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

shRNA-Based Screen Identifies Endocytic Recycling Pathway Components That Act as Genetic Modifiers of Alpha-Synuclein Aggregation, Secretion and Toxicity

28 Apr 2016

Abstract excerpt

Alpha-Synuclein (aSyn) misfolding and aggregation is common in several neurodegenerative diseases, including Parkinson's disease and dementia with Lewy bodies, which are known as synucleinopathies. Accumulating evidence suggests that secretion and cell-to-cell trafficking of pathological forms of aSyn may explain the typical patterns of disease progression. However, the molecular mechanisms controlling aSyn...

Read the complete abstract on PubMed

Topics

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

Share to Alzheimer's disease research and treatments
Share to Cellular transport and secretion
Share to Parkinson's Disease Mechanisms and Treatments

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 27123591
DOI: 10.1371/journal.pgen.1005995

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

shRNA-Based Screen Identifies Endocytic Recycling Pathway Components That Act as Genetic Modifiers of Alpha-Synuclein Aggregation, Secretion and ToxicityPMID 27123591Read ↗

The effects of the novel A53E alpha-synuclein mutation on its oligomerization and aggregationSemantic proximity Read ↗

Membrane binding, internalization, and sorting of alpha-synuclein in the cell.Semantic proximity Read ↗

Parkinson's: A Disease of Aberrant Vesicle TraffickingSemantic proximity Read ↗

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

Alpha-synuclein: from secretion to dysfunction and deathSemantic proximity Read ↗

WDR44 drives de novo α-synuclein aggregation at the lysosomal membrane and promotes neuronal dysfunction in Parkinson’s DiseaseSemantic proximity Read ↗

Yeast Reveal a “Druggable” Rsp5/Nedd4 Network that Ameliorates α-Synuclein Toxicity in NeuronsSemantic proximity Read ↗

The LRRK2-RAB axis in regulation of vesicle trafficking and α-synuclein propagationSemantic proximity Read ↗

Limelight on Alpha-Synuclein: Pathological and Mechanistic Implications in NeurodegenerationSemantic proximity Read ↗

Identification of novel ATP13A2 interactors and their role in α-synuclein misfolding and toxicitySemantic proximity Read ↗

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

alpha-synuclein and Parkinson's disease: the first roadblock.Semantic proximity Read ↗

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