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

Appears in Networks 4

In-Edges 4

path(MESH:"Parkinson Disease") positiveCorrelation p(HGNC:LRRK2) View Subject | View Object

Using mass spectrometry, we identified multiple sites on recombinant tau that are phosphorylated by LRRK2 in vitro, including pT149 and pT153, which are phospho-epitopes that to date have been largely unexplored. Importantly, we demonstrate that expression of transgenic LRRK2 in a mouse model of tauopathy increased the aggregation of insoluble tau and its phosphorylation at T149, T153, T205, and S199/S202/T205 epitopes. PubMed:24113872

Appears in Networks:

g(HGNC:MIR205) regulates p(HGNC:LRRK2) View Subject | View Object

It has also been shown that miR‐205 can regulate LRRK2 and that PD is associated with a significant reduction in the level of miR‐205 in the frontal cortex and striatum PubMed:30663117

g(HGNC:MIR205) regulates p(HGNC:LRRK2) View Subject | View Object

Expression of miR‐205 affects the level of LRRK2 expression, and LRRK2, in turn, affects two miRNAs called let‐7 and miR‐184. This effect is associated with decreased activity and level of let‐7 and miR‐184 within the cell PubMed:30663117

Out-Edges 13

p(HGNC:LRRK2) positiveCorrelation path(MESH:"Parkinson Disease") View Subject | View Object

Using mass spectrometry, we identified multiple sites on recombinant tau that are phosphorylated by LRRK2 in vitro, including pT149 and pT153, which are phospho-epitopes that to date have been largely unexplored. Importantly, we demonstrate that expression of transgenic LRRK2 in a mouse model of tauopathy increased the aggregation of insoluble tau and its phosphorylation at T149, T153, T205, and S199/S202/T205 epitopes. PubMed:24113872

Appears in Networks:

act(p(HGNC:LRRK2), ma(kin)) directlyIncreases p(MGI:Mapt, pmod(Ph, Thr, 149)) View Subject | View Object

Using mass spectrometry, we identified multiple sites on recombinant tau that are phosphorylated by LRRK2 in vitro, including pT149 and pT153, which are phospho-epitopes that to date have been largely unexplored. Importantly, we demonstrate that expression of transgenic LRRK2 in a mouse model of tauopathy increased the aggregation of insoluble tau and its phosphorylation at T149, T153, T205, and S199/S202/T205 epitopes. PubMed:24113872

Appears in Networks:

act(p(HGNC:LRRK2), ma(kin)) directlyIncreases p(MGI:Mapt, pmod(Ph, Thr, 153)) View Subject | View Object

Using mass spectrometry, we identified multiple sites on recombinant tau that are phosphorylated by LRRK2 in vitro, including pT149 and pT153, which are phospho-epitopes that to date have been largely unexplored. Importantly, we demonstrate that expression of transgenic LRRK2 in a mouse model of tauopathy increased the aggregation of insoluble tau and its phosphorylation at T149, T153, T205, and S199/S202/T205 epitopes. PubMed:24113872

Appears in Networks:

act(p(HGNC:LRRK2), ma(kin)) directlyIncreases p(MGI:Mapt, pmod(Ph, Thr, 205)) View Subject | View Object

Using mass spectrometry, we identified multiple sites on recombinant tau that are phosphorylated by LRRK2 in vitro, including pT149 and pT153, which are phospho-epitopes that to date have been largely unexplored. Importantly, we demonstrate that expression of transgenic LRRK2 in a mouse model of tauopathy increased the aggregation of insoluble tau and its phosphorylation at T149, T153, T205, and S199/S202/T205 epitopes. PubMed:24113872

Appears in Networks:

act(p(HGNC:LRRK2), ma(kin)) directlyIncreases p(HBP:"Tau epitope, AT8") View Subject | View Object

Using mass spectrometry, we identified multiple sites on recombinant tau that are phosphorylated by LRRK2 in vitro, including pT149 and pT153, which are phospho-epitopes that to date have been largely unexplored. Importantly, we demonstrate that expression of transgenic LRRK2 in a mouse model of tauopathy increased the aggregation of insoluble tau and its phosphorylation at T149, T153, T205, and S199/S202/T205 epitopes. PubMed:24113872

Appears in Networks:

act(p(HGNC:LRRK2), ma(kin)) directlyIncreases p(HBP:"Tau aggregates") View Subject | View Object

Using mass spectrometry, we identified multiple sites on recombinant tau that are phosphorylated by LRRK2 in vitro, including pT149 and pT153, which are phospho-epitopes that to date have been largely unexplored. Importantly, we demonstrate that expression of transgenic LRRK2 in a mouse model of tauopathy increased the aggregation of insoluble tau and its phosphorylation at T149, T153, T205, and S199/S202/T205 epitopes. PubMed:24113872

Appears in Networks:

p(HGNC:LRRK2) decreases g(HGNC:MIRLET7A1) View Subject | View Object

Expression of miR‐205 affects the level of LRRK2 expression, and LRRK2, in turn, affects two miRNAs called let‐7 and miR‐184. This effect is associated with decreased activity and level of let‐7 and miR‐184 within the cell PubMed:30663117

p(HGNC:LRRK2) decreases act(g(HGNC:MIRLET7A1)) View Subject | View Object

Expression of miR‐205 affects the level of LRRK2 expression, and LRRK2, in turn, affects two miRNAs called let‐7 and miR‐184. This effect is associated with decreased activity and level of let‐7 and miR‐184 within the cell PubMed:30663117

p(HGNC:LRRK2) decreases g(HGNC:MIR184) View Subject | View Object

Expression of miR‐205 affects the level of LRRK2 expression, and LRRK2, in turn, affects two miRNAs called let‐7 and miR‐184. This effect is associated with decreased activity and level of let‐7 and miR‐184 within the cell PubMed:30663117

p(HGNC:LRRK2) decreases act(g(HGNC:MIR184)) View Subject | View Object

Expression of miR‐205 affects the level of LRRK2 expression, and LRRK2, in turn, affects two miRNAs called let‐7 and miR‐184. This effect is associated with decreased activity and level of let‐7 and miR‐184 within the cell PubMed:30663117

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.