Results 51 to 60 of about 5,915,409 (225)

An Update on Blood-Based Markers of Alzheimer’s Disease Using the SiMoA Platform

Neurology and Therapy, 2019
The development of blood-based biomarkers of Alzheimer’s disease (AD) pathology as tools for screening the general population, and as the first step in a multistep process to determine which non-demented individuals are at greatest risk of developing AD ...
Danni Li, Michelle M. Mielke
doaj   +1 more source

DnaJC7 specifically regulates tau seeding

eLife, 2023
Neurodegenerative tauopathies are caused by accumulation of toxic tau protein assemblies. This appears to involve template-based seeding events, whereby tau monomer changes conformation and is recruited to a growing aggregate.
Valerie Ann Perez, David W Sanders, Ayde Mendoza-Oliva, Barbara Elena Stopschinski, Vishruth Mullapudi, Charles L White, Lukasz A Joachimiak, Marc I Diamond   +7 more
doaj   +1 more source

Phosphorylated tau interactome in the human Alzheimer’s disease brain

Brain : a journal of neurology, 2020
Accumulation of phosphorylated tau (pTau) is a key pathological feature of Alzheimer’s disease (AD). pTau accumulation causes synaptic impairment, neuronal dysfunction and formation of neurofibrillary tangles (NFTs).
Eleanor Drummond, Geoffrey Pires, Claire MacMurray, M. Askenazi, Shruti D Nayak, M. Bourdon, J. Safar, B. Ueberheide, T. Wisniewski   +8 more
semanticscholar   +1 more source

Transgenic Zebrafish as a Novel Animal Model to Study Tauopathies and Other Neurodegenerative Disorders in vivo [PDF]

, 2010
Our ageing society is confronted with a dramatic increase in patients suffering from tauopathies such as Alzheimer's disease, frontotemporal dementia and others.
Haass, Christian, Paquet, Dominik, Schmid, Bettina   +2 more
core   +1 more source

Differences Between Human and Murine Tau at the N-terminal End

Frontiers in Aging Neuroscience, 2020
Human tauopathies, such as Alzheimer’s disease (AD), have been widely studied in transgenic mice overexpressing human tau in the brain. The longest brain isoforms of Tau in mice and humans show 89% amino acid identity; however, the expression of the ...
Félix Hernández, Félix Hernández, Jesús Merchán-Rubira, Laura Vallés-Saiz, Alberto Rodríguez-Matellán, Jesús Avila, Jesús Avila   +6 more
doaj   +1 more source

MAPping out distribution routes for kinesin couriers [PDF]

, 2013
In the crowded environment of eukaryotic cells, diffusion is an inefficient distribution mechanism for cellular components. Long-distance active transport is required and is performed by molecular motors including kinesins.
*Ackmann, Adams, Akhmanova, Akhmanova, Akiyama, Al-Bassam, Amadoro, Amos, Audebert, Baas, Baas, Bai, Bananis, Barlan, Bechstedt, Bieling, Binder, Black, Bobinnec, Bonnet, Boucher, Bouquet, Boyne, Bulinski, Bulinski, Burbridge, Burgess, Byrd, Cai, Charalambous, Chu, Cierpicki, Congdon, Cook, Corbo, De Vos, des Portes, des Portes, Desai, Deshpande, Deuel, Dijkmans, Dimitrov, DiTella, Dixit, Douglas, Drewes, Drewes, Duan, Dubey, Duff, Dunn, Eastwood, Ebneth, Erck, Faire, Fourniol, Francis, Friocourt, Fu, Fukushima, Fung, Galaburda, Garnham, Gleeson, Gleeson, Goldstein, Guillaud, Gurland, Hagiwara, Hammond, Hanger, Hanlon, Harada, Hardy, Heins, Hepp, Hidaka, Hirokawa, Hirokawa, Hoang, Horesh, Horiguchi, Huang, Hyman, Iijima, Ikegami, Ikegami, Iqbal, Iqbal, Ittner, Jacobson, Janke, Jenkins, Jimenez-Mateos, Ju, Kamal, Kanaan, Kanai, Kappeler, Kar, Kaslow, Kawaguchi, Kayadjanian, Khatoon, Khawaja, Kim, Klebe, Koizumi, Kondo, Konishi, Kosik, Kowall, Kreitzer, Kueh, LaPointe, Larcher, Larkin, Lawrence, Lazarov, Lee, Leger, Lewis, Liao, Lin, Liu, Liu, Liu, Liu, Lopez, Maas, Makrides, Mandelkow, Mandelkow, Mandell, Marcos, Marszalek, Massinen, Massow, Maurer, McVicker, Meng, Metzger, Miki, Miki, Mok, Moores, Moores, Morfini, Muresan, Nadar, Nakata, Nakata, Nakata, Navone, Nguyen, Nishimura, Noda, Noda, Nogales, Nosten-Bertrand, Omori, Pagon, Palazzo, Paturle-Lafanechere, Peck, Perez, Peterman, Pettersen, Pfenninger, Pfister, Polydoro, Reed, Reifert, Reiner, Saito, Santarella, Sapir, Saragoni, Schaar, Seidel, Seitz, Setou, Setou, Sharp, Shirasu, Silverman, Sindelar, Small, Song, Soppina, Sossey-Alaoui, Spiliotis, Spronsen, Stamer, Stokin, Stoothoff, Sung, Takei, Takemura, Tapia, Taylor, Teng, Terwel, Thinakaran, Thorn, Tien, Tilney, Tint, Tischfield, Trinczek, Tsai, Uchida, Utton, Vale, Vale, Verhey, Verhey, Vershinin, Vreugdenhil, Wade, Wagner, Walter, Wordeman, Xu, Yajima, Yamazaki, Yang, Yang, Ye, Yonekawa, Yoshimura, Yu, Yuan, Zempel, Zhang   +235 more
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Revisiting protein aggregation as pathogenic in sporadic Parkinson and Alzheimer diseases. [PDF]

, 2019
The gold standard for a definitive diagnosis of Parkinson disease (PD) is the pathologic finding of aggregated α-synuclein into Lewy bodies and for Alzheimer disease (AD) aggregated amyloid into plaques and hyperphosphorylated tau into tangles.
Brundin, P, Cambi, F, Espay, AJ, Fasano, A, Fernandez, HH, Gan-Or, Z, Greenamyre, JT, Josephs, KA, Kauffman, MA, Lang, AE, Leverenz, JB, Litvan, I, Marsili, L, Mata, IF, Merola, A, Morgante, F, Perry, G, Sardi, SP, Savica, R, Schwarzschild, MA, Sherer, T, Simon, DK, Standaert, DG, Tanner, CM, Vizcarra, JA, Yamasaki, TR, Zabetian, CP   +26 more
core   +3 more sources

Differential effects of an O-GlcNAcase inhibitor on tau phosphorylation. [PDF]

PLoS ONE, 2012
Abnormal hyperphosphorylation of microtubule-associated protein tau plays a crucial role in neurodegeneration in Alzheimer's disease (AD). The aggregation of hyperphosphorylated tau into neurofibrillary tangles is also a hallmark brain lesion of AD.
Yang Yu, Lan Zhang, Xiaojing Li, Xiaoqin Run, Zhihou Liang, Yi Li, Ying Liu, Moon H Lee, Inge Grundke-Iqbal, Khalid Iqbal, David J Vocadlo, Fei Liu, Cheng-Xin Gong   +12 more
doaj   +1 more source

The Ca2+ sensor protein Swiprosin-1/EFhd2 is present in neurites and involved in kinesin-mediated transport in neurons [PDF]

, 2014
This work was supported by grants from the German Science Foundation (Deutsche Forschungsgemeinschaft, DFG; FOR832, to DM), the German Federal Ministry of Education and Research (01GQ113; to BW), the Bavarian Ministry of Sciences, Research and the Arts ...
Bohm, KJ, Borger, Eva, Brachs, S, Buslei, R, Fritsch, K, Gromer, TW, Gunn-Moore, Frank J, Holzer, M, Loy, K, Mielenz, D, Perez-Branguli , F, Prots, I, Purohit, P, Regensburger, M, Welzel, O, Wenzel, EM, Winner, B   +16 more
core   +3 more sources

SUMO1 modification of 0N4R-tau is regulated by PIASx, SENP1, SENP2, and TRIM11

Biochemistry and Biophysics Reports
Tau is a microtubule-associated protein that contributes to cytoskeletal stabilization. Aggregation of tau proteins is associated with neurodegenerative disorders such as Alzheimer's disease.
Harmony Wada, Takuma Maruyama, Takako Niikura   +2 more
doaj   +1 more source