about
Inhibition and disaggregation of α-synuclein oligomers by natural polyphenolic compoundsIncreased alpha-synuclein aggregation following limited cleavage by certain matrix metalloproteinasesHistopathology and clinical course of MOG-antibody-associated encephalomyelitisDevelopment and implementation of a high-throughput compound screening assay for targeting disrupted ER calcium homeostasis in Alzheimer's diseaseAnle138b: a novel oligomer modulator for disease-modifying therapy of neurodegenerative diseases such as prion and Parkinson's disease.Systematic identification of antiprion drugs by high-throughput screening based on scanning for intensely fluorescent targets.Modelling Ser129 phosphorylation inhibits membrane binding of pore-forming alpha-synuclein oligomersSeeding and transgenic overexpression of alpha-synuclein triggers dendritic spine pathology in the neocortexDiphenylpyrazole-derived compounds increase survival time of mice after prion infection.Agent strain variation in human prion disease: insights from a molecular and pathological review of the National Institutes of Health series of experimentally transmitted disease.Autocatalytic self-propagation of misfolded prion proteinSingle-channel electrophysiology reveals a distinct and uniform pore complex formed by α-synuclein oligomers in lipid membranesPiperazine derivatives inhibit PrP/PrP(res) propagation in vitro and in vivo.Cell-free formation of misfolded prion protein with authentic prion infectivity.Consensus classification of human prion disease histotypes allows reliable identification of molecular subtypes: an inter-rater study among surveillance centres in Europe and USACharacterization of truncated forms of abnormal prion protein in Creutzfeldt-Jakob disease.Design of anti- and pro-aggregation variants to assess the effects of methionine oxidation in human prion protein.Analyses of protease resistance and aggregation state of abnormal prion protein across the spectrum of human prionsIncidence and spectrum of sporadic Creutzfeldt-Jakob disease variants with mixed phenotype and co-occurrence of PrPSc types: an updated classificationEstablishing quantitative real-time quaking-induced conversion (qRT-QuIC) for highly sensitive detection and quantification of PrPSc in prion-infected tissues.Phenotypic variability of sporadic human prion disease and its molecular basis: past, present, and future.Extracellular vesicle sorting of α-Synuclein is regulated by sumoylation.Mitochondrial membrane permeabilisation by amyloid aggregates and protection by polyphenols.Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with α-synuclein at the single molecule level.Synthesis of benzamide derivatives and their evaluation as antiprion agents.Inhibition of mitochondrial fusion by α-synuclein is rescued by PINK1, Parkin and DJ-1.Divergent molecular effects of desmin mutations on protein assembly in myofibrillar myopathy.Converse modulation of toxic alpha-synuclein oligomers in living cells by N'-benzylidene-benzohydrazide derivates and ferric iron.CADASIL mutations enhance spontaneous multimerization of NOTCH3.Molecular dynamics simulations indicate a possible role of parallel beta-helices in seeded aggregation of poly-Gln.Neuronal cell death in scrapie-infected mice is due to apoptosis.Two different binding modes of α-synuclein to lipid vesicles depending on its aggregation state.Reduced spiral ganglion neuronal loss by adjunctive neurotrophin-3 in experimental pneumococcal meningitis.Adjunctive N-acetyl-L-cysteine in treatment of murine pneumococcal meningitis.The oligomer modulator anle138b inhibits disease progression in a Parkinson mouse model even with treatment started after disease onset.Elevated levels of methylmalonate and homocysteine in Parkinson's disease, progressive supranuclear palsy and amyotrophic lateral sclerosis.Presence of phosphodiesterase type 5 in the spinal cord and its involvement in bladder outflow obstruction related bladder overactivity.Generation of ferric iron links oxidative stress to α-synuclein oligomer formation.Identification of anti-prion compounds as efficient inhibitors of polyglutamine protein aggregation in a zebrafish model.Single particle analysis of manganese-induced prion protein aggregates.
P50
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Armin Giese
@ast
Armin Giese
@en
Armin Giese
@es
Armin Giese
@nl
Armin Giese
@sl
type
label
Armin Giese
@ast
Armin Giese
@en
Armin Giese
@es
Armin Giese
@nl
Armin Giese
@sl
altLabel
Giese A
@en
prefLabel
Armin Giese
@ast
Armin Giese
@en
Armin Giese
@es
Armin Giese
@nl
Armin Giese
@sl
P1053
F-3271-2010
P106
P21
P31
P3829
P496
0000-0002-8238-4102