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a(MESH:"HSP70 Heat-Shock Proteins")

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Entity

Name
HSP70 Heat-Shock Proteins
Namespace
MeSH
Namespace Version
20181007
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/01c9daa61012b37dd0a1bc962521ba51a15b38f1/external/mesh-names.belns

Appears in Networks 2

Carboxy terminus heat shock protein 70 interacting protein reduces tau-associated degenerative changes v1.0.0

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

In-Edges 11

complex(a(MESH:"HSP70 Heat-Shock Proteins"), p(FPLX:HSP90), p(HGNC:STUB1)) hasComponent a(MESH:"HSP70 Heat-Shock Proteins") View Subject | View Object

Appears in Networks:

complex(a(MESH:"HSP70 Heat-Shock Proteins"), p(HGNC:STUB1)) hasComponent a(MESH:"HSP70 Heat-Shock Proteins") View Subject | View Object

Appears in Networks:

complex(a(MESH:"HSP70 Heat-Shock Proteins"), p(HGNC:STUB1), p(MESH:Proteins, pmod(HBP:misfolded))) hasComponent a(MESH:"HSP70 Heat-Shock Proteins") View Subject | View Object

Appears in Networks:

composite(p(HBP:"4R tau", var("p.Lys280del")), p(HGNC:STUB1)) causesNoChange a(MESH:"HSP70 Heat-Shock Proteins") View Subject | View Object

Co-transfection of CHIP with 4R-tau leads to a significant increase in Hsp70 levels, however this is not the case with wither tauC3 or K18DK280 constructs (Supplementary Fig. 2) suggesting that increased HSP70 protein levels are not necessary for the observed reduction in tau levels. PubMed:25374103

Appears in Networks:

composite(p(HBP:"Tau C3"), p(HGNC:STUB1)) causesNoChange a(MESH:"HSP70 Heat-Shock Proteins") View Subject | View Object

Co-transfection of CHIP with 4R-tau leads to a significant increase in Hsp70 levels, however this is not the case with wither tauC3 or K18DK280 constructs (Supplementary Fig. 2) suggesting that increased HSP70 protein levels are not necessary for the observed reduction in tau levels. PubMed:25374103

Appears in Networks:

composite(p(HBP:"Tau isoform F (441 aa)"), p(HGNC:STUB1)) increases a(MESH:"HSP70 Heat-Shock Proteins") View Subject | View Object

Co-transfection of CHIP with 4R-tau leads to a significant increase in Hsp70 levels, however this is not the case with wither tauC3 or K18DK280 constructs (Supplementary Fig. 2) suggesting that increased HSP70 protein levels are not necessary for the observed reduction in tau levels. PubMed:25374103

Appears in Networks:

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

complex(a(MESH:"HSP70 Heat-Shock Proteins"), g(NCBIGENE:406950)) hasComponent a(MESH:"HSP70 Heat-Shock Proteins") View Subject | View Object

Appears in Networks:

complex(a(MESH:"HSP70 Heat-Shock Proteins"), g(NCBIGENE:406950)) regulates act(a(MESH:"HSP70 Heat-Shock Proteins")) 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) decreases 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

g(NCBIGENE:406950) negativeCorrelation a(MESH:"HSP70 Heat-Shock Proteins") 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

Out-Edges 4

a(MESH:"HSP70 Heat-Shock Proteins") increases deg(p(HGNC:MAPT, pmod(HBP:misfolded))) View Subject | View Object

Several publications suggest that molecular chaperones, e.g., heat shock protein 70 and 90 (Hsp70, Hsp90) play a fundamental role in the clearance of misfolded proteins including tau [12]. PubMed:25374103

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

a(MESH:"HSP70 Heat-Shock Proteins") negativeCorrelation g(NCBIGENE:406950) 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

About

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.