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Relevant bibliographies by topics / Paired Helical Filaments

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Academic literature on the topic 'Paired Helical Filaments'

Author: Grafiati

Published: 14 March 2023

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Journal articles on the topic "Paired Helical Filaments"

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Iqbal, K., I. Griindke-Iqbnl, and H. M. Wisniewaki. "ALZHEIMER PAIRED HELICAL FILAMENTS." Journal of Neuropathology and Experimental Neurology 44, no. 3 (May 1985): 366. http://dx.doi.org/10.1097/00005072-198505000-00187.

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Metuzals, J. "Neurofilaments and Paired Helical Filaments." Proceedings, annual meeting, Electron Microscopy Society of America 43 (August 1985): 740–43. http://dx.doi.org/10.1017/s0424820100120357.

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It has been demonstrated that the neurofibrillary tangles in biopsies of Alzheimer patients, composed of typical paired helical filaments (PHF), consist also of typical neurofilaments (NF) and 15nm wide filaments. Close structural relationships, and even continuity between NF and PHF, have been observed. In this paper, such relationships are investigated from the standpoint that the PHF are formed through posttranslational modifications of NF. To investigate the validity of the posttranslational modification hypothesis of PHF formation, we have identified in thin sections from frontal lobe biopsies of Alzheimer patients all existing conformations of NF and PHF and ordered these conformations in a hypothetical sequence. However, only experiments with animal model preparations will prove or disprove the validity of the interpretations of static structural observations made on patients. For this purpose, the results of in vitro experiments with the squid giant axon preparations are compared with those obtained from human patients. This approach is essential in discovering etiological factors of Alzheimer's disease and its early diagnosis.

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Yoshida, Hirotaka, and Yasuo Ihara. "? in Paired Helical Filaments Is Functionally Distinct from Fetal ?: Assembly Incompetence of Paired Helical Filament-?" Journal of Neurochemistry 61, no. 3 (September 1993): 1183–86. http://dx.doi.org/10.1111/j.1471-4159.1993.tb03642.x.

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Chen, Shu G. "Molecular profiling of paired helical filaments." Journal of Alzheimer's Disease 3, no. 5 (September 30, 2001): 467–69. http://dx.doi.org/10.3233/jad-2001-3505.

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Anderton, Brian H. "Paired helical filaments and the cytoskeleton." Nature 335, no. 6190 (October 1988): 497–98. http://dx.doi.org/10.1038/335497a0.

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Lhara, Yasuo, and Jun Kondo. "Polypeptide Composition of Paired Helical Filaments." Annals of Medicine 21, no. 2 (January 1989): 121–25. http://dx.doi.org/10.3109/07853898909149198.

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Mori, H., J. Kondo, S. Kuzuhara, and Y. Ihara. "UBIQUITIN IN ALZHEIMERʼS PAIRED HELICAL FILAMENTS." Journal of Neuropathology and Experimental Neurology 46, no. 3 (May 1987): 332. http://dx.doi.org/10.1097/00005072-198705000-00009.

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Kidd, Michael. "The history of the paired helical filaments." Journal of Alzheimer's Disease 9, s3 (July 27, 2006): 71–75. http://dx.doi.org/10.3233/jad-2006-9s309.

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Ihara, Yasuo. "Neurofibrillary tangles/paired helical filaments (1981–83)." Journal of Alzheimer's Disease 9, s3 (July 27, 2006): 209–17. http://dx.doi.org/10.3233/jad-2006-9s324.

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GRAY, E. G., M. PAULA-BARBOSA, and A. ROHER. "ALZHEIMER'S DISEASE: PAIRED HELICAL FILAMENTS AND CYTOMEMBRANES." Neuropathology and Applied Neurobiology 13, no. 2 (March 1987): 91–110. http://dx.doi.org/10.1111/j.1365-2990.1987.tb00174.x.

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Dissertations / Theses on the topic "Paired Helical Filaments"

1

Wischik, Claude M. "The structure and biochemistry of paired helical filaments in Alzheimer's disease." Thesis, University of Cambridge, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.315916.

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Li, Li. "Tryptophan and proline scanning mutagenesis a tool to study the aggregation of tau protein into Alzheimer paired helical filaments /." [S.l.] : [s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=967241790.

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Guix, Ràfols Francesc Xavier. "Study of the pathophysiological role of nitric oxide on the amyloid-induced toxicity attending to the biochemical modifications and cellular damages." Doctoral thesis, Universitat Pompeu Fabra, 2009. http://hdl.handle.net/10803/7162.

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Aquesta tesi demostra que el peroxinitrit produït com a conseqüència del pèptid beta-amiloide (A) contribueix l'augment de la relació A42/A40 que ocorre a la malaltia d'Alzheimer. L'A42 contribueix a l'aparició de la malaltia degut a la seva major toxicitat (quan es compara amb l'A40) que resulta d'una gran estabilitat i capacitat agregativa. A més el peroxinitrit incrementa la toxicitat d'aquest degut a què potencia la seva agregació en forma d'oligomers altament tòxics. De fet els oligomers formats de nitro-A42 presenten una major toxicitat que aquells formats de A42 . En conjunt aquest resultats senyalen l'important paper que l'A42 té en la malaltia d'Alzheimer.
Per altra banda, des de la identificació dels agregats d'A i la subseqüent formació dels cabdells neurofibrilars (NFT) com a els dos trets distintius de la malaltia, un gran esforç s'ha dedicat a establir els mecanismes moleculars que uneixen ambdós processos. Aquesta tesi demostra que el peroxinitrit format a partir de l'agregació de d'Ai la conseqüent nitrotirosinació de proteïnes, potencia l'agregació de la proteïna tau en forma de fibres. D'aquesta forma, la nitrotirosinació de la proteïna triosafosfat isomerasa (TPI) podria ser el vincle entre la toxicitat derivada del agregats d'Ai la patologia derivada de la proteïna tau. Per tant, la nitrotirosinació de la TPI podria explicar la progressió temporal que ocorre als cervells de pacients amb la malaltia d'Alzheimer des de la toxicitat induïda per l'Ai l'aparició dels NFT. Els resultats presentats en aquesta tesi podrien obrir nous aspectes en la recerca de la malaltia d'Alzheimer així com en altres malalties que cursin amb estrès oxidatiu i plegament erroni de proteïnes.
This thesis demonstrates that amyloid ß-peptide (Aß)-induced peroxynitrite contributes to the switch of the Aβ42/Aβ40 ratio that occurs in Alzheimer's disease (AD). Since Aβ42 is more toxic due to its higher aggregation and stability, it contributes to the trigger of the disease. In addition the aggregation of Aβ42 in form of the highly toxic oligomers is incremented by the presence of peroxynitrite. Moreover, these nitro-Aß42 oligomers are more toxic than those non-nitrated. All these results support the important role of peroxynitrite in AD etiology.
Furthermore, since the identification of Aß accumulation and the subsequent formation of neurofibrillary tangles (NFT) as the two defining pathological hallmarks of AD, a fair amount of research on AD has been driven by the need to find the molecular mechanism linking Aß and NFT. This thesis shows the Aß-induced peroxynitrite, and the consequent nitrotyrosination of proteins, promotes tau fibrillization. Thus triosephosphate isomerase (TPI) nitrotyrosination could be the link between Aß-induced toxicity and tau pathology. Therefore, TPI nitrotyrosination may explain the temporal progression from Aß toxicity to NFT formation in AD brain. The work presented in this thesis could open a novel angle in the research of the pathophysiology of AD and could also have an impact to the research in other neurodegenerative diseases involving oxidative stress and protein misfolding.

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Li, Li [Verfasser]. "Tryptophan and proline scanning mutagenesis : a tool to study the aggregation of tau protein into Alzheimer paired helical filaments / presented by Li Li." 2003. http://d-nb.info/967241790/34.

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Book chapters on the topic "Paired Helical Filaments"

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Wisniewski, H. M., and K. Iqbal. "Paired Helical Filaments (PHF): Update 1988." In Genetics and Alzheimer’s Disease, 157–63. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73647-6_17.

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Mandelkow, E., M. von Bergen, A. Marx, J. Biernat, and E. M. Mandelkow. "The Search for structure of tau and paired helical filaments." In Alzheimer: 100 Years and Beyond, 355–64. Berlin, Heidelberg: Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/978-3-540-37652-1_45.

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Mandelkow, E., J. Biernat, B. Lichtenberg-Kraag, G. Drewes, H. Wille, N. Gustke, K. Baumann, and E. M. Mandelkow. "Microtubules, Tau Protein,and Paired Helical Filaments in Alzheimer’s Disease." In The Cytoskeleton, 143–60. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79482-7_16.

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Delacourte, A., and A. Defossez. "Paired Helical Filaments in Alzheimer’s Disease: Their Formation and Transformation." In Immunology and Alzheimer’s Disease, 55–67. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-46634-2_6.

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Mandelkow, E. M., J. Biernat, B. Lichtenberg-Kraag, G. Drewes, H. Wille, N. Gustke, K. Baumann, and E. Mandelkow. "Phosphorylation of Tau and Its Relationship with Alzheimer Paired Helical Filaments." In Alzheimer’s Disease: Lessons from Cell Biology, 103–20. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79423-0_10.

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Mandelkow, Eckhard, Peter Friedhoff, Jacek Biernat, and Eva-Maria Mandelkow. "The Conformations of Tau Protein and its Aggregation into Alzheimer Paired Helical Filaments." In Advances in Behavioral Biology, 223–33. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5337-3_32.

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Otvos, Laszlo, Virginia M. Y. Lee, Susan Leight, Peter Davies, and Ralf Hoffmann. "Multiphosphorylated synthetic peptides as antigens and immunogens in Alzheimer’s disease paired helical filaments." In Peptides Frontiers of Peptide Science, 695–97. Dordrecht: Springer Netherlands, 2002. http://dx.doi.org/10.1007/0-306-46862-x_304.

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Selkoe, Dennis J., Carmela Abraham, and C. G. Rasool. "Molecular Properties of Paired Helical Filaments and Senile Plaque Amyloid Fibers in Alzheimer’s Disease." In Advances in Behavioral Biology, 37–42. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2179-8_5.

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Lee, Virginia M. Y., and Laszlo Otvos. "Identification of an abnormal phosphorylation site in Alzheimer’s disease paired helical filaments using synthetic peptides." In Peptides, 109–12. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2264-1_34.

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Selkoe, Dennis J., and Carmela Abraham. "Biochemical and Structural Studies of Paired Helical Filaments and Senile Plaque Amyloid in Alzheimer’s Disease." In Amyloidosis, 709–15. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2199-6_90.

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Conference papers on the topic "Paired Helical Filaments"

1

Stork, Larissa Rosa, Lucca Stephani Ribeiro, Izabella Savergnini Deprá, Luísa D’Ávila Camargo, and Maria Angélica Santos Novaes. "Tau protein and its role in Alzheimer’s disease physiopathology: a literature review." In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.132.

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Background: Alzheimer’s disease (AD) is a neurodegenerative disorder characterized by a double proteinopathy: deposition of amyloid-β into plaques and hyperphosphorylation of Tau protein. Objectives: To understand the genetic and molecular aspects of Tau protein and its relationship with Alzheimer’s disease. Methods: We conducted a systematic literature search using Pubmed/ MEDLINE and ClinicalKey databases, applying the descriptors: “Alzheimer Disease” AND “Tau proteins’’ AND Tauopathies, during July and August of 2020. The inclusion criteria were English and Portuguese articles published between 2015 and 2020, with human limited study and free full text, excluding images, books, clinical tests, and narrative reviews. After analyzing titles and abstracts, we selected 12 articles and included 7 additional studies. Results: Mapt, the encoder gene of Tau, is located in the 17q21.3 locus and presents 16 exons that, when transcripted, originates 12 copies of mRNA by alternative splicing and 6 Tau’s isoforms. Tau is a microtubule-associated protein (MAP) responsible for cellular cytoskeleton stabilization and maintenance, promoting neuronal axonal transport. A kinase-phosphatase imbalance turns Tau hyperphosphorylated, disassociating it from tubulin and grouping it into insoluble paired helical filaments, which originates neurofibrillary tangles. The tauopathy’s progress causes neurotransmitter destabilization and neuronal death, inducing AD symptomatic manifestations. Conclusions: Due to the gradual worsening of the disease to more debilitating stages, studies focused on deepening the knowledge of genetic and molecular aspects of Tau protein are viable and promising alternatives to improve the quality of patient’s lives.

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