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Entity

Name
neuron apoptotic process
Namespace
go
Namespace Version
20180921
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/go-names.belns

Appears in Networks 6

In-Edges 13

p(HGNC:PRKN) decreases bp(GO:"neuron apoptotic process") View Subject | View Object

Overexpression of Parkin is reported to attenuate cyclin E accumulation and rescue the cells from apoptosis PubMed:14556719

p(HGNC:CCNE1) positiveCorrelation bp(GO:"neuron apoptotic process") View Subject | View Object

Consistent with the notion that cyclin E is targeted by the Parkin ligase complex is the finding that Parkin deficiency leads to accumulation of cyclin E in cultured postmitotic neurons exposed to the glutamatergic excitotoxin kainite and promotes their apoptosis. PubMed:14556719

a(CHEBI:"alpha,alpha-trehalose") decreases bp(GO:"neuron apoptotic process") View Subject | View Object

Trehalose, an natural disaccharide and mTOR-independent activator of autophagy (Sarkar et al., 2007), showed an effect on neuronal survival, reducing the level of tau aggregates in the brain of human tauopathy model mice (Kruger et al., 2011; Rodriguez-Navarro et al., 2010; Schaeffer et al., 2012). PubMed:23528736

p(HGNC:PPID) decreases bp(GO:"neuron apoptotic process") View Subject | View Object

CyP40 was recently shown to disaggregate tau fibrils in vitro and prevents toxic tau accumulation in vivo preserving memory, demonstrating a neuroprotective role for CyP40 in the brain (Baker et al., 2017). PubMed:29311797

p(HGNC:AHSA1) increases bp(GO:"neuron apoptotic process") View Subject | View Object

In the same study, we found that high levels of Aha1 in a tau transgenic mouse model increased tau oligomers as well as neuronal loss concomitant with cognitive deficits (Shelton et al., 2017). PubMed:29311797

p(HGNC:HSPB1) negativeCorrelation bp(GO:"neuron apoptotic process") View Subject | View Object

Taken together, pathological hyperphosphorylated tau caused cell death, and Hsp27 attenuated the cell toxicity of pathological hyperphosphorylated tau. PubMed:14963027

Annotations
Uberon
temporal cortex

act(p(HGNC:MAPT, pmod(Ph))) increases bp(GO:"neuron apoptotic process") View Subject | View Object

Taken together, pathological hyperphosphorylated tau caused cell death, and Hsp27 attenuated the cell toxicity of pathological hyperphosphorylated tau. PubMed:14963027

Annotations
Uberon
temporal cortex

complex(p(MGI:Dapk1), p(MGI:Mapt)) increases bp(GO:"neuron apoptotic process") View Subject | View Object

Direct interaction of DAPK1 with Tau causes spine loss and subsequently neuronal death. DAPK1 phosphorylates Tau protein at Ser262 (pS(262)) in cortical neurons of stroke mice. PubMed:25995053

Appears in Networks:
Annotations
MeSH
Stroke

p(HGNC:CASP3) increases bp(GO:"neuron apoptotic process") View Subject | View Object

Overexpression of wild-type UNC5C causes low-grade death, intensified by an AD-linked mutation T835M inhibited by a AD-linked survival factor, calmodulin-like skin protein (CLSP), and a natural ligand of UNC5C, netrin1. T835M-UNC5C-induced neuronal cell death is mediated by an intracellular death-signaling cascade, consisting of DAPK1/protein kinase D/apoptosis signal-regulating kinase 1 (ASK1)/JNK/NADPH oxidase/caspases, which merges at ASK1 with a death-signaling cascade, mediated by amyloid ß precursor protein (APP). PubMed:27068745

Appears in Networks:

act(p(HGNC:DAPK1)) increases bp(GO:"neuron apoptotic process") View Subject | View Object

Overexpression of UNC5B induces neuronal death by activating death-associated protein kinase (DAPK1) (19) via protein phosphatase 2A-mediated dephosphorylation of DAPK1 (20). PubMed:27068745

Appears in Networks:

p(HGNC:UNC5C) positiveCorrelation bp(GO:"neuron apoptotic process") View Subject | View Object

Overexpression of wild-type UNC5C causes low-grade death, intensified by an AD-linked mutation T835M inhibited by a AD-linked survival factor, calmodulin-like skin protein (CLSP), and a natural ligand of UNC5C, netrin1. T835M-UNC5C-induced neuronal cell death is mediated by an intracellular death-signaling cascade, consisting of DAPK1/protein kinase D/apoptosis signal-regulating kinase 1 (ASK1)/JNK/NADPH oxidase/caspases, which merges at ASK1 with a death-signaling cascade, mediated by amyloid ß precursor protein (APP). PubMed:27068745

Appears in Networks:

p(HGNC:UNC5C, var("p.Thr835Met")) increases bp(GO:"neuron apoptotic process") View Subject | View Object

Overexpression of wild-type UNC5C causes low-grade death, intensified by an AD-linked mutation T835M inhibited by a AD-linked survival factor, calmodulin-like skin protein (CLSP), and a natural ligand of UNC5C, netrin1. T835M-UNC5C-induced neuronal cell death is mediated by an intracellular death-signaling cascade, consisting of DAPK1/protein kinase D/apoptosis signal-regulating kinase 1 (ASK1)/JNK/NADPH oxidase/caspases, which merges at ASK1 with a death-signaling cascade, mediated by amyloid ß precursor protein (APP). PubMed:27068745

Appears in Networks:

p(HGNC:RELA) decreases bp(GO:"neuron apoptotic process") View Subject | View Object

Activation of AKT augments the transactivating activity and produces higher nuclear levels of p65-NF- κB, which is important for neuroprotection. PubMed:27288790

Out-Edges 3

bp(GO:"neuron apoptotic process") positiveCorrelation p(HGNC:CCNE1) View Subject | View Object

Consistent with the notion that cyclin E is targeted by the Parkin ligase complex is the finding that Parkin deficiency leads to accumulation of cyclin E in cultured postmitotic neurons exposed to the glutamatergic excitotoxin kainite and promotes their apoptosis. PubMed:14556719

bp(GO:"neuron apoptotic process") negativeCorrelation p(HGNC:HSPB1) View Subject | View Object

Taken together, pathological hyperphosphorylated tau caused cell death, and Hsp27 attenuated the cell toxicity of pathological hyperphosphorylated tau. PubMed:14963027

Annotations
Uberon
temporal cortex

bp(GO:"neuron apoptotic process") positiveCorrelation p(HGNC:UNC5C) View Subject | View Object

Overexpression of wild-type UNC5C causes low-grade death, intensified by an AD-linked mutation T835M inhibited by a AD-linked survival factor, calmodulin-like skin protein (CLSP), and a natural ligand of UNC5C, netrin1. T835M-UNC5C-induced neuronal cell death is mediated by an intracellular death-signaling cascade, consisting of DAPK1/protein kinase D/apoptosis signal-regulating kinase 1 (ASK1)/JNK/NADPH oxidase/caspases, which merges at ASK1 with a death-signaling cascade, mediated by amyloid ß precursor protein (APP). PubMed:27068745

Appears in Networks:

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.