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complex(GO:"neurofibrillary tangle")

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Entity

Name
neurofibrillary tangle
Namespace
go
Namespace Version
20180921
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/go-names.belns

Appears in Networks 6

Estrogen receptor-α is localized to neurofibrillary tangles in Alzheimer's disease v1.0.0

Amyloid β oligomers (AβOs) in Alzheimer’s disease v1.0.0

Tau Biochemistry v1.2.5

Tau Biochemistry Section of NESTOR

TAU and Interaction Partners v1.2.5

TAU Interactions Section of NESTOR

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

Inflammasome Involvement in Alzheimer’s Disease v1.0.0

In-Edges 15

a(CHEBI:"amyloid-beta") increases complex(GO:"neurofibrillary tangle") View Subject | View Object

These Aβ deposits lead to subsequent molecular and cellular alterations, such as NTFs, neuronal dystrophy, or microgliosis, i.e., pathological events that are closer to dementia and more relevant to neuronal dysfunction. PubMed:29196815

Appears in Networks:
Annotations
Confidence
Medium

p(HGNC:ESR1) association complex(GO:"neurofibrillary tangle") View Subject | View Object

In the hippocampal and cortical tissues of all AD cases examined, neuronal staining for ERα was a prominent finding, both with a weak cytoplasmic stain, but often specifically with a fibrillar appearance suggesting ERα was in neurofibrillary tangles (Fig. 1A), also shown at a higher magnification (Fig. 1B). PubMed:26837465

Appears in Networks:
Annotations
Confidence
Medium
MeSH
Cerebral Cortex
MeSH
Hippocampus

p(HGNC:ESR1) association complex(GO:"neurofibrillary tangle") View Subject | View Object

To confirm the localization of ERα in NFTs, double fluorescence staining with antibodies to ERα and hyperphosphorylated tau (PHF-1) revealed that ERα -positive NFTs were also positive for PHF-1 (Fig. 2A–F). PubMed:26837465

Appears in Networks:
Annotations
Confidence
Medium
MeSH
Cerebral Cortex
MeSH
Hippocampus

p(HBP:"3R tau") partOf complex(GO:"neurofibrillary tangle") View Subject | View Object

Appears in Networks:

p(HBP:"4R tau") partOf complex(GO:"neurofibrillary tangle") View Subject | View Object

Appears in Networks:

p(HGNC:MAPT, pmod(Ph)) partOf complex(GO:"neurofibrillary tangle") View Subject | View Object

Appears in Networks:

p(HGNC:MAPT, pmod(Ph)) partOf complex(GO:"neurofibrillary tangle") View Subject | View Object

Appears in Networks:

p(HGNC:PICALM) partOf complex(GO:"neurofibrillary tangle") View Subject | View Object

Appears in Networks:

p(HGNC:PICALM) partOf complex(GO:"neurofibrillary tangle") View Subject | View Object

Appears in Networks:

complex(p(HGNC:MAPT, pmod(Ph, Thr, 231)), p(HGNC:PIN1, frag("5_39"))) association complex(GO:"neurofibrillary tangle") View Subject | View Object

This result confirms previous findings that T231 is an important Cdc2 phosphorylation site in tau, and is also consistent with Pin1 binding mitotically pTau (Fig. 1a) and being sequestered on to PHFs in AD brains, where Cdc2 is upregulated (Fig. 3). PubMed:10391244

Appears in Networks:

composite(p(HGNC:MAPT), p(HGNC:SNCA)) increases complex(GO:"neurofibrillary tangle") View Subject | View Object

We also observed that tau and alpha-synuclein synergistically promote and propagate each other’s polymerization into fibrils PubMed:12714745

Appears in Networks:

g(DBSNP:rs104893877) positiveCorrelation complex(GO:"neurofibrillary tangle") View Subject | View Object

Recent studies of an individual with Parkinson’s disease (IX-47) of the Contursi kindred with the rare A53T alpha-synuclein mutation revealed widespread -syn and tau inclusions (15). Post-mortem examination of another affected member (IX-51) of this kindred also demonstrated abundant -syn and tau inclusions(figs. S1 and S2). Thus, a pathogenic mutation in alpha-synuclein that is known to increase the propensity of alpha-synuclein to fibrillize (8, 9) also promotes formation of tau inclusions in humans. PubMed:12714745

Appears in Networks:
Annotations
Disease Ontology (DO)
Parkinson's disease

p(HGNC:CDK1) positiveCorrelation complex(GO:"neurofibrillary tangle") View Subject | View Object

This result confirms previous findings that T231 is an important Cdc2 phosphorylation site in tau, and is also consistent with Pin1 binding mitotically pTau (Fig. 1a) and being sequestered on to PHFs in AD brains, where Cdc2 is upregulated (Fig. 3). PubMed:10391244

Appears in Networks:

a(HBP:"paired helical filaments") partOf complex(GO:"neurofibrillary tangle") View Subject | View Object

Appears in Networks:

bp(GO:"p38MAPK cascade") increases complex(GO:"neurofibrillary tangle") View Subject | View Object

Additionally, it can induce phosphorylation of the tau protein and promote for- mation of neurofibrillary tangles through the mitogen activated protein kinases-p38 (MAPK-p38) stress pathway [22, 54]. PubMed:27314526

Appears in Networks:
Annotations
Confidence
High
MeSH
Alzheimer Disease
NeuroMMSigDB
MAPK-JNK subgraph
NeuroMMSigDB
Nitric oxide subgraph
NeuroMMSigDB
Tau protein subgraph

Out-Edges 7

complex(GO:"neurofibrillary tangle") association p(HGNC:ESR1) View Subject | View Object

In the hippocampal and cortical tissues of all AD cases examined, neuronal staining for ERα was a prominent finding, both with a weak cytoplasmic stain, but often specifically with a fibrillar appearance suggesting ERα was in neurofibrillary tangles (Fig. 1A), also shown at a higher magnification (Fig. 1B). PubMed:26837465

Appears in Networks:
Annotations
Confidence
Medium
MeSH
Cerebral Cortex
MeSH
Hippocampus

complex(GO:"neurofibrillary tangle") association p(HGNC:ESR1) View Subject | View Object

To confirm the localization of ERα in NFTs, double fluorescence staining with antibodies to ERα and hyperphosphorylated tau (PHF-1) revealed that ERα -positive NFTs were also positive for PHF-1 (Fig. 2A–F). PubMed:26837465

Appears in Networks:
Annotations
Confidence
Medium
MeSH
Cerebral Cortex
MeSH
Hippocampus

complex(GO:"neurofibrillary tangle") causesNoChange act(a(MESH:Neurons)) View Subject | View Object

We found that in the visual cortex, neurons containing conspicuous quantities of mislocalized and aggregated tau nonetheless appear to have a normal capacity to integrate dendritic inputs and respond robustly to visual stimuli and also maintain normal somatic baseline calcium levels. In particular, we show that individual NFT-bearing neurons can respond robustly after integrating sensory inputs and are functionally indistinguishable from neighboring non–NFT-bearing neurons. These results demonstrate that NFT-bearing neurons remain functionally integrated in cortical circuits. PubMed:24368848

Appears in Networks:
Annotations
Uberon
visual cortex
MeSH
Frontotemporal Dementia

complex(GO:"neurofibrillary tangle") decreases complex(GO:"dendritic tree") View Subject | View Object

Dendritic arborization was abundant in RD3-/4+ pretangles, attenuated in RD3+/4+ neurons, and further attenuated in RD3+/4- ghost tangles. PubMed:23407988

Appears in Networks:
Annotations
Disease Ontology (DO)
Alzheimer's disease

complex(GO:"neurofibrillary tangle") association complex(p(HGNC:MAPT, pmod(Ph, Thr, 231)), p(HGNC:PIN1, frag("5_39"))) View Subject | View Object

This result confirms previous findings that T231 is an important Cdc2 phosphorylation site in tau, and is also consistent with Pin1 binding mitotically pTau (Fig. 1a) and being sequestered on to PHFs in AD brains, where Cdc2 is upregulated (Fig. 3). PubMed:10391244

Appears in Networks:

complex(GO:"neurofibrillary tangle") positiveCorrelation p(HGNC:CDK1) View Subject | View Object

This result confirms previous findings that T231 is an important Cdc2 phosphorylation site in tau, and is also consistent with Pin1 binding mitotically pTau (Fig. 1a) and being sequestered on to PHFs in AD brains, where Cdc2 is upregulated (Fig. 3). PubMed:10391244

Appears in Networks:

complex(GO:"neurofibrillary tangle") positiveCorrelation g(DBSNP:rs104893877) View Subject | View Object

Recent studies of an individual with Parkinson’s disease (IX-47) of the Contursi kindred with the rare A53T alpha-synuclein mutation revealed widespread -syn and tau inclusions (15). Post-mortem examination of another affected member (IX-51) of this kindred also demonstrated abundant -syn and tau inclusions(figs. S1 and S2). Thus, a pathogenic mutation in alpha-synuclein that is known to increase the propensity of alpha-synuclein to fibrillize (8, 9) also promotes formation of tau inclusions in humans. PubMed:12714745

Appears in Networks:
Annotations
Disease Ontology (DO)
Parkinson's disease

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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.