Glutathione s-transferase omega 1 activity is sufficient to suppress neurodegeneration in a Drosophila model of Parkinson disease.
Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions.
Wild-type but not Parkinson's disease-related ala-53 --> Thr mutant alpha -synuclein protects neuronal cells from apoptotic stimuli.
Conformational properties of alpha-synuclein in its free and lipid-associated states.
Ca2+ binding to alpha-synuclein regulates ligand binding and oligomerization.
Tubulin seeds alpha-synuclein fibril formation.
Magnesium inhibits spontaneous and iron-induced aggregation of alpha-synuclein.
A role for alpha-synuclein in the regulation of dopamine biosynthesis.
Synphilin-1 is developmentally localized to synaptic terminals, and its association with synaptic vesicles is modulated by alpha-synuclein.
Analysis of synphilin-1 and synuclein interactions by yeast two-hybrid beta-galactosidase liquid assay.
Mutant and wild-type alpha-synuclein interact with mitochondrial cytochrome C oxidase.
Evidence that alpha-synuclein functions as a negative regulator of Ca(++)-dependent alpha-granule release from human platelets.
Upregulation of alpha-synuclein by lipopolysaccharide and interleukin-1 in human macrophages.
Nuclear localization of alpha-synuclein and its interaction with histones.
Modulation of dopamine transporter function by alpha-synuclein is altered by impairment of cell adhesion and by induction of oxidative stress.
Abnormal alpha-synuclein interactions with rab3a and rabphilin in diffuse Lewy body disease.
Lipid rafts mediate the synaptic localization of alpha-synuclein.
DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation.
p25alpha Stimulates alpha-synuclein aggregation and is co-localized with aggregated alpha-synuclein in alpha-synucleinopathies.
Fluorescence studies suggest a role for alpha-synuclein in the phosphatidylinositol lipid signaling pathway.
Heat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar species.
Proteolytic cleavage of extracellular secreted {alpha}-synuclein via matrix metalloproteinases.
Molecular motors implicated in the axonal transport of tau and alpha-synuclein.
Dequalinium-induced protofibril formation of alpha-synuclein.
Synphilin-1A: an aggregation-prone isoform of synphilin-1 that causes neuronal death and is present in aggregates from alpha-synucleinopathy patients.
Interactions between fatty acids and alpha-synuclein.
Acceleration of alpha-synuclein aggregation by homologous peptides.
Modulation of the trafficking of the human serotonin transporter by human alpha-synuclein.
Alpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity.
Interaction of TPPP/p25 protein with glyceraldehyde-3-phosphate dehydrogenase and their co-localization in Lewy bodies.
Attenuation of the norepinephrine transporter activity and trafficking via interactions with alpha-synuclein.
Relationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicity.
alpha-Synuclein and its disease-related mutants interact differentially with the microtubule protein tau and associate with the actin cytoskeleton.
Regulated interactions of the norepineprhine transporter by the actin and microtubule cytoskeletons.
FK506 binding protein 12 differentially accelerates fibril formation of wild type alpha-synuclein and its clinical mutants A30P or A53T.
Proteomics analysis identifies phosphorylation-dependent alpha-synuclein protein interactions.
Interactions between Hsp70 and the hydrophobic core of alpha-synuclein inhibit fibril assembly.
Alpha-synuclein and polyunsaturated fatty acids promote clathrin-mediated endocytosis and synaptic vesicle recycling.
Evidence that alpha-synuclein does not inhibit phospholipase D.
Fluorescence microscopy and 3D image reconstruction of cytokine initiated disruption of the Parkinson disease associated proteins alpha-synuclein, tau and ubiquitin in cultured glial cells.
Functional dissection of the alpha-synuclein promoter: transcriptional regulation by ZSCAN21 and ZNF219.
Pre-fibrillar alpha-synuclein variants with impaired beta-structure increase neurotoxicity in Parkinson's disease models.
Interaction with synphilin-1 promotes inclusion formation of alpha-synuclein: mechanistic insights and pathological implication.
Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by Hip.
Association of metallothionein-III with oligodendroglial cytoplasmic inclusions in multiple system atrophy.
A combinatorial NMR and EPR approach for evaluating the structural ensemble of partially folded proteins.
Chaperone-mediated autophagy markers in Parkinson disease brains.
Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro.
Parkinsonian neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and alpha-synuclein mutations promote Tau protein phosphorylation at Ser262 and destabilize microtubule cytoskeleton in vitro.
Coordination features and affinity of the Cu²+ site in the α-synuclein protein of Parkinson's disease.
Redox activity of α-synuclein-Cu is silenced by Zn₇-metallothionein-3.
Ubiquitinylation of α-synuclein by carboxyl terminus Hsp70-interacting protein (CHIP) is regulated by Bcl-2-associated athanogene 5 (BAG5).
Inhibition and disaggregation of α-synuclein oligomers by natural polyphenolic compounds.
Human α-synuclein modulates vesicle trafficking through its interaction with prenylated Rab acceptor protein 1.
α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation.
Stimulatory effect of α-synuclein on the tau-phosphorylation by GSK-3β.
α-Synuclein modifies huntingtin aggregation in living cells.
Redistribution of DAT/α-synuclein complexes visualized by "in situ" proximity ligation assay in transgenic mice modelling early Parkinson's disease.
α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer.
SERF protein is a direct modifier of amyloid fiber assembly.
LRRK2 interactions with α-synuclein in Parkinson's disease brains and in cell models.
α-Synuclein-mediated defense against oxidative stress via modulation of glutathione peroxidase.
α-Synuclein as an intrinsically disordered monomer--fact or artefact?
Polo-like kinase 2 regulates selective autophagic α-synuclein clearance and suppresses its toxicity in vivo.
The role of oxidative stress in Parkinson's disease.
The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes.
Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies.
c-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson's disease.
Reduced glucocerebrosidase is associated with increased α-synuclein in sporadic Parkinson's disease.
The chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicity.
The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity.
α-Synuclein interacts with the switch region of Rab8a in a Ser129 phosphorylation-dependent manner.
Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network.
Differences in the binding of copper(I) to α- and β-synuclein.
Parkinson's disease genes VPS35 and EIF4G1 interact genetically and converge on α-synuclein.
Molecular determinants of α-synuclein mutants' oligomerization and membrane interactions.
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation.
Direct visualization of alpha-synuclein oligomers reveals previously undetected pathology in Parkinson's disease brain.
Dopamine Transporter Activity Is Modulated by α-Synuclein.
α-synuclein interacts with SOD1 and promotes its oligomerization.
Effects of different isoforms of apoE on aggregation of the α-synuclein protein implicated in Parkinson's disease.
Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1.
Activation of tyrosine kinase c-Abl contributes to α-synuclein-induced neurodegeneration.
α-Synuclein is a Novel Microtubule Dynamase.
Challenging drug target for Parkinson's disease: Pathological complex of the chameleon TPPP/p25 and alpha-synuclein proteins.
α-Synuclein promotes dilation of the exocytotic fusion pore.
α-Synuclein Interacts with Lipoproteins in Plasma.
α-synuclein expression from a single copy transgene increases sensitivity to stress and accelerates neuronal loss in genetic models of Parkinson's disease.
Soluble α-synuclein facilitates priming and fusion by releasing Ca(2+) from the thapsigargin-sensitive Ca(2+) pool in PC12 cells.
Increased Aggregation Tendency of Alpha-Synuclein in a Fully Disordered Protein Complex.
α-synuclein-lipoprotein interactions and elevated ApoE level in cerebrospinal fluid from Parkinson's disease patients.
Structures of α-synuclein filaments from multiple system atrophy.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
DEAD-box RNA helicase Dbp4/DDX10 is an enhancer of α-synuclein toxicity and oligomerization.
Interactions between SARS-CoV-2 N-Protein and α-Synuclein Accelerate Amyloid Formation.
Tau interactome maps synaptic and mitochondrial processes associated with neurodegeneration.
Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease.
NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded.
SNCAIP binds alpha-synuclein
SIAH1:UBE2L6:Ubiquitin binds SNCA
USP9X deubiquitinates Ub-SNCA
SIAH1:UBE2L6:Ubiquitin ubiquitinates SNCA
Ub-SNCA dissociates from the conjugating enzyme
Amyloid fibrils have additional components
Amyloid precursor proteins form ordered fibrils
p-PKR dimer phosphorylates SNCA
Alpha-synuclein immunoreactivity in normal and neoplastic Schwann cells.