1. Catalog
  2. Nodes
  3. p(FPLX:ERK)

p(FPLX:ERK)

Equivalencies: 0 | Classes: 0 | Children: 0 | Explore

Entity

Name
ERK
Namespace
FPLX
Namespace Version
20180917
Namespace URL
https://raw.githubusercontent.com/sorgerlab/famplex/e8ae9926ff95266032cb74f77973c84939bffbeb/export/famplex.belns

Appears in Networks 8

Nicotinic acetylcholine receptor signalling: roles in Alzheimer's disease and amyloid neuroprotection. v1.0.0

Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5 v1.0.0

MMP-9 and MMP-2 Contribute to Neuronal Cell Death in iPSC Models of Frontotemporal Dementia with MAPT Mutations v1.0.0

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

Protein phosphatase 2A dysfunction in Alzheimer’s disease v1.0.0

Axonal Transport, Tau Protein, and Neurodegeneration in Alzheimer’s Disease v1.0.0

Phytochemicals as inhibitors of NF-κB for treatment of Alzheimer’s disease v1.0.0

Upstream regulators and downstream effectors of NF-κBinAlzheimer's disease v1.0.0

In-Edges 30

a(CHEBI:"amyloid-beta") increases act(p(FPLX:ERK)) View Subject | View Object

In neuroblastoma cells, as well as cultured hippocampal neurons, Abeta activates JNK and ERK, and blocking these prevents Abeta hyperphosphorylating tau protein, as does alpha7 antisense oligonucleotides or alpha7 antagonists, suggesting that Abeta may trigger tau protein phosphorylation through ERK and JNK via alpha7 receptors (Wang et al., 2003b). Abeta leads to phosphorylation of AKT in cultured mouse neurons through a mechanism that requires alpha7 nAChRs (Abbott et al., 2008), AKT phosphorylation levels returning to baseline upon prolonged application of Abeta. PubMed:19293145

Appears in Networks:

a(CHEBI:nicotine) association p(FPLX:ERK) View Subject | View Object

Nicotine protects PC12 cells from cell death resulting from serum depletion through a mechanism that depends upon the function of IP3 receptors, L-type calcium channels, ryanodine receptors, and ERK, suggesting that the protective effect of nicotine is mediated by calcium signaling pathways (Ren et al., 2005). PubMed:19293145

Appears in Networks:
Annotations
Experimental Factor Ontology (EFO)
PC12

a(HBP:"amyloid-beta oligomers") decreases act(p(FPLX:ERK)) View Subject | View Object

Which pathway is activated by Abeta depends upon the time of exposure to the amyloid peptide: chronic applications of oligomeric Abeta to hippocampal slice cultures activate the JNK/MAPK pathway but inhibit the ERK/MAPK pathway, whereas short-term applications of Abeta oligomers do not activate JNK (Bell et al., 2004). This may be one of the routes whereby Abeta impairs memory, because ERK-1 and ERK-2 play key roles in the signaling events central to memory (Satoh et al., 2007). PubMed:19293145

Appears in Networks:
Annotations
MeSH
Hippocampus

composite(p(FPLX:ERK), p(FPLX:RAF), p(FPLX:RAS), p(HGNC:MAP2K1)) hasComponent p(FPLX:ERK) View Subject | View Object

Appears in Networks:

composite(p(FPLX:ERK), p(HGNC:CHRNA7)) hasComponent p(FPLX:ERK) View Subject | View Object

Appears in Networks:

a(GO:microtubule) association p(FPLX:ERK) View Subject | View Object

In this regard, cdk5 is similar to PKA [30], MAP kinase, and GSK-3 [12,17,26], but distinct from PKC or CaMK which do not copurify with microtubules [34] PubMed:8282104

Appears in Networks:
Annotations
Confidence
High

a(HBP:HBP00006) association p(FPLX:ERK) View Subject | View Object

In this regard, cdk5 is similar to PKA [30], MAP kinase, and GSK-3 [12,17,26], but distinct from PKC or CaMK which do not copurify with microtubules [34] PubMed:8282104

Appears in Networks:
Annotations
Confidence
High

path(MESH:"Alzheimer Disease") positiveCorrelation p(FPLX:ERK) View Subject | View Object

Thus, we now know three kinases, cdk5, MAP kinase, and GSK-3, all of which are present in neurons, which are capable of transforming tau into the Alzheimer-like state, and therefore could account for the pathological phosphorylation of tau in Alzheimer brains PubMed:8282104

Appears in Networks:
Annotations
Confidence
High
MeSH
Neurons

a(CHEBI:"dimethyl fumarate") increases act(p(FPLX:ERK)) View Subject | View Object

Wild-type MEFs treated with DMF (20 μM) showed a time-dependent response effect activating phosphorylation of ERK (Fig. 2A, B) and p38 (Fig. 2A, C), that was maximal within 5 min. The Ser/Thr protein kinase AKT, an upstream regulator of GSK-3β, was also activated after 5 min as determined by increased phosphorylation of S473 (Fig. 2A, D) PubMed:29121589

Appears in Networks:

a(CHEBI:peroxynitrite) causesNoChange act(p(FPLX:ERK)) View Subject | View Object

In the present study we injected bilaterally 3-morpholino-sydnonimine (SIN-1), a recognized and widely used peroxynitrite donor (25–30), into rat hippocampus, and investigated whether or not peroxynitrite could induce simultaneously nitration and hyperphosphorylation of tau and the underlying mechanisms in vivo. The level of nitrated and hyperphosphorylated tau was markedly increased in rat hippocampus 24 h, and prevented by preinjection of uric acid, a natural scavenger of peroxynitrite. GSK-3beta and p38 MAPKs, including p38alpha, p38beta, and p38delta activity was increased, but no change in the activity of p38gamma, ERK, and c-Jun amino-terminal kinase (JNK). Both nitrated tau and hyperphosphorylated tau were aggregated in the hippocampus, with activity of 20S proteasome significantly arrested in SIN-1-injected rats. Hyperphosphorylated tau was degraded as efficiently as normal tau by 20S proteasome, but the nitrated tau with an unorderly secondary structure became more resistant to the proteolysis, providing evidence that peroxynitrite simultaneously induces tau hyperphosphorylation, nitration, and accumulation, and that activation of GSK-3beta, p38alpha, p38beta, p38delta isoforms and the inhibition of proteasome activity are respectively responsible for the peroxynitrite-induced tau hyperphosphorylation and accumulation. PubMed:16816118

Appears in Networks:
Annotations
Uberon
hippocampal formation

p(FPLX:ERK, pmod(Ph)) increases act(p(FPLX:ERK)) View Subject | View Object

Here we show through systematic epigenetic studies that the histone acetyltransferase p300/CBP-associated factor (PCAF) promotes acetylation of histone 3 Lys 9 at the promoters of established key regeneration-associated genes following a peripheral but not a central axonal injury. Furthermore, we find that extracellular signal-regulated kinase (ERK)-mediated retrograde signalling is required for PCAF-dependent regenerative gene reprogramming. Finally, PCAF is necessary for conditioning-dependent axonal regeneration and also singularly promotes regeneration after spinal cord injury. PubMed:24686445

Appears in Networks:
Annotations
Uberon
dorsal root ganglion

act(p(HGNC:KAT2B)) positiveCorrelation act(p(FPLX:ERK)) View Subject | View Object

Here we show through systematic epigenetic studies that the histone acetyltransferase p300/CBP-associated factor (PCAF) promotes acetylation of histone 3 Lys 9 at the promoters of established key regeneration-associated genes following a peripheral but not a central axonal injury. Furthermore, we find that extracellular signal-regulated kinase (ERK)-mediated retrograde signalling is required for PCAF-dependent regenerative gene reprogramming. Finally, PCAF is necessary for conditioning-dependent axonal regeneration and also singularly promotes regeneration after spinal cord injury. PubMed:24686445

Appears in Networks:
Annotations
Uberon
dorsal root ganglion

a(GO:"microtubule cytoskeleton") negativeCorrelation act(p(FPLX:ERK)) View Subject | View Object

Apart from affecting tau phosphorylation, abnormal activation of GSK3β, cdk5, and ERK has been linked to cytoskeletal abnormalities (microtubules, neurofilaments), alterations in amyloid precursor protein (APP) phosphorylation and processing, impairment of neurogenesis, alterations in synaptic plasticity and induction of apoptotic processes (Reviewed in Crews and Masliah, 2010; Medina and Avila, 2013, 2014). PubMed:24653673

Appears in Networks:

a(GO:"neurofilament cytoskeleton") negativeCorrelation act(p(FPLX:ERK)) View Subject | View Object

Apart from affecting tau phosphorylation, abnormal activation of GSK3β, cdk5, and ERK has been linked to cytoskeletal abnormalities (microtubules, neurofilaments), alterations in amyloid precursor protein (APP) phosphorylation and processing, impairment of neurogenesis, alterations in synaptic plasticity and induction of apoptotic processes (Reviewed in Crews and Masliah, 2010; Medina and Avila, 2013, 2014). PubMed:24653673

Appears in Networks:

bp(GO:"apoptotic process") positiveCorrelation act(p(FPLX:ERK)) View Subject | View Object

Apart from affecting tau phosphorylation, abnormal activation of GSK3β, cdk5, and ERK has been linked to cytoskeletal abnormalities (microtubules, neurofilaments), alterations in amyloid precursor protein (APP) phosphorylation and processing, impairment of neurogenesis, alterations in synaptic plasticity and induction of apoptotic processes (Reviewed in Crews and Masliah, 2010; Medina and Avila, 2013, 2014). PubMed:24653673

Appears in Networks:

bp(GO:"negative regulation of synaptic plasticity") positiveCorrelation act(p(FPLX:ERK)) View Subject | View Object

Apart from affecting tau phosphorylation, abnormal activation of GSK3β, cdk5, and ERK has been linked to cytoskeletal abnormalities (microtubules, neurofilaments), alterations in amyloid precursor protein (APP) phosphorylation and processing, impairment of neurogenesis, alterations in synaptic plasticity and induction of apoptotic processes (Reviewed in Crews and Masliah, 2010; Medina and Avila, 2013, 2014). PubMed:24653673

Appears in Networks:

bp(GO:neurogenesis) negativeCorrelation act(p(FPLX:ERK)) View Subject | View Object

Apart from affecting tau phosphorylation, abnormal activation of GSK3β, cdk5, and ERK has been linked to cytoskeletal abnormalities (microtubules, neurofilaments), alterations in amyloid precursor protein (APP) phosphorylation and processing, impairment of neurogenesis, alterations in synaptic plasticity and induction of apoptotic processes (Reviewed in Crews and Masliah, 2010; Medina and Avila, 2013, 2014). PubMed:24653673

Appears in Networks:

bp(HBP:"APP processing") negativeCorrelation act(p(FPLX:ERK)) View Subject | View Object

Apart from affecting tau phosphorylation, abnormal activation of GSK3β, cdk5, and ERK has been linked to cytoskeletal abnormalities (microtubules, neurofilaments), alterations in amyloid precursor protein (APP) phosphorylation and processing, impairment of neurogenesis, alterations in synaptic plasticity and induction of apoptotic processes (Reviewed in Crews and Masliah, 2010; Medina and Avila, 2013, 2014). PubMed:24653673

Appears in Networks:

act(complex(GO:"protein phosphatase type 2A complex")) increases act(p(FPLX:ERK)) View Subject | View Object

Specific PP2A inhibition has been proven to lead to in vivo deregulation of many major brain Ser/Thr kinases implicated in AD, including GSK3β (Wang et al., 2010; Louis et al., 2011), cdk5 (Louis et al., 2011; Kimura et al., 2013), extracellular signal- regulated kinase (ERK) and JNK (Kins et al., 2003). PubMed:24653673

Appears in Networks:

p(HGNC:APP, pmod(Ph)) negativeCorrelation act(p(FPLX:ERK)) View Subject | View Object

Apart from affecting tau phosphorylation, abnormal activation of GSK3β, cdk5, and ERK has been linked to cytoskeletal abnormalities (microtubules, neurofilaments), alterations in amyloid precursor protein (APP) phosphorylation and processing, impairment of neurogenesis, alterations in synaptic plasticity and induction of apoptotic processes (Reviewed in Crews and Masliah, 2010; Medina and Avila, 2013, 2014). PubMed:24653673

Appears in Networks:

a(CHEBI:"N(5)-ethyl-L-glutamine") decreases act(p(FPLX:ERK)) View Subject | View Object

Besides, extracellular signal-regulated kinase (ERK), p38 MAPK and NF-B pathway were disrupted byL-theanine [128]. PubMed:29179999

Appears in Networks:

a(CHEBI:"reactive oxygen species") increases act(p(FPLX:ERK)) View Subject | View Object

ROS activate various downstream signaling molecules, such as PKC and mitogen-activated protein kinases (MAPKs) that induce nuclear translocation of NF-B and the expression of pro-inflammatory genes [41]. PubMed:29179999

Appears in Networks:

a(CHEBI:Geniposide) decreases act(p(FPLX:ERK)) View Subject | View Object

Geniposide considerably suppressed RAGE-related signaling such as ERK and IB/NF-B, the expression of TNF-, IL-1 and cerebral A accumulation in vivo[245] PubMed:29179999

Appears in Networks:

a(CHEBI:berberine) decreases act(p(FPLX:ERK)) View Subject | View Object

Berberine inhibited the p38,ERK and Akt signaling pathways, which were stimulated by A PubMed:29179999

Appears in Networks:

a(PUBCHEM:102336202) decreases act(p(FPLX:ERK)) View Subject | View Object

Xanthoceraside decreased the expression of A 25-35/IFN--stimulated NO, IL-1,and TNF- in microglia, which implicated the down-regulation of the activities of MAPK and NF-B pathways [248] PubMed:29179999

Appears in Networks:
Annotations
Cell Ontology (CL)
microglial cell

a(PUBCHEM:440312) decreases act(p(FPLX:ERK)) View Subject | View Object

Besides, it significantly decreased the generation of ROS and affected LPS-induced activation of MAPK, including p38 and NF-B signaling[243]. PubMed:29179999

Appears in Networks:

a(CHEBI:"hydrogen peroxide") increases act(p(FPLX:ERK)) View Subject | View Object

Omega-6 phospholipids, e.g. dilinoleoylphosphatidylcholine (DLPC), have been shown to block TNF-α and H 2 O 2 activation of MAPK as well as blocks IκBα phosphorylation in the SH-SY5Y cells and prevents the phosphorylation and activation of NF-κB. PubMed:27288790

Appears in Networks:
Annotations
MeSH
Cerebral Cortex
MeSH
Hippocampus

a(PUBCHEM:439378) decreases p(FPLX:ERK) View Subject | View Object

L-Theanine, an amino acid in green tea, reduced Aβ 42 levels in the cortex and hippocampus of the brain, which is mediated by suppres- sion of ERK/p38 and NF-κB as well as the reduction of macromolecular oxidative damage [81]. PubMed:27288790

Appears in Networks:
Annotations
MeSH
Cerebral Cortex
MeSH
Hippocampus

a(PUBCHEM:6440944) decreases act(p(FPLX:ERK)) View Subject | View Object

Omega-6 phospholipids, e.g. dilinoleoylphosphatidylcholine (DLPC), have been shown to block TNF-α and H 2 O 2 activation of MAPK as well as blocks IκBα phosphorylation in the SH-SY5Y cells and prevents the phosphorylation and activation of NF-κB. PubMed:27288790

Appears in Networks:
Annotations
MeSH
Cerebral Cortex
MeSH
Hippocampus

p(HGNC:TNF) increases act(p(FPLX:ERK)) View Subject | View Object

Omega-6 phospholipids, e.g. dilinoleoylphosphatidylcholine (DLPC), have been shown to block TNF-α and H 2 O 2 activation of MAPK as well as blocks IκBα phosphorylation in the SH-SY5Y cells and prevents the phosphorylation and activation of NF-κB. PubMed:27288790

Appears in Networks:
Annotations
MeSH
Cerebral Cortex
MeSH
Hippocampus

Out-Edges 23

p(FPLX:ERK) association a(CHEBI:nicotine) View Subject | View Object

Nicotine protects PC12 cells from cell death resulting from serum depletion through a mechanism that depends upon the function of IP3 receptors, L-type calcium channels, ryanodine receptors, and ERK, suggesting that the protective effect of nicotine is mediated by calcium signaling pathways (Ren et al., 2005). PubMed:19293145

Appears in Networks:
Annotations
Experimental Factor Ontology (EFO)
PC12

p(FPLX:ERK) directlyIncreases p(HGNC:MAPT, pmod(Ph)) View Subject | View Object

The Mr shifts up with time in several stages, very similar to our earlier observations with the brain kinase activity, MAP kinase and GSK3 (Fig. 2,) PubMed:8282104

Appears in Networks:
Annotations
Confidence
High

p(FPLX:ERK) directlyIncreases p(HGNC:MAPT, pmod(Ph, Ser, 199)) View Subject | View Object

The reaction with the diagnostic antibodies (Fig. 4) is similar to the examples shown previously for cdk2 (Fig. 2), MAP kinase [8], or GSK-3 [26], indicating the phosphorylation of the SP motifs for which these antibodies are sensitive (serines 199, 202, 235, 396, 404; see Fig. 1) PubMed:8282104

Appears in Networks:
Annotations
Confidence
High

p(FPLX:ERK) directlyIncreases p(HGNC:MAPT, pmod(Ph, Ser, 202)) View Subject | View Object

The reaction with the diagnostic antibodies (Fig. 4) is similar to the examples shown previously for cdk2 (Fig. 2), MAP kinase [8], or GSK-3 [26], indicating the phosphorylation of the SP motifs for which these antibodies are sensitive (serines 199, 202, 235, 396, 404; see Fig. 1) PubMed:8282104

Appears in Networks:
Annotations
Confidence
High

p(FPLX:ERK) directlyIncreases p(HGNC:MAPT, pmod(Ph, Ser, 235)) View Subject | View Object

The reaction with the diagnostic antibodies (Fig. 4) is similar to the examples shown previously for cdk2 (Fig. 2), MAP kinase [8], or GSK-3 [26], indicating the phosphorylation of the SP motifs for which these antibodies are sensitive (serines 199, 202, 235, 396, 404; see Fig. 1) PubMed:8282104

Appears in Networks:
Annotations
Confidence
High

p(FPLX:ERK) directlyIncreases p(HGNC:MAPT, pmod(Ph, Ser, 396)) View Subject | View Object

The reaction with the diagnostic antibodies (Fig. 4) is similar to the examples shown previously for cdk2 (Fig. 2), MAP kinase [8], or GSK-3 [26], indicating the phosphorylation of the SP motifs for which these antibodies are sensitive (serines 199, 202, 235, 396, 404; see Fig. 1) PubMed:8282104

Appears in Networks:
Annotations
Confidence
High

p(FPLX:ERK) regulates p(HGNC:MMP9) View Subject | View Object

It is known that MMP-9 expression is regulated by ERK (Wang et al., 2006) PubMed:27594586

Appears in Networks:
Annotations
Confidence
Medium
MeSH
Cerebral Cortex
MeSH
Neurons
MeSH
Frontotemporal Dementia

p(FPLX:ERK) directlyIncreases p(HGNC:MAPT, pmod(Ph, Ser, 404)) View Subject | View Object

The reaction with the diagnostic antibodies (Fig. 4) is similar to the examples shown previously for cdk2 (Fig. 2), MAP kinase [8], or GSK-3 [26], indicating the phosphorylation of the SP motifs for which these antibodies are sensitive (serines 199, 202, 235, 396, 404; see Fig. 1) PubMed:8282104

Appears in Networks:
Annotations
Confidence
High

p(FPLX:ERK) association a(GO:microtubule) View Subject | View Object

In this regard, cdk5 is similar to PKA [30], MAP kinase, and GSK-3 [12,17,26], but distinct from PKC or CaMK which do not copurify with microtubules [34] PubMed:8282104

Appears in Networks:
Annotations
Confidence
High

p(FPLX:ERK) association a(HBP:HBP00006) View Subject | View Object

In this regard, cdk5 is similar to PKA [30], MAP kinase, and GSK-3 [12,17,26], but distinct from PKC or CaMK which do not copurify with microtubules [34] PubMed:8282104

Appears in Networks:
Annotations
Confidence
High

p(FPLX:ERK) increases rxn(reactants(p(HGNC:MAPT)), products(p(HGNC:MAPT, pmod(Ph)))) View Subject | View Object

Thus, we now know three kinases, cdk5, MAP kinase, and GSK-3, all of which are present in neurons, which are capable of transforming tau into the Alzheimer-like state, and therefore could account for the pathological phosphorylation of tau in Alzheimer brains PubMed:8282104

Appears in Networks:
Annotations
Confidence
High
MeSH
Neurons

p(FPLX:ERK) positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

Thus, we now know three kinases, cdk5, MAP kinase, and GSK-3, all of which are present in neurons, which are capable of transforming tau into the Alzheimer-like state, and therefore could account for the pathological phosphorylation of tau in Alzheimer brains PubMed:8282104

Appears in Networks:
Annotations
Confidence
High
MeSH
Neurons

p(FPLX:ERK) hasVariant p(FPLX:ERK, pmod(Ph)) View Subject | View Object

Appears in Networks:

act(p(FPLX:ERK)) positiveCorrelation act(p(HGNC:KAT2B)) View Subject | View Object

Here we show through systematic epigenetic studies that the histone acetyltransferase p300/CBP-associated factor (PCAF) promotes acetylation of histone 3 Lys 9 at the promoters of established key regeneration-associated genes following a peripheral but not a central axonal injury. Furthermore, we find that extracellular signal-regulated kinase (ERK)-mediated retrograde signalling is required for PCAF-dependent regenerative gene reprogramming. Finally, PCAF is necessary for conditioning-dependent axonal regeneration and also singularly promotes regeneration after spinal cord injury. PubMed:24686445

Appears in Networks:
Annotations
Uberon
dorsal root ganglion

act(p(FPLX:ERK)) negativeCorrelation a(GO:"microtubule cytoskeleton") View Subject | View Object

Apart from affecting tau phosphorylation, abnormal activation of GSK3β, cdk5, and ERK has been linked to cytoskeletal abnormalities (microtubules, neurofilaments), alterations in amyloid precursor protein (APP) phosphorylation and processing, impairment of neurogenesis, alterations in synaptic plasticity and induction of apoptotic processes (Reviewed in Crews and Masliah, 2010; Medina and Avila, 2013, 2014). PubMed:24653673

Appears in Networks:

act(p(FPLX:ERK)) negativeCorrelation a(GO:"neurofilament cytoskeleton") View Subject | View Object

Apart from affecting tau phosphorylation, abnormal activation of GSK3β, cdk5, and ERK has been linked to cytoskeletal abnormalities (microtubules, neurofilaments), alterations in amyloid precursor protein (APP) phosphorylation and processing, impairment of neurogenesis, alterations in synaptic plasticity and induction of apoptotic processes (Reviewed in Crews and Masliah, 2010; Medina and Avila, 2013, 2014). PubMed:24653673

Appears in Networks:

act(p(FPLX:ERK)) negativeCorrelation p(HGNC:APP, pmod(Ph)) View Subject | View Object

Apart from affecting tau phosphorylation, abnormal activation of GSK3β, cdk5, and ERK has been linked to cytoskeletal abnormalities (microtubules, neurofilaments), alterations in amyloid precursor protein (APP) phosphorylation and processing, impairment of neurogenesis, alterations in synaptic plasticity and induction of apoptotic processes (Reviewed in Crews and Masliah, 2010; Medina and Avila, 2013, 2014). PubMed:24653673

Appears in Networks:

act(p(FPLX:ERK)) negativeCorrelation bp(HBP:"APP processing") View Subject | View Object

Apart from affecting tau phosphorylation, abnormal activation of GSK3β, cdk5, and ERK has been linked to cytoskeletal abnormalities (microtubules, neurofilaments), alterations in amyloid precursor protein (APP) phosphorylation and processing, impairment of neurogenesis, alterations in synaptic plasticity and induction of apoptotic processes (Reviewed in Crews and Masliah, 2010; Medina and Avila, 2013, 2014). PubMed:24653673

Appears in Networks:

act(p(FPLX:ERK)) negativeCorrelation bp(GO:neurogenesis) View Subject | View Object

Apart from affecting tau phosphorylation, abnormal activation of GSK3β, cdk5, and ERK has been linked to cytoskeletal abnormalities (microtubules, neurofilaments), alterations in amyloid precursor protein (APP) phosphorylation and processing, impairment of neurogenesis, alterations in synaptic plasticity and induction of apoptotic processes (Reviewed in Crews and Masliah, 2010; Medina and Avila, 2013, 2014). PubMed:24653673

Appears in Networks:

act(p(FPLX:ERK)) positiveCorrelation bp(GO:"negative regulation of synaptic plasticity") View Subject | View Object

Apart from affecting tau phosphorylation, abnormal activation of GSK3β, cdk5, and ERK has been linked to cytoskeletal abnormalities (microtubules, neurofilaments), alterations in amyloid precursor protein (APP) phosphorylation and processing, impairment of neurogenesis, alterations in synaptic plasticity and induction of apoptotic processes (Reviewed in Crews and Masliah, 2010; Medina and Avila, 2013, 2014). PubMed:24653673

Appears in Networks:

act(p(FPLX:ERK)) positiveCorrelation bp(GO:"apoptotic process") View Subject | View Object

Apart from affecting tau phosphorylation, abnormal activation of GSK3β, cdk5, and ERK has been linked to cytoskeletal abnormalities (microtubules, neurofilaments), alterations in amyloid precursor protein (APP) phosphorylation and processing, impairment of neurogenesis, alterations in synaptic plasticity and induction of apoptotic processes (Reviewed in Crews and Masliah, 2010; Medina and Avila, 2013, 2014). PubMed:24653673

Appears in Networks:

p(FPLX:ERK) increases p(HGNC:MAPT, pmod(Ph)) View Subject | View Object

Among the specific “proline-dependent” kinases that can phosphorylate protein tau at dif- ferent sites in vitro, special attention is dedicated to glycogen-synthase kinase-3β (GSK-3β) (Michel et al., 1998), mitogen-activated protein kinase (MAPK) (Drewes et al., 1992), stress-activated protein kinases (SAPKs) (Goedert et al., 1997) and cyclin-dependent kinases (CDKs) including cdc2 and cdk5 (Baumann et al., 1993; Patrick et al., 1999). PubMed:12428809

Appears in Networks:

p(FPLX:ERK) increases act(p(FPLX:NFkappaB)) View Subject | View Object

Pharmacologic inhibition of ERK and p38 MAPK and dominant- negative mutation of both enzymes suppressed Aβ-induced NF-κB transactivation thus neurotoxicity by Aβ [45,46]. PubMed:27288790

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.