Results 51 to 60 of about 1,185,249 (285)
Effects of Amyloid Beta Peptide on Neurovascular Cells
Central Asian Journal of Global Health, 2013 Alzheimer’s disease (AD) is a chronic neurodegenerative disorder, which is characterized by the accumulation of amyloid plaques and neurofibrillary tangles in specific regions of the brain, accompanied by impairment of the neurons, and progressive deterioration of cognition and memory of affected individuals.
Sholpan Askarova +3 more
openaire +4 more sources
Estudo bioquímico e comportamental em camundongos submetidos à infusão intracerebroventricular dos peptídeos beta-amilóide AB1-40 E AB25-35 e o papel neuroprotetor da atorvastatina [PDF]
, 2009 Dissertação (mestrado) - Universidade Federal de Santa Catarina. Centro de Ciências Biológicas. Programa de Pós-Graduação em Neurociências.The accumulation and aggregation of beta-amyloid peptide (Aâ) in brain of patients with Alzheimer's disease results
Piermartiri, Tetsade Camboim Bizerra
core
Leucine‐rich glioma inactivated 1 (LGI1) is a ganglioside‐binding protein
FEBS Letters, EarlyView.Neuronal hyperexcitability associated with a decrease/absence of the extracellular protein LGI1 has been suggested to be primarily due to the downregulation of Kv1 channel expression. The molecular mechanisms underlying this decrease have not yet been elucidated.
Kévin Debreux +7 more
wiley +1 more source
Abeta(1-42) induces abnormal alternative splicing of tau exons 2/3 in NGF-induced PC12 cells
Anais da Academia Brasileira de Ciências, 2014 Protein tau plays a pivotal role in the pathophysiology of Alzheimer's disease, where its hyperphos-phorylation promotes aggregation and microtubule destabilization.
TERESA LAGUNES +3 more
doaj +1 more source
Smaller is better: nanobodies meet NMR
FEBS Letters, EarlyView.Nanobodies are single‐domain antigen‐binding fragments derived from camelid heavy chain antibodies. Their small size, high stability, and exceptional specificity make nanobodies uniquely useful probes for NMR studies of protein dynamics, transient conformational states, and protein–protein interactions.
Oleg Y. Dmitriev
wiley +1 more source
FEBS Letters, EarlyView.Transient oligomers formed by intrinsically disordered proteins may be ‘invisible’ to direct detection yet remain accessible to solution NMR through equilibrium‐exchange measurements and pressure‐jump experiments. Complementary methods report on mass, stoichiometry, selected distance distributions, morphology, and internal packing.
Martin D. Gelenter, Ad Bax
wiley +1 more source
Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms
Nature Communications, 2019 Amyloid beta (Aβ42) peptides form heterogeneous mixtures of aggregates, which are closely linked to Alzheimer’s disease.
Suman De +16 more
doaj +1 more source
The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer
Molecular Oncology, EarlyView.Mutations, environmental stress, and chaperone dysfunction can destabilize pVHL, promoting its conversion from the native folded state into amyloid‐like assemblies. This transition may contribute to protein storage, cell dormancy, survival, and drug resistance.
Lara Abad +2 more
wiley +1 more source
Amyloid fibril proteomics of AD brains reveals modifiers of aggregation and toxicity
Molecular Neurodegeneration, 2023 Background The accumulation of amyloid beta (Aβ) peptides in fibrils is prerequisite for Alzheimer’s disease (AD). Our understanding of the proteins that promote Aβ fibril formation and mediate neurotoxicity has been limited due to technical challenges ...
Arun Upadhyay +6 more
doaj +1 more source
Adenosine triphosphate as a modulator of protein interactions and stability
FEBS Open Bio, EarlyView.ATP is best known as the cell's energy currency, but it also shapes how proteins fold, interact, aggregate and form biomolecular condensates. This review explains the emerging physical principles behind these effects, including weak binding to charged protein regions, magnesium‐dependent behaviour and concentration‐dependent control of protein ...
Shuyuan Tan, Robin Curtis
wiley +1 more source