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p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins")

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Entity

Name
DNAJ (HSP40) heat shock proteins
Namespace
hgnc.genefamily
Namespace Version
20181015
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/3074b85b858455d8eeb76cfcdef685ced19bbe11/external/hgnc.genefamily-names.belns

Appears in Networks 4

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

The Biology of Proteostasis in Aging and Disease v1.0.0

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

Molecular Chaperone Functions in Protein Folding and Proteostasis v1.0.0

In-Edges 10

bp(MESH:Aging) decreases p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") View Subject | View Object

TPR proteins tend to be induced, whereas HSP40s are repressed (Figure 1B). PubMed:25437566

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bp(MESH:Aging) decreases p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") View Subject | View Object

Among the genes that are repressed in both aging and AD, the HSP70- HSP40 system corresponds to 36% of the 58 genes (Table S3D). PubMed:25437566

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Annotations
MeSH
Alzheimer Disease

bp(MESH:Aging) decreases p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") View Subject | View Object

Ranked by decreasing median aging correlation, the induction of sHSPs and TPR genes consistently ranked high and the HSP60s, HSP40s, and HSP70s were consistently repressed. PubMed:25437566

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bp(MESH:Aging) decreases p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") View Subject | View Object

Among repressed genes, the HSP40s exhibited significant change (p = 0.04875), with 62% of 48 HSP40 genes repressed in aging (p < 0.05) and 51% repressed in AD. PubMed:25437566

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

bp(MESH:Aging) decreases p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") View Subject | View Object

Additionally, an investigation of chaperone and cochaperone gene expression in young (36±4 years of age) and aged (73 ±4 years of age) human brain tissue revealed that of 332 genes examined, 101 are significantly repressed with age, including HSP70, HSP40, HSP90, and TRiC genes (113). Furthermore, 62 chaperone genes, including several small HSPs, were found to be significantly induced, likely as a result of the cellular response to accumulating protein damage with age (113). PubMed:25784053

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Annotations
Cell Ontology (CL)
motor neuron

bp(GO:aging) decreases p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") View Subject | View Object

The HSP70 and HSP40 family members exhibit significantly altered expression dynamics during aging in the human brain, both being consistently repressed with age (Brehme et al., 2014). PubMed:27491084

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bp(HBP:Proteostasis) association p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") View Subject | View Object

Many studies based on model systems support a role for candidates from each of the major chaperome families; HSP100, HSP90, HSP70, HSP60, HSP40, sHSPs, and TPR-domain-containing proteins in proteostasis. PubMed:27491084

Appears in Networks:

bp(MESH:Aging) decreases p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") View Subject | View Object

The HSP40, HSP60 and HSP70 families were amongst the most repressed chaperones, with HSP70s being the most repressed group overall. However, in contrast with the broad spectrum of repressed chaperone families, sHSPs and the TPR co-chaperone proteins were the only families that were significantly induced. PubMed:27491084

Appears in Networks:

path(MESH:"Alzheimer Disease") decreases p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") View Subject | View Object

Among repressed genes, HSP40s were found to show significant changes as a family, with 62% of overall 48 HSP40 family members repressed in aging brain (superior frontal gyrus), 51% repressed in AD, and 41% repressed in both aging and AD. PubMed:27491084

Appears in Networks:

composite(p(FPLX:HSPA), p(HGNC:HSPH1), p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins")) hasComponent p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") View Subject | View Object

Appears in Networks:

Out-Edges 6

p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") isA a(MESH:"Molecular Chaperones") View Subject | View Object

Appears in Networks:

p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") association bp(HBP:Proteostasis) View Subject | View Object

Many studies based on model systems support a role for candidates from each of the major chaperome families; HSP100, HSP90, HSP70, HSP60, HSP40, sHSPs, and TPR-domain-containing proteins in proteostasis. PubMed:27491084

Appears in Networks:

p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") increases act(p(FPLX:HSPA), ma(GO:"ATPase activity")) View Subject | View Object

HSP40s play a fundamental role as part of the HSP70-HSP40 system, as co-chaperones, stimulating HSP70 ATP hydrolysis (Fig. 3) (Kampinga and Craig, 2010; Kakkar et al., 2014). PubMed:27491084

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p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") regulates act(p(FPLX:HSPA)) View Subject | View Object

Hsp40 ( J protein) and NEF cochaperones regulate the Hsp70 reaction cy- cle (38, 100). PubMed:23746257

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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:

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:

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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.