mediated by soluble aggregates of neurodegeneration-causing proteins." Acta Neuropathologica 139, no. 3 (December 18, 2019): 503–26. http://dx.doi.org/10.1007/s00401-019-02114-9.
Повний текст джерелаZhu, Yuanhui, Xi Wang, Miaoyang Hu, Tingyu Yang, Huaisha Xu, Xiuwen Kang, Xufeng Chen, Lei Jiang, Rong Gao та Jun Wang. "Targeting Aβ and p-Tau Clearance in Methamphetamine-Induced Alzheimer’s Disease-Like Pathology: Roles of Syntaxin 17 in Autophagic Degradation in Primary Hippocampal Neurons". Oxidative Medicine and Cellular Longevity 2022 (18 травня 2022): 1–18. http://dx.doi.org/10.1155/2022/3344569.
Повний текст джерелаJENKINS, Scott M., Marcus ZINNERMAN, Craig GARNER, and Gail V. W. JOHNSON. "Modulation of tau phosphorylation and intracellular localization by cellular stress." Biochemical Journal 345, no. 2 (January 10, 2000): 263–70. http://dx.doi.org/10.1042/bj3450263.
Повний текст джерелаPenke, Botond, Ferenc Bogár, Gábor Paragi, János Gera, and Lívia Fülöp. "Key Peptides and Proteins in Alzheimer’s Disease." Current Protein & Peptide Science 20, no. 6 (May 20, 2019): 577–99. http://dx.doi.org/10.2174/1389203720666190103123434.
Повний текст джерелаLo, Chih Hung. "Heterogeneous Tau Oligomers as Molecular Targets for Alzheimer’s Disease and Related Tauopathies." Biophysica 2, no. 4 (November 11, 2022): 440–51. http://dx.doi.org/10.3390/biophysica2040039.
Повний текст джерелаSontag, Jean-Marie, Viyada Nunbhakdi-Craig, and Estelle Sontag. "Leucine Carboxyl Methyltransferase 1 (LCMT1)-dependent Methylation Regulates the Association of Protein Phosphatase 2A and Tau Protein with Plasma Membrane Microdomains in Neuroblastoma Cells." Journal of Biological Chemistry 288, no. 38 (August 13, 2013): 27396–405. http://dx.doi.org/10.1074/jbc.m113.490102.
Повний текст джерелаDeng, Juan, Ahsan Habib, Demian F. Obregon, Steven W. Barger, Brian Giunta, Yan-Jiang Wang, Huayan Hou, Darrell Sawmiller та Jun Tan. "Soluble amyloid precursor protein alpha inhibits tau phosphorylation through modulation of GSK3β signaling pathway". Journal of Neurochemistry 135, № 3 (24 вересня 2015): 630–37. http://dx.doi.org/10.1111/jnc.13351.
Повний текст джерелаO'Neill, Cora, Aoife P. Kiely, Meghan F. Coakley, Sean Manning, and Caitriona M. Long-Smith. "Insulin and IGF-1 signalling: longevity, protein homoeostasis and Alzheimer's disease." Biochemical Society Transactions 40, no. 4 (July 20, 2012): 721–27. http://dx.doi.org/10.1042/bst20120080.
Повний текст джерелаJeppsson, Anna, Carsten Wikkelsö, Kaj Blennow, Henrik Zetterberg, Radu Constantinescu, Anne M. Remes, Sanna-Kaisa Herukka, et al. "CSF biomarkers distinguish idiopathic normal pressure hydrocephalus from its mimics." Journal of Neurology, Neurosurgery & Psychiatry 90, no. 10 (June 5, 2019): 1117–23. http://dx.doi.org/10.1136/jnnp-2019-320826.
Повний текст джерелаSong, Liqing, Evan A. Wells, and Anne Skaja Robinson. "Critical Molecular and Cellular Contributors to Tau Pathology." Biomedicines 9, no. 2 (February 14, 2021): 190. http://dx.doi.org/10.3390/biomedicines9020190.
Повний текст джерелаHanger, D. P., J. P. Brion, J. M. Gallo, N. J. Cairns, P. J. Luthert, and B. H. Anderton. "Tau in Alzheimer's disease and Down's syndrome is insoluble and abnormally phosphorylated." Biochemical Journal 275, no. 1 (April 1, 1991): 99–104. http://dx.doi.org/10.1042/bj2750099.
Повний текст джерелаLesné, Sylvain E. "Breaking the Code of Amyloid-βOligomers". International Journal of Cell Biology 2013 (2013): 1–6. http://dx.doi.org/10.1155/2013/950783.
Повний текст джерелаMoszczynski, Alexander J., Wendy Strong, Kathy Xu, Ann McKee, Arthur Brown, and Michael J. Strong. "Pathologic Thr175 tau phosphorylation in CTE and CTE with ALS." Neurology 90, no. 5 (January 3, 2018): e380-e387. http://dx.doi.org/10.1212/wnl.0000000000004899.
Повний текст джерелаKawasaki, Ryosuke, and Shin-ichi Tate. "Impact of the Hereditary P301L Mutation on the Correlated Conformational Dynamics of Human Tau Protein Revealed by the Paramagnetic Relaxation Enhancement NMR Experiments." International Journal of Molecular Sciences 21, no. 11 (May 30, 2020): 3920. http://dx.doi.org/10.3390/ijms21113920.
Повний текст джерелаMaté de Gérando, Anastasie, Marie d’Orange, Emma Augustin, Charlène Joséphine, Gwénaelle Aurégan, Mylène Gaudin-Guérif, Martine Guillermier, et al. "Neuronal tau species transfer to astrocytes and induce their loss according to tau aggregation state." Brain 144, no. 4 (April 1, 2021): 1167–82. http://dx.doi.org/10.1093/brain/awab011.
Повний текст джерелаHonisch, Claudia, Federica Torni, Rohanah Hussain, Paolo Ruzza, and Giuliano Siligardi. "Effect of Trehalose and Ceftriaxone on the Stability of Aggregating-Prone Tau Peptide Containing PHF6* Sequence: An SRCD Study." International Journal of Molecular Sciences 23, no. 6 (March 8, 2022): 2932. http://dx.doi.org/10.3390/ijms23062932.
Повний текст джерелаRamser, Elisa M., Kathlyn J. Gan, Helena Decker, Emily Y. Fan, Matthew M. Suzuki, Sergio T. Ferreira та Michael A. Silverman. "Amyloid-β oligomers induce tau-independent disruption of BDNF axonal transport via calcineurin activation in cultured hippocampal neurons". Molecular Biology of the Cell 24, № 16 (15 серпня 2013): 2494–505. http://dx.doi.org/10.1091/mbc.e12-12-0858.
Повний текст джерелаJin, M., N. Shepardson, T. Yang, G. Chen, D. Walsh, and D. J. Selkoe. "Soluble amyloid -protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration." Proceedings of the National Academy of Sciences 108, no. 14 (March 18, 2011): 5819–24. http://dx.doi.org/10.1073/pnas.1017033108.
Повний текст джерелаEckert, Anne, Susanne Hauptmann, Isabel Scherping, Virginie Rhein, Franz Müller-Spahn, Jürgen Götz, and Walter E. Müller. "Soluble Beta-Amyloid Leads to Mitochondrial Defects in Amyloid Precursor Protein and Tau Transgenic Mice." Neurodegenerative Diseases 5, no. 3-4 (2008): 157–59. http://dx.doi.org/10.1159/000113689.
Повний текст джерелаOndrejcak, Tomas, Igor Klyubin, Grant T. Corbett, Graham Fraser, Wei Hong, Alexandra J. Mably, Matthew Gardener, et al. "Cellular Prion Protein Mediates the Disruption of Hippocampal Synaptic Plasticity by Soluble Tau In Vivo." Journal of Neuroscience 38, no. 50 (October 24, 2018): 10595–606. http://dx.doi.org/10.1523/jneurosci.1700-18.2018.
Повний текст джерелаVieira, Marcelo N. N., Letícia Forny-Germano, Leonardo M. Saraiva, Adriano Sebollela, Ana M. Blanco Martinez, Jean-Christophe Houzel, Fernanda G. De Felice та Sérgio T. Ferreira. "Soluble oligomers from a non-disease related protein mimic Aβ-induced tau hyperphosphorylation and neurodegeneration". Journal of Neurochemistry 103, № 2 (11 липня 2007): 736–48. http://dx.doi.org/10.1111/j.1471-4159.2007.04809.x.
Повний текст джерелаCarroll, Trae, Sanjib Guha, Keith Nehrke, and Gail V. W. Johnson. "Tau Post-Translational Modifications: Potentiators of Selective Vulnerability in Sporadic Alzheimer’s Disease." Biology 10, no. 10 (October 15, 2021): 1047. http://dx.doi.org/10.3390/biology10101047.
Повний текст джерелаSiano, Giacomo, Chiara Falcicchia, Nicola Origlia, Antonino Cattaneo, and Cristina Di Primio. "Non-Canonical Roles of Tau and Their Contribution to Synaptic Dysfunction." International Journal of Molecular Sciences 22, no. 18 (September 20, 2021): 10145. http://dx.doi.org/10.3390/ijms221810145.
Повний текст джерелаHromadkova, Lenka, and Saak Victor Ovsepian. "Tau-Reactive Endogenous Antibodies: Origin, Functionality, and Implications for the Pathophysiology of Alzheimer’s Disease." Journal of Immunology Research 2019 (August 6, 2019): 1–11. http://dx.doi.org/10.1155/2019/7406810.
Повний текст джерелаFeuillette, Sébastien, Laetitia Miguel, Thierry Frébourg, Dominique Campion, and Magalie Lecourtois. "Drosophilamodels of human tauopathies indicate that Tau protein toxicityin vivois mediated by soluble cytosolic phosphorylated forms of the protein." Journal of Neurochemistry 113, no. 4 (May 2010): 895–903. http://dx.doi.org/10.1111/j.1471-4159.2010.06663.x.
Повний текст джерелаAbdelhamid, Mona, Chunyu Zhou, Cha-Gyun Jung, and Makoto Michikawa. "Probiotic Bifidobacterium breve MCC1274 Mitigates Alzheimer’s Disease-Related Pathologies in Wild-Type Mice." Nutrients 14, no. 12 (June 19, 2022): 2543. http://dx.doi.org/10.3390/nu14122543.
Повний текст джерелаLiu, Zhenzhen, Tao Li, Ping Li, Nannan Wei, Zhiquan Zhao, Huimin Liang, Xinying Ji, Wenwu Chen, Mengzhou Xue, and Jianshe Wei. "The Ambiguous Relationship of Oxidative Stress, Tau Hyperphosphorylation, and Autophagy Dysfunction in Alzheimer’s Disease." Oxidative Medicine and Cellular Longevity 2015 (2015): 1–12. http://dx.doi.org/10.1155/2015/352723.
Повний текст джерелаDe Strooper, Bart. "Proteases and Proteolysis in Alzheimer Disease: A Multifactorial View on the Disease Process." Physiological Reviews 90, no. 2 (April 2010): 465–94. http://dx.doi.org/10.1152/physrev.00023.2009.
Повний текст джерелаLemke, Nora, Valeria Melis, Dilyara Lauer, Mandy Magbagbeolu, Boris Neumann, Charles R. Harrington, Gernot Riedel, Claude M. Wischik, Franz Theuring, and Karima Schwab. "Differential compartmental processing and phosphorylation of pathogenic human tau and native mouse tau in the line 66 model of frontotemporal dementia." Journal of Biological Chemistry 295, no. 52 (October 30, 2020): 18508–23. http://dx.doi.org/10.1074/jbc.ra120.014890.
Повний текст джерелаNatale, Carmina, Maria Monica Barzago, and Luisa Diomede. "Caenorhabditis elegans Models to Investigate the Mechanisms Underlying Tau Toxicity in Tauopathies." Brain Sciences 10, no. 11 (November 11, 2020): 838. http://dx.doi.org/10.3390/brainsci10110838.
Повний текст джерелаSayner, Sarah L., Ron Balczon, Dara W. Frank, Dermot M. F. Cooper, and Troy Stevens. "Filamin A is a phosphorylation target of membrane but not cytosolic adenylyl cyclase activity." American Journal of Physiology-Lung Cellular and Molecular Physiology 301, no. 1 (July 2011): L117—L124. http://dx.doi.org/10.1152/ajplung.00417.2009.
Повний текст джерелаMaron, Ruth, Gad Armony, Michael Tsoory, Meir Wilchek, Dan Frenkel, and Ruth Arnon. "Peptide Interference with APP and Tau Association: Relevance to Alzheimer’s Disease Amelioration." International Journal of Molecular Sciences 21, no. 9 (May 5, 2020): 3270. http://dx.doi.org/10.3390/ijms21093270.
Повний текст джерелаPinzi, Luca, Annachiara Tinivella, and Giulio Rastelli. "Chemoinformatics Analyses of Tau Ligands Reveal Key Molecular Requirements for the Identification of Potential Drug Candidates against Tauopathies." Molecules 26, no. 16 (August 20, 2021): 5039. http://dx.doi.org/10.3390/molecules26165039.
Повний текст джерелаZhang, Xiang, Shengnan Zhang, Li Zhang, Jinxia Lu, Chunyu Zhao, Feng Luo, Dan Li, Xueming Li, and Cong Liu. "Heat shock protein 104 (HSP104) chaperones soluble Tau via a mechanism distinct from its disaggregase activity." Journal of Biological Chemistry 294, no. 13 (February 4, 2019): 4956–65. http://dx.doi.org/10.1074/jbc.ra118.005980.
Повний текст джерелаPerea, Juan Ramón, Marta Bolós, and Jesús Avila. "Microglia in Alzheimer’s Disease in the Context of Tau Pathology." Biomolecules 10, no. 10 (October 14, 2020): 1439. http://dx.doi.org/10.3390/biom10101439.
Повний текст джерелаKumar, Arvind. "A Review on: Alzheimer’s disease and mechanistic insights of bioactive compounds in its treatment." YMER Digital 21, no. 07 (July 31, 2022): 1297–307. http://dx.doi.org/10.37896/ymer21.07/a9.
Повний текст джерелаMelo, Ana M., Juliana Coraor, Garrett Alpha-Cobb, Shana Elbaum-Garfinkle, Abhinav Nath, and Elizabeth Rhoades. "A functional role for intrinsic disorder in the tau-tubulin complex." Proceedings of the National Academy of Sciences 113, no. 50 (November 23, 2016): 14336–41. http://dx.doi.org/10.1073/pnas.1610137113.
Повний текст джерелаSteen Jensen, Camilla, Erik Portelius, Volkert Siersma, Peter Høgh, Lene Wermuth, Kaj Blennow, Henrik Zetterberg, Gunhild Waldemar, Steen Gregers Hasselbalch, and Anja Hviid Simonsen. "Cerebrospinal Fluid Amyloid Beta and Tau Concentrations Are Not Modulated by 16 Weeks of Moderate- to High-Intensity Physical Exercise in Patients with Alzheimer Disease." Dementia and Geriatric Cognitive Disorders 42, no. 3-4 (2016): 146–58. http://dx.doi.org/10.1159/000449408.
Повний текст джерелаBansal, Aditya, Yari Carlomagno, Leonard Petrucelli, Val Lowe, Casey Cook, and Mukesh Pandey. "In-vitro binding assessment of soluble and insoluble tau protein variants with [18F]-AV1451 and [18F]-MK6240." Nuclear Medicine and Biology 108-109 (May 2022): S99—S100. http://dx.doi.org/10.1016/s0969-8051(22)00228-1.
Повний текст джерелаBloom, George S., and Andrés Norambuena. "Alzheimer’s disease as a metabolic disorder." OCL 25, no. 4 (July 2018): D403. http://dx.doi.org/10.1051/ocl/2018044.
Повний текст джерела