Equivalencies: 0 | Classes: 0 | Children: 0 | Explore

Entity

Name
Neurofibrillary Tangles
Namespace
mesh
Namespace Version
20181007
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/8ccfed235e418e4c8aa576f9a5ef0f838e794c7f/external/mesh-names.belns

Appears in Networks 7

In-Edges 14

p(HGNC:MAPT) association a(MESH:"Neurofibrillary Tangles") View Subject | View Object

AD is characterized pathologically by the occurrence of intracellular neurofibrillary tangles rich in tau protein and extracellular plaques containing amyloid peptides (Price et al., 1991). PubMed:19293145

path(MESH:"Alzheimer Disease") positiveCorrelation a(MESH:"Neurofibrillary Tangles") View Subject | View Object

AD is characterized pathologically by the occurrence of intracellular neurofibrillary tangles rich in tau protein and extracellular plaques containing amyloid peptides (Price et al., 1991). PubMed:19293145

complex(a(GO:"proteasome complex"), a(MESH:"Inclusion Bodies")) positiveCorrelation a(MESH:"Neurofibrillary Tangles") View Subject | View Object

Accumulation of ubiquitin conjugates and/or inclusion bodies associated with ubiquitin, proteasome, and certain disease-characteristic proteins have been reported in a broad array of chronic neurodegenerative diseases, such as the neurofibrillary tangles of Alzheimer’s disease (AD), brainstem Lewy bodies (LBs) (the neuropathological hallmark in Parkinson’s disease [PD]), Bunina bodies in Amyotrophic Lateral Sclerosis (ALS), and nuclear inclusions in CAG repeat expansion (polyglutamine/Q extension) disorders such as Huntington’s disease, Spinocerebellar Ataxias (SCAs), and Spinal and Bulbar Muscular Atrophy (SBMA; Kennedy’s disease) (reviewed recently by Alves-Rodrigues et al., 1998; Sherman and Goldberg, 2001) (Figure 2) PubMed:14556719

complex(a(MESH:"Inclusion Bodies"), a(MESH:Ubiquitin)) positiveCorrelation a(MESH:"Neurofibrillary Tangles") View Subject | View Object

Accumulation of ubiquitin conjugates and/or inclusion bodies associated with ubiquitin, proteasome, and certain disease-characteristic proteins have been reported in a broad array of chronic neurodegenerative diseases, such as the neurofibrillary tangles of Alzheimer’s disease (AD), brainstem Lewy bodies (LBs) (the neuropathological hallmark in Parkinson’s disease [PD]), Bunina bodies in Amyotrophic Lateral Sclerosis (ALS), and nuclear inclusions in CAG repeat expansion (polyglutamine/Q extension) disorders such as Huntington’s disease, Spinocerebellar Ataxias (SCAs), and Spinal and Bulbar Muscular Atrophy (SBMA; Kennedy’s disease) (reviewed recently by Alves-Rodrigues et al., 1998; Sherman and Goldberg, 2001) (Figure 2) PubMed:14556719

p(HGNC:MAPT) association a(MESH:"Neurofibrillary Tangles") View Subject | View Object

In contrast, the neurofibrillary tangles are intracellular and are rich in tau, a structural protein that is normally associated with microtubuli PubMed:14556719

deg(p(HGNC:MAPT)) increases a(MESH:"Neurofibrillary Tangles") View Subject | View Object

Proteolytic processing/degradation of tau is also believed to be important for the formation of the neurofibrillary tangles,although the molecular pathways involved in this process are not fully understood PubMed:14556719

path(MESH:"Alzheimer Disease") increases a(MESH:"Neurofibrillary Tangles") View Subject | View Object

Patients with AD display two types of protein deposits: extracellular amyloid plaques and intracellular neurofibrillary tangles (Hardy and Selkoe, 2002). PubMed:14556719

a(HBP:"Tau oligomers") association a(MESH:"Neurofibrillary Tangles") View Subject | View Object

In severe AD cases (i.e. Braak stage V-VI), all markers continue to colocalize in classic NFTs within the hippocampus that characterize AD tau pathology (Fig. 5E–H) PubMed:27574109

a(HBP:"phosphatase-activating domain") association a(MESH:"Neurofibrillary Tangles") View Subject | View Object

In severe AD cases (i.e. Braak stage V-VI), all markers continue to colocalize in classic NFTs within the hippocampus that characterize AD tau pathology (Fig. 5E–H) PubMed:27574109

p(HGNC:MAPT) association a(MESH:"Neurofibrillary Tangles") View Subject | View Object

In severe AD cases (i.e. Braak stage V-VI), all markers continue to colocalize in classic NFTs within the hippocampus that characterize AD tau pathology (Fig. 5E–H) PubMed:27574109

p(HBP:"UBB+1") association a(MESH:"Neurofibrillary Tangles") View Subject | View Object

A Ub with a 19-residue C-terminal extension from the UBB gene, or UBB+1 (Fig.2A) is selectively expressed in the brains of AD patients (van Leeuwen et al.,1998) and is often found to be accumulated in NFT in Alzheimer’s disease and other tauopathies PubMed:23528736

p(HGNC:TFEB) regulates deg(a(MESH:"Neurofibrillary Tangles")) View Subject | View Object

For example, like Aβ, clearance of pTau/NFT also can be regulated by TFEB, which increases the activity of autophagy and lysosome (Polito et al. 2014) PubMed:29626319

p(FPLX:PPP2C, pmod(Ph)) association a(MESH:"Neurofibrillary Tangles") View Subject | View Object

Furthermore, phosphorylated PP2A C decorates neurofibrillary tangles. PubMed:22299660

Out-Edges 12

a(MESH:"Neurofibrillary Tangles") positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

AD is characterized pathologically by the occurrence of intracellular neurofibrillary tangles rich in tau protein and extracellular plaques containing amyloid peptides (Price et al., 1991). PubMed:19293145

a(MESH:"Neurofibrillary Tangles") association p(HGNC:MAPT) View Subject | View Object

AD is characterized pathologically by the occurrence of intracellular neurofibrillary tangles rich in tau protein and extracellular plaques containing amyloid peptides (Price et al., 1991). PubMed:19293145

a(MESH:"Neurofibrillary Tangles") positiveCorrelation complex(a(MESH:"Inclusion Bodies"), a(MESH:Ubiquitin)) View Subject | View Object

Accumulation of ubiquitin conjugates and/or inclusion bodies associated with ubiquitin, proteasome, and certain disease-characteristic proteins have been reported in a broad array of chronic neurodegenerative diseases, such as the neurofibrillary tangles of Alzheimer’s disease (AD), brainstem Lewy bodies (LBs) (the neuropathological hallmark in Parkinson’s disease [PD]), Bunina bodies in Amyotrophic Lateral Sclerosis (ALS), and nuclear inclusions in CAG repeat expansion (polyglutamine/Q extension) disorders such as Huntington’s disease, Spinocerebellar Ataxias (SCAs), and Spinal and Bulbar Muscular Atrophy (SBMA; Kennedy’s disease) (reviewed recently by Alves-Rodrigues et al., 1998; Sherman and Goldberg, 2001) (Figure 2) PubMed:14556719

a(MESH:"Neurofibrillary Tangles") positiveCorrelation complex(a(GO:"proteasome complex"), a(MESH:"Inclusion Bodies")) View Subject | View Object

Accumulation of ubiquitin conjugates and/or inclusion bodies associated with ubiquitin, proteasome, and certain disease-characteristic proteins have been reported in a broad array of chronic neurodegenerative diseases, such as the neurofibrillary tangles of Alzheimer’s disease (AD), brainstem Lewy bodies (LBs) (the neuropathological hallmark in Parkinson’s disease [PD]), Bunina bodies in Amyotrophic Lateral Sclerosis (ALS), and nuclear inclusions in CAG repeat expansion (polyglutamine/Q extension) disorders such as Huntington’s disease, Spinocerebellar Ataxias (SCAs), and Spinal and Bulbar Muscular Atrophy (SBMA; Kennedy’s disease) (reviewed recently by Alves-Rodrigues et al., 1998; Sherman and Goldberg, 2001) (Figure 2) PubMed:14556719

a(MESH:"Neurofibrillary Tangles") association p(HGNC:MAPT) View Subject | View Object

In contrast, the neurofibrillary tangles are intracellular and are rich in tau, a structural protein that is normally associated with microtubuli PubMed:14556719

a(MESH:"Neurofibrillary Tangles") increases p(HGNC:MAPT) View Subject | View Object

In conjunction with the formation of neurofibrillary tangles, the synthesis of the tau protein increases, and it undergoes an abnormal posttranslational modification characterized by hyperphosphorylation PubMed:14556719

a(MESH:"Neurofibrillary Tangles") increases p(HGNC:MAPT, pmod(HBP:hyperphosphorylation)) View Subject | View Object

In conjunction with the formation of neurofibrillary tangles, the synthesis of the tau protein increases, and it undergoes an abnormal posttranslational modification characterized by hyperphosphorylation PubMed:14556719

a(MESH:"Neurofibrillary Tangles") association a(HBP:"Tau oligomers") View Subject | View Object

In severe AD cases (i.e. Braak stage V-VI), all markers continue to colocalize in classic NFTs within the hippocampus that characterize AD tau pathology (Fig. 5E–H) PubMed:27574109

a(MESH:"Neurofibrillary Tangles") association a(HBP:"phosphatase-activating domain") View Subject | View Object

In severe AD cases (i.e. Braak stage V-VI), all markers continue to colocalize in classic NFTs within the hippocampus that characterize AD tau pathology (Fig. 5E–H) PubMed:27574109

a(MESH:"Neurofibrillary Tangles") association p(HGNC:MAPT) View Subject | View Object

In severe AD cases (i.e. Braak stage V-VI), all markers continue to colocalize in classic NFTs within the hippocampus that characterize AD tau pathology (Fig. 5E–H) PubMed:27574109

a(MESH:"Neurofibrillary Tangles") association p(HBP:"UBB+1") View Subject | View Object

A Ub with a 19-residue C-terminal extension from the UBB gene, or UBB+1 (Fig.2A) is selectively expressed in the brains of AD patients (van Leeuwen et al.,1998) and is often found to be accumulated in NFT in Alzheimer’s disease and other tauopathies PubMed:23528736

a(MESH:"Neurofibrillary Tangles") association p(FPLX:PPP2C, pmod(Ph)) View Subject | View Object

Furthermore, phosphorylated PP2A C decorates neurofibrillary tangles. PubMed:22299660

About

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.