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Tau oligomers-Cytotoxicity, propagation, and mitochondrial damage v1.0.0

Tau oligomers-Cytotoxicity, propagation, and mitochondrial damage from Shafiei et al., 2017

Tau oligomers and tau toxicity in neurodegenerative disease v1.0.0

Tau oligomers and tau toxicity in neurodegenerative disease by Ward et al., 2012

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

In-Edges 85

bp(MESH:Autophagy) increases deg(a(HBP:"Tau oligomers")) View Subject | View Object

For example, as discussed above, certain modified forms of tau, such as caspase-cleaved tau, have a stronger tendency to aggregate. As tau begins to assemble into oligomers, it may become increasingly undesirable as a proteasomal substrate. These low-order, soluble oligomers may be preferentially degraded by autophagy. PubMed:24027553

act(p(HGNCGENEFAMILY:Proteasome)) causesNoChange deg(a(HBP:"Tau oligomers")) View Subject | View Object

For example, as discussed above, certain modified forms of tau, such as caspase-cleaved tau, have a stronger tendency to aggregate. As tau begins to assemble into oligomers, it may become increasingly undesirable as a proteasomal substrate. These low-order, soluble oligomers may be preferentially degraded by autophagy. PubMed:24027553

a(HBP:"Braak_Stage II") association a(HBP:"Tau oligomers") View Subject | View Object

Indeed, early pre-tangle neurons within the hippocampus were labeled with all antibodies in Braak I-II cases (Fig. 5A–D) PubMed:27574109

a(GO:"Pick body") association a(HBP:"Tau oligomers") View Subject | View Object

Similarly, the characteristic Pick bodies in the frontal cortex were well labeled by TNT1, TOC1 and R1 in PiD tissue (Fig. 5M–P) PubMed:27574109

a(HBP:"Braak_Stage I") association a(HBP:"Tau oligomers") View Subject | View Object

Indeed, early pre-tangle neurons within the hippocampus were labeled with all antibodies in Braak I-II cases (Fig. 5A–D) PubMed:27574109

a(HBP:"Corticobasal Degeneration") association a(HBP:"Tau oligomers") View Subject | View Object

In CBD, the characteristic astrocytic pathology (e.g. astrocytic plaques) showed extensive co-localization between TNT1, TOC1 and R1 in the frontal cortex (Fig. 5I–L). PubMed:27574109

a(HBP:"Corticobasal Degeneration") positiveCorrelation a(HBP:"Tau oligomers") View Subject | View Object

Similarly, the soluble fraction from AD contained the greatest level of TOC1 reactivity, followed by CBD and then PiD had the lowest signal (Fig. 6D; one-way ANOVA with Holm-Sidak post-hoc, F(2,9) = 16.57, p = 0.001) PubMed:27574109

a(HBP:"Corticobasal Degeneration") positiveCorrelation a(HBP:"Tau oligomers") View Subject | View Object

TOC1 detected significantly more oligomeric tau in AD compared to CBD and PiD and more in CBD compared to PiD (Fig. 6G; one-way ANOVA with Holm-Sidak post-hoc, F(2,9) = 35.32, p < 0.0001) PubMed:27574109

a(HBP:"Tau isoform B (381 aa)") increases a(HBP:"Tau oligomers") View Subject | View Object

As expected, monomer and aggregated samples of all six tau isoforms showed equal reactivity for TNT1 and TOC1 when the samples were denatured because this exposes the epitopes making them equally accessible (Student’s t-tests, for all comparisons p > 0.05; Fig. 3C–H) PubMed:27574109

a(HBP:"Tau isoform C (410 aa)") increases a(HBP:"Tau oligomers") View Subject | View Object

Comparisons between isoform monomers showed that hT39 monomer signal was significantly higher than hT24 and hT23 monomers (Kruskal-Wallis ANOVA with Dunn’s post-hoc, H = 18.6, p = 0.0023) PubMed:27574109

a(HBP:"Tau isoform C (410 aa)") increases a(HBP:"Tau oligomers") View Subject | View Object

As expected, monomer and aggregated samples of all six tau isoforms showed equal reactivity for TNT1 and TOC1 when the samples were denatured because this exposes the epitopes making them equally accessible (Student’s t-tests, for all comparisons p > 0.05; Fig. 3C–H) PubMed:27574109

a(HBP:"Tau isoform D (383 aa)") increases a(HBP:"Tau oligomers") View Subject | View Object

Comparisons between isoform monomers showed that hT39 monomer signal was significantly higher than hT24 and hT23 monomers (Kruskal-Wallis ANOVA with Dunn’s post-hoc, H = 18.6, p = 0.0023) PubMed:27574109

a(HBP:"Tau isoform D (383 aa)") increases a(HBP:"Tau oligomers") View Subject | View Object

As expected, monomer and aggregated samples of all six tau isoforms showed equal reactivity for TNT1 and TOC1 when the samples were denatured because this exposes the epitopes making them equally accessible (Student’s t-tests, for all comparisons p > 0.05; Fig. 3C–H) PubMed:27574109

a(HBP:"Tau isoform E (412 aa)") increases a(HBP:"Tau oligomers") View Subject | View Object

As expected, monomer and aggregated samples of all six tau isoforms showed equal reactivity for TNT1 and TOC1 when the samples were denatured because this exposes the epitopes making them equally accessible (Student’s t-tests, for all comparisons p > 0.05; Fig. 3C–H) PubMed:27574109

a(HBP:"Tau isoform F (441 aa)") increases a(HBP:"Tau oligomers") View Subject | View Object

As expected, monomer and aggregated samples of all six tau isoforms showed equal reactivity for TNT1 and TOC1 when the samples were denatured because this exposes the epitopes making them equally accessible (Student’s t-tests, for all comparisons p > 0.05; Fig. 3C–H) PubMed:27574109

a(HBP:"Tau isoform Fetal-tau (352 aa)") increases a(HBP:"Tau oligomers") View Subject | View Object

Comparisons between isoform monomers showed that hT39 monomer signal was significantly higher than hT24 and hT23 monomers (Kruskal-Wallis ANOVA with Dunn’s post-hoc, H = 18.6, p = 0.0023) PubMed:27574109

a(HBP:"Tau isoform Fetal-tau (352 aa)") increases a(HBP:"Tau oligomers") View Subject | View Object

As expected, monomer and aggregated samples of all six tau isoforms showed equal reactivity for TNT1 and TOC1 when the samples were denatured because this exposes the epitopes making them equally accessible (Student’s t-tests, for all comparisons p > 0.05; Fig. 3C–H) PubMed:27574109

a(HBP:pretangles) association a(HBP:"Tau oligomers") View Subject | View Object

Indeed, early pre-tangle neurons within the hippocampus were labeled with all antibodies in Braak I-II cases (Fig. 5A–D) PubMed:27574109

a(MESH:"Neurofibrillary Tangles") association a(HBP:"Tau oligomers") View Subject | View Object

In severe AD cases (i.e. Braak stage V-VI), all markers continue to colocalize in classic NFTs within the hippocampus that characterize AD tau pathology (Fig. 5E–H) PubMed:27574109

p(HBP:"Tau isoform B (381 aa)", pmod(HBP:"protein aggregation")) increases a(HBP:"Tau oligomers") View Subject | View Object

The hT24 aggregates showed the highest TOC1 signal, which reached significance compared to hT40, hT39, hT37 and hT23 aggregates, while hT34 aggregates were significantly different from hT39, hT37 and hT23 aggregates, and both hT40 and hT39 aggregates are significantly higher than hT37 and hT23 (one-way ANOVA with Holm-Sidak post-hoc, F(5, 18) = 50.77, p < 0.0001) PubMed:27574109

p(HBP:"Tau isoform B (381 aa)", pmod(HBP:"protein aggregation")) increases a(HBP:"Tau oligomers") View Subject | View Object

Aggregated samples for all six isoforms showed significant increases in TOC1 reactivity when compared to their respective monomer samples (Fig. 3B; Mann-Whitney tests, for all comparisons p = 0.029) PubMed:27574109

p(HBP:"Tau isoform B (381 aa)", pmod(HBP:"protein aggregation")) increases a(HBP:"Tau oligomers") View Subject | View Object

As expected, monomer and aggregated samples of all six tau isoforms showed equal reactivity for TNT1 and TOC1 when the samples were denatured because this exposes the epitopes making them equally accessible (Student’s t-tests, for all comparisons p > 0.05; Fig. 3C–H) PubMed:27574109

p(HBP:"Tau isoform C (410 aa)", pmod(HBP:"protein aggregation")) increases a(HBP:"Tau oligomers") View Subject | View Object

The hT24 aggregates showed the highest TOC1 signal, which reached significance compared to hT40, hT39, hT37 and hT23 aggregates, while hT34 aggregates were significantly different from hT39, hT37 and hT23 aggregates, and both hT40 and hT39 aggregates are significantly higher than hT37 and hT23 (one-way ANOVA with Holm-Sidak post-hoc, F(5, 18) = 50.77, p < 0.0001) PubMed:27574109

p(HBP:"Tau isoform C (410 aa)", pmod(HBP:"protein aggregation")) increases a(HBP:"Tau oligomers") View Subject | View Object

Aggregated samples for all six isoforms showed significant increases in TOC1 reactivity when compared to their respective monomer samples (Fig. 3B; Mann-Whitney tests, for all comparisons p = 0.029) PubMed:27574109

p(HBP:"Tau isoform C (410 aa)", pmod(HBP:"protein aggregation")) increases a(HBP:"Tau oligomers") View Subject | View Object

As expected, monomer and aggregated samples of all six tau isoforms showed equal reactivity for TNT1 and TOC1 when the samples were denatured because this exposes the epitopes making them equally accessible (Student’s t-tests, for all comparisons p > 0.05; Fig. 3C–H) PubMed:27574109

p(HBP:"Tau isoform D (383 aa)", pmod(HBP:"protein aggregation")) increases a(HBP:"Tau oligomers") View Subject | View Object

The hT24 aggregates showed the highest TOC1 signal, which reached significance compared to hT40, hT39, hT37 and hT23 aggregates, while hT34 aggregates were significantly different from hT39, hT37 and hT23 aggregates, and both hT40 and hT39 aggregates are significantly higher than hT37 and hT23 (one-way ANOVA with Holm-Sidak post-hoc, F(5, 18) = 50.77, p < 0.0001) PubMed:27574109

p(HBP:"Tau isoform D (383 aa)", pmod(HBP:"protein aggregation")) increases a(HBP:"Tau oligomers") View Subject | View Object

Aggregated samples for all six isoforms showed significant increases in TOC1 reactivity when compared to their respective monomer samples (Fig. 3B; Mann-Whitney tests, for all comparisons p = 0.029) PubMed:27574109

p(HBP:"Tau isoform D (383 aa)", pmod(HBP:"protein aggregation")) increases a(HBP:"Tau oligomers") View Subject | View Object

As expected, monomer and aggregated samples of all six tau isoforms showed equal reactivity for TNT1 and TOC1 when the samples were denatured because this exposes the epitopes making them equally accessible (Student’s t-tests, for all comparisons p > 0.05; Fig. 3C–H) PubMed:27574109

p(HBP:"Tau isoform E (412 aa)", pmod(HBP:"protein aggregation")) increases a(HBP:"Tau oligomers") View Subject | View Object

The hT24 aggregates showed the highest TOC1 signal, which reached significance compared to hT40, hT39, hT37 and hT23 aggregates, while hT34 aggregates were significantly different from hT39, hT37 and hT23 aggregates, and both hT40 and hT39 aggregates are significantly higher than hT37 and hT23 (one-way ANOVA with Holm-Sidak post-hoc, F(5, 18) = 50.77, p < 0.0001) PubMed:27574109

p(HBP:"Tau isoform E (412 aa)", pmod(HBP:"protein aggregation")) increases a(HBP:"Tau oligomers") View Subject | View Object

Aggregated samples for all six isoforms showed significant increases in TOC1 reactivity when compared to their respective monomer samples (Fig. 3B; Mann-Whitney tests, for all comparisons p = 0.029) PubMed:27574109

p(HBP:"Tau isoform E (412 aa)", pmod(HBP:"protein aggregation")) increases a(HBP:"Tau oligomers") View Subject | View Object

As expected, monomer and aggregated samples of all six tau isoforms showed equal reactivity for TNT1 and TOC1 when the samples were denatured because this exposes the epitopes making them equally accessible (Student’s t-tests, for all comparisons p > 0.05; Fig. 3C–H) PubMed:27574109

p(HBP:"Tau isoform F (441 aa)", pmod(HBP:"protein aggregation")) increases a(HBP:"Tau oligomers") View Subject | View Object

The hT24 aggregates showed the highest TOC1 signal, which reached significance compared to hT40, hT39, hT37 and hT23 aggregates, while hT34 aggregates were significantly different from hT39, hT37 and hT23 aggregates, and both hT40 and hT39 aggregates are significantly higher than hT37 and hT23 (one-way ANOVA with Holm-Sidak post-hoc, F(5, 18) = 50.77, p < 0.0001) PubMed:27574109

p(HBP:"Tau isoform F (441 aa)", pmod(HBP:"protein aggregation")) increases a(HBP:"Tau oligomers") View Subject | View Object

Aggregated samples for all six isoforms showed significant increases in TOC1 reactivity when compared to their respective monomer samples (Fig. 3B; Mann-Whitney tests, for all comparisons p = 0.029) PubMed:27574109

p(HBP:"Tau isoform F (441 aa)", pmod(HBP:"protein aggregation")) increases a(HBP:"Tau oligomers") View Subject | View Object

As expected, monomer and aggregated samples of all six tau isoforms showed equal reactivity for TNT1 and TOC1 when the samples were denatured because this exposes the epitopes making them equally accessible (Student’s t-tests, for all comparisons p > 0.05; Fig. 3C–H) PubMed:27574109

p(HBP:"Tau isoform Fetal-tau (352 aa)", pmod(HBP:"protein aggregation")) increases a(HBP:"Tau oligomers") View Subject | View Object

The hT24 aggregates showed the highest TOC1 signal, which reached significance compared to hT40, hT39, hT37 and hT23 aggregates, while hT34 aggregates were significantly different from hT39, hT37 and hT23 aggregates, and both hT40 and hT39 aggregates are significantly higher than hT37 and hT23 (one-way ANOVA with Holm-Sidak post-hoc, F(5, 18) = 50.77, p < 0.0001) PubMed:27574109

p(HBP:"Tau isoform Fetal-tau (352 aa)", pmod(HBP:"protein aggregation")) increases a(HBP:"Tau oligomers") View Subject | View Object

Aggregated samples for all six isoforms showed significant increases in TOC1 reactivity when compared to their respective monomer samples (Fig. 3B; Mann-Whitney tests, for all comparisons p = 0.029) PubMed:27574109

p(HBP:"Tau isoform Fetal-tau (352 aa)", pmod(HBP:"protein aggregation")) increases a(HBP:"Tau oligomers") View Subject | View Object

As expected, monomer and aggregated samples of all six tau isoforms showed equal reactivity for TNT1 and TOC1 when the samples were denatured because this exposes the epitopes making them equally accessible (Student’s t-tests, for all comparisons p > 0.05; Fig. 3C–H) PubMed:27574109

path(MESH:"Alzheimer Disease") positiveCorrelation a(HBP:"Tau oligomers") View Subject | View Object

Similarly, the soluble fraction from AD contained the greatest level of TOC1 reactivity, followed by CBD and then PiD had the lowest signal (Fig. 6D; one-way ANOVA with Holm-Sidak post-hoc, F(2,9) = 16.57, p = 0.001) PubMed:27574109

path(MESH:"Alzheimer Disease") positiveCorrelation a(HBP:"Tau oligomers") View Subject | View Object

TOC1 detected significantly more oligomeric tau in AD compared to CBD and PiD and more in CBD compared to PiD (Fig. 6G; one-way ANOVA with Holm-Sidak post-hoc, F(2,9) = 35.32, p < 0.0001) PubMed:27574109

path(MESH:"Pick Disease of the Brain") positiveCorrelation a(HBP:"Tau oligomers") View Subject | View Object

Similarly, the soluble fraction from AD contained the greatest level of TOC1 reactivity, followed by CBD and then PiD had the lowest signal (Fig. 6D; one-way ANOVA with Holm-Sidak post-hoc, F(2,9) = 16.57, p = 0.001) PubMed:27574109

path(MESH:"Pick Disease of the Brain") positiveCorrelation a(HBP:"Tau oligomers") View Subject | View Object

TOC1 detected significantly more oligomeric tau in AD compared to CBD and PiD and more in CBD compared to PiD (Fig. 6G; one-way ANOVA with Holm-Sidak post-hoc, F(2,9) = 35.32, p < 0.0001) PubMed:27574109

path(MESH:Tauopathies) positiveCorrelation a(HBP:"Tau oligomers") View Subject | View Object

In general, the remarkable co-localization between TNT1, TOC1 and R1 in all tauopathies confirms that PAD exposure and tau oligomerization occur simultaneously in cells displaying tau pathology, irrespective of isoform composition PubMed:27574109

a(CHEBI:Anatabine) decreases a(HBP:"Tau oligomers") View Subject | View Object

Additionally, a significant reduction (P<0.05) in tau oligomers levels (TOC1 immunopositive) was detected both in the brain and the spinal cord of Tg Tau P301S treated with anatabine using dot-blots (Figure 8). DOI:10.4172/2168-975X.1000126

a(CHEBI:Anatabine) decreases a(HBP:"Tau oligomers") View Subject | View Object

We observed that anatabine significantly prevented the formation of MC1-positive tau oligomers (Figure 9) by western-blots in both the brain and the spinal cord of Tg Tau P301S mice (T-tests, P<0.05) further confirming the data obtained with the dot-blots DOI:10.4172/2168-975X.1000126

a(HBP:"Tau oligomers") positiveCorrelation tloc(a(HBP:"Tau oligomers"), fromLoc(GO:"extracellular region"), toLoc(GO:intracellular)) View Subject | View Object

Monomeric, oligomeric and sonicated fibrils were efficiently internalized, while fibril samples were not (Fig. 1c and Supplementary Fig. 1d) PubMed:29686391

tloc(a(HBP:"Tau oligomers"), fromLoc(GO:"extracellular region"), toLoc(GO:intracellular)) positiveCorrelation a(HBP:"Tau oligomers") View Subject | View Object

Monomeric, oligomeric and sonicated fibrils were efficiently internalized, while fibril samples were not (Fig. 1c and Supplementary Fig. 1d) PubMed:29686391

bp(HBP:neurotoxicity) positiveCorrelation a(HBP:"Tau oligomers") View Subject | View Object

Tau protein can form multiple quaternary structures in solution, and recent evidence suggests that small tau oligomeric species may play a critical role in the spread of tau pathology and neurotoxicity PubMed:29686391

p(HGNC:DNM2) increases tloc(a(HBP:"Tau oligomers"), fromLoc(GO:"extracellular region"), toLoc(GO:intracellular)) View Subject | View Object

These single gene knockdowns repressed uptake of tau monomer by over 50% (Fig. 2b) and also reduced the uptake of tau oligomers (Fig. 2c) PubMed:29686391

p(HGNC:EXT2) increases tloc(a(HBP:"Tau oligomers"), fromLoc(GO:"extracellular region"), toLoc(GO:intracellular)) View Subject | View Object

These single gene knockdowns repressed uptake of tau monomer by over 50% (Fig. 2b) and also reduced the uptake of tau oligomers (Fig. 2c) PubMed:29686391

p(HGNC:HS6ST1) increases tloc(a(HBP:"Tau oligomers"), fromLoc(GO:"extracellular region"), toLoc(GO:intracellular)) View Subject | View Object

These single gene knockdowns repressed uptake of tau monomer by over 50% (Fig. 2b) and also reduced the uptake of tau oligomers (Fig. 2c) PubMed:29686391

path(MESH:Tauopathies) positiveCorrelation a(HBP:"Tau oligomers") View Subject | View Object

Tau protein can form multiple quaternary structures in solution, and recent evidence suggests that small tau oligomeric species may play a critical role in the spread of tau pathology and neurotoxicity PubMed:29686391

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

Hyper-phosphorylated tau assembles into small aggregates known as tau oligomers in route of NFT formation PubMed:28420982

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

As hyperphosphorylated tau dislodges from microtubules, its affinity for other tau monomers leads individual tau to bind each other, forming oligomeric tau, a detergent-soluble aggregate PubMed:28420982

p(HGNC:PRNP) association a(HBP:"Tau oligomers") View Subject | View Object

Recently, data has shown that injected tau oligomers colocalize with the mitochondrial marker porin, suggesting a pathological relationship PubMed:28420982

path(MESH:"Alzheimer Disease") positiveCorrelation a(HBP:"Tau oligomers") View Subject | View Object

The onset of clinical symptoms in AD and PSP brains correlate with elevated levels of tau oligomer (Maeda et al., 2006, 2007; Patterson et al., 2011; Lasagna-Reeves et al., 2012b; Gerson et al., 2014a) PubMed:28420982

path(MESH:"Supranuclear Palsy, Progressive") positiveCorrelation a(HBP:"Tau oligomers") View Subject | View Object

The onset of clinical symptoms in AD and PSP brains correlate with elevated levels of tau oligomer (Maeda et al., 2006, 2007; Patterson et al., 2011; Lasagna-Reeves et al., 2012b; Gerson et al., 2014a) PubMed:28420982

p(HGNC:AHSA1) increases a(HBP:"Tau oligomers") 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

a(CHEBI:"arachidonic acid") increases a(HBP:"Tau oligomers") View Subject | View Object

Employing recombinant full-length hT40, we observe the presence of oligomers approximately 15 min after the addition of the anionic inducer arachidonic acid, whereas filament formation requires 5–6 h to attain steady state (Figures 1A–1C) PubMed:22817713

composite(a(HBP:"Tau aggregates"), p(HGNC:MAPT)) increases a(HBP:"Tau oligomers") View Subject | View Object

Compared to monomers, aggregation significantly increased PAD exposure for both hT40 and S422E samples (Fig. 3B; F(1,12) = 685.8, p b 0.0001), as indicated by increased TNT1 reactivity. Aggregation also significantly increased oligomer formation (TOC1 reactivity) compared to monomers in both hT40 and S422E samples (Fig. 3C; F(1,12) = 109.3, p b 0.0001). PubMed:27373205

p(HGNC:MAPT) increases a(HBP:"Tau oligomers") View Subject | View Object

For both tau constructs, there were significantly more oligomer-type aggregates than short or long filaments formed, but no significant difference between the numbers of short or long filament (Fig. 2E; F(2,12) = 86.64, p b 0.0001). S422E did not differ significantly from hT40 in the number of oligomers, short filaments, or long filaments formed (F(1,12) = 0.05, p = 0.83). PubMed:27373205

composite(a(HBP:"Tau aggregates"), p(HGNC:MAPT, var("p.S422E"))) increases a(HBP:"Tau oligomers") View Subject | View Object

Compared to monomers, aggregation significantly increased PAD exposure for both hT40 and S422E samples (Fig. 3B; F(1,12) = 685.8, p b 0.0001), as indicated by increased TNT1 reactivity. Aggregation also significantly increased oligomer formation (TOC1 reactivity) compared to monomers in both hT40 and S422E samples (Fig. 3C; F(1,12) = 109.3, p b 0.0001). PubMed:27373205

p(HGNC:MAPT, var("p.S422E")) increases a(HBP:"Tau oligomers") View Subject | View Object

For both tau constructs, there were significantly more oligomer-type aggregates than short or long filaments formed, but no significant difference between the numbers of short or long filament (Fig. 2E; F(2,12) = 86.64, p b 0.0001). S422E did not differ significantly from hT40 in the number of oligomers, short filaments, or long filaments formed (F(1,12) = 0.05, p = 0.83). PubMed:27373205

complex(p(HGNC:MAPT), p(HGNC:MAPT)) increases a(HBP:"Tau oligomers") View Subject | View Object

Time-course aggregation analysis revealed that dimerization precedes tau oligomerization which, in turn, is an earlier event than the formation of full-length filaments PubMed:22817713

p(HGNC:MAPT, pmod(Ph, Ser, 202)) association a(HBP:"Tau oligomers") View Subject | View Object

TNT1 also co-localizes in tissue with the phospho-epitope defined by the AT8 antibody, indicating that PAD exposure represents an early event in AD pathology PubMed:22817713

p(HGNC:MAPT, pmod(Ph, Ser, 422)) association a(HBP:"Tau oligomers") View Subject | View Object

TOC1’s immunoreactivity is greatly elevated in AD brains compared with healthy controls, but co-localizes best with early-stage markers for AD pathogenesis such as pS422 [16] PubMed:22817713

p(HGNC:MAPT, pmod(Ph, Thr, 205)) association a(HBP:"Tau oligomers") View Subject | View Object

TNT1 also co-localizes in tissue with the phospho-epitope defined by the AT8 antibody, indicating that PAD exposure represents an early event in AD pathology PubMed:22817713

path(MESH:"Alzheimer Disease") increases a(HBP:"Tau oligomers") View Subject | View Object

TOC1’s immunoreactivity is greatly elevated in AD brains compared with healthy controls, but co-localizes best with early-stage markers for AD pathogenesis such as pS422 [16] PubMed:22817713

a(HBP:"8-nitro-cGMP") decreases a(HBP:"Tau oligomers") View Subject | View Object

Tau contains cysteine residues in the microtubule binding region following alternative splicing of exon 10, and formation of intermolecular cysteine disulfide bonds accelerates tau aggregation. 8-Nitro-cGMP (novel second messenger of NO) exposure induced S-guanylation of tau both in vitro and in tau-overexpressed HEK293T cells. S-guanylated tau inhibited heparin-induced tau aggregation (thioflavin T). S-guanylated tau could not form tau granules and fibrils (AFM) inhibited at the step of tau oligomer formation. In P301L tau-expressing Neuro2A cells, 8-nitro-cGMP reduced the amount of sarcosyl-insoluble tau. NO-linked chemical modification on cysteine residues of tau could block tau aggregation PubMed:27601475

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a(HBP:neuroinflammation) positiveCorrelation a(HBP:"Tau oligomers") View Subject | View Object

Tau Oligomers co-localize with astrocytes, microglia, and HMGB1, a pro-inflammatory cytokine, are present in the retina and are associated with inflammatory cells. PubMed:27716675

Appears in Networks:

p(HBP:"phosphatase-activating domain") positiveCorrelation act(a(HBP:"Tau oligomers")) View Subject | View Object

Several lines of evidence in other tauopathies suggest that tau oligomer formation induces neurotoxicity and that tau oligomer-mediated neurotoxicity involves induction of axonal dysfunction through exposure of an N-terminal motif in tau, the phosphatase-activating domain (PAD). PubMed:26671985

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p(HGNC:OTUB1) increases a(HBP:"Tau oligomers") View Subject | View Object

This revealed a significant increase of oligomeric Tau forms in AAV– Otub1-infected neurons compared with AAV–GFP-infected neurons (Fig. 4c). PubMed:28083634

p(HGNC:OTUB1) increases a(HBP:"Tau oligomers") View Subject | View Object

The induction of oligomeric Tau forms was further confirmed using dot-blot analysis with T22 antibody (Fig. 4d), revealing a significant increase in oligomeric Tau following expression of Otub1. PubMed:28083634

p(MGI:Otub1) increases a(HBP:"Tau oligomers") View Subject | View Object

This revealed a significant increase of monomeric Tau and oligomeric Tau in AAV– Otub1-injected mice compared with AAV–GFP-injected mice (Fig. 7c). PubMed:28083634

p(MGI:Otub1) increases a(HBP:"Tau oligomers") View Subject | View Object

This revealed significantly increased oligomeric Tau in AAV– Otub1-injected mice compared with AAV–GFP-injected control cases (Fig. 7d). PubMed:28083634

p(MGI:Otub1) increases a(HBP:"Tau oligomers") View Subject | View Object

This revealed significantly increased oligomeric Tau forms, following expression of wild-type Otub1, but not following expression of GFP or of the catalytically inactive form of Otub1 (C91A) (Fig. 8c). PubMed:28083634

p(MGI:Otub1, var("p.Cys91Ala")) causesNoChange a(HBP:"Tau oligomers") View Subject | View Object

This revealed significantly increased oligomeric Tau forms, following expression of wild-type Otub1, but not following expression of GFP or of the catalytically inactive form of Otub1 (C91A) (Fig. 8c). PubMed:28083634

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

Analysis of sarkosyl extracts of brain homogenates of mice expressing the pro-aggregant repeat domain TauRDΔK revealed that oligomers are present, partly in a disulfide–cross-linked form (Supplementary Fig. 1). PubMed:28528849

path(MESH:"Alzheimer Disease") positiveCorrelation a(HBP:"Tau oligomers") View Subject | View Object

Whereas control brain homogenate exhibited mainly Tau monomer, the AD brain contained a range of Tau assemblies ranging from n = 1 to n > 20 (Fig. 7, A and B). PubMed:25887395

p(HGNC:MAPT, var("p.Ala152Thr")) increases a(HBP:"Tau oligomers") View Subject | View Object

In addition, this A152T tau enhances the formation of oligomers but not fibres PubMed:26631930

path(MESH:"Alzheimer Disease") positiveCorrelation a(HBP:"Tau oligomers") View Subject | View Object

In an analogy to the evolution of concepts in the ‘amyloid cascade hypothesis’, which proposes that soluble oligomers — rather than insoluble aggregates of amyloid peptides — are the causative agents of neurodegeneration in AD, recent studies have suggested tau oligomers to be the toxic species, and indeed levels of SDS-stable tau oligomers are increased in AD and PSP brains. PubMed:26631930

Annotations
MeSH
Brain

path(MESH:"Supranuclear Palsy, Progressive") positiveCorrelation a(HBP:"Tau oligomers") View Subject | View Object

In an analogy to the evolution of concepts in the ‘amyloid cascade hypothesis’, which proposes that soluble oligomers — rather than insoluble aggregates of amyloid peptides — are the causative agents of neurodegeneration in AD, recent studies have suggested tau oligomers to be the toxic species, and indeed levels of SDS-stable tau oligomers are increased in AD and PSP brains. PubMed:26631930

Annotations
MeSH
Brain

Out-Edges 62

a(HBP:"Tau oligomers") association a(HBP:pretangles) View Subject | View Object

Indeed, early pre-tangle neurons within the hippocampus were labeled with all antibodies in Braak I-II cases (Fig. 5A–D) PubMed:27574109

a(HBP:"Tau oligomers") association a(HBP:"Braak_Stage I") View Subject | View Object

Indeed, early pre-tangle neurons within the hippocampus were labeled with all antibodies in Braak I-II cases (Fig. 5A–D) PubMed:27574109

a(HBP:"Tau oligomers") association a(HBP:"Braak_Stage II") View Subject | View Object

Indeed, early pre-tangle neurons within the hippocampus were labeled with all antibodies in Braak I-II cases (Fig. 5A–D) PubMed:27574109

a(HBP:"Tau oligomers") association a(MESH:"Neurofibrillary Tangles") View Subject | View Object

In severe AD cases (i.e. Braak stage V-VI), all markers continue to colocalize in classic NFTs within the hippocampus that characterize AD tau pathology (Fig. 5E–H) PubMed:27574109

a(HBP:"Tau oligomers") association a(HBP:"Corticobasal Degeneration") View Subject | View Object

In CBD, the characteristic astrocytic pathology (e.g. astrocytic plaques) showed extensive co-localization between TNT1, TOC1 and R1 in the frontal cortex (Fig. 5I–L). PubMed:27574109

a(HBP:"Tau oligomers") positiveCorrelation a(HBP:"Corticobasal Degeneration") View Subject | View Object

Similarly, the soluble fraction from AD contained the greatest level of TOC1 reactivity, followed by CBD and then PiD had the lowest signal (Fig. 6D; one-way ANOVA with Holm-Sidak post-hoc, F(2,9) = 16.57, p = 0.001) PubMed:27574109

a(HBP:"Tau oligomers") positiveCorrelation a(HBP:"Corticobasal Degeneration") View Subject | View Object

TOC1 detected significantly more oligomeric tau in AD compared to CBD and PiD and more in CBD compared to PiD (Fig. 6G; one-way ANOVA with Holm-Sidak post-hoc, F(2,9) = 35.32, p < 0.0001) PubMed:27574109

a(HBP:"Tau oligomers") association a(GO:"Pick body") View Subject | View Object

Similarly, the characteristic Pick bodies in the frontal cortex were well labeled by TNT1, TOC1 and R1 in PiD tissue (Fig. 5M–P) PubMed:27574109

a(HBP:"Tau oligomers") positiveCorrelation path(MESH:Tauopathies) View Subject | View Object

In general, the remarkable co-localization between TNT1, TOC1 and R1 in all tauopathies confirms that PAD exposure and tau oligomerization occur simultaneously in cells displaying tau pathology, irrespective of isoform composition PubMed:27574109

a(HBP:"Tau oligomers") positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

Similarly, the soluble fraction from AD contained the greatest level of TOC1 reactivity, followed by CBD and then PiD had the lowest signal (Fig. 6D; one-way ANOVA with Holm-Sidak post-hoc, F(2,9) = 16.57, p = 0.001) PubMed:27574109

a(HBP:"Tau oligomers") positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

TOC1 detected significantly more oligomeric tau in AD compared to CBD and PiD and more in CBD compared to PiD (Fig. 6G; one-way ANOVA with Holm-Sidak post-hoc, F(2,9) = 35.32, p < 0.0001) PubMed:27574109

a(HBP:"Tau oligomers") positiveCorrelation path(MESH:"Pick Disease of the Brain") View Subject | View Object

Similarly, the soluble fraction from AD contained the greatest level of TOC1 reactivity, followed by CBD and then PiD had the lowest signal (Fig. 6D; one-way ANOVA with Holm-Sidak post-hoc, F(2,9) = 16.57, p = 0.001) PubMed:27574109

a(HBP:"Tau oligomers") positiveCorrelation path(MESH:"Pick Disease of the Brain") View Subject | View Object

TOC1 detected significantly more oligomeric tau in AD compared to CBD and PiD and more in CBD compared to PiD (Fig. 6G; one-way ANOVA with Holm-Sidak post-hoc, F(2,9) = 35.32, p < 0.0001) PubMed:27574109

a(HBP:"Tau oligomers") positiveCorrelation path(MESH:Tauopathies) View Subject | View Object

Tau protein can form multiple quaternary structures in solution, and recent evidence suggests that small tau oligomeric species may play a critical role in the spread of tau pathology and neurotoxicity PubMed:29686391

a(HBP:"Tau oligomers") positiveCorrelation bp(HBP:neurotoxicity) View Subject | View Object

Tau protein can form multiple quaternary structures in solution, and recent evidence suggests that small tau oligomeric species may play a critical role in the spread of tau pathology and neurotoxicity PubMed:29686391

a(HBP:"Tau oligomers") positiveCorrelation tloc(a(HBP:"Tau oligomers"), fromLoc(GO:"extracellular region"), toLoc(GO:intracellular)) View Subject | View Object

Monomeric, oligomeric and sonicated fibrils were efficiently internalized, while fibril samples were not (Fig. 1c and Supplementary Fig. 1d) PubMed:29686391

tloc(a(HBP:"Tau oligomers"), fromLoc(GO:"extracellular region"), toLoc(GO:intracellular)) positiveCorrelation a(HBP:"Tau oligomers") View Subject | View Object

Monomeric, oligomeric and sonicated fibrils were efficiently internalized, while fibril samples were not (Fig. 1c and Supplementary Fig. 1d) PubMed:29686391

a(HBP:"Tau oligomers") increases path(MESH:Disease) View Subject | View Object

While evidence indicates that these deposits are not toxic, many studies suggest that the tau oligomer, an intermediate entity, is likely responsible for disease onset PubMed:28420982

a(HBP:"Tau oligomers") increases bp(HP:Neurodegeneration) View Subject | View Object

These tau oligomers potentiate neuronal damage, leading to neurodegeneration and traumatic brain injury (Hawkins et al., 2013; Gerson et al., 2014a, 2016; Sengupta et al., 2015). Moreover, they have been implicated in synaptic loss as shown in studies of wild-type human tau transgenic mice (Spires et al., 2006; Berger et al., 2007; Clavaguera et al., 2013) PubMed:28420982

a(HBP:"Tau oligomers") increases bp(HP:Neurodegeneration) View Subject | View Object

These studies demonstrate that tau oligomers may be the toxic entities responsible for neurodegeneration in tauopathies (Ward et al., 2012 PubMed:28420982

a(HBP:"Tau oligomers") increases path(MESH:"Brain Injuries, Traumatic") View Subject | View Object

These tau oligomers potentiate neuronal damage, leading to neurodegeneration and traumatic brain injury (Hawkins et al., 2013; Gerson et al., 2014a, 2016; Sengupta et al., 2015). Moreover, they have been implicated in synaptic loss as shown in studies of wild-type human tau transgenic mice (Spires et al., 2006; Berger et al., 2007; Clavaguera et al., 2013) PubMed:28420982

a(HBP:"Tau oligomers") decreases a(GO:synapse) View Subject | View Object

These tau oligomers potentiate neuronal damage, leading to neurodegeneration and traumatic brain injury (Hawkins et al., 2013; Gerson et al., 2014a, 2016; Sengupta et al., 2015). Moreover, they have been implicated in synaptic loss as shown in studies of wild-type human tau transgenic mice (Spires et al., 2006; Berger et al., 2007; Clavaguera et al., 2013) PubMed:28420982

a(HBP:"Tau oligomers") increases a(HBP:"granular tau oligomers") View Subject | View Object

When the oligomer lengthens, it adapts a beta-sheet structure and transforms into a detergent-insoluble aggregate with granular appearance under Atomic Force Microscopy (AFM) PubMed:28420982

a(HBP:"Tau oligomers") positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

The onset of clinical symptoms in AD and PSP brains correlate with elevated levels of tau oligomer (Maeda et al., 2006, 2007; Patterson et al., 2011; Lasagna-Reeves et al., 2012b; Gerson et al., 2014a) PubMed:28420982

a(HBP:"Tau oligomers") positiveCorrelation path(MESH:"Supranuclear Palsy, Progressive") View Subject | View Object

The onset of clinical symptoms in AD and PSP brains correlate with elevated levels of tau oligomer (Maeda et al., 2006, 2007; Patterson et al., 2011; Lasagna-Reeves et al., 2012b; Gerson et al., 2014a) PubMed:28420982

a(HBP:"Tau oligomers") decreases bp(GO:cognition) View Subject | View Object

When tau oligomers, rather than tau monomers or fibrils, are injected into the brain of wild-type mice, cognitive, synaptic, and mitochondrial abnormalities follow (Lasagna- Reeves et al., 2011; Castillo-Carranza et al., 2014b) PubMed:28420982

a(HBP:"Tau oligomers") decreases bp(GO:"mitochondrion organization") View Subject | View Object

When tau oligomers, rather than tau monomers or fibrils, are injected into the brain of wild-type mice, cognitive, synaptic, and mitochondrial abnormalities follow (Lasagna- Reeves et al., 2011; Castillo-Carranza et al., 2014b) PubMed:28420982

a(HBP:"Tau oligomers") decreases bp(GO:"maintenance of synapse structure") View Subject | View Object

When tau oligomers, rather than tau monomers or fibrils, are injected into the brain of wild-type mice, cognitive, synaptic, and mitochondrial abnormalities follow (Lasagna- Reeves et al., 2011; Castillo-Carranza et al., 2014b) PubMed:28420982

a(HBP:"Tau oligomers") increases path(MESH:Tauopathies) View Subject | View Object

This indicates that tauopathies progress via a prion-like mechanism dependent upon tau oligomers (Gerson and Kayed, 2013; Castillo-Carranza et al., 2014b) PubMed:28420982

a(HBP:"Tau oligomers") increases path(MESH:Tauopathies) View Subject | View Object

These studies demonstrate that tau oligomers may be the toxic entities responsible for neurodegeneration in tauopathies (Ward et al., 2012 PubMed:28420982

a(HBP:"Tau oligomers") increases tloc(p(HGNC:MAPT), fromLoc(GO:"neuron part"), toLoc(GO:"neuron part")) View Subject | View Object

With this concept, tau may be able to translocate between neurons and augment toxic tau components; in fact, evidence suggests probability of tau oligomer propagation between synaptically connected neurons (Gendreau and Hall, 2013; Pooler et al., 2013b) PubMed:28420982

a(HBP:"Tau oligomers") decreases bp(GO:memory) View Subject | View Object

Further, mice injected with tau oligomers in the proximity of the hippocampus experienced immediate memory impairment (Lasagna-Reeves et al., 2011) PubMed:28420982

a(HBP:"Tau oligomers") increases a(HBP:"Tau annular protofibrils") View Subject | View Object

The study discovered that APFs form after tau oligomer formation and bypass higher NFT aggregate formation PubMed:28420982

a(HBP:"Tau oligomers") decreases bp(MESH:"Cell Survival") View Subject | View Object

Oligomeric tau intermediates decrease cell viability (Flach et al., 2012) PubMed:28420982

a(HBP:"Tau oligomers") association p(HGNC:PRNP) View Subject | View Object

Recently, data has shown that injected tau oligomers colocalize with the mitochondrial marker porin, suggesting a pathological relationship PubMed:28420982

a(HBP:"Tau oligomers") decreases act(a(GO:microtubule)) View Subject | View Object

In fact, tau oligomers might disrupt microtubule stability and trafficking, thus affecting organelle distribution PubMed:28420982

a(HBP:"Tau oligomers") decreases a(MESH:"Electron Transport Complex I") View Subject | View Object

Also, data shows low levels of complex I in brain hemispheres injected with tau oligomers when compared to brains injected with monomers or fibrils PubMed:28420982

a(HBP:"Tau oligomers") decreases act(a(MESH:"Electron Transport Complex I")) View Subject | View Object

These results imply that tau oligomers initially affect complex I activity and may directly or indirectly disturb the later stage of complex V ATP synthesis (Lasagna-Reeves et al., 2011) PubMed:28420982

a(HBP:"Tau oligomers") decreases bp(GO:"ATP synthesis coupled proton transport") View Subject | View Object

These results imply that tau oligomers initially affect complex I activity and may directly or indirectly disturb the later stage of complex V ATP synthesis (Lasagna-Reeves et al., 2011) PubMed:28420982

a(HBP:"Tau oligomers") increases act(p(HGNC:CASP9)) View Subject | View Object

Hemispheres injected with tau oligomers were found to have increased levels of caspase-9 activation (Lasagna-Reeves et al., 2011) PubMed:28420982

a(HBP:"Tau oligomers") increases sec(p(HGNC:CYCS)) View Subject | View Object

Suggestively, as tau oligomers concentrate at the mitochondrial membrane, cytochrome C is released, leading to caspase-9 activation via a complex with apoptotic-peptidase activating- factor-1 (Apaf-1; Li et al., 1997) PubMed:28420982

a(HBP:"Tau oligomers") increases bp(HBP:neurotoxicity) View Subject | View Object

Together, these findings support the hypothesis that tau oligomers are the toxic form of tau in neurodegenerative disease PubMed:22817713

a(HBP:"Tau oligomers") increases bp(HBP:neurotoxicity) View Subject | View Object

This indicates that tau oligomers represent the main toxic species responsible for neurodegeneration associated with AD PubMed:22817713

a(HBP:"Tau oligomers") increases a(HBP:"Tau aggregates") View Subject | View Object

Time-course aggregation analysis revealed that dimerization precedes tau oligomerization which, in turn, is an earlier event than the formation of full-length filaments PubMed:22817713

a(HBP:"Tau oligomers") association p(HGNC:MAPT, pmod(Ph, Ser, 422)) View Subject | View Object

TOC1’s immunoreactivity is greatly elevated in AD brains compared with healthy controls, but co-localizes best with early-stage markers for AD pathogenesis such as pS422 [16] PubMed:22817713

a(HBP:"Tau oligomers") association p(HGNC:MAPT, pmod(Ph, Ser, 202)) View Subject | View Object

TNT1 also co-localizes in tissue with the phospho-epitope defined by the AT8 antibody, indicating that PAD exposure represents an early event in AD pathology PubMed:22817713

a(HBP:"Tau oligomers") association p(HGNC:MAPT, pmod(Ph, Thr, 205)) View Subject | View Object

TNT1 also co-localizes in tissue with the phospho-epitope defined by the AT8 antibody, indicating that PAD exposure represents an early event in AD pathology PubMed:22817713

a(HBP:"Tau oligomers") increases bp(HP:Neurodegeneration) View Subject | View Object

This indicates that tau oligomers represent the main toxic species responsible for neurodegeneration associated with AD PubMed:22817713

a(HBP:"Tau oligomers") positiveCorrelation a(HBP:neuroinflammation) View Subject | View Object

Tau Oligomers co-localize with astrocytes, microglia, and HMGB1, a pro-inflammatory cytokine, are present in the retina and are associated with inflammatory cells. PubMed:27716675

Appears in Networks:

a(HBP:"Tau oligomers") increases a(HBP:"Pathological Tau Spreading") View Subject | View Object

This work supports the hypothesis that tau oligomers are toxic species that can drive the spread of tau pathology and neurodegeneration. PubMed:27716675

Appears in Networks:

act(a(HBP:"Tau oligomers")) decreases act(complex(GO:axon)) View Subject | View Object

Several lines of evidence in other tauopathies suggest that tau oligomer formation induces neurotoxicity and that tau oligomer-mediated neurotoxicity involves induction of axonal dysfunction through exposure of an N-terminal motif in tau, the phosphatase-activating domain (PAD). PubMed:26671985

Appears in Networks:

act(a(HBP:"Tau oligomers")) positiveCorrelation p(HBP:"phosphatase-activating domain") View Subject | View Object

Several lines of evidence in other tauopathies suggest that tau oligomer formation induces neurotoxicity and that tau oligomer-mediated neurotoxicity involves induction of axonal dysfunction through exposure of an N-terminal motif in tau, the phosphatase-activating domain (PAD). PubMed:26671985

Appears in Networks:

act(a(HBP:"Tau oligomers")) increases a(HBP:neurotoxicity) View Subject | View Object

Several lines of evidence in other tauopathies suggest that tau oligomer formation induces neurotoxicity and that tau oligomer-mediated neurotoxicity involves induction of axonal dysfunction through exposure of an N-terminal motif in tau, the phosphatase-activating domain (PAD). PubMed:26671985

Appears in Networks:

a(HBP:"Tau oligomers") decreases bp(GO:"long-term synaptic potentiation") View Subject | View Object

Recently, extracellular tau oligomers were shown to impair long term potentiation (LTP) and memory [40]. PubMed:28528849

a(HBP:"Tau oligomers") decreases bp(GO:memory) View Subject | View Object

Recently, extracellular tau oligomers were shown to impair long term potentiation (LTP) and memory [40]. PubMed:28528849

a(HBP:"Tau oligomers") positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

Whereas control brain homogenate exhibited mainly Tau monomer, the AD brain contained a range of Tau assemblies ranging from n = 1 to n > 20 (Fig. 7, A and B). PubMed:25887395

a(HBP:"Tau oligomers") decreases a(MESH:Neurons) View Subject | View Object

Indeed, evidence from both human and mouse studies indicates that soluble oligomers rather than insoluble aggregates are toxic to normal neurons (70). PubMed:29191965

a(HBP:"Tau oligomers") increases path(HBP:Neurodegeneration) View Subject | View Object

In an analogy to the evolution of concepts in the ‘amyloid cascade hypothesis’, which proposes that soluble oligomers — rather than insoluble aggregates of amyloid peptides — are the causative agents of neurodegeneration in AD, recent studies have suggested tau oligomers to be the toxic species, and indeed levels of SDS-stable tau oligomers are increased in AD and PSP brains. PubMed:26631930

Annotations
MeSH
Brain

a(HBP:"Tau oligomers") positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

In an analogy to the evolution of concepts in the ‘amyloid cascade hypothesis’, which proposes that soluble oligomers — rather than insoluble aggregates of amyloid peptides — are the causative agents of neurodegeneration in AD, recent studies have suggested tau oligomers to be the toxic species, and indeed levels of SDS-stable tau oligomers are increased in AD and PSP brains. PubMed:26631930

Annotations
MeSH
Brain

a(HBP:"Tau oligomers") positiveCorrelation path(MESH:"Supranuclear Palsy, Progressive") View Subject | View Object

In an analogy to the evolution of concepts in the ‘amyloid cascade hypothesis’, which proposes that soluble oligomers — rather than insoluble aggregates of amyloid peptides — are the causative agents of neurodegeneration in AD, recent studies have suggested tau oligomers to be the toxic species, and indeed levels of SDS-stable tau oligomers are increased in AD and PSP brains. PubMed:26631930

Annotations
MeSH
Brain

a(HBP:"Tau oligomers") decreases a(MESH:"Dendritic Spines") View Subject | View Object

Some studies showed in cell toxicity assays that tau oligomers made from pro-aggregant recombinant tau were toxic to cultured cells; other studies in cultured neurons found that oligomers induced only local neurotoxicity that led to loss of spines PubMed:26631930

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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.