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a(HM:"oxidative reactions")

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Entity

Name
oxidative reactions
Namespace
HM
Namespace Version
None
Pattern
.*

Appears in Networks 1

Heme Curation v0.0.1-dev

Mechanistic knowledge surrounding heme

In-Edges 9

a(CHEBI:heme) positiveCorrelation a(HM:"oxidative reactions") View Subject | View Object

Ferryl heme and associated protein radicals with high redox potentials (~1.0 V) can induce a wide variety of oxidative reactions that affect the protein and nearby molecules [2]. PubMed:24486321

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Discussion

a(CHEBI:heme) increases a(HM:"oxidative reactions") View Subject | View Object

Extracellular hemoglobin and heme are pro-oxidative, proinflammatory, and cytotoxic [10–12], and can contribute to the pathology of hemolytic diseases. PubMed:26875449

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Text Location
Review

a(MESH:"haptoglobin-hemoglobin complex") decreases a(HM:"oxidative reactions") View Subject | View Object

This result is in accord with recent work, which showed that Hp binding to Hb prevents oxidative damage to the globin. PubMed:24486321

Appears in Networks:
Annotations
MeSH
Anemia, Sickle Cell
Text Location
Discussion

p(HGNC:HBB) increases a(HM:"oxidative reactions") View Subject | View Object

Extracellular hemoglobin and heme are pro-oxidative, proinflammatory, and cytotoxic [10–12], and can contribute to the pathology of hemolytic diseases. PubMed:26875449

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Text Location
Review

p(HGNC:HBB) positiveCorrelation a(HM:"oxidative reactions") View Subject | View Object

The second biochemical process relates to the ability of Hb to facilitate oxidative reactions outside of the reducing environment of the RBC, leading to the accumulation of ferric metHb(Fe3+) in tissue.24 PubMed:29610666

Appears in Networks:
Annotations
Cell Ontology (CL)
macrophage
MeSH
Mitochondria
Text Location
Discussion

p(HGNC:HBB) increases a(HM:"oxidative reactions") View Subject | View Object

This is a principal requirement for hemoglobin and hemin to induce adverse reactivity in tissues, including nitric oxide and oxidative reactions, release of free hemin, and molecular-signaling effects of hemin (reviewed by Schaer DJ et al.) [13] and Hill A et al. [14]. PubMed:29929138

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
Cell Ontology (CL)
neutrophil
Cell Ontology (CL)
platelet
MeSH
Hemoglobinuria, Paroxysmal
Text Location
Results

p(HGNC:HPX) decreases a(HM:"oxidative reactions") View Subject | View Object

The heme-binding protein, hemopexin, which likely prevents heme:lipid interactions and blocks the oxidative scission of heme,26 significantly inhibited the oxidative reactions. PubMed:20378845

Appears in Networks:
Annotations
Cell Ontology (CL)
endothelial cell
MeSH
Atherosclerosis
Text Location
Discussion

complex(a(CHEBI:hemin), p(HGNC:HPX)) decreases a(HM:"oxidative reactions") View Subject | View Object

Once bound to hemin, the Hpx-hemin complex prevents oxidative reactions and facilitates clearance of the complex through macrophage CD91, also referred to as lowdensity lipoprotein receptor-related protein 1. PubMed:30281034

Appears in Networks:
Annotations
Cell Ontology (CL)
erythrocyte
MeSH
Anemia, Sickle Cell
MeSH
beta-Thalassemia
Text Location
Review

p(HGNC:HP) decreases a(HM:"oxidative reactions") View Subject | View Object

Probably the most important Hp-mediated abrogation of Hb toxicity is stabilization of heme within the central cavity of the Hb subunits, which almost completely prevents its dissociation and subsequent free heme-mediated oxidative reactions and inflammatory responses. PubMed:24486321

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Text Location
Discussion

Out-Edges 2

a(HM:"oxidative reactions") positiveCorrelation a(CHEBI:heme) View Subject | View Object

Ferryl heme and associated protein radicals with high redox potentials (~1.0 V) can induce a wide variety of oxidative reactions that affect the protein and nearby molecules [2]. PubMed:24486321

Appears in Networks:
Annotations
Text Location
Discussion

a(HM:"oxidative reactions") positiveCorrelation p(HGNC:HBB) View Subject | View Object

The second biochemical process relates to the ability of Hb to facilitate oxidative reactions outside of the reducing environment of the RBC, leading to the accumulation of ferric metHb(Fe3+) in tissue.24 PubMed:29610666

Appears in Networks:
Annotations
Cell Ontology (CL)
macrophage
MeSH
Mitochondria
Text Location
Discussion

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.