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

Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein.

Journal of molecular biology - 11 Jul 2008

Heise Henrike, Celej M Soledad, Becker Stefan, Riedel Dietmar, Pelah Avishay, Kumar Ashutosh, Jovin Thomas M, Baldus Marc

Abstract excerpt

Fibrils from the Parkinson's-disease-related A53T mutant of alpha-synuclein were investigated by solid-state NMR spectroscopy, electron microscopy, and atomic force microscopy. Sequential solid-state NMR resonance assignments were obtained for a large fraction of the fibril core. Experiments conducted above and below the freezing point suggest that the fibrils contain regions with increased mobility and...

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 Freezing

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microscopy, Atomic Force

Share to Microscopy, Electron

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Parkinson Disease

Share to Protein Structure, Secondary

Share to Recombinant Proteins

Source

Identifiers

PMID: 18539297
DOI: 10.1016/j.jmb.2008.05.026

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein.PMID 18539297Read ↗

Site-specific perturbations of alpha-synuclein fibril structure by the Parkinson's disease associated mutations A53T and E46K.Semantic proximity Read ↗

Distinct residual and disordered structures of alpha-synuclein analyzed by amide-proton exchange and NMR signal intensity.Semantic proximity Read ↗

Familial mutants of alpha-synuclein with increased neurotoxicity have a destabilized conformation.Semantic proximity Read ↗

Cryo-EM structure of full-length α-synuclein amyloid fibril with Parkinson’s disease familial A53T mutationSemantic proximity Read ↗

Familial Mutations May Switch Conformational Preferences in α-Synuclein Fibrils.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 ↗

Dopamine differentially induces aggregation of A53T mutant and wild type alpha-synuclein: insights into the protein chemistry of Parkinson's disease.Semantic proximity Read ↗

Perturbation in Long-Range Contacts Modulates the Kinetics of Amyloid Formation in α-Synuclein Familial Mutants.Semantic proximity Read ↗

Cryo-EM structure of alpha-synuclein fibrils.Semantic proximity Read ↗

Mutant protein A30P α-synuclein adopts wild-type fibril structure, despite slower fibrillation kinetics.Semantic proximity Read ↗

Comparison of Kinetics, Toxicity, Oligomer Formation, and Membrane Binding Capacity of α-Synuclein Familial Mutations at the A53 Site, Including the Newly Discovered A53V Mutation.Semantic proximity Read ↗

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