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Entity

Name
retrograde axonal protein transport
Namespace
go
Namespace Version
20180921
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/go-names.belns

Appears in Networks 3

In-Edges 10

p(HBP:"AT8 tau") causesNoChange bp(GO:"retrograde axonal protein transport") View Subject | View Object

Soluble AT8 tau monomers inhibited anterograde FAT (Fig. 6 A, C), while retrograde trans- port was unaffected (Fig. 6 A, D). These data indicate that phos- phorylation of tau at the AT8 epitope, which is associated with hyperphosphorylation of tau in AD and other tauopathies, renders soluble monomeric tau capable of inhibiting antero- grade FAT. PubMed:21734277

p(HBP:"delta 144-273 tau") causesNoChange bp(GO:"retrograde axonal protein transport") View Subject | View Object

Consistent with our model, 􏰁144 –273 tau monomers significantly inhibited antero- grade FAT (Fig. 6 B, C), while retrograde FAT remained unaf- fected (Fig. 6 B, D).Together, these data indicate that disease- associated modifications and mutations in tau that increase exposure of PAD promote activation of the PP1–GSK3 pathway and inhibition of anterograde FAT. PubMed:21734277

composite(a(HBP:"Tau aggregates"), p(HGNC:MAPT)) causesNoChange bp(GO:"retrograde axonal protein transport") View Subject | View Object

As previously reported, perfusion of hT40 monomer had no effect on the rate of anterograde FAT in the squid axoplasm (Fig. 5A), whereas perfusion of hT40 aggregates significantly inhibited anterograde FAT as compared to hT40 monomer (Fig. 5B; Fig. 6A; p = 0.003) (LaPointe et al., 2009b). Neither hT40 monomers nor hT40 aggregates altered the rate of retrograde FAT (Fig. 5A, B; Fig. 6B). PubMed:27373205

p(HGNC:MAPT) causesNoChange bp(GO:"retrograde axonal protein transport") View Subject | View Object

As previously reported, perfusion of hT40 monomer had no effect on the rate of anterograde FAT in the squid axoplasm (Fig. 5A), whereas perfusion of hT40 aggregates significantly inhibited anterograde FAT as compared to hT40 monomer (Fig. 5B; Fig. 6A; p = 0.003) (LaPointe et al., 2009b). Neither hT40 monomers nor hT40 aggregates altered the rate of retrograde FAT (Fig. 5A, B; Fig. 6B). PubMed:27373205

composite(a(HBP:"Tau aggregates"), p(HGNC:MAPT, var("p.S422E"))) decreases bp(GO:"retrograde axonal protein transport") View Subject | View Object

In contrast to hT40 monomer, perfusion of S422E monomer selectively inhibited anterograde transport (Fig. 5C; Fig. 6A; p = 0.028), but not retrograde FAT. Surprisingly, aggregated S422E significantly inhibited both anterograde and retrograde FAT rates (Fig. 5D; Fig. 6A, B) compared to S422E monomer (anterograde, p = 0.012; retrograde, p = 0.002) and hT40 aggregates (retrograde only, p = 0.019). PubMed:27373205

p(HGNC:MAPT, var("p.S422E")) causesNoChange bp(GO:"retrograde axonal protein transport") View Subject | View Object

In contrast to hT40 monomer, perfusion of S422E monomer selectively inhibited anterograde transport (Fig. 5C; Fig. 6A; p = 0.028), but not retrograde FAT. Surprisingly, aggregated S422E significantly inhibited both anterograde and retrograde FAT rates (Fig. 5D; Fig. 6A, B) compared to S422E monomer (anterograde, p = 0.012; retrograde, p = 0.002) and hT40 aggregates (retrograde only, p = 0.019). PubMed:27373205

p(HGNC:MAPT) increases bp(GO:"retrograde axonal protein transport") View Subject | View Object

Tau serves an important function by enabling microtubules to connect with cytoskeletal components and facilitates anterograde and retrograde axonal transport of vesicles and organelles [39]. PubMed:29758300

Out-Edges 0

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.