PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
16838953-2	2005	The calculated dissociation energies of the HOF-SO(3), HOCl-SO(3), and HOBr-SO(3) complexes are 5.43, 6.02, and 5.98 kcal mol(-1) at MP2/6-311++G(3df,3pd) level, respectively.	hypobromous acid	71-75	tryptase pseudogene 1	Homo sapiens	133-136
16300375-0	2005	The role of aromatic amino acid oxidation, protein unfolding, and aggregation in the hypobromous acid-induced inactivation of trypsin inhibitor and lysozyme.	hypobromous acid	85-101	kunitz trypsin protease inhibitor	Glycine max	126-143
11425491-5	2001	Compared to HOCl, HOBr caused 2-3-fold greater oxidation of tryptophan and cysteine residues of the protein moiety (apoB) of LDL and 4-fold greater formation of fatty acid halohydrins from the lipids in LDL.	hypobromous acid	18-22	apolipoprotein B	Homo sapiens	116-120
15260531-1	2004	The potential energy surface (PES) for the HOBr.H(2)O complex has been investigated using second- and fourth-order Moller-Plesset perturbation theory (MP2, MP4) and coupled cluster theory with single and doubles excitations (CCSD), and a perturbative approximation of triple excitations (CCSD-T), correlated ab initio levels of theory employing basis sets of triple zeta quality with polarization and diffuse functions up to the 6-311++G(3dp,3df ) standard Pople"s basis set.	hypobromous acid	43-47	tryptase pseudogene 1	Homo sapiens	151-154
15260531-5	2004	The CCSD-T/6-311++G(3df,3pd)//MP2/6-311G(d,p) barrier for the syn<-->anti interconversion is 0.3 kcal mol(-1), indicating that a mixture of the syn and anti forms of the HOBr.H(2)O complex is likely to exist.	hypobromous acid	176-180	tryptase pseudogene 1	Homo sapiens	30-33
15260531-5	2004	The CCSD-T/6-311++G(3df,3pd)//MP2/6-311G(d,p) barrier for the syn<-->anti interconversion is 0.3 kcal mol(-1), indicating that a mixture of the syn and anti forms of the HOBr.H(2)O complex is likely to exist.	hypobromous acid	176-180	synemin	Homo sapiens	62-65
15260531-5	2004	The CCSD-T/6-311++G(3df,3pd)//MP2/6-311G(d,p) barrier for the syn<-->anti interconversion is 0.3 kcal mol(-1), indicating that a mixture of the syn and anti forms of the HOBr.H(2)O complex is likely to exist.	hypobromous acid	176-180	synemin	Homo sapiens	150-153
12208372-11	2002	We conclude that eosinophil peroxidase produces substantial amounts of hypobromous acid in the airways of stable asthmatics.	hypobromous acid	71-87	eosinophil peroxidase	Homo sapiens	17-38
11697850-1	2001	Activated leukocytes generate the potent oxidants HOCl and HOBr via the formation of H(2)O(2) and the release of peroxidase enzymes (myeloperoxidase, eosinophil peroxidase).	hypobromous acid	59-63	myeloperoxidase	Homo sapiens	133-148
11697850-1	2001	Activated leukocytes generate the potent oxidants HOCl and HOBr via the formation of H(2)O(2) and the release of peroxidase enzymes (myeloperoxidase, eosinophil peroxidase).	hypobromous acid	59-63	eosinophil peroxidase	Homo sapiens	150-171
15364942-3	2004	Leukocyte-derived peroxidases, such as myeloperoxidase and eosinophil peroxidase, use hydrogen peroxide and halides (Cl- and Br-) to generate hypohalous acids (HOCl and HOBr), halogenating intermediates.	hypobromous acid	169-173	myeloperoxidase	Mus musculus	39-54
15364942-3	2004	Leukocyte-derived peroxidases, such as myeloperoxidase and eosinophil peroxidase, use hydrogen peroxide and halides (Cl- and Br-) to generate hypohalous acids (HOCl and HOBr), halogenating intermediates.	hypobromous acid	169-173	eosinophil peroxidase	Mus musculus	59-80
12208372-0	2002	Eosinophil peroxidase produces hypobromous acid in the airways of stable asthmatics.	hypobromous acid	31-47	eosinophil peroxidase	Homo sapiens	0-21
12208372-1	2002	Eosinophil peroxidase and myeloperoxidase use hydrogen peroxide to produce hypobromous acid and hypochlorous acid.	hypobromous acid	75-91	eosinophil peroxidase	Homo sapiens	0-21
12208372-1	2002	Eosinophil peroxidase and myeloperoxidase use hydrogen peroxide to produce hypobromous acid and hypochlorous acid.	hypobromous acid	75-91	myeloperoxidase	Homo sapiens	26-41
12071050-4	2002	Myeloperoxidase easily oxidizes thiocyanate to hypothiocyanate and Br- to HOBr, which are involved in protective reactions.	hypobromous acid	74-78	myeloperoxidase	Homo sapiens	0-15
11485572-11	2001	We conclude that at plasma concentrations of bromide (20-120 microM) and thiocyanate (20-100 microM), hypobromous acid and oxidation products of thiocyanate are produced by eosinophil peroxidase.	hypobromous acid	102-118	eosinophil peroxidase	Homo sapiens	173-194
11425491-8	2001	Similar apoB modifications were observed with HOBr generated by MPO/H(2)O(2)/Br(-).	hypobromous acid	46-50	apolipoprotein B	Homo sapiens	8-12
11425491-8	2001	Similar apoB modifications were observed with HOBr generated by MPO/H(2)O(2)/Br(-).	hypobromous acid	46-50	myeloperoxidase	Homo sapiens	64-67
11096071-5	2001	In contrast, eosinophil peroxidase preferentially converts Br(-) to HOBr.	hypobromous acid	68-72	eosinophil peroxidase	Homo sapiens	13-34
11432558-10	2001	pH depression shifts the HOBr/ OBr- equilibrium to HOBr and also affects the ozone chemistry.	hypobromous acid	51-55	leptin receptor	Homo sapiens	26-29
10090740-13	1999	They also suggest that in biological mixtures where amine groups are abundant, the trapping of EPO-generated HOBr/OBr- as N-bromoamines will serve to effectively "funnel" reactive brominating equivalents to stable ring-brominated forms of tyrosine.	hypobromous acid	109-113	eosinophil peroxidase	Homo sapiens	95-98
11329272-7	2001	Eosinophil peroxidase required H(2)O(2) and Br(-) to produce 5-bromouracil, implicating HOBr as an intermediate in the reaction.	hypobromous acid	88-92	eosinophil peroxidase	Homo sapiens	0-21
11329272-11	2001	Collectively, these results indicate that HOBr generated by eosinophil peroxidase oxidizes uracil to 5-bromouracil.	hypobromous acid	42-46	eosinophil peroxidase	Homo sapiens	60-81
11172002-2	2001	Eosinophil peroxidase, a heme enzyme released by eosinophils, generates hypobromous acid that damages tissue in inflammatory conditions.	hypobromous acid	72-88	eosinophil peroxidase	Homo sapiens	0-21
10866624-6	2000	Additions of HOBr, HOCl, and DMTSF to highly functionalized substrates proceed predictably with syn selectivity, giving predominantly or exclusively one product.	hypobromous acid	13-17	synemin	Homo sapiens	96-99
11329272-1	2001	Eosinophils use eosinophil peroxidase, hydrogen peroxide (H(2)O(2)), and bromide ion (Br(-)) to generate hypobromous acid (HOBr), a brominating intermediate.	hypobromous acid	105-121	eosinophil peroxidase	Homo sapiens	16-37
11329272-1	2001	Eosinophils use eosinophil peroxidase, hydrogen peroxide (H(2)O(2)), and bromide ion (Br(-)) to generate hypobromous acid (HOBr), a brominating intermediate.	hypobromous acid	123-127	eosinophil peroxidase	Homo sapiens	16-37
11329272-3	2001	In this study, we explore the possibility that HOBr generated by eosinophil peroxidase might oxidize nucleic acids.	hypobromous acid	47-51	eosinophil peroxidase	Homo sapiens	65-86
10452808-5	1999	The MPO-specific reaction is believed to proceed in two steps: (i) the enzymatic generation of hypobromous acid (HOBr) from KBr and H(2)O(2) at pH 5 and (ii) the spontaneous reaction of HOBr and H(2)O(2) with luminol to give a Br-CL signal.	hypobromous acid	95-111	myeloperoxidase	Homo sapiens	4-7
10452808-5	1999	The MPO-specific reaction is believed to proceed in two steps: (i) the enzymatic generation of hypobromous acid (HOBr) from KBr and H(2)O(2) at pH 5 and (ii) the spontaneous reaction of HOBr and H(2)O(2) with luminol to give a Br-CL signal.	hypobromous acid	113-117	myeloperoxidase	Homo sapiens	4-7
10452808-5	1999	The MPO-specific reaction is believed to proceed in two steps: (i) the enzymatic generation of hypobromous acid (HOBr) from KBr and H(2)O(2) at pH 5 and (ii) the spontaneous reaction of HOBr and H(2)O(2) with luminol to give a Br-CL signal.	hypobromous acid	186-190	myeloperoxidase	Homo sapiens	4-7
10452808-8	1999	Although EPX can also oxidize bromide to generate HOBr, activities of MPO and EPX can be distinguished at different pHs.	hypobromous acid	50-54	eosinophil peroxidase	Homo sapiens	9-12
1667454-2	1991	The chemiluminescence method was based on the detection of 1O2 generated by myeloperoxidase-catalyzed HOBr formation followed by the interaction of HOBr with H2O2 at pH 4.5.	hypobromous acid	102-106	myeloperoxidase	Homo sapiens	76-91
8619607-1	1996	Eosinophil peroxidase and myeloperoxidase (MPO) catalyze the oxidation of bromide by hydrogen peroxide to produce hypobromous acid (HOBr).	hypobromous acid	132-136	myeloperoxidase	Homo sapiens	26-41
8619607-1	1996	Eosinophil peroxidase and myeloperoxidase (MPO) catalyze the oxidation of bromide by hydrogen peroxide to produce hypobromous acid (HOBr).	hypobromous acid	132-136	myeloperoxidase	Homo sapiens	43-46
8619607-3	1996	In this study the equivalent reaction of HOBr, produced from MPO, bromide, and hydrogen peroxide, with oleic (18:1), linoleic (18:2), and arachidonic (20:4) acids has been investigated.	hypobromous acid	41-45	myeloperoxidase	Homo sapiens	61-64
8860070-3	1996	EPO in the presence of hydrogen peroxide (H(2)O(2)) and bromide (Br(-)) catalyzes the production of hypobromous acid (HOBr), which is felt to have a toxic effect on airway epithelial cells.	hypobromous acid	100-116	eosinophil peroxidase	Cavia porcellus	0-3
8860070-3	1996	EPO in the presence of hydrogen peroxide (H(2)O(2)) and bromide (Br(-)) catalyzes the production of hypobromous acid (HOBr), which is felt to have a toxic effect on airway epithelial cells.	hypobromous acid	118-122	eosinophil peroxidase	Cavia porcellus	0-3
7852368-3	1995	Results were consistent with oxidation of bromide to an equilibrium mixture of hypobromous acid (HOBr) and hypobromite ion (OBr-).	hypobromous acid	79-95	leptin receptor	Homo sapiens	98-101
15104210-5	2004	Hypobromous acid is likely a short-lived intermediate in this H2O2/MPO/bromide apoptosis, and reagent hypobromous acid and bromamines induce apoptosis in HL-60 cells.	hypobromous acid	0-16	myeloperoxidase	Homo sapiens	67-70
2002037-2	1991	The potent cytotoxic capacity of eosinophils for parasites and host tissue has in part been attributed to the catalytic action of eosinophil peroxidase (EPO), which preferentially oxidizes Br- to the powerful bleaching oxidant HOBr in buffers that mimic serum halide composition (100 mM Cl-, 20-100 microM Br-, less than 1 microM I-).	hypobromous acid	227-231	eosinophil peroxidase	Rattus norvegicus	130-151
2002037-2	1991	The potent cytotoxic capacity of eosinophils for parasites and host tissue has in part been attributed to the catalytic action of eosinophil peroxidase (EPO), which preferentially oxidizes Br- to the powerful bleaching oxidant HOBr in buffers that mimic serum halide composition (100 mM Cl-, 20-100 microM Br-, less than 1 microM I-).	hypobromous acid	227-231	eosinophil peroxidase	Rattus norvegicus	153-156
1972179-5	1990	EOs adherent to FCS-coated plastic wells more than double their production of superoxide anion and the cytotoxic EPO-derived oxidant HOBr when exposed to TNF, showing that TNF activates the respiratory burst of EOs attached to a "physiologic" surface.	hypobromous acid	133-137	tumor necrosis factor	Homo sapiens	154-157
1972179-5	1990	EOs adherent to FCS-coated plastic wells more than double their production of superoxide anion and the cytotoxic EPO-derived oxidant HOBr when exposed to TNF, showing that TNF activates the respiratory burst of EOs attached to a "physiologic" surface.	hypobromous acid	133-137	tumor necrosis factor	Homo sapiens	172-175
1985118-4	1991	Because EPO preferentially oxidizes Br- to hypobromous acid (HOBr) rather than Cl- to hypochlorous acid (HOCl) at physiologic halide concentrations, we characterized the Br(-)-dependent toxicity of both activated EOs and purified human EPO towards several types of endothelial cells and isolated working rat hearts.	hypobromous acid	43-59	eosinophil peroxidase	Rattus norvegicus	8-11
1985118-4	1991	Because EPO preferentially oxidizes Br- to hypobromous acid (HOBr) rather than Cl- to hypochlorous acid (HOCl) at physiologic halide concentrations, we characterized the Br(-)-dependent toxicity of both activated EOs and purified human EPO towards several types of endothelial cells and isolated working rat hearts.	hypobromous acid	61-65	eosinophil peroxidase	Rattus norvegicus	8-11
1985118-6	1991	H2O2 and purified human EPO, especially when bound to cell surfaces, mediated extraordinarily potent, completely Br(-)-dependent cytolysis of endothelial cells that was reversed by peroxidase inhibitors, HOBr scavengers, and competitive substrates.	hypobromous acid	204-208	eosinophil peroxidase	Rattus norvegicus	24-27
1985118-9	1991	These findings raise the possibility that EPO bound to endocardial cells might utilize H2O2 generated either by overlying phagocytes or endogenous cardiac metabolism along with the virtually inexhaustible supply of Br- from flowing blood to fuel HOBr-mediated cell damage.	hypobromous acid	246-250	eosinophil peroxidase	Rattus norvegicus	42-45
34984290-5	2021	Similar results followed the exposure of IL-6 to N-chlorotaurine (NCT) and hypobromous acid (HOBr), two other reactive species produced in vivo.	hypobromous acid	75-91	interleukin 6	Homo sapiens	41-45
34863835-1	2022	Previously we have shown that lactoferrin (LTF), a protein of secondary neutrophilic granules, can be efficiently modified by hypohalous acids (HOCl and HOBr), which are produced at high concentrations during inflammation and oxidative/halogenative stress by myeloperoxidase, an enzyme of azurophilic neutrophilic granules.	hypobromous acid	153-157	lactotransferrin	Homo sapiens	30-41
34863835-1	2022	Previously we have shown that lactoferrin (LTF), a protein of secondary neutrophilic granules, can be efficiently modified by hypohalous acids (HOCl and HOBr), which are produced at high concentrations during inflammation and oxidative/halogenative stress by myeloperoxidase, an enzyme of azurophilic neutrophilic granules.	hypobromous acid	153-157	lactotransferrin	Homo sapiens	43-46
34863835-1	2022	Previously we have shown that lactoferrin (LTF), a protein of secondary neutrophilic granules, can be efficiently modified by hypohalous acids (HOCl and HOBr), which are produced at high concentrations during inflammation and oxidative/halogenative stress by myeloperoxidase, an enzyme of azurophilic neutrophilic granules.	hypobromous acid	153-157	myeloperoxidase	Homo sapiens	259-274
34984290-5	2021	Similar results followed the exposure of IL-6 to N-chlorotaurine (NCT) and hypobromous acid (HOBr), two other reactive species produced in vivo.	hypobromous acid	93-97	interleukin 6	Homo sapiens	41-45
34984290-9	2021	Further studies on how HOCl and HOBr and their halogenated amine derivatives interact with IL-6 and related cytokines in vivo may open up alternative therapeutic interventions with these compounds in COVID-19 and other hyperinflammatory diseases.	hypobromous acid	32-36	interleukin 6	Homo sapiens	91-95
35349263-5	2022	For example, the total organic bromine was less than 0.25 muM (as Br) at environmentally relevant bromine radicals" exposures of ~10-9 M s. The results give robust evidence that the scavenging of bromine radicals by DOM is a crucial step to prevent inorganic bromine radical chemistry from producing free bromine (HOBr/OBr-) and subsequent brominated byproducts.	hypobromous acid	314-318	leptin receptor	Homo sapiens	319-322
34438259-7	2021	The only well-established physiological role of peroxidasin is in the formation of a sulfilimine bond, which cross-links collagen IV in basement membranes via catalyzed oxidation of bromide to hypobromous acid.	hypobromous acid	193-209	peroxidasin	Homo sapiens	48-59
34438259-8	2021	We found that peroxidasin secreted from melanoma cells formed sulfilimine bonds in uncross-linked collagen IV, confirming peroxidasin activity and hypobromous acid formation.	hypobromous acid	147-163	peroxidasin	Homo sapiens	14-25
34438259-9	2021	Moreover, 3-bromotyrosine, a stable product of hypobromous acid reacting with tyrosine residues, was detected in invasive melanoma cells, substantiating that their expression of peroxidasin generates hypobromous acid, and showing that it does not exclusively react with collagen IV, but also with other biomolecules.	hypobromous acid	47-63	peroxidasin	Homo sapiens	178-189
34438259-9	2021	Moreover, 3-bromotyrosine, a stable product of hypobromous acid reacting with tyrosine residues, was detected in invasive melanoma cells, substantiating that their expression of peroxidasin generates hypobromous acid, and showing that it does not exclusively react with collagen IV, but also with other biomolecules.	hypobromous acid	200-216	peroxidasin	Homo sapiens	178-189
34116271-7	2021	The formation of bromate would be increased through increasing radical oxidation by synergistic ozonation, but can be depressed by relative higher H2O2 as the reducing agent of HOBr/OBr- intermediate.	hypobromous acid	177-181	leptin receptor	Homo sapiens	182-185
35077976-10	2022	ii) The inhibitory effects of chloride, bromide, HOBr/OBr- and HOCl/ClO- are dominant in neutral and alkaline conditions and may result in the formation of secondary oxidants (e.g., chlorine atoms or free bromine), which in turn contribute to pollutant degradation or form undesired oxidation by-products such as BrO3-, ClO3- and halogenated organic products.	hypobromous acid	49-53	leptin receptor	Homo sapiens	54-57
2474536-6	1989	The ability of either hypochlorous acid or hypobromous acid to directly disrupt alpha 2M function and structure was confirmed under cell-free conditions.	hypobromous acid	43-59	alpha-2-macroglobulin	Homo sapiens	80-88
2562426-6	1989	This suggested that, in the presence of MPO/H2O2 + Cl- + Br-, oxidation was due to HOBr from HOCl oxidation of Br- and/or oxidation of Br- by MPO/H2O2.	hypobromous acid	83-87	myeloperoxidase	Homo sapiens	40-43
32675287-11	2020	They show that HOBr produced by peroxidasin is selective for, but not limited to, the crosslinking of collagen IV.	hypobromous acid	15-19	peroxidasin	Mus musculus	32-43
32675287-12	2020	Based on our findings, the use of 3-bromotyrosine as a specific biomarker of oxidative damage by HOBr warrants further investigation in clinical conditions linked to high peroxidasin expression.	hypobromous acid	97-101	peroxidasin	Mus musculus	171-182
32675287-1	2020	Peroxidasin is a heme peroxidase that oxidizes bromide to hypobromous acid (HOBr), a powerful oxidant that promotes the formation of the sulfilimine crosslink in collagen IV in basement membranes.	hypobromous acid	58-74	peroxidasin	Mus musculus	0-11
32675287-1	2020	Peroxidasin is a heme peroxidase that oxidizes bromide to hypobromous acid (HOBr), a powerful oxidant that promotes the formation of the sulfilimine crosslink in collagen IV in basement membranes.	hypobromous acid	76-80	peroxidasin	Mus musculus	0-11
31015146-6	2019	The myeloperoxidase-derived oxidants hypochlorous acid, taurine chloramine, hypobromous acid, and hypothiocyanous acid, all at 10 muM, cross-linked calprotectin (5 muM) via reversible disulfide bonds.	hypobromous acid	76-92	myeloperoxidase	Homo sapiens	4-19
32675287-2	2020	We investigated whether HOBr released by peroxidasin leads to other oxidative modifications of proteins, particularly bromination of tyrosine residues, in peroxidasin-expressing PFHR9 cells.	hypobromous acid	24-28	peroxidasin	Mus musculus	41-52
32675287-2	2020	We investigated whether HOBr released by peroxidasin leads to other oxidative modifications of proteins, particularly bromination of tyrosine residues, in peroxidasin-expressing PFHR9 cells.	hypobromous acid	24-28	peroxidasin	Mus musculus	155-166
32571911-3	2020	The formation of sulfilimine cross-links depends on the ability of peroxidasin to use bromide and hydrogen peroxide substrates to produce hypobromous acid (HOBr).	hypobromous acid	138-154	peroxidasin	Homo sapiens	67-78
32571911-3	2020	The formation of sulfilimine cross-links depends on the ability of peroxidasin to use bromide and hydrogen peroxide substrates to produce hypobromous acid (HOBr).	hypobromous acid	156-160	peroxidasin	Homo sapiens	67-78
32571911-5	2020	Whether the HOBr generated by peroxidasin is used very selectively for creating sulfilimine cross-links or whether it also causes oxidative damage to bystander molecules (e.g., generating bromotyrosine residues in basement membrane proteins) is unclear.	hypobromous acid	12-16	peroxidasin	Homo sapiens	30-41
30279272-2	2018	Exposure of the cryptic epitope is thought to occur via disruption of sulfilimine crosslinks in the NC1 domain that are formed by peroxidasin-dependent production of hypobromous acid.	hypobromous acid	166-182	peroxidasin	Homo sapiens	130-141
30279272-9	2018	Enriched anti-peroxidasin antibodies inhibited peroxidasin-mediated hypobromous acid production in vitro.	hypobromous acid	68-84	peroxidasin	Homo sapiens	14-25
30279272-9	2018	Enriched anti-peroxidasin antibodies inhibited peroxidasin-mediated hypobromous acid production in vitro.	hypobromous acid	68-84	peroxidasin	Homo sapiens	47-58
29653357-7	2018	However, the oxidation/degradation of NHBrCl in the Co(II)/PMS process reforms HOBr, and, although less in quantity, is oxidized to BrO3- at higher Co(II) and Br- concentrations.	hypobromous acid	79-83	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	52-58
30156836-1	2018	The specific detection of eosinophil peroxidase (EPO) activity requires the difficult distinction between hypobromous acid generated by EPO and hypochlorous acid generated by other haloperoxidases.	hypobromous acid	106-122	eosinophil peroxidase	Mus musculus	26-47
30156836-1	2018	The specific detection of eosinophil peroxidase (EPO) activity requires the difficult distinction between hypobromous acid generated by EPO and hypochlorous acid generated by other haloperoxidases.	hypobromous acid	106-122	eosinophil peroxidase	Mus musculus	49-52
28657332-5	2017	Recent Advances: Peroxidasin (PXDN), a BM-associated animal heme peroxidase, generates hypobromous acid (HOBr) to form sulfilimine cross-links within the collagen IV network of BM.	hypobromous acid	87-103	peroxidasin	Homo sapiens	17-28
29626421-7	2018	Results from NADH bromohydrin measurements indicates that low micromolar HOBr generated by peroxidasin was sufficient for maximum sulfilimine cross-linking, whereas 100 muM reagent HOBr or taurine bromamine was less efficient.	hypobromous acid	73-77	peroxidasin	Homo sapiens	91-102
29626421-11	2018	In conclusion, HOBr is produced by peroxidasin in the extracellular matrix.	hypobromous acid	15-19	peroxidasin	Homo sapiens	35-46
28657332-5	2017	Recent Advances: Peroxidasin (PXDN), a BM-associated animal heme peroxidase, generates hypobromous acid (HOBr) to form sulfilimine cross-links within the collagen IV network of BM.	hypobromous acid	87-103	peroxidasin	Homo sapiens	30-34
28657332-5	2017	Recent Advances: Peroxidasin (PXDN), a BM-associated animal heme peroxidase, generates hypobromous acid (HOBr) to form sulfilimine cross-links within the collagen IV network of BM.	hypobromous acid	105-109	peroxidasin	Homo sapiens	17-28
28657332-5	2017	Recent Advances: Peroxidasin (PXDN), a BM-associated animal heme peroxidase, generates hypobromous acid (HOBr) to form sulfilimine cross-links within the collagen IV network of BM.	hypobromous acid	105-109	peroxidasin	Homo sapiens	30-34
28657332-8	2017	CRITICAL ISSUES: The molecular mechanism whereby PXDN uses HOBr as a reactive intermediate to cross-link collagen IV, yet avoid collateral damage to nearby BM proteins, remains unclear.	hypobromous acid	59-63	peroxidasin	Homo sapiens	49-53
28825741-0	2017	Kinetics of the BrO + HO2 reaction over the temperature range T = 246-314 K. The kinetics of the reaction between gas phase BrO and HO2 radicals, BrO + HO2   HOBr + O2 (1), have been studied over the atmospherically relevant temperature range T = 246-314 K and at ambient pressure, p = 760 +- 20 Torr, using laser flash photolysis coupled with ultraviolet absorption spectroscopy.	hypobromous acid	158-162	heme oxygenase 2	Homo sapiens	22-25
28587811-2	2017	Here, we present the development of a sensitive and specific assay for determination of the halogenating enzymatic activity of MPO and EPO based on the electrophilic attack of HOCl and HOBr on aromatic ring of dansylglycine (DG).	hypobromous acid	185-189	myeloperoxidase	Homo sapiens	127-130
28587811-2	2017	Here, we present the development of a sensitive and specific assay for determination of the halogenating enzymatic activity of MPO and EPO based on the electrophilic attack of HOCl and HOBr on aromatic ring of dansylglycine (DG).	hypobromous acid	185-189	eosinophil peroxidase	Homo sapiens	135-138
25912480-5	2015	Human 5-LOX was incubated with increasing amounts of HOCl or HOBr.	hypobromous acid	61-65	arachidonate 5-lipoxygenase	Homo sapiens	6-11
26456401-1	2015	At the sites of inflammation, hypohalous acids, such as hypochlorous acid and hypobromous acid (HOBr), are produced by myeloperoxidase.	hypobromous acid	78-94	myeloperoxidase	Homo sapiens	119-134
26456401-1	2015	At the sites of inflammation, hypohalous acids, such as hypochlorous acid and hypobromous acid (HOBr), are produced by myeloperoxidase.	hypobromous acid	96-100	myeloperoxidase	Homo sapiens	119-134
27785502-0	2016	A theoretical study of the atmospherically important radical-radical reaction BrO + HO2; the product channel O2(a1Deltag) + HOBr is formed with the highest rate.	hypobromous acid	124-128	heme oxygenase 2	Homo sapiens	84-87
27785502-1	2016	A theoretical study has been made of the BrO + HO2 reaction, a radical-radical reaction which contributes to ozone depletion in the atmosphere via production of HOBr.	hypobromous acid	161-165	heme oxygenase 2	Homo sapiens	47-50
25912480-10	2015	Additionally, the formation of 8-HpETE and 12-HpETE by 5-LOX rose slightly with increasing HOCl and HOBr.	hypobromous acid	100-104	arachidonate 5-lipoxygenase	Homo sapiens	55-60
25264081-8	2014	This dye is selectively oxidized by the MPO and EPO halogenation products hypochlorous and hypobromous acid.	hypobromous acid	91-107	myeloperoxidase	Homo sapiens	40-43
25611970-7	2015	H2O2 is thus consumed in a catalytic cycle and leads to less efficient HOBr scavenging at even low iodide concentrations (<1 muM).	hypobromous acid	71-75	latexin	Homo sapiens	128-131
25264081-8	2014	This dye is selectively oxidized by the MPO and EPO halogenation products hypochlorous and hypobromous acid.	hypobromous acid	91-107	erythropoietin	Homo sapiens	48-51
24632382-6	2014	This article reviews recent developments in our understanding of the cellular reactivity of hypochlorous acid, hypobromous acid, and hypothiocyanous acid, the major oxidants produced by myeloperoxidase under physiological conditions.	hypobromous acid	111-127	myeloperoxidase	Homo sapiens	186-201
25438766-5	2014	Fourteen compounds were found to be potent inhibitors with IC50 values <1muM, suggesting these compounds could be considered as potential modulators of pro-oxidative tissue injury pertubated by the inflammatory MPO/H2O2/HOCl/HOBr system.	hypobromous acid	228-232	myeloperoxidase	Homo sapiens	214-217
23719833-11	2013	Inhibition of myeloperoxidase involves paracetamol oxidation and concomitant decreased formation of halogenating oxidants (e.g. hypochlorous acid, hypobromous acid) that may be associated with multiple inflammatory pathologies including atherosclerosis and rheumatic diseases.	hypobromous acid	147-163	myeloperoxidase	Homo sapiens	14-29
24384524-1	2014	Halogenated lipids, proteins, and lipoproteins formed in reactions with myeloperoxidase (MPO)-derived hypochlorous acid (HOCl) and hypobromous acid (HOBr) can contribute to the regulation of functional activity of cells and serve as mediators of inflammation.	hypobromous acid	149-153	myeloperoxidase	Homo sapiens	72-87
24384524-1	2014	Halogenated lipids, proteins, and lipoproteins formed in reactions with myeloperoxidase (MPO)-derived hypochlorous acid (HOCl) and hypobromous acid (HOBr) can contribute to the regulation of functional activity of cells and serve as mediators of inflammation.	hypobromous acid	149-153	myeloperoxidase	Homo sapiens	89-92
23865454-4	2013	Here we show for the first time a direct comparison of the abilities of Sec-containing mTR3 and the Cys-orthologue from D. melanogaster (DmTR) to resist inactivation by oxidation from a variety of oxidants including H2O2, hydroxyl radical, peroxynitrite, hypochlorous acid, hypobromous acid, and hypothiocyanous acid.	hypobromous acid	274-290	thioredoxin reductase 2	Mus musculus	87-91
23685182-1	2013	Hypobromous acid (HOBr) is formed by eosinophil peroxidase and myeloperoxidase in the presence of H2O2, Cl(-), and Br(-) in the host defense system of humans, protecting against invading bacteria.	hypobromous acid	0-16	myeloperoxidase	Homo sapiens	63-78
23685182-1	2013	Hypobromous acid (HOBr) is formed by eosinophil peroxidase and myeloperoxidase in the presence of H2O2, Cl(-), and Br(-) in the host defense system of humans, protecting against invading bacteria.	hypobromous acid	18-22	myeloperoxidase	Homo sapiens	63-78
23590281-2	2013	Taurine, a non-protein amino acid present in high amounts in the leukocytes, reacts instantaneously with HOBr leading to their haloamine derivative taurine dibromamine (Tau-NBr2).	hypobromous acid	105-109	neighbor of BRCA1 lncRNA 2	Homo sapiens	173-177
23590281-6	2013	We found that the oxidation of lysozyme by Tau-NBr2 decreased its enzymatic activity in 80%, which was significant higher compared to the effect of its precursor HOBr (30%).	hypobromous acid	162-166	neighbor of BRCA1 lncRNA 2	Homo sapiens	47-51
23590281-7	2013	The study and comparison of Tau-NBr2 and HOBr regarding the alterations provoked in the intrinsic fluorescence, synchronous fluorescence, resonance light scattering and near and far-UV circular dichroism spectra of lysozyme and oxidized lysozyme revealed that tryptophan residues in the active site of the protein were the main target for Tau-NBr2 and could explain its efficacy as inhibitor of lysozyme enzymatic activity.	hypobromous acid	41-45	neighbor of BRCA1 lncRNA 2	Homo sapiens	343-347
23865454-4	2013	Here we show for the first time a direct comparison of the abilities of Sec-containing mTR3 and the Cys-orthologue from D. melanogaster (DmTR) to resist inactivation by oxidation from a variety of oxidants including H2O2, hydroxyl radical, peroxynitrite, hypochlorous acid, hypobromous acid, and hypothiocyanous acid.	hypobromous acid	274-290	eukaryotic elongation factor, selenocysteine-tRNA-specific	Mus musculus	72-75
23323704-1	2013	HOBr, formed via oxidation of bromide by free available chlorine (FAC), is frequently assumed to be the sole species responsible for generating brominated disinfection byproducts (DBPs).	hypobromous acid	0-4	FA complementation group C	Homo sapiens	66-69
23327477-3	2013	Herein, reactions of HOCl and HOBr with three well-characterized proteins [adenylate kinase (ADK), ribose binding protein, and bovine serum albumin] were characterized.	hypobromous acid	30-34	adenosine kinase	Homo sapiens	75-91
23327477-3	2013	Herein, reactions of HOCl and HOBr with three well-characterized proteins [adenylate kinase (ADK), ribose binding protein, and bovine serum albumin] were characterized.	hypobromous acid	30-34	adenosine kinase	Homo sapiens	93-96
22982576-3	2012	Phagocyte-derived myeloperoxidase (MPO) utilizes chloride and bromide, in the presence of hydrogen peroxide (H(2)O(2)), to generate hypochlorous acid and hypobromous acid, potent oxidizing species that are known to kill invading pathogens.	hypobromous acid	154-170	myeloperoxidase	Homo sapiens	35-38
23438648-5	2013	Another major participant of inflammatory response is the enzyme myeloperoxidase (MPO) which is secreted by neutrophils in the focus of inflammation and catalyzes formation of HOCl and HOBr.	hypobromous acid	185-189	myeloperoxidase	Homo sapiens	65-80
23438648-5	2013	Another major participant of inflammatory response is the enzyme myeloperoxidase (MPO) which is secreted by neutrophils in the focus of inflammation and catalyzes formation of HOCl and HOBr.	hypobromous acid	185-189	myeloperoxidase	Homo sapiens	82-85
22982576-8	2012	Under physiological pH and concentrations of halides (100muM KBr, 100muM KSCN, and 100mM NaCl), VPO1 utilizes approximately 45% of H(2)O(2) for the generation of hypobromous acid, 35% for hypothiocyanous acid, and 18% for hypochlorous acid.	hypobromous acid	162-178	peroxidasin	Homo sapiens	96-100
22982576-7	2012	VPO1, like MPO but unlike lactoperoxidase, is able to generate hypochlorous acid, hypobromous acid, and hypothiocyanous acid in the presence of H(2)O(2).	hypobromous acid	82-98	peroxidasin	Homo sapiens	0-4
20932962-4	2011	In contrast, chloro- and bromohydrins as well as dihalogenides are formed by the addition of HOCl or HOBr to the olefinic groups of the fatty acyl residues of lipids or under the influence of the enzyme myeloperoxidase (MPO) from Cl(-) and H(2)O(2).	hypobromous acid	101-105	myeloperoxidase	Homo sapiens	203-218
22963047-9	2012	Bromate formation is initiated by the formation of a complex between CuO and HOBr/OBr(-), which then reacts with HOBr to generate bromite.	hypobromous acid	113-117	leptin receptor	Homo sapiens	78-81
21892922-2	2012	MPO catalyses the oxidation of Cl-, Br- and SCN- by H2O2 to generate the powerful oxidants hypochlorous acid (HOCl), hypobromous acid (HOBr) and hypothiocyanous acid (HOSCN) respectively.	hypobromous acid	135-139	myeloperoxidase	Homo sapiens	0-3
21241706-2	2011	Under inflammatory condition, cellular DNA is damaged by hypobromous acid, which is generated by myeloperoxidase and eosinophil peroxidase.	hypobromous acid	57-73	myeloperoxidase	Homo sapiens	97-112
21241706-2	2011	Under inflammatory condition, cellular DNA is damaged by hypobromous acid, which is generated by myeloperoxidase and eosinophil peroxidase.	hypobromous acid	57-73	eosinophil peroxidase	Homo sapiens	117-138
20932962-4	2011	In contrast, chloro- and bromohydrins as well as dihalogenides are formed by the addition of HOCl or HOBr to the olefinic groups of the fatty acyl residues of lipids or under the influence of the enzyme myeloperoxidase (MPO) from Cl(-) and H(2)O(2).	hypobromous acid	101-105	myeloperoxidase	Homo sapiens	220-223
20408436-2	2010	Primary AH (HOCl and HOBr) are produced through oxidation of Cl- and Br- respectively by hydrogen peroxide catalyzed by myeloperoxidase or oesinophilic peroxidase.	hypobromous acid	21-25	myeloperoxidase	Homo sapiens	120-135
20647044-11	2010	Our findings suggest that MPO produces hypobromous acid as well as hypochlorous acid in the airways of children with CF and that these oxidants are involved in the early pathogenesis of CF.	hypobromous acid	39-55	myeloperoxidase	Homo sapiens	26-29
20528774-1	2010	MPO (myeloperoxidase) catalyses the oxidation of chloride, bromide and thiocyanate by hydrogen peroxide to HOCl (hypochlorous acid), HOBr (hypobromous acid) and HOSCN (hypothiocyanous acid) respectively.	hypobromous acid	133-137	myeloperoxidase	Mus musculus	0-3
20528774-1	2010	MPO (myeloperoxidase) catalyses the oxidation of chloride, bromide and thiocyanate by hydrogen peroxide to HOCl (hypochlorous acid), HOBr (hypobromous acid) and HOSCN (hypothiocyanous acid) respectively.	hypobromous acid	133-137	myeloperoxidase	Mus musculus	5-20
20528774-1	2010	MPO (myeloperoxidase) catalyses the oxidation of chloride, bromide and thiocyanate by hydrogen peroxide to HOCl (hypochlorous acid), HOBr (hypobromous acid) and HOSCN (hypothiocyanous acid) respectively.	hypobromous acid	139-155	myeloperoxidase	Mus musculus	0-3
20528774-1	2010	MPO (myeloperoxidase) catalyses the oxidation of chloride, bromide and thiocyanate by hydrogen peroxide to HOCl (hypochlorous acid), HOBr (hypobromous acid) and HOSCN (hypothiocyanous acid) respectively.	hypobromous acid	139-155	myeloperoxidase	Mus musculus	5-20
20528774-6	2010	Inhibition also occurs with MPO-generated HOCl and HOBr, but is more marked with MPO-generated HOSCN, particularly at longer incubation times.	hypobromous acid	51-55	myeloperoxidase	Mus musculus	28-31
19788922-1	2010	The potent oxidants hypochlorous acid (HOCl) and hypobromous acid (HOBr) are produced extracellularly by myeloperoxidase, following release of this enzyme from activated leukocytes.	hypobromous acid	67-71	myeloperoxidase	Homo sapiens	105-120
19788922-7	2010	In contrast, the heparan sulfate chains of HOCl/HOBr-modified perlecan retained their ability to bind FGF-2 and collagen V and were able to promote FGF-2-dependent cellular proliferation.	hypobromous acid	48-52	fibroblast growth factor 2	Homo sapiens	102-107
19788922-7	2010	In contrast, the heparan sulfate chains of HOCl/HOBr-modified perlecan retained their ability to bind FGF-2 and collagen V and were able to promote FGF-2-dependent cellular proliferation.	hypobromous acid	48-52	fibroblast growth factor 2	Homo sapiens	148-153
19968966-1	2010	The heme peroxidase enzyme myeloperoxidase (MPO) is released by activated neutrophils and monocytes, where it uses hydrogen peroxide (H(2)O(2)) to catalyze the production of the potent oxidants hypochlorous acid (HOCl), hypobromous acid (HOBr) and hypothiocyanous acid (HOSCN) from halide and pseudohalide (SCN(-)) ions.	hypobromous acid	238-242	myeloperoxidase	Homo sapiens	27-42
19968966-1	2010	The heme peroxidase enzyme myeloperoxidase (MPO) is released by activated neutrophils and monocytes, where it uses hydrogen peroxide (H(2)O(2)) to catalyze the production of the potent oxidants hypochlorous acid (HOCl), hypobromous acid (HOBr) and hypothiocyanous acid (HOSCN) from halide and pseudohalide (SCN(-)) ions.	hypobromous acid	238-242	myeloperoxidase	Homo sapiens	44-47
19968966-3	2010	It is shown here that acetaminophen (paracetamol), a phenol-based drug with analgesic and antipyretic actions, is an efficient inhibitor of HOCl and HOBr generation by isolated MPO-H(2)O(2)-halide systems.	hypobromous acid	149-153	myeloperoxidase	Homo sapiens	177-180
19708016-1	2009	Hypobromous acid (HOBr) produced by both eosinophil peroxidase (EPO) and myeloperoxidase (MPO) is a stronger oxidant than HOCl, and is also essential for optimal and efficient microbial killing.	hypobromous acid	0-16	eosinophil peroxidase	Homo sapiens	41-62
19708016-1	2009	Hypobromous acid (HOBr) produced by both eosinophil peroxidase (EPO) and myeloperoxidase (MPO) is a stronger oxidant than HOCl, and is also essential for optimal and efficient microbial killing.	hypobromous acid	0-16	eosinophil peroxidase	Homo sapiens	64-67
19708016-1	2009	Hypobromous acid (HOBr) produced by both eosinophil peroxidase (EPO) and myeloperoxidase (MPO) is a stronger oxidant than HOCl, and is also essential for optimal and efficient microbial killing.	hypobromous acid	0-16	myeloperoxidase	Homo sapiens	73-88
19708016-1	2009	Hypobromous acid (HOBr) produced by both eosinophil peroxidase (EPO) and myeloperoxidase (MPO) is a stronger oxidant than HOCl, and is also essential for optimal and efficient microbial killing.	hypobromous acid	0-16	myeloperoxidase	Homo sapiens	90-93
19708016-1	2009	Hypobromous acid (HOBr) produced by both eosinophil peroxidase (EPO) and myeloperoxidase (MPO) is a stronger oxidant than HOCl, and is also essential for optimal and efficient microbial killing.	hypobromous acid	18-22	eosinophil peroxidase	Homo sapiens	41-62
19708016-1	2009	Hypobromous acid (HOBr) produced by both eosinophil peroxidase (EPO) and myeloperoxidase (MPO) is a stronger oxidant than HOCl, and is also essential for optimal and efficient microbial killing.	hypobromous acid	18-22	eosinophil peroxidase	Homo sapiens	64-67
19708016-1	2009	Hypobromous acid (HOBr) produced by both eosinophil peroxidase (EPO) and myeloperoxidase (MPO) is a stronger oxidant than HOCl, and is also essential for optimal and efficient microbial killing.	hypobromous acid	18-22	myeloperoxidase	Homo sapiens	73-88
19708016-1	2009	Hypobromous acid (HOBr) produced by both eosinophil peroxidase (EPO) and myeloperoxidase (MPO) is a stronger oxidant than HOCl, and is also essential for optimal and efficient microbial killing.	hypobromous acid	18-22	myeloperoxidase	Homo sapiens	90-93
18851713-6	2009	Addition of SOD (superoxide dismutase) doubled the amount of HOBr detected.	hypobromous acid	61-65	superoxide dismutase 1	Homo sapiens	12-15
18851713-6	2009	Addition of SOD (superoxide dismutase) doubled the amount of HOBr detected.	hypobromous acid	61-65	superoxide dismutase 1	Homo sapiens	17-37
18657284-5	2008	Further investigation indicates that the effective BFP minimization can be ascribed to neither the surface adsorption of BrO(3)(-) or Br(-) on CeO(2) nor the surface reduction of BrO(3)(-) to HOBr/OBr(-) by CeO(2).	hypobromous acid	192-196	ring finger protein 112	Homo sapiens	51-54
18759245-15	2008	Eosinophil peroxidase catalyzes the H2O2 oxidation of Br- to HOBr, which N-brominates taurine to N-bromotaurine at its concentration of 15 mM in eosinophils.	hypobromous acid	61-65	eosinophil peroxidase	Homo sapiens	0-21
18605737-2	2008	These lipids, in contrast to other phospholipids, have been reported to be targets of HOCl/HOBr generated by myeloperoxidase, with elevated levels of the products of these reactions (alpha-chloro/alpha-bromo aldehydes and unsaturated lysophospholipids) having been detected in human atherosclerotic lesions.	hypobromous acid	91-95	myeloperoxidase	Homo sapiens	109-124
18657284-8	2008	Another possible reason for the BFP minimization is that the CeO(2) could possibly reduce BrO() to HOBr/OBr(-) during the decomposition of H(2)O(2).	hypobromous acid	99-103	ring finger protein 112	Homo sapiens	32-35
17209551-3	2007	The enzyme uses hydrogen peroxide (H2O2) and bromide (Br-), a preferred cosubstrate of EPO, to generate the cytotoxic oxidant hypobromous acid.	hypobromous acid	126-142	eosinophil peroxidase	Homo sapiens	87-90
17604010-1	2007	The leukocyte enzyme myeloperoxidase (MPO) is capable of catalyzing the oxidation of chloride and bromide ions, at physiological concentrations of these substrates, by hydrogen peroxide, generating hypochlorous acid (HOCl) and hypobromous acid (HOBr), respectively.	hypobromous acid	245-249	myeloperoxidase	Homo sapiens	21-36
17604010-1	2007	The leukocyte enzyme myeloperoxidase (MPO) is capable of catalyzing the oxidation of chloride and bromide ions, at physiological concentrations of these substrates, by hydrogen peroxide, generating hypochlorous acid (HOCl) and hypobromous acid (HOBr), respectively.	hypobromous acid	245-249	myeloperoxidase	Homo sapiens	38-41
17141727-3	2007	The flavonols rutin, quercetin, myricetin, and kaempferol inhibited the inactivation of alpha1-antitrypsin by HOCl and HOBr with rutin having the most pronounced effect.	hypobromous acid	119-123	serpin family A member 1	Homo sapiens	88-106
17604010-8	2007	We attributed these effects to the involvement of HOBr arising from the reaction of MPO-derived HOCl with bromide rather than to the exchange of bromide with chlorine atoms of chlorohydrins or direct formation of HOBr by MPO.	hypobromous acid	50-54	myeloperoxidase	Homo sapiens	84-87
17604010-8	2007	We attributed these effects to the involvement of HOBr arising from the reaction of MPO-derived HOCl with bromide rather than to the exchange of bromide with chlorine atoms of chlorohydrins or direct formation of HOBr by MPO.	hypobromous acid	50-54	myeloperoxidase	Homo sapiens	221-224
17604010-8	2007	We attributed these effects to the involvement of HOBr arising from the reaction of MPO-derived HOCl with bromide rather than to the exchange of bromide with chlorine atoms of chlorohydrins or direct formation of HOBr by MPO.	hypobromous acid	213-217	myeloperoxidase	Homo sapiens	221-224
17348389-1	2007	We have demonstrated that hypochlorite (HOCI/OCl-) and hypobromite (HOBr/OBr-) can react with tert-butyl hydroperoxide with close rate constants (k(HOCl) = 10,8 M(-1) x s(1); k(HOBr) = 8,9 M(-1) x (s(-1)).	hypobromous acid	177-181	leptin receptor	Homo sapiens	69-72
17014424-1	2007	EPO (eosinophil peroxidase) and MPO (myeloperoxidase) are highly basic haem enzymes that can catalyse the production of HOBr (hypobromous acid).	hypobromous acid	120-124	eosinophil peroxidase	Homo sapiens	0-3
17014424-1	2007	EPO (eosinophil peroxidase) and MPO (myeloperoxidase) are highly basic haem enzymes that can catalyse the production of HOBr (hypobromous acid).	hypobromous acid	120-124	eosinophil peroxidase	Homo sapiens	5-26
17014424-1	2007	EPO (eosinophil peroxidase) and MPO (myeloperoxidase) are highly basic haem enzymes that can catalyse the production of HOBr (hypobromous acid).	hypobromous acid	120-124	myeloperoxidase	Homo sapiens	32-35
17014424-1	2007	EPO (eosinophil peroxidase) and MPO (myeloperoxidase) are highly basic haem enzymes that can catalyse the production of HOBr (hypobromous acid).	hypobromous acid	120-124	myeloperoxidase	Homo sapiens	37-52
17014424-1	2007	EPO (eosinophil peroxidase) and MPO (myeloperoxidase) are highly basic haem enzymes that can catalyse the production of HOBr (hypobromous acid).	hypobromous acid	126-142	eosinophil peroxidase	Homo sapiens	0-3
17014424-1	2007	EPO (eosinophil peroxidase) and MPO (myeloperoxidase) are highly basic haem enzymes that can catalyse the production of HOBr (hypobromous acid).	hypobromous acid	126-142	eosinophil peroxidase	Homo sapiens	5-26
17014424-1	2007	EPO (eosinophil peroxidase) and MPO (myeloperoxidase) are highly basic haem enzymes that can catalyse the production of HOBr (hypobromous acid).	hypobromous acid	126-142	myeloperoxidase	Homo sapiens	32-35
17014424-1	2007	EPO (eosinophil peroxidase) and MPO (myeloperoxidase) are highly basic haem enzymes that can catalyse the production of HOBr (hypobromous acid).	hypobromous acid	126-142	myeloperoxidase	Homo sapiens	37-52
16608171-1	2006	Second-order rate constants for the reaction of HOBr/OBr- (a putative killing agent of eosinophils and a reactive oxygen species that is implicated in mutagenesis and in human inflammatory diseases) with SCN- (an endogenous species in human physiologic fluids) are determined by stopped-flow spectroscopy.	hypobromous acid	48-52	sorcin	Homo sapiens	204-207
16608171-2	2006	The proposed mechanism includes parallel pathways with Br+ transfer to SCN- by general acid catalysis and by direct reaction with HOBr.	hypobromous acid	130-134	sorcin	Homo sapiens	71-74
16608171-3	2006	HOBr reacts with SCN- with a second-order rate constant (2.3 x 10(9) M(-1) s(-1)) that is 2 orders of magnitude larger than that previously measured for the reaction of HOCl with SCN- (2.3 x 10(7) M(-1) s(-1)), and very close to the diffusion limit.	hypobromous acid	0-4	sorcin	Homo sapiens	17-20
16608171-3	2006	HOBr reacts with SCN- with a second-order rate constant (2.3 x 10(9) M(-1) s(-1)) that is 2 orders of magnitude larger than that previously measured for the reaction of HOCl with SCN- (2.3 x 10(7) M(-1) s(-1)), and very close to the diffusion limit.	hypobromous acid	0-4	sorcin	Homo sapiens	179-182
16608171-5	2006	On a molar basis, SCN- is the most effective scavenger of HOBr to be reported to date (200 times more effective than cysteine and 650 times more effective than methionine).	hypobromous acid	58-62	sorcin	Homo sapiens	18-21
16608171-6	2006	Computational models suggest that SCN- is competitive with respect to other scavengers at physiologically relevant concentrations, which leads us to propose it may limit the lifetime of HOBr and its propensity to inflict host tissue damage during inflammatory response, especially during eosinophilia.	hypobromous acid	186-190	sorcin	Homo sapiens	34-37
16608171-8	2006	Since one of the principal charges of eosinophil cells is to clear extracellular parasites via nonphagocytic mechanisms that involve degranulation of eosinophil peroxidase (EPO, the principal mammalian enzyme that produces HOBr), a larger role for OSCN- is suggested for parasitic infection.	hypobromous acid	223-227	eosinophil peroxidase	Homo sapiens	150-171
16608171-8	2006	Since one of the principal charges of eosinophil cells is to clear extracellular parasites via nonphagocytic mechanisms that involve degranulation of eosinophil peroxidase (EPO, the principal mammalian enzyme that produces HOBr), a larger role for OSCN- is suggested for parasitic infection.	hypobromous acid	223-227	eosinophil peroxidase	Homo sapiens	173-176
16375846-2	2006	In contrast, the mammalian homologues such as lactoperoxidase (LPO) and myeloperoxidase primarily oxidize halides and pseudohalides to the corresponding hypohalides (e.g., Br(-) to HOBr, Cl(-) to HOCl).	hypobromous acid	181-185	lactoperoxidase	Homo sapiens	46-61
16375846-2	2006	In contrast, the mammalian homologues such as lactoperoxidase (LPO) and myeloperoxidase primarily oxidize halides and pseudohalides to the corresponding hypohalides (e.g., Br(-) to HOBr, Cl(-) to HOCl).	hypobromous acid	181-185	lactoperoxidase	Homo sapiens	63-66
16297853-1	2006	Three unusual substrates-bromide (Br(-)), nitrite (NO(2)(-)), and thiocyanate (SCN(-))-compete for oxidation by eosinophil peroxidase (EPO) in physiologic fluids in the presence of H(2)O(2) to yield, respectively, hypobromous acid (HOBr), nitrogen dioxide (NO(2)()), or hypothiocyanous acid (HOSCN).	hypobromous acid	214-230	eosinophil peroxidase	Mus musculus	112-133
16125131-5	2006	In accord with previous studies, between pH 5 and 7, myeloperoxidase converted about 90% of available hydrogen peroxide to hypochlorous acid and the remainder to hypobromous acid.	hypobromous acid	162-178	myeloperoxidase	Homo sapiens	53-68
16125131-15	2006	We conclude that at physiological concentrations of chloride and bromide, hypobromous acid can be a major oxidant produced by myeloperoxidase.	hypobromous acid	74-90	myeloperoxidase	Homo sapiens	126-141
16111649-5	2006	However, the eosinophil peroxidase-H(2)O(2)-halide system forms directly HOCl and HOBr.	hypobromous acid	82-86	eosinophil peroxidase	Homo sapiens	13-34
16125131-3	2006	Hypobromous acid and hypothiocyanite are the major products of eosinophil peroxidase.	hypobromous acid	0-16	eosinophil peroxidase	Homo sapiens	63-84
16125131-4	2006	We have investigated the ability of myeloperoxidase to produce hypobromous acid in the presence of physiological concentrations of chloride and bromide.	hypobromous acid	63-79	myeloperoxidase	Homo sapiens	36-51
16297853-1	2006	Three unusual substrates-bromide (Br(-)), nitrite (NO(2)(-)), and thiocyanate (SCN(-))-compete for oxidation by eosinophil peroxidase (EPO) in physiologic fluids in the presence of H(2)O(2) to yield, respectively, hypobromous acid (HOBr), nitrogen dioxide (NO(2)()), or hypothiocyanous acid (HOSCN).	hypobromous acid	214-230	eosinophil peroxidase	Mus musculus	135-138
16297853-1	2006	Three unusual substrates-bromide (Br(-)), nitrite (NO(2)(-)), and thiocyanate (SCN(-))-compete for oxidation by eosinophil peroxidase (EPO) in physiologic fluids in the presence of H(2)O(2) to yield, respectively, hypobromous acid (HOBr), nitrogen dioxide (NO(2)()), or hypothiocyanous acid (HOSCN).	hypobromous acid	232-236	eosinophil peroxidase	Mus musculus	112-133
16297853-1	2006	Three unusual substrates-bromide (Br(-)), nitrite (NO(2)(-)), and thiocyanate (SCN(-))-compete for oxidation by eosinophil peroxidase (EPO) in physiologic fluids in the presence of H(2)O(2) to yield, respectively, hypobromous acid (HOBr), nitrogen dioxide (NO(2)()), or hypothiocyanous acid (HOSCN).	hypobromous acid	232-236	eosinophil peroxidase	Mus musculus	135-138
16166591-1	2006	In vivo, bromide (Br(-)), nitrite (NO(2)(-)), and thiocyanate (SCN(-)) compete for oxidation by eosinophil peroxidase (EPO) and H(2)O(2), yielding, respectively, HOBr, NO(2)., and HOSCN.	hypobromous acid	162-166	eosinophil peroxidase	Homo sapiens	96-117
16166591-1	2006	In vivo, bromide (Br(-)), nitrite (NO(2)(-)), and thiocyanate (SCN(-)) compete for oxidation by eosinophil peroxidase (EPO) and H(2)O(2), yielding, respectively, HOBr, NO(2)., and HOSCN.	hypobromous acid	162-166	eosinophil peroxidase	Homo sapiens	119-122