about
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicityDirect observation of the interconversion of normal and toxic forms of α-synucleinThe relationship between aggregation and toxicity of polyglutamine-containing ataxin-3 in the intracellular environment of Escherichia coli.Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain.Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation.Rational design of antibodies targeting specific epitopes within intrinsically disordered proteins.Structure of a low-population binding intermediate in protein-RNA recognition.Identification of an RNA Polymerase III Regulator Linked to Disease-Associated Protein Aggregation.Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates.The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation.Methods of probing the interactions between small molecules and disordered proteins.Cell surface localised Hsp70 is a cancer specific regulator of clathrin-independent endocytosis.Structure and dynamics of the integrin LFA-1 I-domain in the inactive state underlie its inside-out/outside-in signaling and allosteric mechanisms.Microfluidic Diffusion Analysis of the Sizes and Interactions of Proteins under Native Solution Conditions.Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method.NMR characterization of the conformational fluctuations of the human lymphocyte function-associated antigen-1 I-domainThe polyglutamine protein ataxin-3 enables normal growth under heat shock conditions in the methylotrophic yeast Pichia pastoris.Structure of a low-population intermediate state in the release of an enzyme product.Inhibition of α-Synuclein Fibril Elongation by Hsp70 Is Governed by a Kinetic Binding Competition between α-Synuclein Species.Delivery of Native Proteins into C. elegans Using a Transduction Protocol Based on Lipid Vesicles.Sequence Specificity in the Entropy-Driven Binding of a Small Molecule and a Disordered Peptide.A Water-Bridged Cysteine-Cysteine Redox Regulation Mechanism in Bacterial Protein Tyrosine Phosphatases.A Rational Design Strategy for the Selective Activity Enhancement of a Molecular Chaperone toward a Target Substrate.The CamSol method of rational design of protein mutants with enhanced solubility.Microfluidic Diffusion Viscometer for Rapid Analysis of Complex Solutions.A Rationally Designed Hsp70 Variant Rescues the Aggregation-Associated Toxicity of Human IAPP in Cultured Pancreatic Islet β-Cells.Publisher Correction: The polyglutamine protein ataxin-3 enables normal growth under heat shock conditions in the methylotrophic yeast Pichia pastoris.Nanobodies Raised against Monomeric α-Synuclein Distinguish between Fibrils at Different Maturation StagesTargeting Amyloid Aggregation: An Overview of Strategies and MechanismsThird generation antibody discovery methods: in silico rational designCooperative Assembly of Hsp70 Subdomain ClustersMultistep Inhibition of α-Synuclein Aggregation and Toxicity in Vitro and in Vivo by TrodusquemineDifferent soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanismsAutomated Behavioral Analysis of Large C. elegans Populations Using a Wide Field-of-view Tracking PlatformSoluble aggregates present in cerebrospinal fluid change in size and mechanism of toxicity during Alzheimer's disease progressionC. elegans expressing D76N β2-microglobulin: a model for in vivo screening of drug candidates targeting amyloidosisEnhancement of the Anti-Aggregation Activity of a Molecular Chaperone Using a Rationally Designed Post-Translational ModificationRational design of a conformation-specific antibody for the quantification of Aβ oligomers
P50
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P50
description
onderzoeker
@nl
researcher ORCID ID = 0000-0002-5040-4420
@en
name
Francesco Antonio Aprile
@ast
Francesco Antonio Aprile
@en
Francesco Antonio Aprile
@es
Francesco Antonio Aprile
@nl
type
label
Francesco Antonio Aprile
@ast
Francesco Antonio Aprile
@en
Francesco Antonio Aprile
@es
Francesco Antonio Aprile
@nl
prefLabel
Francesco Antonio Aprile
@ast
Francesco Antonio Aprile
@en
Francesco Antonio Aprile
@es
Francesco Antonio Aprile
@nl
P108
P106
P21
P31
P496
0000-0002-5040-4420