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α-Synuclein modifies huntingtin aggregation in living cellsSIRT1 and SIRT2: emerging targets in neurodegenerationElevated α-synuclein caused by SNCA gene triplication impairs neuronal differentiation and maturation in Parkinson's patient-derived induced pluripotent stem cellsC-Terminal Tyrosine Residue Modifications Modulate the Protective Phosphorylation of Serine 129 of α-Synuclein in a Yeast Model of Parkinson's Disease.Yeast DJ-1 superfamily members are required for diauxic-shift reprogramming and cell survival in stationary phaseIdebenone and resveratrol extend lifespan and improve motor function of HtrA2 knockout miceAssessing the subcellular dynamics of alpha-synuclein using photoactivation microscopy.A Novel Microfluidic Cell Co-culture Platform for the Study of the Molecular Mechanisms of Parkinson's Disease and Other SynucleinopathiesDopamine-induced conformational changes in alpha-synucleinIdentification and quantitative analysis of human transthyretin variants in human serum by Fourier transform ion-cyclotron resonance mass spectrometry.Copy-number variation of the neuronal glucose transporter gene SLC2A3 and age of onset in Huntington's disease.A non-invasive method based on saliva to characterize transthyretin in familial amyloidotic polyneuropathy patients using FT-ICR high-resolution MS.Visualization of cell-to-cell transmission of mutant huntingtin oligomersTreatment with diphenyl-pyrazole compound anle138b/c reveals that α-synuclein protects melanoma cells from autophagic cell death.Modulating Alzheimer's disease through caffeine: a putative link to epigenetics.Small Molecules Detected by Second-Harmonic Generation Modulate the Conformation of Monomeric α-Synuclein and Reduce Its Aggregation in CellsMechanisms of disease II: cellular protein quality control.Therapeutic role of sirtuins in neurodegenerative disease.The caffeine-binding adenosine A2A receptor induces age-like HPA-axis dysfunction by targeting glucocorticoid receptor function.The NAD-dependent deacetylase sirtuin 2 is a suppressor of microglial activation and brain inflammation.Environmental and genetic factors support the dissociation between α-synuclein aggregation and toxicity.Glycation potentiates neurodegeneration in models of Huntington's disease.Contribution of Neuroepigenetics to Huntington's Disease.Alzheimer's disease: the quest to understand complexity.Simple is good: yeast models of neurodegeneration.Epigenetics in neurodegeneration: a new layer of complexity.Sirtuins: common targets in aging and in neurodegeneration.Aggresome formation and segregation of inclusions influence toxicity of α-synuclein and synphilin-1 in yeast.Oxidative and nitrative alpha-synuclein modifications and proteostatic stress: implications for disease mechanisms and interventions in synucleinopathies.Harnessing the power of yeast to unravel the molecular basis of neurodegeneration.Alpha-synuclein and intracellular trafficking: impact on the spreading of Parkinson's disease pathology.The causative role and therapeutic potential of the kynurenine pathway in neurodegenerative disease.Limelight on alpha-synuclein: pathological and mechanistic implications in neurodegeneration.Challenges and promises in the development of neurotrophic factor-based therapies for Parkinson's disease.Protein phosphorylation in neurodegeneration: friend or foe?Structure, function and toxicity of alpha-synuclein: the Bermuda triangle in synucleinopathies.Tau deletion promotes brain insulin resistanceSodium butyrate rescues dopaminergic cells from alpha-synuclein-induced transcriptional deregulation and DNA damage.Glycation in Parkinson's disease and Alzheimer's disease.Linking alpha-synuclein phosphorylation to reactive oxygen species formation and mitochondrial dysfunction in SH-SY5Y cells.
P50
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P50
description
Forscher
@de
investigador
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onderzoeker
@nl
researcher
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ricercatore
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研究員
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研究者
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name
Tiago Fleming Outeiro
@en
Tiago Fleming Outeiro
@nl
type
label
Tiago Fleming Outeiro
@en
Tiago Fleming Outeiro
@nl
prefLabel
Tiago Fleming Outeiro
@en
Tiago Fleming Outeiro
@nl
P106
P31
P496
0000-0003-1679-1727