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Appears in Networks 5

In-Edges 11

p(HGNC:LGMN) increases p(HGNC:MAPT, frag("?")) View Subject | View Object

In addition to decreased degradation, one consequence is leakage of asparaginyl endopeptidase into the cytosol, where it generates toxic fragments of tau 61 . PubMed:30116051

a(MESH:"3-methyladenine") increases p(HGNC:MAPT, frag("?")) View Subject | View Object

Overexpressing only the repeat domain of tau containing an FTDP-17 mutation in neuroblastoma cells leads to tau aggregation as well as the appearance of smaller proteolytic fragments. Using the autophagy inhibitor 3-methyladenine (3-MA) to block the formation of autophagosomes led to an increase in both soluble and insoluble tau (94). PubMed:24027553

bp(GO:"lysosomal microautophagy") increases p(HGNC:MAPT, frag("?")) View Subject | View Object

On the other hand, it brings about tau fragmentation into pro-aggregating forms due to the failure of F1 to enter the lysosome PubMed:29626319

p(FPLX:CAPN) increases p(HGNC:MAPT, frag("?")) View Subject | View Object

However, there was a study indicating that calpain-mediated tau cleavage can result in the generation of tau fragments, which may possess neurotoxicity in AD (Ferreira and Bigio 2011) PubMed:29626319

bp(GO:macroautophagy) increases deg(p(HGNC:MAPT, frag("?"))) View Subject | View Object

Incomplete charperone-mediated autophagy of tau generates fragments that aggregate and are cleared by macroautophagy (Wang et al. 2009). PubMed:22908190

deg(p(HGNC:MAPT)) increases p(HGNC:MAPT, frag("?")) View Subject | View Object

Incomplete charperone-mediated autophagy of tau generates fragments that aggregate and are cleared by macroautophagy (Wang et al. 2009). PubMed:22908190

p(HGNC:CASP3) increases p(HGNC:MAPT, frag("?")) View Subject | View Object

For instance, the phosphorylation of tau at Ser422 inhibits the cleavage of tau by caspase 3 at Asp421 PubMed:26631930

p(HGNC:MAPT, pmod(Ph, Ser, 422)) decreases p(HGNC:MAPT, frag("?")) View Subject | View Object

For instance, the phosphorylation of tau at Ser422 inhibits the cleavage of tau by caspase 3 at Asp421 PubMed:26631930

path(MESH:"Alzheimer Disease") increases p(HGNC:MAPT, frag("?")) View Subject | View Object

The truncation of tau occurs in AD and in other tauopathies PubMed:26631930

path(MESH:Tauopathies) increases p(HGNC:MAPT, frag("?")) View Subject | View Object

The truncation of tau occurs in AD and in other tauopathies PubMed:26631930

Out-Edges 6

p(HGNC:MAPT, frag("?")) decreases bp(GO:"chaperone-mediated autophagy") View Subject | View Object

Finally, while physiological tau possesses KFERQ motifs and is degraded by CMA, aggregates, mutant forms and frag- ments interfere with CMA 45,47 . PubMed:30116051

p(HGNC:MAPT, frag("?")) increases bp(HBP:neurotoxicity) View Subject | View Object

However, there was a study indicating that calpain-mediated tau cleavage can result in the generation of tau fragments, which may possess neurotoxicity in AD (Ferreira and Bigio 2011) PubMed:29626319

p(HGNC:MAPT, frag("?")) increases path(HBP:Neurodegeneration) View Subject | View Object

In addition, the truncation of tau may result in tau fragments that induce neurodegeneration independently of tau aggregation. PubMed:26631930

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

Truncation of tau prevents the formation of this structure and might thereby promote tau aggregation PubMed:26631930

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

Truncation of tau could generate tau fragments with a higher tendency for aggregation (see below), probably owing to the disruption of the paperclip structure of tau, as described above. PubMed:26631930

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

Truncated tau fragments that contain the repeat domain have a higher tendency for aggregation, probably owing to the disruption of the usual paperclip structure PubMed:26631930

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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.