Each study has a usefulness score out of 100 (rubric version 4.0). Tap a score to see what makes it up.
Highest usefulness score first. Studies without a score come last.
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Since its discovery in 1984, the beta amyloid peptide has treaded the boards of neurosciences as the star molecule in Alzheimer's disease pathogenesis.
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Alzheimer's disease (AD) is a devastating neurodegenerative disorder without a cure.
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A hallmark of Alzheimer's disease (AD) is the aggregation of β-amyloid peptides (Aβ) into amyloid plaques in patient brain.
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Chemical synapses are the predominant neuron-to-neuron contact in the central nervous system.
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In addition to a prominent role in glycemic control, glucagon-like peptide 1 (GLP-1) receptor agonists exhibit neuroprotective properties.
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The pathological assembly of Aβ, tau, and α-synuclein is at the heart of Alzheimer's and Parkinson's diseases.
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Misfolded protein aggregates represent a continuum with overlapping features in neurodegenerative diseases, but differences in protein components and affected brain regions.
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We detected immunoreactivity for all proteins along the optic pathway.
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In Alzheimer's disease (AD), memory impairment is the most prominent feature that afflicts patients and their families.
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Autophagy is a lysosomal degradative process used to recycle obsolete cellular constituents and eliminate damaged organelles and protein aggregates.
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The microtubule-associated protein tau has risk alleles for both Alzheimer's disease and Parkinson's disease and mutations that cause brain degenerative diseases termed tauopathies.
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Most proteins must fold into defined three-dimensional structures to gain functional activity.
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During the past century, treatments for the diseases of youth and middle age have helped raise life expectancy significantly.
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Amyloids are highly organized cross-beta-sheet-rich protein or peptide aggregates that are associated with pathological conditions including Alzheimer's disease and type II diabetes.
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No treatment effect on GSK-3 activity or CSF-based biomarker concentrations (P >. 05) was observed.
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41/100
Mitochondria continuously undergo two opposing processes, fission and fusion.
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Cyclophilin D (CypD, encoded by Ppif) is an integral part of the mitochondrial permeability transition pore, whose opening leads to cell death.
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Recent efforts have revealed that numerous protein-coding messenger RNAs have natural antisense transcript partners, most of which seem to be noncoding RNAs.
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Neurodegenerative diseases of the central nervous system are often associated with impaired learning and memory, eventually leading to dementia.
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Amyloid fibrils formed from different proteins, each associated with a particular disease, contain a common cross-beta spine.
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Although BACE1 (beta-site amyloid precursor protein-cleaving enzyme 1) is essential for the generation of amyloid-b peptide in Alzheimer's disease, its physiological function is unclear.
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Protein aggregation is an established pathogenic mechanism in Alzheimer's disease, but little is known about the initiation of this process in vivo.
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Stress proteins located in the cytosol or endoplasmic reticulum (ER) maintain cell homeostasis and afford tolerance to severe insults.
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Incorrect folding of proteins, leading to aggregation and amyloid formation, is associated with a group of highly debilitating medical conditions including Alzheimer's disease and late-onset diabetes.
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The self-renewing epithelium of the small intestine is ordered into stem/progenitor crypt compartments and differentiated villus compartments.
From across this topic
9 of the 1,352 studies in this topic, picked by a fixed rule (a hash of each study's address), not by score or date; each page of this list shows a different 9. The same 9 appear here every time.
- Gut-induced alpha-Synuclein and Tau propagation initiate Parkinson's and Alzheimer's disease co-pathology and behavior impairments
- Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71
- Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
- Use of Curcumin, a Natural Polyphenol for Targeting Molecular Pathways in Treating Age-Related Neurodegenerative Diseases
- iPSC-Based Compound Screening and In Vitro Trials Identify a Synergistic Anti-amyloid β Combination for Alzheimer's Disease
- Neurodegenerative disease: amyloid pores from pathogenic mutations
- Age-related cognitive deficits, impaired long-term potentiation and reduction in synaptic marker density in mice lacking the beta-amyloid precursor protein
- Multi-omic approach characterises the neuroprotective role of retromer in regulating lysosomal health
- The secreted beta-amyloid precursor protein ectodomain APPs alpha is sufficient to rescue the anatomical, behavioral, and electrophysiological abnormalities of APP-deficient mice