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Appears in Networks 4

In-Edges 7

p(MGI:Mapt, var("p.Ala152Thr")) increases a(GO:autolysosome) View Subject | View Object

We found that abundance of autophagic vacuoles (autophagosomes + autolysosomes) significantly increased in cells expressing either of the two tau mutants (Fig. 4d,e). This increase was mainly due to higher content of autolysosomes (red puncta) (Fig. 4d,e), in support of increased macroautophagic flux PubMed:29024336

p(MGI:Mapt, var("p.Pro301Leu")) increases a(GO:autolysosome) View Subject | View Object

We found that abundance of autophagic vacuoles (autophagosomes + autolysosomes) significantly increased in cells expressing either of the two tau mutants (Fig. 4d,e). This increase was mainly due to higher content of autolysosomes (red puncta) (Fig. 4d,e), in support of increased macroautophagic flux PubMed:29024336

path(MESH:"Alzheimer Disease") increases a(GO:autolysosome) View Subject | View Object

Pathologically, the AD brains show both accumulated autophagosomes and autolysosomes, suggesting the basal autophagy process in neurons is abnormal in AD (Fig. 3A). PubMed:23528736

bp(GO:"lysosomal protein catabolic process") decreases a(GO:autolysosome) View Subject | View Object

Other studies have also demonstrated the accumulation of autolysosomes in the AD brain and experimentally when lysosomal proteolysis is compromised via genetic knockdown of specific cathepsins or use of pharmacological inhibition of lysosomes [2,3,15] PubMed:29758300

path(MESH:"Alzheimer Disease") positiveCorrelation a(GO:autolysosome) View Subject | View Object

Other studies have also demonstrated the accumulation of autolysosomes in the AD brain and experimentally when lysosomal proteolysis is compromised via genetic knockdown of specific cathepsins or use of pharmacological inhibition of lysosomes [2,3,15] PubMed:29758300

complex(a(GO:amphisome), a(GO:lysosome)) increases a(GO:autolysosome) View Subject | View Object

In mammals, autophagosomes first fuse with endosomes and multivesicular bodies to form amphisomes, which subsequently fuse with lysosomes to create degradative vacuoles termed autolysosomes [17]. PubMed:18930136

path(MESH:"Huntington Disease") positiveCorrelation a(GO:autolysosome) View Subject | View Object

In Huntington’s disease, affected neurons show accumulation of huntingtin in cathepsin-D-positive vacuoles [24]. Cathepsin-D is a lysosomal protease enriched in neuronal tissues, suggesting that these are autolysosomes PubMed:18930136

Out-Edges 3

a(GO:autolysosome) positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

Other studies have also demonstrated the accumulation of autolysosomes in the AD brain and experimentally when lysosomal proteolysis is compromised via genetic knockdown of specific cathepsins or use of pharmacological inhibition of lysosomes [2,3,15] PubMed:29758300

a(GO:autolysosome) positiveCorrelation path(MESH:"Huntington Disease") View Subject | View Object

In Huntington’s disease, affected neurons show accumulation of huntingtin in cathepsin-D-positive vacuoles [24]. Cathepsin-D is a lysosomal protease enriched in neuronal tissues, suggesting that these are autolysosomes PubMed:18930136

a(GO:autolysosome) decreases path(HBP:Neurodegeneration) View Subject | View Object

CLN3-related neurodegeneration appears to be a consequence of reduced autophagosome-lysosome fusion [42]. PubMed:18930136

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.