Structural Predictive Model of Presenilin-2 Protein and Analysis of Structural Effects of Familial Alzheimer’s Disease Mutations by Alejandro Soto-Ospina, Pedronel Araque Marín, Gabriel de Jesús Bedoya, Andrés Villegas Lanau

“…Alzheimer’s disease manifests itself in brain tissue by neuronal death, due to aggregation of β-amyloid, produced by senile plaques, and hyperphosphorylation of the tau protein, which produces neurofibrillary tangles. …”
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Second-generation anti-amyloid monoclonal antibodies for Alzheimer’s disease: current landscape and future perspectives by Byeong-Hyeon Kim, Sujin Kim, Yunkwon Nam, Yong Ho Park, Seong Min Shin, Minho Moon

“…Monoclonal antibodies (MABs) serve as a promising therapeutic approach for AD by selectively targeting key pathogenic factors, such as amyloid-β (Aβ) peptide, tau protein, and neuroinflammation. Specifically, based on their efficacy in removing Aβ plaques from the brains of patients with AD, the U.S. …”
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Visual Features in Alzheimer’s Disease: From Basic Mechanisms to Clinical Overview by María Alejandra Cerquera-Jaramillo, Mauricio O. Nava-Mesa, Rodrigo E. González-Reyes, Carlos Tellez-Conti, Alejandra de-la-Torre

“…AD is characterized by brain atrophy due to neuronal and synaptic loss, extracellular amyloid plaques composed of amyloid-beta peptide (Aβ), and neurofibrillary tangles of hyperphosphorylated tau protein. The visual system and central nervous system share many functional components. …”
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Molecular Mechanisms of Alzheimer’s Disease Induced by Amyloid-β and Tau Phosphorylation Along with RhoA Activity: Perspective of RhoA/Rho-Associated Protein Kinase Inhibitors for... by Eun Hee Ahn, Jae-Bong Park

“…It is generated from amyloid precursor protein (APP) through cleavages by β-secretase and γ-secretase. γ-Secretase, which includes presenilin, is regulated by several stimuli. Tau protein has also been identified as a significant factor in AD. …”
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The Emerging Roles of the Calcineurin-Nuclear Factor of Activated T-Lymphocytes Pathway in Nervous System Functions and Diseases by Maulilio John Kipanyula, Wahabu Hamisi Kimaro, Paul F. Seke Etet

“…Neurotoxins such as amyloid-β, tau protein, and α-synuclein trigger abnormal calcineurin/NFAT signaling activities. …”
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Cilostazol Combats Lipopolysaccharide-Induced Hippocampal Injury in Rats: Role of AKT/GSK3β/CREB Curbing Neuroinflammation by Doaa Abou El-ezz, Waleed Aldahmash, Tuba Esatbeyoglu, Sherif M. Afifi, Marawan Abd Elbaset

“…Furthermore, cilostazol therapy lowered hippocampal levels of amyloid beta 1–42 (Aβ1-42) and p-tau protein, both of which are critical pathological indicators of neurodegenerative disorders. …”
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Brain-derived tau oligomer polymorphs: distinct aggregations, stability profiles, and biological activities by Filippa Lo Cascio, Suhyeorn Park, Urmi Sengupta, Nicha Puangmalai, Nemil Bhatt, Nikita Shchankin, Cynthia Jerez, Naomi Moreno, Alice Bittar, Rhea Xavier, Yingxin Zhao, Cankun Wang, Hongjun Fu, Qin Ma, Mauro Montalbano, Rakez Kayed

“…Abstract Aggregation of microtubule-associated tau protein is a distinct hallmark of several neurodegenerative disorders such as Alzheimer’s disease (AD), dementia with Lewy bodies (DLB), and progressive supranuclear palsy (PSP). …”
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Effectiveness of Contrast Agents and Molecular Indicators in Alzheimer's Diagnosis Through PET and SPECT Imaging on Animal Models by Yasaman Abaszadeh, Ramin Ardalani, Athena Dehghan Najm Abadi

“…Respectively, Amyloid beta, Tau protein, Translocator protein (TSPO), Acetylcholinesterase (AChE), Monoamine oxidase B (MAO-B), and Gonadotropin-releasing hormone receptor (GnRHR) were identified the most as biomarkers in studies. …”
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Changes in the transcriptome of the prefrontal cortex of OXYS rats as the signs of Alzheimer’s disease development by N. A. Stefanova, E. E. Korbolina, N. I. Ershov, E. I. Rogaev, N. G. Kolosova

“…Recently, we showed that senescence-accelerated OXYS rats represent a promis­ing model of AD; in these rats, accelerated aging of the brain is accompanied by the typical signs of AD: degenerative alterations and death of neurons, a de­crease in synaptic density, mitochondrial dysfunction, hyperphosphorylation of the tau protein, an increased level of amyloid β (Aβ1–42), and the formation of amyloid plaques. …”
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Assessment of the Impact of Different Types and Intensities of Physical Exercise on the Quality of Life of Patients with Alzheimer’s Disease: A Literature Review by Katarzyna Barabasz, Paulina Więcławek, Piotr Juda, Patrycja Kłaptocz, Katarzyna Łukoś-Karcz, Dominik Bańkowski, Gabriela Pabian, Karol Musiał, Kamil Bielak

“…Methods Studies from PubMed, Scopus, Cochrane Library, and Web of Science (2000–2024) were analyzed, focusing on the effects of aerobic, resistance, and combined exercises on memory, executive functions, biomarkers (amyloid beta, tau protein, BDNF), daily living abilities (ADL), and quality of life. …”
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RIPK1 expression and inhibition in tauopathies: implications for neuroinflammation and neuroprotection by Ignacio Silva-Llanes, Ignacio Silva-Llanes, Ignacio Silva-Llanes, Enrique Madruga, Enrique Madruga, Ana Martínez, Ana Martínez, Isabel Lastres-Becker, Isabel Lastres-Becker, Isabel Lastres-Becker, Isabel Lastres-Becker

“…Tauopathies are a group of neurodegenerative diseases characterized by the alteration/aggregation of TAU protein. One of the main challenges of these diseases is that they have neither biomarkers nor pharmacological targets to stop the neurodegenerative process. …”
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Neurofilament Light Chain Levels in Serum and Cerebrospinal Fluid Do Not Correlate with Survival Times in Patients with Prion Disease by Mika Shimamura, Kong Weijie, Toshiaki Nonaka, Koki Kosami, Ryusuke Ae, Koji Fujita, Taiki Matsubayashi, Tadashi Tsukamoto, Nobuo Sanjo, Katsuya Satoh

“…In this study, we employed a fully automated multiplex ELISA (Ella^®) to measure the concentrations of 14-3-3 protein, total tau protein, and neurofilament light chain (NF-L) in cerebrospinal fluid (CSF) and serum samples from patients with prion disease and analyzed their link to disease prognosis. …”
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The Evaluation of Tau Deposition with [18F]PI-2620 by Using a Semiquantitative Method in Cognitively Normal Subjects and Patients with Mild Cognitive Impairment and Alzheimer’s Dis... by Attapon Jantarato, Sira Vachatimanont, Natphimol Boonkawin, Sukanya Yaset, Anchisa Kunawudhi, Chetsadaporn Promteangtrong, Jintana Assanasen, Nithi Mahanonda, Chanisa Chotipanich

“…A significantly higher mean SUVr of [18F]PI-2620 was observed in the AD group; a significant area of the brain in the AD group demonstrated tau protein deposit in concordance with Braak Stages III–V, providing useful information to differentiate AD from CN and MCI. …”
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Metabolism: A Novel Shared Link between Diabetes Mellitus and Alzheimer’s Disease by Yanan Sun, Cao Ma, Hui Sun, Huan Wang, Wei Peng, Zibo Zhou, Hongwei Wang, Chenchen Pi, Yingai Shi, Xu He

“…Protein changes in the unfolded protein response or endoplasmic reticulum stress can regulate Aβ production and are closely associated with tau protein pathology. Altogether, metabolic disorders including glucose/lipid metabolism, oxidative stress, mitochondrial dysfunction, and protein changes caused by DM are associated with an impaired insulin signal pathway. …”
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Blockade of NR2A-Containing NMDA Receptors Induces Tau Phosphorylation in Rat Hippocampal Slices by Julie Allyson, Eve Dontigny, Yves Auberson, Michel Cyr, Guy Massicotte

“…In the present study, we used selective NMDA receptor antagonists to investigate the involvement of NR2A and NR2B subunits in the modulatory effect of basal NMDA receptor activity on the phosphorylation of Tau proteins. We observed, in acute hippocampal slice preparations, that blockade of NR2A-containing NMDA receptors by the NR2A antagonist NVP-AAM077 provoked the hyperphosphorylation of a residue located in the proline-rich domain of Tau (i.e., Ser199). …”
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Electroacupuncture Improves Cognitive Function in Senescence-Accelerated P8 (SAMP8) Mice via the NLRP3/Caspase-1 Pathway by Zhitao Hou, Ruijin Qiu, Qingshuang Wei, Yitian Liu, Meng Wang, Tingting Mei, Yue Zhang, Liying Song, Xianming Shao, Hongcai Shang, Jing Chen, Zhongren Sun

“…Hippocampal NLRP3, ASC, caspase-1, GSDM-D, IL-1β, IL-18, Aβ, and tau proteins were detected by Western blotting. Key Findings. …”
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The Science of Memory Loss: Insights into Alzheimer’s Disease by Agnieszka Starzyk, Piotr Charzewski

“…Emerging therapies, such as monoclonal antibodies targeting amyloid-beta and tau proteins, show promise but are hindered by challenges in efficacy and safety. …”
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Exposure to nano-polystyrene during pregnancy leads to Alzheimer's disease-related pathological changes in adult offspring by Fengxu Wang, Jin Wang, Na Luo, Yonghua Luo, Zhengnan Gao, Ye Cui, Mengna Jiang, Zhaoping Shen, Jing Xiao, Peng Xue, Xiaoke Wang, Shali Yu, Qiyun Wu, Xinyuan Zhao

“…Furthermore, the phosphorylation levels of tau proteins at ser396 and ser199 were dramatically enhanced in the PS-NPs exposed group. …”
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Developing non-invasive molecular markers for early risk assessment of Alzheimer's disease by Tapas K. Sur, Tanmoy Mondal, Zarish Noreen, Jheannelle Johnson, Gail Nunlee-Bland, Christopher A. Loffredo, Brent E. Korba, Vijay Chandra, Siddhartha S. Jana, Bernard Kwabi-Addo, Sumit Sarkar, Somiranjan Ghosh

“…Current improvements have unveiled the disease's pathophysiology and clinical diagnostic tests, targeting the neurological changes (neurodegeneration, amyloid precursor protein metabolism and tangle pathology) with precise PET/MRI imaging and xMAP/SIMOA (Multiplex simultaneous detection/single molecule array) to identify and quantify β-amyloids (Aβ40, Aβ42), total tau (T-tau) and phosphorylated tau (P-tau) proteins in the brain and cerebrospinal fluid (CSF) of patients. …”
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Upregulated astrocyte HDAC7 induces Alzheimer-like tau pathologies via deacetylating transcription factor-EB and inhibiting lysosome biogenesis by Jinwang Ye, Suyue Zhong, Huali Wan, Xing Guo, Xuanbao Yao, Qiong Liu, Liming Chen, Jian-Zhi Wang, Shifeng Xiao

“…HDAC7 could modulate astrocytic uptake and lysosomal degradation of tau proteins through a transcriptional factor EB (TFEB) acetylation-dependent manner. …”
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