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Entity

Name
Amyloid beta-Peptides
Namespace
mesh
Namespace Version
20180906
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/mesh-names.belns

Appears in Networks 11

In-Edges 19

path(MESH:"Alzheimer Disease") positiveCorrelation a(MESH:"Amyloid beta-Peptides") View Subject | View Object

The histopathological changes in the brain include the presence of extracellular amyloid plaques consisted of various peptide variants of amyloid β (Aβ) and accumulation of intracellular neurofibrillary tangles (NFTs) composed mainly of phosphorylated Tau proteins (pTau), localized predominantly in neurons (reviewed by Serrano-Pozo et al. 2011). PubMed:29196815

complex(FPLX:"Gamma_secretase") increases a(MESH:"Amyloid beta-Peptides") View Subject | View Object

γ-Secretase cleaves at multiple sites within the transmembrane domain of APP, generating Aβ peptides ranging in length from 38 to 43 residues (4). PubMed:18650430

a(HBP:HBP00018) association a(MESH:"Amyloid beta-Peptides") View Subject | View Object

The amyloid plaques associated with AD were first purified and found to consist of multimeric aggregates of Abeta polypeptide containing about 40 amino acid residues in the mid-1980s (Glenner and Wong 1984; Masters et al. 1985) PubMed:22122372

p(HGNC:APP) increases a(MESH:"Amyloid beta-Peptides") View Subject | View Object

APP undergoes post-translational proteolysis/processing to generate the hydrophobic beta-amyloid (Abeta) peptides PubMed:22122372

path(MESH:"Alzheimer Disease") association a(MESH:"Amyloid beta-Peptides") View Subject | View Object

Plaques consisting of beta-amyloid (Abeta) peptide (Selkoe 1998), neurofibrillary tangles consisting largely of hyperphosphorylated microtubule-associated tau protein (Buee et al. 2000; Gendron and Petrucelli 2009) and neuron loss in the hippocampus and cortex regions are the major pathological hallmarks of Alzheimer’s disease. PubMed:22122372

a(MESH:"Amyloid Precursor Protein Secretases") decreases a(MESH:"Amyloid beta-Peptides") View Subject | View Object

Moreover, AF267B treatment leads to an increase in alpha secretase, which is an enzyme that can prevent the production of Aβ peptide PubMed:26813123

p(FPLX:CHRN) negativeCorrelation a(MESH:"Amyloid beta-Peptides") View Subject | View Object

Possible factors such as amyloid peptide accumulation, hyperphosphorylation of tau protein, oxidative stress, and modification of cell membrane during the development of AD may be related to decreased protein levels of nAChRs (Farooqui et al 1995; Smith et al 1996) PubMed:11230871

p(HGNC:APP) increases a(MESH:"Amyloid beta-Peptides") View Subject | View Object

The plaques in AD are rich in amyloid beta peptides (Abeta) that are produced by proteolytic cleavage of the amyloid precursor peptide (APP), a glycolipid located in the outer cell membrane PubMed:14556719

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

The plaques in AD are rich in amyloid beta peptides (Abeta) that are produced by proteolytic cleavage of the amyloid precursor peptide (APP), a glycolipid located in the outer cell membrane PubMed:14556719

a(CHEBI:cholesterol) increases a(MESH:"Amyloid beta-Peptides") View Subject | View Object

Cellular cholesterol can directly impact the level of Aβ, as decreases in cholesterol levels inhibit the generation of Aβ peptides through direct modulation of γ-secretase activity [78,79]. PubMed:29758300

p(HGNC:APP) increases a(MESH:"Amyloid beta-Peptides") View Subject | View Object

Aβ peptides originate from the transmembrane protein amyloid precursor protein (APP) which undergoes sequential cleavage via two distinct pathways by the enzyme complexes β- and γ-secretase [31] PubMed:29758300

p(HGNC:BECN1) decreases a(MESH:"Amyloid beta-Peptides") View Subject | View Object

In line with this, reduced Beclin 1 levels, as seen in AD models [16], increase the levels of intracellular and extracellular Aβ peptides, supporting the role of macroautophagy in the generation and degradation of Aβ [33,35]. PubMed:29758300

bp(GO:"lysosomal protein catabolic process") increases deg(a(MESH:"Amyloid beta-Peptides")) View Subject | View Object

AVs are also enriched in APP substrates and secretases and, during autophagy, Ab peptide is generated from APP (Yu et al. 2005), although it is subsequently degraded in lysosomes under normal circumstances (Heinrich et al. 1999; Bahr et al. 2002; Florez-McClure et al. 2007). PubMed:22908190

p(HGNC:TNF) increases a(MESH:"Amyloid beta-Peptides") View Subject | View Object

Tumor necrosis factor-α (TNFα) has been shown to induce BACE-1 expression and to contribute to brain accumulation of Aβ peptides PubMed:25331948

Out-Edges 6

a(MESH:"Amyloid beta-Peptides") positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

The histopathological changes in the brain include the presence of extracellular amyloid plaques consisted of various peptide variants of amyloid β (Aβ) and accumulation of intracellular neurofibrillary tangles (NFTs) composed mainly of phosphorylated Tau proteins (pTau), localized predominantly in neurons (reviewed by Serrano-Pozo et al. 2011). PubMed:29196815

a(MESH:"Amyloid beta-Peptides") increases bp(GO:"cell adhesion") View Subject | View Object

Interestingly, because the RHDS sequence is contained within the N terminus of Aβ, similar cell adhesion-promoting properties have also been attributed to the Aβ peptide itself. PubMed:18650430

a(MESH:"Amyloid beta-Peptides") association path(MESH:"Alzheimer Disease") View Subject | View Object

Plaques consisting of beta-amyloid (Abeta) peptide (Selkoe 1998), neurofibrillary tangles consisting largely of hyperphosphorylated microtubule-associated tau protein (Buee et al. 2000; Gendron and Petrucelli 2009) and neuron loss in the hippocampus and cortex regions are the major pathological hallmarks of Alzheimer’s disease. PubMed:22122372

a(MESH:"Amyloid beta-Peptides") association a(HBP:HBP00018) View Subject | View Object

The amyloid plaques associated with AD were first purified and found to consist of multimeric aggregates of Abeta polypeptide containing about 40 amino acid residues in the mid-1980s (Glenner and Wong 1984; Masters et al. 1985) PubMed:22122372

a(MESH:"Amyloid beta-Peptides") negativeCorrelation p(FPLX:CHRN) View Subject | View Object

Possible factors such as amyloid peptide accumulation, hyperphosphorylation of tau protein, oxidative stress, and modification of cell membrane during the development of AD may be related to decreased protein levels of nAChRs (Farooqui et al 1995; Smith et al 1996) PubMed:11230871

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

The plaques in AD are rich in amyloid beta peptides (Abeta) that are produced by proteolytic cleavage of the amyloid precursor peptide (APP), a glycolipid located in the outer cell membrane PubMed:14556719

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.