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a(CHEBI:ATP)

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Entity

Name
ATP
Namespace
chebi
Namespace Version
20180906
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/chebi-names.belns

Appears in Networks 15

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

Perilous journey: a tour of the ubiquitin–proteasome system v1.0.0

Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease v1.0.0

Adenosine A1 receptor antagonist 64627 alleviates axonopathy caused by human Tau ΔK280 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

The role of inflammasome in Alzheimer’s disease v1.0.3

Amyloid-Binding Alcohol Dehydrogenase (ABAD) Inhibitors for the Treatment of Alzheimer’s Disease v1.0.0

Phosphatase: PP2A structural importance, regulation and its aberrant expression in cancer 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

The Ubiquitin–Proteasome System and the Autophagic–Lysosomal System in Alzheimer Disease v1.0.0

Molecular Chaperone Functions in Protein Folding and Proteostasis v1.0.0

Heme Curation v0.0.1-dev

Mechanistic knowledge surrounding heme

In-Edges 20

act(p(FPLX:HSP90)) association a(CHEBI:ATP) View Subject | View Object

The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566

Appears in Networks:

act(p(FPLX:HSPA)) association a(CHEBI:ATP) View Subject | View Object

The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566

Appears in Networks:

act(p(HGNC:HSPD1)) association a(CHEBI:ATP) View Subject | View Object

The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566

Appears in Networks:

composite(a(CHEBI:ATP), p(HGNC:UBA1)) hasComponent a(CHEBI:ATP) View Subject | View Object

Appears in Networks:

complex(a(CHEBI:ATP), p(HGNC:UBA1)) hasComponent a(CHEBI:ATP) View Subject | View Object

Appears in Networks:

composite(a(CHEBI:"magnesium(2+)"), a(CHEBI:ATP)) hasComponent a(CHEBI:ATP) View Subject | View Object

Appears in Networks:

a(GO:mitochondrion) positiveCorrelation a(CHEBI:ATP) View Subject | View Object

ATP is reduced in the proaggregant transgenic slices, matching the lower mitochondrial density, compared with littermate controls or antiaggregant Tau transgenic slices (Fig. 3H) PubMed:27671637

Appears in Networks:

p(HBP:"Tau isoform F (441 aa)", var("p.Lys280del")) decreases a(CHEBI:ATP) View Subject | View Object

ATP is reduced in the proaggregant transgenic slices, matching the lower mitochondrial density, compared with littermate controls or antiaggregant Tau transgenic slices (Fig. 3H) PubMed:27671637

Appears in Networks:

p(HBP:"Tau isoform F (441 aa)", var("p.Lys280del")) decreases a(CHEBI:ATP) View Subject | View Object

This suggests that the energy status of the neurons is compromised by proaggregant but not by antiaggregant Tau PubMed:27671637

Appears in Networks:
Annotations
MeSH
Neurons

rxn(reactants(a(CHEBI:ATP)), products(a(CHEBI:"phosphate(3-)"), a(CHEBI:ADP))) hasReactant a(CHEBI:ATP) View Subject | View Object

Appears in Networks:

complex(a(CHEBI:ATP), p(FPLX:HSP90)) hasComponent a(CHEBI:ATP) View Subject | View Object

Appears in Networks:

bp(GO:"cell death") increases sec(a(CHEBI:ATP)) View Subject | View Object

In human astrocytes, ATP released from damaged or dying cells after traumatic brain injury activates the NLRP2 inflammasome, leading to the maturation of both IL-1β and IL-18 (Minkiewicz et al., 2013) PubMed:24561250

Appears in Networks:
Annotations
Cell Ontology (CL)
astrocyte
Confidence
Medium
NeuroMMSigDB
Interleukin signaling subgraph

path(MESH:"Spinal Cord Injuries") increases a(CHEBI:ATP) View Subject | View Object

Spinal cord injury elevates extracellular ATP levels during neuroinflammation, which may act on purinergic receptors to trigger the activation of inflammasome (de Rivero Vaccari et al., 2012; Minkiewicz et al., 2013) PubMed:24561250

Appears in Networks:
Annotations
Confidence
Medium
MeSH
Extracellular Space

complex(p(HGNC:APP), p(HGNC:HSD17B10)) decreases a(CHEBI:ATP) View Subject | View Object

In another study, neurons from Tg mAPP/ABAD mice were shown to exhibit decreased activity of cyclooxygenase (COX) enzyme, spontaneous release of ROS, loss of mitochondrial membrane potential, a decrease in ATP production and release of cytochrome c from mitochondria with subsequent induction of caspase-3-like activity followed by apoptotic cell death. PubMed:30444369

Appears in Networks:
Annotations
MeSH
Neurons

complex(a(CHEBI:ATP), p(HGNC:HSPA1A)) hasComponent a(CHEBI:ATP) View Subject | View Object

Appears in Networks:

complex(a(CHEBI:ATP), p(HGNC:HSPA1B)) hasComponent a(CHEBI:ATP) View Subject | View Object

Appears in Networks:

path(HBP:"mitochondrial dysfunction") decreases a(CHEBI:ATP) View Subject | View Object

Dysfunctional mitochondria are critically harmful to cells, as this leads to decreased synthesis of cellular ATP and accumulation of ROS, which further overburden and damage other functional mitochondria. PubMed:29758300

Appears in Networks:

complex(a(CHEBI:ATP), p(HGNC:HSPD1)) hasComponent a(CHEBI:ATP) View Subject | View Object

Appears in Networks:

a(CHEBI:heme) decreases a(CHEBI:ATP) View Subject | View Object

Accordingly, heme exposures of more than 10 μM caused the significant and progressive depletion of cellular ATP, which was measured after an 8-h exposure period. PubMed:26794659

Appears in Networks:
Annotations
Cell Ontology (CL)
epithelial cell
MeSH
Kidney
Text Location
Results

p(HGNC:HPX) positiveCorrelation a(CHEBI:ATP) View Subject | View Object

This ATP depletion was prevented by the addition of the heme scavenger, hemopexin (Figure 5b). PubMed:26794659

Appears in Networks:
Annotations
Cell Ontology (CL)
epithelial cell
MeSH
Kidney
Text Location
Results

Out-Edges 18

a(CHEBI:ATP) association act(p(FPLX:HSP90)) View Subject | View Object

The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566

Appears in Networks:

a(CHEBI:ATP) association act(p(FPLX:HSPA)) View Subject | View Object

The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566

Appears in Networks:

a(CHEBI:ATP) association act(p(HGNC:HSPD1)) View Subject | View Object

The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566

Appears in Networks:

a(CHEBI:ATP) decreases complex(a(MESH:Proteins), a(MESH:Ubiquitin)) View Subject | View Object

Another key early finding was that the cleavage of the ubiquitin chain from the substrate was ATP-dependent and was coupled to the translocation of the protein substrate into the 20S core PubMed:24457024

Appears in Networks:

a(CHEBI:ATP) increases tloc(a(MESH:Proteins), fromLoc(GO:cytosol), toLoc(HBP:"20 S Proteasome")) View Subject | View Object

Another key early finding was that the cleavage of the ubiquitin chain from the substrate was ATP-dependent and was coupled to the translocation of the protein substrate into the 20S core PubMed:24457024

Appears in Networks:

a(CHEBI:ATP) positiveCorrelation a(GO:mitochondrion) View Subject | View Object

ATP is reduced in the proaggregant transgenic slices, matching the lower mitochondrial density, compared with littermate controls or antiaggregant Tau transgenic slices (Fig. 3H) PubMed:27671637

Appears in Networks:

a(CHEBI:ATP) increases act(complex(GO:"inflammasome complex")) View Subject | View Object

Activators include bacteria, virus, fungus, protoza, microbial proteins, crystalline urea, RNA, Alum, ATP, potassium efflux, fatty acids, Aβ, and most recently, degraded mitochondrial DNA (Liu et al., 2013a; Mathew et al., 2012; Schmidt and Lenz, 2012) PubMed:24561250

Appears in Networks:
Annotations
Confidence
High

a(CHEBI:ATP) increases act(complex(GO:"inflammasome complex")) View Subject | View Object

Spinal cord injury elevates extracellular ATP levels during neuroinflammation, which may act on purinergic receptors to trigger the activation of inflammasome (de Rivero Vaccari et al., 2012; Minkiewicz et al., 2013) PubMed:24561250

Appears in Networks:
Annotations
Confidence
Medium

a(CHEBI:ATP) increases composite(complex(GO:"inflammasome complex"), p(HGNC:NLRP2)) View Subject | View Object

ATP, a danger-associated molecular pattern that is released from damaged cells after brain injury, activates the NLRP2 inflammasome, which consists of the NLRP2 receptor, ASC and caspase-1, in human astrocytes (Minkiewicz et al., 2013) PubMed:24561250

Appears in Networks:
Annotations
Confidence
High
NeuroMMSigDB
Caspase subgraph

a(CHEBI:ATP) increases composite(complex(GO:"inflammasome complex"), p(HGNC:NLRP2)) View Subject | View Object

The ATP-induced activation of the NLRP2 inflammasome interacts with the ATP-release pannexin 1 channel and ATP-gated P2X7 receptor leading to the maturation of IL-1β (Minkiewicz et al., 2013) PubMed:24561250

Appears in Networks:
Annotations
Confidence
High
NeuroMMSigDB
Interleukin signaling subgraph

a(CHEBI:ATP) increases composite(complex(GO:"inflammasome complex"), p(HGNC:NLRP2)) View Subject | View Object

In human astrocytes, ATP released from damaged or dying cells after traumatic brain injury activates the NLRP2 inflammasome, leading to the maturation of both IL-1β and IL-18 (Minkiewicz et al., 2013) PubMed:24561250

Appears in Networks:
Annotations
Cell Ontology (CL)
astrocyte
Confidence
Medium
NeuroMMSigDB
Interleukin signaling subgraph

a(CHEBI:ATP) increases composite(complex(GO:"inflammasome complex"), p(HGNC:NLRP2)) View Subject | View Object

In addition, Brilliant Blue G (BBG), a P2X7 receptor antagonist, inhibits ATP-induced activation of the NLRP2 inflammasome in human astrocytes (Minkiewicz et al., 2013) PubMed:24561250

Appears in Networks:
Annotations
Cell Ontology (CL)
astrocyte
Confidence
Medium

a(CHEBI:ATP) regulates act(p(HGNCGENEFAMILY:Chaperonins)) View Subject | View Object

Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257

Appears in Networks:

a(CHEBI:ATP) regulates act(p(FPLX:HSPA)) View Subject | View Object

Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257

Appears in Networks:

a(CHEBI:ATP) regulates act(p(FPLX:HSP90)) View Subject | View Object

Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257

Appears in Networks:

a(CHEBI:ATP) causesNoChange act(p(FPLX:HSPB)) View Subject | View Object

ATP-independent chaperones, such as the small Hsps, may function as additional holdases that buffer aggregation. PubMed:23746257

Appears in Networks:

a(CHEBI:ATP) regulates complex(p(HGNC:HSPD1), p(HGNC:HSPE1)) View Subject | View Object

GroEL and GroES undergo a complex binding-and-release cycle that is allosterically regulated by ATP binding and hydrolysis in the GroEL subunits (Figure 6b) (4, 77, 100, 136). PubMed:23746257

Appears in Networks:

a(CHEBI:ATP) positiveCorrelation p(HGNC:HPX) View Subject | View Object

This ATP depletion was prevented by the addition of the heme scavenger, hemopexin (Figure 5b). PubMed:26794659

Appears in Networks:
Annotations
Cell Ontology (CL)
epithelial cell
MeSH
Kidney
Text Location
Results

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.