Results 1 to 10 of about 125,755 (100)

Amyloid oligomers as on-pathway precursors or off-pathway competitors of fibrils

open access: yesFrontiers in Molecular Biosciences, 2023
Amyloid Diseases involve the growth of disease specific proteins into amyloid fibrils and their deposition in protein plaques. Amyloid fibril formation is typically preceded by oligomeric intermediates.
Martin Muschol   +2 more
doaj   +1 more source

Reactions of a trans-diamminediaquaplatinum(II) complex with L-cysteine

open access: yesMacedonian Journal of Chemistry and Chemical Engineering, 2021
The reaction of a trans-diamminediaquaplatinum(II) complex, trans-[Pt(15NH3)2(H2O)2]2+ (1), and L-cysteine (R–SH) has been performed to confirm the formation of the products in the solution.
Sutopo Hadi   +4 more
doaj   +1 more source

Oligomerization and tyrosine nitration enhance the allergenic potential of the birch and grass pollen allergens Bet v 1 and Phl p 5

open access: yesFrontiers in Allergy, 2023
Protein modifications such as oligomerization and tyrosine nitration alter the immune response to allergens and may contribute to the increasing prevalence of allergic diseases.
Janine Fröhlich-Nowoisky   +4 more
doaj   +1 more source

Synaptic Disruption by Soluble Oligomers in Patients with Alzheimer’s and Parkinson’s Disease

open access: yesBiomedicines, 2022
Neurodegenerative diseases are the result of progressive dysfunction of the neuronal activity and subsequent neuronal death. Currently, the most prevalent neurodegenerative diseases are by far Alzheimer’s (AD) and Parkinson’s (PD) disease, affecting ...
Berenice A. Gutierrez, Agenor Limon
doaj   +1 more source

Frondoside A Attenuates Amyloid-β Proteotoxicity in Transgenic Caenorhabditis elegans by Suppressing Its Formation

open access: yesFrontiers in Pharmacology, 2020
Oligomeric assembly of Amyloid-β (Aβ) is the main toxic species that contribute to early cognitive impairment in Alzheimer’s patients. Therefore, drugs that reduce the formation of Aβ oligomers could halt the disease progression.
Taweesak Tangrodchanapong   +2 more
doaj   +1 more source

Extracellular Alpha-Synuclein: Mechanisms for Glial Cell Internalization and Activation

open access: yesBiomolecules, 2022
Alpha-synuclein (α-syn) is a small protein composed of 140 amino acids and belongs to the group of intrinsically disordered proteins. It is a soluble protein that is highly expressed in neurons and expressed at low levels in glial cells.
Cecilia Chavarría   +2 more
doaj   +1 more source

Proteostasis Response to Protein Misfolding in Controlled Hypertension

open access: yesCells, 2022
Hypertension is the most determinant risk factor for cardiovascular diseases. Early intervention and future therapies targeting hypertension mechanisms may improve the quality of life and clinical outcomes.
Manuel Teixeira   +12 more
doaj   +1 more source

Neuropathology of the Alzheimer's continuum: an update

open access: yesFree Neuropathology, 2020
Alzheimer’s disease (AD), the most common form of dementia worldwide, is a mixed proteinopathy (amyloid and tau). Originally defined as a clinicopathological entity, it is a heterogenous, multifactorial disorder, currently referred to as the Alzheimer’s ...
Kurt A. Jellinger
doaj   +1 more source

The elusive nature and diagnostics of misfolded Aβ oligomers.

open access: yesFrontiers in Chemistry, 2015
Amyloid-beta (Aβ) peptide oligomers are believed to be the causative agents of Alzheimer’s disease (AD). Though post-mortem examination shows that insoluble fibrils are deposited in the brains of AD patients in the form of intracellular (tangles) and ...
Eleonora eCerasoli   +2 more
doaj   +1 more source

The HSP40 chaperone Ydj1 drives amyloid beta 42 toxicity

open access: yesEMBO Molecular Medicine, 2022
Amyloid beta 42 (Abeta42) is the principal trigger of neurodegeneration during Alzheimer’s disease (AD). However, the etiology of its noxious cellular effects remains elusive.
Julia Ring   +39 more
doaj   +1 more source

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