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

Quantitative analysis of α-synuclein solubility in living cells using split GFP complementation.

PloS one - 1 Jan 2012

Kothawala Ahmed, Kilpatrick Kiri, Novoa Jose Andres, Segatori Laura

Abstract excerpt

Presently incurable, Parkinson's disease (PD) is the most common neurodegenerative movement disorder and affects 1% of the population over 60 years of age. The hallmarks of PD pathogenesis are the loss of dopaminergic neurons in the substantia nigra pars compacta, and the occurrence of proteinaceous cytoplasmic inclusions (Lewy bodies) in surviving neurons. Lewy bodies are mainly composed of the pre-synaptic...

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 Green Fluorescent Proteins
Share to HeLa Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Proteasome Endopeptidase Complex

Share to Protein Multimerization

Share to Proteolysis

Share to Solubility

Share to Spectrometry, Fluorescence

Source

Open in PubMed Open full text

Identifiers

PMID: 22927976
DOI: 10.1371/journal.pone.0043505
PMCID: PMC3425482

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

Quantitative analysis of α-synuclein solubility in living cells using split GFP complementation.PMID 22927976Read ↗

Rationally Designed Variants of α-Synuclein Illuminate Its in vivo Structural Properties in Health and DiseaseSemantic proximity Read ↗

Unveiling a Selective Mechanism for the Inhibition of α-Synuclein Aggregation by β-Synuclein.Semantic proximity Read ↗

Rapid iPSC inclusionopathy models shed light on formation, consequence, and molecular subtype of α-synuclein inclusionsSemantic proximity Read ↗

In vivo and in vitro protein solubility assays using split GFPSemantic proximity Read ↗

Formation and toxicity of soluble polyglutamine oligomers in living cells.Semantic proximity Read ↗

Parkinson's disease-specific α-Synuclein variants potentially drive Lewy body formation by engaging in promiscuous and non-functional interactions.Semantic proximity Read ↗

A high-content imaging workflow to screen for molecules that reduce cellular uptake of α-synuclein preformed fibrilsSemantic proximity Read ↗

In Vivo Protein Complementation Demonstrates Presynaptic α-Synuclein Oligomerization and Age-Dependent Accumulation of 8–16-mer Oligomer SpeciesSemantic proximity Read ↗

Foldamers rescue synucleinopathy phenotypes in multiple in vitro and in vivo models.Semantic proximity Read ↗

A Facile Method to Produce N-Terminally Truncated α-SynucleinSemantic proximity Read ↗

Reconstitution of Helical Soluble α-Synuclein through Transient Interaction with Lipid InterfacesSemantic proximity Read ↗

Disulfide engineering reveals unexpected pro- and anti-aggregation conformers of human α-synucleinSemantic proximity Read ↗

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