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bp(HBP:Proteostasis)

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Entity

Name
Proteostasis
Namespace
HBP
Namespace Version
20190207
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/cf4d8bb88754f036b943b4d94ad96e103dcb7149/export/hbp-names.belns

Appears in Networks 6

The Biology of Proteostasis in Aging and Disease v1.0.0

Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies v1.0.0

Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies 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

Molecular chaperones and proteostasis regulation during redox imbalance v1.0.0

In-Edges 27

bp(MESH:"Growth and Development") regulates bp(HBP:Proteostasis) View Subject | View Object

Furthermore, the activity of the PN can be altered permanently or transiently by development and aging, alterations in physiology, or exposure to environmental stress (1). PubMed:25784053

Appears in Networks:

bp(GO:"protein folding") association bp(HBP:Proteostasis) View Subject | View Object

Proteome fidelity is maintained by the protein homeostasis (proteostasis) network (PN), a multi-compartmental system that coordinatesprotein synthesis, folding, disaggregation, and degradation (1). PubMed:25784053

Appears in Networks:

bp(MESH:"Protein Biosynthesis") association bp(HBP:Proteostasis) View Subject | View Object

Proteome fidelity is maintained by the protein homeostasis (proteostasis) network (PN), a multi-compartmental system that coordinatesprotein synthesis, folding, disaggregation, and degradation (1). PubMed:25784053

Appears in Networks:

bp(MESH:"Stress, Physiological") regulates bp(HBP:Proteostasis) View Subject | View Object

Furthermore, the activity of the PN can be altered permanently or transiently by development and aging, alterations in physiology, or exposure to environmental stress (1). PubMed:25784053

Appears in Networks:

bp(MESH:Aging) regulates bp(HBP:Proteostasis) View Subject | View Object

Furthermore, the activity of the PN can be altered permanently or transiently by development and aging, alterations in physiology, or exposure to environmental stress (1). PubMed:25784053

Appears in Networks:

bp(MESH:Proteolysis) association bp(HBP:Proteostasis) View Subject | View Object

Proteome fidelity is maintained by the protein homeostasis (proteostasis) network (PN), a multi-compartmental system that coordinatesprotein synthesis, folding, disaggregation, and degradation (1). PubMed:25784053

Appears in Networks:

p(HGNC:HSPD1) increases bp(HBP:Proteostasis) View Subject | View Object

HSP60 is essential for maturation and maintenance of the mitochondrial proteome and is therefore intimately linked to energy production. PubMed:25784053

Appears in Networks:
Annotations
MeSH
Mitochondria

path(MESH:"Protein Aggregation, Pathological") association bp(HBP:Proteostasis) View Subject | View Object

Proteome fidelity is maintained by the protein homeostasis (proteostasis) network (PN), a multi-compartmental system that coordinatesprotein synthesis, folding, disaggregation, and degradation (1). PubMed:25784053

Appears in Networks:

p(HGNC:HSF1) increases bp(HBP:Proteostasis) View Subject | View Object

However, the mechanisms that link HSF1 induction to improved proteostasis are not yet clear PubMed:21882945

Appears in Networks:

p(FPLX:HSP90) association bp(HBP:Proteostasis) View Subject | View Object

Hsp90 is critical to maintaining proteostasis (Brehme et al., 2014) and accounts for up to 6% of all protein within the cell during times of stress (Picard, 2002; Prodromou, 2016). PubMed:29311797

Appears in Networks:

p(FPLX:HSP90) 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(FPLX:HSPA) 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(FPLX:HSPB) 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(HGNC:HSF1) increases bp(HBP:Proteostasis) View Subject | View Object

Therapeutic approaches to overcome proteostasis deficiencies have largely focused on the activation of HSF1, the heat shock transcription factor responsible for simultaneous upregulation of the expression of multiple molecular chaperones during stress (Calamini et al., 2011; Pierce et al., 2013). PubMed:27491084

Appears in Networks:

p(HGNC:HSPD1) 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(HGNC:TPR) 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:"AAA ATPases") 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") 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:

bp(GO:"behavioral response to starvation") association bp(HBP:Proteostasis) View Subject | View Object

Additionally, PN regulation is integrated with pathways involved in inflam- mation, response to oxidative stress, caloric restriction/starvation, and longevity. PubMed:23746257

Appears in Networks:

bp(GO:"cell death") negativeCorrelation bp(HBP:Proteostasis) View Subject | View Object

Additionally, PN regulation is integrated with pathways involved in inflam- mation, response to oxidative stress, caloric restriction/starvation, and longevity. PubMed:23746257

Appears in Networks:

bp(GO:"inflammatory response") association bp(HBP:Proteostasis) View Subject | View Object

Additionally, PN regulation is integrated with pathways involved in inflam- mation, response to oxidative stress, caloric restriction/starvation, and longevity. PubMed:23746257

Appears in Networks:

bp(GO:"response to oxidative stress") association bp(HBP:Proteostasis) View Subject | View Object

Additionally, PN regulation is integrated with pathways involved in inflam- mation, response to oxidative stress, caloric restriction/starvation, and longevity. PubMed:23746257

Appears in Networks:

bp(GO:"response to unfolded protein") regulates bp(HBP:Proteostasis) View Subject | View Object

The PN is regulated by interconnected pathways that respond to specific forms of cellular stress, including the cytosolic heat shock response (HSR) (191), the unfolded protein response (UPR) in the endoplas- mic reticulum (192), and the mitochondrial UPR (193). PubMed:23746257

Appears in Networks:
Annotations
MeSH
Endoplasmic Reticulum
MeSH
Mitochondria

bp(GO:aging) decreases bp(HBP:Proteostasis) View Subject | View Object

Indeed, studies using model organisms demonstrate that a gradual decline in cellular proteostasis capacity occurs with aging (10). PubMed:23746257

Appears in Networks:

bp(GO:aging) decreases bp(HBP:Proteostasis) View Subject | View Object

As shown in Caenorhabditis elegans, Drosophila, and the mouse, the ability of cells and tissues to maintain proteostasis declines during aging, concurrent with the capacity to respond to conformational stresses (214–220). PubMed:23746257

Appears in Networks:

bp(MESH:"Heat-Shock Response") regulates bp(HBP:Proteostasis) View Subject | View Object

The PN is regulated by interconnected pathways that respond to specific forms of cellular stress, including the cytosolic heat shock response (HSR) (191), the unfolded protein response (UPR) in the endoplas- mic reticulum (192), and the mitochondrial UPR (193). PubMed:23746257

Appears in Networks:
Annotations
MeSH
Cytosol

p(HGNC:NFE2L2) increases bp(HBP:Proteostasis) View Subject | View Object

Moreover, Nrf2 contributes to cellular proteostasis by regulating the expression of molecular chaperones [89], as well as of additional players of proteome stability and maintenance, namely the proteasome subunits [90–92]. PubMed:24563850

Appears in Networks:

Out-Edges 19

bp(HBP:Proteostasis) association bp(MESH:"Protein Biosynthesis") View Subject | View Object

Proteome fidelity is maintained by the protein homeostasis (proteostasis) network (PN), a multi-compartmental system that coordinatesprotein synthesis, folding, disaggregation, and degradation (1). PubMed:25784053

Appears in Networks:

bp(HBP:Proteostasis) association bp(GO:"protein folding") View Subject | View Object

Proteome fidelity is maintained by the protein homeostasis (proteostasis) network (PN), a multi-compartmental system that coordinatesprotein synthesis, folding, disaggregation, and degradation (1). PubMed:25784053

Appears in Networks:

bp(HBP:Proteostasis) association path(MESH:"Protein Aggregation, Pathological") View Subject | View Object

Proteome fidelity is maintained by the protein homeostasis (proteostasis) network (PN), a multi-compartmental system that coordinatesprotein synthesis, folding, disaggregation, and degradation (1). PubMed:25784053

Appears in Networks:

bp(HBP:Proteostasis) association bp(MESH:Proteolysis) View Subject | View Object

Proteome fidelity is maintained by the protein homeostasis (proteostasis) network (PN), a multi-compartmental system that coordinatesprotein synthesis, folding, disaggregation, and degradation (1). PubMed:25784053

Appears in Networks:

bp(HBP:Proteostasis) decreases bp(MESH:Aging) View Subject | View Object

As such, it is feasible that any reduction in the protein degradation capacity of a cell could contribute to proteostasis collapse and promote aging. PubMed:25784053

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

bp(HBP:Proteostasis) regulates p(HGNC:MAPT) View Subject | View Object

All proteins, including tau, are subject to extensive regulation by the cellular quality control pathways, which carefully control the balance between protein expression and turnover to maintain healthy protein homeostasis (or proteostasis) PubMed:21882945

Appears in Networks:

bp(HBP:Proteostasis) regulates a(MESH:Proteins) View Subject | View Object

All proteins, including tau, are subject to extensive regulation by the cellular quality control pathways, which carefully control the balance between protein expression and turnover to maintain healthy protein homeostasis (or proteostasis) PubMed:21882945

Appears in Networks:

bp(HBP:Proteostasis) association p(FPLX:HSP90) View Subject | View Object

Hsp90 is critical to maintaining proteostasis (Brehme et al., 2014) and accounts for up to 6% of all protein within the cell during times of stress (Picard, 2002; Prodromou, 2016). PubMed:29311797

Appears in Networks:

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(HBP:Proteostasis) association p(HGNC:HSPD1) 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(HBP:Proteostasis) association p(FPLX:HSPA) 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(HBP:Proteostasis) association p(HGNC:TPR) 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(HBP:Proteostasis) association p(FPLX:HSPB) 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(HBP:Proteostasis) association p(FPLX:HSP90) 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(HBP:Proteostasis) association p(HGNCGENEFAMILY:"AAA ATPases") 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(HBP:Proteostasis) association bp(GO:"inflammatory response") View Subject | View Object

Additionally, PN regulation is integrated with pathways involved in inflam- mation, response to oxidative stress, caloric restriction/starvation, and longevity. PubMed:23746257

Appears in Networks:

bp(HBP:Proteostasis) association bp(GO:"response to oxidative stress") View Subject | View Object

Additionally, PN regulation is integrated with pathways involved in inflam- mation, response to oxidative stress, caloric restriction/starvation, and longevity. PubMed:23746257

Appears in Networks:

bp(HBP:Proteostasis) association bp(GO:"behavioral response to starvation") View Subject | View Object

Additionally, PN regulation is integrated with pathways involved in inflam- mation, response to oxidative stress, caloric restriction/starvation, and longevity. PubMed:23746257

Appears in Networks:

bp(HBP:Proteostasis) negativeCorrelation bp(GO:"cell death") View Subject | View Object

Additionally, PN regulation is integrated with pathways involved in inflam- mation, response to oxidative stress, caloric restriction/starvation, and longevity. PubMed:23746257

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.