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Appears in Networks 2

In-Edges 5

p(HGNC:PRDX2, pmod(Ph, Thr, 89)) decreases act(p(HGNC:PRDX2)) View Subject | View Object

Inactivation of Prdx-2 is controlled by a kinase that has been shown to be elevated in AD, CDK5, 107, 108 which phosphorylates Thr 89 and results in deactivation of Prdx-2. PubMed:30444369

path(MESH:"Alzheimer Disease") negativeCorrelation act(p(HGNC:PRDX2)) View Subject | View Object

The first, peroxiredoxin-2 (Prdx-2), functions as an antioxidant and has been shown to be inactivated in AD. PubMed:30444369

path(MESH:"Alzheimer Disease") positiveCorrelation p(HGNC:PRDX2) View Subject | View Object

In transgenic AD mice and the post-mortem human brain of AD patients, the expression of Prdx-2 is shown to be elevated, due to the attempted protection of neurons from Aβ-induced toxicity. PubMed:30444369

a(CHEBI:"hydrogen peroxide") negativeCorrelation p(HGNC:PRDX2) View Subject | View Object

Prx-2 has emerged as the key antioxidant protein that protects RBCs against biologically relevant concentrations of H2O2 produced endogenously (via hemoglobin autoxidation) or exogenously by inflammatory cells25,26. PubMed:26202471

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bp(MESH:"Oxidative Stress") negativeCorrelation p(HGNC:PRDX2) View Subject | View Object

While it is clear that PRDX2 plays an important role in protecting RBCs from oxidative stress, the relative importance of PRDX2 in scavenging H2O2 in RBC has not been fully elucidated. PubMed:23215741

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Introduction

Out-Edges 5

act(p(HGNC:PRDX2)) negativeCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

The first, peroxiredoxin-2 (Prdx-2), functions as an antioxidant and has been shown to be inactivated in AD. PubMed:30444369

p(HGNC:PRDX2) positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

In transgenic AD mice and the post-mortem human brain of AD patients, the expression of Prdx-2 is shown to be elevated, due to the attempted protection of neurons from Aβ-induced toxicity. PubMed:30444369

p(HGNC:PRDX2) negativeCorrelation bp(MESH:"Oxidative Stress") View Subject | View Object

While it is clear that PRDX2 plays an important role in protecting RBCs from oxidative stress, the relative importance of PRDX2 in scavenging H2O2 in RBC has not been fully elucidated. PubMed:23215741

Appears in Networks:
Annotations
Text Location
Introduction

p(HGNC:PRDX2) negativeCorrelation a(CHEBI:"hydrogen peroxide") View Subject | View Object

Prx-2 has emerged as the key antioxidant protein that protects RBCs against biologically relevant concentrations of H2O2 produced endogenously (via hemoglobin autoxidation) or exogenously by inflammatory cells25,26. PubMed:26202471

Appears in Networks:
Annotations
Text Location
Introduction

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.