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a(HBP:"amyloid-beta aggregates")

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Entity

Name
amyloid-beta aggregates
Namespace
HBP
Namespace Version
20181029
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/785431732a26d6809b4162d98b95687d16404e63/export/hbp-names.belns

Appears in Networks 12

Nicotinic acetylcholine receptor signalling: roles in Alzheimer's disease and amyloid neuroprotection. v1.0.0

Activation of M1 and M4 muscarinic receptors as potential treatments for Alzheimer's disease and schizophrenia. v1.0.0

This file encodes the article Activation of M1 and M4 muscarinic receptors as potential treatments for Alzheimer’s disease and schizophrenia by Choi et al, 2014

Nicotinic Acetylcholine Receptors and Nicotinic Cholinergic Mechanisms of the Central Nervous System v1.0.0

M1 muscarinic acetylcholine receptor in Alzheimer’s disease v1.0.0

This file encodes the article M1 muscarinic acetylcholine receptor in Alzheimer’s disease by Jiang et al, 2014

Role of the nicotinic acetylcholine receptor in Alzheimer's disease pathology and treatment v1.0.1

The Ubiquitin Proteasome System in Neurodegenerative Diseases: Sometimes the Chicken, Sometimes the Egg v1.0.0

Tau oligomers and tau toxicity in neurodegenerative disease v1.0.0

Tau oligomers and tau toxicity in neurodegenerative disease by Ward et al., 2012

Amyloid-Binding Alcohol Dehydrogenase (ABAD) Inhibitors for the Treatment of Alzheimer’s Disease v1.0.0

Model systems of protein-misfolding diseases reveal chaperone modifiers of proteotoxicity v1.0.0

Alzheimer's disease pathological lesions activate the spleen tyrosine kinase. v1.0.0

Phytochemicals as inhibitors of NF-κB for treatment of Alzheimer’s disease v1.0.0

Upstream regulators and downstream effectors of NF-κBinAlzheimer's disease v1.0.0

In-Edges 22

path(MESH:"Alzheimer Disease") association a(HBP:"amyloid-beta aggregates") View Subject | View Object

It is generally agreed that the beta-amyloid peptide (Abeta) plays an important role in the development of AD. The brains of patients with AD contain deposits of Abeta, and Abeta is toxic to cultured neurons (Kihara et al., 1997a; Yao et al., 2005). In addition, mice transgenically overexpressing Abeta or with mutations that enhance Abeta aggregation show many of the symptoms of AD (Hsiao et al., 1996; van Groen et al., 2006). PubMed:19293145

Appears in Networks:
Annotations
MeSH
Brain

path(MESH:"Plaque, Amyloid") association a(HBP:"amyloid-beta aggregates") View Subject | View Object

The hallmarks of AD pathology are the accumulation of amyloid-beta (Abeta) peptide aggregates (neuritic plaques) and hyperphosphorylated tau protein (neurofibrillary tangles). PubMed:24511233

Appears in Networks:

p(HGNC:CHRNA7) association a(HBP:"amyloid-beta aggregates") View Subject | View Object

This prospect was supported by the finding that α7 nAChRs were found in plaques (159), and α7 and α4 subunits positively correlated with neurons that accumulated Aβ and hyperphosphorylated tau in AD brain tissue (161). PubMed:17009926

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

complex(a(CHEBI:"amyloid-beta"), a(MESH:"alpha7 Nicotinic Acetylcholine Receptor")) decreases a(HBP:"amyloid-beta aggregates") View Subject | View Object

The mechanism proposed is that the Aß-alpha7 nAChR interaction could activate neuroprotective downstream pathways (Parri et al., 2011), and that at the same time the interaction engages Abeta preventing its aggregation PubMed:25514383

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

path(MESH:"Alzheimer Disease") positiveCorrelation a(HBP:"amyloid-beta aggregates") View Subject | View Object

With the progression of the disease the amount of Abeta increases, it starts to accumulate, and becomes toxic for the neurons (Hernandez et al., 2010) PubMed:25514383

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

p(HGNC:APP, var("?")) increases a(HBP:"amyloid-beta aggregates") View Subject | View Object

They have demonstrated that AD can be caused by mutations in the APP gene, either in the vicinity of the secretase cleavage sites, causing abnormal APP processing, or in the sequence coding for Abeta, giving rise to a peptide that is more likely to self-aggregate PubMed:14556719

Appears in Networks:

path(MESH:"Prion Diseases") increases a(HBP:"amyloid-beta aggregates") View Subject | View Object

Prion disease neuropathology is characterized by widespread neuronal death, accompanied by spongiform vacuolation and astrogliosis, usually combined with widespread deposits of extracellular amyloid aggregates. PubMed:14556719

Appears in Networks:

path(MESH:"Alzheimer Disease") positiveCorrelation a(HBP:"amyloid-beta aggregates") View Subject | View Object

AD (Alzheimer’s disease) is a progressive neurodegenerative disorder characterized by the extracellular accumulation of amyloid beta-peptide and the intracellular accumulation of tau PubMed:22817713

Appears in Networks:
Annotations
Confidence
Medium
MeSH
Extracellular Space

a(CHEBI:"methylene blue") decreases a(HBP:"amyloid-beta aggregates") View Subject | View Object

In mechanistic studies, it was proposed that methylene blue inhibits the Aβ-ABAD interaction and decreases mitochondrial dysfunction by decreasing the expression of ABAD levels, in addition to decreasing Aβ levels. PubMed:30444369

Appears in Networks:

a(HBP:AG18051) decreases act(a(HBP:"amyloid-beta aggregates")) View Subject | View Object

Moreover, it has been shown to ameliorate Aβ-induced toxicity at the cellular level. 7 PubMed:30444369

Appears in Networks:
Annotations
MeSH
Neurons

a(PUBCHEM:5757) decreases a(HBP:"amyloid-beta aggregates") View Subject | View Object

For example, estradiol can reduce the generation of Aβ by altering the metabolism of APP and disrupting it’s trafficking. PubMed:30444369

Appears in Networks:

p(HGNC:CSNK1A1) association a(HBP:"amyloid-beta aggregates") View Subject | View Object

Isoforms of CK1 are responsible for tau phosphorylation. 129 The enzyme can modulate the activity of γ-secretase and consequently the production of Aβ. PubMed:30444369

Appears in Networks:
Annotations
MeSH
Neurons

p(HGNC:CRYAB) association a(HBP:"amyloid-beta aggregates") View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

Appears in Networks:

p(HGNC:HSPB1) association a(HBP:"amyloid-beta aggregates") View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

Appears in Networks:

p(HGNC:HSPB6) association a(HBP:"amyloid-beta aggregates") View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

Appears in Networks:

p(HGNC:HSPB8) association a(HBP:"amyloid-beta aggregates") View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

Appears in Networks:

act(p(HGNC:SYK)) positiveCorrelation a(HBP:"amyloid-beta aggregates") View Subject | View Object

In addition, we observed that pSyk immunoreactivity is upregulated near A β plaques but neither colocalizes with microglia nor astrocytes suggesting that it could be of neuronal origin. (Fig. 1e). PubMed:28877763

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease

act(p(HGNC:SYK)) positiveCorrelation a(HBP:"amyloid-beta aggregates") View Subject | View Object

In conclusion, activated Syk is not only found in microglia but also in neurons near A β deposits, par- ticularly in dystrophic neurites of Tg APPsw and Tg PS1/APPsw mice supporting a possible role of Syk activation in the formation of dystrophic neurites. PubMed:28877763

Appears in Networks:
Annotations
MeSH
Neurites
MeSH
Neurons

act(p(HGNC:SYK)) positiveCorrelation a(HBP:"amyloid-beta aggregates") View Subject | View Object

We found an increase in Syk activation in DNs surrounding A β deposits as well as in neurons displaying an accumu- lation of phosphorylated Tau at Y18 and elevated levels of MC1 pathogenic tau conformers in AD brain sections whereas only weak immunoreactivity for pSyk was ob- served in brain sections from a non-demented control (Figs. 15, 16 and 17). PubMed:28877763

Appears in Networks:
Annotations
MeSH
Neurites
MeSH
Brain
MeSH
Alzheimer Disease

a(PUBCHEM:155160) decreases a(HBP:"amyloid-beta aggregates") View Subject | View Object

Beneficial effects of 4-O-methylhonokinol on memory were observed by the reduction of Aaggregation in A 1-42-injected mice and memory-impaired mice with its anti-oxidative and anti-inflammatory qualities [141–143]. PubMed:29179999

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

a(PUBCHEM:442534) decreases a(HBP:"amyloid-beta aggregates") View Subject | View Object

Paeoniflorin improved memory impairments and lowered A accumulation in APP/PS1 trans-genic mice [1]. PubMed:29179999

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

p(HGNC:PTGS2) association a(HBP:"amyloid-beta aggregates") View Subject | View Object

In addition, COX-2, mainly regulated by NF-κB, is notably upregulated in the brains of AD patients, which may be associated with the formation of Aβ plaque [65]. PubMed:27288790

Appears in Networks:
Annotations
MeSH
Brain

Out-Edges 19

a(HBP:"amyloid-beta aggregates") association path(MESH:"Alzheimer Disease") View Subject | View Object

It is generally agreed that the beta-amyloid peptide (Abeta) plays an important role in the development of AD. The brains of patients with AD contain deposits of Abeta, and Abeta is toxic to cultured neurons (Kihara et al., 1997a; Yao et al., 2005). In addition, mice transgenically overexpressing Abeta or with mutations that enhance Abeta aggregation show many of the symptoms of AD (Hsiao et al., 1996; van Groen et al., 2006). PubMed:19293145

Appears in Networks:
Annotations
MeSH
Brain

a(HBP:"amyloid-beta aggregates") association path(MESH:"Plaque, Amyloid") View Subject | View Object

The hallmarks of AD pathology are the accumulation of amyloid-beta (Abeta) peptide aggregates (neuritic plaques) and hyperphosphorylated tau protein (neurofibrillary tangles). PubMed:24511233

Appears in Networks:

a(HBP:"amyloid-beta aggregates") association p(HGNC:CHRNA7) View Subject | View Object

This prospect was supported by the finding that α7 nAChRs were found in plaques (159), and α7 and α4 subunits positively correlated with neurons that accumulated Aβ and hyperphosphorylated tau in AD brain tissue (161). PubMed:17009926

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

a(HBP:"amyloid-beta aggregates") increases path(MESH:"Plaque, Amyloid") View Subject | View Object

Senile plaques consist of deposits of small peptides called beta-amyloid (Abeta). Multiple lines of evidence suggest that the overproduction/ aggregation of neurotoxic Abeta in vulnerable brain regions is the primary cause of AD PubMed:24590577

Appears in Networks:

a(HBP:"amyloid-beta aggregates") increases path(MESH:"Alzheimer Disease") View Subject | View Object

Senile plaques consist of deposits of small peptides called beta-amyloid (Abeta). Multiple lines of evidence suggest that the overproduction/ aggregation of neurotoxic Abeta in vulnerable brain regions is the primary cause of AD PubMed:24590577

Appears in Networks:

a(HBP:"amyloid-beta aggregates") positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

With the progression of the disease the amount of Abeta increases, it starts to accumulate, and becomes toxic for the neurons (Hernandez et al., 2010) PubMed:25514383

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

a(HBP:"amyloid-beta aggregates") positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

AD (Alzheimer’s disease) is a progressive neurodegenerative disorder characterized by the extracellular accumulation of amyloid beta-peptide and the intracellular accumulation of tau PubMed:22817713

Appears in Networks:
Annotations
Confidence
Medium
MeSH
Extracellular Space

a(HBP:"amyloid-beta aggregates") increases path(HBP:"mitochondrial dysfunction") View Subject | View Object

Mitochondrial dysfunction is the hallmark of Aβ-induced toxicity. 50-52 PubMed:30444369

Appears in Networks:

a(HBP:"amyloid-beta aggregates") decreases act(p(FPLX:COX)) View Subject | View Object

Accumulation of Aβ has also been associated with a decrease in the activity of cytochrome c oxidase, the terminal enzyme in the electron transport chain. PubMed:30444369

Appears in Networks:

a(HBP:"amyloid-beta aggregates") association p(HGNC:CSNK1A1) View Subject | View Object

Isoforms of CK1 are responsible for tau phosphorylation. 129 The enzyme can modulate the activity of γ-secretase and consequently the production of Aβ. PubMed:30444369

Appears in Networks:
Annotations
MeSH
Neurons

a(HBP:"amyloid-beta aggregates") association p(HGNC:HSPB1) View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

Appears in Networks:

a(HBP:"amyloid-beta aggregates") association p(HGNC:CRYAB) View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

Appears in Networks:

a(HBP:"amyloid-beta aggregates") association p(HGNC:HSPB6) View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

Appears in Networks:

a(HBP:"amyloid-beta aggregates") association p(HGNC:HSPB8) View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

Appears in Networks:

a(HBP:"amyloid-beta aggregates") positiveCorrelation act(p(HGNC:SYK)) View Subject | View Object

In addition, we observed that pSyk immunoreactivity is upregulated near A β plaques but neither colocalizes with microglia nor astrocytes suggesting that it could be of neuronal origin. (Fig. 1e). PubMed:28877763

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease

a(HBP:"amyloid-beta aggregates") positiveCorrelation act(p(HGNC:SYK)) View Subject | View Object

In conclusion, activated Syk is not only found in microglia but also in neurons near A β deposits, par- ticularly in dystrophic neurites of Tg APPsw and Tg PS1/APPsw mice supporting a possible role of Syk activation in the formation of dystrophic neurites. PubMed:28877763

Appears in Networks:
Annotations
MeSH
Neurites
MeSH
Neurons

a(HBP:"amyloid-beta aggregates") positiveCorrelation act(p(HGNC:SYK)) View Subject | View Object

We found an increase in Syk activation in DNs surrounding A β deposits as well as in neurons displaying an accumu- lation of phosphorylated Tau at Y18 and elevated levels of MC1 pathogenic tau conformers in AD brain sections whereas only weak immunoreactivity for pSyk was ob- served in brain sections from a non-demented control (Figs. 15, 16 and 17). PubMed:28877763

Appears in Networks:
Annotations
MeSH
Neurites
MeSH
Brain
MeSH
Alzheimer Disease

a(HBP:"amyloid-beta aggregates") increases act(p(FPLX:"IKK_complex")) View Subject | View Object

Under different envi- ronmental conditions such as Aβ/ROS/cytokines accumulation, the IκB kinase (IKK) complex becomes activated and mediates the phosphoryla- tion of IκBs, then IκBs are degradated and the remaining NF-κB dimer is activated and thus translocates to the nucleus where it binds to the DNA consensus sequence of various target genes [9–11]. PubMed:27288790

Appears in Networks:

a(HBP:"amyloid-beta aggregates") association p(HGNC:PTGS2) View Subject | View Object

In addition, COX-2, mainly regulated by NF-κB, is notably upregulated in the brains of AD patients, which may be associated with the formation of Aβ plaque [65]. PubMed:27288790

Appears in Networks:
Annotations
MeSH
Brain

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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.