Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Role of glycine-33 and methionine-35 in Alzheimer's amyloid beta-peptide 1-42-associated oxidative stress and neurotoxicity.

Biochimica et biophysica acta - 16 Mar 2002

Kanski Jaroslaw, Varadarajan Sridhar, Aksenova Marina, Butterfield D Allan

Abstract excerpt

Recent theoretical calculations predicted that Gly33 of one molecule of amyloid beta-peptide (1-42) (Abeta(1-42)) is attacked by a putative sulfur-based free radical of methionine residue 35 of an adjacent peptide. This would lead to a carbon-centered free radical on Gly33 that would immediately bind oxygen to form a peroxyl free radical. Such peroxyl free radicals could contribute to the reported...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amyloid beta-Peptides
Share to Electron Spin Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluoresceins

Share to Free Radicals

Share to Glycine

Share to Methionine

Share to Synaptosomes

Share to Valine

Source

Identifiers

PMID: 11959460
DOI: 10.1016/s0925-4439(01)00097-7

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of glycine-33 and methionine-35 in Alzheimer's amyloid beta-peptide 1-42-associated oxidative stress and neurotoxicity.PMID 11959460Read ↗

Methionine-35 of A<i>β</i>(1–42): Importance for Oxidative Stress in Alzheimer DiseaseSemantic proximity Read ↗

The turn formation at positions 22 and 23 in the 42-mer amyloid beta peptide: the emerging role in the pathogenesis of Alzheimer's disease.Semantic proximity Read ↗

Oxidation of methionine 35 reduces toxicity of the amyloid beta-peptide(1–42) in neuroblastoma cells (IMR-32) via enzyme methionine sulfoxide reductase A expression and functionSemantic proximity Read ↗

Toxicity in rat primary neurons through the cellular oxidative stress induced by the turn formation at positions 22 and 23 of Aβ42.Semantic proximity Read ↗

In vivo oxidative stress in brain of Alzheimer disease transgenic mice: Requirement for methionine 35 in amyloid β-peptide of APPSemantic proximity Read ↗

Mutations in amyloid precursor protein and presenilin-1 genes increase the basal oxidative stress in murine neuronal cells and lead to increased sensitivity to oxidative stress mediated by amyloid beta-peptide (1-42), HO and kainic acid: implications for Alzheimer's disease.Semantic proximity Read ↗

Enhanced toxicity and cellular binding of a modified amyloid beta peptide with a methionine to valine substitution.Semantic proximity Read ↗

Synthetic and Biophysical Studies on the Toxic Conformer in Amyloid β with the E22Δ Mutation in Alzheimer Pathology.Semantic proximity Read ↗

The Aβ(1–38) peptide is a negative regulator of the Aβ(1–42) peptide implicated in Alzheimer disease progressionSemantic proximity Read ↗

Redox reactivities of membrane-bound Amyloid-β-Cu complexes and their targeting by metallothionein-3Semantic proximity Read ↗

Modulating Amyloid-β Toxicity: In Vitro Analysis of Aβ42(G37V) Variant Impact on Aβ42 Aggregation and CytotoxicitySemantic proximity Read ↗

Identification of physiological and toxic conformations in Abeta42 aggregates.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.