PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
32254396-3	2018	The DA in the specimen would be specifically captured on the DBA-aptachip, then released from the DBA in alkaline solution to form DA-quinone (DAQ), thus leading to a color change (from colorless to brown) and inducing a dramatic decrease in the fluorescence intensity as a result of the photoinduced electron transfer (PET) for bovine serum albumin (BSA)-stabilized Au nanoclusters (BSA-Au NCs).	dopamine quinone	131-141	albumin	Bos taurus	336-349
31161325-5	2019	When DA-functionalized CuInS2/ZnS quantum dots were added to the sandwich system, TYR catalyzed the transformation of DA to dopamine quinone, which acted as an effective electron acceptor and triggered fluorescence quenching.	dopamine quinone	124-140	tyrosinase	Homo sapiens	82-85
30625605-3	2019	Dopamine quinone was produced by tyrosinase-mediated oxidation of dopamine on the surface of UCNPs, which acted as electron accepter to quench the FL emission of UCNPs.	dopamine quinone	0-16	tyrosinase	Homo sapiens	33-43
31432267-4	2019	The dopamine on the rQDs is catalytically oxidized by TYR to form dopamine quinone, and this leads to a reduction of the intensity of red fluorescence (peaking at 644 nm).	dopamine quinone	66-82	tyrosinase	Homo sapiens	54-57
30283922-3	2018	DA was easily oxidized to DA quinone under the catalysis of TYR by dissolved O2, which effectively quenched the fluorescence of the QDs.	dopamine quinone	26-36	tyrosinase	Homo sapiens	60-63
32254396-3	2018	The DA in the specimen would be specifically captured on the DBA-aptachip, then released from the DBA in alkaline solution to form DA-quinone (DAQ), thus leading to a color change (from colorless to brown) and inducing a dramatic decrease in the fluorescence intensity as a result of the photoinduced electron transfer (PET) for bovine serum albumin (BSA)-stabilized Au nanoclusters (BSA-Au NCs).	dopamine quinone	143-146	albumin	Bos taurus	336-349
26908040-7	2016	Tyrosinase, which catalyzes the oxidation of DA to DA quionone (DAQ), accelerated the inhibitory effect of DA on LPS-induced NO production.	dopamine quinone	64-67	tyrosinase	Mus musculus	0-10
27001148-4	2016	We previously demonstrated that mitochondrial Mic60 protein is susceptible to both covalent modification and loss in abundance following exposure to dopamine quinone.	dopamine quinone	149-165	inner membrane mitochondrial protein	Homo sapiens	46-51
24374372-10	2014	However, deleterious effects caused by PINK1 mutations may be alleviated by iron-chelating agents and antioxidant agents with DA quinone-conjugating capacity.	dopamine quinone	126-136	PTEN induced kinase 1	Homo sapiens	39-44
23816523-7	2013	Exposing intact rat brain mitochondria to DAQ resulted in similar decreases in GPx4 activity and monomeric protein levels as well as detection of multiple forms of DA-conjugated GPx4 protein.	dopamine quinone	42-45	glutathione peroxidase 4	Rattus norvegicus	79-83
23816523-5	2013	Here we report the findings of our studies on the effect of DA oxidation and DAQ on the mitochondrial antioxidant selenoprotein glutathione peroxidase 4 (GPx4).	dopamine quinone	77-80	glutathione peroxidase 4	Rattus norvegicus	154-158
23816523-6	2013	Purified GPx4 could be covalently modified by DAQ, and the addition of DAQ to rat testes lysate resulted in dose-dependent decreases in GPx4 activity and monomeric protein levels.	dopamine quinone	46-49	glutathione peroxidase 4	Rattus norvegicus	9-13
23816523-6	2013	Purified GPx4 could be covalently modified by DAQ, and the addition of DAQ to rat testes lysate resulted in dose-dependent decreases in GPx4 activity and monomeric protein levels.	dopamine quinone	71-74	glutathione peroxidase 4	Rattus norvegicus	9-13
23816523-6	2013	Purified GPx4 could be covalently modified by DAQ, and the addition of DAQ to rat testes lysate resulted in dose-dependent decreases in GPx4 activity and monomeric protein levels.	dopamine quinone	71-74	glutathione peroxidase 4	Rattus norvegicus	136-140
23816523-8	2013	Evidence of both GPx4 degradation and polymerization was observed following DAQ exposure.	dopamine quinone	76-79	glutathione peroxidase 4	Rattus norvegicus	17-21
21540292-6	2011	In vitro experiments using purified enzymes showed that catecholamines inhibited CPE, PC1/3, and PC2, with dopamine quinone the most potent inhibitor (IC(50) values of ~50-500 muM); dopamine, norepinephrine, and epinephrine exhibited inhibition in the micromolar range.	dopamine quinone	107-123	carboxypeptidase E	Rattus norvegicus	81-84
22720719-6	2012	Specifically, good-quality signal of dopamine and its oxidized form, dopamine o-quinone, was obtained using 10 muL of 1 muM solution of dopamine on the IDA.	dopamine quinone	69-87	latexin	Homo sapiens	120-123
22431735-6	2012	We analyzed the structural modifications induced on human DJ-1 by DAQs in vitro.	dopamine quinone	66-70	Parkinsonism associated deglycase	Homo sapiens	58-62
22431735-7	2012	We described the structural perturbations induced by DAQ adduct formation on each of the three cysteine residues of DJ-1 using specific mutants.	dopamine quinone	53-56	Parkinsonism associated deglycase	Homo sapiens	116-120
21540292-6	2011	In vitro experiments using purified enzymes showed that catecholamines inhibited CPE, PC1/3, and PC2, with dopamine quinone the most potent inhibitor (IC(50) values of ~50-500 muM); dopamine, norepinephrine, and epinephrine exhibited inhibition in the micromolar range.	dopamine quinone	107-123	proprotein convertase subtilisin/kexin type 2	Rattus norvegicus	97-100
21540292-7	2011	The inhibition of purified CPE with catecholamines was time-dependent and, for dopamine quinone, dilution-independent, suggesting covalent modification of the protein by the catecholamine.	dopamine quinone	79-95	carboxypeptidase E	Rattus norvegicus	27-30
20309679-6	2010	We propose on the basis of these and earlier data that oxidation of the four methionine residues at the C- and N-terminal ends of alpha-syn molecules prevents their end-to-end association and stabilises oligomers formed by cross linking with DA-quinone/DA-melanin, which are formed as a result of the redox process, thus inhibiting formation of the beta-sheet structure found in other pre-fibrillar forms of alpha-syn.	dopamine quinone	242-252	synuclein alpha	Homo sapiens	130-139
18226537-6	2008	Western blot analyses for mitochondrial creatine kinase and mitofilin confirmed significant losses in isolated brain mitochondria exposed to dopamine quinone and PC12 cells exposed to dopamine.	dopamine quinone	141-157	inner membrane mitochondrial protein	Rattus norvegicus	60-69
18455424-2	2008	Because oxidative stress caused by dopamine oxidation to dopamine quinone is suggested as a major factor contributing to the pathogenesis of PD, the induction of the enzyme that catalyzes the reduction of quinones, NAD(P)H quinone oxidoreductase1 (NQO1), could be a desirable therapeutic strategy to protect cells from oxidative damage.	dopamine quinone	57-73	NAD(P)H quinone dehydrogenase 1	Rattus norvegicus	215-246
18455424-2	2008	Because oxidative stress caused by dopamine oxidation to dopamine quinone is suggested as a major factor contributing to the pathogenesis of PD, the induction of the enzyme that catalyzes the reduction of quinones, NAD(P)H quinone oxidoreductase1 (NQO1), could be a desirable therapeutic strategy to protect cells from oxidative damage.	dopamine quinone	57-73	NAD(P)H quinone dehydrogenase 1	Rattus norvegicus	248-252
20226175-0	2010	Dopamine quinones interact with alpha-synuclein to form unstructured adducts.	dopamine quinone	0-17	synuclein alpha	Homo sapiens	32-47
17910954-2	2007	Here, we examined the effects of cysteine-rich metal-binding proteins, metallothionein (MT)-1 and -2, on DA quinone-induced neurotoxicity.	dopamine quinone	105-115	metallothionein 1	Mus musculus	71-100
18022268-1	2008	The neurotoxicity of dopamine (DA) quinones as dopaminergic neuron-specific oxidative stress is considered to play a role in the pathogenesis and/or progression of Parkinson"s disease (PD), since DA quinones conjugate with several key PD pathogenic molecules (e.g., tyrosine hydroxylase, alpha-synuclein and parkin) to form protein-bound quinone (quinoprotein) and consequently inhibit their functions.	dopamine quinone	196-207	synuclein, alpha	Mus musculus	288-303
17394461-7	2007	Dopamine-induced Nrf2 activity in both cell types by generating oxidative stressors, H2O2 and dopamine-quinones.	dopamine quinone	94-111	nuclear factor, erythroid derived 2, like 2	Mus musculus	17-21
16403784-6	2006	We also showed the protective effect of tyrosinase, which rapidly oxidizes DA and DA quinone to form stable melanin, against METH-induced dopaminergic neurotoxicity in vitro and in vivo using tyrosinase null mice.	dopamine quinone	82-92	tyrosinase	Mus musculus	40-50
16978807-1	2006	NAD(P)H quinone oxidoreductase 1 (NQO1) can metabolize dopamine-derived quinones (DAQ) and absence of NQO1 due to the NQO1*2 polymorphism has been suggested to be a risk factor for Parkinson"s disease.	dopamine quinone	82-85	NAD(P)H quinone dehydrogenase 1	Homo sapiens	0-32
16978807-1	2006	NAD(P)H quinone oxidoreductase 1 (NQO1) can metabolize dopamine-derived quinones (DAQ) and absence of NQO1 due to the NQO1*2 polymorphism has been suggested to be a risk factor for Parkinson"s disease.	dopamine quinone	82-85	NAD(P)H quinone dehydrogenase 1	Homo sapiens	34-38
16403784-2	2006	In the present study, we examined DA quinone formation in methamphetamine (METH)-induced dopaminergic neuronal cell death using METH-treated dopaminergic cultured CATH.a cells and METH-injected mouse brain.	dopamine quinone	34-44	cathepsin H	Mus musculus	163-167
8405659-2	1993	The oxidation of 3,4-dihydroxyphenylethylamine (dopamine) by O2 catalyzed by tyrosinase yields 4-(2-aminoethyl)-1,2-benzoquinone, with its amino group protonated (o-dopaminequinone-H+), which evolves non-enzymatically through two branches or sequences of reactions, whose respective operations are determined by the pH of the medium.	dopamine quinone	95-128	tyrosinase	Homo sapiens	77-87
15718289-12	2005	Instead, the peroxidase activity associated with COX-2, which can lead to the formation of reactive oxygen species and dopamine quinones, can account for its role.	dopamine quinone	119-136	prostaglandin-endoperoxide synthase 2	Mus musculus	49-54
15312971-3	2004	In this respect, the inducible flavoprotein NAD(P)H:quinone oxidoreductase (NQO1) is of particular interest as it is directly implicated in the detoxication of DA-quinones and, in addition, has broad spectrum anti-oxidant properties.	dopamine quinone	160-171	crystallin zeta	Homo sapiens	52-74
15312971-3	2004	In this respect, the inducible flavoprotein NAD(P)H:quinone oxidoreductase (NQO1) is of particular interest as it is directly implicated in the detoxication of DA-quinones and, in addition, has broad spectrum anti-oxidant properties.	dopamine quinone	160-171	NAD(P)H quinone dehydrogenase 1	Homo sapiens	76-80
12835121-6	2003	For example, the formation of DA quinone-alpha-synuclein consequently increases cytotoxic protofibrils and the covalent modification of tyrosine hydroxylase by DA quinones.	dopamine quinone	30-40	synuclein alpha	Homo sapiens	41-56
12835121-6	2003	For example, the formation of DA quinone-alpha-synuclein consequently increases cytotoxic protofibrils and the covalent modification of tyrosine hydroxylase by DA quinones.	dopamine quinone	160-171	synuclein alpha	Homo sapiens	41-56
15462376-7	2004	For example, the formation of DA quinone-alpha-synuclein complex consequently increases cytotoxic protofibrils and covalent modification of functional enzymes.	dopamine quinone	30-40	synuclein alpha	Homo sapiens	41-56
11181843-4	2001	DAQ reactivity was inferred from its effects on the binding of [(3)H]2-beta-carbomethoxy-3-beta-(4-fluorophenyl)tropane (beta-CFT) to hDAT cysteine mutant constructs.	dopamine quinone	0-3	solute carrier family 6 member 3	Homo sapiens	134-138
9843160-5	1998	The present studies demonstrated that dopamine quinone, the formation of which was enhanced through the activity of the melanin biosynthetic enzyme, tyrosinase, covalently modified and inactivated tyrosine hydroxylase.	dopamine quinone	38-54	tyrosinase	Homo sapiens	149-159
9659366-0	1998	Metabolic activation of dopamine o-quinones to o-semiquinones by NADPH cytochrome P450 reductase may play an important role in oxidative stress and apoptotic effects.	dopamine quinone	24-43	cytochrome p450 oxidoreductase	Homo sapiens	65-96
9659366-1	1998	In this study, it is shown that considerable evidence for the possible pathway by which dopamine o-quinone, o-quinone and aminochrome can be activated metabolically by NADPH cytochrome P450 reductase to high reactive semiquinones.	dopamine quinone	88-106	cytochrome p450 oxidoreductase	Homo sapiens	168-199
8915597-3	1996	The conversion of dopamine to reactive dopamine quinone is accelerated by the enzyme tyrosinase.	dopamine quinone	39-55	tyrosinase	Homo sapiens	85-95
22723845-6	2012	Using radioactive DA, we demonstrated that SOD2 is a target of DAQs.	dopamine quinone	63-67	superoxide dismutase 2	Homo sapiens	43-47
1910309-1	1991	The oxidation of 3,4-dihydroxyphenylethylamine (dopamine) by O2 catalyzed by tyrosinase yields 4-(2-aminoethyl)-1, 2-benzoquinone (o-dopaminequinone), which evolves nonenzymatically through two branches or sequences of reactions, whose respective operations are determined by the pH of the medium.	dopamine quinone	95-129	tyrosinase	Homo sapiens	77-87
22723845-7	2012	Exposure to micromolar DAQ concentrations induces a loss of up to 50% of SOD2 enzymatic activity in a dose-dependent manner, which is correlated to the concomitant formation of protein aggregates, while the coordination geometry of the active site appears unaffected by DAQ modifications.	dopamine quinone	23-26	superoxide dismutase 2	Homo sapiens	73-77
22723845-7	2012	Exposure to micromolar DAQ concentrations induces a loss of up to 50% of SOD2 enzymatic activity in a dose-dependent manner, which is correlated to the concomitant formation of protein aggregates, while the coordination geometry of the active site appears unaffected by DAQ modifications.	dopamine quinone	270-273	superoxide dismutase 2	Homo sapiens	73-77
22723845-8	2012	Our findings support a model in which DAQ-mediated SOD2 inactivation increases mitochondrial ROS production, suggesting a link between oxidative stress and mitochondrial dysfunction.	dopamine quinone	38-41	superoxide dismutase 2	Homo sapiens	51-55
32538547-6	2020	RESULTS: DA modifies alpha-syn with the addition of dopamine-quinone (DAQ) into lysine sites of alpha-syn in vitro and the addition of DAQ and DOPAL (3,4-dihydroxyphenylacetaldehyde) in plasma samples.	dopamine quinone	70-73	synuclein alpha	Homo sapiens	21-30
35456994-5	2022	DA in cytoplasm is highly reactive and is assumed to be oxidized spontaneously or by an unidentified tyrosinase to DAQ and then, synthesized to NM.	dopamine quinone	115-118	tyrosinase	Homo sapiens	101-111
32538547-6	2020	RESULTS: DA modifies alpha-syn with the addition of dopamine-quinone (DAQ) into lysine sites of alpha-syn in vitro and the addition of DAQ and DOPAL (3,4-dihydroxyphenylacetaldehyde) in plasma samples.	dopamine quinone	70-73	synuclein alpha	Homo sapiens	96-105