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p(HGNC:SNCA)

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Entity

Name
SNCA
Namespace
hgnc
Namespace Version
20180906
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

Appears in Networks 12

The Ubiquitin Proteasome System in Neurodegenerative Diseases: Sometimes the Chicken, Sometimes the Egg v1.0.0

The Biology of Proteostasis in Aging and Disease v1.0.0

Alpha-synuclein oligomers: a new hope v1.0.0

Promoting the clearance of neurotoxic proteins in neurodegenerative disorders of ageing v1.0.0

TAU and Interaction Partners v1.2.5

TAU Interactions Section of NESTOR

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

Model systems of protein-misfolding diseases reveal chaperone modifiers of proteotoxicity v1.0.0

Alzheimer’s disease and the autophagic-lysosomal system v1.0.0

The Ubiquitin–Proteasome System and the Autophagic–Lysosomal System in Alzheimer Disease v1.0.0

Autophagy and the ubiquitin-proteasome system: collaborators in neuroprotection v1.0.0

New insights into the role of microRNAs and long noncoding RNAs in most common neurodegenerative diseases v1.0.0

mTOR-Related Brain Dysfunctions in Neuropsychiatric Disorders v1.0.0

In-Edges 51

a(MESH:"Inclusion Bodies") association p(HGNC:SNCA) View Subject | View Object

In addition, other proteins, e.g., alphaSYN (Waelter et al., 2001) and the transcriptional cofactor CREB binding protein (CBP) (Jiang et al., 2003),colocalize with the protein inclusions PubMed:14556719

Appears in Networks:

bp(HBP:"Alpha-synuclein Oligomerization") positiveCorrelation p(HGNC:SNCA) View Subject | View Object

Wild-type alphaSYN is monomeric, but at high concentration, it oligomerizes to beta-pleated sheets known as protofibrils PubMed:14556719

Appears in Networks:

p(HGNC:PRKN) decreases act(p(HGNC:SNCA)) View Subject | View Object

Of note is that overexpression of Parkin also suppresses alpha-synuclein (alphSYN) toxicity, suggesting that Parkin may play a role in regulating this protein as well (see below) PubMed:14556719

Appears in Networks:

p(HGNC:PRKN) regulates p(HGNC:SNCA) View Subject | View Object

Of note is that overexpression of Parkin also suppresses alpha-synuclein (alphSYN) toxicity, suggesting that Parkin may play a role in regulating this protein as well (see below) PubMed:14556719

Appears in Networks:

complex(p(HGNC:PSMC4), p(HGNC:SNCA)) hasComponent p(HGNC:SNCA) View Subject | View Object

Appears in Networks:

composite(p(HGNC:SNCA), p(HGNC:SNCAIP)) hasComponent p(HGNC:SNCA) View Subject | View Object

Appears in Networks:

p(HGNC:SNCAIP) association p(HGNC:SNCA) View Subject | View Object

Parkin also ubiquitinates Synphilin-1, a protein of hitherto unknown function that contains a coiled-coiled domain and an ATP/GTP binding motif and that associates with alphaSYN (Chung et al., 2001). PubMed:14556719

Appears in Networks:

p(HGNC:PRKN, var("?")) causesNoChange deg(p(HGNC:SNCA)) View Subject | View Object

Therefore, patients with AR-JP—who cannot degrade it because of the mutation in the Parkin E3 (see above)—develop neurodegeneration PubMed:14556719

Appears in Networks:
Annotations
MeSH
Parkinsonian Disorders

p(HGNC:USP19) increases sec(p(HGNC:SNCA)) View Subject | View Object

USP19 promoted the secretion of a-syn, suggesting that MAPS is an unconventional secretion pathway utilized by a-syn, particularly under conditions of proteasomal impairment, which has been repeatedly linked to Parkinson’s disease. PubMed:28803412

Appears in Networks:
Annotations
Confidence
High
MeSH
Microglia

path(MESH:"Parkinson Disease") association p(HGNC:SNCA) View Subject | View Object

Over the past two decades, the pre-synaptic protein alphasynuclein (a-syn) has been irrefutably tied to the neurodegenerative disorder Parkinson’s disease. PubMed:28803412

Appears in Networks:
Annotations
Confidence
Medium

a(CHEBI:"lithium(1+)") decreases p(HGNC:SNCA) View Subject | View Object

This mechanism may be involved in its promotion of autophagy, reduction in cel- lular levels of α-synuclein, SOD1, Htt and tau 126 , ame- lioration of motor function in a P301L mouse model of tauopathy 127 and slowing of disease progression in SOD1 mice 128 . PubMed:30116051

Appears in Networks:
Annotations
MeSH
Dopaminergic Neurons

a(CHEBI:ambroxol) increases deg(p(HGNC:SNCA)) View Subject | View Object

It increased expression of βGCase, normalized autophagy and accelerated degradation of α-synuclein in a stem cell model of dopaminergic neurons derived from patients with PD bearing mutations in βGCase 200 . PubMed:30116051

Appears in Networks:
Annotations
MeSH
Parkinson Disease

a(CHEBI:ambroxol) decreases p(HGNC:SNCA) View Subject | View Object

Ambroxol, which also decreased ER stress in D. mela- nogaster 201 , reduced α-synuclein levels in overexpress- ing, transgenic mice 202 . PubMed:30116051

Appears in Networks:

a(CHEBI:sirolimus) decreases p(HGNC:SNCA) View Subject | View Object

Enhancing auto- phagy with rapamycin reduced levels of α-synuclein, FUS and Htt 130–132 . PubMed:30116051

Appears in Networks:
Annotations
MeSH
Dopaminergic Neurons

bp(GO:"chaperone-mediated autophagy") increases deg(p(HGNC:SNCA)) View Subject | View Object

Tau, α-synuclein and TDP43 are substrates for CMA degradation, as are amyloid precursor protein (APP) but not amyloid-β fragment 42 (Aβ42) itself 3,45–47,48 . PubMed:30116051

Appears in Networks:

bp(GO:"chaperone-mediated autophagy") increases deg(p(HGNC:SNCA)) View Subject | View Object

CMA dysfunction in PD favours the accumulation of α- synuclein and leads to inactivation of the dopaminergic neuron survival factor, myocyte-specific enhancer factor 2D (MEF2D) 2,45,47,55 . PubMed:30116051

Appears in Networks:
Annotations
MeSH
Dopaminergic Neurons
MeSH
Parkinson Disease

p(HGNC:CAST) increases deg(p(HGNC:SNCA)) View Subject | View Object

Calpain inhibition by cal- pastatin or pharmacological agents also confers neuropro- tective effects in other NDA models, including improved clearance of tau, α-synuclein and SOD1 (REFS54,106,107) . PubMed:30116051

Appears in Networks:
Annotations
MeSH
Dopaminergic Neurons

p(HGNC:KLK6) increases deg(p(HGNC:SNCA)) View Subject | View Object

Finally, the extracellular and intracellular serine protease neurosin (also known as KLK6) cleaves α- synuclein. PubMed:30116051

Appears in Networks:

p(HGNC:LAMP2) increases deg(p(HGNC:SNCA)) View Subject | View Object

Nonetheless, overexpression of LAMP2A accelerated CMA-related clearance of α-synuclein and afforded pro- tection of dopaminergic neurons 45 , and several routes to potential pharmacological exploitation exist. PubMed:30116051

Appears in Networks:

p(HGNC:PLG) increases deg(p(HGNC:SNCA)) View Subject | View Object

Plasmin also degrades α-synuclein to retard intercellular spreading 262 . PubMed:30116051

Appears in Networks:

composite(p(HGNC:MAPT), p(HGNC:SNCA)) hasComponent p(HGNC:SNCA) View Subject | View Object

Appears in Networks:

bp(GO:"chaperone-mediated autophagy") association p(HGNC:SNCA) View Subject | View Object

Cuervo et al. have revealed a distinct interaction of wild-type and mutant α-synuclein proteins with CMA [64] PubMed:29758300

Appears in Networks:

bp(GO:"chaperone-mediated autophagy") increases deg(p(HGNC:SNCA)) View Subject | View Object

While wild-type α-synuclein protein efficiently clears via CMA, the pathogenic A53T and A30P variants remain bound to LAMP-2, blocking lysosomal degradation by preventing binding of other substrate complexes to the receptor [64]. PubMed:29758300

Appears in Networks:

bp(GO:"proteasome-mediated ubiquitin-dependent protein catabolic process") increases deg(p(HGNC:SNCA)) View Subject | View Object

These experimental differences may be attributed to the intricate interplay between the UPS and autophagy, as α-synuclein is degraded by both proteolytic systems [62,63]. PubMed:29758300

Appears in Networks:

bp(GO:autophagy) increases deg(p(HGNC:SNCA)) View Subject | View Object

These experimental differences may be attributed to the intricate interplay between the UPS and autophagy, as α-synuclein is degraded by both proteolytic systems [62,63]. PubMed:29758300

Appears in Networks:

complex(GO:"proteasome complex") increases deg(p(HGNC:SNCA)) View Subject | View Object

Since the initial finding of proteasome-dependent degradation of α-synuclein [58], significant efforts have been made to clarify the modes of α-synuclein metabolism PubMed:29758300

Appears in Networks:

path(MESH:"Alzheimer Disease") positiveCorrelation p(HGNC:SNCA) View Subject | View Object

While misfolding of Aβ peptide and hyperphosphorylation of tau are recognized as pathogenic mechanisms of AD, accumulation of α-synuclein, which is recognized more as a risk factor for Parkinson’s disease (PD), also plays a pathological role in AD [29]. PubMed:29758300

Appears in Networks:

complex(a(GO:"Lewy body"), p(HGNC:SNCA)) hasComponent p(HGNC:SNCA) View Subject | View Object

Appears in Networks:

p(HGNC:SNCA, pmod(Ub)) positiveCorrelation p(HGNC:SNCA) View Subject | View Object

In 1997, a-synuclein was shown to be the principal component of Lewy bodies (Spillantini et al. 1997). The accumulated a-synuclein was then shown to be ubiquitinated (Hasegawa et al. 2002). PubMed:22908190

Appears in Networks:

bp(GO:"chaperone-mediated autophagy") increases deg(p(HGNC:SNCA)) View Subject | View Object

CMA has also been found to contribute to the degradation of α-synuclein [29]. PubMed:18930136

Appears in Networks:

bp(GO:"chaperone-mediated autophagy") increases deg(p(HGNC:SNCA)) View Subject | View Object

For example, α-synuclein is degraded at least in part by CMA [29]. PubMed:18930136

Appears in Networks:

bp(GO:"chaperone-mediated autophagy") increases deg(p(HGNC:SNCA)) View Subject | View Object

The neuronal protein α-synuclein, for example, can be degraded by the UPS, macroautophagy and chaperone-mediated autophagy [26,29]. PubMed:18930136

Appears in Networks:

bp(GO:"proteasome-mediated ubiquitin-dependent protein catabolic process") increases deg(p(HGNC:SNCA)) View Subject | View Object

In the case of α-synuclein, for example, Webb et al. concluded that soluble forms of the disease protein are efficiently degraded by the UPS, while aggregated or oligomeric α-synuclein require autophagy for clearance [26]. PubMed:18930136

Appears in Networks:

bp(GO:"proteasome-mediated ubiquitin-dependent protein catabolic process") increases deg(p(HGNC:SNCA)) View Subject | View Object

The neuronal protein α-synuclein, for example, can be degraded by the UPS, macroautophagy and chaperone-mediated autophagy [26,29]. PubMed:18930136

Appears in Networks:

bp(GO:autophagy) increases deg(p(HGNC:SNCA)) View Subject | View Object

That neurodegenerative disease-causing proteins are frequently degraded by autophagy was demonstrated by a series of in vitro studies which showed that pharmacological induction or inhibition of macroautophagy alters the rate of turnover of a number of disease-related proteins including polyglutamine-expanded proteins, polyalanine-expanded proteins, as well as wild type and mutant forms of α-synuclein [25,26] PubMed:18930136

Appears in Networks:

bp(GO:macroautophagy) increases deg(p(HGNC:SNCA)) View Subject | View Object

The neuronal protein α-synuclein, for example, can be degraded by the UPS, macroautophagy and chaperone-mediated autophagy [26,29]. PubMed:18930136

Appears in Networks:

a(GO:"Lewy body", loc(MESH:"Dopaminergic Neurons")) positiveCorrelation p(HGNC:SNCA) View Subject | View Object

The accumulation of α‐synuclein gives rise to the formation of a nucleus for the accumulation of other proteins, which ultimately leads to the formation of Lewy bodies (within the dopamine secreting cells). PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

bp(GO:"synaptic transmission, dopaminergic") association p(HGNC:SNCA) View Subject | View Object

This protein is commonly found in the presynaptic terminus and is a factor in the transmission of synaptic dopaminergic neurons. PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

g(HGNC:"MIR153-1") regulates p(HGNC:SNCA) View Subject | View Object

Two miRNAs that play an important role in regulating α‐synuclein expression are miR‐153 and miR‐7 PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

g(HGNC:"MIR153-1") regulates p(HGNC:SNCA) View Subject | View Object

That is, in the event that miRNAs regulating α‐synuclein that reduce its accumulation (including miR‐153, miR‐7, miR‐132, and miR‐133‐b) are decreased, the progression of PD will be accelerated. PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

complex(g(HGNC:"MIR153-1"), r(HGNC:SNCA)) decreases act(p(HGNC:SNCA)) View Subject | View Object

These two miRNAs downregulate the α‐synuclein by binding to the 3′‐UTR portion in the mRNA transcribed from SNCA. PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

complex(g(HGNC:"MIR153-1"), r(HGNC:SNCA)) decreases p(HGNC:SNCA) View Subject | View Object

In an experiment conducted to investigate this, pre‐miR‐34b and premiR‐ 34c were introduced into human dopaminergic SH‐SY5S cells and it was found that the amount of α‐synuclein protein had decreased significantly. PubMed:30663117

Appears in Networks:
Annotations
Experimental Factor Ontology (EFO)
SH-SY5Y
MeSH
Parkinson Disease

complex(g(HGNC:"MIR7-1"), r(HGNC:SNCA)) decreases act(p(HGNC:SNCA)) View Subject | View Object

These two miRNAs downregulate the α‐synuclein by binding to the 3′‐UTR portion in the mRNA transcribed from SNCA. PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

complex(g(HGNC:"MIR7-1"), r(HGNC:SNCA)) decreases p(HGNC:SNCA) View Subject | View Object

In an experiment conducted to investigate this, pre‐miR‐34b and premiR‐ 34c were introduced into human dopaminergic SH‐SY5S cells and it was found that the amount of α‐synuclein protein had decreased significantly. PubMed:30663117

Appears in Networks:
Annotations
Experimental Factor Ontology (EFO)
SH-SY5Y
MeSH
Parkinson Disease

g(HGNC:"MIR7-1") regulates p(HGNC:SNCA) View Subject | View Object

Two miRNAs that play an important role in regulating α‐synuclein expression are miR‐153 and miR‐7 PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

g(HGNC:"MIR7-1") decreases p(HGNC:SNCA) View Subject | View Object

It has been shown that miR‐7 inhibition increases the expression of α‐synuclein PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

g(HGNC:"MIR7-1") regulates p(HGNC:SNCA) View Subject | View Object

That is, in the event that miRNAs regulating α‐synuclein that reduce its accumulation (including miR‐153, miR‐7, miR‐132, and miR‐133‐b) are decreased, the progression of PD will be accelerated. PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

g(HGNC:MIR132) regulates p(HGNC:SNCA) View Subject | View Object

miR‐132 is another miRNA that has a regulatory effect on α‐synuclein. The downregulation of this miRNA results in the accumulation of α‐synuclein protein PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

g(HGNC:MIR132) decreases p(HGNC:SNCA) View Subject | View Object

miR‐132 is another miRNA that has a regulatory effect on α‐synuclein. The downregulation of this miRNA results in the accumulation of α‐synuclein protein PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

g(HGNC:MIR132) regulates p(HGNC:SNCA) View Subject | View Object

That is, in the event that miRNAs regulating α‐synuclein that reduce its accumulation (including miR‐153, miR‐7, miR‐132, and miR‐133‐b) are decreased, the progression of PD will be accelerated. PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

g(HGNC:MIR133B) regulates p(HGNC:SNCA) View Subject | View Object

That is, in the event that miRNAs regulating α‐synuclein that reduce its accumulation (including miR‐153, miR‐7, miR‐132, and miR‐133‐b) are decreased, the progression of PD will be accelerated. PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

Out-Edges 33

p(HGNC:SNCA) hasVariant p(HGNC:SNCA, var("p.Ala30Pro")) View Subject | View Object

Appears in Networks:

p(HGNC:SNCA) hasVariant p(HGNC:SNCA, var("p.Ala53Thr")) View Subject | View Object

Appears in Networks:

p(HGNC:SNCA) association bp(GO:"chaperone-mediated autophagy") View Subject | View Object

Cuervo et al. have revealed a distinct interaction of wild-type and mutant α-synuclein proteins with CMA [64] PubMed:29758300

Appears in Networks:

p(HGNC:SNCA) hasVariant p(HGNC:SNCA, pmod(Glyco)) View Subject | View Object

Appears in Networks:

p(HGNC:SNCA) hasVariant p(HGNC:SNCA, pmod(OGlyco)) View Subject | View Object

Appears in Networks:

p(HGNC:SNCA) hasVariant p(HGNC:SNCA, pmod(Ub)) View Subject | View Object

Appears in Networks:

p(HGNC:SNCA) hasVariant p(HGNC:SNCA, var("?")) View Subject | View Object

Appears in Networks:

p(HGNC:SNCA) association p(HGNC:SNCAIP) View Subject | View Object

Parkin also ubiquitinates Synphilin-1, a protein of hitherto unknown function that contains a coiled-coiled domain and an ATP/GTP binding motif and that associates with alphaSYN (Chung et al., 2001). PubMed:14556719

Appears in Networks:

p(HGNC:SNCA) regulates bp(GO:"dopamine secretion, neurotransmission") View Subject | View Object

alphaSYN is a small, 140 amino acid residue protein that is thought to regulate/participate in dopamine neurotransmission/release via effects on vesicular storage PubMed:14556719

Appears in Networks:

p(HGNC:SNCA) regulates bp(GO:"dopamine secretion") View Subject | View Object

alphaSYN is a small, 140 amino acid residue protein that is thought to regulate/participate in dopamine neurotransmission/release via effects on vesicular storage PubMed:14556719

Appears in Networks:

p(HGNC:SNCA) positiveCorrelation bp(HBP:"Alpha-synuclein Oligomerization") View Subject | View Object

Wild-type alphaSYN is monomeric, but at high concentration, it oligomerizes to beta-pleated sheets known as protofibrils PubMed:14556719

Appears in Networks:

p(HGNC:SNCA) increases bp(GO:"apoptotic process") View Subject | View Object

Overexpression of wild-type, but in particular mutant alphaSYN in many cell types but not in all, induces apoptosis or sensitizes the cells to toxic agents, including proteasome inhibitors (see, for example, Lee et al.,2001a). PubMed:14556719

Appears in Networks:

act(p(HGNC:SNCA)) increases p(HGNC:SNCAIP, pmod(Ub)) View Subject | View Object

Instead, impairment of alphaSYN function may disturb ubiquitination of alphaSYN-associated proteins, such as Synphilin (Chung et al., 2001) and tyrosine hydroxylase (Doskeland and Flatmark, 2002), and thereby perturb neuronal homeostasis PubMed:14556719

Appears in Networks:

act(p(HGNC:SNCA)) increases p(HGNC:TH, pmod(Ub)) View Subject | View Object

Instead, impairment of alphaSYN function may disturb ubiquitination of alphaSYN-associated proteins, such as Synphilin (Chung et al., 2001) and tyrosine hydroxylase (Doskeland and Flatmark, 2002), and thereby perturb neuronal homeostasis PubMed:14556719

Appears in Networks:

act(p(HGNC:SNCA)) regulates bp(GO:"homeostatic process") View Subject | View Object

Instead, impairment of alphaSYN function may disturb ubiquitination of alphaSYN-associated proteins, such as Synphilin (Chung et al., 2001) and tyrosine hydroxylase (Doskeland and Flatmark, 2002), and thereby perturb neuronal homeostasis PubMed:14556719

Appears in Networks:
Annotations
MeSH
Neurons

p(HGNC:SNCA) association a(MESH:"Inclusion Bodies") View Subject | View Object

In addition, other proteins, e.g., alphaSYN (Waelter et al., 2001) and the transcriptional cofactor CREB binding protein (CBP) (Jiang et al., 2003),colocalize with the protein inclusions PubMed:14556719

Appears in Networks:

p(HGNC:SNCA) decreases bp(GO:autophagy) View Subject | View Object

In contrast, α-synuclein overexpression impairs autophagy in mammalian cells and mice through reduced expression of RAB1A, thereby inhibiting autophagosome formation (88). PubMed:25784053

Appears in Networks:

p(HGNC:SNCA) decreases p(HGNC:RAB1A) View Subject | View Object

In contrast, α-synuclein overexpression impairs autophagy in mammalian cells and mice through reduced expression of RAB1A, thereby inhibiting autophagosome formation (88). PubMed:25784053

Appears in Networks:

p(HGNC:SNCA) hasVariant p(HGNC:SNCA, var("p.Ala53Glu")) View Subject | View Object

Appears in Networks:

p(HGNC:SNCA) hasVariant p(HGNC:SNCA, var("p.Glu46Lys")) View Subject | View Object

Appears in Networks:

p(HGNC:SNCA) hasVariant p(HGNC:SNCA, var("p.Gly51Asp")) View Subject | View Object

Appears in Networks:

p(HGNC:SNCA) hasVariant p(HGNC:SNCA, var("p.His50Gln")) View Subject | View Object

Appears in Networks:

p(HGNC:SNCA) association path(MESH:"Parkinson Disease") View Subject | View Object

Over the past two decades, the pre-synaptic protein alphasynuclein (a-syn) has been irrefutably tied to the neurodegenerative disorder Parkinson’s disease. PubMed:28803412

Appears in Networks:
Annotations
Confidence
Medium

p(HGNC:SNCA) hasVariant p(HGNC:SNCA, pmod(Sumo)) View Subject | View Object

Appears in Networks:

p(HGNC:SNCA) hasVariant p(HGNC:SNCA, pmod(HBP:misfolding)) View Subject | View Object

Appears in Networks:

p(HGNC:SNCA) positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

While misfolding of Aβ peptide and hyperphosphorylation of tau are recognized as pathogenic mechanisms of AD, accumulation of α-synuclein, which is recognized more as a risk factor for Parkinson’s disease (PD), also plays a pathological role in AD [29]. PubMed:29758300

Appears in Networks:

p(HGNC:SNCA) increases path(MESH:"Alzheimer Disease") View Subject | View Object

Recent clinical and immunohistochemistry studies demonstrate the contribution of α-synuclein in the development of AD pathology PubMed:29758300

Appears in Networks:

p(HGNC:SNCA) increases path(MESH:"Parkinson Disease") View Subject | View Object

While misfolding of Aβ peptide and hyperphosphorylation of tau are recognized as pathogenic mechanisms of AD, accumulation of α-synuclein, which is recognized more as a risk factor for Parkinson’s disease (PD), also plays a pathological role in AD [29]. PubMed:29758300

Appears in Networks:

p(HGNC:SNCA) positiveCorrelation p(HGNC:SNCA, pmod(Ub)) View Subject | View Object

In 1997, a-synuclein was shown to be the principal component of Lewy bodies (Spillantini et al. 1997). The accumulated a-synuclein was then shown to be ubiquitinated (Hasegawa et al. 2002). PubMed:22908190

Appears in Networks:

p(HGNC:SNCA) increases complex(a(GO:"Lewy body"), p(HGNC:SNCA)) View Subject | View Object

In 1997, a-synuclein was shown to be the principal component of Lewy bodies (Spillantini et al. 1997). The accumulated a-synuclein was then shown to be ubiquitinated (Hasegawa et al. 2002). PubMed:22908190

Appears in Networks:

p(HGNC:SNCA) association bp(GO:"synaptic transmission, dopaminergic") View Subject | View Object

This protein is commonly found in the presynaptic terminus and is a factor in the transmission of synaptic dopaminergic neurons. PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

p(HGNC:SNCA) positiveCorrelation a(GO:"Lewy body", loc(MESH:"Dopaminergic Neurons")) View Subject | View Object

The accumulation of α‐synuclein gives rise to the formation of a nucleus for the accumulation of other proteins, which ultimately leads to the formation of Lewy bodies (within the dopamine secreting cells). PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

p(HGNC:SNCA) hasVariant p(HGNC:SNCA, pmod(HBP:misfolded)) View Subject | View Object

Appears in Networks:

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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.