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a(HBP:"huntingtin aggregates")

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Entity

Name
huntingtin aggregates
Namespace
HBP
Namespace Version
20190206
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/3c85897632afa791ac78fb3aa2e392963ab155b1/export/hbp-names.belns

Appears in Networks 6

A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease. v1.0.0

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

Molecular Chaperone Functions in Protein Folding and Proteostasis v1.0.0

Protein aggregation can inhibit clathrin-mediated endocytosis by chaperone competition v1.0.0

mTOR-Related Brain Dysfunctions in Neuropsychiatric Disorders v1.0.0

In-Edges 18

a(PUBCHEM:1560402) decreases a(HBP:"huntingtin aggregates") View Subject | View Object

In addition, SMER-10, -18, and -28 were effective at suppressing mHTT aggregation and toxicity in COS-7 cells and flies (146). PubMed:25784053

Appears in Networks:
Annotations
Cell Ontology (CL)
motor neuron

a(PUBCHEM:799645) decreases a(HBP:"huntingtin aggregates") View Subject | View Object

In addition, SMER-10, -18, and -28 were effective at suppressing mHTT aggregation and toxicity in COS-7 cells and flies (146). PubMed:25784053

Appears in Networks:
Annotations
Cell Ontology (CL)
motor neuron

p(FPLX:"CCT_complex") increases a(HBP:"huntingtin aggregates") View Subject | View Object

These included all subunits of the CCT/TRiC complex (except CCT5); HSP40 and HSP70 family members DNAJA1 (HDJ-2), DNAJA4, HSPA8 (HSC70), and HSPA14 (Figures 5B and 5C); and the TPR-domain APC/C subunits CDC23 and CDC27 that, upon knockdown, led to significantly elevated aggregation (Figure S5B). PubMed:25437566

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease
MeSH
Huntington Disease
MeSH
Parkinson Disease

p(HGNC:CCT5) causesNoChange a(HBP:"huntingtin aggregates") View Subject | View Object

These included all subunits of the CCT/TRiC complex (except CCT5); HSP40 and HSP70 family members DNAJA1 (HDJ-2), DNAJA4, HSPA8 (HSC70), and HSPA14 (Figures 5B and 5C); and the TPR-domain APC/C subunits CDC23 and CDC27 that, upon knockdown, led to significantly elevated aggregation (Figure S5B). PubMed:25437566

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease
MeSH
Huntington Disease
MeSH
Parkinson Disease

p(HGNC:CDC23) increases a(HBP:"huntingtin aggregates") View Subject | View Object

These included all subunits of the CCT/TRiC complex (except CCT5); HSP40 and HSP70 family members DNAJA1 (HDJ-2), DNAJA4, HSPA8 (HSC70), and HSPA14 (Figures 5B and 5C); and the TPR-domain APC/C subunits CDC23 and CDC27 that, upon knockdown, led to significantly elevated aggregation (Figure S5B). PubMed:25437566

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease
MeSH
Huntington Disease
MeSH
Parkinson Disease

p(HGNC:CDC27) increases a(HBP:"huntingtin aggregates") View Subject | View Object

These included all subunits of the CCT/TRiC complex (except CCT5); HSP40 and HSP70 family members DNAJA1 (HDJ-2), DNAJA4, HSPA8 (HSC70), and HSPA14 (Figures 5B and 5C); and the TPR-domain APC/C subunits CDC23 and CDC27 that, upon knockdown, led to significantly elevated aggregation (Figure S5B). PubMed:25437566

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease
MeSH
Huntington Disease
MeSH
Parkinson Disease

p(HGNC:DNAJA1) increases a(HBP:"huntingtin aggregates") View Subject | View Object

These included all subunits of the CCT/TRiC complex (except CCT5); HSP40 and HSP70 family members DNAJA1 (HDJ-2), DNAJA4, HSPA8 (HSC70), and HSPA14 (Figures 5B and 5C); and the TPR-domain APC/C subunits CDC23 and CDC27 that, upon knockdown, led to significantly elevated aggregation (Figure S5B). PubMed:25437566

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease
MeSH
Huntington Disease
MeSH
Parkinson Disease

p(HGNC:DNAJA4) increases a(HBP:"huntingtin aggregates") View Subject | View Object

These included all subunits of the CCT/TRiC complex (except CCT5); HSP40 and HSP70 family members DNAJA1 (HDJ-2), DNAJA4, HSPA8 (HSC70), and HSPA14 (Figures 5B and 5C); and the TPR-domain APC/C subunits CDC23 and CDC27 that, upon knockdown, led to significantly elevated aggregation (Figure S5B). PubMed:25437566

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease
MeSH
Huntington Disease
MeSH
Parkinson Disease

p(HGNC:HSPA14) increases a(HBP:"huntingtin aggregates") View Subject | View Object

These included all subunits of the CCT/TRiC complex (except CCT5); HSP40 and HSP70 family members DNAJA1 (HDJ-2), DNAJA4, HSPA8 (HSC70), and HSPA14 (Figures 5B and 5C); and the TPR-domain APC/C subunits CDC23 and CDC27 that, upon knockdown, led to significantly elevated aggregation (Figure S5B). PubMed:25437566

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease
MeSH
Huntington Disease
MeSH
Parkinson Disease

p(HGNC:HSPA8) increases a(HBP:"huntingtin aggregates") View Subject | View Object

These included all subunits of the CCT/TRiC complex (except CCT5); HSP40 and HSP70 family members DNAJA1 (HDJ-2), DNAJA4, HSPA8 (HSC70), and HSPA14 (Figures 5B and 5C); and the TPR-domain APC/C subunits CDC23 and CDC27 that, upon knockdown, led to significantly elevated aggregation (Figure S5B). PubMed:25437566

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease
MeSH
Huntington Disease
MeSH
Parkinson Disease

a(CHEBI:"Congo Red") decreases a(HBP:"huntingtin aggregates") View Subject | View Object

If oligomerization of mutant Huntingtin is inhibited by administration of Congo red starting at this age, no aggregates can be detected in the brain 5weeks later (Sanchez et al., 2003). PubMed:14556719

Appears in Networks:

p(HGNC:HTT, var("?")) increases a(HBP:"huntingtin aggregates") View Subject | View Object

However, a contribution to the pathogenesis by loss of function of Huntingtin encoded from the wild-type allele has not been excluded in HD (Cattaneo et al., 2001), since the mutant protein not only aggregates itself but can also promote aggregation of the wild-type protein (Busch et al.,2003). PubMed:14556719

Appears in Networks:

a(PUBCHEM:877863) decreases a(HBP:"huntingtin aggregates") View Subject | View Object

In addition, SMER-10, -18, and -28 were effective at suppressing mHTT aggregation and toxicity in COS-7 cells and flies (146). PubMed:25784053

Appears in Networks:
Annotations
Cell Ontology (CL)
motor neuron

p(FPLX:"CCT_complex") decreases a(HBP:"huntingtin aggregates") View Subject | View Object

TRiC also interacts with N-terminal fragments of mutant huntingtin that contain an expanded polyglutamine repeat sequence (165–168). Binding to TRiC modulates the aggregation properties of this protein and reduces its cytotoxicity. PubMed:23746257

Appears in Networks:

p(FPLX:HSPA) decreases a(HBP:"huntingtin 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:

composite(p(FPLX:"CCT_complex"), p(FPLX:HSPA)) decreases a(HBP:"huntingtin aggregates") View Subject | View Object

The Hsp70 system acts synergistically with the cytosolic chaperonin TRiC to prevent aggregation of proteins with expanded polyglutamine tracts (165–168). PubMed:23746257

Appears in Networks:

p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") decreases a(HBP:"huntingtin 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:

a(CHEBI:haloperidol) decreases a(HBP:"huntingtin aggregates") View Subject | View Object

For instance, haloperidol occludes huntingtin aggregation PubMed:30061532

Appears in Networks:
Annotations
MeSH
Frontal Lobe

Out-Edges 2

a(HBP:"huntingtin aggregates") decreases bp(GO:"clathrin-dependent endocytosis") View Subject | View Object

CME inhibition was also observed in cells containing aggregated forms of polyQ- expanded Htt exon 1 (Htt Q53); these cells exhibited 50 ± 15% reduced levels of internalized transferrin compared with cells with soluble Htt Q23 or Htt Q53 protein (Fig. S2 A–C ). PubMed:24706768

Appears in Networks:

a(HBP:"huntingtin aggregates") decreases bp(GO:"clathrin-dependent endocytosis") View Subject | View Object

In contrast, there was a marked reduction in CME in neurons containing mutant Htt exon 1 Q73-CFP aggregates compared with nonexpressing cells (Fig. 5 B , Center ; quantification in Fig. 5 D ); PubMed:24706768

Appears in Networks:
Annotations
Cell Ontology (CL)
neuron
MeSH
Huntington 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.