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Appears in Networks 1

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

In-Edges 6

a(CHEBI:peroxynitrite) increases p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 197)) View Subject | View Object

Select nitration of residues Tyr18, Tyr29, Tyr197, and Tyr394, events known to stabilize the pathological Alz-50 conformation inhibits the ability of monomeric tau to promote tubulin assembly, effect specific for the 3-NT modification, as mutant tau proteins pseudophosphorylated at each Tyr residue are fully competent to stabilize MTs, suggesting that ONOO(-)-mediated modifications stabilize tau filaments via 3,3'-DT bonding and destabilize MTs by site-selective nitration of tau monomers. PubMed:16566606

Appears in Networks:

a(HBP:"paired helical filaments") positiveCorrelation p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 197)) View Subject | View Object

Select nitration of residues Tyr18, Tyr29, Tyr197, and Tyr394, events known to stabilize the pathological Alz-50 conformation inhibits the ability of monomeric tau to promote tubulin assembly, effect specific for the 3-NT modification, as mutant tau proteins pseudophosphorylated at each Tyr residue are fully competent to stabilize MTs, suggesting that ONOO(-)-mediated modifications stabilize tau filaments via 3,3'-DT bonding and destabilize MTs by site-selective nitration of tau monomers. PubMed:16566606

Appears in Networks:

act(p(HGNC:MAPT)) negativeCorrelation p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 197)) View Subject | View Object

Select nitration of residues Tyr18, Tyr29, Tyr197, and Tyr394, events known to stabilize the pathological Alz-50 conformation inhibits the ability of monomeric tau to promote tubulin assembly, effect specific for the 3-NT modification, as mutant tau proteins pseudophosphorylated at each Tyr residue are fully competent to stabilize MTs, suggesting that ONOO(-)-mediated modifications stabilize tau filaments via 3,3'-DT bonding and destabilize MTs by site-selective nitration of tau monomers. PubMed:16566606

Appears in Networks:

path(HBP:"Corticobasal Degeneration") positiveCorrelation p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 197)) View Subject | View Object

Tau-nY18 did not label the classical pathological lesions of CBD or PSP but did label the neuronal lesions associated with PiD. Tau-nY29 revealed some, but not all classes of tau inclusions associated with both CBD and PSP but did label numerous Pick body inclusions in PiD. Tau-nY197 was restricted to the neuropil threads in both CBD and PSP; however, similar to Tau-nY29, extensive Pick body pathology was clearly labeled. Tau-nY394 did not detect any of the lesions associated with these disorders. PubMed:22057784

Appears in Networks:
Annotations
Uberon
neuropil
Disease Ontology (DO)
progressive supranuclear palsy

path(MESH:"Supranuclear Palsy, Progressive") positiveCorrelation p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 197)) View Subject | View Object

Tau-nY18 did not label the classical pathological lesions of CBD or PSP but did label the neuronal lesions associated with PiD. Tau-nY29 revealed some, but not all classes of tau inclusions associated with both CBD and PSP but did label numerous Pick body inclusions in PiD. Tau-nY197 was restricted to the neuropil threads in both CBD and PSP; however, similar to Tau-nY29, extensive Pick body pathology was clearly labeled. Tau-nY394 did not detect any of the lesions associated with these disorders. PubMed:22057784

Appears in Networks:
Annotations
Uberon
neuropil
Disease Ontology (DO)
progressive supranuclear palsy

Out-Edges 7

p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 197)) decreases bp(GO:"tubulin complex assembly") View Subject | View Object

Further, select nitration of residues Tyr18, Tyr29, Tyr197, and Tyr394, events known to stabilize the pathological Alz-50 conformation [Reynolds et al. (2005) Biochemistry 44, 13997-14009], inhibits the ability of monomeric tau to promote tubulin assembly. PubMed:16566606

Appears in Networks:

p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 197)) positiveCorrelation path(MESH:"Supranuclear Palsy, Progressive") View Subject | View Object

Tau-nY18 did not label the classical pathological lesions of CBD or PSP but did label the neuronal lesions associated with PiD. Tau-nY29 revealed some, but not all classes of tau inclusions associated with both CBD and PSP but did label numerous Pick body inclusions in PiD. Tau-nY197 was restricted to the neuropil threads in both CBD and PSP; however, similar to Tau-nY29, extensive Pick body pathology was clearly labeled. Tau-nY394 did not detect any of the lesions associated with these disorders. PubMed:22057784

Appears in Networks:
Annotations
Uberon
neuropil
Disease Ontology (DO)
progressive supranuclear palsy

p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 197)) positiveCorrelation path(HBP:"Corticobasal Degeneration") View Subject | View Object

Tau-nY18 did not label the classical pathological lesions of CBD or PSP but did label the neuronal lesions associated with PiD. Tau-nY29 revealed some, but not all classes of tau inclusions associated with both CBD and PSP but did label numerous Pick body inclusions in PiD. Tau-nY197 was restricted to the neuropil threads in both CBD and PSP; however, similar to Tau-nY29, extensive Pick body pathology was clearly labeled. Tau-nY394 did not detect any of the lesions associated with these disorders. PubMed:22057784

Appears in Networks:
Annotations
Uberon
neuropil
Disease Ontology (DO)
progressive supranuclear palsy

p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 197)) positiveCorrelation a(HBP:"paired helical filaments") View Subject | View Object

Select nitration of residues Tyr18, Tyr29, Tyr197, and Tyr394, events known to stabilize the pathological Alz-50 conformation inhibits the ability of monomeric tau to promote tubulin assembly, effect specific for the 3-NT modification, as mutant tau proteins pseudophosphorylated at each Tyr residue are fully competent to stabilize MTs, suggesting that ONOO(-)-mediated modifications stabilize tau filaments via 3,3'-DT bonding and destabilize MTs by site-selective nitration of tau monomers. PubMed:16566606

Appears in Networks:

p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 197)) negativeCorrelation act(p(HGNC:MAPT)) View Subject | View Object

Select nitration of residues Tyr18, Tyr29, Tyr197, and Tyr394, events known to stabilize the pathological Alz-50 conformation inhibits the ability of monomeric tau to promote tubulin assembly, effect specific for the 3-NT modification, as mutant tau proteins pseudophosphorylated at each Tyr residue are fully competent to stabilize MTs, suggesting that ONOO(-)-mediated modifications stabilize tau filaments via 3,3'-DT bonding and destabilize MTs by site-selective nitration of tau monomers. PubMed:16566606

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.