about
α-Synuclein interacts with the switch region of Rab8a in a Ser129 phosphorylation-dependent mannerMetal-ligand interactions in perturbed blue copper sites: a paramagnetic (1)H NMR study of Co(II)-pseudoazurin.Spectroscopic and Theoretical Study of Cu(I) Binding to His111 in the Human Prion Protein Fragment 106-115.Dissociation of amyloid fibrils of alpha-synuclein in supercooled water.cDNA cloning, sequence, and regulation of a major female-specific and growth hormone-inducible rat liver cytochrome P-450 active in 15 beta-hydroxylation of steroid sulfates.Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein.Environmental and genetic factors support the dissociation between α-synuclein aggregation and toxicity.Repurposing doxycycline for synucleinopathies: remodelling of α-synuclein oligomers towards non-toxic parallel beta-sheet structured species.Toward the discovery of effective polycyclic inhibitors of alpha-synuclein amyloid assembly.Bioinorganic Chemistry of Parkinson's Disease: Affinity and Structural Features of Cu(I) Binding to the Full-Length β-Synuclein Protein.Phthalocyanines as Molecular Scaffolds to Block Disease-Associated Protein Aggregation.NMR of alpha-synuclein-polyamine complexes elucidates the mechanism and kinetics of induced aggregation.Copper(II) and the pathological H50Q α-synuclein mutant: Environment meets genetics.Structural characterization of alpha-synuclein in an aggregation prone state.Structural basis behind the interaction of Zn²⁺ with the protein α-synuclein and the Aβ peptide: a comparative analysis.Bioinorganic chemistry of synucleinopathies: deciphering the binding features of Met motifs and His-50 in AS-Cu(I) interactions.Role of N-terminal methionine residues in the redox activity of copper bound to alpha-synuclein.Site-specific copper-catalyzed oxidation of α-synuclein: tightening the link between metal binding and protein oxidative damage in Parkinson's disease.Disruption of zinc and copper interactions with Aβ(1-40) by a non-toxic, isoniazid-derived, hydrazone: a novel biometal homeostasis restoring agent in Alzheimer's disease therapy?A moderate metal-binding hydrazone meets the criteria for a bioinorganic approach towards Parkinson's disease: Therapeutic potential, blood-brain barrier crossing evaluation and preliminary toxicological studies.Small molecule-mediated stabilization of vesicle-associated helical α-synuclein inhibits pathogenic misfolding and aggregation.Copper Coordination Features of Human Islet Amyloid Polypeptide: The Type 2 Diabetes Peptide.Conformational ensemble of human α-synuclein physiological form predicted by molecular simulationsStructural properties of pore-forming oligomers of alpha-synucleinBioinorganic Chemistry of Parkinson’s Disease: Structural Determinants for the Copper-Mediated Amyloid Formation of Alpha-SynucleinLong-Range Correlated Dynamics in Intrinsically Disordered ProteinsStructural Characterization of the Intrinsically Unfolded Protein β-Synuclein, a Natural Negative Regulator of α-Synuclein AggregationInteraction of α-Synuclein with Divalent Metal Ions Reveals Key Differences: A Link between Structure, Binding Specificity and Fibrillation EnhancementFamilial Mutants of α-Synuclein with Increased Neurotoxicity Have a Destabilized ConformationCharge-induced molecular alignment of intrinsically disordered proteinsAmino acid bulkiness defines the local conformations and dynamics of natively unfolded alpha-synuclein and tauStructural comparison of mouse and human α-synuclein amyloid fibrils by solid-state NMRX1INH, an improved next-generation affinity-optimized hydrazonic ligand, attenuates abnormal copper(i)/copper(ii)-α-Syn interactions and affects protein aggregation in a cellular model of synucleinopathy
P50
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P50
description
researcher, ORCID id # 0000-0003-0454-7735
@en
wetenschapper
@nl
name
Claudio O. Fernandez
@ast
Claudio O. Fernandez
@en
Claudio O. Fernandez
@es
Claudio O. Fernandez
@nl
type
label
Claudio O. Fernandez
@ast
Claudio O. Fernandez
@en
Claudio O. Fernandez
@es
Claudio O. Fernandez
@nl
altLabel
Claudio Oscar Fernandez
@en
prefLabel
Claudio O. Fernandez
@ast
Claudio O. Fernandez
@en
Claudio O. Fernandez
@es
Claudio O. Fernandez
@nl
P106
P1153
7403176934
P21
P31
P496
0000-0003-0454-7735