Equivalencies: 0 | Classes: 1 | Children: 0 | Explore

Entity

Name
amyloid-beta oligomers
Namespace
HBP
Namespace Version
20181221
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/bd0996a28201cad363557315043c6392e31abf58/export/hbp-names.belns

Appears in Networks 13

albuquerque2009 v1.0.0

This file encodes the article Mammalian Nicotinic Acetylcholine Receptors: From Structure to Function by Albuquerque et al, 2009

Alzheimer's disease-type neuronal tau hyperphosphorylation induced by A beta oligomers v1.0.0

This document contains the bel code for the Article Alzheimer’s disease-type neuronal tau hyperphosphorylation induced by Abeta oligomers by De Felice et al

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

In-Edges 13

path(HBP:neurotoxicity) association a(HBP:"amyloid-beta oligomers") View Subject | View Object

Early work on AD considered the fibrillar form to be the toxic species. However, a lack of correlation between plaque burden and cognitive score contrasted with a strong positive correlation between total soluble amyloid and cognitive decline pointing to soluble, oligomeric forms as the primary toxic factor (Walsh and Selkoe, 2007). PubMed:19293145

path(MESH:"Cognitive Dysfunction") positiveCorrelation a(HBP:"amyloid-beta oligomers") View Subject | View Object

Early work on AD considered the fibrillar form to be the toxic species. However, a lack of correlation between plaque burden and cognitive score contrasted with a strong positive correlation between total soluble amyloid and cognitive decline pointing to soluble, oligomeric forms as the primary toxic factor (Walsh and Selkoe, 2007). PubMed:19293145

act(a(GO:"cholinergic synapse")) association a(HBP:"amyloid-beta oligomers") View Subject | View Object

It has been demonstrated that cholinergic synapses are particularly affected by Aβ oligomers early neurotoxicity [218, 219] and that synaptic loss is the major correlate of cognitive impairment PubMed:26813123

a(CHEBI:nicotine) decreases a(HBP:"amyloid-beta oligomers") View Subject | View Object

The amount of Abeta was quantified, and following nicotine injections a reduction in Abeta, particularly in the oligomeric form, was found PubMed:25514383

p(MGI:App, frag("25_35")) increases a(HBP:"amyloid-beta oligomers", loc(GO:"extracellular region")) View Subject | View Object

In contrast, brain sections of animals treated with 10-nmol-aged Ab25–35 peptide demonstrated the presence of numerous and distinct extracellular amyloid deposits, widely disseminated throughout the brain (Fig. 5). PubMed:25881725

p(INTERPRO:"Kinase associated domain 1 (KA1)") positiveCorrelation act(a(HBP:"amyloid-beta oligomers")) View Subject | View Object

To probe the involvement of endogenous MARK kinases in mediating the synaptic toxicity of Aβ, we employed a peptide inhibitor capable of effectively and specifically inhibiting the activities of all PAR-1/MARK family members. This inhibitor abrogated the toxic effects of Aβ oligomers on dendritic spines and synapses as assayed at the morphological and electrophysiological levels. PubMed:22156579

Appears in Networks:

bp(GO:"response to acidic pH") increases a(HBP:"amyloid-beta oligomers") View Subject | View Object

The acidic environment in lysosomes is particularly favorable for the initial stages of Ab oligomerization (Peralvarez-Marin et al. 2008). PubMed:22908190

p(HGNC:MAPT, pmod(Ph, Ser, 202)) positiveCorrelation a(HBP:"amyloid-beta oligomers") View Subject | View Object

In addition, it has been reported that in cultured neurons, Aβ oligomers induce MAPT missorting into the somatodendritic compartment, and the missorted MAPT is phosphorylated mainly at the 12E8 (p-S262/p-S356) and AT8 (p-S202/p-T205) sites [6]. PubMed:30145931

p(HGNC:MAPT, pmod(Ph, Ser, 262)) positiveCorrelation a(HBP:"amyloid-beta oligomers") View Subject | View Object

In addition, it has been reported that in cultured neurons, Aβ oligomers induce MAPT missorting into the somatodendritic compartment, and the missorted MAPT is phosphorylated mainly at the 12E8 (p-S262/p-S356) and AT8 (p-S202/p-T205) sites [6]. PubMed:30145931

p(HGNC:MAPT, pmod(Ph, Ser, 356)) positiveCorrelation a(HBP:"amyloid-beta oligomers") View Subject | View Object

In addition, it has been reported that in cultured neurons, Aβ oligomers induce MAPT missorting into the somatodendritic compartment, and the missorted MAPT is phosphorylated mainly at the 12E8 (p-S262/p-S356) and AT8 (p-S202/p-T205) sites [6]. PubMed:30145931

p(HGNC:MAPT, pmod(Ph, Thr, 205)) positiveCorrelation a(HBP:"amyloid-beta oligomers") View Subject | View Object

In addition, it has been reported that in cultured neurons, Aβ oligomers induce MAPT missorting into the somatodendritic compartment, and the missorted MAPT is phosphorylated mainly at the 12E8 (p-S262/p-S356) and AT8 (p-S202/p-T205) sites [6]. PubMed:30145931

p(HGNC:MAPT, pmod(Ph, Ser, 202), pmod(Ph, Thr, 205)) positiveCorrelation a(HBP:"amyloid-beta oligomers") View Subject | View Object

In addition, it has been reported that in cultured neurons, Aβ oligomers induce MAPT missorting into the somatodendritic compartment, and the missorted MAPT is phosphorylated mainly at the 12E8 (p-S262/p-S356) and AT8 (p-S202/p-T205) sites [6]. PubMed:30145931

p(HGNC:MAPT, pmod(Ph, Ser, 262), pmod(Ph, Ser, 356)) positiveCorrelation a(HBP:"amyloid-beta oligomers") View Subject | View Object

In addition, it has been reported that in cultured neurons, Aβ oligomers induce MAPT missorting into the somatodendritic compartment, and the missorted MAPT is phosphorylated mainly at the 12E8 (p-S262/p-S356) and AT8 (p-S202/p-T205) sites [6]. PubMed:30145931

Out-Edges 37

a(HBP:"amyloid-beta oligomers") regulates act(p(HGNC:CHRNA7)) View Subject | View Object

However, this appealing scenario is complicated by recent findings that beta-amyloid peptides directly modify alpha7 nAChR function (242, 278). PubMed:19126755

Appears in Networks:
Annotations
Text Location
Review

a(HBP:"amyloid-beta oligomers") positiveCorrelation path(MESH:"Cognitive Dysfunction") View Subject | View Object

Early work on AD considered the fibrillar form to be the toxic species. However, a lack of correlation between plaque burden and cognitive score contrasted with a strong positive correlation between total soluble amyloid and cognitive decline pointing to soluble, oligomeric forms as the primary toxic factor (Walsh and Selkoe, 2007). PubMed:19293145

a(HBP:"amyloid-beta oligomers") association path(HBP:neurotoxicity) View Subject | View Object

Early work on AD considered the fibrillar form to be the toxic species. However, a lack of correlation between plaque burden and cognitive score contrasted with a strong positive correlation between total soluble amyloid and cognitive decline pointing to soluble, oligomeric forms as the primary toxic factor (Walsh and Selkoe, 2007). PubMed:19293145

a(HBP:"amyloid-beta oligomers") directlyIncreases path(HBP:neurotoxicity) View Subject | View Object

However, other naturally occurring oligomeric forms of Abeta are also toxic (Deshpande et al., 2006; Shankar et al., 2008), and evidence is accumulating that the capacity of Abeta, mutant Abeta, or fragments of Abeta to aggregate into oligomers is directly related to toxicity (Luheshi et al., 2007). PubMed:19293145

a(HBP:"amyloid-beta oligomers") increases act(p(FPLX:JNK)) 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

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

a(HBP:"amyloid-beta oligomers") association act(a(GO:"cholinergic synapse")) View Subject | View Object

It has been demonstrated that cholinergic synapses are particularly affected by Aβ oligomers early neurotoxicity [218, 219] and that synaptic loss is the major correlate of cognitive impairment PubMed:26813123

a(HBP:"amyloid-beta oligomers") increases p(HGNC:MAPT, pmod(HBP:hyperphosphorylation)) View Subject | View Object

These results confirm that the tau hyperphosphorylation stimulated by soluble ADDL preparations is indeed oligomer-induced. Tau hyperphosphorylation induced by 10M Abeta fibrils (Fig. 3N) was partially blocked (Fig. 3O), consistent with shared epitopes between oligomers and fibrils. PubMed:17403556

a(HBP:"amyloid-beta oligomers") increases p(HGNC:MAPT, pmod(HBP:hyperphosphorylation)) View Subject | View Object

Importantly, pre-incubation of AD brain extracts with NU1 significantly blocked the increase in Thr231 phosphotau immunofluorescence (Fig. 6G), establishing the tau hyperphosphorylation was induced by Abeta oligomers in the AD brain extracts. NU1 also prevented the binding of brain-derived ADDLs to synaptic hot-spots (Fig. 6H and I). In NU1-treated cultures, the presence of large extracellular aggregates indicates that the antibody sequesters ADDLs and prevents their interactions with neurons (Fig. 6I). PubMed:17403556

a(HBP:"amyloid-beta oligomers") increases p(HGNC:MAPT, loc(MESH:"Post-Synaptic Density")) View Subject | View Object

Abetao exposure induced a translocation of tau into the PSD fraction (***p  0.0002, 2-tailed Student’s t test; control 20.12  1228 vs Abetao 29.74  1.748, N  12 independent culture). There was also an increase of PSD-95 (***p0.0006, 2-tailed Student’s t test; control 19.10  2.557 vs Abetao 33.3  2153, N  9 independent culture), GluA1 (**p  0.0078, 2-tailed Student’s t test; control 18.841.930 vs Abetao 26.221.475,N9 independent culture) and fyn (**p  0.0041, 2-tailed Student’s t test; control 19.42  1.337 vs Abetao 29.67  2.181, N  6 independent cultures; Fig. 6D). PubMed:24760868

a(HBP:"amyloid-beta oligomers") decreases p(HGNC:MAPT, loc(GO:synapse)) View Subject | View Object

After Abetao treatment, synaptic activation did not trigger any increase in synaptic markers and in fact decreased synaptic actin (***p  0.0009, 2-tailed Student’s t test; Abetao 29.64  1.495, Abetao Bic/4-AP 18.56 2.030, N  7 independent cultures; Fig. 7C), PSD-95 (***p0.0007, 2-tailed Student’s t test; Abetao 33.37  2.153, Abetao Bic/4-AP 19.25 2.550, N  7 independent cultures) and tau levels (**p0.0014, 2-tailed Student’s t test; Abetao 29.74 1.748, Abetao Bic/4-AP 20.68 1.751, N  12 independent cultures). PubMed:24760868

a(HBP:"amyloid-beta oligomers") increases tloc(p(HGNC:MAPT)) View Subject | View Object

When we investigated Abetao-driven tau translocation to the synapse, we did not see any change in half-life recovery (4.729 s) from those measured with synaptic activation. However, the plateau value was drastically modified (71.20%), illustrating that, whereas Abetao induced tau translocation and subsequently its interaction with actin filament, the resulting synaptic tau is less stable. PubMed:24760868

a(HBP:"amyloid-beta oligomers") increases p(HGNC:DLG4) View Subject | View Object

Abetao exposure induced a translocation of tau into the PSD fraction (***p  0.0002, 2-tailed Student’s t test; control 20.12  1228 vs Abetao 29.74  1.748, N  12 independent culture). There was also an increase of PSD-95 (***p0.0006, 2-tailed Student’s t test; control 19.10  2.557 vs Abetao 33.3  2153, N  9 independent culture), GluA1 (**p  0.0078, 2-tailed Student’s t test; control 18.841.930 vs Abetao 26.221.475,N9 independent culture) and fyn (**p  0.0041, 2-tailed Student’s t test; control 19.42  1.337 vs Abetao 29.67  2.181, N  6 independent cultures; Fig. 6D). PubMed:24760868

a(HBP:"amyloid-beta oligomers") decreases p(HGNC:DLG4, loc(GO:synapse)) View Subject | View Object

After Abetao treatment, synaptic activation did not trigger any increase in synaptic markers and in fact decreased synaptic actin (***p  0.0009, 2-tailed Student’s t test; Abetao 29.64  1.495, Abetao Bic/4-AP 18.56 2.030, N  7 independent cultures; Fig. 7C), PSD-95 (***p0.0007, 2-tailed Student’s t test; Abetao 33.37  2.153, Abetao Bic/4-AP 19.25 2.550, N  7 independent cultures) and tau levels (**p0.0014, 2-tailed Student’s t test; Abetao 29.74 1.748, Abetao Bic/4-AP 20.68 1.751, N  12 independent cultures). PubMed:24760868

a(HBP:"amyloid-beta oligomers") increases p(HGNC:GRIA1) View Subject | View Object

Abetao exposure induced a translocation of tau into the PSD fraction (***p  0.0002, 2-tailed Student’s t test; control 20.12  1228 vs Abetao 29.74  1.748, N  12 independent culture). There was also an increase of PSD-95 (***p0.0006, 2-tailed Student’s t test; control 19.10  2.557 vs Abetao 33.3  2153, N  9 independent culture), GluA1 (**p  0.0078, 2-tailed Student’s t test; control 18.841.930 vs Abetao 26.221.475,N9 independent culture) and fyn (**p  0.0041, 2-tailed Student’s t test; control 19.42  1.337 vs Abetao 29.67  2.181, N  6 independent cultures; Fig. 6D). PubMed:24760868

a(HBP:"amyloid-beta oligomers") increases p(HGNC:FYN) View Subject | View Object

Abetao exposure induced a translocation of tau into the PSD fraction (***p  0.0002, 2-tailed Student’s t test; control 20.12  1228 vs Abetao 29.74  1.748, N  12 independent culture). There was also an increase of PSD-95 (***p0.0006, 2-tailed Student’s t test; control 19.10  2.557 vs Abetao 33.3  2153, N  9 independent culture), GluA1 (**p  0.0078, 2-tailed Student’s t test; control 18.841.930 vs Abetao 26.221.475,N9 independent culture) and fyn (**p  0.0041, 2-tailed Student’s t test; control 19.42  1.337 vs Abetao 29.67  2.181, N  6 independent cultures; Fig. 6D). PubMed:24760868

a(HBP:"amyloid-beta oligomers") decreases bp(GO:"actin filament polymerization") View Subject | View Object

Preceded by 15 min Abetao treatment, synaptic activation disrupted LifeAct-RFP fluorescence, suggesting an alteration of F-actin organization and no additional EGFPtau recruitment at the synapse. PubMed:24760868

a(HBP:"amyloid-beta oligomers") decreases a(MESH:Actins, loc(GO:synapse)) View Subject | View Object

After Abetao treatment, synaptic activation did not trigger any increase in synaptic markers and in fact decreased synaptic actin (***p  0.0009, 2-tailed Student’s t test; Abetao 29.64  1.495, Abetao Bic/4-AP 18.56 2.030, N  7 independent cultures; Fig. 7C), PSD-95 (***p0.0007, 2-tailed Student’s t test; Abetao 33.37  2.153, Abetao Bic/4-AP 19.25 2.550, N  7 independent cultures) and tau levels (**p0.0014, 2-tailed Student’s t test; Abetao 29.74 1.748, Abetao Bic/4-AP 20.68 1.751, N  12 independent cultures). PubMed:24760868

a(HBP:"amyloid-beta oligomers") increases complex(complex(GO:"filamentous actin"), p(HGNC:MAPT)) View Subject | View Object

Finally, we performed a phalloidin precipitation assay after a 15 min Abetao treatment on our neuron culture (Fig. 8A) and observed that tau/F-actin content was increased (**,*p 0.05 relative to control, #p  0.05 relative to Abetao, 1-way ANOVA; control 15.45  1.529, Abetao 32.90  3.181, Abetao Bic/ 4-AP 20.182671 for actin; control 16.342.618, Abetao 31.77 1.952, Abetao Bic/4-AP 17.704.080 for tau,N5 independent cultures Fig. 8B). A subsequent synaptic activation did alter tau interaction with F-actin. PubMed:24760868

a(HBP:"amyloid-beta oligomers") increases complex(complex(GO:"filamentous actin"), p(HGNC:MAPT)) View Subject | View Object

When we investigated Abetao-driven tau translocation to the synapse, we did not see any change in half-life recovery (4.729 s) from those measured with synaptic activation. However, the plateau value was drastically modified (71.20%), illustrating that, whereas Abetao induced tau translocation and subsequently its interaction with actin filament, the resulting synaptic tau is less stable. PubMed:24760868

a(HBP:"amyloid-beta oligomers") decreases complex(a(MESH:"Dendritic Spines"), p(HGNC:MAPT)) View Subject | View Object

When we investigated Abetao-driven tau translocation to the synapse, we did not see any change in half-life recovery (4.729 s) from those measured with synaptic activation. However, the plateau value was drastically modified (71.20%), illustrating that, whereas Abetao induced tau translocation and subsequently its interaction with actin filament, the resulting synaptic tau is less stable. PubMed:24760868

a(HBP:"amyloid-beta oligomers") decreases p(HGNC:MAPT, pmod(Ph, Thr, 205)) View Subject | View Object

Thr-205 phosphorylated tau was only increased under synaptic activation in the PSD fraction (control 24.57  0.9754 vs Bic/4-AP 38.90  1.936; Fig. 9E), whereas it was decreased after Abetao treatment (control 24.57  0.9754 vs Abeta 13.64  2.416). Synaptic activation after Abetao exposure did not produce any significant Thr-205 phosphorylation of tau (Abeta Bic/4-AP 22.892.796 vs Bic/ 4-AP 38.90  1.93 vs Abeta 13.642.50). PubMed:24760868

a(HBP:"amyloid-beta oligomers") increases p(HGNC:MAPT, pmod(Ph, Ser, 404)) View Subject | View Object

Conversely, only Abetao exposure promoted significant tau phosphorylation on Ser 404 (**p0.05, 1-way ANOVA; control 15.672.418 vs Abetao 32.65  3.76 vs Bic/4-AP 26.75  1.17 vs Abetao Bic/4-AP 24.97  4.48, N  4). These results revealed that, although synaptic activation or Abetao promote tau translocation to PSD fractions, the synaptic tau displays a different phosphorylation profile that may be responsible for the conditional tau properties observed. PubMed:24760868

a(HBP:"amyloid-beta oligomers") regulates p(HGNC:MAPT, pmod(Ph)) View Subject | View Object

Conversely, only Abetao exposure promoted significant tau phosphorylation on Ser 404 (**p0.05, 1-way ANOVA; control 15.672.418 vs Abetao 32.65  3.76 vs Bic/4-AP 26.75  1.17 vs Abetao Bic/4-AP 24.97  4.48, N  4). These results revealed that, although synaptic activation or Abetao promote tau translocation to PSD fractions, the synaptic tau displays a different phosphorylation profile that may be responsible for the conditional tau properties observed. PubMed:24760868

a(HBP:"amyloid-beta oligomers") causesNoChange p(HGNC:MAPT, var("p.S404A"), loc(MESH:"Dendritic Spines")) View Subject | View Object

We observed that synaptic activation promoted EGFP-Tau T205A translocation to the spine but FRAP experiments revealed a shorter tau turnover time in the spine (Fig. 9B), whereas Abetao driven translocation to the spine was no longer observable in EGFP-Tau S404A-transfected neurons (Fig. 9F,G). These experiments highlight the pivotal role of these phosphorylations in tau translocation features to the spine. PubMed:24760868

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

Blocking proteasomes using Ab oligomers also effectively facilitates tau accumulation in AD mice (Tseng et al., 2008). PubMed:23528736

a(HBP:"amyloid-beta oligomers") increases p(HGNC:MAPT) View Subject | View Object

Blocking proteasomes using Ab oligomers also effectively facilitates tau accumulation in AD mice (Tseng et al., 2008). PubMed:23528736

a(HBP:"amyloid-beta oligomers") increases p(HGNC:MAPT, pmod(Ph)) View Subject | View Object

Soluble oligomers of Ab42 serve as the prominent synapto- toxic form and induce tau hyperphosphorylation PubMed:22419736

act(a(HBP:"amyloid-beta oligomers")) positiveCorrelation p(INTERPRO:"Kinase associated domain 1 (KA1)") View Subject | View Object

To probe the involvement of endogenous MARK kinases in mediating the synaptic toxicity of Aβ, we employed a peptide inhibitor capable of effectively and specifically inhibiting the activities of all PAR-1/MARK family members. This inhibitor abrogated the toxic effects of Aβ oligomers on dendritic spines and synapses as assayed at the morphological and electrophysiological levels. PubMed:22156579

Appears in Networks:

a(HBP:"amyloid-beta oligomers") increases p(HGNC:MAPT, loc(MESH:Dendrites)) View Subject | View Object

In addition, it has been reported that in cultured neurons, Aβ oligomers induce MAPT missorting into the somatodendritic compartment, and the missorted MAPT is phosphorylated mainly at the 12E8 (p-S262/p-S356) and AT8 (p-S202/p-T205) sites [6]. PubMed:30145931

a(HBP:"amyloid-beta oligomers") positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 262)) View Subject | View Object

In addition, it has been reported that in cultured neurons, Aβ oligomers induce MAPT missorting into the somatodendritic compartment, and the missorted MAPT is phosphorylated mainly at the 12E8 (p-S262/p-S356) and AT8 (p-S202/p-T205) sites [6]. PubMed:30145931

a(HBP:"amyloid-beta oligomers") positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 356)) View Subject | View Object

In addition, it has been reported that in cultured neurons, Aβ oligomers induce MAPT missorting into the somatodendritic compartment, and the missorted MAPT is phosphorylated mainly at the 12E8 (p-S262/p-S356) and AT8 (p-S202/p-T205) sites [6]. PubMed:30145931

a(HBP:"amyloid-beta oligomers") positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 202)) View Subject | View Object

In addition, it has been reported that in cultured neurons, Aβ oligomers induce MAPT missorting into the somatodendritic compartment, and the missorted MAPT is phosphorylated mainly at the 12E8 (p-S262/p-S356) and AT8 (p-S202/p-T205) sites [6]. PubMed:30145931

a(HBP:"amyloid-beta oligomers") positiveCorrelation p(HGNC:MAPT, pmod(Ph, Thr, 205)) View Subject | View Object

In addition, it has been reported that in cultured neurons, Aβ oligomers induce MAPT missorting into the somatodendritic compartment, and the missorted MAPT is phosphorylated mainly at the 12E8 (p-S262/p-S356) and AT8 (p-S202/p-T205) sites [6]. PubMed:30145931

a(HBP:"amyloid-beta oligomers") positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 262), pmod(Ph, Ser, 356)) View Subject | View Object

In addition, it has been reported that in cultured neurons, Aβ oligomers induce MAPT missorting into the somatodendritic compartment, and the missorted MAPT is phosphorylated mainly at the 12E8 (p-S262/p-S356) and AT8 (p-S202/p-T205) sites [6]. PubMed:30145931

a(HBP:"amyloid-beta oligomers") positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 202), pmod(Ph, Thr, 205)) View Subject | View Object

In addition, it has been reported that in cultured neurons, Aβ oligomers induce MAPT missorting into the somatodendritic compartment, and the missorted MAPT is phosphorylated mainly at the 12E8 (p-S262/p-S356) and AT8 (p-S202/p-T205) sites [6]. PubMed:30145931

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.