Academic literature on the topic 'Phosphorylated tau'
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Journal articles on the topic "Phosphorylated tau"
LITERSKY, Joel M., Gail V. W. JOHNSON, Ross JAKES, Michel GOEDERT, Michael LEE, and Peter SEUBERT. "Tau protein is phosphorylated by cyclic AMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II within its microtubule-binding domains at Ser-262 and Ser-356." Biochemical Journal 316, no. 2 (June 1, 1996): 655–60. http://dx.doi.org/10.1042/bj3160655.
Full textSen, Tanusree, Pampa Saha, Tong Jiang, and Nilkantha Sen. "Sulfhydration of AKT triggers Tau-phosphorylation by activating glycogen synthase kinase 3β in Alzheimer’s disease." Proceedings of the National Academy of Sciences 117, no. 8 (February 12, 2020): 4418–27. http://dx.doi.org/10.1073/pnas.1916895117.
Full textGoedert, Michel. "Pinning down phosphorylated tau." Nature 399, no. 6738 (June 1999): 739–40. http://dx.doi.org/10.1038/21550.
Full text陈, 亦刚. "Abnormally Phosphorylated Tau and Tauopathies." International Journal of Psychiatry and Neurology 06, no. 02 (2017): 7–12. http://dx.doi.org/10.12677/ijpn.2017.62002.
Full textWOODS, Yvonne L., Philip COHEN, Walter BECKER, Ross JAKES, Michel GOEDERT, Xuemin WANG, and Christopher G. PROUD. "The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bɛ at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase." Biochemical Journal 355, no. 3 (April 24, 2001): 609–15. http://dx.doi.org/10.1042/bj3550609.
Full textAnderton, Brian H., Joanna Betts, Walter P. Blackstock, Jean-Pierre Brion, Sara Chapman, James Connell, Rejith Dayanandan, et al. "Sites of phosphorylation in tau and factors affecting their regulation." Biochemical Society Symposia 67 (February 1, 2001): 73–80. http://dx.doi.org/10.1042/bss0670073.
Full textArai, Tetsuaki, Jian-Ping Guo, and Patrick L. McGeer. "Proteolysis of Non-phosphorylated and Phosphorylated Tau by Thrombin." Journal of Biological Chemistry 280, no. 7 (November 12, 2004): 5145–53. http://dx.doi.org/10.1074/jbc.m409234200.
Full textGoedert, M., R. Jakes, R. A. Crowther, P. Cohen, E. Vanmechelen, M. Vandermeeren, and P. Cras. "Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: identification of phosphorylation sites in tau protein." Biochemical Journal 301, no. 3 (August 1, 1994): 871–77. http://dx.doi.org/10.1042/bj3010871.
Full textDrummond, Eleanor, Geoffrey Pires, Claire MacMurray, Manor Askenazi, Shruti Nayak, Marie Bourdon, Jiri Safar, Beatrix Ueberheide, and Thomas Wisniewski. "Phosphorylated tau interactome in the human Alzheimer’s disease brain." Brain 143, no. 9 (August 19, 2020): 2803–17. http://dx.doi.org/10.1093/brain/awaa223.
Full textTseng, H. C., Q. Lu, E. Henderson, and D. J. Graves. "Phosphorylated tau can promote tubulin assembly." Proceedings of the National Academy of Sciences 96, no. 17 (August 17, 1999): 9503–8. http://dx.doi.org/10.1073/pnas.96.17.9503.
Full textDissertations / Theses on the topic "Phosphorylated tau"
Kamble, Praful Narayan. "Role of TLR3/TLR4 and NF-kB in BAG2 mediated phosphorylated Tau degradation." reponame:Repositório Institucional da UFABC, 2015.
Find full textTese (doutorado) - Universidade Federal do ABC, Programa de Pós-Graduação em Neurociência e Cognição, 2015.
Doenca de Alzheimer (DA) e uma doenca neurodegenerativa progressiva provocada por perda de sinapses e neuronios, caracterizado por disfuncao da memoria e comprometimento cognitivo global. O anormalmente hiperfosforilada, insoluvel, a proteina tau filamentosa mostrou-se ser o componente principal de emaranhados neurofibrilares, uma caracteristica patologica da DA. Neuroinflamacao e o indutor secundario resposta patologica a deposicao de A e morte celular neuronal associada com DA. Pesquisas documentaram o envolvimento de receptores Toll-like (TLRs) na neuroinflamacao, contribuindo para a patogenese da DA. Todos os TLR ativam as vias inflamatorias conservadas, ativando adicionalmente o Fator Nuclear-kB (NF-kB), resultando na libertacao e a producao de citocinas pro-inflamatorias. Entre a familia TLR, varios estudos indicaram o envolvimento de TLR3 e TLR4 contribuindo para neuroinflamacao. Alem disso, um corpo de dados indica o envolvimento de BAG2 na degradacao da tau fosforilada. Neste contexto, foi investigado o papel de TLR3 e TLR4 na modulacao da BAG2 promovida a degradacao de p-Tau em celulas SH-SY5Y. Neste estudo utilizamos LPS e pIpC para ativar TLR4 e TLR3 respectivamente. Linha de celulas SH-SY5Y foi usadae estabelecendo que o Tau induza a formacao de microtubulos sem limites que esta de acordo com a sua funcao como uma proteina associada amicro tubulos em DA. E tambem, utilizaram-se as celulas SH-SY5Y indiferenciadas uma vez que a expressao de BAG2 e inferior e indiferenciada, em comparacao com celulas diferenciadas. Neste estudo, a ativacao de TLR3 com diferentes concentracoes dem pIpC (1, 10, 50 e 100¿Êg/ml) resultou na regulacao negativa significativa de p-Tau em BAG2 expressao excessiva. Por outro lado, a ativacao de TLR4 com diferentes concentracoes de LPS (10, 50 e 100¿Êg/ml) resultaram em diminuicao dependente da dose na BAG2 expressao excessiva. Alem disso, usou-se JSH-23 para a inibicao de NF-kB. JSH-23 a uma concentracao de 25¿ÊM mostraram regulacao negativa significativa em p-Tau independente do BAG2 expressao excessiva e/ou a estimulacao de TLR3 e TLR4. Inibicao de NF-kB com JSH-23 25¿ÊM resultou na supra regulacao de transcricao significativa BAG2 endogena resultando na degradacao de ptau. Em contraste, a inibicao do NF-kB resultou na supra regulacao de HMW p-tau. BAG2 exogeno sobre a estimulacao TLR4 resultou nodecrescimo da regulacao de HMW p-tau. No entanto JSH-23 endogena induzida BAG2 falhou para regular negativamente HMW p-tau. A ativacao de TLR3/TLR4 nao mostrou toxicidade celular, nem a fosforilacao tau nas celulas SHSY5Y. Alem disso, a estimulacao por LPS na presenca/ausencia de sobre expressao BAG2 nao participa na proliferacao celular. No geral, os resultados demonstram a modulacao BAG2 em TLR4 e TLR3 estimulacao e inibicao de NF-kB degradacao em p-Tau e ou HMW p-Tau em DA.
Alzheimer¿s disease (AD) is a neurodegenerative disorder caused by progressive loss of synapses and neurons, characterized by memory dysfunction and global cognitive impairment. The abnormally hyperphosphorylated, insoluble, filamentous tau protein was shown to be the main component of NFTs, a pathological hallmark of AD. Neuroinflammation is the pathological secondary inducer response to deposition of A and neuronal cell death associated with AD. Considerable research has documented the involvement of Toll-like receptors (TLRs) in neuroinflammation, contributing to the pathogenesis of AD. All TLRs activate conserved inflammatory pathways, further activating nuclear factor-kB (NF-kB) resulting in the release and production of pro-inflammatory cytokines. Among the TLRs family, several studies have indicated the involvement of TLR3 and TLR4 contributing to neuroinflammation. Furthermore, a body of data indicates the involvement of BAG2 in phosphorylated Tau degradation. In this context we investigated the role of TLR3 and TLR4 in modulation of BAG2 promoted p-Tau degradation in SH-SY5Y cells. In this study we used LPS and pIpC to activate TLR4 and TLR3 respectively. SH-SY5Y cell line was used since it is established that the Tau induces the formation of microtubule bundles which is in accord with its function as a microtubule-associated protein in AD. And also, we used undifferentiated SH-SY5Y cells since the expression of BAG2 is lower in undifferentiated as compared to differentiated cell. In this study, activation of TLR3 with different concentration of pIpC (1, 10, 50 and 100ìg/mL) resulted in significant downregulation of p-Tau on BAG2 overexpression. On the other hand, activation of TLR4 with different concentration of LPS (10, 50 and 100ìg/mL) resulted in dose dependent decrease on BAG2 overexpression. . Further we used JSH-23 for NF-kB inhibition. JSH-23 at a concentration of 25ìM showed significant downregulation in p-Tau independent of BAG2 overexpression and/or on TLR4 and TLR3 stimulation. NF-kB inhibition with JSH-23 25ìM resulted in significant upregulation of endogenous BAG2 transcript resulting in p-Tau degradation. In contrast, NF-kB inhibition resulted in upregulation of HMW p-Tau. Exogenous BAG2 on TLR4 stimulation resulted in downregulation of HMW p-Tau. However JSH-23 induced endogenous BAG2 failed to downregulate HMW p-Tau. Activation of TLR3/TLR4 neither showed cell toxicity nor Tau phosphorylation in SH-SY5Y cells. Further LPS stimulation in presence/absence of BAG2 overexpression does not participate in cell proliferation. Overall, our findings demonstrate BAG2 modulation on TLR4 and TLR3 stimulation, and NF-kB inhibition in p-Tau and/or HMW p-Tau degradation in AD.
Adhikari, Rajan Deep. "MRI T2 Signal Changes Indicate Tau Pathophysiology in a Murine Alzheimer's Disease Model." BYU ScholarsArchive, 2017. https://scholarsarchive.byu.edu/etd/6944.
Full textAlbaret, Marie Alexandra. "Rôle potentiel du virus herpes simplex de type I dans la maladie d'Alzheimer." Thesis, Lyon 1, 2009. http://www.theses.fr/2009LYO10117.
Full textThe origin of the sporadic form of the Alzheimer's disease (AD) remains still widely unknown. However, an adequacy between environmental and genetic factors is highly probable. Numerous arguments suggest that the virus herpes simplex of type 1 (HSV1) by infecting and replicating in the central nervous system, could be a co-factor involved in the AD process. To evaluate this hypothesis, we set up a model made of rat neurons infected by HSV1 in order to analyse the virally-induced modifications of their gene expression. Using this model we have shown: i) an over-production of the amyloid peptide Aß42 and of phosphorylated form of Tau accompanied by their concentration within an intracellular aggresome; ii) variations of the transcription levels of numerous genes equivalent to that observed in AD patients. Furthermore, the study of the molecular mechanisms underlying the virally-induced apoptosis allowed to point out a correlation between caspase activation and Aß42 production as well as a correlation between abortosis and aggresome formation. All together these results demonstrate that this cellular model represents, at least in part, some aspects of the early stages of AD and bring evidences that HSV1 could be a co-factor in the AD process
Alves, Steven Ribeiro. "The relevence of insulin signalling in Alzheimer's disease." Master's thesis, Universidade de Aveiro, 2017. http://hdl.handle.net/10773/22020.
Full textAlzheimer’s disease (AD) is the most common type of dementia worldwide. It is molecularly characterized by deposition of extracellular senile plaques (SPs) composed by aggregated amyloid beta (Aβ) peptide, the formation of neurofibrillary tangles (NFTs) derived from hyperphosphorylation of the microtubule-associated protein Tau, synaptic dysfunction due to the deposits of SPs and NFTs and oxidative stress induced by impaired metabolic pathways. The insulin signalling pathway can play a major role in diverse AD related pathways, such as APP cleavage, Tau hyperphosphorylation, Apolipoprotein E (ApoE) influence in insulin signalling efficiency and the insulin degrading enzyme, which is also the major Aβ degrading enzyme. Growing evidence links AD with type 2 diabetes (T2D) due to impaired insulin signalling (IS) and brain insulin resistance. In a cohort based study in the Aveiro region, a correlation between diabetes and poor cognitive scores in the Mini Mental State Examination (MMSE) test were observed, with a p-value of 0.072. Additionally, carriers of the allele ApoE-ɛ2 appeared to be protective against diabetes, in the literature the same allele appears to be protective for AD. Posteriorly, the analysis of protein interactions, via the development of interactome networks, identified several proteins involved in both AD and the IS pathways. Also, by correlating these pathways with the synapse proteome, a very high overlap was observed (88% for AD, 79% for IS and 96% for AD and IS coincident proteins), enforcing the importance of both pathways in synaptic signalling and plasticity. From gene ontology studies, it was possible to assess the principal biological processes and molecular functions of the dataset of proteins. For AD, response to stimulus, cellular component organization, cell communication, signalling, protein binding, receptor binding and kinase binding were categories with elevated representation. Regarding coincident proteins between AD and IS pathways, an increase in all categories was observed, meaning that insulin plays a pivotal role in many AD events. Finally, the analysis of SH-SY5Y differentiated cells treated with 0, 1, 10 and 100 nM of insulin for 0, 10 and 60 minutes, showed a decrease on the intracellular total levels of protein Tau and an increase in the phosphorylation at serine 396. Regarding the amyloid precursor protein (APP), increases in intracellular levels were observed, when treated with insulin for 10 minutes, followed by a decrease for 60 minutes exposure. The phosphorylation of APP at threonine 668, has previously been related to increased production of Aβ, by promoting APP cleavage via the amyloidogenic pathway. In cells treated with insulin, a clear increase was detected at the 10-minute time point. At 60 minutes, the levels of phosphorylation were low probably due to low total APP levels.
A doença de Alzheimer (DA) é o tipo mais comum de demência no mundo. É caracterizada molecularmente pela deposição extracelular de placas senis (PS) compostas por agregados do péptido amiloide beta (Aβ), pela formação de emaranhados neurofibrilares (EN) derivados da hiperfosforilação da proteína Tau, pela disfunção sináptica devido aos depósitos de PS e EN e também pelo stress oxidativo induzido pelo enfraquecimento das vias metabólicas. A via de sinalização da insulina desempenha um papel principal em diversas vias da DA, tal como na clivagem da APP, hiperfosforilação da proteína Tau, eficiência da sinalização da insulina influenciada pela Apolipoproteína E (ApoE) e pela enzima envolvida na degradação de insulina que também é a enzima principal na degradação de Aβ. Crescente evidência relaciona a DA com a diabetes de tipo 2 (T2D) devido ao mau funcionamento da sinalização pela insulina e da resistência cerebral à mesma. Num estudo baseado num cohort da região de Aveiro, foi observada uma correlação entre a diabetes e um mau resultado no teste do ‘Mini Mental State Examination’. Adicionalmente, também foi observada uma correlação entre os portadores do alelo ApoE-ɛ2 e um estado protetor contra a T2D. Este alelo também foi observado na literatura como sendo protetor contra a DA. Posteriormente, uma análise de interações entre proteínas, identificou várias proteínas envolvidas tanto na DA como na sinalização da insulina. Correlacionando estes dados com o proteoma da sinapse, foi possível observar que existe uma grande representação das duas condições e também das proteínas coincidentes às duas (88% para a DA, 79% para a sinalização da insulina e 96% para as proteínas relacionadas com ambas), reforçando o papel de ambas as vias na sinalização e plasticidade sináptica. Do estudo de ontologia genética para a DA, foi possível identificar diversas vias importantes, tais como, resposta a um estímulo, organização de componentes celulares, comunicação celular, ligação proteica e ligação a uma cinase. Em relação à sinalização da insulina, as mesmas categorias apareciam com maior representação, significando que a insulina tem um papel importante em muitos eventos da DA. Por fim, o tratamento de SH-SY5Y diferenciadas com 0, 1, 10 e 100 nM de insulina por 0, 10 e 60 minutos mostraram uma diminuição nos níveis intracelulares da proteína Tau e um aumento na sua fosforilação na serina 396. Em relação à proteína percursora amiloide (APP), o tratamento de insulina levou a um aumento nos níveis intracelulares, quando exposta por 10 minutos seguido por uma diminuição aos 60 minutos. Quanto à fosforilação da treonina 668 da APP, foi previamente demonstrado que um aumento na fosforilação desse resíduo, promove a clivagem pela via amiloidogénica, levando à produção de Aβ. Nas células tratadas com insulina, um aumento claro da fosforilação desse resíduo da APP foi observado aos 10 minutos. Aos 60 minutos, os níveis da fosforilação eram baixos provavelmente devido aos baixos níveis de APP total.
McAteer, Kelly Marie. "The role of Substance P in chronic traumatic encephalopathy." Thesis, 2018. http://hdl.handle.net/2440/115184.
Full textThesis (Ph.D.) -- University of Adelaide, Adelaide Medical School, 2018
CHEN, YI-YIN, and 陳怡吟. "Astragaloside IV and nesfatin-1 encapsulated into duel-functional phosphatidylserine liposomes grafted with leptin and wheat germ agglutinin activate anti-apototic pathway to stimulate dopamine production and block expression of phosphorylated tau protein." Thesis, 2019. http://ndltd.ncl.edu.tw/handle/7ncy3m.
Full text國立中正大學
化學工程研究所
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The heap up of α-synuclein (α-syn) and its interaction with tau protein i trigger the onset of PD. The purpose of this study was to develop target specific liposomes incorporated with 1,2-distearoyl-sn-glycero-3-phosphocholine (DSPC), cholesterol (CHOL), 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) and phosphatidy-l-serine (PS). PS with negative charge has high affinity towards α-syn Liposomes were loaded with anti-oxidant drug, astragaloside IV (AS-IV) and the specific inhibitory gene, nestifin-1 (NF-1) followed by surface modification with wheat germ agglutinin (WGA) and leptin (Lep). This study established two in vitro models of 1-methyl-4-phenylpyridinium (MPP+) induced toxic human neuroblastoma SH-SY5Y cells to mimic PD neurodegeneration and human blood-brain barrier (BBB). Experimental results demonstrated that increasing mole percentage of DSPC and PS increased the particles size, stability, entrapment efficiency, and reduced releasing rate of AS-IV and NF-1. Optimal mathematical statistics was established to determine the optimal composition ratio for liposomes to carry out in vitro experiments. In this study, the electrostatic interaction between PS and NF-1 was observed by NMR spectrum. The Western blotting data analysis of the in vitro PD model found that it can effectively increase the specific treatment of α-syn and protein aggregation by the interaction between PS and drugs. PS played a dual role by targeting α-syn and inhibiting the conversion of a β sheet structure into an αhelix structure. In the course of WGA-Lep-AS-IV-NF-1-PS-liposomes treatment, the combined activity of target specific ability from liposomes with drug, and following antioxidant pathway to decrease the expression of α-syn and simultaneously inhibit the expression of phosphor-tau by AS-IV. Moreover, NF-1 was be taken to the pathogen of α-syn accumulation through the electrostatic interaction with PS, and following the gene pathway to reduce the expression of α-syn by specifically inhibiting PTEN-induced kinase 1 (PINK1), and simultaneously inhibit glycogen synthase kinase 3 beta (GSK3β) pathway is effective in reducing the amount of p-tau (S396) expression. The images of immunocytochemistry staining assay evidenced the ability of liposomes specifically target Lep receptor and α-syn and improved the therapeutic efficiency of drugs. The coexistence of α-syn and protein in PD disease was an important mark, in this study, using dual-target liposomes, the aid of PS, and the contribution of drugs between materials interaction each other to achieve more effective treatment of PD.
Bigley, Andrew N. "Investigations on the Mechanism of Allosteric Activtion of Rabbit Muscle Glycogen Phosphorylase b by AMP." Thesis, 2009. http://hdl.handle.net/1969.1/ETD-TAMU-2009-05-483.
Full textBrandenburg, Sören. "Über die differentielle Regulation von Ionenkanälen in spezifischen Nanodomänen atrialer und ventrikulärer Kardiomyozyten." Doctoral thesis, 2017. http://hdl.handle.net/11858/00-1735-0000-0023-3E50-C.
Full textBook chapters on the topic "Phosphorylated tau"
Tanaka, T., H. Yamamori, K. Wada-Isoe, I. Tsujio, and M. Takeda. "Activated Protein Kinases and Phosphorylated Tau Protein in Alzheimer Disease." In Molecular Neurobiology of Alzheimer Disease and Related Disorders, 225–35. Basel: KARGER, 2004. http://dx.doi.org/10.1159/000078542.
Full textHugon, J., P. Sindou, M. Lesort, P. Couratier, F. Esclaire, and C. Yardin. "Modifications of Phosphorylated Tau Immunoreactivity Linked to Excitotoxicity in Neuronal Cultures." In Alzheimer’s Disease: Lessons from Cell Biology, 172–79. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79423-0_14.
Full textBlennow, Kaj, and Henrik Zetterberg. "The Neurochemistry of Alzheimer’s Disease: One of the Most Common Causes of Reduced Capability in the Adult Population." In International Perspectives on Aging, 81–93. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-78063-0_7.
Full textPires, Geoffrey, Beatrix Ueberheide, Thomas Wisniewski, and Eleanor Drummond. "Use of Affinity Purification–Mass Spectrometry to Identify Phosphorylated Tau Interactors in Alzheimer’s Disease." In Methods in Molecular Biology, 263–77. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2655-9_14.
Full textBrion, J. P., A. M. Couck, J. L. Conreur, and J. N. Octave. "A Phosphorylated Tau Species Is Transiently Present in Developing Cortical Neurons and Is Not Associated with Stable Microtubules." In Alzheimer’s Disease: Lessons from Cell Biology, 150–71. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79423-0_13.
Full textHampel, H., S. Teipel, F. Faltraco, S. Brettschneider, A. Goernitz, K. Buerger, and H. J. Moeller. "Advances in the Development of Biomarkers for Alzheimer�s Disease - From CSF Total Tau and Amyloid-β(1-42) Proteins to Phosphorylated Tau and Amyloid-β-Antibodies." In Molecular Neurobiology of Alzheimer Disease and Related Disorders, 134–56. Basel: KARGER, 2004. http://dx.doi.org/10.1159/000078534.
Full textKinoshita, Eiji, Emiko Kinoshita-Kikuta, and Tohru Koike. "Enrichment of Low-Molecular-Weight Phosphorylated Biomolecules Using Phos-Tag Tip." In Neuromethods, 75–84. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9662-9_7.
Full textKinoshita-Kikuta, Emiko, Eiji Kinoshita, and Tohru Koike. "Phos-Tag Fluorescent Gel Staining for the Quantitative Detection of His- and Asp-Phosphorylated Proteins." In Methods in Molecular Biology, 73–78. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1186-9_6.
Full textKomis, George, Tomáš Takáč, Slávka Bekešová, Pavol Vadovič, and Jozef Šamaj. "Affinity-Based SDS PAGE Identification of Phosphorylated Arabidopsis MAPKs and Substrates by Acrylamide Pendant Phos-Tag™." In Methods in Molecular Biology, 47–63. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0922-3_5.
Full textCalderón-Garcidueñas, Lilian, Partha S. Mukherjee, Katharina Waniek, Max Holzer, Chih-kai Chao, Charles Thompson, Rubén Ruiz-Ramos, et al. "Non-Phosphorylated Tau in Cerebrospinal Fluid is a Marker of Alzheimer’s Disease Continuum in Young Urbanites Exposed to Air Pollution." In Advances in Alzheimer’s Disease. IOS Press, 2021. http://dx.doi.org/10.3233/aiad210040.
Full textConference papers on the topic "Phosphorylated tau"
Sturm, Deborah, Alejandra Alonso, Christopher Corbo, Isaac Osores, and Cynthia Murillo. "Quantitative analysis of the effect of phosphorylated tau on cellular microfilament networks." In SPIE Medical Imaging, edited by John B. Weaver and Robert C. Molthen. SPIE, 2013. http://dx.doi.org/10.1117/12.2007056.
Full textMariano, Luciano, Larissa Salvador, Patrícia Peles, Clarisse Friedlaender, Viviane Carvalho, Etelvina dos Santos, Leonardo de Souza, and Paulo Caramelli. "AT(N) MODEL AND ITS ASSOCIATION WITH NEUROPSYCHOLOGICAL MARKERS." In XIII Meeting of Researchers on Alzheimer's Disease and Related Disorders. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1980-5764.rpda019.
Full textChen, Dandan, Jin Li, Hongwei Liu, Lang Ao, and Qiushi Zhang. "Genome-Wide Association and Interaction Study on Quantitative Traits of CSF Phosphorylated Tau in ADNI cohort." In HP3C'22: 2022 6th International Conference on High Performance Compilation, Computing and Communications. New York, NY, USA: ACM, 2022. http://dx.doi.org/10.1145/3546000.3546008.
Full textDu, Xiaoxi, Yosef Koronyo, Chengshuai Yang, Maya Koronyo-Hamaoui, and Liang Gao. "Label-Free Hyperspectral Imaging and Deep-Learning Prediction of Retinal Amyloid β-Protein and Phosphorylated Tau." In 2022 IEEE Photonics Conference (IPC). IEEE, 2022. http://dx.doi.org/10.1109/ipc53466.2022.9975636.
Full textCosta, Larissa Maria de Paula Rebouças da, Gabriel de Souza Torres, Kauan Alves Sousa Madruga, and Poliana Rafaela dos Santos. "Biomarkers in Alzheimer’s disease." In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.670.
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