Results 81 to 90 of about 45,801 (303)

A Physiological Role for Amyloid Beta Protein: Enhancement of Learning and Memory [PDF]

, 2008
Amyloid beta protein (A[beta]) is well recognized as having a significant role in the pathogenesis of Alzheimer's disease (AD). The reason for the presence of A[beta] and its physiological role in non-disease states is not clear.
John Morley, Kelvin A. Yamada, Lin Xu, Steven N. Johnson, Susan Farr, William Banks   +5 more
core   +1 more source

Hypoxic regulation of ion channel function and expression [PDF]

, 2002
Acute hypoxia regulates the activity of specific ion channels in a rapid and reversible manner. Such effects underlie appropriate cellular responses to hypoxia which are designed to initiate cardiorespiratory reflexes and contribute importantly to other ...
Peers, C.
core   +1 more source

Amyloid β Instigates Cardiac Neurotrophic Signaling Impairment, Driving Alzheimer's Associated Heart Disease

Advanced Science, EarlyView.
This research identified cardiac amyloid pathology, neurotrophic factor depletion, and reduced myocardial nerve function in a transgenic model of cerebral amyloidosis (Tg2576), Aβ‐challenged cardiomyocytes, and in human AD heart tissue. These findings carry significant diagnostic and therapeutic implications, emphasizing the role of neuro‐signaling ...
Andrea Elia, Rebecca Parodi‐Rullan, Rafael Vazquez‐Torres, Ashley Carey, Huaqing Zhao, Sabzali Javadov, Silvia Fossati   +6 more
wiley   +1 more source

The role of astrocytes in Alzheimer's disease, A systematic review

Journal of Current Oncology and Medical Sciences, 2023
Introduction: Alzheimer's disease (AD), the most common neurodegenerative disease in the world, appears in two forms, early and late. Pathologically, an amyloid beta peptide is the hallmark of this disease which is followed by synaptic dysfunction, brain
Seyyed Mohammad Taghi Razavi-Toosi, Parvin Babaei, Arefeh Salehi   +2 more
doaj  

Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spine. [PDF]

PLoS Computational Biology, 2009
At the core of amyloid fibrils is the cross-beta spine, a long tape of beta-sheets formed by the constituent proteins. Recent high-resolution x-ray studies show that the unit of this filamentous structure is a beta-sheet bilayer with side chains within ...
Jiyong Park, Byungnam Kahng, Wonmuk Hwang   +2 more
doaj   +1 more source

APOE‐stratified Proteomic and Metabolomic Analysis Reveals Mitochondrial Dysfunction Inflammation and Lipid Dysregulation in Alzheimer's Disease

Advanced Science, EarlyView.
A large‐scale multiomic dataset (proteomic and metabolomic) comprising 3,060 plasma samples were analyzed to identify proteins, metabolites, pathways, and protein‐associated drugs linked to Alzheimer’s Disease (AD) independently of apolipoprotein E (APOE). AD was associated with a distinct molecular signature that captures.
Fuhai Li, Yike Chen, Daniel Western, Muhammad Ali, Menghan Liu, Katherine Gong, Ying Xu, Joseph Lowery, David M. Holtzman, Chloe Robins, John D. Eicher, Yen‐Ning Huang, ShiWei Liu, Tamina Park, Andrew J. Saykin, Kwangsik Nho, Mahdi Moqri, Richard C. Mohs, Amelia Farinas, Patricia Moran‐Losada, Hamilton Se‐Hwee Oh, Tony Wyss‐Coray, Carlos Cruchaga   +22 more
wiley   +1 more source

Interaction of amyloid inhibitor proteins with amyloid beta peptides: insight from molecular dynamics simulations.

PLoS ONE, 2014
Knowledge of the detailed mechanism by which proteins such as human αB- crystallin and human lysozyme inhibit amyloid beta (Aβ) peptide aggregation is crucial for designing treatment for Alzheimer's disease.
Payel Das, Seung-gu Kang, Sally Temple, Georges Belfort   +3 more
doaj   +1 more source

Structure of amyloid-β (20-34) with Alzheimer's-associated isomerization at Asp23 reveals a distinct protofilament interface. [PDF]

, 2019
Amyloid-β (Aβ) harbors numerous posttranslational modifications (PTMs) that may affect Alzheimer's disease (AD) pathogenesis. Here we present the 1.1 Å resolution MicroED structure of an Aβ 20-34 fibril with and without the disease-associated PTM, L ...
Boyer, David R, Cascio, Duilio, Clarke, Steven G, Eisenberg, David S, Gonen, Tamir, Richards, Logan S, Sawaya, Michael R, Warmack, Rebeccah A, Zee, Chih-Te   +8 more
core  

The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process. [PDF]

, 2004
Formation of misfolded aggregates is an essential part of what proteins can do. The process of protein aggregation is central to many human diseases and any aggregating event needs to be prevented within a cell and in protein design.
AMORESANO, ANGELA, B. L. GAROLLA DI BARD, F. CHITI, G. CALLONI, G. RAMPONI, MONTI, MARIA, PUCCI, PIETRO   +6 more
core   +1 more source

Autophagy Activators Normalize Aberrant Tau Proteostasis and Rescue Synapses in Human Familial Alzheimer's Disease iPSC‐Derived Cortical Organoids

Advanced Science, EarlyView.
A new cerebrocortical organoid model using isogenic hiPSCs with familial Alzheimer's mutations recapitulates key AD features, including amyloid‐beta and phospho‐Tau aggregation, neuronal hyperexcitability, and synapse loss. Single‐cell RNA‐seq reveals aberrant pathways in excitatory and inhibitory neurons.
Sergio R. Labra, Jadon Compher, Akhil Prabhavalkar, Mireya Almaraz, Claudia Cedeño Kwong, Christine Baal, Maria Talantova, Nima Dolatabadi, Julian Piña‐Sanz, Yubo Wang, Leonard Yoon, Swagata Ghatak, Zi Gao, Yuting Zhang, Dorit Trudler, Lynee Massey, Wei Lin, Anthony Balistreri, Michael Bula, Nicholas J. Schork, Tony S. Mondala, Steven R. Head, Jeffery W. Kelly, Stuart A. Lipton   +23 more
wiley   +1 more source