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

A familial ATP13A2 mutation enhances alpha-synuclein aggregation and promotes cell death.

Human molecular genetics - 15 Jul 2016

Lopes da Fonseca Tomás, Pinho Raquel, Outeiro Tiago F

Abstract excerpt

Aberrant protein-protein interactions are a common pathological hallmark among neurodegenerative diseases, including Parkinson's disease (PD). Thus far, mutations in more than 20 genes have been associated with PD. These genes encode for proteins involved in distinct intracellular pathways, complicating our understanding of the precise molecular mechanisms underlying the disease. Recent reports suggested that the...

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 Cell Death
Share to Endoplasmic Reticulum

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endosomes

Share to Lysosomes

Share to Parkinson Disease

Share to Protein Aggregation, Pathological

Share to Proton-Translocating ATPases

Source

Identifiers

PMID: 27282395
DOI: 10.1093/hmg/ddw147

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

A familial ATP13A2 mutation enhances alpha-synuclein aggregation and promotes cell death.PMID 27282395Read ↗

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

ATP13A2 Regulates Cellular α-Synuclein Multimerization, Membrane Association, and Externalization.Semantic proximity Read ↗

Alpha-synuclein at the intracellular and the extracellular side: functional and dysfunctional implications.Semantic proximity Read ↗

Mutant Atp13a2 proteins involved in parkinsonism are degraded by ER-associated degradation and sensitize cells to ER-stress induced cell death.Semantic proximity Read ↗

Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase.Semantic proximity Read ↗

The Roles of ATP13A2 Gene Mutations Leading to Abnormal Aggregation of α-Synuclein in Parkinson’s DiseaseSemantic proximity Read ↗

Deficiency of ATP13A2 leads to lysosomal dysfunction, α-synuclein accumulation, and neurotoxicity.Semantic proximity Read ↗

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

Alpha‐synuclein‐associated changes in PINK1‐PRKN‐mediated mitophagy are disease context dependentSemantic proximity Read ↗

Pathogenic effects of novel mutations in the P-type ATPase ATP13A2 (PARK9) causing Kufor-Rakeb syndrome, a form of early-onset parkinsonism.Semantic proximity Read ↗

Cellular α-synuclein pathology is associated with bioenergetic dysfunction in Parkinson’s iPSC-derived dopamine neuronsSemantic proximity Read ↗

ATP13A2/PARK9 regulates endo-/lysosomal cargo sorting and proteostasis through a novel PI(3, 5)P2-mediated scaffolding function.Semantic proximity Read ↗

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