PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
32196080-5	2020	We further show that NNT loss elicits mitochondrial dysfunction independent of substantial increases in oxidative stress, but rather marked by the diminished activities of proteins dependent on resident iron-sulfur clusters.	Iron	203-207	nicotinamide nucleotide transhydrogenase	Mus musculus	21-24
34043997-4	2021	Further comparisons between SMM from both Nnt mouse genotypes revealed that the NADPH supplied by NNT supports up to 600 pmol/mg/min of H2O2 removal under selected conditions.	Hydrogen Peroxide	136-140	nicotinamide nucleotide transhydrogenase	Mus musculus	98-101
34043997-5	2021	Surprisingly, SMM from Nnt-/- mice removed exogenous H2O2 at wild-type levels and exhibited a maintained or even decreased net emission of endogenous H2O2 when substrates that support Krebs cycle reactions were present (e.g., pyruvate plus malate or palmitoylcarnitine plus malate).	Hydrogen Peroxide	53-57	nicotinamide nucleotide transhydrogenase	Mus musculus	23-26
34043997-5	2021	Surprisingly, SMM from Nnt-/- mice removed exogenous H2O2 at wild-type levels and exhibited a maintained or even decreased net emission of endogenous H2O2 when substrates that support Krebs cycle reactions were present (e.g., pyruvate plus malate or palmitoylcarnitine plus malate).	Hydrogen Peroxide	150-154	nicotinamide nucleotide transhydrogenase	Mus musculus	23-26
34043997-5	2021	Surprisingly, SMM from Nnt-/- mice removed exogenous H2O2 at wild-type levels and exhibited a maintained or even decreased net emission of endogenous H2O2 when substrates that support Krebs cycle reactions were present (e.g., pyruvate plus malate or palmitoylcarnitine plus malate).	krebs	184-189	nicotinamide nucleotide transhydrogenase	Mus musculus	23-26
34043997-6	2021	These results may be explained by a compensation for the lack of NNT, since the total activities of concurrent NADP+-reducing enzymes (IDH2, malic enzymes and glutamate dehydrogenase) were ~70% elevated in Nnt-/- mice.	NADP	111-116	nicotinamide nucleotide transhydrogenase	Mus musculus	206-209
34043997-7	2021	Importantly, respiratory rates were similar between SMM from both Nnt genotypes despite differing NNT contributions to H2O2 removal and their implications for an evolving concept in the literature are discussed.	Hydrogen Peroxide	119-123	nicotinamide nucleotide transhydrogenase	Mus musculus	98-101
34043997-8	2021	We concluded that NNT is capable of meaningfully sustaining NADPH-dependent H2O2 removal in intact SMM.	Hydrogen Peroxide	76-80	nicotinamide nucleotide transhydrogenase	Mus musculus	18-21
34043997-9	2021	Nonetheless, if the available substrates favor non-NNT sources of NADPH, the H2O2 removal by SMM is maintained in Nnt-/- mice SMM.	Hydrogen Peroxide	77-81	nicotinamide nucleotide transhydrogenase	Mus musculus	114-117
32629517-6	2020	Both sexes of BC1 hybrids indicate that mice with Nnt wild type allele are highly sensitive to DIO and exhibit higher relative fat mass.	3,3'-Dioctadecyloxacarbocyanine perchlorate	95-98	nicotinamide nucleotide transhydrogenase	Mus musculus	50-53
32629517-7	2020	In summary, our data indicate that the Nnt mutation in mice is associated with sensitivity to DIO and fat mass.	3,3'-Dioctadecyloxacarbocyanine perchlorate	94-97	nicotinamide nucleotide transhydrogenase	Mus musculus	39-42
11513952-1	2001	Proton-pumping nicotinamide nucleotide transhydrogenase (Nnt) is a membrane-bound enzyme that catalyzes the reversible reduction of NADP(+) by NADH.	NADP	132-136	nicotinamide nucleotide transhydrogenase	Mus musculus	57-60
11513952-1	2001	Proton-pumping nicotinamide nucleotide transhydrogenase (Nnt) is a membrane-bound enzyme that catalyzes the reversible reduction of NADP(+) by NADH.	NAD	143-147	nicotinamide nucleotide transhydrogenase	Mus musculus	57-60
34043997-0	2021	NADPH supply and the contribution of NAD(P)+ transhydrogenase (NNT) to H2O2 balance in skeletal muscle mitochondria.	Hydrogen Peroxide	71-75	nicotinamide nucleotide transhydrogenase	Mus musculus	63-66
32196080-5	2020	We further show that NNT loss elicits mitochondrial dysfunction independent of substantial increases in oxidative stress, but rather marked by the diminished activities of proteins dependent on resident iron-sulfur clusters.	Sulfur	208-214	nicotinamide nucleotide transhydrogenase	Mus musculus	21-24
32196080-6	2020	These defects were associated with both NADPH availability and ROS accumulation, suggesting that NNT serves a specific role in mitigating the oxidation of these critical protein cofactors.	NADP	40-45	nicotinamide nucleotide transhydrogenase	Mus musculus	97-100
32196080-6	2020	These defects were associated with both NADPH availability and ROS accumulation, suggesting that NNT serves a specific role in mitigating the oxidation of these critical protein cofactors.	ros	63-66	nicotinamide nucleotide transhydrogenase	Mus musculus	97-100
31639438-1	2020	Here, we demonstrate that the upregulation of catalase is required to compensate for the loss of nicotinamide nucleotide transhydrogenase (NNT) to maintain hydrogen peroxide (H2O2) steady-state levels in C57BL/6J liver mitochondria.	Hydrogen Peroxide	156-173	nicotinamide nucleotide transhydrogenase	Mus musculus	97-137
31639438-1	2020	Here, we demonstrate that the upregulation of catalase is required to compensate for the loss of nicotinamide nucleotide transhydrogenase (NNT) to maintain hydrogen peroxide (H2O2) steady-state levels in C57BL/6J liver mitochondria.	Hydrogen Peroxide	156-173	nicotinamide nucleotide transhydrogenase	Mus musculus	139-142
31639438-1	2020	Here, we demonstrate that the upregulation of catalase is required to compensate for the loss of nicotinamide nucleotide transhydrogenase (NNT) to maintain hydrogen peroxide (H2O2) steady-state levels in C57BL/6J liver mitochondria.	Water	175-179	nicotinamide nucleotide transhydrogenase	Mus musculus	97-137
31639438-1	2020	Here, we demonstrate that the upregulation of catalase is required to compensate for the loss of nicotinamide nucleotide transhydrogenase (NNT) to maintain hydrogen peroxide (H2O2) steady-state levels in C57BL/6J liver mitochondria.	Water	175-179	nicotinamide nucleotide transhydrogenase	Mus musculus	139-142
31639438-2	2020	Our investigations using the closely related mouse strains C57BL/6NJ (6NJ; +NNT) and C57BL/6J (6J; -NNT) revealed that NNT is required for the provision of NADPH and that the upregulation of isocitrate dehydrogenase-2 (IDH2) activity is not enough to compensate for the absence of NNT, which is consistent with previous observations.	NADP	156-161	nicotinamide nucleotide transhydrogenase	Mus musculus	76-79
31639438-2	2020	Our investigations using the closely related mouse strains C57BL/6NJ (6NJ; +NNT) and C57BL/6J (6J; -NNT) revealed that NNT is required for the provision of NADPH and that the upregulation of isocitrate dehydrogenase-2 (IDH2) activity is not enough to compensate for the absence of NNT, which is consistent with previous observations.	NADP	156-161	nicotinamide nucleotide transhydrogenase	Mus musculus	100-103
31639438-2	2020	Our investigations using the closely related mouse strains C57BL/6NJ (6NJ; +NNT) and C57BL/6J (6J; -NNT) revealed that NNT is required for the provision of NADPH and that the upregulation of isocitrate dehydrogenase-2 (IDH2) activity is not enough to compensate for the absence of NNT, which is consistent with previous observations.	NADP	156-161	nicotinamide nucleotide transhydrogenase	Mus musculus	100-103
31639438-2	2020	Our investigations using the closely related mouse strains C57BL/6NJ (6NJ; +NNT) and C57BL/6J (6J; -NNT) revealed that NNT is required for the provision of NADPH and that the upregulation of isocitrate dehydrogenase-2 (IDH2) activity is not enough to compensate for the absence of NNT, which is consistent with previous observations.	NADP	156-161	nicotinamide nucleotide transhydrogenase	Mus musculus	100-103
28964917-2	2017	We hypothesized that a HFD would increase mitochondrial reliance on NAD(P)-transhydrogenase (NNT) as the source of NADPH for antioxidant systems that counteract NAFLD development.	NADP	115-120	nicotinamide nucleotide transhydrogenase	Mus musculus	93-96
31639438-4	2020	However, 6NJ mitochondria energized with succinate produced significantly less H2O2 (59.95 +- 2.13 pmol mg-1 min-1) when compared to samples from 6J mice (116.39 +- 20.74 pmol mg-1 min-1), an effect that was attributed to the presence of NNT.	Succinates	41-50	nicotinamide nucleotide transhydrogenase	Mus musculus	238-241
31639438-5	2020	Further investigations into the H2O2 eliminating capacities of these mitochondria led to the novel observation that 6J mitochondria compensate for the loss of NNT by upregulating catalase.	Water	32-36	nicotinamide nucleotide transhydrogenase	Mus musculus	159-162
31639438-6	2020	Indeed, 6NJ and 6J mitochondria energized with pyruvate or succinate displayed similar rates for H2O2 elimination, quenching ~84% and ~86% of the H2O2, respectively, in the surrounding medium within 30 s. However, inclusion of palmitoyl-CoA, an NNT inhibitor, significantly limited H2O2 degradation by 6NJ mitochondria only (~55% of H2O2 eliminated in 30 s).	Pyruvates	47-55	nicotinamide nucleotide transhydrogenase	Mus musculus	245-248
31639438-6	2020	Indeed, 6NJ and 6J mitochondria energized with pyruvate or succinate displayed similar rates for H2O2 elimination, quenching ~84% and ~86% of the H2O2, respectively, in the surrounding medium within 30 s. However, inclusion of palmitoyl-CoA, an NNT inhibitor, significantly limited H2O2 degradation by 6NJ mitochondria only (~55% of H2O2 eliminated in 30 s).	Succinates	59-68	nicotinamide nucleotide transhydrogenase	Mus musculus	245-248
31639438-13	2020	Collectively, our findings demonstrate for the first time that 6J liver mitochondria compensate for the loss of NNT by increasing catalase levels for the maintenance of H2O2 steady-state levels.	Water	169-173	nicotinamide nucleotide transhydrogenase	Mus musculus	112-115
30281804-1	2018	Among mitochondrial NADP-reducing enzymes, nicotinamide nucleotide transhydrogenase (NNT) establishes an elevated matrix NADPH/NADP+ by catalyzing the reduction of NADP+ at the expense of NADH oxidation coupled to inward proton translocation across the inner mitochondrial membrane.	NADP	20-24	nicotinamide nucleotide transhydrogenase	Mus musculus	85-88
30281804-1	2018	Among mitochondrial NADP-reducing enzymes, nicotinamide nucleotide transhydrogenase (NNT) establishes an elevated matrix NADPH/NADP+ by catalyzing the reduction of NADP+ at the expense of NADH oxidation coupled to inward proton translocation across the inner mitochondrial membrane.	NADP	121-126	nicotinamide nucleotide transhydrogenase	Mus musculus	85-88
30281804-1	2018	Among mitochondrial NADP-reducing enzymes, nicotinamide nucleotide transhydrogenase (NNT) establishes an elevated matrix NADPH/NADP+ by catalyzing the reduction of NADP+ at the expense of NADH oxidation coupled to inward proton translocation across the inner mitochondrial membrane.	NADP	127-132	nicotinamide nucleotide transhydrogenase	Mus musculus	85-88
30281804-1	2018	Among mitochondrial NADP-reducing enzymes, nicotinamide nucleotide transhydrogenase (NNT) establishes an elevated matrix NADPH/NADP+ by catalyzing the reduction of NADP+ at the expense of NADH oxidation coupled to inward proton translocation across the inner mitochondrial membrane.	NADP	164-169	nicotinamide nucleotide transhydrogenase	Mus musculus	85-88
30281804-1	2018	Among mitochondrial NADP-reducing enzymes, nicotinamide nucleotide transhydrogenase (NNT) establishes an elevated matrix NADPH/NADP+ by catalyzing the reduction of NADP+ at the expense of NADH oxidation coupled to inward proton translocation across the inner mitochondrial membrane.	NAD	188-192	nicotinamide nucleotide transhydrogenase	Mus musculus	85-88
30281804-3	2018	The absence of NNT activity resulted in lower total NADPH sources activity in the brain mitochondria of young mice, an effect that was partially compensated in aged mice.	NADP	52-57	nicotinamide nucleotide transhydrogenase	Mus musculus	15-18
30281804-5	2018	In the absence of NNT, an increased release of H2 O2 from mitochondria was observed when the metabolism of respiratory substrates occurred with restricted flux through relevant mitochondrial NADPH sources or when respiratory complex I was inhibited.	Hydrogen Peroxide	47-52	nicotinamide nucleotide transhydrogenase	Mus musculus	18-21
30281804-6	2018	In accordance, mitochondria from Nnt-/- brains were unable to sustain NADP in its reduced state when energized in the absence of carbon substrates, an effect aggravated after H2 O2 bolus metabolism.	Hydrogen Peroxide	175-180	nicotinamide nucleotide transhydrogenase	Mus musculus	33-36
30281804-7	2018	These data indicate that the lack of NNT in brain mitochondria impairs peroxide detoxification, but peroxide detoxification can be partially counterbalanced by concurrent NADPH sources depending on substrate availability.	Peroxides	71-79	nicotinamide nucleotide transhydrogenase	Mus musculus	37-40
29046340-2	2018	NNT produces high concentrations of NADPH for detoxification of reactive oxygen species by glutathione and thioredoxin pathways.	NADP	36-41	nicotinamide nucleotide transhydrogenase	Mus musculus	0-3
29046340-2	2018	NNT produces high concentrations of NADPH for detoxification of reactive oxygen species by glutathione and thioredoxin pathways.	Reactive Oxygen Species	64-87	nicotinamide nucleotide transhydrogenase	Mus musculus	0-3
29046340-2	2018	NNT produces high concentrations of NADPH for detoxification of reactive oxygen species by glutathione and thioredoxin pathways.	Glutathione	91-102	nicotinamide nucleotide transhydrogenase	Mus musculus	0-3
29046340-10	2018	Further, we demonstrated that both under expression or overexpression of NNT reduced corticosterone output implying a central role for it in the control of steroidogenesis.	Corticosterone	85-99	nicotinamide nucleotide transhydrogenase	Mus musculus	73-76
29455203-12	2018	CONCLUSION: These data indicate that loss of NNT increases vascular ROS production and exacerbates atherosclerotic plaque development.	Reactive Oxygen Species	68-71	nicotinamide nucleotide transhydrogenase	Mus musculus	45-48
28964917-4	2017	After 20 weeks on a HFD, Nnt-/- mice exhibited a higher prevalence of steatohepatitis and content of liver triglycerides compared to Nnt+/+ mice on an identical diet.	Triglycerides	107-120	nicotinamide nucleotide transhydrogenase	Mus musculus	25-28
28964917-5	2017	Under a HFD, the aggravated NAFLD phenotype in the Nnt-/- mice was accompanied by an increased H2O2 release rate from mitochondria, decreased aconitase activity (a redox-sensitive mitochondrial enzyme) and higher susceptibility to Ca2+-induced mitochondrial permeability transition.	Hydrogen Peroxide	95-99	nicotinamide nucleotide transhydrogenase	Mus musculus	51-54
28964917-6	2017	In addition, HFD led to the phosphorylation (inhibition) of pyruvate dehydrogenase (PDH) and markedly reduced the ability of liver mitochondria to remove peroxide in Nnt-/- mice.	Peroxides	154-162	nicotinamide nucleotide transhydrogenase	Mus musculus	166-169
28964917-7	2017	Bypass or pharmacological reactivation of PDH by dichloroacetate restored the peroxide removal capability of mitochondria from Nnt-/- mice on a HFD.	Dichloroacetic Acid	49-64	nicotinamide nucleotide transhydrogenase	Mus musculus	127-130
28964917-7	2017	Bypass or pharmacological reactivation of PDH by dichloroacetate restored the peroxide removal capability of mitochondria from Nnt-/- mice on a HFD.	Peroxides	78-86	nicotinamide nucleotide transhydrogenase	Mus musculus	127-130
28964917-9	2017	Therefore, HFD interacted with Nnt mutation to generate PDH inhibition and further suppression of peroxide removal.	Peroxides	98-106	nicotinamide nucleotide transhydrogenase	Mus musculus	31-34
28580284-2	2017	Nicotinamide nucleotide transhydrogenase (NNT) typically produces NADPH at the expense of NADH and DeltapH in energized mitochondria.	NAD	90-94	nicotinamide nucleotide transhydrogenase	Mus musculus	0-40
28580284-2	2017	Nicotinamide nucleotide transhydrogenase (NNT) typically produces NADPH at the expense of NADH and DeltapH in energized mitochondria.	NAD	90-94	nicotinamide nucleotide transhydrogenase	Mus musculus	42-45
28580284-4	2017	Here, we tested the role of NNT in the glucose regulation of mitochondrial NADPH and glutathione redox state and reinvestigated its role in GSIS coupling events in mouse pancreatic islets.	Glucose	39-46	nicotinamide nucleotide transhydrogenase	Mus musculus	28-31
28580284-4	2017	Here, we tested the role of NNT in the glucose regulation of mitochondrial NADPH and glutathione redox state and reinvestigated its role in GSIS coupling events in mouse pancreatic islets.	NADP	75-80	nicotinamide nucleotide transhydrogenase	Mus musculus	28-31
28580284-4	2017	Here, we tested the role of NNT in the glucose regulation of mitochondrial NADPH and glutathione redox state and reinvestigated its role in GSIS coupling events in mouse pancreatic islets.	Glutathione	85-96	nicotinamide nucleotide transhydrogenase	Mus musculus	28-31
28580284-10	2017	RESULTS: NNT is largely responsible for the acute glucose-induced rise in islet NADPH/NADP+ ratio and decrease in mitochondrial glutathione oxidation, with a small impact on cytosolic glutathione.	Glucose	50-57	nicotinamide nucleotide transhydrogenase	Mus musculus	9-12
28580284-10	2017	RESULTS: NNT is largely responsible for the acute glucose-induced rise in islet NADPH/NADP+ ratio and decrease in mitochondrial glutathione oxidation, with a small impact on cytosolic glutathione.	NADP	80-85	nicotinamide nucleotide transhydrogenase	Mus musculus	9-12
28580284-10	2017	RESULTS: NNT is largely responsible for the acute glucose-induced rise in islet NADPH/NADP+ ratio and decrease in mitochondrial glutathione oxidation, with a small impact on cytosolic glutathione.	NADP	86-91	nicotinamide nucleotide transhydrogenase	Mus musculus	9-12
28580284-10	2017	RESULTS: NNT is largely responsible for the acute glucose-induced rise in islet NADPH/NADP+ ratio and decrease in mitochondrial glutathione oxidation, with a small impact on cytosolic glutathione.	Glutathione	128-139	nicotinamide nucleotide transhydrogenase	Mus musculus	9-12
28580284-10	2017	RESULTS: NNT is largely responsible for the acute glucose-induced rise in islet NADPH/NADP+ ratio and decrease in mitochondrial glutathione oxidation, with a small impact on cytosolic glutathione.	Glutathione	184-195	nicotinamide nucleotide transhydrogenase	Mus musculus	9-12
28580284-11	2017	However, contrary to current views on NNT in beta-cells, these effects resulted from a glucose-dependent reduction in NADPH consumption by NNT reverse mode of operation, rather than from a stimulation of its forward mode of operation.	Glucose	87-94	nicotinamide nucleotide transhydrogenase	Mus musculus	139-142
28580284-11	2017	However, contrary to current views on NNT in beta-cells, these effects resulted from a glucose-dependent reduction in NADPH consumption by NNT reverse mode of operation, rather than from a stimulation of its forward mode of operation.	NADP	118-123	nicotinamide nucleotide transhydrogenase	Mus musculus	139-142
28580284-12	2017	Accordingly, the lack of NNT in J-islets decreased their sensitivity to exogenous H2O2 at non-stimulating glucose.	Hydrogen Peroxide	82-86	nicotinamide nucleotide transhydrogenase	Mus musculus	25-28
28580284-12	2017	Accordingly, the lack of NNT in J-islets decreased their sensitivity to exogenous H2O2 at non-stimulating glucose.	Glucose	106-113	nicotinamide nucleotide transhydrogenase	Mus musculus	25-28
17052203-0	2006	Nicotinamide nucleotide transhydrogenase: a link between insulin secretion, glucose metabolism and oxidative stress.	Glucose	76-83	nicotinamide nucleotide transhydrogenase	Mus musculus	0-40
28087333-5	2017	We demonstrate that the absence of NNT in 6J cells led to distinct mitochondrial bioenergetic profiles and a pro-oxidative mitochondrial phenotype characterized by increased superoxide production and reduced glutathione peroxidase activity.	Superoxides	174-184	nicotinamide nucleotide transhydrogenase	Mus musculus	35-38
23747984-2	2013	Nicotinamide nucleotide transhydrogenase (NNT), an integral protein located in the inner mitochondrial membrane, contributes to an elevated mitochondrial NADPH/NADP(+) ratio.	NADP	154-159	nicotinamide nucleotide transhydrogenase	Mus musculus	0-40
23747984-2	2013	Nicotinamide nucleotide transhydrogenase (NNT), an integral protein located in the inner mitochondrial membrane, contributes to an elevated mitochondrial NADPH/NADP(+) ratio.	NADP	154-159	nicotinamide nucleotide transhydrogenase	Mus musculus	42-45
23747984-2	2013	Nicotinamide nucleotide transhydrogenase (NNT), an integral protein located in the inner mitochondrial membrane, contributes to an elevated mitochondrial NADPH/NADP(+) ratio.	NADP	160-167	nicotinamide nucleotide transhydrogenase	Mus musculus	0-40
23747984-2	2013	Nicotinamide nucleotide transhydrogenase (NNT), an integral protein located in the inner mitochondrial membrane, contributes to an elevated mitochondrial NADPH/NADP(+) ratio.	NADP	160-167	nicotinamide nucleotide transhydrogenase	Mus musculus	42-45
23747984-7	2013	The functional evaluation of respiring mitochondria revealed major redox alterations in B6J-Nnt(MUT) mice, including an absence of transhydrogenation between NAD and NADP, higher rates of H2O2 release, the spontaneous oxidation of NADPH, the poor ability to metabolize organic peroxide, and a higher susceptibility to undergo Ca(2+)-induced mitochondrial permeability transition.	Hydrogen Peroxide	188-192	nicotinamide nucleotide transhydrogenase	Mus musculus	92-95
22593545-1	2012	Nicotinamide nucleotide transhydrogenase (NNT) is a mitochondrial redox-driven proton pump that couples the production of NADPH to the mitochondrial metabolic rate.	NADP	122-127	nicotinamide nucleotide transhydrogenase	Mus musculus	0-40
22593545-1	2012	Nicotinamide nucleotide transhydrogenase (NNT) is a mitochondrial redox-driven proton pump that couples the production of NADPH to the mitochondrial metabolic rate.	NADP	122-127	nicotinamide nucleotide transhydrogenase	Mus musculus	42-45
22593545-4	2012	Overexpression of NNT in a macrophage cell-line resulted in decreased levels of reactive oxygen species (ROS) and nitric oxide upon induction of the macrophage inflammatory responses.	Reactive Oxygen Species	80-103	nicotinamide nucleotide transhydrogenase	Mus musculus	18-21
22593545-4	2012	Overexpression of NNT in a macrophage cell-line resulted in decreased levels of reactive oxygen species (ROS) and nitric oxide upon induction of the macrophage inflammatory responses.	Reactive Oxygen Species	105-108	nicotinamide nucleotide transhydrogenase	Mus musculus	18-21
22593545-4	2012	Overexpression of NNT in a macrophage cell-line resulted in decreased levels of reactive oxygen species (ROS) and nitric oxide upon induction of the macrophage inflammatory responses.	Nitric Oxide	114-126	nicotinamide nucleotide transhydrogenase	Mus musculus	18-21
17052203-12	2006	We hypothesize that Nnt mutations enhance glucose-dependent ROS production and thereby impair beta-cell mitochondrial metabolism, possibly via activation of uncoupling proteins.	Reactive Oxygen Species	60-63	nicotinamide nucleotide transhydrogenase	Mus musculus	20-23
28580284-0	2017	NNT reverse mode of operation mediates glucose control of mitochondrial NADPH and glutathione redox state in mouse pancreatic beta-cells.	Glucose	39-46	nicotinamide nucleotide transhydrogenase	Mus musculus	0-3
28580284-0	2017	NNT reverse mode of operation mediates glucose control of mitochondrial NADPH and glutathione redox state in mouse pancreatic beta-cells.	NADP	72-77	nicotinamide nucleotide transhydrogenase	Mus musculus	0-3
28580284-0	2017	NNT reverse mode of operation mediates glucose control of mitochondrial NADPH and glutathione redox state in mouse pancreatic beta-cells.	Glutathione	82-93	nicotinamide nucleotide transhydrogenase	Mus musculus	0-3
28580284-2	2017	Nicotinamide nucleotide transhydrogenase (NNT) typically produces NADPH at the expense of NADH and DeltapH in energized mitochondria.	NADP	66-71	nicotinamide nucleotide transhydrogenase	Mus musculus	0-40
28580284-2	2017	Nicotinamide nucleotide transhydrogenase (NNT) typically produces NADPH at the expense of NADH and DeltapH in energized mitochondria.	NADP	66-71	nicotinamide nucleotide transhydrogenase	Mus musculus	42-45
23747984-7	2013	The functional evaluation of respiring mitochondria revealed major redox alterations in B6J-Nnt(MUT) mice, including an absence of transhydrogenation between NAD and NADP, higher rates of H2O2 release, the spontaneous oxidation of NADPH, the poor ability to metabolize organic peroxide, and a higher susceptibility to undergo Ca(2+)-induced mitochondrial permeability transition.	NADP	231-236	nicotinamide nucleotide transhydrogenase	Mus musculus	92-95
23747984-7	2013	The functional evaluation of respiring mitochondria revealed major redox alterations in B6J-Nnt(MUT) mice, including an absence of transhydrogenation between NAD and NADP, higher rates of H2O2 release, the spontaneous oxidation of NADPH, the poor ability to metabolize organic peroxide, and a higher susceptibility to undergo Ca(2+)-induced mitochondrial permeability transition.	organic	269-276	nicotinamide nucleotide transhydrogenase	Mus musculus	92-95
23747984-7	2013	The functional evaluation of respiring mitochondria revealed major redox alterations in B6J-Nnt(MUT) mice, including an absence of transhydrogenation between NAD and NADP, higher rates of H2O2 release, the spontaneous oxidation of NADPH, the poor ability to metabolize organic peroxide, and a higher susceptibility to undergo Ca(2+)-induced mitochondrial permeability transition.	Peroxides	277-285	nicotinamide nucleotide transhydrogenase	Mus musculus	92-95
23747984-8	2013	In addition, the mitochondria of B6J-Nnt(MUT) mice exhibited increased oxidized/reduced glutathione ratios as compared to B6JUnib-Nnt(W) mice.	Glutathione	88-99	nicotinamide nucleotide transhydrogenase	Mus musculus	37-40
23747984-10	2013	Altogether, our data suggest that NNT functions as a high-capacity source of mitochondrial NADPH and that its functional loss due to the Nnt mutation results in mitochondrial redox abnormalities, most notably a poor ability to sustain NADP and glutathione in their reduced states.	NADP	91-96	nicotinamide nucleotide transhydrogenase	Mus musculus	34-37
23747984-10	2013	Altogether, our data suggest that NNT functions as a high-capacity source of mitochondrial NADPH and that its functional loss due to the Nnt mutation results in mitochondrial redox abnormalities, most notably a poor ability to sustain NADP and glutathione in their reduced states.	NADP	91-95	nicotinamide nucleotide transhydrogenase	Mus musculus	34-37
23747984-10	2013	Altogether, our data suggest that NNT functions as a high-capacity source of mitochondrial NADPH and that its functional loss due to the Nnt mutation results in mitochondrial redox abnormalities, most notably a poor ability to sustain NADP and glutathione in their reduced states.	Glutathione	244-255	nicotinamide nucleotide transhydrogenase	Mus musculus	34-37
23747984-10	2013	Altogether, our data suggest that NNT functions as a high-capacity source of mitochondrial NADPH and that its functional loss due to the Nnt mutation results in mitochondrial redox abnormalities, most notably a poor ability to sustain NADP and glutathione in their reduced states.	Glutathione	244-255	nicotinamide nucleotide transhydrogenase	Mus musculus	137-140
17052203-1	2006	This paper reviews recent studies on the role of Nnt (nicotinamide nucleotide transhydrogenase) in insulin secretion and detoxification of ROS (reactive oxygen species).	Reactive Oxygen Species	139-142	nicotinamide nucleotide transhydrogenase	Mus musculus	49-52
17052203-1	2006	This paper reviews recent studies on the role of Nnt (nicotinamide nucleotide transhydrogenase) in insulin secretion and detoxification of ROS (reactive oxygen species).	Reactive Oxygen Species	139-142	nicotinamide nucleotide transhydrogenase	Mus musculus	54-94
17052203-1	2006	This paper reviews recent studies on the role of Nnt (nicotinamide nucleotide transhydrogenase) in insulin secretion and detoxification of ROS (reactive oxygen species).	Reactive Oxygen Species	144-167	nicotinamide nucleotide transhydrogenase	Mus musculus	49-52
17052203-1	2006	This paper reviews recent studies on the role of Nnt (nicotinamide nucleotide transhydrogenase) in insulin secretion and detoxification of ROS (reactive oxygen species).	Reactive Oxygen Species	144-167	nicotinamide nucleotide transhydrogenase	Mus musculus	54-94
17052203-4	2006	The C57BL/6J mouse displays glucose intolerance and reduced insulin secretion, which results from a naturally occurring deletion in the Nnt gene.	Glucose	28-35	nicotinamide nucleotide transhydrogenase	Mus musculus	136-139
17052203-7	2006	Similarly, mice carrying ENU (N-ethyl-N-nitrosourea)-induced loss-of-function mutations in Nnt were glucose intolerant and secreted less insulin during a glucose tolerance test.	Ethylnitrosourea	30-51	nicotinamide nucleotide transhydrogenase	Mus musculus	91-94
17052203-7	2006	Similarly, mice carrying ENU (N-ethyl-N-nitrosourea)-induced loss-of-function mutations in Nnt were glucose intolerant and secreted less insulin during a glucose tolerance test.	Glucose	100-107	nicotinamide nucleotide transhydrogenase	Mus musculus	91-94
17052203-10	2006	Nnt is a nuclear-encoded mitochondrial protein involved in detoxification of ROS.	Reactive Oxygen Species	77-80	nicotinamide nucleotide transhydrogenase	Mus musculus	0-3
17052203-11	2006	beta-Cells isolated from Nnt mutant mice showed increased ROS production on glucose stimulation.	Reactive Oxygen Species	58-61	nicotinamide nucleotide transhydrogenase	Mus musculus	25-28
17052203-11	2006	beta-Cells isolated from Nnt mutant mice showed increased ROS production on glucose stimulation.	Glucose	76-83	nicotinamide nucleotide transhydrogenase	Mus musculus	25-28
17052203-12	2006	We hypothesize that Nnt mutations enhance glucose-dependent ROS production and thereby impair beta-cell mitochondrial metabolism, possibly via activation of uncoupling proteins.	Glucose	42-49	nicotinamide nucleotide transhydrogenase	Mus musculus	20-23
16804088-0	2006	Deletion of nicotinamide nucleotide transhydrogenase: a new quantitive trait locus accounting for glucose intolerance in C57BL/6J mice.	Glucose	98-105	nicotinamide nucleotide transhydrogenase	Mus musculus	12-52
16497723-6	2006	The forward reaction of NNT, a nuclear-encoded mitochondrial inner membrane protein, couples the generation of NADPH to proton transport and provides NADPH for the regeneration of two important antioxidant compounds, glutathione and thioredoxin, in the mitochondria.	NADP	111-116	nicotinamide nucleotide transhydrogenase	Mus musculus	24-27
16497723-6	2006	The forward reaction of NNT, a nuclear-encoded mitochondrial inner membrane protein, couples the generation of NADPH to proton transport and provides NADPH for the regeneration of two important antioxidant compounds, glutathione and thioredoxin, in the mitochondria.	NADP	150-155	nicotinamide nucleotide transhydrogenase	Mus musculus	24-27
16497723-6	2006	The forward reaction of NNT, a nuclear-encoded mitochondrial inner membrane protein, couples the generation of NADPH to proton transport and provides NADPH for the regeneration of two important antioxidant compounds, glutathione and thioredoxin, in the mitochondria.	Glutathione	217-228	nicotinamide nucleotide transhydrogenase	Mus musculus	24-27
16399503-6	2006	Nnt mutant mice were glucose intolerant and secreted less insulin during a glucose tolerance test.	Glucose	21-28	nicotinamide nucleotide transhydrogenase	Mus musculus	0-3
16399503-8	2006	Glucose utilization and production of reactive oxygen species were increased in Nnt beta cells.	Glucose	0-7	nicotinamide nucleotide transhydrogenase	Mus musculus	80-83
16399503-8	2006	Glucose utilization and production of reactive oxygen species were increased in Nnt beta cells.	Reactive Oxygen Species	38-61	nicotinamide nucleotide transhydrogenase	Mus musculus	80-83
16399503-9	2006	We hypothesize that Nnt mutations/deletion uncouple beta cell mitochondrial metabolism leading to less ATP production, enhanced KATP channel activity, and consequently impaired insulin secretion.	Adenosine Triphosphate	103-106	nicotinamide nucleotide transhydrogenase	Mus musculus	20-23