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

Copper- and iron-induced differential fibril formation in alpha-synuclein: TEM study.

Neuroscience letters - 7 Sept 2007

Bharathi, Indi S S, Rao K S J

Abstract excerpt

alpha-Synuclein filaments are the central component of intracytoplasmic inclusion bodies characteristic of Parkinson's disease (PD) and related disorders. Metals are the significant etiological factors in PD, and their interaction with alpha-synuclein affect dramatically the kinetics of fibrillation. Currently, we have investigated the influence of Cu(II) and Fe(III) on alpha-synuclein fibril formation. Cu(II)...

Read the complete abstract on PubMed

Topics

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

Share to alpha-Synuclein
Share to Copper
Share to Iron

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microscopy, Electron, Transmission

Share to Mutation

Share to Protein Binding

Share to Time Factors

Source

Identifiers

PMID: 17714865
DOI: 10.1016/j.neulet.2007.06.052

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Copper- and iron-induced differential fibril formation in alpha-synuclein: TEM study.PMID 17714865Read ↗

Structural Insights of Fe3+ Induced α-synuclein Fibrillation in Parkinson's Disease.Semantic proximity Read ↗

Interactions between metals and alpha-synuclein--function or artefact?Semantic proximity Read ↗

Alpha-synuclein: relating metals to structure, function and inhibition.Semantic proximity Read ↗

The A53T alpha-synuclein mutation increases iron-dependent aggregation and toxicity.Semantic proximity Read ↗

Copper(II) and the pathological H50Q α-synuclein mutant: Environment meets geneticsSemantic proximity Read ↗

Accelerated proteasomal activity induced by Pb2+, Ga3+, or Cu2+ exposure does not induce degradation of alpha-synuclein.Semantic proximity Read ↗

Environmental and genetic factors support the dissociation between α-synuclein aggregation and toxicity.Semantic proximity Read ↗

Ellagic Acid Modulates Uninduced as well as Mutation and Metal-Induced Aggregation of α-Synuclein: Implications for Parkinson's Disease.Semantic proximity Read ↗

New insights on the structure of alpha-synuclein fibrils using cryo-electron microscopy.Semantic proximity Read ↗

Overexpression of alpha-synuclein at non-toxic levels increases dopaminergic cell death induced by copper exposure via modulation of protein degradation pathways.Semantic proximity Read ↗

Cryo-EM structure of amyloid fibril formed by α-synuclein hereditary A53E mutation reveals a distinct protofilament interface.Semantic proximity Read ↗

Cryo-EM structure of amyloid fibril formed by α-synuclein hereditary A53E mutationSemantic proximity Read ↗

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