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p(HGNC:MAPT, pmod(Ph, Ser, 214))

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Entity

Name
MAPT
Namespace
hgnc
Namespace Version
20180906
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

Appears in Networks 3

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

Tau Biochemistry v1.2.5

Tau Biochemistry Section of NESTOR

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

In-Edges 9

p(HGNC:MAPT) hasVariant p(HGNC:MAPT, pmod(Ph, Ser, 214)) View Subject | View Object

Appears in Networks:

path(MESH:"Alzheimer Disease") positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 214)) View Subject | View Object

3. Putative phosphorylation sites on tau protein and epitopes specific for major tau antibodies. Red color denotes amino acids phosphorylation in AD brain. PubMed:26751493

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

bp(MESH:Mitosis) increases p(HGNC:MAPT, pmod(Ph, Ser, 214)) View Subject | View Object

A further potent detaching site is phosphoS214, which can be phosphorylated by PKA and other kinases of the AGC group (PKA/PKG/PKC group of protein kinases), and is up-regulated during mitosis (16, 63). Tau contains one or two cysteines in the repeat domain (C291 in R2, present in 4R isoforms, and C322 in R3), which can be engaged in intra- or intermolecular cross-linking affecting conformation, dimerization and aggregation (108). PubMed:17493042

Appears in Networks:
Annotations
Uberon
brain

p(FPLX:PKA) increases p(HGNC:MAPT, pmod(Ph, Ser, 214)) View Subject | View Object

A further potent detaching site is phosphoS214, which can be phosphorylated by PKA and other kinases of the AGC group (PKA/PKG/PKC group of protein kinases), and is up-regulated during mitosis (16, 63). Tau contains one or two cysteines in the repeat domain (C291 in R2, present in 4R isoforms, and C322 in R3), which can be engaged in intra- or intermolecular cross-linking affecting conformation, dimerization and aggregation (108). PubMed:17493042

Appears in Networks:
Annotations
Uberon
brain

p(FPLX:PKC) increases p(HGNC:MAPT, pmod(Ph, Ser, 214)) View Subject | View Object

A further potent detaching site is phosphoS214, which can be phosphorylated by PKA and other kinases of the AGC group (PKA/PKG/PKC group of protein kinases), and is up-regulated during mitosis (16, 63). Tau contains one or two cysteines in the repeat domain (C291 in R2, present in 4R isoforms, and C322 in R3), which can be engaged in intra- or intermolecular cross-linking affecting conformation, dimerization and aggregation (108). PubMed:17493042

Appears in Networks:
Annotations
Uberon
brain

p(FPLX:PRKG) increases p(HGNC:MAPT, pmod(Ph, Ser, 214)) View Subject | View Object

A further potent detaching site is phosphoS214, which can be phosphorylated by PKA and other kinases of the AGC group (PKA/PKG/PKC group of protein kinases), and is up-regulated during mitosis (16, 63). Tau contains one or two cysteines in the repeat domain (C291 in R2, present in 4R isoforms, and C322 in R3), which can be engaged in intra- or intermolecular cross-linking affecting conformation, dimerization and aggregation (108). PubMed:17493042

Appears in Networks:
Annotations
Uberon
brain

a(CHEBI:"D-ribose") increases p(HGNC:MAPT, pmod(Ph, Ser, 214)) View Subject | View Object

Here, we show for the first time that the administration of D-ribose, the most active glycator among monosaccharides, produces high levels of advanced glycation end products (AGEs) and, importantly, triggers hyperphosphorylation of Tau in the brain of C57BL/6 mouse and neuroblastoma N2a cells. PubMed:26095350

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a(CHEBI:"D-ribose") positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 214)) View Subject | View Object

Here, we show for the first time that the administration of D-ribose, the most active glycator among monosaccharides, produces high levels of advanced glycation end products (AGEs) and, importantly, triggers hyperphosphorylation of Tau in the brain of C57BL/6 mouse and neuroblastoma N2a cells. PubMed:28176663

Appears in Networks:

a(HBP:"advanced glycation end product") increases p(HGNC:MAPT, pmod(Ph, Ser, 214)) View Subject | View Object

Thus, our results suggest that Tau hyperphosphorylation was a result of ribosylated AGEs, rather than due to a direct reaction involving D-ribose. PubMed:28176663

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Out-Edges 3

p(HGNC:MAPT, pmod(Ph, Ser, 214)) positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

3. Putative phosphorylation sites on tau protein and epitopes specific for major tau antibodies. Red color denotes amino acids phosphorylation in AD brain. PubMed:26751493

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

p(HGNC:MAPT, pmod(Ph, Ser, 214)) positiveCorrelation a(CHEBI:"D-ribose") View Subject | View Object

Here, we show for the first time that the administration of D-ribose, the most active glycator among monosaccharides, produces high levels of advanced glycation end products (AGEs) and, importantly, triggers hyperphosphorylation of Tau in the brain of C57BL/6 mouse and neuroblastoma N2a cells. PubMed:28176663

Appears in Networks:

p(HGNC:MAPT, pmod(Ph, Ser, 214)) decreases act(p(HGNC:MAPT)) View Subject | View Object

>8 phosphates per tau molecules (vs 2 in adult healthy brain); can also be increased during development, hibernation and temperature, heat and oxydative stress These phosphorylated states are detected by specific antibodies and are targets of proline-directed kinases (SP motifs), non-proline kinases (KXGS motif) Weakens tau-MT interaction especially S261 in R1 and S214 in proline-rich domain PubMed:8226987

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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.