bp(GO:"neuron apoptotic process")

Entity

Name

neuron apoptotic process

Namespace

go

Namespace Version

20180921

Namespace URL

https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/go-names.belns

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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