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complex(a(CHEBI:heparin), p(HBP:"Tau aggregates"))

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Appears in Networks 2

Tau Protein Hyperphosphorylation and Aggregation in Alzheimer’s Disease and Other Tauopathies, and Possible Neuroprotective Strategies v1.0.0

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

In-Edges 4

a(CHEBI:heparin) partOf complex(a(CHEBI:heparin), p(HBP:"Tau aggregates")) View Subject | View Object

Appears in Networks:

bp(GO:macropinocytosis) positiveCorrelation complex(a(CHEBI:heparin), p(HBP:"Tau aggregates")) View Subject | View Object

In the case of soluble monomeric or small oligomeric tau protein, the endocytosis appears to be clathrin-dependent (reviewed in [169]). In contrast, larger aggregates of tau could bind heparin in the extracellular matrix and be internalized through macropinocytosis [170]. As a result of exocytosis and endocytosis, the spreading of tau can occur in various neurodegenerative diseases (tauopathies) including AD. Three plausible mechanisms of tau spreading are shown schematically in Figure 6. Additionally, it appea rs that microglial cells may facilitate tau propagation by phagocytosis and exocytosis of tau protein [171]. PubMed:26751493

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p(HBP:"Tau aggregates") increases complex(a(CHEBI:heparin), p(HBP:"Tau aggregates")) View Subject | View Object

In the case of soluble monomeric or small oligomeric tau protein, the endocytosis appears to be clathrin-dependent (reviewed in [169]). In contrast, larger aggregates of tau could bind heparin in the extracellular matrix and be internalized through macropinocytosis [170]. As a result of exocytosis and endocytosis, the spreading of tau can occur in various neurodegenerative diseases (tauopathies) including AD. Three plausible mechanisms of tau spreading are shown schematically in Figure 6. Additionally, it appea rs that microglial cells may facilitate tau propagation by phagocytosis and exocytosis of tau protein [171]. PubMed:26751493

Appears in Networks:

p(HBP:"Tau aggregates") partOf complex(a(CHEBI:heparin), p(HBP:"Tau aggregates")) View Subject | View Object

Appears in Networks:

Out-Edges 3

complex(a(CHEBI:heparin), p(HBP:"Tau aggregates")) hasComponent a(CHEBI:heparin) View Subject | View Object

Appears in Networks:

complex(a(CHEBI:heparin), p(HBP:"Tau aggregates")) hasComponent p(HBP:"Tau aggregates") View Subject | View Object

Appears in Networks:

complex(a(CHEBI:heparin), p(HBP:"Tau aggregates")) positiveCorrelation bp(GO:macropinocytosis) View Subject | View Object

In the case of soluble monomeric or small oligomeric tau protein, the endocytosis appears to be clathrin-dependent (reviewed in [169]). In contrast, larger aggregates of tau could bind heparin in the extracellular matrix and be internalized through macropinocytosis [170]. As a result of exocytosis and endocytosis, the spreading of tau can occur in various neurodegenerative diseases (tauopathies) including AD. Three plausible mechanisms of tau spreading are shown schematically in Figure 6. Additionally, it appea rs that microglial cells may facilitate tau propagation by phagocytosis and exocytosis of tau protein [171]. PubMed:26751493

Appears in Networks:

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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.