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a(HBP:"alpha-synuclein aggregates")

Equivalencies: 0 | Classes: 0 | Children: 0 | Explore

Entity

Name
alpha-synuclein aggregates
Namespace
HBP
Namespace Version
20190126
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/77c0796c3ca82a80cb0eaf1c8380d6ccd7f323af/export/hbp-names.belns

Appears in Networks 6

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

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

Molecular Chaperone Functions in Protein Folding and Proteostasis 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

In-Edges 15

a(HBP:"alpha-synuclein fibrils") increases a(HBP:"alpha-synuclein aggregates") View Subject | View Object

The protofibrils can further aggregate and precipitate as amyloid fibrils that are present in Lewy bodies, the hallmark of sporadic, late-onset PD PubMed:14556719

Appears in Networks:

a(MESH:"Lewy Bodies") association a(HBP:"alpha-synuclein aggregates") View Subject | View Object

The protofibrils can further aggregate and precipitate as amyloid fibrils that are present in Lewy bodies, the hallmark of sporadic, late-onset PD PubMed:14556719

Appears in Networks:

complex(a(HBP:"alpha-synuclein aggregates"), p(HGNC:PSMC4)) hasComponent a(HBP:"alpha-synuclein aggregates") View Subject | View Object

Appears in Networks:

path(MESH:"Parkinsonian Disorders") positiveCorrelation a(HBP:"alpha-synuclein aggregates") View Subject | View Object

AR-JP is characterized by lack of LBs and alphaSYN aggregates PubMed:14556719

Appears in Networks:

p(FPLX:HSPA) decreases a(HBP:"alpha-synuclein aggregates") View Subject | View Object

Although HSP70 was not identified as a modifier of α -synuclein in the screen studies we selected, directed overexpression of HSP70 has been shown to reduce α -synuclein-related proteotoxicity, supporting a central role for HSP70 in diseases of protein misfolding (Auluck et al., 2002). PubMed:27491084

Appears in Networks:

path(MESH:"Alzheimer Disease") association a(HBP:"alpha-synuclein aggregates") View Subject | View Object

While AD is generally considered a disorder with two proteinopathies, other protein aggregates are also seen in AD, like α-synuclein PubMed:29758300

Appears in Networks:

path(MESH:"Alzheimer Disease") positiveCorrelation a(HBP:"alpha-synuclein aggregates") View Subject | View Object

First identified as a nonamyloid component of Aβ plaques in the AD brain, α-synuclein aggregates are detected in the majority of the brains of patients with AD [56,57]. PubMed:29758300

Appears in Networks:
Annotations
MeSH
Brain

p(FPLX:HSPA) decreases a(HBP:"alpha-synuclein aggregates") View Subject | View Object

This approach is based on multiple lines of evidence demonstrating that overexpression of chaperones such as Hsp70 and Hsp40 prevents the aggregation and toxicity of huntingtin and α-synuclein (38, 231–234). PubMed:23746257

Appears in Networks:

p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") decreases a(HBP:"alpha-synuclein aggregates") View Subject | View Object

This approach is based on multiple lines of evidence demonstrating that overexpression of chaperones such as Hsp70 and Hsp40 prevents the aggregation and toxicity of huntingtin and α-synuclein (38, 231–234). PubMed:23746257

Appears in Networks:

bp(GO:autophagy) increases a(HBP:"alpha-synuclein aggregates") 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:

a(MESH:"HSP70 Heat-Shock Proteins") negativeCorrelation a(HBP:"alpha-synuclein aggregates") View Subject | View Object

miR‐16‐1 is a case in point that has been seen in some patients with PD.It has been shown to decrease the expression of Hsp70 by increasing the aggregation of the α‐synuclein protein PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

a(MESH:"HSP70 Heat-Shock Proteins") decreases a(HBP:"alpha-synuclein aggregates") View Subject | View Object

By linking to the 3′‐UTR sequence of Hsp70 mRNA, miR‐16‐1 configures Hsp70. Its increase reduces the Hsp70, which in turn boosts the aggregation of α‐synuclein protein, and this increases the incidence of PD. PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

g(NCBIGENE:406950) increases a(HBP:"alpha-synuclein aggregates") View Subject | View Object

miR‐16‐1 is a case in point that has been seen in some patients with PD.It has been shown to decrease the expression of Hsp70 by increasing the aggregation of the α‐synuclein protein PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

p(HGNC:PARK7) decreases a(HBP:"alpha-synuclein aggregates") View Subject | View Object

The PARK 7 gene on chromosome 1 is responsible for coding the DJ‐1 protein. This protein acts as chaperon in the neurons, thus preventing the aggregation of the α‐synuclein protein PubMed:30663117

Appears in Networks:
Annotations
MeSH
Neurons
MeSH
Parkinson Disease

path(MESH:"Parkinson Disease") association a(HBP:"alpha-synuclein aggregates") View Subject | View Object

PD is a proteinopathy characterized by the misfolding and aggregation of α‐synuclein synucleinopathy, which leads to the destruction of dopaminergic neurons within substantia nigra pars compacta. PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

Out-Edges 9

a(HBP:"alpha-synuclein aggregates") association a(MESH:"Lewy Bodies") View Subject | View Object

The protofibrils can further aggregate and precipitate as amyloid fibrils that are present in Lewy bodies, the hallmark of sporadic, late-onset PD PubMed:14556719

Appears in Networks:

a(HBP:"alpha-synuclein aggregates") positiveCorrelation path(MESH:"Parkinsonian Disorders") View Subject | View Object

AR-JP is characterized by lack of LBs and alphaSYN aggregates PubMed:14556719

Appears in Networks:

a(HBP:"alpha-synuclein aggregates") decreases bp(GO:"proteasome-mediated ubiquitin-dependent protein catabolic process") View Subject | View Object

Thus, aggregation, which is the primary event, may lead to secondary damage by inhibiting the UPS (Bence et al., 2001). PubMed:14556719

Appears in Networks:

a(HBP:"alpha-synuclein aggregates") association path(MESH:"Alzheimer Disease") View Subject | View Object

While AD is generally considered a disorder with two proteinopathies, other protein aggregates are also seen in AD, like α-synuclein PubMed:29758300

Appears in Networks:

a(HBP:"alpha-synuclein aggregates") positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

First identified as a nonamyloid component of Aβ plaques in the AD brain, α-synuclein aggregates are detected in the majority of the brains of patients with AD [56,57]. PubMed:29758300

Appears in Networks:
Annotations
MeSH
Brain

a(HBP:"alpha-synuclein aggregates") association path(MESH:"Parkinson Disease") View Subject | View Object

PD is a proteinopathy characterized by the misfolding and aggregation of α‐synuclein synucleinopathy, which leads to the destruction of dopaminergic neurons within substantia nigra pars compacta. PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

a(HBP:"alpha-synuclein aggregates") increases path(MESH:"Parkinson Disease") View Subject | View Object

By linking to the 3′‐UTR sequence of Hsp70 mRNA, miR‐16‐1 configures Hsp70. Its increase reduces the Hsp70, which in turn boosts the aggregation of α‐synuclein protein, and this increases the incidence of PD. PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

a(HBP:"alpha-synuclein aggregates") decreases a(MESH:"Dopaminergic Neurons") View Subject | View Object

PD is a proteinopathy characterized by the misfolding and aggregation of α‐synuclein synucleinopathy, which leads to the destruction of dopaminergic neurons within substantia nigra pars compacta. PubMed:30663117

Appears in Networks:
Annotations
MeSH
Pars Compacta
MeSH
Parkinson Disease

a(HBP:"alpha-synuclein aggregates") negativeCorrelation a(MESH:"HSP70 Heat-Shock Proteins") View Subject | View Object

miR‐16‐1 is a case in point that has been seen in some patients with PD.It has been shown to decrease the expression of Hsp70 by increasing the aggregation of the α‐synuclein protein PubMed:30663117

Appears in Networks:
Annotations
MeSH
Parkinson Disease

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BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

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.