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

Mimicking phosphorylation at serine 87 inhibits the aggregation of human α-synuclein and protects against its toxicity in a rat model of Parkinson's disease.

The Journal of neuroscience : the official journal of the Society for Neuroscience - 1 Feb 2012

Oueslati Abid, Paleologou Katerina E, Schneider Bernard L, Aebischer Patrick, Lashuel Hilal A

Abstract excerpt

Several lines of evidence suggest that phosphorylation of α-synuclein (α-syn) at S87 or S129 may play an important role in regulating its aggregation, fibrillogenesis, Lewy body formation, and neurotoxicity in vivo. However, whether phosphorylation at these residues enhances or protects against α-syn toxicity in vivo remains unknown. In this study, we investigated the cellular and behavioral effect of...

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 Corpus Striatum

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Transfer Techniques

Share to Parkinson Disease

Share to Phosphorylation

Share to Rats, Wistar

Share to Serine

Source

Open in PubMed Open full text

Identifiers

PMID: 22302797
DOI: 10.1523/JNEUROSCI.3784-11.2012
PMCID: PMC6703371

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

Mimicking phosphorylation at serine 87 inhibits the aggregation of human α-synuclein and protects against its toxicity in a rat model of Parkinson's disease.PMID 22302797Read ↗

Alpha-Synuclein Phosphomimetic Y39E and S129D Knock-In Mice Show Cytosolic Alpha-Synuclein Localization without Developing Neurodegeneration or Motor DeficitsSemantic proximity Read ↗

Authentically phosphorylated α-synuclein at Ser129 accelerates neurodegeneration in a rat model of familial Parkinson's disease.Semantic proximity Read ↗

Ser129D mutant alpha-synuclein induces earlier motor dysfunction while S129A results in distinctive pathology in a rat model of Parkinson's disease.Semantic proximity Read ↗

Parkinson disease mutant E46K enhances α-synuclein phosphorylation in mammalian cell lines, in yeast, and in vivo.Semantic proximity Read ↗

Mutation of Tyrosine Sites in the Human Alpha-Synuclein Gene Induces Neurotoxicity in Transgenic Mice with Soluble Alpha-Synuclein Oligomer Formation.Semantic proximity Read ↗

Alpha-synuclein S129 phosphorylation mutants do not alter nigrostriatal toxicity in a rat model of Parkinson disease.Semantic proximity Read ↗

Modeling Parkinson’s Disease With the Alpha-Synuclein ProteinSemantic proximity Read ↗

N-terminal acetylation reduces α-synuclein pathology in models of Parkinson’s diseaseSemantic proximity Read ↗

Physiology and pathophysiology of alpha-synuclein. Cell culture and transgenic animal models based on a Parkinson's disease-associated protein.Semantic proximity Read ↗

In vivo aggregation of presynaptic alpha-synuclein is not influenced by its phosphorylation at serine-129Semantic proximity Read ↗

Transgenic mice expressing S129 phosphorylation mutations in α-synuclein.Semantic proximity Read ↗

Synapsin III gene silencing redeems alpha-synuclein transgenic mice from Parkinson's disease-like phenotype.Semantic proximity Read ↗

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