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

Appears in Networks 4

Nicotinic receptors: allosteric transitions and therapeutic targets in the nervous system v1.0.0

This document contains the curation of the review article Nicotinic receptors: allosteric transitions and therapeutic targets in the nervous system by Taly et al. 2009

TAU and Interaction Partners v1.2.5

TAU Interactions Section of NESTOR

Heme Curation v0.0.1-dev

Mechanistic knowledge surrounding heme

In-Edges 3

a(CHEBI:"N,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamine") decreases act(a(CHEBI:"zinc(2+)")) View Subject | View Object

TPEN (20 mM), a chelator for Zn2þ, Fe2þ and Mn2þ, abolished the effects of Zn2þ (Fig. 1A). PubMed:29544683

Appears in Networks:
Annotations
MeSH
Erythrocyte Membrane
MeSH
Sepsis
Text Location
Results

a(CHEBI:"N,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamine") decreases act(a(CHEBI:"zinc(2+)")) View Subject | View Object

The Zn2þ (20 mM)-induced expression of PS on erythrocytes, which was inhibited by TPEN, was not observed by other divalent cations, including Mg2þ and Ca2þ (Fig. 2A). PubMed:29544683

Appears in Networks:
Annotations
MeSH
Erythrocyte Membrane
MeSH
Sepsis
Text Location
Results

bp(MESH:"Platelet Activation") increases a(CHEBI:"zinc(2+)") View Subject | View Object

The cascade of immunothrombosis includes platelet activation and secretion, which may result in a local increase in Zn2þ concentration because of the presence of Zn2þ in platelet dense granules. PubMed:29544683

Appears in Networks:
Annotations
MeSH
Erythrocyte Membrane
MeSH
Sepsis
Text Location
Results

Out-Edges 8

a(CHEBI:"zinc(2+)") increases act(p(MESH:"Receptors, Nicotinic")) View Subject | View Object

One group of modulators includes Ca2+􏰆, which potentiates most neuronal nAChRs (99, 100) and binds to the extracellular domain below the ACh site at residues contributed from both sides of the subunit interface (96). Another includes Zn2 􏰆 . PubMed:23038257

a(CHEBI:"zinc(2+)") decreases act(p(HBP:"alpha-4 beta-2 nAChR")) View Subject | View Object

in parallel, a voltage-dependent inhibitory Zn2+-binding site has been identified within the beta2 subunit of the alpha4beta2 nAChR48. PubMed:19721446

a(CHEBI:"zinc(2+)") increases act(p(HGNC:S100B)) View Subject | View Object

We here confirmed the interaction of SlOOb with tau through affinity chromatography and crosslinking and demonstrated that such an interaction also inhibited mode I phosphorylation by a Ca2+/CaM-dependent kinase. Increasing Ca2+c oncentration to the 100 μM range potentiated the SlOOb effect. Therefore, although Ca2+-independent interactions may occur between SlOOb and protein tau, it is the Ca2+ form of SlOOb that has significant affinity for protein tau. In any case, Znz+ and Ca2+ both appear to be capabble of inducing a conformation in SlOOb that promotes its binding to target proteinins, including tau. PubMed:2833519

a(CHEBI:"zinc(2+)") increases bp(MESH:"Erythrocyte Aggregation") View Subject | View Object

Stimulation with 20 mM Zn2þ resulted in aggregation of washed human erythrocytes 1 h after incubation. PubMed:29544683

Appears in Networks:
Annotations
MeSH
Erythrocyte Membrane
MeSH
Sepsis
Text Location
Results

a(CHEBI:"zinc(2+)") increases bp(MESH:"Erythrocyte Aggregation") View Subject | View Object

Thus focusing on Zn2þ-stimulated erythrocytes might be an important new approach that could ultimately reveal the mechanism of immunothrombus formation in sepsis. PubMed:29544683

Appears in Networks:
Annotations
MeSH
Erythrocyte Membrane
MeSH
Sepsis
Text Location
Results

a(CHEBI:"zinc(2+)") increases a(CHEBI:"phosphatidyl-L-serine") View Subject | View Object

The Zn2þ (20 mM)-induced expression of PS on erythrocytes, which was inhibited by TPEN, was not observed by other divalent cations, including Mg2þ and Ca2þ (Fig. 2A). PubMed:29544683

Appears in Networks:
Annotations
MeSH
Erythrocyte Membrane
MeSH
Sepsis
Text Location
Results

a(CHEBI:"zinc(2+)") increases a(HM:"erythrocyte-endothelium adhesion") View Subject | View Object

We found that a considerable number of erythrocytes were attached to the EA.hy926 cells after Zn2þ-stimulation (Fig. 4A). PubMed:29544683

Appears in Networks:
Annotations
MeSH
Erythrocyte Membrane
MeSH
Sepsis
Text Location
Results

a(CHEBI:"zinc(2+)") increases a(HM:"erythrocyte-endothelium adhesion") View Subject | View Object

In addition, we observed that Zn2þ induced the adhesion of erythrocytes to endothelial cells, and this effect was not inhibited by 100 mg/mL of HSA (Fig. 4), suggesting a specific interaction between erythrocytes and HRG. PubMed:29544683

Appears in Networks:
Annotations
MeSH
Erythrocyte Membrane
MeSH
Sepsis
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.