about
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicityA protective role for lipid raft cholesterol against amyloid-induced membrane damage in human neuroblastoma cells.Lipid rafts are primary mediators of amyloid oxidative attack on plasma membrane.Biological membranes as protein aggregation matrices and targets of amyloid toxicity.Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions.Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers.TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells.SIRT1 regulates MAPK pathways in vitiligo skin: insight into the molecular pathways of cell survivalEffect of molecular chaperones on aberrant protein oligomers in vitro: super-versus sub-stoichiometric chaperone concentrations.Single molecule experiments emphasize GM1 as a key player of the different cytotoxicity of structurally distinct Aβ1-42 oligomers.Plasma membrane injury depends on bilayer lipid composition in Alzheimer's disease.S-linolenoyl glutathione intake extends life-span and stress resistance via Sir-2.1 upregulation in Caenorhabditis elegans.Protective properties of novel S-acyl-glutathione thioesters against ultraviolet-induced oxidative stress.Novel S-acyl glutathione derivatives prevent amyloid oxidative stress and cholinergic dysfunction in Alzheimer disease models.A causative link between the structure of aberrant protein oligomers and their toxicity.Generation of reactive oxygen species by beta amyloid fibrils and oligomers involves different intra/extracellular pathways.Replicating neuroblastoma cells in different cell cycle phases display different vulnerability to amyloid toxicity.Insights into the molecular basis of the differing susceptibility of varying cell types to the toxicity of amyloid aggregates.Patterns of cell death triggered in two different cell lines by HypF-N prefibrillar aggregates.Interaction of toxic and non-toxic HypF-N oligomers with lipid bilayers investigated at high resolution with atomic force microscopy.A peptide fraction from factor VIII reduces PKC activity in cultured endothelial cells.Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases.Destabilisation, aggregation, toxicity and cytosolic mislocalisation of nucleophosmin regions associated with acute myeloid leukemia.Oxidative stress and reduced antioxidant defenses in peripheral cells from familial Alzheimer's patients.Lipid rafts mediate amyloid-induced calcium dyshomeostasis and oxidative stress in Alzheimer's disease.Poly(ADP-ribose) polymerase activation and cell injury in the course of rat heart heterotopic transplantation.Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers.Quantitative assessment of the degradation of aggregated TDP-43 mediated by the ubiquitin proteasome system and macroautophagy.Protective effect of new S-acylglutathione derivatives against amyloid-induced oxidative stress.Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity.A complex equilibrium among partially unfolded conformations in monomeric transthyretin.Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro.Acylphosphatase overexpression triggers SH-SY5Y differentiation towards neuronal phenotype.Soluble Oligomers Require a Ganglioside to Trigger Neuronal Calcium Overload.Cerebral soluble ubiquitin is increased in patients with Alzheimer's disease.Increased susceptibility to amyloid toxicity in familial Alzheimer's fibroblasts.Extracellular chaperones prevent Aβ42-induced toxicity in rat brains.Toxic HypF-N Oligomers Selectively Bind the Plasma Membrane to Impair Cell Adhesion Capability.Glycosaminoglycans (GAGs) suppress the toxicity of HypF-N prefibrillar aggregates.Membrane cholesterol enrichment prevents Aβ-induced oxidative stress in Alzheimer's fibroblasts.
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description
researcher ORCID ID = 0000-0001-8387-7737
@en
wetenschapper
@nl
name
Cristina Cecchi
@ast
Cristina Cecchi
@en
Cristina Cecchi
@es
Cristina Cecchi
@nl
type
label
Cristina Cecchi
@ast
Cristina Cecchi
@en
Cristina Cecchi
@es
Cristina Cecchi
@nl
prefLabel
Cristina Cecchi
@ast
Cristina Cecchi
@en
Cristina Cecchi
@es
Cristina Cecchi
@nl
P106
P1153
7005272539
P21
P31
P496
0000-0001-8387-7737