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Appears in Networks 2

In-Edges 9

act(a(BRCO:Astrocyte)) association p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 18)) View Subject | View Object

This antibody detects nitrated tau in soluble preparations from both severe AD brains (Braak stage V, VI) and age-matched controls, suggesting that nitration at Tyr 18 may be linked to astrocyte activation, an early event associated with amyloid plaque formation PubMed:18562203

Appears in Networks:

a(CHEBI:peroxynitrite) increases p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 18)) 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, 18)) 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, 18)) 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(MESH:"Pick Disease of the Brain") positiveCorrelation p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 18)) 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:

path(MESH:"Plaque, Amyloid") positiveCorrelation p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 18)) View Subject | View Object

This antibody detects nitrated tau in soluble preparations from both severe AD brains (Braak stage V, VI) and age-matched controls, suggesting that nitration at Tyr 18 may be linked to astrocyte activation, an early event associated with amyloid plaque formation PubMed:18562203

Appears in Networks:

path(MESH:"Alzheimer Disease") positiveCorrelation p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 18)) View Subject | View Object

The nitration of tau Tyr197 is found in the normal human brain and may have important physiological functions, whereas the nitration of Tyr18, Tyr29 and Tyr394 is detected only in AD or other tauopathies PubMed:26631930

path(MESH:Tauopathies) positiveCorrelation p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 18)) View Subject | View Object

The nitration of tau Tyr197 is found in the normal human brain and may have important physiological functions, whereas the nitration of Tyr18, Tyr29 and Tyr394 is detected only in AD or other tauopathies PubMed:26631930

Out-Edges 10

p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 18)) positiveCorrelation path(MESH:"Plaque, Amyloid") View Subject | View Object

This antibody detects nitrated tau in soluble preparations from both severe AD brains (Braak stage V, VI) and age-matched controls, suggesting that nitration at Tyr 18 may be linked to astrocyte activation, an early event associated with amyloid plaque formation PubMed:18562203

Appears in Networks:

p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 18)) 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, 18)) positiveCorrelation path(MESH:"Pick Disease of the Brain") 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:

p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 18)) association act(a(BRCO:Astrocyte)) View Subject | View Object

This antibody detects nitrated tau in soluble preparations from both severe AD brains (Braak stage V, VI) and age-matched controls, suggesting that nitration at Tyr 18 may be linked to astrocyte activation, an early event associated with amyloid plaque formation PubMed:18562203

Appears in Networks:

p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 18)) 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, 18)) 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:

p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 18)) decreases complex(a(GO:microtubule), p(HGNC:MAPT)) View Subject | View Object

The nitration of these Tyr residues alters the conformation of tau, reduces its binding to microtubules and, depending on the nitration sites, can promote or inhibit aggregation PubMed:26631930

p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 18)) positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

The nitration of tau Tyr197 is found in the normal human brain and may have important physiological functions, whereas the nitration of Tyr18, Tyr29 and Tyr394 is detected only in AD or other tauopathies PubMed:26631930

p(HGNC:MAPT, pmod(HBP:nitration, Tyr, 18)) positiveCorrelation path(MESH:Tauopathies) View Subject | View Object

The nitration of tau Tyr197 is found in the normal human brain and may have important physiological functions, whereas the nitration of Tyr18, Tyr29 and Tyr394 is detected only in AD or other tauopathies PubMed:26631930

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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.