Found: 30
Select item for more details and to access through your institution.
Neuronal Differentiation of Human Mesenchymal Stromal Cells Increases their Resistance to Aβ<sub>42</sub> Aggregate Toxicity.
- Published in:
- Journal of Alzheimer's Disease, 2011, v. 27, n. 3, p. 651, doi. 10.3233/JAD-2011-110590
- By:
- Publication type:
- Article
Single domain antibodies as promising tools for the selective detection and neutralization of neurotoxic Aβ<sub>42</sub> oligomers in the cerebrospinal fluid of Alzheimer's disease patients.
- Published in:
- Alzheimer's & Dementia: The Journal of the Alzheimer's Association, 2023, v. 19, n. 21, p. 1, doi. 10.1002/alz.076650
- By:
- Publication type:
- Article
Single domain antibodies as new detectors of neurotoxic Aβ<sub>42</sub> oligomers.
- Published in:
- Alzheimer's & Dementia: The Journal of the Alzheimer's Association, 2023, v. 19, p. 1, doi. 10.1002/alz.065735
- By:
- Publication type:
- Article
The Toxicity of Protein Aggregates: New Insights into the Mechanisms.
- Published in:
- 2023
- By:
- Publication type:
- Editorial
Calcium Dyshomeostasis in Alzheimer's Disease Pathogenesis.
- Published in:
- International Journal of Molecular Sciences, 2021, v. 22, n. 9, p. 4914, doi. 10.3390/ijms22094914
- By:
- Publication type:
- Article
Partial Failure of Proteostasis Systems Counteracting TDP-43 Aggregates in Neurodegenerative Diseases.
- Published in:
- International Journal of Molecular Sciences, 2019, v. 20, n. 15, p. 3685, doi. 10.3390/ijms20153685
- By:
- Publication type:
- Article
Exploring the Release of Toxic Oligomers from α-Synuclein Fibrils with Antibodies and STED Microscopy.
- Published in:
- Life (2075-1729), 2021, v. 11, n. 5, p. 431, doi. 10.3390/life11050431
- By:
- Publication type:
- Article
The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells.
- Published in:
- Nature Communications, 2021, v. 12, n. 1, p. 1, doi. 10.1038/s41467-021-21937-3
- By:
- Publication type:
- Article
Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases.
- Published in:
- Scientific Reports, 2016, p. 32721, doi. 10.1038/srep32721
- By:
- Publication type:
- Article
TDP-43 Inclusion Bodies Formed in Bacteria Are Structurally Amorphous, Non-Amyloid and Inherently Toxic to Neuroblastoma Cells.
- Published in:
- PLoS ONE, 2014, v. 9, n. 1, p. 1, doi. 10.1371/journal.pone.0086720
- By:
- Publication type:
- Article
Lipid rafts are primary mediators of amyloid oxidative attack on plasma membrane.
- Published in:
- Journal of Molecular Medicine, 2010, v. 88, n. 6, p. 597, doi. 10.1007/s00109-010-0603-8
- By:
- Publication type:
- Article
Trodusquemine enhances Aβ<sub>42</sub> aggregation but suppresses its toxicity by displacing oligomers from cell membranes.
- Published in:
- Nature Communications, 2019, v. 10, n. 1, p. 1, doi. 10.1038/s41467-018-07699-5
- By:
- Publication type:
- Article
Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers.
- Published in:
- Frontiers in Neuroscience, 2021, p. 1, doi. 10.3389/fnins.2021.680026
- By:
- Publication type:
- Article
Sphingosine 1‐phosphate attenuates neuronal dysfunction induced by amyloid‐β oligomers through endocytic internalization of NMDA receptors.
- Published in:
- FEBS Journal, 2023, v. 290, n. 1, p. 112, doi. 10.1111/febs.16579
- By:
- Publication type:
- Article
The acute myeloid leukemia‐associated Nucleophosmin 1 gene mutations dictate amyloidogenicity of the C‐terminal domain.
- Published in:
- FEBS Journal, 2019, v. 286, n. 12, p. 2311, doi. 10.1111/febs.14815
- By:
- Publication type:
- Article
Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism.
- Published in:
- Communications Biology, 2020, v. 3, n. 1, p. 1, doi. 10.1038/s42003-020-01140-8
- By:
- Publication type:
- Article
A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells.
- Published in:
- Journal of Cellular & Molecular Medicine, 2011, v. 15, n. 10, p. 2106, doi. 10.1111/j.1582-4934.2010.01239.x
- By:
- Publication type:
- Article
Misfolded protein oligomers induce an increase of intracellular Ca<sup>2+</sup> causing an escalation of reactive oxidative species.
- Published in:
- Cellular & Molecular Life Sciences, 2022, v. 79, n. 9, p. 1, doi. 10.1007/s00018-022-04513-w
- By:
- Publication type:
- Article
Effects of oligomer toxicity, fibril toxicity and fibril spreading in synucleinopathies.
- Published in:
- Cellular & Molecular Life Sciences, 2022, v. 79, n. 3, p. 1, doi. 10.1007/s00018-022-04166-9
- By:
- Publication type:
- Article
Quantitative assessment of the degradation of aggregated TDP-43 mediated by the ubiquitin proteasome system and macroautophagy.
- Published in:
- FASEB Journal, 2017, v. 31, n. 12, p. 5609, doi. 10.1096/fj.201700292RR
- By:
- Publication type:
- Article
Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions.
- Published in:
- FASEB Journal, 2015, v. 29, n. 9, p. 3689, doi. 10.1096/fj.14-269522
- By:
- Publication type:
- Article
Oxidative Stress and Mitochondrial Damage in Neurodegenerative Diseases: From Molecular Mechanisms to Targeted Therapies.
- Published in:
- Oxidative Medicine & Cellular Longevity, 2020, p. 1, doi. 10.1155/2020/1270256
- By:
- Publication type:
- Article
Proteostasis Failure in Neurodegenerative Diseases: Focus on Oxidative Stress.
- Published in:
- Oxidative Medicine & Cellular Longevity, 2020, p. 1, doi. 10.1155/2020/5497046
- By:
- Publication type:
- Article
Oxidative Stress in Neurodegenerative Diseases: From a Mitochondrial Point of View.
- Published in:
- Oxidative Medicine & Cellular Longevity, 2019, p. 1, doi. 10.1155/2019/2105607
- By:
- Publication type:
- Article
A single-domain antibody detects and neutralises toxic Aβ<sub>42</sub> oligomers in the Alzheimer's disease CSF.
- Published in:
- Alzheimer's Research & Therapy, 2024, v. 16, n. 1, p. 1, doi. 10.1186/s13195-023-01361-z
- By:
- Publication type:
- Article
Putative novel CSF biomarkers of Alzheimer's disease based on the novel concept of generic protein misfolding and proteotoxicity: the PRAMA cohort.
- Published in:
- Translational Neurodegeneration, 2024, v. 13, n. 1, p. 1, doi. 10.1186/s40035-024-00405-0
- By:
- Publication type:
- Article
Amyloid fibrils act as a reservoir of soluble oligomers, the main culprits in protein deposition diseases.
- Published in:
- BioEssays, 2022, v. 44, n. 11, p. 1, doi. 10.1002/bies.202200086
- By:
- Publication type:
- Article
α-Synuclein oligomers and fibrils: partners in crime in synucleinopathies.
- Published in:
- Neural Regeneration Research, 2023, v. 18, n. 11, p. 2332, doi. 10.4103/1673-5374.371345
- By:
- Publication type:
- Article
Effect of molecular chaperones on aberrant protein oligomers in vitro: super-versus sub-stoichiometric chaperone concentrations.
- Published in:
- Biological Chemistry, 2016, v. 397, n. 5, p. 401, doi. 10.1515/hsz-2015-0250
- By:
- Publication type:
- Article
Exploring the Aβ<sub>1-42</sub> fibrillogenesis timeline by atomic force microscopy and surface enhanced Raman spectroscopy.
- Published in:
- Frontiers in Molecular Biosciences, 2024, p. 1, doi. 10.3389/fmolb.2024.1376411
- By:
- Publication type:
- Article