about
Stabilization of a -hairpin in monomeric Alzheimer's amyloid- peptide inhibits amyloid formationSequestration of a β-hairpin for control of α-synuclein aggregationSequestration of the Abeta peptide prevents toxicity and promotes degradation in vivoStructural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment Is Part of the β-Sheet CoreRecombinant amyloid beta-peptide production by coexpression with an affibody ligand.Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR.Engineered aggregation inhibitor fusion for production of highly amyloidogenic human islet amyloid polypeptide.QIAD assay for quantitating a compound's efficacy in elimination of toxic Aβ oligomersNMR of alpha-synuclein-polyamine complexes elucidates the mechanism and kinetics of induced aggregation.β-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation InhibitorA β-hairpin-binding protein for three different disease-related amyloidogenic proteins.The off-rate of monomers dissociating from amyloid-β protofibrils.Opposed Effects of Dityrosine Formation in Soluble and Aggregated α-Synuclein on Fibril Growth.Alternative conformations of the Tau repeat domain in complex with an engineered binding protein.A kinetic trap is an intrinsic feature in the folding pathway of single-chain Fv fragments.Dependence of alpha-synuclein aggregate morphology on solution conditions.Cellular polyamines promote the aggregation of alpha-synuclein.Interaction of Alzheimer's A beta peptide with an engineered binding protein--thermodynamics and kinetics of coupled folding-binding.Impact of subunit linkages in an engineered homodimeric binding protein to α-synuclein.Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy.Impact of the acidic C-terminal region comprising amino acids 109-140 on alpha-synuclein aggregation in vitro.Fibril structure of amyloid-β(1-42) by cryo-electron microscopy.Uncovering the Binding and Specificity of β-Wrapins for Amyloid-β and α-Synuclein.DNP-Enhanced MAS NMR: A Tool to Snapshot Conformational Ensembles of α-Synuclein in Different States.Contact between the β1 and β2 Segments of α-Synuclein that Inhibits Amyloid Formation.Single fibril growth kinetics of α-synuclein.Structural insights from lipid-bilayer nanodiscs link α-Synuclein membrane-binding modes to amyloid fibril formationTranscriptome-wide analysis uncovers the targets of the RNA-binding protein MSI2 and effects of MSI2's RNA-binding activity on IL-6 signalingA D-enantiomeric peptide interferes with hetero-association of amyloid-β oligomers and prion proteinOrigin of metastable oligomers and their effects on amyloid fibril self-assemblyElucidating the multi-targeted anti-amyloid activity and enhanced islet amyloid polypeptide binding of -wrapinsα-Synuclein-derived lipoparticles in the study of α-Synuclein amyloid fibril formationα-Synuclein Aggregation Monitored by Thioflavin T Fluorescence Assay.Double-stranded DNA stimulates the fibrillation of alpha-synuclein in vitro and is associated with the mature fibrils: an electron microscopy studyAn engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrilsAtomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopyCryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-β fibrils
P50
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Wolfgang Hoyer
@ast
Wolfgang Hoyer
@en
Wolfgang Hoyer
@es
Wolfgang Hoyer
@nl
Wolfgang Hoyer
@sl
type
label
Wolfgang Hoyer
@ast
Wolfgang Hoyer
@en
Wolfgang Hoyer
@es
Wolfgang Hoyer
@nl
Wolfgang Hoyer
@sl
prefLabel
Wolfgang Hoyer
@ast
Wolfgang Hoyer
@en
Wolfgang Hoyer
@es
Wolfgang Hoyer
@nl
Wolfgang Hoyer
@sl
P1053
H-6193-2013
P106
P21
P31
P3829
P496
0000-0003-4301-5416