Results 21 to 30 of about 5,828,623 (322)

Interaction between Aβ and Tau in the Pathogenesis of Alzheimer's Disease

International Journal on Biological Sciences, 2021
Extracellular neuritic plaques composed of amyloid‑β (Aβ) protein and intracellular neurofibrillary tangles containing phosphorylated tau protein are the two hallmark proteins of Alzheimer's disease (AD), and the separate neurotoxicity of these proteins ...
Huiqin Zhang, Wei Wei, Ming Zhao, Lina Ma, Xuefan Jiang, Hui Pei, Yu Cao, Hao Li   +7 more
semanticscholar   +1 more source

Predicting AT(N) pathologies in Alzheimer’s disease from blood-based proteomic data using neural networks

Frontiers in Aging Neuroscience, 2022
Background and objectiveBlood-based biomarkers represent a promising approach to help identify early Alzheimer’s disease (AD). Previous research has applied traditional machine learning (ML) to analyze plasma omics data and search for potential ...
Yuting Zhang, Upamanyu Ghose, Noel J. Buckley, Sebastiaan Engelborghs, Sebastiaan Engelborghs, Sebastiaan Engelborghs, Kristel Sleegers, Kristel Sleegers, Giovanni B. Frisoni, Anders Wallin, Alberto Lleó, Julius Popp, Julius Popp, Pablo Martinez-Lage, Cristina Legido-Quigley, Cristina Legido-Quigley, Frederik Barkhof, Frederik Barkhof, Henrik Zetterberg, Henrik Zetterberg, Henrik Zetterberg, Henrik Zetterberg, Henrik Zetterberg, Pieter Jelle Visser, Pieter Jelle Visser, Lars Bertram, Lars Bertram, Simon Lovestone, Simon Lovestone, Alejo J. Nevado-Holgado, Liu Shi   +30 more
doaj   +1 more source

Mapping interactions with the chaperone network reveals factors that protect against tau aggregation. [PDF]

, 2018
A network of molecular chaperones is known to bind proteins ('clients') and balance their folding, function and turnover. However, it is often unclear which chaperones are critical for selective recognition of individual clients. It is also not clear why
A Rodina, AD Thompson, AD Thompson, AL Hsu, AM Pooler, Anne Gillies, B Combs, B Ghetti, BM Dunyak, Bryan M. Dunyak, C Cauwenberghe Van, C Soto, CA Dickey, Carlo Condello, CG Gunawardana, Chad A. Dickey, CL Moore, CP Winsor, CW Lennon, DM Walther, DW Sanders, E Cohen, E Kirschke, F Clavaguera, Francis T. F. Tsai, G Cheng, G Coppola, GE Karagöz, H Mirbaha, H Shinohara, H Sugata, Harindranath Kadavath, J Hansen, J Lee, J Lim, Jason E. Gestwicki, Javier Oroz, JC Augustinack, Jennifer N. Rauch, JF Abisambra, JJ Yerbury, JL Howarth, JN Rauch, JN Rauch, JR Glover, Jungsoon Lee, JZ Wang, K Nakamura, K Voss, KA Verba, KL Gendreau, L Chang, LN Makley, M Arimon, M Bergen von, M Bergen von, M Brehme, M Niblock, M Taipale, Mark R. Wilson, Markus Zweckstetter, MD Mukrasch, MG Spillantini, MR Wilson, N Kfoury, Olivier Julien, P Arosio, P Arosio, R Development Core Team., RA Rissman, Rebecca Freilich, RI Morimoto, S Barghorn, S Krobitsch, S Quan, SB Prusiner, SN Fontaine, Sue-Ann Mok, SW Min, T Ikura, Taylor Arhar, TJ Cohen, TW Mu, UK Jinwal, UK Jinwal, UK Jinwal, V Corsetti, V Kakkar, VA Assimon, Victoria A. Assimon, W Li, X Gao, Y Morishima, YE Kim, ZT Young, ZT Young   +95 more
core   +3 more sources

Expression of Tau Pathology-Related Proteins in Different Brain Regions: A Molecular Basis of Tau Pathogenesis

Frontiers in Aging Neuroscience, 2017
Microtubule-associated protein tau is hyperphosphorylated and aggregated in affected neurons in Alzheimer disease (AD) brains. The tau pathology starts from the entorhinal cortex (EC), spreads to the hippocampus and frontal and temporal cortices, and ...
Wen Hu, Wen Hu, Feng Wu, Yanchong Zhang, Yanchong Zhang, Cheng-Xin Gong, Khalid Iqbal, Fei Liu, Fei Liu   +8 more
doaj   +1 more source

EFhd2 Affects Tau Liquid–Liquid Phase Separation

Frontiers in Neuroscience, 2019
The transition of tau proteins from its soluble physiological conformation to the pathological aggregate forms found in Alzheimer’s disease and related dementias, is poorly understood.
Irving E. Vega, Irving E. Vega, Irving E. Vega, Andrew Umstead, Nicholas M. Kanaan, Nicholas M. Kanaan, Nicholas M. Kanaan   +6 more
doaj   +1 more source

Controlled cortical impact traumatic brain injury in 3xTg-AD mice causes acute intra-axonal amyloid-β accumulation and independently accelerates the development of tau abnormalities [PDF]

, 2011
Alzheimer\u27s disease (AD) is a neurodegenerative disorder characterized pathologically by progressive neuronal loss, extracellular plaques containing the amyloid-β (Aβ) peptides, and neurofibrillary tangles composed of hyperphosphorylated tau proteins.
Brody, David L, Holtzman, David M, LaFerla, Frank M, Tran, Hien T   +3 more
core   +2 more sources

Fibril-forming motifs are essential and sufficient for the fibrillization of human Tau. [PDF]

PLoS ONE, 2012
BACKGROUND: The misfolding of amyloidogenic proteins including human Tau protein, human prion protein, and human α-synuclein is involved in neurodegenerative diseases such as Alzheimer disease, prion disease, and Parkinson disease.
Sheng-Rong Meng, Ying-Zhu Zhu, Tong Guo, Xiao-Ling Liu, Jie Chen, Yi Liang   +5 more
doaj   +1 more source

Blood-based immunoassay of tau proteins for early diagnosis of Alzheimer's disease using surface plasmon resonance fiber sensors

RSC Advances, 2018
We present the immunoassay of tau proteins (total tau and phosphorylated tau) in human sera using surface plasmon resonance (SPR) fiber sensors. This assay aimed at harvesting the advantages of using both SPR fiber sensors and a blood-based assay to ...
Truong Thi Vu Nu, Nhu Hoa Thi Tran, Eunjoo Nam, T. Nguyen, Won Jung Yoon, Sungbo Cho, Jungsuk Kim, Keun-A Chang, H. Ju   +8 more
semanticscholar   +1 more source

The Molecular Chaperone Artemin Efficiently Blocks Fibrillization of TAU Protein In Vitro

Cell Journal, 2017
Objective: Aggregation of the TAU proteins in the form of neurofibrillary tangles (NFTs) in the brain is a common risk factor in tauopathies including Alzheimer’s disease (AD).
Zahra Khosravi, Mohammad Ali Nasiri Khalili, Sharif Moradi, Reza Hassan Sajedi, Mehdi Zeinoddini   +4 more
doaj   +1 more source

Quantitative flow cytometric selection of tau conformational nanobodies specific for pathological aggregates

Frontiers in Immunology, 2023
Single-domain antibodies, also known as nanobodies, are broadly important for studying the structure and conformational states of several classes of proteins, including membrane proteins, enzymes, and amyloidogenic proteins.
Jennifer M. Zupancic, Jennifer M. Zupancic, Matthew D. Smith, Matthew D. Smith, Hanna Trzeciakiewicz, Mary E. Skinner, Sean P. Ferris, Emily K. Makowski, Emily K. Makowski, Michael J. Lucas, Michael J. Lucas, Michael J. Lucas, Nikki McArthur, Ravi S. Kane, Henry L. Paulson, Henry L. Paulson, Henry L. Paulson, Peter M. Tessier, Peter M. Tessier, Peter M. Tessier, Peter M. Tessier, Peter M. Tessier, Peter M. Tessier   +22 more
doaj   +1 more source