PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
29922222-10	2018	Furthermore, anxiety and depression levels were enhanced in WT mice exposed to IH as compared to RA controls, while alterations emerged in Ngb-TG mice exposed to IH.	Thioguanine	143-145	neuroglobin	Mus musculus	139-142
32034988-0	2020	Lack of orientation selectivity of the heme insertion in murine neuroglobin revealed by resonance Raman spectroscopy.	Heme	39-43	neuroglobin	Mus musculus	64-75
32034988-5	2020	The resonance Raman data, together with the corresponding crystal structures, indicate the presence of two neuroglobin conformers with a reversed (A conformer) or a canonical (B conformer) heme insertion orientation.	Heme	189-193	neuroglobin	Mus musculus	107-118
30926858-0	2019	Proximal and distal control for ligand binding in neuroglobin: role of the CD loop and evidence for His64 gating.	Cadmium	75-77	neuroglobin	Mus musculus	50-61
30926858-3	2019	Our results highlight the relevance of the CD loop and of Phe106 as distal and proximal controls involved in ligand binding in murine neuroglobin.	Cadmium	43-45	neuroglobin	Mus musculus	134-145
30926858-4	2019	We observed the effects of individual and combined mutations of the CD loop and Phe106 that conferred to Ngb higher CO binding velocities, which we correlate with the following structural observations: the mutant F106A shows, upon CO binding, a reduced heme sliding hindrance, with the heme present in a peculiar double conformation, whereas in the CD loop mutant "Gly-loop", the original network of interactions between the loop and the heme was abolished, enhancing binding via facilitated gating out of the distal His64.	Cadmium	68-70	neuroglobin	Mus musculus	105-108
30926858-4	2019	We observed the effects of individual and combined mutations of the CD loop and Phe106 that conferred to Ngb higher CO binding velocities, which we correlate with the following structural observations: the mutant F106A shows, upon CO binding, a reduced heme sliding hindrance, with the heme present in a peculiar double conformation, whereas in the CD loop mutant "Gly-loop", the original network of interactions between the loop and the heme was abolished, enhancing binding via facilitated gating out of the distal His64.	Heme	253-257	neuroglobin	Mus musculus	105-108
30926858-4	2019	We observed the effects of individual and combined mutations of the CD loop and Phe106 that conferred to Ngb higher CO binding velocities, which we correlate with the following structural observations: the mutant F106A shows, upon CO binding, a reduced heme sliding hindrance, with the heme present in a peculiar double conformation, whereas in the CD loop mutant "Gly-loop", the original network of interactions between the loop and the heme was abolished, enhancing binding via facilitated gating out of the distal His64.	Heme	286-290	neuroglobin	Mus musculus	105-108
30926858-4	2019	We observed the effects of individual and combined mutations of the CD loop and Phe106 that conferred to Ngb higher CO binding velocities, which we correlate with the following structural observations: the mutant F106A shows, upon CO binding, a reduced heme sliding hindrance, with the heme present in a peculiar double conformation, whereas in the CD loop mutant "Gly-loop", the original network of interactions between the loop and the heme was abolished, enhancing binding via facilitated gating out of the distal His64.	Glycine	365-368	neuroglobin	Mus musculus	105-108
30926858-4	2019	We observed the effects of individual and combined mutations of the CD loop and Phe106 that conferred to Ngb higher CO binding velocities, which we correlate with the following structural observations: the mutant F106A shows, upon CO binding, a reduced heme sliding hindrance, with the heme present in a peculiar double conformation, whereas in the CD loop mutant "Gly-loop", the original network of interactions between the loop and the heme was abolished, enhancing binding via facilitated gating out of the distal His64.	Heme	286-290	neuroglobin	Mus musculus	105-108
33166649-2	2021	Neuroglobin is an oxygen-binding globin found in neurons within the central nervous system as well as in peripheral neurons, that produces a protective effect against hypoxic/ischemic damaging insults by promoting oxygen availability within the mitochondria.	Oxygen	18-24	neuroglobin	Mus musculus	0-11
33166649-2	2021	Neuroglobin is an oxygen-binding globin found in neurons within the central nervous system as well as in peripheral neurons, that produces a protective effect against hypoxic/ischemic damaging insults by promoting oxygen availability within the mitochondria.	Oxygen	214-220	neuroglobin	Mus musculus	0-11
33166649-4	2021	Several in vitro and animal studies have reported the potential of neuroglobin upregulation in improving the neuroprotection through modulation of mitochondrial functions, such as ATP production, clearing reactive oxygen species (ROS), promoting the dynamics of mitochondria, and controlling the cell apoptosis.	Adenosine Triphosphate	180-183	neuroglobin	Mus musculus	67-78
33166649-4	2021	Several in vitro and animal studies have reported the potential of neuroglobin upregulation in improving the neuroprotection through modulation of mitochondrial functions, such as ATP production, clearing reactive oxygen species (ROS), promoting the dynamics of mitochondria, and controlling the cell apoptosis.	Reactive Oxygen Species	205-228	neuroglobin	Mus musculus	67-78
33166649-4	2021	Several in vitro and animal studies have reported the potential of neuroglobin upregulation in improving the neuroprotection through modulation of mitochondrial functions, such as ATP production, clearing reactive oxygen species (ROS), promoting the dynamics of mitochondria, and controlling the cell apoptosis.	Reactive Oxygen Species	230-233	neuroglobin	Mus musculus	67-78
31576217-2	2019	The application of UV-visible microspectroscopy in crystallo, solution X-ray absorption near-edge spectroscopy and X-ray diffraction experiments at 15-40 K provided the structural characterization of an Ngb photolytic intermediate by cryo-trapping and allowed direct observation of the relocation of carbon monoxide within the distal heme pocket after photodissociation.	Carbon Monoxide	300-315	neuroglobin	Mus musculus	203-206
31576217-3	2019	Moreover, X-ray diffraction at 100 K under a high pressure of dioxygen, a physiological ligand of Ngb, unravelled the existence of a storage site for O2 in Ngb which coincides with Xe-III, a previously described docking site for xenon or krypton.	Oxygen	62-70	neuroglobin	Mus musculus	98-101
31576217-3	2019	Moreover, X-ray diffraction at 100 K under a high pressure of dioxygen, a physiological ligand of Ngb, unravelled the existence of a storage site for O2 in Ngb which coincides with Xe-III, a previously described docking site for xenon or krypton.	Oxygen	62-70	neuroglobin	Mus musculus	156-159
31576217-3	2019	Moreover, X-ray diffraction at 100 K under a high pressure of dioxygen, a physiological ligand of Ngb, unravelled the existence of a storage site for O2 in Ngb which coincides with Xe-III, a previously described docking site for xenon or krypton.	Superoxides	150-152	neuroglobin	Mus musculus	98-101
31576217-3	2019	Moreover, X-ray diffraction at 100 K under a high pressure of dioxygen, a physiological ligand of Ngb, unravelled the existence of a storage site for O2 in Ngb which coincides with Xe-III, a previously described docking site for xenon or krypton.	Superoxides	150-152	neuroglobin	Mus musculus	156-159
31576217-3	2019	Moreover, X-ray diffraction at 100 K under a high pressure of dioxygen, a physiological ligand of Ngb, unravelled the existence of a storage site for O2 in Ngb which coincides with Xe-III, a previously described docking site for xenon or krypton.	Xenon	181-187	neuroglobin	Mus musculus	98-101
31576217-3	2019	Moreover, X-ray diffraction at 100 K under a high pressure of dioxygen, a physiological ligand of Ngb, unravelled the existence of a storage site for O2 in Ngb which coincides with Xe-III, a previously described docking site for xenon or krypton.	Xenon	181-187	neuroglobin	Mus musculus	156-159
31576217-3	2019	Moreover, X-ray diffraction at 100 K under a high pressure of dioxygen, a physiological ligand of Ngb, unravelled the existence of a storage site for O2 in Ngb which coincides with Xe-III, a previously described docking site for xenon or krypton.	Xenon	229-234	neuroglobin	Mus musculus	98-101
31576217-3	2019	Moreover, X-ray diffraction at 100 K under a high pressure of dioxygen, a physiological ligand of Ngb, unravelled the existence of a storage site for O2 in Ngb which coincides with Xe-III, a previously described docking site for xenon or krypton.	Xenon	229-234	neuroglobin	Mus musculus	156-159
31576217-3	2019	Moreover, X-ray diffraction at 100 K under a high pressure of dioxygen, a physiological ligand of Ngb, unravelled the existence of a storage site for O2 in Ngb which coincides with Xe-III, a previously described docking site for xenon or krypton.	Krypton	238-245	neuroglobin	Mus musculus	98-101
31576217-3	2019	Moreover, X-ray diffraction at 100 K under a high pressure of dioxygen, a physiological ligand of Ngb, unravelled the existence of a storage site for O2 in Ngb which coincides with Xe-III, a previously described docking site for xenon or krypton.	Krypton	238-245	neuroglobin	Mus musculus	156-159
28948468-8	2018	In conclusion, tibolone protects BV-2 cells by a mechanism involving ERbeta and upregulation of neuroglobin.	tibolone	15-23	neuroglobin	Mus musculus	96-107
29108649-3	2017	In murine Ngb, a large internal cavity is involved in the heme sliding mechanism to achieve binding of gaseous ligands through coordination to the heme iron.	Heme	58-62	neuroglobin	Mus musculus	10-13
29038003-4	2018	The retinal Ngb expression in MNU administered mice attenuated following a time dependent manner, suggesting Ngb was involved in the photoreceptor degeneration.	Methylnitrosourea	30-33	neuroglobin	Mus musculus	12-15
29038003-4	2018	The retinal Ngb expression in MNU administered mice attenuated following a time dependent manner, suggesting Ngb was involved in the photoreceptor degeneration.	Methylnitrosourea	30-33	neuroglobin	Mus musculus	109-112
29038003-5	2018	Conversely, the intravenous delivery of Hemin, a Ngb up-regulator, enhanced the Ngb expressions in the retinas of MNU administered mice.	Hemin	40-45	neuroglobin	Mus musculus	49-52
29038003-5	2018	Conversely, the intravenous delivery of Hemin, a Ngb up-regulator, enhanced the Ngb expressions in the retinas of MNU administered mice.	Hemin	40-45	neuroglobin	Mus musculus	80-83
29038003-5	2018	Conversely, the intravenous delivery of Hemin, a Ngb up-regulator, enhanced the Ngb expressions in the retinas of MNU administered mice.	Methylnitrosourea	114-117	neuroglobin	Mus musculus	49-52
29038003-5	2018	Conversely, the intravenous delivery of Hemin, a Ngb up-regulator, enhanced the Ngb expressions in the retinas of MNU administered mice.	Methylnitrosourea	114-117	neuroglobin	Mus musculus	80-83
29038003-10	2018	In conclusion, the intraperitoneally delivery of Hemin can enhance the Ngb expressions in the MNU administered retinas, thereby ameliorating the photoreceptor degeneration and associated visual impairments.	Hemin	49-54	neuroglobin	Mus musculus	71-74
29038003-10	2018	In conclusion, the intraperitoneally delivery of Hemin can enhance the Ngb expressions in the MNU administered retinas, thereby ameliorating the photoreceptor degeneration and associated visual impairments.	Methylnitrosourea	94-97	neuroglobin	Mus musculus	71-74
28951213-1	2017	Neuroglobin (Ngb) is a recently discovered heme protein in the vertebrate brain that can bind to oxygen molecules.	Oxygen	97-103	neuroglobin	Mus musculus	0-11
28951213-1	2017	Neuroglobin (Ngb) is a recently discovered heme protein in the vertebrate brain that can bind to oxygen molecules.	Oxygen	97-103	neuroglobin	Mus musculus	13-16
29108649-5	2017	We propose that these cavities could store oxygen and allow its relay in the heme proximity, which could correspond to NO location in the nitrite-reductase function of Ngb.	Oxygen	43-49	neuroglobin	Mus musculus	168-171
29108649-5	2017	We propose that these cavities could store oxygen and allow its relay in the heme proximity, which could correspond to NO location in the nitrite-reductase function of Ngb.	Heme	77-81	neuroglobin	Mus musculus	168-171
29108649-7	2017	A new gas binding site on the proximal side of the heme has also been characterized, using xenon pressure on a Ngb mutant (V140W) that binds CO with a similar rate and affinity to the wild-type, despite a reshaping of the internal cavity.	Heme	51-55	neuroglobin	Mus musculus	111-114
29108649-7	2017	A new gas binding site on the proximal side of the heme has also been characterized, using xenon pressure on a Ngb mutant (V140W) that binds CO with a similar rate and affinity to the wild-type, despite a reshaping of the internal cavity.	Xenon	91-96	neuroglobin	Mus musculus	111-114
29101592-1	2018	Neuroglobin (Ngb) is expressed in the central and peripheral nervous system, cerebrospinal fluid, retina, and endocrine tissues where it is involved in binding O2 and other gasotransmitters.	Oxygen	160-162	neuroglobin	Mus musculus	0-11
29101592-1	2018	Neuroglobin (Ngb) is expressed in the central and peripheral nervous system, cerebrospinal fluid, retina, and endocrine tissues where it is involved in binding O2 and other gasotransmitters.	Oxygen	160-162	neuroglobin	Mus musculus	13-16
29108649-3	2017	In murine Ngb, a large internal cavity is involved in the heme sliding mechanism to achieve binding of gaseous ligands through coordination to the heme iron.	Heme	147-151	neuroglobin	Mus musculus	10-13
29108649-3	2017	In murine Ngb, a large internal cavity is involved in the heme sliding mechanism to achieve binding of gaseous ligands through coordination to the heme iron.	Iron	152-156	neuroglobin	Mus musculus	10-13
27787886-0	2017	Neuroglobin protects astroglial cells from hydrogen peroxide-induced oxidative stress and apoptotic cell death.	Hydrogen Peroxide	43-60	neuroglobin	Mus musculus	0-11
29075122-0	2017	Adeno-associated virus-mediated neuroglobin overexpression ameliorates the N-methyl-N-nitrosourea-induced retinal impairments: a novel therapeutic strategy against photoreceptor degeneration.	Methylnitrosourea	75-97	neuroglobin	Mus musculus	32-43
29075122-3	2017	The present study found the retinal neuroglobin (NGB) expression in the MNU-administered mice was significantly lower than in normal controls, suggesting NGB was correlated with RD.	Methylnitrosourea	72-75	neuroglobin	Mus musculus	36-47
29075122-3	2017	The present study found the retinal neuroglobin (NGB) expression in the MNU-administered mice was significantly lower than in normal controls, suggesting NGB was correlated with RD.	Methylnitrosourea	72-75	neuroglobin	Mus musculus	49-52
29075122-3	2017	The present study found the retinal neuroglobin (NGB) expression in the MNU-administered mice was significantly lower than in normal controls, suggesting NGB was correlated with RD.	Methylnitrosourea	72-75	neuroglobin	Mus musculus	154-157
29075122-4	2017	Subsequently, an adeno-associated virus (AAV)-2-mCMV-NGB vector was delivered into the subretinal space of the MNU-administered mice.	Methylnitrosourea	111-114	neuroglobin	Mus musculus	53-56
29075122-6	2017	Further, we found NGB overexpression could alleviate visual impairments and morphological devastations in MNU-administered mice.	Methylnitrosourea	106-109	neuroglobin	Mus musculus	18-21
29075122-7	2017	NGB overexpression could rectify apoptotic abnormalities and ameliorate oxidative stress in MNU-administered mice, thereby promoting photoreceptor survival.	Methylnitrosourea	92-95	neuroglobin	Mus musculus	0-3
29075122-8	2017	The cone photoreceptors in MNU-administered mice were also sensitive to AAV-mediated NGB overexpression.	Methylnitrosourea	27-30	neuroglobin	Mus musculus	85-88
28500341-3	2017	In murine Ngb, reversible coordination is achieved by repositioning the heme more deeply into a large internal cavity, the "heme sliding mechanism".	Heme	72-76	neuroglobin	Mus musculus	10-13
28500341-3	2017	In murine Ngb, reversible coordination is achieved by repositioning the heme more deeply into a large internal cavity, the "heme sliding mechanism".	Heme	124-128	neuroglobin	Mus musculus	10-13
27957684-1	2017	Among several mechanisms underlying the well-known trophic and protective effects of 17beta-estradiol (E2) in the brain, we recently reported that E2 induces the up-regulation of two anti-apoptotic and neuroprotectant proteins: huntingtin (HTT) and neuroglobin (NGB).	Estradiol	85-101	neuroglobin	Mus musculus	249-260
27957684-1	2017	Among several mechanisms underlying the well-known trophic and protective effects of 17beta-estradiol (E2) in the brain, we recently reported that E2 induces the up-regulation of two anti-apoptotic and neuroprotectant proteins: huntingtin (HTT) and neuroglobin (NGB).	Estradiol	85-101	neuroglobin	Mus musculus	262-265
27787886-3	2017	Thus, the purpose of this study was to investigate the potential glioprotective effect of Ngb on hydrogen peroxide (H2 O2 )-induced oxidative stress and apoptosis in cultured mouse astrocytes.	Hydrogen Peroxide	97-114	neuroglobin	Mus musculus	90-93
27787886-3	2017	Thus, the purpose of this study was to investigate the potential glioprotective effect of Ngb on hydrogen peroxide (H2 O2 )-induced oxidative stress and apoptosis in cultured mouse astrocytes.	Hydrogen Peroxide	116-121	neuroglobin	Mus musculus	90-93
27787886-4	2017	Incubation of cells with subnanomolar concentrations of Ngb (10-14 -10-10  M) was found to prevent both H2 O2 -evoked reduction in surviving cells number and accumulation of reactive oxygen species in a concentration-dependent manner.	Hydrogen Peroxide	104-109	neuroglobin	Mus musculus	56-59
27787886-4	2017	Incubation of cells with subnanomolar concentrations of Ngb (10-14 -10-10  M) was found to prevent both H2 O2 -evoked reduction in surviving cells number and accumulation of reactive oxygen species in a concentration-dependent manner.	Reactive Oxygen Species	174-197	neuroglobin	Mus musculus	56-59
27787886-5	2017	Furthermore, Ngb treatment abolishes H2 O2 -induced increase in mitochondrial oxygen consumption rates.	Hydrogen Peroxide	37-42	neuroglobin	Mus musculus	13-16
27787886-5	2017	Furthermore, Ngb treatment abolishes H2 O2 -induced increase in mitochondrial oxygen consumption rates.	Oxygen	78-84	neuroglobin	Mus musculus	13-16
27787886-6	2017	Concomitantly, Ngb treatment rescues H2 O2 -associated reduced expression of endogenous antioxidant enzymes (superoxide dismutases and catalase) and prevents the stimulation of the expression of pro-inflammatory genes (inducible nitric oxide synthase, cyclooxygenase-2, and interleukin (IL) IL-6 and IL-33).	Hydrogen Peroxide	37-42	neuroglobin	Mus musculus	15-18
27787886-7	2017	Moreover, Ngb blocks the stimulation of Bax (pro-apoptotic) and the inhibition of Bcl-2 (anti-apoptotic) gene expression induced by H2 O2 , which in turn abolishes caspase 3 activation.	Hydrogen Peroxide	132-137	neuroglobin	Mus musculus	10-13
27787886-8	2017	The protective effect of Ngb upon H2 O2 induced activation of caspase 3 activity and cell death can be accounted for by activation of protein kinase A and mitogen-activated protein kinase transduction cascade.	Hydrogen Peroxide	34-39	neuroglobin	Mus musculus	25-28
27787886-9	2017	Finally, we demonstrate that Ngb increases Akt phosphorylation and prevents H2 O2 -provoked inhibition of ERK and Akt phosphorylation.	Hydrogen Peroxide	76-81	neuroglobin	Mus musculus	29-32
27787886-10	2017	Taken together, these data demonstrate for the first time that Ngb is a glioprotective agent that prevents H2 O2 -induced oxidative stress and apoptotic astroglial cell death.	Hydrogen Peroxide	107-112	neuroglobin	Mus musculus	63-66
27678372-9	2016	DpC significantly increased levels of phosphorylated JNK, neuroglobin, cytoglobin, and cleaved caspase 3 and 9, while decreasing IkBalpha levels in vitro.	di-2-pyridylketone 4-cyclohexyl-4-methyl-3-thiosemicarbazone	0-3	neuroglobin	Mus musculus	58-69
19820972-0	2010	Molecular dynamics simulation of a carboxy murine neuroglobin mutated on the proximal side: heme displacement and concomitant rearrangement in loop regions.	Heme	92-96	neuroglobin	Mus musculus	50-61
24830543-0	2015	(1)H, (15)N and (13)C backbone resonance assignments of murine met-neuroglobin, free and in complex with cyanide.	Cyanides	105-112	neuroglobin	Mus musculus	67-78
23639789-9	2013	In contrast, Ngb knockdown significantly increased OGD-induced neuron death, and increased OGD-induced mitochondrial NAD(+) release and Cyt c release as well, and these outcomes could be rescued by CsA pretreatment.	Cyclosporine	198-201	neuroglobin	Mus musculus	13-16
23639789-10	2013	In summary, our results demonstrated that Ngb overexpression can inhibit OGD-induced mPTP opening in primary cultured mouse cortical neurons, which may be one of the molecular mechanisms of Ngb"s neuroprotection.	1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine	85-89	neuroglobin	Mus musculus	42-45
23639789-10	2013	In summary, our results demonstrated that Ngb overexpression can inhibit OGD-induced mPTP opening in primary cultured mouse cortical neurons, which may be one of the molecular mechanisms of Ngb"s neuroprotection.	1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine	85-89	neuroglobin	Mus musculus	190-193
23182882-0	2013	Transcriptional regulation of mouse neuroglobin gene by cyclic AMP responsive element binding protein (CREB) in N2a cells.	Cyclic AMP	56-66	neuroglobin	Mus musculus	36-47
23182882-6	2013	Moreover, a cAMP response element (CRE) site located at -854 in the promoter region of mouse Ngb gene was found to be responsible for both basal and CREB-induced Ngb promoter activity.	Cyclic AMP	12-16	neuroglobin	Mus musculus	93-96
23182882-6	2013	Moreover, a cAMP response element (CRE) site located at -854 in the promoter region of mouse Ngb gene was found to be responsible for both basal and CREB-induced Ngb promoter activity.	Cyclic AMP	12-16	neuroglobin	Mus musculus	162-165
22816983-1	2012	Neuroglobin is a hypoxia-inducible O(2)-binding protein with neuroprotective effects in cell and animal models of stroke and Alzheimer"s disease.	o(2)	35-39	neuroglobin	Mus musculus	0-11
22659017-0	2012	Mitochondrial distribution of neuroglobin and its response to oxygen-glucose deprivation in primary-cultured mouse cortical neurons.	oxygen-glucose	62-76	neuroglobin	Mus musculus	30-41
21967817-7	2011	Constitutive overexpression of NGB in transgenic mice prevented RGC damage induced by glutamate cytotoxicity in vitro and/or by chronic IOP elevation in vivo.	Glutamic Acid	86-95	neuroglobin	Mus musculus	31-34
21967817-8	2011	Moreover, overexpression of NGB attenuated ocular hypertension-induced superoxide production and the associated decrease in ATP levels in mice, suggesting that NGB acts as an endogenous neuroprotectant to reduce oxidative stress and improve mitochondrial function, thereby promoting RGC survival.	Superoxides	71-81	neuroglobin	Mus musculus	28-31
21967817-8	2011	Moreover, overexpression of NGB attenuated ocular hypertension-induced superoxide production and the associated decrease in ATP levels in mice, suggesting that NGB acts as an endogenous neuroprotectant to reduce oxidative stress and improve mitochondrial function, thereby promoting RGC survival.	Adenosine Triphosphate	124-127	neuroglobin	Mus musculus	28-31
21093435-8	2011	Compared with the Ngb- and saline-treated group, the group with TAT-Ngb treated 2h before MCAO showed significantly less brain infarct volume and had better neurologic outcomes (p<0.05).	Sodium Chloride	27-33	neuroglobin	Mus musculus	68-71
21093435-8	2011	Compared with the Ngb- and saline-treated group, the group with TAT-Ngb treated 2h before MCAO showed significantly less brain infarct volume and had better neurologic outcomes (p<0.05).	Deuterium	80-82	neuroglobin	Mus musculus	68-71
21228614-1	2011	Neuroglobin (Ngb) is an intracellular, oxygen-binding neuronal protein with protective effects against ischemia and related pathological processes.	Oxygen	39-45	neuroglobin	Mus musculus	0-11
21228614-1	2011	Neuroglobin (Ngb) is an intracellular, oxygen-binding neuronal protein with protective effects against ischemia and related pathological processes.	Oxygen	39-45	neuroglobin	Mus musculus	13-16
21228614-3	2011	In addition to deferoxamine, which was shown previously to enhance Ngb levels, Ngb expression was increased by the short-chain fatty acids cinnamic acid and valproic acid (>= 100 mumol/l), but not by other short-chain fatty acids, histone deacetylase inhibitors, or anticonvulsants.	Deferoxamine	15-27	neuroglobin	Mus musculus	67-70
21228614-3	2011	In addition to deferoxamine, which was shown previously to enhance Ngb levels, Ngb expression was increased by the short-chain fatty acids cinnamic acid and valproic acid (>= 100 mumol/l), but not by other short-chain fatty acids, histone deacetylase inhibitors, or anticonvulsants.	Fatty Acids, Volatile	115-138	neuroglobin	Mus musculus	79-82
21228614-3	2011	In addition to deferoxamine, which was shown previously to enhance Ngb levels, Ngb expression was increased by the short-chain fatty acids cinnamic acid and valproic acid (>= 100 mumol/l), but not by other short-chain fatty acids, histone deacetylase inhibitors, or anticonvulsants.	cinnamic acid	139-152	neuroglobin	Mus musculus	79-82
21228614-3	2011	In addition to deferoxamine, which was shown previously to enhance Ngb levels, Ngb expression was increased by the short-chain fatty acids cinnamic acid and valproic acid (>= 100 mumol/l), but not by other short-chain fatty acids, histone deacetylase inhibitors, or anticonvulsants.	Valproic Acid	157-170	neuroglobin	Mus musculus	79-82
21228614-3	2011	In addition to deferoxamine, which was shown previously to enhance Ngb levels, Ngb expression was increased by the short-chain fatty acids cinnamic acid and valproic acid (>= 100 mumol/l), but not by other short-chain fatty acids, histone deacetylase inhibitors, or anticonvulsants.	Fatty Acids, Volatile	209-232	neuroglobin	Mus musculus	79-82
22164238-1	2011	BACKGROUND: Neuroglobin (Ngb), a neuron-specific globin that binds oxygen in vitro, has been proposed to play a key role in neuronal survival following hypoxic and ischemic insults in the brain.	Oxygen	67-73	neuroglobin	Mus musculus	12-23
22164238-1	2011	BACKGROUND: Neuroglobin (Ngb), a neuron-specific globin that binds oxygen in vitro, has been proposed to play a key role in neuronal survival following hypoxic and ischemic insults in the brain.	Oxygen	67-73	neuroglobin	Mus musculus	25-28
21058400-0	2011	Distal mutation modulates the heme sliding in mouse neuroglobin investigated by molecular dynamics simulation.	Heme	30-34	neuroglobin	Mus musculus	52-63
21058400-2	2011	Ngb can reversibly bind small ligands such as O2 and CO to the heme iron by replacing the distal histidine which is bound to the iron as the endogenous ligand.	Oxygen	46-48	neuroglobin	Mus musculus	0-3
21058400-2	2011	Ngb can reversibly bind small ligands such as O2 and CO to the heme iron by replacing the distal histidine which is bound to the iron as the endogenous ligand.	Heme	63-67	neuroglobin	Mus musculus	0-3
21058400-2	2011	Ngb can reversibly bind small ligands such as O2 and CO to the heme iron by replacing the distal histidine which is bound to the iron as the endogenous ligand.	Iron	68-72	neuroglobin	Mus musculus	0-3
21058400-2	2011	Ngb can reversibly bind small ligands such as O2 and CO to the heme iron by replacing the distal histidine which is bound to the iron as the endogenous ligand.	Histidine	97-106	neuroglobin	Mus musculus	0-3
21058400-2	2011	Ngb can reversibly bind small ligands such as O2 and CO to the heme iron by replacing the distal histidine which is bound to the iron as the endogenous ligand.	Iron	129-133	neuroglobin	Mus musculus	0-3
21058400-7	2011	The work elucidates that the key residues K67 at E10 and H64 at E7 are significant in modulating the heme sliding and hence the structural and physiological function of Ngb.	Heme	101-105	neuroglobin	Mus musculus	169-172
20571522-10	2010	After ischemia-reperfusion, CA1 ROS/RNS production and lipid peroxidation were markedly decreased in Ngb transgenic mice compared with wild-type mice.	Reactive Oxygen Species	32-35	neuroglobin	Mus musculus	101-104
20571522-10	2010	After ischemia-reperfusion, CA1 ROS/RNS production and lipid peroxidation were markedly decreased in Ngb transgenic mice compared with wild-type mice.	Reactive Nitrogen Species	36-39	neuroglobin	Mus musculus	101-104
25616953-3	2016	We found increased ATP production and decreased glycolysis in Ngb-overexpressing immortalized murine hippocampal cell line (HT-22), in parallel with inhibition of AMP-activated protein kinase (AMPK) signaling and activation of acetyl-CoA carboxylase (ACC).	Adenosine Triphosphate	19-22	neuroglobin	Mus musculus	62-65
25616953-4	2016	In addition, lipid and glycogen content was increased in Ngb-overexpressing HT-22 cells.	Glycogen	23-31	neuroglobin	Mus musculus	57-60
24642455-2	2014	One potential neuroprotective mechanism is to increase oxygen binding proteins such as neuroglobin.	Oxygen	55-61	neuroglobin	Mus musculus	87-98
24642455-3	2014	Neuroglobin has a high affinity for oxygen, is an effective free radical scavenger, and is neuroprotective within the brain following hypoxia and ischemia.	Oxygen	36-42	neuroglobin	Mus musculus	0-11
24730682-6	2014	RESULTS: Cortical mitochondria from Ngb transgene, better maintained ATP synthesis-linked oxygen consumption and unlike wild type mitochondria did not increase futile oxygen consumption feeding the proton leak, reflecting lesser smoke-induced mitochondrial compromise.	Adenosine Triphosphate	69-72	neuroglobin	Mus musculus	36-39
24730682-6	2014	RESULTS: Cortical mitochondria from Ngb transgene, better maintained ATP synthesis-linked oxygen consumption and unlike wild type mitochondria did not increase futile oxygen consumption feeding the proton leak, reflecting lesser smoke-induced mitochondrial compromise.	Oxygen	90-96	neuroglobin	Mus musculus	36-39
24316858-10	2013	The genes that were up regulated in the oxygen carriers cluster (12 genes) were: Hbq1, Mb, Ngb, Slc38a1 and Xirp1.	Oxygen	40-46	neuroglobin	Mus musculus	91-94
23612353-1	2013	Neuroglobin (Ngb), a neuron-specific heme-binding protein that binds O2, CO and NO reversibly, and promotes in vivo and in vitro cell survival after hypoxic and ischaemic insult.	Oxygen	69-71	neuroglobin	Mus musculus	0-11
23612353-1	2013	Neuroglobin (Ngb), a neuron-specific heme-binding protein that binds O2, CO and NO reversibly, and promotes in vivo and in vitro cell survival after hypoxic and ischaemic insult.	Oxygen	69-71	neuroglobin	Mus musculus	13-16
23612353-1	2013	Neuroglobin (Ngb), a neuron-specific heme-binding protein that binds O2, CO and NO reversibly, and promotes in vivo and in vitro cell survival after hypoxic and ischaemic insult.	Carbon Monoxide	73-75	neuroglobin	Mus musculus	0-11
23612353-1	2013	Neuroglobin (Ngb), a neuron-specific heme-binding protein that binds O2, CO and NO reversibly, and promotes in vivo and in vitro cell survival after hypoxic and ischaemic insult.	Carbon Monoxide	73-75	neuroglobin	Mus musculus	13-16
23639789-0	2013	Neuroglobin overexpression inhibits oxygen-glucose deprivation-induced mitochondrial permeability transition pore opening in primary cultured mouse cortical neurons.	Oxygen	36-42	neuroglobin	Mus musculus	0-11
23639789-0	2013	Neuroglobin overexpression inhibits oxygen-glucose deprivation-induced mitochondrial permeability transition pore opening in primary cultured mouse cortical neurons.	Glucose	43-50	neuroglobin	Mus musculus	0-11
23639789-7	2013	Same as CsA pretreatment, Ngb overexpression significantly reduced OGD-induced mPTP opening markers including mitochondria swelling, mitochondrial NAD(+) release, and cytochrome c (Cyt c) release in primary cultured neurons.	1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine	79-83	neuroglobin	Mus musculus	26-29
23639789-7	2013	Same as CsA pretreatment, Ngb overexpression significantly reduced OGD-induced mPTP opening markers including mitochondria swelling, mitochondrial NAD(+) release, and cytochrome c (Cyt c) release in primary cultured neurons.	NAD	147-153	neuroglobin	Mus musculus	26-29
23639789-8	2013	Recombinant Ngb incubation significantly reduced OGD-induced NAD(+) release and Cyt c release from isolated mitochondria.	NAD	61-67	neuroglobin	Mus musculus	12-15
23639789-9	2013	In contrast, Ngb knockdown significantly increased OGD-induced neuron death, and increased OGD-induced mitochondrial NAD(+) release and Cyt c release as well, and these outcomes could be rescued by CsA pretreatment.	NAD	117-123	neuroglobin	Mus musculus	13-16
22820193-1	2012	Neuroglobin (Ngb), a neuronal specific oxygen binding heme-globin, reported to be expressed at high levels in most layers of the murine retina.	Oxygen	39-45	neuroglobin	Mus musculus	0-11
22820193-1	2012	Neuroglobin (Ngb), a neuronal specific oxygen binding heme-globin, reported to be expressed at high levels in most layers of the murine retina.	Oxygen	39-45	neuroglobin	Mus musculus	13-16
22820193-2	2012	Ngb"s function is presently unknown, but based on its high expression level and oxygen binding capabilities Ngb was proposed to function as an oxygen reservoir facilitating oxygen metabolism in highly active neurons or to function as a neuroprotectant.	Oxygen	80-86	neuroglobin	Mus musculus	0-3
22820193-2	2012	Ngb"s function is presently unknown, but based on its high expression level and oxygen binding capabilities Ngb was proposed to function as an oxygen reservoir facilitating oxygen metabolism in highly active neurons or to function as a neuroprotectant.	Oxygen	80-86	neuroglobin	Mus musculus	108-111
22820193-2	2012	Ngb"s function is presently unknown, but based on its high expression level and oxygen binding capabilities Ngb was proposed to function as an oxygen reservoir facilitating oxygen metabolism in highly active neurons or to function as a neuroprotectant.	Oxygen	143-149	neuroglobin	Mus musculus	0-3
22820193-2	2012	Ngb"s function is presently unknown, but based on its high expression level and oxygen binding capabilities Ngb was proposed to function as an oxygen reservoir facilitating oxygen metabolism in highly active neurons or to function as a neuroprotectant.	Oxygen	143-149	neuroglobin	Mus musculus	108-111
22820193-2	2012	Ngb"s function is presently unknown, but based on its high expression level and oxygen binding capabilities Ngb was proposed to function as an oxygen reservoir facilitating oxygen metabolism in highly active neurons or to function as a neuroprotectant.	Oxygen	143-149	neuroglobin	Mus musculus	0-3
22820193-2	2012	Ngb"s function is presently unknown, but based on its high expression level and oxygen binding capabilities Ngb was proposed to function as an oxygen reservoir facilitating oxygen metabolism in highly active neurons or to function as a neuroprotectant.	Oxygen	143-149	neuroglobin	Mus musculus	108-111
22496809-1	2012	Neuroglobin (Ngb), a neuron-specific oxygen-binding globin with an unknown function, has been proposed to play a key role in neuronal survival.	Oxygen	37-43	neuroglobin	Mus musculus	0-11
22496809-1	2012	Neuroglobin (Ngb), a neuron-specific oxygen-binding globin with an unknown function, has been proposed to play a key role in neuronal survival.	Oxygen	37-43	neuroglobin	Mus musculus	13-16
19820972-3	2010	Structurally, neuroglobin enjoys unique features, such as bis-histidyl coordination to heme iron in the absence of exogenous ligand, heme orientational heterogeneity, and a heme sliding mechanism accompanying ligand binding.	Heme	87-91	neuroglobin	Mus musculus	14-25
19820972-3	2010	Structurally, neuroglobin enjoys unique features, such as bis-histidyl coordination to heme iron in the absence of exogenous ligand, heme orientational heterogeneity, and a heme sliding mechanism accompanying ligand binding.	Iron	92-96	neuroglobin	Mus musculus	14-25
19820972-3	2010	Structurally, neuroglobin enjoys unique features, such as bis-histidyl coordination to heme iron in the absence of exogenous ligand, heme orientational heterogeneity, and a heme sliding mechanism accompanying ligand binding.	Heme	133-137	neuroglobin	Mus musculus	14-25
19820972-3	2010	Structurally, neuroglobin enjoys unique features, such as bis-histidyl coordination to heme iron in the absence of exogenous ligand, heme orientational heterogeneity, and a heme sliding mechanism accompanying ligand binding.	Heme	133-137	neuroglobin	Mus musculus	14-25
18403737-6	2008	Malondialdehyde levels in ischemic hemispheres of Ngb-Tg were significantly reduced compared with wild-type controls at 8 hours and 22 hours after transient focal cerebral ischemia.	Malondialdehyde	0-15	neuroglobin	Mus musculus	50-53
19850349-8	2009	Compared with mouse neuroglobin, the obtained average ligand orientation of human neuroglobin reflects the changeability of heme environment for the Ngb family.	Heme	124-128	neuroglobin	Mus musculus	20-31
18538917-0	2008	Solution 1H NMR study of the active site structure for the double mutant H64Q/V68F cyanide complex from mouse neuroglobin.	Hydrogen	9-11	neuroglobin	Mus musculus	110-121
18538917-0	2008	Solution 1H NMR study of the active site structure for the double mutant H64Q/V68F cyanide complex from mouse neuroglobin.	Cyanides	83-90	neuroglobin	Mus musculus	110-121
19574997-2	2009	METHODS: A stable N2a neuroblastoma cell line expressing the Ngb-siRNA plasmid (N2a/Ngb-siRNA) was established by neomycin screening.	Neomycin	114-122	neuroglobin	Mus musculus	61-64
19574997-9	2009	A WST-8 assay demonstrated that viability was significantly decreased in N2a/Ngb-siRNA cells and N2a cells transiently transfected with Ngb-siRNA plasmids compared with controls following hydrogen peroxide treatment.	Hydrogen Peroxide	188-205	neuroglobin	Mus musculus	136-139
19574997-10	2009	An LDH assay demonstrated a time-dependent increase in the death of Ngb-siRNA-transfected N2a cells following hydrogen peroxide treatment.	Hydrogen Peroxide	110-127	neuroglobin	Mus musculus	68-71
19574997-11	2009	Hoechst staining demonstrated that the quantity of apoptotic cells among N2a/Ngb-siRNA cells following hydrogen peroxide treatment significantly increased compared with controls.	hoechst	0-7	neuroglobin	Mus musculus	77-80
19574997-11	2009	Hoechst staining demonstrated that the quantity of apoptotic cells among N2a/Ngb-siRNA cells following hydrogen peroxide treatment significantly increased compared with controls.	Hydrogen Peroxide	103-120	neuroglobin	Mus musculus	77-80
19574997-13	2009	Transfection of 14-3-3gamma plasmids significantly enhanced the viability of N2a/Ngb-siRNA cells following hydrogen peroxide treatment compared with vector controls.	Hydrogen Peroxide	107-124	neuroglobin	Mus musculus	81-84
18198211-2	2008	Neuroglobin (Ngb), a recently discovered vertebrate globin expressed predominantly in the brain, shows increased expression in neurons in response to oxygen deprivation and protects neurons from ischemic and hypoxic death.	Oxygen	150-156	neuroglobin	Mus musculus	0-11
18198211-2	2008	Neuroglobin (Ngb), a recently discovered vertebrate globin expressed predominantly in the brain, shows increased expression in neurons in response to oxygen deprivation and protects neurons from ischemic and hypoxic death.	Oxygen	150-156	neuroglobin	Mus musculus	13-16
18403737-7	2008	Compared with wild-type controls, brain infarction volumes 1 day and 14 days after transient focal cerebral ischemia were significantly reduced in Ngb-Tg mice.	Thioguanine	151-153	neuroglobin	Mus musculus	147-150
18035490-0	2008	Neuroglobin protects against nitric oxide toxicity.	Nitric Oxide	29-41	neuroglobin	Mus musculus	0-11
18035490-6	2008	The results suggest that the ability of Ngb to neutralize the neurotoxic effects of reactive nitrogen species may be an important contributor to its neuroprotective properties.	Reactive Nitrogen Species	84-109	neuroglobin	Mus musculus	40-43
15162488-1	2004	Neuroglobin, a recently discovered globin predominantly expressed in neuronal tissue of vertebrates, binds small, gaseous ligands at the sixth coordination position of the heme iron.	Iron	177-181	neuroglobin	Mus musculus	0-11
17286577-7	2007	In eyes, the negative correlation, after reoxygenation, between neuroglobin protein level and H(2)O(2) concentration is a first proof of a reactive oxygen species-scavenging function for neuroglobin.	Hydrogen Peroxide	94-102	neuroglobin	Mus musculus	64-75
17286577-7	2007	In eyes, the negative correlation, after reoxygenation, between neuroglobin protein level and H(2)O(2) concentration is a first proof of a reactive oxygen species-scavenging function for neuroglobin.	Hydrogen Peroxide	94-102	neuroglobin	Mus musculus	187-198
17286577-7	2007	In eyes, the negative correlation, after reoxygenation, between neuroglobin protein level and H(2)O(2) concentration is a first proof of a reactive oxygen species-scavenging function for neuroglobin.	Reactive Oxygen Species	139-162	neuroglobin	Mus musculus	64-75
17286577-7	2007	In eyes, the negative correlation, after reoxygenation, between neuroglobin protein level and H(2)O(2) concentration is a first proof of a reactive oxygen species-scavenging function for neuroglobin.	Reactive Oxygen Species	139-162	neuroglobin	Mus musculus	187-198
16586113-0	2006	The heme environment of mouse neuroglobin: histidine imidazole plane orientations obtained from solution NMR and EPR spectroscopy as compared with X-ray crystallography.	Heme	4-8	neuroglobin	Mus musculus	30-41
16586113-0	2006	The heme environment of mouse neuroglobin: histidine imidazole plane orientations obtained from solution NMR and EPR spectroscopy as compared with X-ray crystallography.	histidine imidazole	43-62	neuroglobin	Mus musculus	30-41
16596390-0	2006	Analyzing heme proteins using EPR techniques: the heme-pocket structure of ferric mouse neuroglobin.	Heme	10-14	neuroglobin	Mus musculus	88-99
16596390-4	2006	In combination with the hyperfine matrices of the imidazole protons, the 14N EPR parameters reveal structural information on the heme pocket of mNgb that is in agreement with previous X-ray diffraction data on neuroglobins.	imidazole	50-59	neuroglobin	Mus musculus	144-148
16596390-4	2006	In combination with the hyperfine matrices of the imidazole protons, the 14N EPR parameters reveal structural information on the heme pocket of mNgb that is in agreement with previous X-ray diffraction data on neuroglobins.	4-(4-methylpiperazin-1-yl)benzoic acid	73-76	neuroglobin	Mus musculus	144-148
16596390-4	2006	In combination with the hyperfine matrices of the imidazole protons, the 14N EPR parameters reveal structural information on the heme pocket of mNgb that is in agreement with previous X-ray diffraction data on neuroglobins.	Heme	129-133	neuroglobin	Mus musculus	144-148
15548613-0	2004	The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity.	Heme	52-56	neuroglobin	Mus musculus	30-41
15548613-1	2004	Neuroglobin (Ngb), a globular heme protein expressed in the brain of vertebrates, binds oxygen reversibly, with an affinity comparable to myoglobin (Mb).	Oxygen	88-94	neuroglobin	Mus musculus	0-11
15548613-1	2004	Neuroglobin (Ngb), a globular heme protein expressed in the brain of vertebrates, binds oxygen reversibly, with an affinity comparable to myoglobin (Mb).	Oxygen	88-94	neuroglobin	Mus musculus	13-16
15548613-3	2004	Unlike in Mb, in Ngb the sixth coordination position of the heme iron is occupied by the distal histidine, in the absence of an exogenous ligand.	Heme	60-64	neuroglobin	Mus musculus	17-20
15548613-3	2004	Unlike in Mb, in Ngb the sixth coordination position of the heme iron is occupied by the distal histidine, in the absence of an exogenous ligand.	Iron	65-69	neuroglobin	Mus musculus	17-20
15548613-3	2004	Unlike in Mb, in Ngb the sixth coordination position of the heme iron is occupied by the distal histidine, in the absence of an exogenous ligand.	Histidine	96-105	neuroglobin	Mus musculus	17-20
15548613-9	2004	The heme relocation is accompanied by a significant decrease of structural disorder, especially of the EF loop, which may be the signal whereby Ngb communicates hypoxic conditions.	Heme	4-8	neuroglobin	Mus musculus	144-147
15548613-10	2004	This unexpected structural change unveils a heme-sliding mechanism of affinity control that may be of significance to understanding Ngb"s role in the pathophysiology of the brain.	Heme	44-48	neuroglobin	Mus musculus	132-135
18025470-2	2007	To investigate the spectrum and mechanism of Ngb"s neuroprotective action, we studied the effect of transgenic overexpression of Ngb on NMDA and beta-amyloid (Abeta) toxicity in murine cortical neuron cultures in vitro and on the phenotype of Alzheimer"s disease (AD) transgenic (APP(Sw,Ind)) mice.	N-Methylaspartate	136-140	neuroglobin	Mus musculus	129-132
18025470-3	2007	Compared with cortical neuron cultures from wild-type mice, cultures from Ngb-overexpressing transgenic (Ngb-Tg mice) were resistant to the toxic effects of NMDA and Abeta(25-35), as measured by polarization of cell membrane lipid rafts, mitochondrial aggregation, lactate dehydrogenase release, and nuclear fragmentation.	N-Methylaspartate	157-161	neuroglobin	Mus musculus	74-77
18025470-3	2007	Compared with cortical neuron cultures from wild-type mice, cultures from Ngb-overexpressing transgenic (Ngb-Tg mice) were resistant to the toxic effects of NMDA and Abeta(25-35), as measured by polarization of cell membrane lipid rafts, mitochondrial aggregation, lactate dehydrogenase release, and nuclear fragmentation.	N-Methylaspartate	157-161	neuroglobin	Mus musculus	105-108
18025470-3	2007	Compared with cortical neuron cultures from wild-type mice, cultures from Ngb-overexpressing transgenic (Ngb-Tg mice) were resistant to the toxic effects of NMDA and Abeta(25-35), as measured by polarization of cell membrane lipid rafts, mitochondrial aggregation, lactate dehydrogenase release, and nuclear fragmentation.	UNII-042A8N37WH	166-171	neuroglobin	Mus musculus	74-77
18025470-3	2007	Compared with cortical neuron cultures from wild-type mice, cultures from Ngb-overexpressing transgenic (Ngb-Tg mice) were resistant to the toxic effects of NMDA and Abeta(25-35), as measured by polarization of cell membrane lipid rafts, mitochondrial aggregation, lactate dehydrogenase release, and nuclear fragmentation.	UNII-042A8N37WH	166-171	neuroglobin	Mus musculus	105-108
18025470-4	2007	In addition, compared with APP(Sw,Ind) mice, double-transgenic (Ngb-Tg x APP(Sw,Ind)) mice showed reductions in thioflavin-S-stained extracellular Abeta deposits, decreased levels of Abeta(1-40) and Abeta(1-42), and improved behavioral performance in a Y-maze test of spontaneous alternations.	thioflavin T	112-124	neuroglobin	Mus musculus	64-67
18025470-6	2007	Ngb may protect neurons from NMDA and Abeta toxicity by inhibiting the formation of a death-signaling membrane complex, and interventions that increase Ngb expression could have therapeutic application in AD and other neurodegenerative disorders.	N-Methylaspartate	29-33	neuroglobin	Mus musculus	0-3
17468165-0	2007	Molecular dynamics simulation of deoxy and carboxy murine neuroglobin in water.	Water	73-78	neuroglobin	Mus musculus	58-69
17468165-5	2007	Oxygen, nitric oxide, or carbon monoxide can displace the distal histidine which, in ferrous Ngb as well as in ferric Ngb, is bound to the iron, yielding a reversible adduct.	Oxygen	0-6	neuroglobin	Mus musculus	93-96
17468165-5	2007	Oxygen, nitric oxide, or carbon monoxide can displace the distal histidine which, in ferrous Ngb as well as in ferric Ngb, is bound to the iron, yielding a reversible adduct.	Oxygen	0-6	neuroglobin	Mus musculus	118-121
17468165-5	2007	Oxygen, nitric oxide, or carbon monoxide can displace the distal histidine which, in ferrous Ngb as well as in ferric Ngb, is bound to the iron, yielding a reversible adduct.	Nitric Oxide	8-20	neuroglobin	Mus musculus	93-96
17468165-5	2007	Oxygen, nitric oxide, or carbon monoxide can displace the distal histidine which, in ferrous Ngb as well as in ferric Ngb, is bound to the iron, yielding a reversible adduct.	Nitric Oxide	8-20	neuroglobin	Mus musculus	118-121
17468165-5	2007	Oxygen, nitric oxide, or carbon monoxide can displace the distal histidine which, in ferrous Ngb as well as in ferric Ngb, is bound to the iron, yielding a reversible adduct.	Carbon Monoxide	25-40	neuroglobin	Mus musculus	93-96
17468165-5	2007	Oxygen, nitric oxide, or carbon monoxide can displace the distal histidine which, in ferrous Ngb as well as in ferric Ngb, is bound to the iron, yielding a reversible adduct.	Carbon Monoxide	25-40	neuroglobin	Mus musculus	118-121
17468165-5	2007	Oxygen, nitric oxide, or carbon monoxide can displace the distal histidine which, in ferrous Ngb as well as in ferric Ngb, is bound to the iron, yielding a reversible adduct.	Histidine	65-74	neuroglobin	Mus musculus	93-96
17468165-5	2007	Oxygen, nitric oxide, or carbon monoxide can displace the distal histidine which, in ferrous Ngb as well as in ferric Ngb, is bound to the iron, yielding a reversible adduct.	Histidine	65-74	neuroglobin	Mus musculus	118-121
17468165-5	2007	Oxygen, nitric oxide, or carbon monoxide can displace the distal histidine which, in ferrous Ngb as well as in ferric Ngb, is bound to the iron, yielding a reversible adduct.	Iron	139-143	neuroglobin	Mus musculus	93-96
17468165-5	2007	Oxygen, nitric oxide, or carbon monoxide can displace the distal histidine which, in ferrous Ngb as well as in ferric Ngb, is bound to the iron, yielding a reversible adduct.	Iron	139-143	neuroglobin	Mus musculus	118-121
17468165-6	2007	Recent crystallographic data on carboxy Ngb show that binding of an exogenous ligand is associated to structural changes involving heme sliding and a topological reorganization of the internal cavities; in particular, the huge internal tunnel that connects the bulk with the active site, peculiar to Ngb, is heavily reorganized.	Heme	131-135	neuroglobin	Mus musculus	40-43
17468165-7	2007	We report the results of extended (90 ns) molecular dynamics simulations in water of ferrous deoxy and carboxy murine neuroglobin, which are both coordinated on the distal site, in the latter case by CO and in the former one by the distal His(64)(E7).	Water	76-81	neuroglobin	Mus musculus	118-129
17468165-7	2007	We report the results of extended (90 ns) molecular dynamics simulations in water of ferrous deoxy and carboxy murine neuroglobin, which are both coordinated on the distal site, in the latter case by CO and in the former one by the distal His(64)(E7).	Histidine	239-242	neuroglobin	Mus musculus	118-129
16094504-0	2005	Effects of neuroglobin gene transfer in vivo on hearing response properties of neurons in the inferior colliculus in mice after administration of sodium salicylate.	Sodium Salicylate	146-163	neuroglobin	Mus musculus	11-22
16094504-17	2005	In vivo transfer of NGB gene reverses the change of intensity-rate functions, intensity-latency functions and the code styles after administration of sodium salicylate in IC neurons in mice.	Sodium Salicylate	150-167	neuroglobin	Mus musculus	20-23
15657899-1	2005	Neuroglobin (Ngb), a recently discovered intracellular respiratory globin in neurons, may play a crucial role in oxygen homeostasis in the brain.	Oxygen	113-119	neuroglobin	Mus musculus	0-11
15657899-1	2005	Neuroglobin (Ngb), a recently discovered intracellular respiratory globin in neurons, may play a crucial role in oxygen homeostasis in the brain.	Oxygen	113-119	neuroglobin	Mus musculus	13-16
15657899-5	2005	The discovery of Ngb in astrocytes may provide some insight into how oxygen homeostasis is regulated in the brain.	Oxygen	69-75	neuroglobin	Mus musculus	17-20
15663964-8	2005	While neuroglobin seems to be associated with oxygen consumption, a respiratory function of cytoglobin is unlikely.	Oxygen	46-52	neuroglobin	Mus musculus	6-17
15162488-1	2004	Neuroglobin, a recently discovered globin predominantly expressed in neuronal tissue of vertebrates, binds small, gaseous ligands at the sixth coordination position of the heme iron.	Heme	172-176	neuroglobin	Mus musculus	0-11
15016813-1	2004	We have examined the effects of active site residues on ligand binding to the heme iron of mouse neuroglobin using steady-state and time-resolved visible spectroscopy.	Heme	78-82	neuroglobin	Mus musculus	97-108
15016813-1	2004	We have examined the effects of active site residues on ligand binding to the heme iron of mouse neuroglobin using steady-state and time-resolved visible spectroscopy.	Iron	83-87	neuroglobin	Mus musculus	97-108
12837059-0	2003	Solution 1h NMR characterization of equilibrium heme orientational disorder with functional consequences in mouse neuroglobin.	Hydrogen	9-11	neuroglobin	Mus musculus	114-125
12837059-1	2003	The solution 1H NMR spectrum of oxidized (met) mouse neuroglobin, metNgb, demonstrates that it is low-spin and hexacoordinate with strong spectral similarities to ferricytochrome b5.	Hydrogen	13-15	neuroglobin	Mus musculus	53-64
11473111-0	2001	The heme environment of mouse neuroglobin.	Heme	4-8	neuroglobin	Mus musculus	30-41
12480932-0	2003	Nitric oxide binding properties of neuroglobin.	Nitric Oxide	0-12	neuroglobin	Mus musculus	35-46
12480932-3	2003	Combined electron paramagnetic resonance and optical measurements show that, in Escherichia coli cell cultures with low O(2) concentration overexpressing wild-type mouse recombinant neuroglobin, the heme protein is mainly in a hexacoordinated deoxy ferrous form (F8His-Fe(2+)-E7His), whereby for a small fraction of the protein the endogenous protein ligand is replaced by NO.	f8his	263-268	neuroglobin	Mus musculus	182-193
12480932-3	2003	Combined electron paramagnetic resonance and optical measurements show that, in Escherichia coli cell cultures with low O(2) concentration overexpressing wild-type mouse recombinant neuroglobin, the heme protein is mainly in a hexacoordinated deoxy ferrous form (F8His-Fe(2+)-E7His), whereby for a small fraction of the protein the endogenous protein ligand is replaced by NO.	ammonium ferrous sulfate	269-275	neuroglobin	Mus musculus	182-193
12480932-3	2003	Combined electron paramagnetic resonance and optical measurements show that, in Escherichia coli cell cultures with low O(2) concentration overexpressing wild-type mouse recombinant neuroglobin, the heme protein is mainly in a hexacoordinated deoxy ferrous form (F8His-Fe(2+)-E7His), whereby for a small fraction of the protein the endogenous protein ligand is replaced by NO.	e7his	276-281	neuroglobin	Mus musculus	182-193
12480932-4	2003	Analogous studies for mutated neuroglobin (mutation of E7-His to Leu, Val, or Gln) reveal the predominant presence of the nitrosyl ferrous form.	Histidine	58-61	neuroglobin	Mus musculus	30-41
12480932-4	2003	Analogous studies for mutated neuroglobin (mutation of E7-His to Leu, Val, or Gln) reveal the predominant presence of the nitrosyl ferrous form.	Leucine	65-68	neuroglobin	Mus musculus	30-41
12480932-4	2003	Analogous studies for mutated neuroglobin (mutation of E7-His to Leu, Val, or Gln) reveal the predominant presence of the nitrosyl ferrous form.	Valine	70-73	neuroglobin	Mus musculus	30-41
12480932-4	2003	Analogous studies for mutated neuroglobin (mutation of E7-His to Leu, Val, or Gln) reveal the predominant presence of the nitrosyl ferrous form.	Glutamine	78-81	neuroglobin	Mus musculus	30-41
12480932-5	2003	After sonication of the cells wild-type neuroglobin oxidizes rapidly to the hexacoordinated ferric form, whereas NO ligation initially protects the mutants from oxidation.	Ferric enterobactin ion	92-98	neuroglobin	Mus musculus	40-51
11473128-1	2001	Neuroglobin is a recently discovered member of the globin superfamily that is suggested to enhance the O(2) supply of the vertebrate brain.	o(2)	103-107	neuroglobin	Mus musculus	0-11
11473128-2	2001	Spectral measurements with human and mouse recombinant neuroglobin provide evidence for a hexacoordinated deoxy ferrous (Fe(2+)) form, indicating a His-Fe(2+)-His binding scheme.	deoxy ferrous	106-119	neuroglobin	Mus musculus	55-66
11473128-2	2001	Spectral measurements with human and mouse recombinant neuroglobin provide evidence for a hexacoordinated deoxy ferrous (Fe(2+)) form, indicating a His-Fe(2+)-His binding scheme.	ammonium ferrous sulfate	121-127	neuroglobin	Mus musculus	55-66
11473128-2	2001	Spectral measurements with human and mouse recombinant neuroglobin provide evidence for a hexacoordinated deoxy ferrous (Fe(2+)) form, indicating a His-Fe(2+)-His binding scheme.	Histidine	148-151	neuroglobin	Mus musculus	55-66
11473128-2	2001	Spectral measurements with human and mouse recombinant neuroglobin provide evidence for a hexacoordinated deoxy ferrous (Fe(2+)) form, indicating a His-Fe(2+)-His binding scheme.	ammonium ferrous sulfate	152-158	neuroglobin	Mus musculus	55-66
11473128-2	2001	Spectral measurements with human and mouse recombinant neuroglobin provide evidence for a hexacoordinated deoxy ferrous (Fe(2+)) form, indicating a His-Fe(2+)-His binding scheme.	Histidine	159-162	neuroglobin	Mus musculus	55-66
11473128-4	2001	The ferric (Fe(3+)) form of neuroglobin is also hexacoordinated with the protein ligand E7-His and does not exhibit pH dependence.	Ferric enterobactin ion	4-10	neuroglobin	Mus musculus	28-39
11473128-4	2001	The ferric (Fe(3+)) form of neuroglobin is also hexacoordinated with the protein ligand E7-His and does not exhibit pH dependence.	ferric sulfate	12-18	neuroglobin	Mus musculus	28-39
11473128-4	2001	The ferric (Fe(3+)) form of neuroglobin is also hexacoordinated with the protein ligand E7-His and does not exhibit pH dependence.	Histidine	91-94	neuroglobin	Mus musculus	28-39
11473128-10	2001	Under natural conditions, recombinant mouse neuroglobin occurs as a monomer with disulfide-dependent formation of dimers.	Disulfides	81-90	neuroglobin	Mus musculus	44-55
12486081-3	2002	Although the functional role of this novel member of the globin family remains unclear, neuroglobin contains a heme-binding domain and may participate in diverse processes such as oxygen transport, oxygen storage, nitric oxide detoxification, or modulation of terminal oxidase activity.	Heme	111-115	neuroglobin	Mus musculus	88-99
12486081-3	2002	Although the functional role of this novel member of the globin family remains unclear, neuroglobin contains a heme-binding domain and may participate in diverse processes such as oxygen transport, oxygen storage, nitric oxide detoxification, or modulation of terminal oxidase activity.	Oxygen	180-186	neuroglobin	Mus musculus	88-99
12486081-3	2002	Although the functional role of this novel member of the globin family remains unclear, neuroglobin contains a heme-binding domain and may participate in diverse processes such as oxygen transport, oxygen storage, nitric oxide detoxification, or modulation of terminal oxidase activity.	Oxygen	198-204	neuroglobin	Mus musculus	88-99
12486081-3	2002	Although the functional role of this novel member of the globin family remains unclear, neuroglobin contains a heme-binding domain and may participate in diverse processes such as oxygen transport, oxygen storage, nitric oxide detoxification, or modulation of terminal oxidase activity.	Nitric Oxide	214-226	neuroglobin	Mus musculus	88-99
11473111-3	2001	To characterize the structure/function relationships of this new heme protein, we have used resonance Raman spectroscopy to determine the structure of the heme environment in Ngb from mice.	Heme	65-69	neuroglobin	Mus musculus	175-178
11473111-3	2001	To characterize the structure/function relationships of this new heme protein, we have used resonance Raman spectroscopy to determine the structure of the heme environment in Ngb from mice.	Heme	155-159	neuroglobin	Mus musculus	175-178
11473111-6	2001	Based on the Fe-C-O frequencies of the closed conformation of Ngb, a highly polar distal environment is indicated from which the O(2) off-rate is predicted to be lower than that of Mb.	fe-c-o	13-19	neuroglobin	Mus musculus	62-65
11473111-8	2001	These structural properties of the heme pocket of Ngb are discussed with respect to its proposed in vivo oxygen delivery function.	Heme	35-39	neuroglobin	Mus musculus	50-53
11473111-8	2001	These structural properties of the heme pocket of Ngb are discussed with respect to its proposed in vivo oxygen delivery function.	Oxygen	105-111	neuroglobin	Mus musculus	50-53
34751416-11	2022	The results indicated that PD protected neuronal cells from H2O2 by activating CREB/Ngb signaling in neuronal cells, indicating that PD has a neuroprotective effect against neurodegenerative diseases.	Hydrogen Peroxide	60-64	neuroglobin	Mus musculus	84-87
11029004-4	2000	Mouse neuroglobin is a monomer with a high oxygen affinity (half saturation pressure, P50 approximately 2 torr).	Oxygen	43-49	neuroglobin	Mus musculus	6-17
22548980-1	2012	Among endogenous adaptive systems to hypoxia, neuroglobin, a recently discovered heme protein, was suggested as a novel oxygen-dependent neuroprotectant.	Oxygen	120-126	neuroglobin	Mus musculus	46-57
22548980-5	2012	Exposure of the immature brains (P0, P7) to acute (8% O(2), 6h) and chronic systemic hypoxia (10% O(2), 7 days) led to differential activation of neuroglobin varying with maturational stage (P0, P7) and severity of hypoxia.	Oxygen	54-58	neuroglobin	Mus musculus	146-157
22548980-5	2012	Exposure of the immature brains (P0, P7) to acute (8% O(2), 6h) and chronic systemic hypoxia (10% O(2), 7 days) led to differential activation of neuroglobin varying with maturational stage (P0, P7) and severity of hypoxia.	Oxygen	98-102	neuroglobin	Mus musculus	146-157
34751416-0	2022	Polydatin protects neuronal cells from hydrogen peroxide damage by activating CREB/Ngb signaling.	polydatin	0-9	neuroglobin	Mus musculus	83-86
34751416-4	2022	The current study suggested that PD activates AKT/cAMP response element-binding protein (CREB) signaling and induces neuroglobin (Ngb) to protect neuronal cells from hydrogen peroxide (H2O2) in vitro.	Hydrogen Peroxide	166-183	neuroglobin	Mus musculus	117-128
34751416-4	2022	The current study suggested that PD activates AKT/cAMP response element-binding protein (CREB) signaling and induces neuroglobin (Ngb) to protect neuronal cells from hydrogen peroxide (H2O2) in vitro.	Hydrogen Peroxide	166-183	neuroglobin	Mus musculus	130-133
34751416-4	2022	The current study suggested that PD activates AKT/cAMP response element-binding protein (CREB) signaling and induces neuroglobin (Ngb) to protect neuronal cells from hydrogen peroxide (H2O2) in vitro.	Hydrogen Peroxide	185-189	neuroglobin	Mus musculus	117-128
34751416-4	2022	The current study suggested that PD activates AKT/cAMP response element-binding protein (CREB) signaling and induces neuroglobin (Ngb) to protect neuronal cells from hydrogen peroxide (H2O2) in vitro.	Hydrogen Peroxide	185-189	neuroglobin	Mus musculus	130-133
34751416-10	2022	Finally, Ngb knockdown largely attenuated the neuroprotective role of PD against H2O2.	polydatin	70-72	neuroglobin	Mus musculus	9-12
34943874-3	2021	Therefore, the heme-based reactivity of Ngb is modulated by the dissociation of the distal HisE7-heme-Fe bond, which reflects in turn the redox state of the cell.	Heme	15-19	neuroglobin	Mus musculus	40-43
34943874-3	2021	Therefore, the heme-based reactivity of Ngb is modulated by the dissociation of the distal HisE7-heme-Fe bond, which reflects in turn the redox state of the cell.	hise7	91-96	neuroglobin	Mus musculus	40-43
34943874-3	2021	Therefore, the heme-based reactivity of Ngb is modulated by the dissociation of the distal HisE7-heme-Fe bond, which reflects in turn the redox state of the cell.	Heme	97-101	neuroglobin	Mus musculus	40-43
34943874-3	2021	Therefore, the heme-based reactivity of Ngb is modulated by the dissociation of the distal HisE7-heme-Fe bond, which reflects in turn the redox state of the cell.	Iron	102-104	neuroglobin	Mus musculus	40-43
34943874-4	2021	The high Ngb levels (~100-200 muM) present in the retinal ganglion cell layer and in the optic nerve facilitate the O2 buffer and delivery.	Oxygen	116-118	neuroglobin	Mus musculus	9-12
34943874-5	2021	In contrast, the very low levels of Ngb (~1 muM) in most tissues and organs support (pseudo-)enzymatic properties including NO/O2 metabolism, peroxynitrite and free radical scavenging, nitrite, hydroxylamine, hydrogen sulfide reduction, and the nitration of aromatic compounds.	Oxygen	127-129	neuroglobin	Mus musculus	36-39
34943874-5	2021	In contrast, the very low levels of Ngb (~1 muM) in most tissues and organs support (pseudo-)enzymatic properties including NO/O2 metabolism, peroxynitrite and free radical scavenging, nitrite, hydroxylamine, hydrogen sulfide reduction, and the nitration of aromatic compounds.	Peroxynitrous Acid	142-155	neuroglobin	Mus musculus	36-39
34943874-5	2021	In contrast, the very low levels of Ngb (~1 muM) in most tissues and organs support (pseudo-)enzymatic properties including NO/O2 metabolism, peroxynitrite and free radical scavenging, nitrite, hydroxylamine, hydrogen sulfide reduction, and the nitration of aromatic compounds.	Nitrites	185-192	neuroglobin	Mus musculus	36-39
34943874-5	2021	In contrast, the very low levels of Ngb (~1 muM) in most tissues and organs support (pseudo-)enzymatic properties including NO/O2 metabolism, peroxynitrite and free radical scavenging, nitrite, hydroxylamine, hydrogen sulfide reduction, and the nitration of aromatic compounds.	Hydroxylamine	194-207	neuroglobin	Mus musculus	36-39
34943874-5	2021	In contrast, the very low levels of Ngb (~1 muM) in most tissues and organs support (pseudo-)enzymatic properties including NO/O2 metabolism, peroxynitrite and free radical scavenging, nitrite, hydroxylamine, hydrogen sulfide reduction, and the nitration of aromatic compounds.	Hydrogen Sulfide	209-225	neuroglobin	Mus musculus	36-39
34797521-0	2022	Carbon Monoxide-Neuroglobin Axis Targeting Metabolism Against Inflammation in BV-2 Microglial Cells.	Carbon Monoxide	0-15	neuroglobin	Mus musculus	16-27
34797521-8	2022	CO-induced Ngb upregulation correlated in time with CO"s anti-inflammatory effect.	Carbon Monoxide	0-2	neuroglobin	Mus musculus	11-14
34797521-8	2022	CO-induced Ngb upregulation correlated in time with CO"s anti-inflammatory effect.	Carbon Monoxide	52-54	neuroglobin	Mus musculus	11-14
34797521-10	2022	CO-induced Ngb upregulation was independent on ROS signalling, but partially dependent on the transcriptional factor SP1.	ros	47-50	neuroglobin	Mus musculus	11-14
34584546-9	2021	In the CATH.a cells, the dexmedetomidine treatment upregulated the NGB levels.	Dexmedetomidine	25-40	neuroglobin	Mus musculus	67-70
34584546-10	2021	Moreover, upon pre-incubation with NGB and LPS stimulation, dexmedetomidine elevated cell viability.	Dexmedetomidine	60-75	neuroglobin	Mus musculus	35-38
35121559-8	2022	Downregulation of CYGB and NGB induced nitride oxide (NO) release, blocked cell cycle progression, reduced testosterone production and increased inflammatory and apoptotic pathway gene expression in the presence and absence of LPS.	nitride oxide	39-52	neuroglobin	Mus musculus	27-30
35121559-8	2022	Downregulation of CYGB and NGB induced nitride oxide (NO) release, blocked cell cycle progression, reduced testosterone production and increased inflammatory and apoptotic pathway gene expression in the presence and absence of LPS.	Testosterone	107-119	neuroglobin	Mus musculus	27-30
35121559-9	2022	On the other hand, CYGB and NGB overexpression reduced TNFalpha and COX-2 protein expressions and increased the expression of testosterone biogenesis pathway genes upon LPS stimulation.	Testosterone	126-138	neuroglobin	Mus musculus	28-31
35121559-10	2022	In addition, CYGB and NGB overexpression upregulated testosterone production.	Testosterone	53-65	neuroglobin	Mus musculus	22-25