count	source_label	source_id	relationship	target_label	target_id	entity_type	solr_id	publication_id	sentences
8	HBQ1	UNIPROT:P09105	activates		MESH:D004249	Phenotype	59642b70-374e-11e8-9fbf-001a4a160176	28774615	This is consistent with the known mechanisms of HBQ-induced cytotoxicity, as studies have shown that HBQ exposure results in the formation of reactive oxygen species and causes oxidative DNA damage in cells (Du et al., 2013; Li et al., 2014, 2016).
6	HBQ1	UNIPROT:P09105	inhibits		CHEBI:37613	Chemical	3f87af78-1bf4-11f0-a2ca-0050569a1f61	10.1016/j.scitotenv.2023.169860	Identification of HBQ products in ozonated 2,3-DCP As proven in our previous research, Na2SO3(S(IV)) and NaBH4can reduce HBQs to form sulfonated cyclohexadiene-1-one and cyclohexadiene, respectively (Wei et al., 2023).|||Identification of HBQ products and their risk assessment As proven in our previous research, Na2SO3(S(IV)) and NaBH4can reduce HBQs to form sulfonated cyclohexadiene-1-one and cyclohexadiene, respectively (Wei et al., 2023).
4	HBQ1	UNIPROT:P09105	activates		UNIPROT:Q96C86	Protein	3f87af78-1bf4-11f0-a2ca-0050569a1f61	10.1016/j.scitotenv.2023.169860	Based on this, chlorinated HBQ compounds are potentially causing increased toxicity in the ozonated DCPs.
4	HBQ1	UNIPROT:P09105	activates		MESH:D017382	Phenotype	59642b70-374e-11e8-9fbf-001a4a160176	28774615	This is consistent with the known mechanisms of HBQ-induced cytotoxicity, as studies have shown that HBQ exposure results in the formation of reactive oxygen species and causes oxidative DNA damage in cells (Du et al., 2013; Li et al., 2014, 2016).
4	HBQ1	UNIPROT:P09105	activates		GO:0097484	Phenotype	a601bb5e-452a-11f0-afc2-0050569a791b	10.1016/j.jes.2022.03.042	The aberrant expression of thegfapandα1-tubulingenes suggests that HBQ exposure leads to impaired axon and dendrite extension in zebrafish neuronal cells, which in turn leads to poor neurotransmitter formation and release.
4	HBQ1	UNIPROT:P09105	activates		PF:PF04886	ProteinFamily	ec1c1b2a-4728-11f0-8978-0050569a1f61	10.1016/j.comptc.2017.05.008	N distances of IPDO and IPRO derivatives are found to be longer than that of HBQ which might cause the higher PT barrier.
2	HBQ1	UNIPROT:P09105	activates		UNIPROT:P22303	Protein	a601bb5e-452a-11f0-afc2-0050569a791b	10.1016/j.jes.2022.03.042	Effect of HBQ exposure on the levels of neurotransmitters in zebrafish embryos The changes in the early spontaneous movement of embryos (Fig. 1) and locomotor performance of larvae (Fig. 2) led us to examine the effects of HBQ exposure on neurotransmitters.Figure 3and Appendix A Table S4 present the levels of two neurotransmitters, dopamine (DA) and gamma-aminobutyric acid (GABA), and acetylcholinesterase (AchE) after HBQ exposure.
2	HBQ1	UNIPROT:P09105	activates		UNIPROT:P08922	Protein	a601bb5e-452a-11f0-afc2-0050569a791b	10.1016/j.jes.2022.03.042	HBQ exposure activates reactive oxygen species (ROS), resulting in a variety of oxidative damage (Duet al., 2013;Liet al., 2018;Louet al., 2019;Wanget al., 2018), such as peroxidation of neurolipids, which results in neurotoxic effects (Al Olayanet al., 2020;Garza-Lomboet al., 2018;Shawet al., 2020;Wuet al., 2012).
2	HBQ1	UNIPROT:P09105	activates		CHEBI:49470	Chemical	a601bb5e-452a-11f0-afc2-0050569a791b	10.1016/j.jes.2022.03.042	HBQ exposure activates reactive oxygen species (ROS), resulting in a variety of oxidative damage (Duet al., 2013;Liet al., 2018;Louet al., 2019;Wanget al., 2018), such as peroxidation of neurolipids, which results in neurotoxic effects (Al Olayanet al., 2020;Garza-Lomboet al., 2018;Shawet al., 2020;Wuet al., 2012).
2	HBQ1	UNIPROT:P09105	activates		MESH:D005978	Phenotype	59642b70-374e-11e8-9fbf-001a4a160176	28774615	Furthermore, the depletion of cellular glutathione (GSH) was found to sensitize cells to HBQs, and extracellular GSH supplementation could reduce HBQ-induced cytotoxicity, emphasizing the role of GSH-mediated and GSH-related enzyme-mediated detoxification of HBQs (Li et al., 2014).
2	HBQ1	UNIPROT:P09105	activates		MESH:D005680	Phenotype	a601bb5e-452a-11f0-afc2-0050569a791b	10.1016/j.jes.2022.03.042	Effect of HBQ exposure on the levels of neurotransmitters in zebrafish embryos The changes in the early spontaneous movement of embryos (Fig. 1) and locomotor performance of larvae (Fig. 2) led us to examine the effects of HBQ exposure on neurotransmitters.Figure 3and Appendix A Table S4 present the levels of two neurotransmitters, dopamine (DA) and gamma-aminobutyric acid (GABA), and acetylcholinesterase (AchE) after HBQ exposure.
2	HBQ1	UNIPROT:P09105	activates		MESH:D017382	Phenotype	a601bb5e-452a-11f0-afc2-0050569a791b	10.1016/j.jes.2022.03.042	HBQ exposure activates reactive oxygen species (ROS), resulting in a variety of oxidative damage (Duet al., 2013;Liet al., 2018;Louet al., 2019;Wanget al., 2018), such as peroxidation of neurolipids, which results in neurotoxic effects (Al Olayanet al., 2020;Garza-Lomboet al., 2018;Shawet al., 2020;Wuet al., 2012).
2	HBQ1	UNIPROT:P09105	activates		MESH:D004298	Phenotype	a601bb5e-452a-11f0-afc2-0050569a791b	10.1016/j.jes.2022.03.042	Effect of HBQ exposure on the levels of neurotransmitters in zebrafish embryos The changes in the early spontaneous movement of embryos (Fig. 1) and locomotor performance of larvae (Fig. 2) led us to examine the effects of HBQ exposure on neurotransmitters.Figure 3and Appendix A Table S4 present the levels of two neurotransmitters, dopamine (DA) and gamma-aminobutyric acid (GABA), and acetylcholinesterase (AchE) after HBQ exposure.
2		MESH:D005978	inhibits	HBQ1	UNIPROT:P09105	Phenotype	59642b70-374e-11e8-9fbf-001a4a160176	28774615	Furthermore, the depletion of cellular glutathione (GSH) was found to sensitize cells to HBQs, and extracellular GSH supplementation could reduce HBQ-induced cytotoxicity, emphasizing the role of GSH-mediated and GSH-related enzyme-mediated detoxification of HBQs (Li et al., 2014).
1	HBQ1	UNIPROT:P09105	activates		UNIPROT:P16104	Protein	6c1b1912-c687-11ee-b346-0050569a791b	10.1016/j.envint.2023.108407	At each exposure time, γH2AX induced by each HBQ was statistically higher than their concurrent negative control (P< 0.05).
1	HBQ1	UNIPROT:P09105	decreases		UNIPROT:P02008	Protein	1def4dac-3327-11e8-aa95-001a4a160176	PMC5891078	Nevertheless, within a whole blood eQTL study of up to 5,311 individual adults[36,37], we identified genome-wide significant associations for the rs11865131-A allele with decreased expression of the functional embryonic ζ-globin gene (HBZ), increased expression of the canonically non-functional θ-globin gene (HBQ1), and decreased expression for 2 proximal non-globin genes,NPRL3andSNRNP2(Fig 1A), all of which are highly expressed in cultured adult erythroblasts[38].
1	HBQ1	UNIPROT:P09105	activates		UNIPROT:P08922	Protein	252dd5c6-c9d9-11ee-9133-0050569a1f61	10.1016/j.chemosphere.2022.136763	This finding is consistent with our previous study that dipole moment was correlated with cytotoxicity and ROS production induced by HBQ isomers (Li et al., 2016).
1	HBQ1	UNIPROT:P09105	activates		GO:0098754	Phenotype	b424bd58-c46a-11e5-8491-001a4ae51247	24812012	"Taken together, GSH depletion enhanced the cytotoxicity of HBQs and GSH supplementation attenuated the HBQ-induced cytotoxicity
                            in T24 cells, supporting the hypothesis that GSH plays one of the key roles in detoxification of HBQs."
1	HBQ1	UNIPROT:P09105	activates		MESH:D051379	Phenotype	b424bd58-c46a-11e5-8491-001a4ae51247	24812012	"The protection of extracellular GSH against HBQ-cytotoxicity is consistent with our previous result that N-acetylcysteine
                      (NAC) treatment prevents HBQ-induced cytotoxic effects (Duet al.,2013), and also consistent with other findings that exogenous GSH can protect cells and mice from toxicity (Hagenet al.,1986; Jinet al.,2010; Lashet al.,1986)."
1		FPLX:GATA	inhibits	HBQ1	UNIPROT:P09105	ProteinFamily	98578c10-7478-11ee-9572-0050569a1f61	10.1007/s00204-023-03541-0	The chromatin occupancy of GATA factors at erythroid gene clusters in HQ-exposed K562 cells The results of ChIP-seq indicated that HQ decreased the GATA1 occupancy atHBG1,HBQ1,HBA1, andHBD, whereas increased the GATA2 occupancy atHBB,HBM,HBP1, andHBG2(Fig.6a).
1		MESH:D011809	activates	HBQ1	UNIPROT:P09105	Phenotype	d063436e-c464-11e5-9da3-001a4ae51247	PMC3789946	The resulting HBQ is enzymatically reduced to hydroxyhydroquinone by a quinone reductase and then to β-ketoadipate by TftH and TftE, respectively (4).
1		UNIPROT:Q45072	inhibits	HBQ1	UNIPROT:P09105	Protein	d063436e-c464-11e5-9da3-001a4ae51247	PMC3789946	The resulting HBQ is enzymatically reduced to hydroxyhydroquinone by a quinone reductase and then to β-ketoadipate by TftH and TftE, respectively (4).