PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
34509082-6	2021	Furthermore, cellular total ROS and mitochondrial ROS generation, and impairment of mitochondrial membrane potential (MMP) were highly induced by ox-LDL in THP1 cells, while being considerably reversed upon CISD1 over-expression.	ros	28-31	CDGSH iron sulfur domain 1	Homo sapiens	207-212
34509082-6	2021	Furthermore, cellular total ROS and mitochondrial ROS generation, and impairment of mitochondrial membrane potential (MMP) were highly induced by ox-LDL in THP1 cells, while being considerably reversed upon CISD1 over-expression.	ros	50-53	CDGSH iron sulfur domain 1	Homo sapiens	207-212
34672568-0	2021	Controlled Protonation of (2Fe-2S) Leading to MitoNEET Analogues and Concurrent Cluster Modification.	2fe-2s	27-33	CDGSH iron sulfur domain 1	Homo sapiens	46-54
34672568-1	2021	MitoNEET, a key regulatory protein in mitochondrial energy metabolism, exhibits a uniquely ligated (2Fe-2S) cluster with one histidine and three cysteines.	Histidine	125-134	CDGSH iron sulfur domain 1	Homo sapiens	0-8
34672568-1	2021	MitoNEET, a key regulatory protein in mitochondrial energy metabolism, exhibits a uniquely ligated (2Fe-2S) cluster with one histidine and three cysteines.	Cysteine	145-154	CDGSH iron sulfur domain 1	Homo sapiens	0-8
34672568-6	2021	The current study provides insight into how mitoNEET releases its (2Fe-2S) in response to highly tuned acidic conditions, the chemistry of which may have further implications in Fe-S biogenesis.	Iron	178-182	CDGSH iron sulfur domain 1	Homo sapiens	44-52
35608094-1	2022	The outer mitochondrial membrane protein mitoNEET (mNT) is a recently identified iron-sulfur protein containing a unique Fe2 S2 (His)1 (Cys)3 metal cluster with a single Fe-N(His87) coordinating bond.	Cysteine	136-139	CDGSH iron sulfur domain 1	Homo sapiens	41-49
34587896-1	2021	BACKGROUND: Cisd1 and Cisd2 proteins share very similar structures with an N-terminal membrane-anchoring domain and a C-terminal cytosolic domain containing an iron-cluster binding domain and ending with a C-terminal KKxx sequence.	Iron	160-164	CDGSH iron sulfur domain 1	Homo sapiens	12-17
34421355-8	2021	Taken together, our findings suggest that MTX1 is upregulated in HCC and contributes to sorafenib resistance via a possible mechanism involving CISD1 mediated autophagy.	Sorafenib	88-97	CDGSH iron sulfur domain 1	Homo sapiens	144-149
35608094-1	2022	The outer mitochondrial membrane protein mitoNEET (mNT) is a recently identified iron-sulfur protein containing a unique Fe2 S2 (His)1 (Cys)3 metal cluster with a single Fe-N(His87) coordinating bond.	fe-n	170-174	CDGSH iron sulfur domain 1	Homo sapiens	41-49
34496224-8	2021	Lastly, the KO of mitoNEET was associated with decreased proliferation as compared to control cells when exposed to the standard of care agent cytarabine (Ara-C).	Cytarabine	143-153	CDGSH iron sulfur domain 1	Homo sapiens	18-26
34496224-8	2021	Lastly, the KO of mitoNEET was associated with decreased proliferation as compared to control cells when exposed to the standard of care agent cytarabine (Ara-C).	Cytarabine	155-160	CDGSH iron sulfur domain 1	Homo sapiens	18-26
34310123-1	2021	The human mitochondrial protein, mitoNEET (mNT), belongs to the family of small (2Fe-2S) NEET proteins that bind their iron-sulfur clusters with a novel and characteristic 3Cys:1His coordination motif.	Iron	119-123	CDGSH iron sulfur domain 1	Homo sapiens	33-41
34310123-1	2021	The human mitochondrial protein, mitoNEET (mNT), belongs to the family of small (2Fe-2S) NEET proteins that bind their iron-sulfur clusters with a novel and characteristic 3Cys:1His coordination motif.	Iron	119-123	CDGSH iron sulfur domain 1	Homo sapiens	89-93
34310123-1	2021	The human mitochondrial protein, mitoNEET (mNT), belongs to the family of small (2Fe-2S) NEET proteins that bind their iron-sulfur clusters with a novel and characteristic 3Cys:1His coordination motif.	Sulfur	124-130	CDGSH iron sulfur domain 1	Homo sapiens	33-41
34310123-1	2021	The human mitochondrial protein, mitoNEET (mNT), belongs to the family of small (2Fe-2S) NEET proteins that bind their iron-sulfur clusters with a novel and characteristic 3Cys:1His coordination motif.	Sulfur	124-130	CDGSH iron sulfur domain 1	Homo sapiens	89-93
34310123-1	2021	The human mitochondrial protein, mitoNEET (mNT), belongs to the family of small (2Fe-2S) NEET proteins that bind their iron-sulfur clusters with a novel and characteristic 3Cys:1His coordination motif.	3cys	172-176	CDGSH iron sulfur domain 1	Homo sapiens	33-41
34310123-1	2021	The human mitochondrial protein, mitoNEET (mNT), belongs to the family of small (2Fe-2S) NEET proteins that bind their iron-sulfur clusters with a novel and characteristic 3Cys:1His coordination motif.	3cys	172-176	CDGSH iron sulfur domain 1	Homo sapiens	89-93
34310123-1	2021	The human mitochondrial protein, mitoNEET (mNT), belongs to the family of small (2Fe-2S) NEET proteins that bind their iron-sulfur clusters with a novel and characteristic 3Cys:1His coordination motif.	1his	177-181	CDGSH iron sulfur domain 1	Homo sapiens	33-41
34310123-1	2021	The human mitochondrial protein, mitoNEET (mNT), belongs to the family of small (2Fe-2S) NEET proteins that bind their iron-sulfur clusters with a novel and characteristic 3Cys:1His coordination motif.	1his	177-181	CDGSH iron sulfur domain 1	Homo sapiens	89-93
35609862-1	2022	MitoNEET is the first iron-sulfur protein found in mitochondrial outer membrane.	ferrous sulfide	22-33	CDGSH iron sulfur domain 1	Homo sapiens	0-8
35609862-4	2022	The C-terminal cytosolic domain of mitoNEET binds a (2Fe-2S) cluster via three cysteine and one histidine residues.	Cysteine	79-87	CDGSH iron sulfur domain 1	Homo sapiens	35-43
35609862-4	2022	The C-terminal cytosolic domain of mitoNEET binds a (2Fe-2S) cluster via three cysteine and one histidine residues.	Histidine	96-105	CDGSH iron sulfur domain 1	Homo sapiens	35-43
35609862-5	2022	It has been shown that mitoNEET has a crucial role in energy metabolism, iron homeostasis, and free radical production in cells.	Iron	73-77	CDGSH iron sulfur domain 1	Homo sapiens	23-31
35609862-7	2022	Previously, we reported that the C-terminal soluble domain of mitoNEET has a specific binding site for flavin mononucleotide (FMN) and can transfer electrons from FMNH2 to oxygen or ubiquinone-2 via its (2Fe-2S) cluster.	Flavin Mononucleotide	103-124	CDGSH iron sulfur domain 1	Homo sapiens	62-70
35609862-7	2022	Previously, we reported that the C-terminal soluble domain of mitoNEET has a specific binding site for flavin mononucleotide (FMN) and can transfer electrons from FMNH2 to oxygen or ubiquinone-2 via its (2Fe-2S) cluster.	Flavin Mononucleotide	126-129	CDGSH iron sulfur domain 1	Homo sapiens	62-70
35609862-7	2022	Previously, we reported that the C-terminal soluble domain of mitoNEET has a specific binding site for flavin mononucleotide (FMN) and can transfer electrons from FMNH2 to oxygen or ubiquinone-2 via its (2Fe-2S) cluster.	flavin mononucleotide hydroquinone	163-168	CDGSH iron sulfur domain 1	Homo sapiens	62-70
35609862-7	2022	Previously, we reported that the C-terminal soluble domain of mitoNEET has a specific binding site for flavin mononucleotide (FMN) and can transfer electrons from FMNH2 to oxygen or ubiquinone-2 via its (2Fe-2S) cluster.	Oxygen	172-178	CDGSH iron sulfur domain 1	Homo sapiens	62-70
35609862-7	2022	Previously, we reported that the C-terminal soluble domain of mitoNEET has a specific binding site for flavin mononucleotide (FMN) and can transfer electrons from FMNH2 to oxygen or ubiquinone-2 via its (2Fe-2S) cluster.	Ubiquinone	182-192	CDGSH iron sulfur domain 1	Homo sapiens	62-70
35609862-12	2022	Because NADH oxidation is required for cellular glycolytic activity, we propose that the mitochondrial outer membrane protein mitoNEET may promote glycolysis by transferring electrons from FMNH2 to oxygen or ubiquinone-10 in mitochondria.	NAD	8-12	CDGSH iron sulfur domain 1	Homo sapiens	126-134
35609862-12	2022	Because NADH oxidation is required for cellular glycolytic activity, we propose that the mitochondrial outer membrane protein mitoNEET may promote glycolysis by transferring electrons from FMNH2 to oxygen or ubiquinone-10 in mitochondria.	flavin mononucleotide hydroquinone	189-194	CDGSH iron sulfur domain 1	Homo sapiens	126-134
35609862-12	2022	Because NADH oxidation is required for cellular glycolytic activity, we propose that the mitochondrial outer membrane protein mitoNEET may promote glycolysis by transferring electrons from FMNH2 to oxygen or ubiquinone-10 in mitochondria.	Oxygen	198-204	CDGSH iron sulfur domain 1	Homo sapiens	126-134
35609862-12	2022	Because NADH oxidation is required for cellular glycolytic activity, we propose that the mitochondrial outer membrane protein mitoNEET may promote glycolysis by transferring electrons from FMNH2 to oxygen or ubiquinone-10 in mitochondria.	Ubiquinone	208-221	CDGSH iron sulfur domain 1	Homo sapiens	126-134
35557955-0	2022	Multiple Poses and Thermodynamics of Ligands Targeting Protein Surfaces: The Case of Furosemide Binding to mitoNEET in Aqueous Solution.	Furosemide	85-95	CDGSH iron sulfur domain 1	Homo sapiens	107-115
35557955-1	2022	Human NEET proteins, such as NAF-1 and mitoNEET, are homodimeric, redox iron-sulfur proteins characterized by triple cysteine and one histidine-coordinated (2Fe-2S) cluster.	Iron	72-76	CDGSH iron sulfur domain 1	Homo sapiens	39-47
35557955-1	2022	Human NEET proteins, such as NAF-1 and mitoNEET, are homodimeric, redox iron-sulfur proteins characterized by triple cysteine and one histidine-coordinated (2Fe-2S) cluster.	Sulfur	77-83	CDGSH iron sulfur domain 1	Homo sapiens	39-47
35557955-1	2022	Human NEET proteins, such as NAF-1 and mitoNEET, are homodimeric, redox iron-sulfur proteins characterized by triple cysteine and one histidine-coordinated (2Fe-2S) cluster.	Cysteine	117-125	CDGSH iron sulfur domain 1	Homo sapiens	39-47
35557955-1	2022	Human NEET proteins, such as NAF-1 and mitoNEET, are homodimeric, redox iron-sulfur proteins characterized by triple cysteine and one histidine-coordinated (2Fe-2S) cluster.	Histidine	134-143	CDGSH iron sulfur domain 1	Homo sapiens	39-47
35557955-6	2022	This is the X-ray structure of furosemide bound to oxidized mitoNEET.	Furosemide	31-41	CDGSH iron sulfur domain 1	Homo sapiens	60-68
35557955-7	2022	Here we employ an enhanced sampling approach, Localized Volume-based Metadynamics, developed by some of us, to identify binding poses of furosemide to human mitoNEET protein in solution.	Furosemide	137-147	CDGSH iron sulfur domain 1	Homo sapiens	157-165
35608094-1	2022	The outer mitochondrial membrane protein mitoNEET (mNT) is a recently identified iron-sulfur protein containing a unique Fe2 S2 (His)1 (Cys)3 metal cluster with a single Fe-N(His87) coordinating bond.	Metals	142-147	CDGSH iron sulfur domain 1	Homo sapiens	41-49
35136051-1	2022	MitoNEET (mitochondrial protein containing Asn-Glu-Glu-Thr (NEET) sequence) is a 2Fe-2S cluster-containing integral membrane protein that resides in the mitochondrial outer membrane and participates in a redox-sensitive signaling and Fe-S cluster transfer.	asn-glu-glu-thr	43-58	CDGSH iron sulfur domain 1	Homo sapiens	0-8
35136051-1	2022	MitoNEET (mitochondrial protein containing Asn-Glu-Glu-Thr (NEET) sequence) is a 2Fe-2S cluster-containing integral membrane protein that resides in the mitochondrial outer membrane and participates in a redox-sensitive signaling and Fe-S cluster transfer.	asn-glu-glu-thr	43-58	CDGSH iron sulfur domain 1	Homo sapiens	60-64
35136051-1	2022	MitoNEET (mitochondrial protein containing Asn-Glu-Glu-Thr (NEET) sequence) is a 2Fe-2S cluster-containing integral membrane protein that resides in the mitochondrial outer membrane and participates in a redox-sensitive signaling and Fe-S cluster transfer.	Iron	234-236	CDGSH iron sulfur domain 1	Homo sapiens	0-8
35136051-1	2022	MitoNEET (mitochondrial protein containing Asn-Glu-Glu-Thr (NEET) sequence) is a 2Fe-2S cluster-containing integral membrane protein that resides in the mitochondrial outer membrane and participates in a redox-sensitive signaling and Fe-S cluster transfer.	Iron	234-236	CDGSH iron sulfur domain 1	Homo sapiens	60-64
35136051-2	2022	Thus, mitoNEET is a key regulator of mitochondrial oxidative capacity and iron homeostasis.	Iron	74-78	CDGSH iron sulfur domain 1	Homo sapiens	6-14
35136051-10	2022	Inhibition of mitoNEET using NL-1 or mitoNEET shRNA abrogated LPS-induced ROS formation and mitochondrial dysfunction.	Reactive Oxygen Species	74-77	CDGSH iron sulfur domain 1	Homo sapiens	37-45
32445867-3	2020	Previously, we reported that the [2Fe-2S] clusters in mitoNEET can be reduced by the reduced flavin mononucleotide (FMNH2) and oxidized by oxygen or ubiquinone-2, suggesting that mitoNEET may act as a novel redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	2fe	34-37	CDGSH iron sulfur domain 1	Homo sapiens	179-187
33856229-0	2021	Pioglitazone Inhibits Metal Cluster Transfer of mitoNEET by Stabilizing the Labile Fe-N Bond Revealed at Single-Bond Level.	Pioglitazone	0-12	CDGSH iron sulfur domain 1	Homo sapiens	48-56
33856229-0	2021	Pioglitazone Inhibits Metal Cluster Transfer of mitoNEET by Stabilizing the Labile Fe-N Bond Revealed at Single-Bond Level.	Metals	22-27	CDGSH iron sulfur domain 1	Homo sapiens	48-56
33856229-0	2021	Pioglitazone Inhibits Metal Cluster Transfer of mitoNEET by Stabilizing the Labile Fe-N Bond Revealed at Single-Bond Level.	Iron	83-85	CDGSH iron sulfur domain 1	Homo sapiens	48-56
33856229-1	2021	Outer mitochondrial membrane protein mitoNEET (mNT) is a target of the type 2 diabetes drug pioglitazone.	Pioglitazone	92-104	CDGSH iron sulfur domain 1	Homo sapiens	37-45
33916457-1	2021	Human CISD2 and mitoNEET are two NEET proteins anchored in the endoplasmic reticulum and mitochondria membranes respectively, with an Fe-S containing domain stretching out in the cytosol.	Iron	134-138	CDGSH iron sulfur domain 1	Homo sapiens	16-24
33048522-0	2020	Single-Molecule Force Spectroscopy Reveals that the Fe-N Bond Enables Multiple Rupture Pathways of the 2Fe2S Cluster in a MitoNEET Monomer.	Iron	52-54	CDGSH iron sulfur domain 1	Homo sapiens	122-130
33048522-0	2020	Single-Molecule Force Spectroscopy Reveals that the Fe-N Bond Enables Multiple Rupture Pathways of the 2Fe2S Cluster in a MitoNEET Monomer.	Nitrogen	55-56	CDGSH iron sulfur domain 1	Homo sapiens	122-130
33048522-1	2020	The mitochondrial outer membrane protein, mitoNEET (mNT), is an iron-sulfur protein containing an Fe2S2(His)1(Cys)3 cluster with a unique single Fe-N bond.	Iron	98-100	CDGSH iron sulfur domain 1	Homo sapiens	42-50
32445867-0	2020	Exploring the FMN binding site in the mitochondrial outer membrane protein mitoNEET.	Flavin Mononucleotide	14-17	CDGSH iron sulfur domain 1	Homo sapiens	75-83
32445867-3	2020	Previously, we reported that the [2Fe-2S] clusters in mitoNEET can be reduced by the reduced flavin mononucleotide (FMNH2) and oxidized by oxygen or ubiquinone-2, suggesting that mitoNEET may act as a novel redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	2fe	34-37	CDGSH iron sulfur domain 1	Homo sapiens	54-62
32445867-3	2020	Previously, we reported that the [2Fe-2S] clusters in mitoNEET can be reduced by the reduced flavin mononucleotide (FMNH2) and oxidized by oxygen or ubiquinone-2, suggesting that mitoNEET may act as a novel redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	Flavin Mononucleotide	93-114	CDGSH iron sulfur domain 1	Homo sapiens	54-62
32445867-3	2020	Previously, we reported that the [2Fe-2S] clusters in mitoNEET can be reduced by the reduced flavin mononucleotide (FMNH2) and oxidized by oxygen or ubiquinone-2, suggesting that mitoNEET may act as a novel redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	Flavin Mononucleotide	93-114	CDGSH iron sulfur domain 1	Homo sapiens	179-187
32445867-3	2020	Previously, we reported that the [2Fe-2S] clusters in mitoNEET can be reduced by the reduced flavin mononucleotide (FMNH2) and oxidized by oxygen or ubiquinone-2, suggesting that mitoNEET may act as a novel redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	flavin mononucleotide hydroquinone	116-121	CDGSH iron sulfur domain 1	Homo sapiens	54-62
32445867-3	2020	Previously, we reported that the [2Fe-2S] clusters in mitoNEET can be reduced by the reduced flavin mononucleotide (FMNH2) and oxidized by oxygen or ubiquinone-2, suggesting that mitoNEET may act as a novel redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	flavin mononucleotide hydroquinone	116-121	CDGSH iron sulfur domain 1	Homo sapiens	179-187
32445867-3	2020	Previously, we reported that the [2Fe-2S] clusters in mitoNEET can be reduced by the reduced flavin mononucleotide (FMNH2) and oxidized by oxygen or ubiquinone-2, suggesting that mitoNEET may act as a novel redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	Oxygen	139-145	CDGSH iron sulfur domain 1	Homo sapiens	54-62
32445867-3	2020	Previously, we reported that the [2Fe-2S] clusters in mitoNEET can be reduced by the reduced flavin mononucleotide (FMNH2) and oxidized by oxygen or ubiquinone-2, suggesting that mitoNEET may act as a novel redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	Oxygen	139-145	CDGSH iron sulfur domain 1	Homo sapiens	179-187
32445867-3	2020	Previously, we reported that the [2Fe-2S] clusters in mitoNEET can be reduced by the reduced flavin mononucleotide (FMNH2) and oxidized by oxygen or ubiquinone-2, suggesting that mitoNEET may act as a novel redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	Ubiquinone	149-159	CDGSH iron sulfur domain 1	Homo sapiens	54-62
32445867-3	2020	Previously, we reported that the [2Fe-2S] clusters in mitoNEET can be reduced by the reduced flavin mononucleotide (FMNH2) and oxidized by oxygen or ubiquinone-2, suggesting that mitoNEET may act as a novel redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	Ubiquinone	149-159	CDGSH iron sulfur domain 1	Homo sapiens	179-187
32445867-3	2020	Previously, we reported that the [2Fe-2S] clusters in mitoNEET can be reduced by the reduced flavin mononucleotide (FMNH2) and oxidized by oxygen or ubiquinone-2, suggesting that mitoNEET may act as a novel redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	flavin mononucleotide hydroquinone	254-259	CDGSH iron sulfur domain 1	Homo sapiens	54-62
32445867-3	2020	Previously, we reported that the [2Fe-2S] clusters in mitoNEET can be reduced by the reduced flavin mononucleotide (FMNH2) and oxidized by oxygen or ubiquinone-2, suggesting that mitoNEET may act as a novel redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	flavin mononucleotide hydroquinone	254-259	CDGSH iron sulfur domain 1	Homo sapiens	179-187
32445867-3	2020	Previously, we reported that the [2Fe-2S] clusters in mitoNEET can be reduced by the reduced flavin mononucleotide (FMNH2) and oxidized by oxygen or ubiquinone-2, suggesting that mitoNEET may act as a novel redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	Oxygen	263-269	CDGSH iron sulfur domain 1	Homo sapiens	54-62
32445867-3	2020	Previously, we reported that the [2Fe-2S] clusters in mitoNEET can be reduced by the reduced flavin mononucleotide (FMNH2) and oxidized by oxygen or ubiquinone-2, suggesting that mitoNEET may act as a novel redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	Oxygen	263-269	CDGSH iron sulfur domain 1	Homo sapiens	179-187
32445867-3	2020	Previously, we reported that the [2Fe-2S] clusters in mitoNEET can be reduced by the reduced flavin mononucleotide (FMNH2) and oxidized by oxygen or ubiquinone-2, suggesting that mitoNEET may act as a novel redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	Ubiquinone	273-283	CDGSH iron sulfur domain 1	Homo sapiens	54-62
32445867-3	2020	Previously, we reported that the [2Fe-2S] clusters in mitoNEET can be reduced by the reduced flavin mononucleotide (FMNH2) and oxidized by oxygen or ubiquinone-2, suggesting that mitoNEET may act as a novel redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	Ubiquinone	273-283	CDGSH iron sulfur domain 1	Homo sapiens	179-187
32445867-4	2020	Here, we explore the FMN binding site in mitoNEET by using FMN analogs and find that lumiflavin, like FMN, at nanomolar concentrations can mediate the redox transition of the mitoNEET [2Fe-2S] clusters in the presence of flavin reductase and NADH (100 muM) under aerobic conditions.	lumiflavin	85-95	CDGSH iron sulfur domain 1	Homo sapiens	41-49
32445867-4	2020	Here, we explore the FMN binding site in mitoNEET by using FMN analogs and find that lumiflavin, like FMN, at nanomolar concentrations can mediate the redox transition of the mitoNEET [2Fe-2S] clusters in the presence of flavin reductase and NADH (100 muM) under aerobic conditions.	lumiflavin	85-95	CDGSH iron sulfur domain 1	Homo sapiens	175-183
32445867-4	2020	Here, we explore the FMN binding site in mitoNEET by using FMN analogs and find that lumiflavin, like FMN, at nanomolar concentrations can mediate the redox transition of the mitoNEET [2Fe-2S] clusters in the presence of flavin reductase and NADH (100 muM) under aerobic conditions.	2fe-2s	185-191	CDGSH iron sulfur domain 1	Homo sapiens	41-49
32445867-4	2020	Here, we explore the FMN binding site in mitoNEET by using FMN analogs and find that lumiflavin, like FMN, at nanomolar concentrations can mediate the redox transition of the mitoNEET [2Fe-2S] clusters in the presence of flavin reductase and NADH (100 muM) under aerobic conditions.	2fe-2s	185-191	CDGSH iron sulfur domain 1	Homo sapiens	175-183
32445867-4	2020	Here, we explore the FMN binding site in mitoNEET by using FMN analogs and find that lumiflavin, like FMN, at nanomolar concentrations can mediate the redox transition of the mitoNEET [2Fe-2S] clusters in the presence of flavin reductase and NADH (100 muM) under aerobic conditions.	NAD	242-246	CDGSH iron sulfur domain 1	Homo sapiens	175-183
32445867-5	2020	The electron paramagnetic resonance (EPR) measurements show that both FMN and lumiflavin can dramatically change the EPR spectrum of the reduced mitoNEET [2Fe-2S] clusters and form a covalently bound complex with mitoNEET under blue light exposure, suggesting that FMN/lumiflavin has specific interactions with the [2Fe-2S] clusters in mitoNEET.	Flavin Mononucleotide	70-73	CDGSH iron sulfur domain 1	Homo sapiens	145-153
32445867-5	2020	The electron paramagnetic resonance (EPR) measurements show that both FMN and lumiflavin can dramatically change the EPR spectrum of the reduced mitoNEET [2Fe-2S] clusters and form a covalently bound complex with mitoNEET under blue light exposure, suggesting that FMN/lumiflavin has specific interactions with the [2Fe-2S] clusters in mitoNEET.	Flavin Mononucleotide	70-73	CDGSH iron sulfur domain 1	Homo sapiens	213-221
32445867-5	2020	The electron paramagnetic resonance (EPR) measurements show that both FMN and lumiflavin can dramatically change the EPR spectrum of the reduced mitoNEET [2Fe-2S] clusters and form a covalently bound complex with mitoNEET under blue light exposure, suggesting that FMN/lumiflavin has specific interactions with the [2Fe-2S] clusters in mitoNEET.	Flavin Mononucleotide	70-73	CDGSH iron sulfur domain 1	Homo sapiens	213-221
32445867-5	2020	The electron paramagnetic resonance (EPR) measurements show that both FMN and lumiflavin can dramatically change the EPR spectrum of the reduced mitoNEET [2Fe-2S] clusters and form a covalently bound complex with mitoNEET under blue light exposure, suggesting that FMN/lumiflavin has specific interactions with the [2Fe-2S] clusters in mitoNEET.	lumiflavin	78-88	CDGSH iron sulfur domain 1	Homo sapiens	145-153
32445867-5	2020	The electron paramagnetic resonance (EPR) measurements show that both FMN and lumiflavin can dramatically change the EPR spectrum of the reduced mitoNEET [2Fe-2S] clusters and form a covalently bound complex with mitoNEET under blue light exposure, suggesting that FMN/lumiflavin has specific interactions with the [2Fe-2S] clusters in mitoNEET.	lumiflavin	78-88	CDGSH iron sulfur domain 1	Homo sapiens	213-221
32445867-5	2020	The electron paramagnetic resonance (EPR) measurements show that both FMN and lumiflavin can dramatically change the EPR spectrum of the reduced mitoNEET [2Fe-2S] clusters and form a covalently bound complex with mitoNEET under blue light exposure, suggesting that FMN/lumiflavin has specific interactions with the [2Fe-2S] clusters in mitoNEET.	lumiflavin	78-88	CDGSH iron sulfur domain 1	Homo sapiens	213-221
32445867-5	2020	The electron paramagnetic resonance (EPR) measurements show that both FMN and lumiflavin can dramatically change the EPR spectrum of the reduced mitoNEET [2Fe-2S] clusters and form a covalently bound complex with mitoNEET under blue light exposure, suggesting that FMN/lumiflavin has specific interactions with the [2Fe-2S] clusters in mitoNEET.	2fe	155-158	CDGSH iron sulfur domain 1	Homo sapiens	145-153
32445867-5	2020	The electron paramagnetic resonance (EPR) measurements show that both FMN and lumiflavin can dramatically change the EPR spectrum of the reduced mitoNEET [2Fe-2S] clusters and form a covalently bound complex with mitoNEET under blue light exposure, suggesting that FMN/lumiflavin has specific interactions with the [2Fe-2S] clusters in mitoNEET.	Flavin Mononucleotide	265-268	CDGSH iron sulfur domain 1	Homo sapiens	145-153
32445867-5	2020	The electron paramagnetic resonance (EPR) measurements show that both FMN and lumiflavin can dramatically change the EPR spectrum of the reduced mitoNEET [2Fe-2S] clusters and form a covalently bound complex with mitoNEET under blue light exposure, suggesting that FMN/lumiflavin has specific interactions with the [2Fe-2S] clusters in mitoNEET.	Flavin Mononucleotide	265-268	CDGSH iron sulfur domain 1	Homo sapiens	213-221
32445867-5	2020	The electron paramagnetic resonance (EPR) measurements show that both FMN and lumiflavin can dramatically change the EPR spectrum of the reduced mitoNEET [2Fe-2S] clusters and form a covalently bound complex with mitoNEET under blue light exposure, suggesting that FMN/lumiflavin has specific interactions with the [2Fe-2S] clusters in mitoNEET.	Flavin Mononucleotide	265-268	CDGSH iron sulfur domain 1	Homo sapiens	213-221
32445867-5	2020	The electron paramagnetic resonance (EPR) measurements show that both FMN and lumiflavin can dramatically change the EPR spectrum of the reduced mitoNEET [2Fe-2S] clusters and form a covalently bound complex with mitoNEET under blue light exposure, suggesting that FMN/lumiflavin has specific interactions with the [2Fe-2S] clusters in mitoNEET.	lumiflavin	269-279	CDGSH iron sulfur domain 1	Homo sapiens	145-153
32445867-5	2020	The electron paramagnetic resonance (EPR) measurements show that both FMN and lumiflavin can dramatically change the EPR spectrum of the reduced mitoNEET [2Fe-2S] clusters and form a covalently bound complex with mitoNEET under blue light exposure, suggesting that FMN/lumiflavin has specific interactions with the [2Fe-2S] clusters in mitoNEET.	lumiflavin	269-279	CDGSH iron sulfur domain 1	Homo sapiens	213-221
32445867-5	2020	The electron paramagnetic resonance (EPR) measurements show that both FMN and lumiflavin can dramatically change the EPR spectrum of the reduced mitoNEET [2Fe-2S] clusters and form a covalently bound complex with mitoNEET under blue light exposure, suggesting that FMN/lumiflavin has specific interactions with the [2Fe-2S] clusters in mitoNEET.	lumiflavin	269-279	CDGSH iron sulfur domain 1	Homo sapiens	213-221
31784520-0	2019	Glycogen branching enzyme controls cellular iron homeostasis via Iron Regulatory Protein 1 and mitoNEET.	Iron	44-48	CDGSH iron sulfur domain 1	Homo sapiens	95-103
31784520-6	2019	AGBE binds specifically to holo-IRP1 and to mitoNEET, a protein capable of repairing IRP1 iron-sulphur clusters.	Iron	90-94	CDGSH iron sulfur domain 1	Homo sapiens	44-52
29666474-3	2019	Other members of the CDGSH iron sulfur domain (CISD) family include mitoNEET/CISD1 and Miner2/CISD3.	Iron	27-31	CDGSH iron sulfur domain 1	Homo sapiens	68-76
31050203-4	2019	In addition to elevated levels of proteins known to be involved in ATP metabolic processes, our results identified increased levels of mitoNEET (Cisd1), an iron-sulfur containing protein that regulates mitochondrial bioenergetics.	Adenosine Triphosphate	67-70	CDGSH iron sulfur domain 1	Homo sapiens	135-143
31050203-4	2019	In addition to elevated levels of proteins known to be involved in ATP metabolic processes, our results identified increased levels of mitoNEET (Cisd1), an iron-sulfur containing protein that regulates mitochondrial bioenergetics.	Adenosine Triphosphate	67-70	CDGSH iron sulfur domain 1	Homo sapiens	145-150
31050203-4	2019	In addition to elevated levels of proteins known to be involved in ATP metabolic processes, our results identified increased levels of mitoNEET (Cisd1), an iron-sulfur containing protein that regulates mitochondrial bioenergetics.	Iron	156-160	CDGSH iron sulfur domain 1	Homo sapiens	135-143
31050203-4	2019	In addition to elevated levels of proteins known to be involved in ATP metabolic processes, our results identified increased levels of mitoNEET (Cisd1), an iron-sulfur containing protein that regulates mitochondrial bioenergetics.	Iron	156-160	CDGSH iron sulfur domain 1	Homo sapiens	145-150
31050203-4	2019	In addition to elevated levels of proteins known to be involved in ATP metabolic processes, our results identified increased levels of mitoNEET (Cisd1), an iron-sulfur containing protein that regulates mitochondrial bioenergetics.	Sulfur	161-167	CDGSH iron sulfur domain 1	Homo sapiens	135-143
31050203-4	2019	In addition to elevated levels of proteins known to be involved in ATP metabolic processes, our results identified increased levels of mitoNEET (Cisd1), an iron-sulfur containing protein that regulates mitochondrial bioenergetics.	Sulfur	161-167	CDGSH iron sulfur domain 1	Homo sapiens	145-150
31050203-5	2019	We found that mitoNEET overexpression plays a cell-type specific role in ATP synthesis and in neuronal cells promotes ATP generation.	Adenosine Triphosphate	73-76	CDGSH iron sulfur domain 1	Homo sapiens	14-22
31050203-5	2019	We found that mitoNEET overexpression plays a cell-type specific role in ATP synthesis and in neuronal cells promotes ATP generation.	Adenosine Triphosphate	118-121	CDGSH iron sulfur domain 1	Homo sapiens	14-22
31050203-6	2019	The elevated ATP levels in SH-SY5Y neuroblastoma cells were associated with increased mitochondrial membrane potential and a fragmented mitochondrial network, further supporting a role for mitoNEET as a key regulator of mitochondrial function.	Adenosine Triphosphate	13-16	CDGSH iron sulfur domain 1	Homo sapiens	189-197
30805086-0	2019	Isoliquiritigenin Induces Mitochondrial Dysfunction and Apoptosis by Inhibiting mitoNEET in a Reactive Oxygen Species-Dependent Manner in A375 Human Melanoma Cells.	isoliquiritigenin	0-17	CDGSH iron sulfur domain 1	Homo sapiens	80-88
30805086-0	2019	Isoliquiritigenin Induces Mitochondrial Dysfunction and Apoptosis by Inhibiting mitoNEET in a Reactive Oxygen Species-Dependent Manner in A375 Human Melanoma Cells.	Reactive Oxygen Species	94-117	CDGSH iron sulfur domain 1	Homo sapiens	80-88
30805086-2	2019	In the current study, we found that isoliquiritigenin (ISL), one of the components of the root of Glycyrrhiza glabra L., could decrease the expression of mitoNEET in A375 melanoma cells.	isoliquiritigenin	36-53	CDGSH iron sulfur domain 1	Homo sapiens	154-162
30805086-3	2019	We also demonstrated that mitoNEET could regulate the content of reactive oxygen species (ROS), by showing that the ISL-mediated increase in the cellular ROS content could be mitigated by the mitoNEET overexpression.	Reactive Oxygen Species	65-88	CDGSH iron sulfur domain 1	Homo sapiens	26-34
30805086-3	2019	We also demonstrated that mitoNEET could regulate the content of reactive oxygen species (ROS), by showing that the ISL-mediated increase in the cellular ROS content could be mitigated by the mitoNEET overexpression.	Reactive Oxygen Species	65-88	CDGSH iron sulfur domain 1	Homo sapiens	192-200
30805086-3	2019	We also demonstrated that mitoNEET could regulate the content of reactive oxygen species (ROS), by showing that the ISL-mediated increase in the cellular ROS content could be mitigated by the mitoNEET overexpression.	Reactive Oxygen Species	90-93	CDGSH iron sulfur domain 1	Homo sapiens	26-34
30805086-3	2019	We also demonstrated that mitoNEET could regulate the content of reactive oxygen species (ROS), by showing that the ISL-mediated increase in the cellular ROS content could be mitigated by the mitoNEET overexpression.	Reactive Oxygen Species	90-93	CDGSH iron sulfur domain 1	Homo sapiens	192-200
30805086-3	2019	We also demonstrated that mitoNEET could regulate the content of reactive oxygen species (ROS), by showing that the ISL-mediated increase in the cellular ROS content could be mitigated by the mitoNEET overexpression.	Reactive Oxygen Species	154-157	CDGSH iron sulfur domain 1	Homo sapiens	26-34
30805086-3	2019	We also demonstrated that mitoNEET could regulate the content of reactive oxygen species (ROS), by showing that the ISL-mediated increase in the cellular ROS content could be mitigated by the mitoNEET overexpression.	Reactive Oxygen Species	154-157	CDGSH iron sulfur domain 1	Homo sapiens	192-200
30805086-6	2019	These findings indicated that ISL could decrease the expression of mitoNEET, which regulated ROS content and subsequently induced mitochondrial dysfunction and apoptosis in A375 cells.	Reactive Oxygen Species	93-96	CDGSH iron sulfur domain 1	Homo sapiens	67-75
30576128-13	2019	These findings add to the understanding of [2Fe-2S] cluster nitrosylation and will help to identify DNICs resulting from the reaction of NO with Fe/S cofactors featuring alternative, proton-responsive histidine ligands such as the Rieske and mitoNEET [2Fe-2S] clusters.	Histidine	201-210	CDGSH iron sulfur domain 1	Homo sapiens	242-250
31527235-1	2019	MitoNEET is an outer mitochondrial membrane protein essential for sensing and regulation of iron and reactive oxygen species (ROS) homeostasis.	Iron	92-96	CDGSH iron sulfur domain 1	Homo sapiens	0-8
31527235-1	2019	MitoNEET is an outer mitochondrial membrane protein essential for sensing and regulation of iron and reactive oxygen species (ROS) homeostasis.	Reactive Oxygen Species	101-124	CDGSH iron sulfur domain 1	Homo sapiens	0-8
31527235-1	2019	MitoNEET is an outer mitochondrial membrane protein essential for sensing and regulation of iron and reactive oxygen species (ROS) homeostasis.	Reactive Oxygen Species	126-129	CDGSH iron sulfur domain 1	Homo sapiens	0-8
31527235-8	2019	Addition of the VDAC inhibitor 4,4"-diisothiocyanatostilbene-2,2"-disulfonate (DIDS) prevents both mitoNEET binding in vitro and mitoNEET-dependent mitochondrial iron accumulation in situ.	4,4"-diisothiocyanatostilbene-2,2"-disulfonate	31-77	CDGSH iron sulfur domain 1	Homo sapiens	99-107
31527235-8	2019	Addition of the VDAC inhibitor 4,4"-diisothiocyanatostilbene-2,2"-disulfonate (DIDS) prevents both mitoNEET binding in vitro and mitoNEET-dependent mitochondrial iron accumulation in situ.	4,4"-diisothiocyanatostilbene-2,2"-disulfonate	31-77	CDGSH iron sulfur domain 1	Homo sapiens	129-137
31527235-8	2019	Addition of the VDAC inhibitor 4,4"-diisothiocyanatostilbene-2,2"-disulfonate (DIDS) prevents both mitoNEET binding in vitro and mitoNEET-dependent mitochondrial iron accumulation in situ.	4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid	79-83	CDGSH iron sulfur domain 1	Homo sapiens	99-107
31527235-8	2019	Addition of the VDAC inhibitor 4,4"-diisothiocyanatostilbene-2,2"-disulfonate (DIDS) prevents both mitoNEET binding in vitro and mitoNEET-dependent mitochondrial iron accumulation in situ.	4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid	79-83	CDGSH iron sulfur domain 1	Homo sapiens	129-137
31527235-8	2019	Addition of the VDAC inhibitor 4,4"-diisothiocyanatostilbene-2,2"-disulfonate (DIDS) prevents both mitoNEET binding in vitro and mitoNEET-dependent mitochondrial iron accumulation in situ.	Iron	162-166	CDGSH iron sulfur domain 1	Homo sapiens	129-137
31010844-3	2019	REH/Ara-C 1) was not crossresistant to vincristine or methotrexate; 2) showed a similar proliferation rate and cell surface marker expression as parental REH; 3) demonstrated decreased chemotaxis toward bone marrow stromal cells; and 4) expressed higher transcript levels of cytidine deaminase (CDA) and mitoNEET (CISD1) than the parental REH cell line.	Cytarabine	4-9	CDGSH iron sulfur domain 1	Homo sapiens	304-312
31010844-3	2019	REH/Ara-C 1) was not crossresistant to vincristine or methotrexate; 2) showed a similar proliferation rate and cell surface marker expression as parental REH; 3) demonstrated decreased chemotaxis toward bone marrow stromal cells; and 4) expressed higher transcript levels of cytidine deaminase (CDA) and mitoNEET (CISD1) than the parental REH cell line.	Cytarabine	4-9	CDGSH iron sulfur domain 1	Homo sapiens	314-319
31117349-0	2019	4-Hydroxynonenal and 4-Oxononenal Differentially Bind to the Redox Sensor MitoNEET.	4-hydroxy-2-nonenal	0-16	CDGSH iron sulfur domain 1	Homo sapiens	74-82
31117349-0	2019	4-Hydroxynonenal and 4-Oxononenal Differentially Bind to the Redox Sensor MitoNEET.	ORTHO-ONE	21-33	CDGSH iron sulfur domain 1	Homo sapiens	74-82
31117349-1	2019	MitoNEET is a CDGSH iron-sulfur protein that has been a target for drug development for diseases such as type-2 diabetes, cancer, and Parkinson"s disease.	Iron	20-24	CDGSH iron sulfur domain 1	Homo sapiens	0-8
31117349-1	2019	MitoNEET is a CDGSH iron-sulfur protein that has been a target for drug development for diseases such as type-2 diabetes, cancer, and Parkinson"s disease.	Sulfur	25-31	CDGSH iron sulfur domain 1	Homo sapiens	0-8
31117349-2	2019	Functions proposed for mitoNEET are as a redox sensor and regulator of free iron in the mitochondria.	Iron	76-80	CDGSH iron sulfur domain 1	Homo sapiens	23-31
31117349-3	2019	We have investigated the reactivity of mitoNEET toward the reactive electrophiles 4-hydroxynonenal (HNE) and 4-oxononenal (ONE) that are produced from the oxidation of polyunsaturated fatty acid during oxidative stress.	4-hydroxy-2-nonenal	82-98	CDGSH iron sulfur domain 1	Homo sapiens	39-47
31117349-3	2019	We have investigated the reactivity of mitoNEET toward the reactive electrophiles 4-hydroxynonenal (HNE) and 4-oxononenal (ONE) that are produced from the oxidation of polyunsaturated fatty acid during oxidative stress.	4-hydroxy-2-nonenal	100-103	CDGSH iron sulfur domain 1	Homo sapiens	39-47
31117349-3	2019	We have investigated the reactivity of mitoNEET toward the reactive electrophiles 4-hydroxynonenal (HNE) and 4-oxononenal (ONE) that are produced from the oxidation of polyunsaturated fatty acid during oxidative stress.	ORTHO-ONE	109-121	CDGSH iron sulfur domain 1	Homo sapiens	39-47
31117349-3	2019	We have investigated the reactivity of mitoNEET toward the reactive electrophiles 4-hydroxynonenal (HNE) and 4-oxononenal (ONE) that are produced from the oxidation of polyunsaturated fatty acid during oxidative stress.	Fatty Acids, Unsaturated	168-194	CDGSH iron sulfur domain 1	Homo sapiens	39-47
29666474-3	2019	Other members of the CDGSH iron sulfur domain (CISD) family include mitoNEET/CISD1 and Miner2/CISD3.	Iron	27-31	CDGSH iron sulfur domain 1	Homo sapiens	77-82
29666474-3	2019	Other members of the CDGSH iron sulfur domain (CISD) family include mitoNEET/CISD1 and Miner2/CISD3.	Sulfur	32-38	CDGSH iron sulfur domain 1	Homo sapiens	68-76
29666474-3	2019	Other members of the CDGSH iron sulfur domain (CISD) family include mitoNEET/CISD1 and Miner2/CISD3.	Sulfur	32-38	CDGSH iron sulfur domain 1	Homo sapiens	77-82
30204426-0	2018	The H2O2-Resistant Fe-S Redox Switch MitoNEET Acts as a pH Sensor To Repair Stress-Damaged Fe-S Protein.	Hydrogen Peroxide	4-8	CDGSH iron sulfur domain 1	Homo sapiens	37-45
29666474-3	2019	Other members of the CDGSH iron sulfur domain (CISD) family include mitoNEET/CISD1 and Miner2/CISD3.	cdgsh	21-26	CDGSH iron sulfur domain 1	Homo sapiens	68-76
29666474-3	2019	Other members of the CDGSH iron sulfur domain (CISD) family include mitoNEET/CISD1 and Miner2/CISD3.	cdgsh	21-26	CDGSH iron sulfur domain 1	Homo sapiens	77-82
32382661-0	2019	Crystal structure of the mitochondrial protein mitoNEET bound to a benze-sulfonide ligand.	benze-sulfonide	67-82	CDGSH iron sulfur domain 1	Homo sapiens	47-55
32382661-3	2019	Here we report the crystal structure of the soluble domain of human mitoNEET with a sulfonamide ligand, furosemide.	Sulfonamides	84-95	CDGSH iron sulfur domain 1	Homo sapiens	68-76
32382661-3	2019	Here we report the crystal structure of the soluble domain of human mitoNEET with a sulfonamide ligand, furosemide.	Furosemide	104-114	CDGSH iron sulfur domain 1	Homo sapiens	68-76
30204426-0	2018	The H2O2-Resistant Fe-S Redox Switch MitoNEET Acts as a pH Sensor To Repair Stress-Damaged Fe-S Protein.	Iron	19-23	CDGSH iron sulfur domain 1	Homo sapiens	37-45
30204426-0	2018	The H2O2-Resistant Fe-S Redox Switch MitoNEET Acts as a pH Sensor To Repair Stress-Damaged Fe-S Protein.	Iron	91-95	CDGSH iron sulfur domain 1	Homo sapiens	37-45
29704621-1	2018	Increasing evidence suggests that the mitochondrial outer membrane protein mitoNEET is a key regulator of energy metabolism, iron homeostasis, and production of reactive oxygen species in mitochondria.	Iron	125-129	CDGSH iron sulfur domain 1	Homo sapiens	75-83
29704621-1	2018	Increasing evidence suggests that the mitochondrial outer membrane protein mitoNEET is a key regulator of energy metabolism, iron homeostasis, and production of reactive oxygen species in mitochondria.	Reactive Oxygen Species	161-184	CDGSH iron sulfur domain 1	Homo sapiens	75-83
29704621-2	2018	Previously, we reported that mitoNEET is a redox enzyme that catalyzes electron transfer from the reduced flavin mononucleotide (FMNH2) to oxygen or ubiquinone via its unique [2Fe-2S] clusters.	Flavin Mononucleotide	106-127	CDGSH iron sulfur domain 1	Homo sapiens	29-37
29704621-2	2018	Previously, we reported that mitoNEET is a redox enzyme that catalyzes electron transfer from the reduced flavin mononucleotide (FMNH2) to oxygen or ubiquinone via its unique [2Fe-2S] clusters.	flavin mononucleotide hydroquinone	129-134	CDGSH iron sulfur domain 1	Homo sapiens	29-37
29704621-2	2018	Previously, we reported that mitoNEET is a redox enzyme that catalyzes electron transfer from the reduced flavin mononucleotide (FMNH2) to oxygen or ubiquinone via its unique [2Fe-2S] clusters.	Oxygen	139-145	CDGSH iron sulfur domain 1	Homo sapiens	29-37
29704621-2	2018	Previously, we reported that mitoNEET is a redox enzyme that catalyzes electron transfer from the reduced flavin mononucleotide (FMNH2) to oxygen or ubiquinone via its unique [2Fe-2S] clusters.	Ubiquinone	149-159	CDGSH iron sulfur domain 1	Homo sapiens	29-37
29704621-4	2018	We find that the mitoNEET [2Fe-2S] clusters are rapidly reduced by a catalytic amount of FMNH2 which is reduced by flavin reductase and an equivalent amount of NADH under anaerobic conditions.	NAD	160-164	CDGSH iron sulfur domain 1	Homo sapiens	17-25
29704621-5	2018	When the reduced mitoNEET [2Fe-2S] clusters are exposed to air, the [2Fe-2S] clusters are slowly oxidized by oxygen at a rate constant of about 6.0 M-1 s-1.	Oxygen	109-115	CDGSH iron sulfur domain 1	Homo sapiens	17-25
29704621-6	2018	Compared with oxygen, ubiquinone-2 has a much higher activity to oxidize the reduced mitoNEET [2Fe-2S] clusters at a rate constant of about 3.0 x 103 M-1 s-1 under anaerobic conditions.	Oxygen	14-20	CDGSH iron sulfur domain 1	Homo sapiens	85-93
29704621-7	2018	Under aerobic conditions, the mitoNEET [2Fe-2S] clusters can still be reduced by FMNH2 in the presence of flavin reductase and excess NADH.	NAD	134-138	CDGSH iron sulfur domain 1	Homo sapiens	30-38
29704621-8	2018	However, when NADH is completely consumed, the reduced mitoNEET [2Fe-2S] clusters are gradually oxidized by oxygen.	NAD	14-18	CDGSH iron sulfur domain 1	Homo sapiens	55-63
29704621-8	2018	However, when NADH is completely consumed, the reduced mitoNEET [2Fe-2S] clusters are gradually oxidized by oxygen.	Oxygen	108-114	CDGSH iron sulfur domain 1	Homo sapiens	55-63
29704621-9	2018	Addition of ubiquinone-2 also rapidly oxidizes the pre-reduced mitoNEET [2Fe-2S] clusters and effectively prevents the FMNH2-mediated reduction of the mitoNEET [2Fe-2S] clusters under aerobic conditions.	Ubiquinone	12-22	CDGSH iron sulfur domain 1	Homo sapiens	63-71
29704621-9	2018	Addition of ubiquinone-2 also rapidly oxidizes the pre-reduced mitoNEET [2Fe-2S] clusters and effectively prevents the FMNH2-mediated reduction of the mitoNEET [2Fe-2S] clusters under aerobic conditions.	Ubiquinone	12-22	CDGSH iron sulfur domain 1	Homo sapiens	151-159
29704621-10	2018	The results suggest that ubiquinone may act as an intrinsic oxidant of the reduced mitoNEET [2Fe-2S] clusters in mitochondria under aerobic and anaerobic conditions.	Ubiquinone	25-35	CDGSH iron sulfur domain 1	Homo sapiens	83-91
28648056-2	2017	Recently, human mitoNEET has been shown to be implicated in Fe/S cluster repair of cytosolic iron regulatory protein 1 (IRP1), a key regulator of cellular iron homeostasis in mammalian cells.	Iron	93-97	CDGSH iron sulfur domain 1	Homo sapiens	16-24
29239323-0	2017	Targeting mitoNEET with pioglitazone for therapeutic neuroprotection after spinal cord injury.	Pioglitazone	24-36	CDGSH iron sulfur domain 1	Homo sapiens	10-18
28461337-0	2017	The mitochondrial outer membrane protein mitoNEET is a redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	flavin mononucleotide hydroquinone	102-107	CDGSH iron sulfur domain 1	Homo sapiens	41-49
28461337-0	2017	The mitochondrial outer membrane protein mitoNEET is a redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	Oxygen	111-117	CDGSH iron sulfur domain 1	Homo sapiens	41-49
28461337-6	2017	In the presence of FMN, NADH, and flavin reductase, which reduces FMN to FMNH2 using NADH as the electron donor, mitoNEET mediates oxidation of NADH with a concomitant reduction of oxygen.	NAD	85-89	CDGSH iron sulfur domain 1	Homo sapiens	113-121
28461337-6	2017	In the presence of FMN, NADH, and flavin reductase, which reduces FMN to FMNH2 using NADH as the electron donor, mitoNEET mediates oxidation of NADH with a concomitant reduction of oxygen.	NAD	85-89	CDGSH iron sulfur domain 1	Homo sapiens	113-121
28461337-0	2017	The mitochondrial outer membrane protein mitoNEET is a redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.	Ubiquinone	121-131	CDGSH iron sulfur domain 1	Homo sapiens	41-49
28461337-6	2017	In the presence of FMN, NADH, and flavin reductase, which reduces FMN to FMNH2 using NADH as the electron donor, mitoNEET mediates oxidation of NADH with a concomitant reduction of oxygen.	Oxygen	181-187	CDGSH iron sulfur domain 1	Homo sapiens	113-121
28461337-1	2017	Increasing evidence suggests that mitoNEET, a target of the type II diabetes drug pioglitazone, is a key regulator of energy metabolism in mitochondria.	Pioglitazone	82-94	CDGSH iron sulfur domain 1	Homo sapiens	34-42
28461337-4	2017	Previous studies have shown that mitoNEET specifically interacts with the reduced flavin mononucleotide (FMNH2) and that FMNH2 can quickly reduce the mitoNEET [2Fe-2S] clusters.	Flavin Mononucleotide	82-103	CDGSH iron sulfur domain 1	Homo sapiens	33-41
28461337-7	2017	Ubiquinone-2, an analog of ubiquinone-10, can also oxidize the reduced mitoNEET [2Fe-2S] clusters under anaerobic or aerobic conditions.	Ubiquinone Q2	0-12	CDGSH iron sulfur domain 1	Homo sapiens	71-79
28461337-7	2017	Ubiquinone-2, an analog of ubiquinone-10, can also oxidize the reduced mitoNEET [2Fe-2S] clusters under anaerobic or aerobic conditions.	Ubiquinone Q2	27-40	CDGSH iron sulfur domain 1	Homo sapiens	71-79
28461337-5	2017	Here we report that the reduced mitoNEET [2Fe-2S] clusters can be readily oxidized by oxygen.	Oxygen	86-92	CDGSH iron sulfur domain 1	Homo sapiens	32-40
28461337-8	2017	Compared with oxygen, ubiquinone-2 is more efficient in oxidizing the mitoNEET [2Fe-2S] clusters, suggesting that ubiquinone could be an intrinsic electron acceptor of the reduced mitoNEET [2Fe-2S] clusters in mitochondria.	Oxygen	14-20	CDGSH iron sulfur domain 1	Homo sapiens	70-78
28461337-6	2017	In the presence of FMN, NADH, and flavin reductase, which reduces FMN to FMNH2 using NADH as the electron donor, mitoNEET mediates oxidation of NADH with a concomitant reduction of oxygen.	Flavin Mononucleotide	19-22	CDGSH iron sulfur domain 1	Homo sapiens	113-121
28461337-8	2017	Compared with oxygen, ubiquinone-2 is more efficient in oxidizing the mitoNEET [2Fe-2S] clusters, suggesting that ubiquinone could be an intrinsic electron acceptor of the reduced mitoNEET [2Fe-2S] clusters in mitochondria.	Oxygen	14-20	CDGSH iron sulfur domain 1	Homo sapiens	180-188
28461337-6	2017	In the presence of FMN, NADH, and flavin reductase, which reduces FMN to FMNH2 using NADH as the electron donor, mitoNEET mediates oxidation of NADH with a concomitant reduction of oxygen.	NAD	24-28	CDGSH iron sulfur domain 1	Homo sapiens	113-121
28461337-8	2017	Compared with oxygen, ubiquinone-2 is more efficient in oxidizing the mitoNEET [2Fe-2S] clusters, suggesting that ubiquinone could be an intrinsic electron acceptor of the reduced mitoNEET [2Fe-2S] clusters in mitochondria.	Ubiquinone Q2	22-34	CDGSH iron sulfur domain 1	Homo sapiens	70-78
28461337-8	2017	Compared with oxygen, ubiquinone-2 is more efficient in oxidizing the mitoNEET [2Fe-2S] clusters, suggesting that ubiquinone could be an intrinsic electron acceptor of the reduced mitoNEET [2Fe-2S] clusters in mitochondria.	Ubiquinone Q2	22-34	CDGSH iron sulfur domain 1	Homo sapiens	180-188
28461337-6	2017	In the presence of FMN, NADH, and flavin reductase, which reduces FMN to FMNH2 using NADH as the electron donor, mitoNEET mediates oxidation of NADH with a concomitant reduction of oxygen.	Flavin Mononucleotide	66-69	CDGSH iron sulfur domain 1	Homo sapiens	113-121
28082676-8	2017	Although the [2Fe-2S] cluster in purified human mitoNEET and Miner1 fails to bind nitric oxide, a single mutation of Asp-96 to Val in mitoNEET or Asp-123 to Val in Miner1 facilitates nitric oxide binding in the [2Fe-2S] cluster, indicating that a subtle change of protein structure may switch mitoNEET and Miner1 to bind nitric oxide.	Nitric Oxide	82-94	CDGSH iron sulfur domain 1	Homo sapiens	48-56
28461337-8	2017	Compared with oxygen, ubiquinone-2 is more efficient in oxidizing the mitoNEET [2Fe-2S] clusters, suggesting that ubiquinone could be an intrinsic electron acceptor of the reduced mitoNEET [2Fe-2S] clusters in mitochondria.	2fe-2s	80-86	CDGSH iron sulfur domain 1	Homo sapiens	70-78
28461337-8	2017	Compared with oxygen, ubiquinone-2 is more efficient in oxidizing the mitoNEET [2Fe-2S] clusters, suggesting that ubiquinone could be an intrinsic electron acceptor of the reduced mitoNEET [2Fe-2S] clusters in mitochondria.	2fe-2s	80-86	CDGSH iron sulfur domain 1	Homo sapiens	180-188
28461337-8	2017	Compared with oxygen, ubiquinone-2 is more efficient in oxidizing the mitoNEET [2Fe-2S] clusters, suggesting that ubiquinone could be an intrinsic electron acceptor of the reduced mitoNEET [2Fe-2S] clusters in mitochondria.	Ubiquinone	22-32	CDGSH iron sulfur domain 1	Homo sapiens	70-78
28461337-8	2017	Compared with oxygen, ubiquinone-2 is more efficient in oxidizing the mitoNEET [2Fe-2S] clusters, suggesting that ubiquinone could be an intrinsic electron acceptor of the reduced mitoNEET [2Fe-2S] clusters in mitochondria.	Ubiquinone	22-32	CDGSH iron sulfur domain 1	Homo sapiens	180-188
28461337-8	2017	Compared with oxygen, ubiquinone-2 is more efficient in oxidizing the mitoNEET [2Fe-2S] clusters, suggesting that ubiquinone could be an intrinsic electron acceptor of the reduced mitoNEET [2Fe-2S] clusters in mitochondria.	2fe-2s	190-196	CDGSH iron sulfur domain 1	Homo sapiens	70-78
28461337-8	2017	Compared with oxygen, ubiquinone-2 is more efficient in oxidizing the mitoNEET [2Fe-2S] clusters, suggesting that ubiquinone could be an intrinsic electron acceptor of the reduced mitoNEET [2Fe-2S] clusters in mitochondria.	2fe-2s	190-196	CDGSH iron sulfur domain 1	Homo sapiens	180-188
28461337-9	2017	Pioglitazone or its analog NL-1 appears to inhibit the electron transfer activity of mitoNEET by forming a unique complex with mitoNEET and FMNH2 The results suggest that mitoNEET is a redox enzyme that may promote oxidation of NADH to facilitate enhanced glycolysis in the cytosol and that pioglitazone may regulate energy metabolism in mitochondria by inhibiting the electron transfer activity of mitoNEET.	Pioglitazone	0-12	CDGSH iron sulfur domain 1	Homo sapiens	85-93
28461337-9	2017	Pioglitazone or its analog NL-1 appears to inhibit the electron transfer activity of mitoNEET by forming a unique complex with mitoNEET and FMNH2 The results suggest that mitoNEET is a redox enzyme that may promote oxidation of NADH to facilitate enhanced glycolysis in the cytosol and that pioglitazone may regulate energy metabolism in mitochondria by inhibiting the electron transfer activity of mitoNEET.	Pioglitazone	0-12	CDGSH iron sulfur domain 1	Homo sapiens	127-135
28461337-9	2017	Pioglitazone or its analog NL-1 appears to inhibit the electron transfer activity of mitoNEET by forming a unique complex with mitoNEET and FMNH2 The results suggest that mitoNEET is a redox enzyme that may promote oxidation of NADH to facilitate enhanced glycolysis in the cytosol and that pioglitazone may regulate energy metabolism in mitochondria by inhibiting the electron transfer activity of mitoNEET.	Pioglitazone	0-12	CDGSH iron sulfur domain 1	Homo sapiens	127-135
28461337-9	2017	Pioglitazone or its analog NL-1 appears to inhibit the electron transfer activity of mitoNEET by forming a unique complex with mitoNEET and FMNH2 The results suggest that mitoNEET is a redox enzyme that may promote oxidation of NADH to facilitate enhanced glycolysis in the cytosol and that pioglitazone may regulate energy metabolism in mitochondria by inhibiting the electron transfer activity of mitoNEET.	Pioglitazone	0-12	CDGSH iron sulfur domain 1	Homo sapiens	127-135
28461337-9	2017	Pioglitazone or its analog NL-1 appears to inhibit the electron transfer activity of mitoNEET by forming a unique complex with mitoNEET and FMNH2 The results suggest that mitoNEET is a redox enzyme that may promote oxidation of NADH to facilitate enhanced glycolysis in the cytosol and that pioglitazone may regulate energy metabolism in mitochondria by inhibiting the electron transfer activity of mitoNEET.	NAD	228-232	CDGSH iron sulfur domain 1	Homo sapiens	85-93
28461337-9	2017	Pioglitazone or its analog NL-1 appears to inhibit the electron transfer activity of mitoNEET by forming a unique complex with mitoNEET and FMNH2 The results suggest that mitoNEET is a redox enzyme that may promote oxidation of NADH to facilitate enhanced glycolysis in the cytosol and that pioglitazone may regulate energy metabolism in mitochondria by inhibiting the electron transfer activity of mitoNEET.	NAD	228-232	CDGSH iron sulfur domain 1	Homo sapiens	127-135
28461337-9	2017	Pioglitazone or its analog NL-1 appears to inhibit the electron transfer activity of mitoNEET by forming a unique complex with mitoNEET and FMNH2 The results suggest that mitoNEET is a redox enzyme that may promote oxidation of NADH to facilitate enhanced glycolysis in the cytosol and that pioglitazone may regulate energy metabolism in mitochondria by inhibiting the electron transfer activity of mitoNEET.	NAD	228-232	CDGSH iron sulfur domain 1	Homo sapiens	127-135
28461337-9	2017	Pioglitazone or its analog NL-1 appears to inhibit the electron transfer activity of mitoNEET by forming a unique complex with mitoNEET and FMNH2 The results suggest that mitoNEET is a redox enzyme that may promote oxidation of NADH to facilitate enhanced glycolysis in the cytosol and that pioglitazone may regulate energy metabolism in mitochondria by inhibiting the electron transfer activity of mitoNEET.	NAD	228-232	CDGSH iron sulfur domain 1	Homo sapiens	127-135
28461337-9	2017	Pioglitazone or its analog NL-1 appears to inhibit the electron transfer activity of mitoNEET by forming a unique complex with mitoNEET and FMNH2 The results suggest that mitoNEET is a redox enzyme that may promote oxidation of NADH to facilitate enhanced glycolysis in the cytosol and that pioglitazone may regulate energy metabolism in mitochondria by inhibiting the electron transfer activity of mitoNEET.	Pioglitazone	291-303	CDGSH iron sulfur domain 1	Homo sapiens	85-93
28461337-9	2017	Pioglitazone or its analog NL-1 appears to inhibit the electron transfer activity of mitoNEET by forming a unique complex with mitoNEET and FMNH2 The results suggest that mitoNEET is a redox enzyme that may promote oxidation of NADH to facilitate enhanced glycolysis in the cytosol and that pioglitazone may regulate energy metabolism in mitochondria by inhibiting the electron transfer activity of mitoNEET.	Pioglitazone	291-303	CDGSH iron sulfur domain 1	Homo sapiens	127-135
28461337-9	2017	Pioglitazone or its analog NL-1 appears to inhibit the electron transfer activity of mitoNEET by forming a unique complex with mitoNEET and FMNH2 The results suggest that mitoNEET is a redox enzyme that may promote oxidation of NADH to facilitate enhanced glycolysis in the cytosol and that pioglitazone may regulate energy metabolism in mitochondria by inhibiting the electron transfer activity of mitoNEET.	Pioglitazone	291-303	CDGSH iron sulfur domain 1	Homo sapiens	127-135
28461337-9	2017	Pioglitazone or its analog NL-1 appears to inhibit the electron transfer activity of mitoNEET by forming a unique complex with mitoNEET and FMNH2 The results suggest that mitoNEET is a redox enzyme that may promote oxidation of NADH to facilitate enhanced glycolysis in the cytosol and that pioglitazone may regulate energy metabolism in mitochondria by inhibiting the electron transfer activity of mitoNEET.	Pioglitazone	291-303	CDGSH iron sulfur domain 1	Homo sapiens	127-135
27923678-0	2017	Flavin nucleotides act as electron shuttles mediating reduction of the [2Fe-2S] clusters in mitochondrial outer membrane protein mitoNEET.	flavin nucleotides	0-18	CDGSH iron sulfur domain 1	Homo sapiens	129-137
27870532-0	2017	Distinguishing the Protonation State of the Histidine Ligand to the Oxidized Iron-Sulfur Cluster from the MitoNEET Family of Proteins.	Histidine	44-53	CDGSH iron sulfur domain 1	Homo sapiens	106-114
27870532-0	2017	Distinguishing the Protonation State of the Histidine Ligand to the Oxidized Iron-Sulfur Cluster from the MitoNEET Family of Proteins.	Iron	77-81	CDGSH iron sulfur domain 1	Homo sapiens	106-114
27870532-0	2017	Distinguishing the Protonation State of the Histidine Ligand to the Oxidized Iron-Sulfur Cluster from the MitoNEET Family of Proteins.	Sulfur	82-88	CDGSH iron sulfur domain 1	Homo sapiens	106-114
27870532-1	2017	The iron-sulfur cluster located in the recently discovered human mitoNEET protein (and related proteins) is structurally similar to the more well-known ferredoxin and Rieske clusters.	Iron	4-8	CDGSH iron sulfur domain 1	Homo sapiens	65-73
27870532-1	2017	The iron-sulfur cluster located in the recently discovered human mitoNEET protein (and related proteins) is structurally similar to the more well-known ferredoxin and Rieske clusters.	Sulfur	9-15	CDGSH iron sulfur domain 1	Homo sapiens	65-73
27870532-2	2017	Although its biological function is uncertain, the iron-sulfur cluster in mitoNEET has been proposed to undergo proton-coupled electron transfer involving the histidine ligand to the cluster.	Iron	51-55	CDGSH iron sulfur domain 1	Homo sapiens	74-82
28055193-1	2017	MitoNEET is an outer membrane protein whose exact function remains unclear, though a role of this protein in redox and iron sensing as well as in controlling maximum mitochondrial respiratory rates has been discussed.	Iron	119-123	CDGSH iron sulfur domain 1	Homo sapiens	0-8
27870532-2	2017	Although its biological function is uncertain, the iron-sulfur cluster in mitoNEET has been proposed to undergo proton-coupled electron transfer involving the histidine ligand to the cluster.	Sulfur	56-62	CDGSH iron sulfur domain 1	Homo sapiens	74-82
27870532-2	2017	Although its biological function is uncertain, the iron-sulfur cluster in mitoNEET has been proposed to undergo proton-coupled electron transfer involving the histidine ligand to the cluster.	Histidine	159-168	CDGSH iron sulfur domain 1	Homo sapiens	74-82
27870532-4	2017	This contribution reports density functional calculations to model the structures, vibrations, and Heisenberg coupling constants (J) for high-spin (HS), broken symmetry (BS) singlet, and extended broken symmetry (EBS) singlet states of the oxidized iron-sulfur cluster from mitoNEET.	Iron	249-253	CDGSH iron sulfur domain 1	Homo sapiens	274-282
27870532-5	2017	This work suggests that J values or 15 N isotopic frequency shifts may provide methods for determining experimentally whether the histidine ligand to the oxidized iron-sulfur cluster in human mitoNEET and mitoNEET-related proteins is protonated or deprotonated.	Histidine	130-139	CDGSH iron sulfur domain 1	Homo sapiens	192-200
27870532-5	2017	This work suggests that J values or 15 N isotopic frequency shifts may provide methods for determining experimentally whether the histidine ligand to the oxidized iron-sulfur cluster in human mitoNEET and mitoNEET-related proteins is protonated or deprotonated.	Histidine	130-139	CDGSH iron sulfur domain 1	Homo sapiens	205-213
27870532-5	2017	This work suggests that J values or 15 N isotopic frequency shifts may provide methods for determining experimentally whether the histidine ligand to the oxidized iron-sulfur cluster in human mitoNEET and mitoNEET-related proteins is protonated or deprotonated.	Iron	163-167	CDGSH iron sulfur domain 1	Homo sapiens	192-200
27870532-5	2017	This work suggests that J values or 15 N isotopic frequency shifts may provide methods for determining experimentally whether the histidine ligand to the oxidized iron-sulfur cluster in human mitoNEET and mitoNEET-related proteins is protonated or deprotonated.	Iron	163-167	CDGSH iron sulfur domain 1	Homo sapiens	205-213
27870532-5	2017	This work suggests that J values or 15 N isotopic frequency shifts may provide methods for determining experimentally whether the histidine ligand to the oxidized iron-sulfur cluster in human mitoNEET and mitoNEET-related proteins is protonated or deprotonated.	Sulfur	168-174	CDGSH iron sulfur domain 1	Homo sapiens	192-200
27870532-5	2017	This work suggests that J values or 15 N isotopic frequency shifts may provide methods for determining experimentally whether the histidine ligand to the oxidized iron-sulfur cluster in human mitoNEET and mitoNEET-related proteins is protonated or deprotonated.	Sulfur	168-174	CDGSH iron sulfur domain 1	Homo sapiens	205-213
27923678-1	2017	MitoNEET, a primary target of type II diabetes drug pioglitazone, has an essential role in regulating energy metabolism, iron homeostasis, and production of reactive oxygen species in mitochondria.	Pioglitazone	52-64	CDGSH iron sulfur domain 1	Homo sapiens	0-8
27923678-1	2017	MitoNEET, a primary target of type II diabetes drug pioglitazone, has an essential role in regulating energy metabolism, iron homeostasis, and production of reactive oxygen species in mitochondria.	Iron	121-125	CDGSH iron sulfur domain 1	Homo sapiens	0-8
27923678-1	2017	MitoNEET, a primary target of type II diabetes drug pioglitazone, has an essential role in regulating energy metabolism, iron homeostasis, and production of reactive oxygen species in mitochondria.	Reactive Oxygen Species	157-180	CDGSH iron sulfur domain 1	Homo sapiens	0-8
27923678-3	2017	The C-terminal cytosolic domain of mitoNEET hosts a redox active [2Fe-2S] cluster via three cysteine and one histidine residues.	Cysteine	92-100	CDGSH iron sulfur domain 1	Homo sapiens	35-43
27923678-3	2017	The C-terminal cytosolic domain of mitoNEET hosts a redox active [2Fe-2S] cluster via three cysteine and one histidine residues.	Histidine	109-118	CDGSH iron sulfur domain 1	Homo sapiens	35-43
27923678-4	2017	Here we report that the reduced flavin nucleotides can rapidly reduce the mitoNEET [2Fe-2S] clusters under anaerobic or aerobic conditions.	flavin nucleotides	32-50	CDGSH iron sulfur domain 1	Homo sapiens	74-82
27923678-5	2017	In the presence of NADH and flavin reductase, 1 molecule of flavin nucleotide is sufficient to reduce about 100 molecules of the mitoNEET [2Fe-2S] clusters in 4min under aerobic conditions.	NAD	19-23	CDGSH iron sulfur domain 1	Homo sapiens	129-137
27923678-5	2017	In the presence of NADH and flavin reductase, 1 molecule of flavin nucleotide is sufficient to reduce about 100 molecules of the mitoNEET [2Fe-2S] clusters in 4min under aerobic conditions.	flavin nucleotide	60-77	CDGSH iron sulfur domain 1	Homo sapiens	129-137
27923678-6	2017	The electron paramagnetic resonance (EPR) measurements show that flavin mononucleotide (FMN), but not flavin adenine dinucleotide (FAD), has a specific interaction with mitoNEET.	Flavin Mononucleotide	65-86	CDGSH iron sulfur domain 1	Homo sapiens	169-177
27923678-6	2017	The electron paramagnetic resonance (EPR) measurements show that flavin mononucleotide (FMN), but not flavin adenine dinucleotide (FAD), has a specific interaction with mitoNEET.	Flavin Mononucleotide	88-91	CDGSH iron sulfur domain 1	Homo sapiens	169-177
27923678-7	2017	Molecular docking models further reveal that flavin mononucleotide binds mitoNEET at the region between the N-terminal transmembrane alpha-helix and the [2Fe-2S] cluster binding domain.	Flavin Mononucleotide	45-66	CDGSH iron sulfur domain 1	Homo sapiens	73-81
27923678-8	2017	The closest distance between the [2Fe-2S] cluster and the bound flavin mononucleotide in mitoNEET is about 10A, which could facilitate rapid electron transfer from the reduced flavin nucleotide to the [2Fe-2S] cluster in mitoNEET.	Flavin Mononucleotide	64-85	CDGSH iron sulfur domain 1	Homo sapiens	89-97
27923678-8	2017	The closest distance between the [2Fe-2S] cluster and the bound flavin mononucleotide in mitoNEET is about 10A, which could facilitate rapid electron transfer from the reduced flavin nucleotide to the [2Fe-2S] cluster in mitoNEET.	Flavin Mononucleotide	64-85	CDGSH iron sulfur domain 1	Homo sapiens	221-229
27923678-8	2017	The closest distance between the [2Fe-2S] cluster and the bound flavin mononucleotide in mitoNEET is about 10A, which could facilitate rapid electron transfer from the reduced flavin nucleotide to the [2Fe-2S] cluster in mitoNEET.	flavin nucleotide	176-193	CDGSH iron sulfur domain 1	Homo sapiens	89-97
27923678-8	2017	The closest distance between the [2Fe-2S] cluster and the bound flavin mononucleotide in mitoNEET is about 10A, which could facilitate rapid electron transfer from the reduced flavin nucleotide to the [2Fe-2S] cluster in mitoNEET.	flavin nucleotide	176-193	CDGSH iron sulfur domain 1	Homo sapiens	221-229
27923678-9	2017	The results suggest that flavin nucleotides may act as electron shuttles to reduce the mitoNEET [2Fe-2S] clusters and regulate mitochondrial functions in human cells.	flavin nucleotides	25-43	CDGSH iron sulfur domain 1	Homo sapiens	87-95
27243905-1	2016	The iron-sulfur cluster containing protein mitoNEET is known to modulate the oxidative capacity of cardiac mitochondria but its function during myocardial reperfusion injury after transient ischemia is unknown.	Iron	4-8	CDGSH iron sulfur domain 1	Homo sapiens	43-51
28882209-1	2017	MitoNEET is the first identified Fe-S protein anchored to mammalian outer mitochondrial membranes with the vast majority of the protein polypeptide located in the cytosol, including its [2Fe-2S] cluster-binding domain.	Iron	33-37	CDGSH iron sulfur domain 1	Homo sapiens	0-8
28882209-5	2017	Recently, we identified cytosolic aconitase/iron regulatory protein 1 (IRP1) as the first physiological protein acceptor of the mitoNEET Fe-S cluster in an Fe-S repair process.	Iron	137-141	CDGSH iron sulfur domain 1	Homo sapiens	128-136
28882209-5	2017	Recently, we identified cytosolic aconitase/iron regulatory protein 1 (IRP1) as the first physiological protein acceptor of the mitoNEET Fe-S cluster in an Fe-S repair process.	Iron	156-160	CDGSH iron sulfur domain 1	Homo sapiens	128-136
28882209-6	2017	This chapter describes methods to study in vitro mitoNEET Fe-S cluster transfer/repair to a bacterial ferredoxin used as a model aporeceptor and in a more comprehensive manner to cytosolic aconitase/IRP1 after a nitrosative stress using in vitro, in cellulo, and in vivo methods.	Iron	58-62	CDGSH iron sulfur domain 1	Homo sapiens	49-57
27687671-1	2016	MitoNEET (CISD1) is a 2Fe-2S iron-sulfur cluster protein belonging to the zinc-finger protein family.	Iron	29-33	CDGSH iron sulfur domain 1	Homo sapiens	0-8
27687671-1	2016	MitoNEET (CISD1) is a 2Fe-2S iron-sulfur cluster protein belonging to the zinc-finger protein family.	Iron	29-33	CDGSH iron sulfur domain 1	Homo sapiens	10-15
27687671-1	2016	MitoNEET (CISD1) is a 2Fe-2S iron-sulfur cluster protein belonging to the zinc-finger protein family.	Sulfur	34-40	CDGSH iron sulfur domain 1	Homo sapiens	0-8
27687671-1	2016	MitoNEET (CISD1) is a 2Fe-2S iron-sulfur cluster protein belonging to the zinc-finger protein family.	Sulfur	34-40	CDGSH iron sulfur domain 1	Homo sapiens	10-15
27687671-3	2016	The anti-diabetic drug pioglitazone and rosiglitazone were the first identified ligands to mitoNEET.	Pioglitazone	23-35	CDGSH iron sulfur domain 1	Homo sapiens	91-99
27687671-3	2016	The anti-diabetic drug pioglitazone and rosiglitazone were the first identified ligands to mitoNEET.	Rosiglitazone	40-53	CDGSH iron sulfur domain 1	Homo sapiens	91-99
27369364-0	2016	Retraction: Mitoneet mediates TNFalpha-induced necroptosis promoted by exposure to fructose and ethanol.	Fructose	83-91	CDGSH iron sulfur domain 1	Homo sapiens	12-20
27369364-0	2016	Retraction: Mitoneet mediates TNFalpha-induced necroptosis promoted by exposure to fructose and ethanol.	Ethanol	96-103	CDGSH iron sulfur domain 1	Homo sapiens	12-20
27510639-3	2016	Here, we show that CDGSH iron sulfur domain 1 (CISD1, also termed mitoNEET), an iron-containing outer mitochondrial membrane protein, negatively regulates ferroptotic cancer cell death.	Iron	25-29	CDGSH iron sulfur domain 1	Homo sapiens	47-52
27510639-3	2016	Here, we show that CDGSH iron sulfur domain 1 (CISD1, also termed mitoNEET), an iron-containing outer mitochondrial membrane protein, negatively regulates ferroptotic cancer cell death.	Iron	25-29	CDGSH iron sulfur domain 1	Homo sapiens	66-74
27510639-4	2016	The classical ferroptosis inducer erastin promotes CISD1 expression in an iron-dependent manner in human hepatocellular carcinoma cells (e.g., HepG2 and Hep3B).	Iron	74-78	CDGSH iron sulfur domain 1	Homo sapiens	51-56
27510639-5	2016	Genetic inhibition of CISD1 increased iron-mediated intramitochondrial lipid peroxidation, which contributes to erastin-induced ferroptosis.	Iron	38-42	CDGSH iron sulfur domain 1	Homo sapiens	22-27
27510639-5	2016	Genetic inhibition of CISD1 increased iron-mediated intramitochondrial lipid peroxidation, which contributes to erastin-induced ferroptosis.	erastin	112-119	CDGSH iron sulfur domain 1	Homo sapiens	22-27
27510639-6	2016	In contrast, stabilization of the iron sulfur cluster of CISD1 by pioglitazone inhibits mitochondrial iron uptake, lipid peroxidation, and subsequent ferroptosis.	Iron	34-38	CDGSH iron sulfur domain 1	Homo sapiens	57-62
27510639-6	2016	In contrast, stabilization of the iron sulfur cluster of CISD1 by pioglitazone inhibits mitochondrial iron uptake, lipid peroxidation, and subsequent ferroptosis.	Pioglitazone	66-78	CDGSH iron sulfur domain 1	Homo sapiens	57-62
27510639-6	2016	In contrast, stabilization of the iron sulfur cluster of CISD1 by pioglitazone inhibits mitochondrial iron uptake, lipid peroxidation, and subsequent ferroptosis.	Iron	102-106	CDGSH iron sulfur domain 1	Homo sapiens	57-62
27243905-1	2016	The iron-sulfur cluster containing protein mitoNEET is known to modulate the oxidative capacity of cardiac mitochondria but its function during myocardial reperfusion injury after transient ischemia is unknown.	Sulfur	9-15	CDGSH iron sulfur domain 1	Homo sapiens	43-51
27243905-2	2016	The purpose of this study was to analyze the impact of mitoNEET on oxidative stress induced cell death and its relation to the glutathione-redox system in cardiomyocytes in an in vitro model of hypoxia and reoxygenation (H/R).	Glutathione	127-138	CDGSH iron sulfur domain 1	Homo sapiens	55-63
27243905-5	2016	Apoptosis of both, mitoNEET-KD and control cells was diminished to comparable levels by using the antioxidants Tiron and glutathione compound glutathione reduced ethyl ester (GSH-MEE), indicating that mitoNEET-dependent apoptosis is mediated by oxidative stress.	1,2-Dihydroxybenzene-3,5-Disulfonic Acid Disodium Salt	111-116	CDGSH iron sulfur domain 1	Homo sapiens	19-27
27243905-5	2016	Apoptosis of both, mitoNEET-KD and control cells was diminished to comparable levels by using the antioxidants Tiron and glutathione compound glutathione reduced ethyl ester (GSH-MEE), indicating that mitoNEET-dependent apoptosis is mediated by oxidative stress.	Glutathione	121-132	CDGSH iron sulfur domain 1	Homo sapiens	19-27
27243905-5	2016	Apoptosis of both, mitoNEET-KD and control cells was diminished to comparable levels by using the antioxidants Tiron and glutathione compound glutathione reduced ethyl ester (GSH-MEE), indicating that mitoNEET-dependent apoptosis is mediated by oxidative stress.	Glutathione	142-153	CDGSH iron sulfur domain 1	Homo sapiens	19-27
27243905-8	2016	This effect on mitoNEET-protein was not accessible by mitoNEET-KD but was reversed by GSH-MEE.	S-ethyl glutathione	86-93	CDGSH iron sulfur domain 1	Homo sapiens	15-23
27243905-5	2016	Apoptosis of both, mitoNEET-KD and control cells was diminished to comparable levels by using the antioxidants Tiron and glutathione compound glutathione reduced ethyl ester (GSH-MEE), indicating that mitoNEET-dependent apoptosis is mediated by oxidative stress.	ethyl ester	162-173	CDGSH iron sulfur domain 1	Homo sapiens	19-27
27243905-10	2016	Inhibition of GSH-recycling, GSR-activity by 2-AAPA increased mitoNEET-protein, accompanied by reduced apoptosis.	Glutathione	14-17	CDGSH iron sulfur domain 1	Homo sapiens	62-70
27243905-5	2016	Apoptosis of both, mitoNEET-KD and control cells was diminished to comparable levels by using the antioxidants Tiron and glutathione compound glutathione reduced ethyl ester (GSH-MEE), indicating that mitoNEET-dependent apoptosis is mediated by oxidative stress.	S-ethyl glutathione	175-182	CDGSH iron sulfur domain 1	Homo sapiens	19-27
27243905-10	2016	Inhibition of GSH-recycling, GSR-activity by 2-AAPA increased mitoNEET-protein, accompanied by reduced apoptosis.	2-acetylamino-3-(4-(2-acetylamino-2-carboxyethylsulfanylthiocarbonylamino)phenylthiocarbamoylsulfanyl)propionic acid	45-51	CDGSH iron sulfur domain 1	Homo sapiens	62-70
27243905-11	2016	Addition of GSH reversed these effects suggesting that mitoNEET can in part compensate for imbalances in the antioxidative glutathione-system and therefore could serve as a potential therapeutic approach for the oxidatively stressed myocardium.	Glutathione	12-15	CDGSH iron sulfur domain 1	Homo sapiens	55-63
27243905-5	2016	Apoptosis of both, mitoNEET-KD and control cells was diminished to comparable levels by using the antioxidants Tiron and glutathione compound glutathione reduced ethyl ester (GSH-MEE), indicating that mitoNEET-dependent apoptosis is mediated by oxidative stress.	S-ethyl glutathione	175-182	CDGSH iron sulfur domain 1	Homo sapiens	201-209
27243905-11	2016	Addition of GSH reversed these effects suggesting that mitoNEET can in part compensate for imbalances in the antioxidative glutathione-system and therefore could serve as a potential therapeutic approach for the oxidatively stressed myocardium.	Glutathione	123-134	CDGSH iron sulfur domain 1	Homo sapiens	55-63
26887944-0	2016	Redox Control of the Human Iron-Sulfur Repair Protein MitoNEET Activity via Its Iron-Sulfur Cluster.	Iron	27-31	CDGSH iron sulfur domain 1	Homo sapiens	54-62
27071088-4	2016	Iron is present in CPSF30 as a 2Fe-2S cluster and uses one of the Cys3His domains; 2Fe-2S clusters with a Cys3His ligand set are rare and notably have also been identified in MitoNEET, a protein that was also annotated as a zinc finger.	Iron	0-4	CDGSH iron sulfur domain 1	Homo sapiens	175-183
26887944-0	2016	Redox Control of the Human Iron-Sulfur Repair Protein MitoNEET Activity via Its Iron-Sulfur Cluster.	Sulfur	32-38	CDGSH iron sulfur domain 1	Homo sapiens	54-62
26887944-0	2016	Redox Control of the Human Iron-Sulfur Repair Protein MitoNEET Activity via Its Iron-Sulfur Cluster.	Iron	80-84	CDGSH iron sulfur domain 1	Homo sapiens	54-62
26887944-0	2016	Redox Control of the Human Iron-Sulfur Repair Protein MitoNEET Activity via Its Iron-Sulfur Cluster.	Sulfur	85-91	CDGSH iron sulfur domain 1	Homo sapiens	54-62
25725808-0	2015	Novel thiazolidinedione mitoNEET ligand-1 acutely improves cardiac stem cell survival under oxidative stress.	2,4-thiazolidinedione	6-23	CDGSH iron sulfur domain 1	Homo sapiens	24-32
26692580-6	2016	In addition, VAT CISD1 gene expression was significantly associated with adipogenic and iron metabolism-related genes.	Iron	88-92	CDGSH iron sulfur domain 1	Homo sapiens	17-22
26905969-0	2016	Expression of Concern: Mitoneet mediates TNFalpha-induced necroptosis promoted by exposure to fructose and ethanol.	Fructose	94-102	CDGSH iron sulfur domain 1	Homo sapiens	23-31
26905969-0	2016	Expression of Concern: Mitoneet mediates TNFalpha-induced necroptosis promoted by exposure to fructose and ethanol.	Ethanol	107-114	CDGSH iron sulfur domain 1	Homo sapiens	23-31
26778000-0	2016	His-87 ligand in mitoNEET is crucial for the transfer of iron sulfur clusters from mitochondria to cytosolic aconitase.	Histidine	0-3	CDGSH iron sulfur domain 1	Homo sapiens	17-25
26778000-0	2016	His-87 ligand in mitoNEET is crucial for the transfer of iron sulfur clusters from mitochondria to cytosolic aconitase.	iron sulfur	57-68	CDGSH iron sulfur domain 1	Homo sapiens	17-25
26778000-1	2016	MitoNEET is the first identified iron sulfur protein that located in the mitochondrial outer membrane.	iron sulfur	33-44	CDGSH iron sulfur domain 1	Homo sapiens	0-8
26778000-4	2016	Our results confirm the observation that mitoNEET is important in transferring the iron sulfur clusters to the cytosolic aconitase in living cells and the His-87 ligand in mitoNEET plays important role in this process.	iron sulfur	83-94	CDGSH iron sulfur domain 1	Homo sapiens	41-49
26778000-4	2016	Our results confirm the observation that mitoNEET is important in transferring the iron sulfur clusters to the cytosolic aconitase in living cells and the His-87 ligand in mitoNEET plays important role in this process.	iron sulfur	83-94	CDGSH iron sulfur domain 1	Homo sapiens	172-180
26778000-4	2016	Our results confirm the observation that mitoNEET is important in transferring the iron sulfur clusters to the cytosolic aconitase in living cells and the His-87 ligand in mitoNEET plays important role in this process.	Histidine	155-158	CDGSH iron sulfur domain 1	Homo sapiens	41-49
26778000-4	2016	Our results confirm the observation that mitoNEET is important in transferring the iron sulfur clusters to the cytosolic aconitase in living cells and the His-87 ligand in mitoNEET plays important role in this process.	Histidine	155-158	CDGSH iron sulfur domain 1	Homo sapiens	172-180
25645953-1	2015	The human mitochondrial outer membrane protein mitoNEET is a newly discovered target of the type 2 diabetes drug pioglitazone.	Pioglitazone	113-125	CDGSH iron sulfur domain 1	Homo sapiens	47-55
25645953-8	2015	N-ethylmaleimide, a potent thiol modifier, completely inhibits human glutathione reductase from reducing the mitoNEET [2Fe-2S] clusters, indicating that the redox-active disulfide in the catalytic center of human glutathione reductase may be directly involved in reducing the mitoNEET [2Fe-2S] clusters.	Ethylmaleimide	0-16	CDGSH iron sulfur domain 1	Homo sapiens	109-117
25645953-8	2015	N-ethylmaleimide, a potent thiol modifier, completely inhibits human glutathione reductase from reducing the mitoNEET [2Fe-2S] clusters, indicating that the redox-active disulfide in the catalytic center of human glutathione reductase may be directly involved in reducing the mitoNEET [2Fe-2S] clusters.	Ethylmaleimide	0-16	CDGSH iron sulfur domain 1	Homo sapiens	276-284
25645953-8	2015	N-ethylmaleimide, a potent thiol modifier, completely inhibits human glutathione reductase from reducing the mitoNEET [2Fe-2S] clusters, indicating that the redox-active disulfide in the catalytic center of human glutathione reductase may be directly involved in reducing the mitoNEET [2Fe-2S] clusters.	Sulfhydryl Compounds	27-32	CDGSH iron sulfur domain 1	Homo sapiens	109-117
25645953-8	2015	N-ethylmaleimide, a potent thiol modifier, completely inhibits human glutathione reductase from reducing the mitoNEET [2Fe-2S] clusters, indicating that the redox-active disulfide in the catalytic center of human glutathione reductase may be directly involved in reducing the mitoNEET [2Fe-2S] clusters.	Disulfides	170-179	CDGSH iron sulfur domain 1	Homo sapiens	109-117
25645953-8	2015	N-ethylmaleimide, a potent thiol modifier, completely inhibits human glutathione reductase from reducing the mitoNEET [2Fe-2S] clusters, indicating that the redox-active disulfide in the catalytic center of human glutathione reductase may be directly involved in reducing the mitoNEET [2Fe-2S] clusters.	Disulfides	170-179	CDGSH iron sulfur domain 1	Homo sapiens	276-284
25725808-4	2015	MitoNEET is a redox-sensitive, mitochondrial target of thiazolidinediones (TZDs), and influences cellular oxidative capacity.	Thiazolidinediones	55-73	CDGSH iron sulfur domain 1	Homo sapiens	0-8
25725808-4	2015	MitoNEET is a redox-sensitive, mitochondrial target of thiazolidinediones (TZDs), and influences cellular oxidative capacity.	Thiazolidinediones	75-79	CDGSH iron sulfur domain 1	Homo sapiens	0-8
25725808-5	2015	Pharmacological targeting of mitoNEET with the novel TZD, mitoNEET Ligand-1 (NL-1), improved cardiac stem cell (CSC) survival compared to vehicle (0.1% DMSO) during in vitro oxidative stress (H2O2).	Dimethyl Sulfoxide	152-156	CDGSH iron sulfur domain 1	Homo sapiens	29-37
25725808-5	2015	Pharmacological targeting of mitoNEET with the novel TZD, mitoNEET Ligand-1 (NL-1), improved cardiac stem cell (CSC) survival compared to vehicle (0.1% DMSO) during in vitro oxidative stress (H2O2).	Dimethyl Sulfoxide	152-156	CDGSH iron sulfur domain 1	Homo sapiens	58-66
25725808-5	2015	Pharmacological targeting of mitoNEET with the novel TZD, mitoNEET Ligand-1 (NL-1), improved cardiac stem cell (CSC) survival compared to vehicle (0.1% DMSO) during in vitro oxidative stress (H2O2).	Hydrogen Peroxide	192-196	CDGSH iron sulfur domain 1	Homo sapiens	29-37
25725808-5	2015	Pharmacological targeting of mitoNEET with the novel TZD, mitoNEET Ligand-1 (NL-1), improved cardiac stem cell (CSC) survival compared to vehicle (0.1% DMSO) during in vitro oxidative stress (H2O2).	Hydrogen Peroxide	192-196	CDGSH iron sulfur domain 1	Homo sapiens	58-66
24814435-3	2014	Recently, the mitochondrial protein mitoNEET [also referred to as CDGSH iron sulfur domain 1 (CISD1)] has emerged as the mitochondrial target of thiazolidinedione drugs such as the antidiabetic pioglitazone.	2,4-thiazolidinedione	145-162	CDGSH iron sulfur domain 1	Homo sapiens	36-44
25762074-0	2015	The Fe-S cluster-containing NEET proteins mitoNEET and NAF-1 as chemotherapeutic targets in breast cancer.	Iron	4-8	CDGSH iron sulfur domain 1	Homo sapiens	42-50
25762074-2	2015	Here, we report that MAD-28, a designed cluvenone (CLV) derivative, binds to and destabilizes two members of a unique class of mitochondrial and endoplasmic reticulum (ER) 2Fe-2S proteins, mitoNEET (mNT) and nutrient-deprivation autophagy factor-1 (NAF-1), recently implicated in cancer cell proliferation.	cluvenone	40-49	CDGSH iron sulfur domain 1	Homo sapiens	189-197
25012650-3	2014	Here we show that Fe-S assembly of mitoNEET, the first identified Fe-S protein anchored in the mitochondrial outer membrane, strictly depends on ISC machineries and not on the CIA or CIAPIN1.	Iron	18-22	CDGSH iron sulfur domain 1	Homo sapiens	35-43
25012650-3	2014	Here we show that Fe-S assembly of mitoNEET, the first identified Fe-S protein anchored in the mitochondrial outer membrane, strictly depends on ISC machineries and not on the CIA or CIAPIN1.	Iron	18-20	CDGSH iron sulfur domain 1	Homo sapiens	35-43
25012650-3	2014	Here we show that Fe-S assembly of mitoNEET, the first identified Fe-S protein anchored in the mitochondrial outer membrane, strictly depends on ISC machineries and not on the CIA or CIAPIN1.	Sulfur	21-22	CDGSH iron sulfur domain 1	Homo sapiens	35-43
25012650-5	2014	When inserted, the Fe-S cluster confers mitoNEET folding and stability in vitro and in vivo.	Iron	19-23	CDGSH iron sulfur domain 1	Homo sapiens	40-48
25012650-6	2014	The holo-form of mitoNEET is resistant to NO and H2O2 and is capable of repairing oxidatively damaged Fe-S of iron regulatory protein 1 (IRP1), a master regulator of cellular iron that has recently been involved in the mitochondrial iron supply.	Hydrogen Peroxide	49-53	CDGSH iron sulfur domain 1	Homo sapiens	17-25
25012650-6	2014	The holo-form of mitoNEET is resistant to NO and H2O2 and is capable of repairing oxidatively damaged Fe-S of iron regulatory protein 1 (IRP1), a master regulator of cellular iron that has recently been involved in the mitochondrial iron supply.	Iron	102-106	CDGSH iron sulfur domain 1	Homo sapiens	17-25
25012650-6	2014	The holo-form of mitoNEET is resistant to NO and H2O2 and is capable of repairing oxidatively damaged Fe-S of iron regulatory protein 1 (IRP1), a master regulator of cellular iron that has recently been involved in the mitochondrial iron supply.	Iron	110-114	CDGSH iron sulfur domain 1	Homo sapiens	17-25
25012650-6	2014	The holo-form of mitoNEET is resistant to NO and H2O2 and is capable of repairing oxidatively damaged Fe-S of iron regulatory protein 1 (IRP1), a master regulator of cellular iron that has recently been involved in the mitochondrial iron supply.	Iron	175-179	CDGSH iron sulfur domain 1	Homo sapiens	17-25
25012650-7	2014	Therefore, our findings point to IRP1 as the missing link to explain the function of mitoNEET in the control of mitochondrial iron homeostasis.	Iron	126-130	CDGSH iron sulfur domain 1	Homo sapiens	85-93
24814435-3	2014	Recently, the mitochondrial protein mitoNEET [also referred to as CDGSH iron sulfur domain 1 (CISD1)] has emerged as the mitochondrial target of thiazolidinedione drugs such as the antidiabetic pioglitazone.	2,4-thiazolidinedione	145-162	CDGSH iron sulfur domain 1	Homo sapiens	66-92
24814435-3	2014	Recently, the mitochondrial protein mitoNEET [also referred to as CDGSH iron sulfur domain 1 (CISD1)] has emerged as the mitochondrial target of thiazolidinedione drugs such as the antidiabetic pioglitazone.	2,4-thiazolidinedione	145-162	CDGSH iron sulfur domain 1	Homo sapiens	94-99
24814435-3	2014	Recently, the mitochondrial protein mitoNEET [also referred to as CDGSH iron sulfur domain 1 (CISD1)] has emerged as the mitochondrial target of thiazolidinedione drugs such as the antidiabetic pioglitazone.	Pioglitazone	194-206	CDGSH iron sulfur domain 1	Homo sapiens	36-44
24814435-3	2014	Recently, the mitochondrial protein mitoNEET [also referred to as CDGSH iron sulfur domain 1 (CISD1)] has emerged as the mitochondrial target of thiazolidinedione drugs such as the antidiabetic pioglitazone.	Pioglitazone	194-206	CDGSH iron sulfur domain 1	Homo sapiens	66-92
24814435-3	2014	Recently, the mitochondrial protein mitoNEET [also referred to as CDGSH iron sulfur domain 1 (CISD1)] has emerged as the mitochondrial target of thiazolidinedione drugs such as the antidiabetic pioglitazone.	Pioglitazone	194-206	CDGSH iron sulfur domain 1	Homo sapiens	94-99
24403080-0	2014	Redox control of human mitochondrial outer membrane protein MitoNEET [2Fe-2S] clusters by biological thiols and hydrogen peroxide.	Sulfhydryl Compounds	101-107	CDGSH iron sulfur domain 1	Homo sapiens	60-68
24403080-0	2014	Redox control of human mitochondrial outer membrane protein MitoNEET [2Fe-2S] clusters by biological thiols and hydrogen peroxide.	Hydrogen Peroxide	112-129	CDGSH iron sulfur domain 1	Homo sapiens	60-68
24403080-1	2014	The human mitochondrial outer membrane protein mitoNEET is a novel target of the type II diabetes drug pioglitazone.	Pioglitazone	103-115	CDGSH iron sulfur domain 1	Homo sapiens	47-55
24403080-2	2014	The C-terminal cytosolic domain of mitoNEET hosts a redox-active [2Fe-2S] cluster via an unusual ligand arrangement of three cysteine residues and one histidine residue.	Cysteine	125-133	CDGSH iron sulfur domain 1	Homo sapiens	35-43
24403080-2	2014	The C-terminal cytosolic domain of mitoNEET hosts a redox-active [2Fe-2S] cluster via an unusual ligand arrangement of three cysteine residues and one histidine residue.	Histidine	151-160	CDGSH iron sulfur domain 1	Homo sapiens	35-43
24403080-4	2014	In vitro studies show that purified mitoNEET [2Fe-2S] clusters can be partially reduced by monothiols such as reduced glutathione, L-cysteine or N-acetyl-L-cysteine and fully reduced by dithiothreitol or the E. coli thioredoxin/thioredoxin reductase system under anaerobic conditions.	monothiols	91-101	CDGSH iron sulfur domain 1	Homo sapiens	36-44
24403080-4	2014	In vitro studies show that purified mitoNEET [2Fe-2S] clusters can be partially reduced by monothiols such as reduced glutathione, L-cysteine or N-acetyl-L-cysteine and fully reduced by dithiothreitol or the E. coli thioredoxin/thioredoxin reductase system under anaerobic conditions.	Glutathione	118-129	CDGSH iron sulfur domain 1	Homo sapiens	36-44
24403080-4	2014	In vitro studies show that purified mitoNEET [2Fe-2S] clusters can be partially reduced by monothiols such as reduced glutathione, L-cysteine or N-acetyl-L-cysteine and fully reduced by dithiothreitol or the E. coli thioredoxin/thioredoxin reductase system under anaerobic conditions.	Cysteine	131-141	CDGSH iron sulfur domain 1	Homo sapiens	36-44
24403080-4	2014	In vitro studies show that purified mitoNEET [2Fe-2S] clusters can be partially reduced by monothiols such as reduced glutathione, L-cysteine or N-acetyl-L-cysteine and fully reduced by dithiothreitol or the E. coli thioredoxin/thioredoxin reductase system under anaerobic conditions.	N-Acetyl-L-cysteine	147-164	CDGSH iron sulfur domain 1	Homo sapiens	36-44
24403080-4	2014	In vitro studies show that purified mitoNEET [2Fe-2S] clusters can be partially reduced by monothiols such as reduced glutathione, L-cysteine or N-acetyl-L-cysteine and fully reduced by dithiothreitol or the E. coli thioredoxin/thioredoxin reductase system under anaerobic conditions.	Dithiothreitol	186-200	CDGSH iron sulfur domain 1	Homo sapiens	36-44
24403080-5	2014	Importantly, thiol-reduced mitoNEET [2Fe-2S] clusters can be reversibly oxidized by hydrogen peroxide without disruption of the clusters in vitro and in E. coli cells, indicating that mitoNEET may act as a sensor of oxidative signals to regulate mitochondrial functions via its [2Fe-2S] clusters.	Sulfhydryl Compounds	13-18	CDGSH iron sulfur domain 1	Homo sapiens	27-35
24403080-5	2014	Importantly, thiol-reduced mitoNEET [2Fe-2S] clusters can be reversibly oxidized by hydrogen peroxide without disruption of the clusters in vitro and in E. coli cells, indicating that mitoNEET may act as a sensor of oxidative signals to regulate mitochondrial functions via its [2Fe-2S] clusters.	Sulfhydryl Compounds	13-18	CDGSH iron sulfur domain 1	Homo sapiens	184-192
24403080-5	2014	Importantly, thiol-reduced mitoNEET [2Fe-2S] clusters can be reversibly oxidized by hydrogen peroxide without disruption of the clusters in vitro and in E. coli cells, indicating that mitoNEET may act as a sensor of oxidative signals to regulate mitochondrial functions via its [2Fe-2S] clusters.	Hydrogen Peroxide	84-101	CDGSH iron sulfur domain 1	Homo sapiens	27-35
24403080-5	2014	Importantly, thiol-reduced mitoNEET [2Fe-2S] clusters can be reversibly oxidized by hydrogen peroxide without disruption of the clusters in vitro and in E. coli cells, indicating that mitoNEET may act as a sensor of oxidative signals to regulate mitochondrial functions via its [2Fe-2S] clusters.	Hydrogen Peroxide	84-101	CDGSH iron sulfur domain 1	Homo sapiens	184-192
24403080-6	2014	Furthermore, the binding of the type II diabetes drug pioglitazone in mitoNEET effectively inhibits the thiol-mediated reduction of [2Fe-2S] clusters, suggesting that pioglitazone may modulate the function of mitoNEET by blocking the thiol-mediated reduction of [2Fe-2S] clusters in the protein.	Pioglitazone	54-66	CDGSH iron sulfur domain 1	Homo sapiens	70-78
24403080-6	2014	Furthermore, the binding of the type II diabetes drug pioglitazone in mitoNEET effectively inhibits the thiol-mediated reduction of [2Fe-2S] clusters, suggesting that pioglitazone may modulate the function of mitoNEET by blocking the thiol-mediated reduction of [2Fe-2S] clusters in the protein.	Pioglitazone	54-66	CDGSH iron sulfur domain 1	Homo sapiens	209-217
24403080-6	2014	Furthermore, the binding of the type II diabetes drug pioglitazone in mitoNEET effectively inhibits the thiol-mediated reduction of [2Fe-2S] clusters, suggesting that pioglitazone may modulate the function of mitoNEET by blocking the thiol-mediated reduction of [2Fe-2S] clusters in the protein.	Sulfhydryl Compounds	104-109	CDGSH iron sulfur domain 1	Homo sapiens	70-78
24403080-6	2014	Furthermore, the binding of the type II diabetes drug pioglitazone in mitoNEET effectively inhibits the thiol-mediated reduction of [2Fe-2S] clusters, suggesting that pioglitazone may modulate the function of mitoNEET by blocking the thiol-mediated reduction of [2Fe-2S] clusters in the protein.	Sulfhydryl Compounds	104-109	CDGSH iron sulfur domain 1	Homo sapiens	209-217
24403080-6	2014	Furthermore, the binding of the type II diabetes drug pioglitazone in mitoNEET effectively inhibits the thiol-mediated reduction of [2Fe-2S] clusters, suggesting that pioglitazone may modulate the function of mitoNEET by blocking the thiol-mediated reduction of [2Fe-2S] clusters in the protein.	Pioglitazone	167-179	CDGSH iron sulfur domain 1	Homo sapiens	70-78
24403080-6	2014	Furthermore, the binding of the type II diabetes drug pioglitazone in mitoNEET effectively inhibits the thiol-mediated reduction of [2Fe-2S] clusters, suggesting that pioglitazone may modulate the function of mitoNEET by blocking the thiol-mediated reduction of [2Fe-2S] clusters in the protein.	Pioglitazone	167-179	CDGSH iron sulfur domain 1	Homo sapiens	209-217
24403080-6	2014	Furthermore, the binding of the type II diabetes drug pioglitazone in mitoNEET effectively inhibits the thiol-mediated reduction of [2Fe-2S] clusters, suggesting that pioglitazone may modulate the function of mitoNEET by blocking the thiol-mediated reduction of [2Fe-2S] clusters in the protein.	Sulfhydryl Compounds	234-239	CDGSH iron sulfur domain 1	Homo sapiens	70-78
24403080-6	2014	Furthermore, the binding of the type II diabetes drug pioglitazone in mitoNEET effectively inhibits the thiol-mediated reduction of [2Fe-2S] clusters, suggesting that pioglitazone may modulate the function of mitoNEET by blocking the thiol-mediated reduction of [2Fe-2S] clusters in the protein.	Sulfhydryl Compounds	234-239	CDGSH iron sulfur domain 1	Homo sapiens	209-217
24295216-0	2013	Identification of disulfide bond formation between MitoNEET and glutamate dehydrogenase 1.	Disulfides	18-27	CDGSH iron sulfur domain 1	Homo sapiens	51-59
24295216-4	2013	MitoNEET forms a covalent complex with GDH1 through disulfide bond formation and acts as an activator.	Disulfides	52-61	CDGSH iron sulfur domain 1	Homo sapiens	0-8
23758282-0	2013	Conserved hydrogen bonding networks of MitoNEET tune Fe-S cluster binding and structural stability.	Hydrogen	10-18	CDGSH iron sulfur domain 1	Homo sapiens	39-47
23627890-7	2013	In this review, a thorough evaluation of the role of PPAR and mitoNEET in rosiglitazone and pioglitazone mediated neuroprotection will be completed in order to shed light on the mechanism of a new possible therapeutic intervention for CNS injury.	Rosiglitazone	74-87	CDGSH iron sulfur domain 1	Homo sapiens	62-70
23758282-0	2013	Conserved hydrogen bonding networks of MitoNEET tune Fe-S cluster binding and structural stability.	Iron	53-57	CDGSH iron sulfur domain 1	Homo sapiens	39-47
23758282-1	2013	While its biological function remains unclear, the three-cysteine, one-histidine ligated human [2Fe-2S] cluster containing protein mitoNEET is of interest because of its interaction with the anti-diabetes drug pioglitazone.	three-cysteine	51-65	CDGSH iron sulfur domain 1	Homo sapiens	131-139
23758282-1	2013	While its biological function remains unclear, the three-cysteine, one-histidine ligated human [2Fe-2S] cluster containing protein mitoNEET is of interest because of its interaction with the anti-diabetes drug pioglitazone.	Histidine	71-80	CDGSH iron sulfur domain 1	Homo sapiens	131-139
23758282-1	2013	While its biological function remains unclear, the three-cysteine, one-histidine ligated human [2Fe-2S] cluster containing protein mitoNEET is of interest because of its interaction with the anti-diabetes drug pioglitazone.	Pioglitazone	210-222	CDGSH iron sulfur domain 1	Homo sapiens	131-139
23758282-2	2013	The mitoNEET [2Fe-2S] cluster demonstrates proton-coupled electron transfer (PCET) and marked cluster instability, which have both been linked to the single His ligand.	Histidine	157-160	CDGSH iron sulfur domain 1	Homo sapiens	4-12
21782425-0	2011	A novel binding assay identifies high affinity ligands to the rosiglitazone binding site of mitoNEET.	Rosiglitazone	62-75	CDGSH iron sulfur domain 1	Homo sapiens	92-100
22945239-1	2012	Human mitochondrial protein mitoNEET is a novel target of type II diabetes drug pioglitazone, and contains a redox active [2Fe-2S] cluster that is hosted by a unique ligand arrangement of three cysteine and one histidine residues.	Pioglitazone	80-92	CDGSH iron sulfur domain 1	Homo sapiens	28-36
22945239-1	2012	Human mitochondrial protein mitoNEET is a novel target of type II diabetes drug pioglitazone, and contains a redox active [2Fe-2S] cluster that is hosted by a unique ligand arrangement of three cysteine and one histidine residues.	Cysteine	194-202	CDGSH iron sulfur domain 1	Homo sapiens	28-36
22945239-1	2012	Human mitochondrial protein mitoNEET is a novel target of type II diabetes drug pioglitazone, and contains a redox active [2Fe-2S] cluster that is hosted by a unique ligand arrangement of three cysteine and one histidine residues.	Histidine	211-220	CDGSH iron sulfur domain 1	Homo sapiens	28-36
22945239-4	2012	Addition of exogenous iron or zinc ion in the media produces mitoNEET bound with a [2Fe-2S] cluster or zinc, respectively.	Iron	22-26	CDGSH iron sulfur domain 1	Homo sapiens	61-69
23410161-5	2013	In an entirely different approach, compounds containing the thiazolidinedione moiety (referred to as glitazones) alter mitochondrial function through the mitochondrial protein mitoNEET, an attractive new drug target for the treatment of neurodegenerative diseases.	2,4-thiazolidinedione	60-77	CDGSH iron sulfur domain 1	Homo sapiens	176-184
23410161-5	2013	In an entirely different approach, compounds containing the thiazolidinedione moiety (referred to as glitazones) alter mitochondrial function through the mitochondrial protein mitoNEET, an attractive new drug target for the treatment of neurodegenerative diseases.	Thiazolidinediones	101-111	CDGSH iron sulfur domain 1	Homo sapiens	176-184
22351774-0	2012	NADPH inhibits [2Fe-2S] cluster protein transfer from diabetes drug target MitoNEET to an apo-acceptor protein.	NADP	0-5	CDGSH iron sulfur domain 1	Homo sapiens	75-83
22308404-0	2012	Strand swapping regulates the iron-sulfur cluster in the diabetes drug target mitoNEET.	Iron	30-34	CDGSH iron sulfur domain 1	Homo sapiens	78-86
22308404-0	2012	Strand swapping regulates the iron-sulfur cluster in the diabetes drug target mitoNEET.	Sulfur	35-41	CDGSH iron sulfur domain 1	Homo sapiens	78-86
21782425-1	2011	A novel outer mitochondrial membrane protein containing [2Fe-2S] clusters, mitoNEET was first identified through its binding to the anti-diabetic drug pioglitazone.	Pioglitazone	151-163	CDGSH iron sulfur domain 1	Homo sapiens	75-83
21782425-3	2011	With the lack of pharmacological tools available to fully elucidate mitoNEET"s function, we developed a binding assay to probe the glitazone binding site with the aim of developing selective and high affinity compounds.	Thiazolidinediones	131-140	CDGSH iron sulfur domain 1	Homo sapiens	68-76
21788481-1	2011	MitoNEET (mNT) is an outer mitochondrial membrane target of the thiazolidinedione diabetes drugs with a unique fold and a labile [2Fe-2S] cluster.	2,4-thiazolidinedione	64-81	CDGSH iron sulfur domain 1	Homo sapiens	0-8
21402934-1	2011	MitoNEET is a recently identified drug target for a commonly prescribed diabetes drug, Pioglitazone.	Pioglitazone	87-99	CDGSH iron sulfur domain 1	Homo sapiens	0-8
21591687-0	2011	Complexes of the outer mitochondrial membrane protein mitoNEET with resveratrol-3-sulfate.	Resveratrol	68-89	CDGSH iron sulfur domain 1	Homo sapiens	54-62
21591687-1	2011	Binding of the thiazolidinedione antidiabetic drug pioglitazone led to the discovery of a novel outer mitochondrial membrane protein of unknown function called mitoNEET.	2,4-thiazolidinedione	15-32	CDGSH iron sulfur domain 1	Homo sapiens	160-168
21591687-1	2011	Binding of the thiazolidinedione antidiabetic drug pioglitazone led to the discovery of a novel outer mitochondrial membrane protein of unknown function called mitoNEET.	Pioglitazone	51-63	CDGSH iron sulfur domain 1	Homo sapiens	160-168
21591687-6	2011	mitoNEET formed complexes with resveratrol-3-sulfate, one of the primary metabolites of the natural product resveratrol.	Resveratrol	31-52	CDGSH iron sulfur domain 1	Homo sapiens	0-8
21591687-6	2011	mitoNEET formed complexes with resveratrol-3-sulfate, one of the primary metabolites of the natural product resveratrol.	Resveratrol	31-42	CDGSH iron sulfur domain 1	Homo sapiens	0-8
21591687-11	2011	The only other known naturally occurring binding partner for mitoNEET at present is NADPH.	NADP	84-89	CDGSH iron sulfur domain 1	Homo sapiens	61-69
20932062-0	2010	Binding of reduced nicotinamide adenine dinucleotide phosphate destabilizes the iron-sulfur clusters of human mitoNEET.	NADP	19-62	CDGSH iron sulfur domain 1	Homo sapiens	110-118
20932062-0	2010	Binding of reduced nicotinamide adenine dinucleotide phosphate destabilizes the iron-sulfur clusters of human mitoNEET.	Iron	80-84	CDGSH iron sulfur domain 1	Homo sapiens	110-118
20932062-0	2010	Binding of reduced nicotinamide adenine dinucleotide phosphate destabilizes the iron-sulfur clusters of human mitoNEET.	Sulfur	85-91	CDGSH iron sulfur domain 1	Homo sapiens	110-118
20812736-2	2010	MitoNEET is homodimeric with each protomer binding a [2Fe-2S] center through a rare 3-Cys and 1-His coordination geometry.	3-cys	84-89	CDGSH iron sulfur domain 1	Homo sapiens	0-8
20932062-1	2010	The outer mitochondrial membrane protein mitoNEET is a cellular target of the antidiabetic drug pioglitazone.	Pioglitazone	96-108	CDGSH iron sulfur domain 1	Homo sapiens	41-49
20932062-3	2010	Here, we report that reduced nicotinamide adenine dinucleotide phosphate (NADPH) can bind to homodimeric mitoNEET, influencing the stability of the [2Fe-2S] cluster that is bound within a loop region (Y71-H87) in each subunit.	NADP	29-72	CDGSH iron sulfur domain 1	Homo sapiens	105-113
20932062-3	2010	Here, we report that reduced nicotinamide adenine dinucleotide phosphate (NADPH) can bind to homodimeric mitoNEET, influencing the stability of the [2Fe-2S] cluster that is bound within a loop region (Y71-H87) in each subunit.	NADP	74-79	CDGSH iron sulfur domain 1	Homo sapiens	105-113
20932062-4	2010	Nuclear magnetic resonance (NMR) and isothermal titration calorimetry experiments demonstrated that NADPH binds weakly to mitoNEET(44-108), a soluble domain of mitoNEET containing residues 44-108.	NADP	100-105	CDGSH iron sulfur domain 1	Homo sapiens	122-130
20932062-4	2010	Nuclear magnetic resonance (NMR) and isothermal titration calorimetry experiments demonstrated that NADPH binds weakly to mitoNEET(44-108), a soluble domain of mitoNEET containing residues 44-108.	NADP	100-105	CDGSH iron sulfur domain 1	Homo sapiens	160-168
20932062-6	2010	Disruption of the three-dimensional structure of mitoNEET(44-108) as a result of decomposition of the iron-sulfur clusters was observed by NMR and circular dichroism experiments.	Iron	102-106	CDGSH iron sulfur domain 1	Homo sapiens	49-57
20932062-6	2010	Disruption of the three-dimensional structure of mitoNEET(44-108) as a result of decomposition of the iron-sulfur clusters was observed by NMR and circular dichroism experiments.	Sulfur	107-113	CDGSH iron sulfur domain 1	Homo sapiens	49-57
20932062-8	2010	Residues K55 and H58 of each subunit of mitoNEET were shown to be involved in NADPH binding.	NADP	78-83	CDGSH iron sulfur domain 1	Homo sapiens	40-48
20812736-2	2010	MitoNEET is homodimeric with each protomer binding a [2Fe-2S] center through a rare 3-Cys and 1-His coordination geometry.	1-his	94-99	CDGSH iron sulfur domain 1	Homo sapiens	0-8
20812736-6	2010	These properties make mitoNEET potentially useful for both physiological studies and industrial applications as a stable, water-soluble, redox agent.	Water	122-127	CDGSH iron sulfur domain 1	Homo sapiens	22-30
19791753-1	2009	MitoNEET is a small mitochondrial protein that has been identified recently as a target for the thiazolidinedione (TZD) class of diabetes drugs.	2,4-thiazolidinedione	96-113	CDGSH iron sulfur domain 1	Homo sapiens	0-8
20099820-0	2010	Binding of histidine in the (Cys)3(His)1-coordinated [2Fe-2S] cluster of human mitoNEET.	Histidine	11-20	CDGSH iron sulfur domain 1	Homo sapiens	79-87
20099820-1	2010	Human mitoNEET is a homodimeric iron-sulfur protein located in the outer mitochondrial membrane with unknown function, but which is known to interact with thiazolidinedione diabetes drugs.	2,4-thiazolidinedione	155-172	CDGSH iron sulfur domain 1	Homo sapiens	6-14
20099820-6	2010	Simulation and least-squares fitting of orientation-selective Ka- and Q-band ENDOR, 1D ESEEM, and HYSCORE spectra of (14)N and (15)N-labeled mitoNEET yield the principal values and orientations of both the hyperfine tensor ((14)N, A(iso) = -6.25 MHz, T = -0.94 MHz) and the quadrupolar tensor (e(2)Qq/h = -2.47 MHz, eta = 0.38) of the ligating histidine nitrogen N(delta).	Histidine	344-353	CDGSH iron sulfur domain 1	Homo sapiens	141-149
20099820-6	2010	Simulation and least-squares fitting of orientation-selective Ka- and Q-band ENDOR, 1D ESEEM, and HYSCORE spectra of (14)N and (15)N-labeled mitoNEET yield the principal values and orientations of both the hyperfine tensor ((14)N, A(iso) = -6.25 MHz, T = -0.94 MHz) and the quadrupolar tensor (e(2)Qq/h = -2.47 MHz, eta = 0.38) of the ligating histidine nitrogen N(delta).	Nitrogen	354-362	CDGSH iron sulfur domain 1	Homo sapiens	141-149
20064719-0	2010	Structure-based design of a thiazolidinedione which targets the mitochondrial protein mitoNEET.	2,4-thiazolidinedione	28-45	CDGSH iron sulfur domain 1	Homo sapiens	86-94
20064719-2	2010	Recently, a search for mitochondrial proteins that bind pioglitazone identified a novel protein, mitoNEET, which was later shown to regulate the oxidative capacity of the mitochondria.	Pioglitazone	56-68	CDGSH iron sulfur domain 1	Homo sapiens	97-105
19791753-1	2009	MitoNEET is a small mitochondrial protein that has been identified recently as a target for the thiazolidinedione (TZD) class of diabetes drugs.	2,4-thiazolidinedione	115-118	CDGSH iron sulfur domain 1	Homo sapiens	0-8
19791753-2	2009	MitoNEET also binds a unique three-Cys- and one-His-ligated [corrected] [2Fe-2S] cluster.	Cysteine	35-38	CDGSH iron sulfur domain 1	Homo sapiens	0-8
19791753-2	2009	MitoNEET also binds a unique three-Cys- and one-His-ligated [corrected] [2Fe-2S] cluster.	Histidine	48-51	CDGSH iron sulfur domain 1	Homo sapiens	0-8
19791753-5	2009	In contrast, a His87Cys mutant negates the ability of TZDs to affect the midpoint potential, suggesting a model of drug binding in which His87 is critical to communication with the FeS center of mitoNEET.	tzds	54-58	CDGSH iron sulfur domain 1	Homo sapiens	195-203
19791753-5	2009	In contrast, a His87Cys mutant negates the ability of TZDs to affect the midpoint potential, suggesting a model of drug binding in which His87 is critical to communication with the FeS center of mitoNEET.	Iron	181-184	CDGSH iron sulfur domain 1	Homo sapiens	195-203
19574633-3	2009	MitoNEET, a 2Fe-2S outer mitochondrial membrane protein, binds pioglitazone [Colca et al.	Pioglitazone	63-75	CDGSH iron sulfur domain 1	Homo sapiens	0-8
19736979-1	2009	CW EPR spectra of reduced [2Fe-2S](Cys)(3)(His)(1) clusters of mammalian mitoNEET soluble domain appear to produce features resulting from the interaction of the electron spins of the two adjacent clusters, which can be explained by employing the local spin model.	Histidine	43-46	CDGSH iron sulfur domain 1	Homo sapiens	73-81
19736979-2	2009	This model favors the reduction of the outermost iron with His87 and Cys83 ligands, which is supported by orientation-selected hyperfine sublevel correlation (HYSCORE) characterization of the uniformly (15)N-labeled mitoNEET showing one strongly coupled nitrogen from the His87 N(delta) ligand with hyperfine coupling (15)a = 8 MHz.	Iron	49-53	CDGSH iron sulfur domain 1	Homo sapiens	216-224
19736979-2	2009	This model favors the reduction of the outermost iron with His87 and Cys83 ligands, which is supported by orientation-selected hyperfine sublevel correlation (HYSCORE) characterization of the uniformly (15)N-labeled mitoNEET showing one strongly coupled nitrogen from the His87 N(delta) ligand with hyperfine coupling (15)a = 8 MHz.	Nitrogen	254-262	CDGSH iron sulfur domain 1	Homo sapiens	216-224
19736979-1	2009	CW EPR spectra of reduced [2Fe-2S](Cys)(3)(His)(1) clusters of mammalian mitoNEET soluble domain appear to produce features resulting from the interaction of the electron spins of the two adjacent clusters, which can be explained by employing the local spin model.	Cysteine	35-38	CDGSH iron sulfur domain 1	Homo sapiens	73-81
19388667-0	2009	Resonance Raman studies of the (His)(Cys)3 2Fe-2S cluster of MitoNEET: comparison to the (Cys)4 mutant and implications of the effects of pH on the labile metal center.	Cysteine	37-40	CDGSH iron sulfur domain 1	Homo sapiens	61-69
19388667-2	2009	It exhibits a novel protein fold, and in contrast to other 2Fe-2S proteins such as Rieske proteins and ferredoxins, the metal clusters in the mitoNEET homodimer are each coordinated by one histidine residue and three cysteine residues.	Metals	120-125	CDGSH iron sulfur domain 1	Homo sapiens	142-150
19388667-2	2009	It exhibits a novel protein fold, and in contrast to other 2Fe-2S proteins such as Rieske proteins and ferredoxins, the metal clusters in the mitoNEET homodimer are each coordinated by one histidine residue and three cysteine residues.	Histidine	189-198	CDGSH iron sulfur domain 1	Homo sapiens	142-150
19388667-2	2009	It exhibits a novel protein fold, and in contrast to other 2Fe-2S proteins such as Rieske proteins and ferredoxins, the metal clusters in the mitoNEET homodimer are each coordinated by one histidine residue and three cysteine residues.	Cysteine	217-225	CDGSH iron sulfur domain 1	Homo sapiens	142-150
19388667-5	2009	Comparison of mitoNEET to its ferredoxin-like H87C mutant indicates that Raman peaks in the approximately 250-300 cm(-1) region of mitoNEET are influenced by the Fe-His87 moiety.	Iron	162-164	CDGSH iron sulfur domain 1	Homo sapiens	14-22
19388667-5	2009	Comparison of mitoNEET to its ferredoxin-like H87C mutant indicates that Raman peaks in the approximately 250-300 cm(-1) region of mitoNEET are influenced by the Fe-His87 moiety.	Iron	162-164	CDGSH iron sulfur domain 1	Homo sapiens	131-139
19388667-7	2009	The approximately 250-300 cm(-1) region of native mitoNEET is also sensitive to phosphate buffer.	Phosphates	80-89	CDGSH iron sulfur domain 1	Homo sapiens	50-58
19388667-9	2009	These results support the hypothesis that the Fe-N(His87) interaction is modulated within the physiological pH range, and this modulation may be critical to the function of mitoNEET.	Iron	46-50	CDGSH iron sulfur domain 1	Homo sapiens	173-181
18047834-4	2008	Inhibition of CFTR chloride transport activity by using glibenclamide (50muM, 24h) or CFTR(inh)-172 (5muM, 24h), resulted in the down-regulation of CISD1 mRNA, and CFTR stimulation with cAMP/isoproterenol/IBMX upregulated its expression.	Glyburide	56-69	CDGSH iron sulfur domain 1	Homo sapiens	148-153
17905743-1	2007	MitoNEET was identified as an outer mitochondrial membrane protein that can potentially bind the anti-diabetes drug pioglitazone.	Pioglitazone	116-128	CDGSH iron sulfur domain 1	Homo sapiens	0-8
17766439-0	2007	Crystal structure of human mitoNEET reveals distinct groups of iron sulfur proteins.	Iron	63-67	CDGSH iron sulfur domain 1	Homo sapiens	27-35
17766439-1	2007	MitoNEET is a protein of unknown function present in the mitochondrial membrane that was recently shown to bind specifically the antidiabetic drug pioglizatone.	pioglizatone	147-159	CDGSH iron sulfur domain 1	Homo sapiens	0-8
17766439-9	2007	Our study suggests an electron transfer function for mitoNEET and for other proteins containing the CCCH motif.	ccch	100-104	CDGSH iron sulfur domain 1	Homo sapiens	53-61
17766440-0	2007	MitoNEET is a uniquely folded 2Fe 2S outer mitochondrial membrane protein stabilized by pioglitazone.	Pioglitazone	88-100	CDGSH iron sulfur domain 1	Homo sapiens	0-8
17766440-7	2007	The biophysical properties of mitoNEET suggest that it may participate in a redox-sensitive signaling and/or in Fe-S cluster transfer.	Iron	112-116	CDGSH iron sulfur domain 1	Homo sapiens	30-38
17584744-1	2007	The outer mitochondrial membrane protein mitoNEET was discovered as a binding target of pioglitazone, an insulin-sensitizing drug of the thiazolidinedione class used to treat type 2 diabetes (Colca, J. R., McDonald, W. G., Waldon, D. J., Leone, J. W., Lull, J. M., Bannow, C. A., Lund, E. T., and Mathews, W. R. (2004) Am.	Pioglitazone	88-100	CDGSH iron sulfur domain 1	Homo sapiens	41-49
17584744-1	2007	The outer mitochondrial membrane protein mitoNEET was discovered as a binding target of pioglitazone, an insulin-sensitizing drug of the thiazolidinedione class used to treat type 2 diabetes (Colca, J. R., McDonald, W. G., Waldon, D. J., Leone, J. W., Lull, J. M., Bannow, C. A., Lund, E. T., and Mathews, W. R. (2004) Am.	2,4-thiazolidinedione	137-154	CDGSH iron sulfur domain 1	Homo sapiens	41-49
17584744-5	2007	Although the CDGSH domain is annotated as a zinc finger motif, mitoNEET was shown to contain iron (Wiley, S. E., Murphy, A. N., Ross, S. A., van der Geer, P., and Dixon, J. E. (2007) Proc.	Iron	93-97	CDGSH iron sulfur domain 1	Homo sapiens	63-71
17584744-16	2007	Based on the biophysical data and domain fusion analysis, mitoNEET may function in Fe-S cluster shuttling and/or in redox reactions.	Iron	83-87	CDGSH iron sulfur domain 1	Homo sapiens	58-66
24489530-1	2006	The mitochondrial membrane protein termed "mitoNEET," is a putative secondary target for insulin-sensitizing thiazolidinedione (TZD) compounds but its role in regulating metabolic flux is not known.	2,4-thiazolidinedione	109-126	CDGSH iron sulfur domain 1	Homo sapiens	43-51
24489530-1	2006	The mitochondrial membrane protein termed "mitoNEET," is a putative secondary target for insulin-sensitizing thiazolidinedione (TZD) compounds but its role in regulating metabolic flux is not known.	2,4-thiazolidinedione	128-131	CDGSH iron sulfur domain 1	Homo sapiens	43-51
24489530-2	2006	PNU-91325 is a thiazolidinedione derivative which exhibits high binding affinity to mitoNEET and lowers cholesterol, fatty acid and blood glucose levels in animal models.	N-neopentyl-N-nitrosourea	0-3	CDGSH iron sulfur domain 1	Homo sapiens	84-92
24489530-2	2006	PNU-91325 is a thiazolidinedione derivative which exhibits high binding affinity to mitoNEET and lowers cholesterol, fatty acid and blood glucose levels in animal models.	2,4-thiazolidinedione	15-32	CDGSH iron sulfur domain 1	Homo sapiens	84-92
24489530-2	2006	PNU-91325 is a thiazolidinedione derivative which exhibits high binding affinity to mitoNEET and lowers cholesterol, fatty acid and blood glucose levels in animal models.	Cholesterol	104-115	CDGSH iron sulfur domain 1	Homo sapiens	84-92
19052371-1	2008	MitoNEET (a mammalian mitochondrial outer membrane protein) is a potential pharmacological and clinical target of the insulin-sensitizer pioglitazone.	Pioglitazone	137-149	CDGSH iron sulfur domain 1	Homo sapiens	0-8
19052371-1	2008	MitoNEET (a mammalian mitochondrial outer membrane protein) is a potential pharmacological and clinical target of the insulin-sensitizer pioglitazone.	Pioglitazone	137-149	CDGSH iron sulfur domain 1	Homo sapiens	22-58
19052371-2	2008	The thermophilic homologue of mitoNEET (TTHA0026) from Thermus thermophilus HB8 has been heterologously overproduced in Escherichia coli and purified as a water-soluble prototypal protein containing the mitoNEET-like [2Fe-2S] cluster.	Water	155-160	CDGSH iron sulfur domain 1	Homo sapiens	30-38
19052371-2	2008	The thermophilic homologue of mitoNEET (TTHA0026) from Thermus thermophilus HB8 has been heterologously overproduced in Escherichia coli and purified as a water-soluble prototypal protein containing the mitoNEET-like [2Fe-2S] cluster.	Water	155-160	CDGSH iron sulfur domain 1	Homo sapiens	203-211
18047834-4	2008	Inhibition of CFTR chloride transport activity by using glibenclamide (50muM, 24h) or CFTR(inh)-172 (5muM, 24h), resulted in the down-regulation of CISD1 mRNA, and CFTR stimulation with cAMP/isoproterenol/IBMX upregulated its expression.	Chlorides	19-27	CDGSH iron sulfur domain 1	Homo sapiens	148-153
24489530-9	2006	We conclude that the entry of acetyl Co-A derived from long-chain fatty acid beta-oxidation into the mitochondria is facilitated by the mitoNEET ligand PNU-91325, which increases glucose-derived long chain fatty acid synthesis and breakdown via beta-oxidation and anaplerosis in the mitochondria.	Acetyl Coenzyme A	30-41	CDGSH iron sulfur domain 1	Homo sapiens	136-144
24489530-9	2006	We conclude that the entry of acetyl Co-A derived from long-chain fatty acid beta-oxidation into the mitochondria is facilitated by the mitoNEET ligand PNU-91325, which increases glucose-derived long chain fatty acid synthesis and breakdown via beta-oxidation and anaplerosis in the mitochondria.	long-chain fatty acid	55-76	CDGSH iron sulfur domain 1	Homo sapiens	136-144
24489530-9	2006	We conclude that the entry of acetyl Co-A derived from long-chain fatty acid beta-oxidation into the mitochondria is facilitated by the mitoNEET ligand PNU-91325, which increases glucose-derived long chain fatty acid synthesis and breakdown via beta-oxidation and anaplerosis in the mitochondria.	N-neopentyl-N-nitrosourea	152-155	CDGSH iron sulfur domain 1	Homo sapiens	136-144
24489530-9	2006	We conclude that the entry of acetyl Co-A derived from long-chain fatty acid beta-oxidation into the mitochondria is facilitated by the mitoNEET ligand PNU-91325, which increases glucose-derived long chain fatty acid synthesis and breakdown via beta-oxidation and anaplerosis in the mitochondria.	glucose-derived long chain fatty acid	179-216	CDGSH iron sulfur domain 1	Homo sapiens	136-144