All Relations between microtubule-associated protein tau and nucleus prepositus

Publication Sentence Publish Date Extraction Date Species
Alexis Fenyi, Audrey Coens, Tracy Bellande, Ronald Melki, Luc Bousse. Assessment of the efficacy of different procedures that remove and disassemble alpha-synuclein, tau and A-beta fibrils from laboratory material and surfaces. Scientific reports. vol 8. issue 1. 2019-11-20. PMID:30018327. we show that commercial detergents and sds are way more suited to detach α-synuclein fibrillar polymorphs, tau and aß 1-42 fibrillar assemblies from contaminated surfaces and disassemble the fibrils than methods designed to decrease prp prion infectivity. 2019-11-20 2023-08-13 Not clear
Keisuke Ishizawa, Takashi Mitsufuji, Kei Shioda, Atsushi Kobayashi, Takashi Komori, Yoshihiko Nakazato, Tetsuyuki Kitamoto, Nobuo Araki, Toshimasa Yamamoto, Atsushi Sasak. An autopsy report of three kindred in a Gerstmann-Sträussler-Scheinker disease P105L family with a special reference to prion protein, tau, and beta-amyloid. Brain and behavior. vol 8. issue 10. 2019-07-22. PMID:30240140. this report describes a clinicopathological analysis of three autopsied kindred from a japanese gss105 family, plus a topological analysis of prp, hyperphosphorylated tau (p-tau), and beta-amyloid (aβ). 2019-07-22 2023-08-13 Not clear
Anne H S Martinelli, Fernanda C Lopes, Elisa B O John, Célia R Carlini, Rodrigo Ligabue-Brau. Modulation of Disordered Proteins with a Focus on Neurodegenerative Diseases and Other Pathologies. International journal of molecular sciences. vol 20. issue 6. 2019-07-03. PMID:30875980. in this review, we discuss some idps that are involved in neurodegenerative diseases (such as beta amyloid, alpha synuclein, tau, and the "idp-like" prp), cancer (p53, c-myc), and diabetes (amylin), focusing on the structural changes of these idps that are linked to such pathologies. 2019-07-03 2023-08-13 Not clear
Franc Llorens, Tomás Barrio, Ângela Correia, Anna Villar-Piqué, Katrin Thüne, Peter Lange, Juan José Badiola, Matthias Schmitz, Ingolf Lachmann, Rosa Bolea, Inga Zer. Cerebrospinal Fluid Prion Disease Biomarkers in Pre-clinical and Clinical Naturally Occurring Scrapie. Molecular neurobiology. vol 55. issue 11. 2018-12-17. PMID:29572672. while decreased total prion protein (prp) levels and positive prp seeding activity were already detectable at pre-symptomatic stages, the surrogate markers of neuronal damage total tau (tau) and 14-3-3 proteins were exclusively increased at clinical stages. 2018-12-17 2023-08-13 human
Isidro Ferre. Diversity of astroglial responses across human neurodegenerative disorders and brain aging. Brain pathology (Zurich, Switzerland). vol 27. issue 5. 2018-08-20. PMID:28804999. in addition to the well-known increase in glial fibrillary acidic protein and other proteins in reactive astrocytes, astrocytopathy is evidenced by deposition of abnormal proteins such as β-amyloid, hyper-phosphorylated tau, abnormal α-synuclein, mutated huntingtin, phosphorylated tdp-43 and mutated sod1, and prp 2018-08-20 2023-08-13 human
Gabor G Kovacs, Jasmin Rahimi, Thomas Ströbel, Mirjam I Lutz, Günther Regelsberger, Nathalie Streichenberger, Armand Perret-Liaudet, Romana Höftberger, Pawel P Liberski, Herbert Budka, Beata Sikorsk. Tau pathology in Creutzfeldt-Jakob disease revisited. Brain pathology (Zurich, Switzerland). vol 27. issue 3. 2017-04-24. PMID:27377321. the frequency of tau pathologies is not unusually high in sporadic cjd and does not precisely relate to prp deposition. 2017-04-24 2023-08-13 human
Ariel A Valiente-Gabioud, Marco C Miotto, María E Chesta, Verónica Lombardo, Andres Binolfi, Claudio O Fernánde. Phthalocyanines as Molecular Scaffolds to Block Disease-Associated Protein Aggregation. Accounts of chemical research. vol 49. issue 5. 2017-03-10. PMID:27136297. these tetrapyrrolic compounds modulate the amyloid assembly of αs, tau, aβ, and the prp in vitro, and protect cells from the toxic effects of amyloid aggregates. 2017-03-10 2023-08-13 mouse
Takashi Miyamoto, Daniel Kim, Joseph A Knox, Erik Johnson, Lennart Muck. Increasing the Receptor Tyrosine Kinase EphB2 Prevents Amyloid-β-induced Depletion of Cell Surface Glutamate Receptors by a Mechanism That Requires the PDZ-binding Motif of EphB2 and Neuronal Activity. The Journal of biological chemistry. vol 291. issue 4. 2016-08-22. PMID:26589795. in addition, we show that the aβ-induced depletion of surface nmdars does not depend on several factors that have been implicated in the pathogenesis of aβ-induced neuronal dysfunction, including aberrant neuronal activity, tau, prion protein (prp(c)), and ephb2 itself. 2016-08-22 2023-08-13 Not clear
Lary C Walker, Mathias Jucke. The Malignant Protein Puzzle. Cerebrum : the Dana forum on brain science. vol 2016. 2016-07-13. PMID:27408676. studying how proteins such as prp, amyloid beta, tau, and others aggregate and spread, and kill brain cells, represents a crucial new frontier in neuroscience. 2016-07-13 2023-08-13 Not clear
C Vergara, L Ordóñez-Gutiérrez, F Wandosell, I Ferrer, J A del Río, R Gaví. Role of PrP(C) Expression in Tau Protein Levels and Phosphorylation in Alzheimer's Disease Evolution. Molecular neurobiology. vol 51. issue 3. 2016-03-10. PMID:24965601. role of prp(c) expression in tau protein levels and phosphorylation in alzheimer's disease evolution. 2016-03-10 2023-08-13 mouse
C Vergara, L Ordóñez-Gutiérrez, F Wandosell, I Ferrer, J A del Río, R Gaví. Role of PrP(C) Expression in Tau Protein Levels and Phosphorylation in Alzheimer's Disease Evolution. Molecular neurobiology. vol 51. issue 3. 2016-03-10. PMID:24965601. reported data suggest a regulatory tendency of prp(c) expression in the development of ad, and a putative relationship between prp(c) and tau processing is emerging. 2016-03-10 2023-08-13 mouse
C Vergara, L Ordóñez-Gutiérrez, F Wandosell, I Ferrer, J A del Río, R Gaví. Role of PrP(C) Expression in Tau Protein Levels and Phosphorylation in Alzheimer's Disease Evolution. Molecular neurobiology. vol 51. issue 3. 2016-03-10. PMID:24965601. in this study, we show increased susceptibility to aβ-derived diffusible ligands (addls) in neuronal primary cultures from prp(c) knockout mice, compared to wild-type, which correlates with increased tau expression. 2016-03-10 2023-08-13 mouse
C Vergara, L Ordóñez-Gutiérrez, F Wandosell, I Ferrer, J A del Río, R Gaví. Role of PrP(C) Expression in Tau Protein Levels and Phosphorylation in Alzheimer's Disease Evolution. Molecular neurobiology. vol 51. issue 3. 2016-03-10. PMID:24965601. moreover, we found increased prp(c) expression that paralleled with tau at early ages in an ad murine model and in early braak stages of ad in affected individuals. 2016-03-10 2023-08-13 mouse
C Vergara, L Ordóñez-Gutiérrez, F Wandosell, I Ferrer, J A del Río, R Gaví. Role of PrP(C) Expression in Tau Protein Levels and Phosphorylation in Alzheimer's Disease Evolution. Molecular neurobiology. vol 51. issue 3. 2016-03-10. PMID:24965601. taken together, these results suggest a protective role for prp(c) in ad by downregulating tau expression, and they point to this protein as being crucial in the molecular events that lead to neurodegeneration in ad. 2016-03-10 2023-08-13 mouse
Thomas Tousseyn, Krystyna Bajsarowicz, Henry Sánchez, Ania Gheyara, Abby Oehler, Michael Geschwind, Bernadette DeArmond, Stephen J DeArmon. Prion Disease Induces Alzheimer Disease-Like Neuropathologic Changes. Journal of neuropathology and experimental neurology. vol 74. issue 9. 2015-11-16. PMID:26226132. we conclude that priond may trigger biochemical changes similar to those triggered by ad and suggest that priond is a disease involving prp, aβ42, apoe-4, and abnormal tau. 2015-11-16 2023-08-13 human
Kathrin Andrich, Jan Bieschk. The Effect of (-)-Epigallo-catechin-(3)-gallate on Amyloidogenic Proteins Suggests a Common Mechanism. Advances in experimental medicine and biology. vol 863. 2015-10-02. PMID:26092630. studies on the interaction of the green tea polyphenol (-)-epigallocatechin-3-gallate (egcg) with fourteen disease-related amyloid polypeptides and prions huntingtin, amyloid-beta, alpha-synuclein, islet amyloid polypeptide (iapp), sup35, nm25 and nm4, tau, msp2, semen-derived enhancer of virus infection (sevi), immunoglobulin light chains, beta-microglobulin, prion protein (prp) and insulin, have yielded a variety of experimental observations. 2015-10-02 2023-08-13 Not clear
Pedro Piccardo, Juraj Cervenak, Ming Bu, Lindsay Miller, David M Ashe. Complex proteinopathy with accumulations of prion protein, hyperphosphorylated tau, α-synuclein and ubiquitin in experimental bovine spongiform encephalopathy of monkeys. The Journal of general virology. vol 95. issue Pt 7. 2014-08-22. PMID:24769839. squirrel monkeys infected with the classical bovine spongiform encephalopathy agent developed an encephalopathy resembling variant creutzfeldt-jakob disease with accumulations not only of abnormal prion protein (prp(tse)), but also three other proteins: hyperphosphorylated tau (p-tau), α-synuclein and ubiquitin; β-amyloid protein (aβ) did not accumulate. 2014-08-22 2023-08-13 mouse
Monique Antoinette David, Daryl Rhys Jones, Mourad Tayeb. Potential candidate camelid antibodies for the treatment of protein-misfolding diseases. Journal of neuroimmunology. vol 272. issue 1-2. 2014-07-31. PMID:24864011. these antibodies could prove to be a valuable tool for the neutralization/clearance of prp(sc), aβ and tau proteins in cellular compartments of affected neurons and could potentially have wider applicability for the treatment of pmds. 2014-07-31 2023-08-13 Not clear
Matthias Schmitz, Katharina Wulf, Sandra C Signore, Walter J Schulz-Schaeffer, Pawel Kermer, Mathias Bähr, Fred S Wouters, Saima Zafar, Inga Zer. Impact of the cellular prion protein on amyloid-β and 3PO-tau processing. Journal of Alzheimer's disease : JAD. vol 38. issue 3. 2014-07-17. PMID:24028865. in the present study, we analyzed the involvement of prp(c) in different pathological mechanisms underlying ad: the processing of the amyloid-β protein precursor (aβpp) and its interaction with aβpp, tau, and different phosphorylated forms of the tau protein (p-tau). 2014-07-17 2023-08-12 mouse
Matthias Schmitz, Katharina Wulf, Sandra C Signore, Walter J Schulz-Schaeffer, Pawel Kermer, Mathias Bähr, Fred S Wouters, Saima Zafar, Inga Zer. Impact of the cellular prion protein on amyloid-β and 3PO-tau processing. Journal of Alzheimer's disease : JAD. vol 38. issue 3. 2014-07-17. PMID:24028865. the effect of prp(c) on tau expression was investigated in various cellular compartments using a hek293 cell model expressing a tau mutant (3po-tau) or wild type (wt)-tau. 2014-07-17 2023-08-12 mouse