PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
33921425-7	2021	The key component of this pathway is Mia40 (called CHCHD4 in human cells), which itself contains cysteine motifs and is subject to redox regulation.	Cysteine	97-105	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	37-42
33921425-7	2021	The key component of this pathway is Mia40 (called CHCHD4 in human cells), which itself contains cysteine motifs and is subject to redox regulation.	Cysteine	97-105	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	51-57
33835027-2	2021	Here, we demonstrate that loss of ALR, a principal component of the MIA40/ALR protein import pathway, results in impaired cytosolic Fe/S cluster biogenesis in mammalian cells.	Iron	132-134	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	68-73
33835027-2	2021	Here, we demonstrate that loss of ALR, a principal component of the MIA40/ALR protein import pathway, results in impaired cytosolic Fe/S cluster biogenesis in mammalian cells.	Sulfur	135-136	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	68-73
33599699-6	2021	Here, we summarise the recent advances made to our understanding of the role of CHCHD4 and the DRS in physiology and disease, with a specific focus on the emerging importance of CHCHD4 in regulating the cellular response to low oxygen (hypoxia) and metabolism in cancer.	Oxygen	228-234	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	178-184
32762682-3	2020	The mitochondrial oxidoreductase MIA40, which catalyzes disulfide formation in the IMS, is imported by the combined action of the protein AIFM1 and MIA40 itself.	Disulfides	56-65	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	33-38
32779864-3	2020	Here, we show that the CHCHD4/GFER disulfide relay system in the mitochondrial intermembrane space (IMS) is required for PINK1 stabilization when mitochondrial membrane potential is lost.	Disulfides	35-44	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	23-29
32971361-0	2020	Glutathionylated and Fe-S cluster containing hMIA40 (CHCHD4) regulates ROS and mitochondrial complex III and IV activities of the electron transport chain.	Iron	21-25	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	45-51
32971361-0	2020	Glutathionylated and Fe-S cluster containing hMIA40 (CHCHD4) regulates ROS and mitochondrial complex III and IV activities of the electron transport chain.	Iron	21-25	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	53-59
32971361-0	2020	Glutathionylated and Fe-S cluster containing hMIA40 (CHCHD4) regulates ROS and mitochondrial complex III and IV activities of the electron transport chain.	Reactive Oxygen Species	71-74	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	45-51
32971361-0	2020	Glutathionylated and Fe-S cluster containing hMIA40 (CHCHD4) regulates ROS and mitochondrial complex III and IV activities of the electron transport chain.	Reactive Oxygen Species	71-74	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	53-59
32971361-2	2020	Site-directed mutagenesis complemented by MALDI on in vivo hMIA40 protein shows that a portion of MIA40 undergoes reversible S-glutathionylation at three cysteines in the twin CX9C motifs and the lone cysteine 4 residue.	Cysteine	154-163	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	59-65
32971361-2	2020	Site-directed mutagenesis complemented by MALDI on in vivo hMIA40 protein shows that a portion of MIA40 undergoes reversible S-glutathionylation at three cysteines in the twin CX9C motifs and the lone cysteine 4 residue.	Cysteine	154-163	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	60-65
32971361-2	2020	Site-directed mutagenesis complemented by MALDI on in vivo hMIA40 protein shows that a portion of MIA40 undergoes reversible S-glutathionylation at three cysteines in the twin CX9C motifs and the lone cysteine 4 residue.	Cysteine	154-162	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	59-65
32971361-2	2020	Site-directed mutagenesis complemented by MALDI on in vivo hMIA40 protein shows that a portion of MIA40 undergoes reversible S-glutathionylation at three cysteines in the twin CX9C motifs and the lone cysteine 4 residue.	Cysteine	154-162	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	60-65
32971361-3	2020	We find that HEK293T cells expressing hMIA40 mutant defective for glutathionylation are compromised in the activities of complexes III and IV of the Electron Transport Chain (ETC) and enhance Reactive Oxygen Species (ROS) levels.	Reactive Oxygen Species	192-215	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	38-44
32971361-3	2020	We find that HEK293T cells expressing hMIA40 mutant defective for glutathionylation are compromised in the activities of complexes III and IV of the Electron Transport Chain (ETC) and enhance Reactive Oxygen Species (ROS) levels.	Reactive Oxygen Species	217-220	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	38-44
32971361-7	2020	These results suggest that hMIA40 undergoes glutathionylation to maintain ROS levels and for optimum function of complexes III and IV of ETC.	Reactive Oxygen Species	74-77	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	27-33
32762682-3	2020	The mitochondrial oxidoreductase MIA40, which catalyzes disulfide formation in the IMS, is imported by the combined action of the protein AIFM1 and MIA40 itself.	Disulfides	56-65	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	148-153
32762682-9	2020	CONCLUSIONS: Our data suggest that the MIA40 precursor contains the stabilizing information to allow for postranslational import of sufficient amounts of MIA40 for full functionality of the essential disulfide relay.	essential disulfide	190-209	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	39-44
32762682-9	2020	CONCLUSIONS: Our data suggest that the MIA40 precursor contains the stabilizing information to allow for postranslational import of sufficient amounts of MIA40 for full functionality of the essential disulfide relay.	essential disulfide	190-209	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	154-159
31578585-10	2019	Overexpression of APE1 and Mia40 enhanced the cisplatin resistance and autophagy of the A549 cells.	Cisplatin	46-55	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	27-32
32105825-4	2020	The redox-regulated CHCHD4/Mia40-dependent import machinery operates in the intermembrane space of the mitochondrion and controls the import of a set of nuclear-encoded cysteine-motif carrying protein substrates.	Cysteine	169-177	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	20-26
32142475-4	2020	After this reaction, MIA40 is reoxidized by the sulfhydryl oxidase ALR, which couples disulfide formation by this machinery to the activity of the respiratory chain.	Disulfides	86-95	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	21-26
30650365-5	2019	We demonstrate that unfolded reduced proteins, upon translocation into the IMS, initiate formation of a metastable disulfide-linked complex with CHCHD4.	Disulfides	115-124	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	145-151
31346464-2	2019	The essential mitochondrial import protein coiled-coil helix coiled-coil helix domain-containing protein 4 (CHCHD4) controls respiratory chain complex activity and oxygen consumption, and regulates the growth of tumours in vivo.	Oxygen	164-170	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	43-106
31346464-2	2019	The essential mitochondrial import protein coiled-coil helix coiled-coil helix domain-containing protein 4 (CHCHD4) controls respiratory chain complex activity and oxygen consumption, and regulates the growth of tumours in vivo.	Oxygen	164-170	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	108-114
30886710-8	2019	We found that loss of CHCHD4 protects tumour cells from respiratory chain inhibition at CI, while elevated CHCHD4 expression in tumour cells leads to significantly increased sensitivity to CI inhibition, in part through the production of mitochondrial reactive oxygen species (ROS).	Reactive Oxygen Species	252-275	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	107-113
30886710-8	2019	We found that loss of CHCHD4 protects tumour cells from respiratory chain inhibition at CI, while elevated CHCHD4 expression in tumour cells leads to significantly increased sensitivity to CI inhibition, in part through the production of mitochondrial reactive oxygen species (ROS).	Reactive Oxygen Species	277-280	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	107-113
30338240-11	2018	Expression of CHCHD4, a key component of the disulphide relay system (DRS) involved in mitochondrial protein import within the intermembrane space (IMS) was elevated by pVHL re-expression alongside enhanced expression of respiratory chain subunits of complex I (NDUFB10) and complex IV (mtCO-2 and COX IV).	disulphide	45-55	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	14-20
29789341-7	2018	Knockdown of Mia40, which introduces disulfide bonds into CHCH domain proteins, blocked mitochondrial import of CHCHD10.	Disulfides	37-46	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	13-18
29789341-8	2018	Overexpression of Mia40 rescued mitochondrial import of CHCHD10 Q108P by enhancing disulfide-bond formation.	Disulfides	83-92	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	18-23
29270408-6	2017	Most IMS proteins lack presequences and instead utilize the IMS receptor Mia40, which facilitates their translocation across the outer membrane in a reaction that is coupled to the formation of disulfide bonds within the protein.	Disulfides	194-203	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	73-78
29241459-3	2017	However, the other essential protein, Mia40, was found to be absent or not required in some organisms, raising questions about how the disulfide relay functions in these organisms.	Disulfides	135-144	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	38-43
29270408-8	2017	Mia40 fulfills two roles: First, it acts as a holdase, which is crucial in the import of IMS proteins and second, it functions as a foldase, introducing disulfide bonds into newly imported proteins, which induces and stabilizes their natively folded state.	Disulfides	153-162	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
29208936-5	2017	Using an integrated real-time approach, including chromatography, fluorescence, CD, FTIR, SAXS, NMR, and MS analysis, we demonstrate that in this mitochondrial protein, the conformational switch between disordered and folded states is controlled by the formation of a single disulfide bond, both in the presence and in the absence of Mia40.	Cadmium	80-82	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	334-339
29208936-5	2017	Using an integrated real-time approach, including chromatography, fluorescence, CD, FTIR, SAXS, NMR, and MS analysis, we demonstrate that in this mitochondrial protein, the conformational switch between disordered and folded states is controlled by the formation of a single disulfide bond, both in the presence and in the absence of Mia40.	Disulfides	275-284	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	334-339
25956655-3	2015	Recent data demonstrate that APE1 interacts with the mitochondrial import and assembly protein Mia40 suggesting the involvement of a redox-assisted mechanism, dependent on the disulfide transfer system, to be responsible of APE1 trafficking into the mitochondria.	Disulfides	176-185	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	95-100
28814504-6	2017	In reconstitution studies with reduced Tim13, Mia40, and Erv1, the addition of Osm1 and fumarate completes the disulfide exchange pathway that results in Tim13 oxidation.	Fumarates	88-96	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	46-51
28814504-6	2017	In reconstitution studies with reduced Tim13, Mia40, and Erv1, the addition of Osm1 and fumarate completes the disulfide exchange pathway that results in Tim13 oxidation.	Disulfides	111-120	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	46-51
28497026-8	2017	Mutation of the functionally important highly conserved cysteines within the Cys-Pro-Cys motif of CHCHD4 or inhibition of complex IV activity (by sodium azide) redistributes mitochondria from the perinuclear region toward the periphery of the cell and blocks HIF activation.	Cysteine	56-65	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	98-104
28497026-8	2017	Mutation of the functionally important highly conserved cysteines within the Cys-Pro-Cys motif of CHCHD4 or inhibition of complex IV activity (by sodium azide) redistributes mitochondria from the perinuclear region toward the periphery of the cell and blocks HIF activation.	Cys-Pro-Cys	77-88	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	98-104
26085103-1	2015	A redox-regulated import pathway consisting of Mia40 and Erv1 mediates the import of cysteine-rich proteins into the mitochondrial intermembrane space.	Cysteine	85-93	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	47-52
26085103-2	2015	Mia40 is the oxidoreductase that inserts two disulfide bonds into the substrate simultaneously.	Disulfides	45-54	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
26085103-3	2015	However, Mia40 has one redox-active cysteine pair, resulting in ambiguity about how Mia40 accepts numerous electrons during substrate oxidation.	Cysteine	36-44	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	9-14
26085103-3	2015	However, Mia40 has one redox-active cysteine pair, resulting in ambiguity about how Mia40 accepts numerous electrons during substrate oxidation.	Cysteine	36-44	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	84-89
26085103-6	2015	In addition, a ternary complex consisting of Erv1, Mia40, and substrate, linked by disulfide bonds, was not detected in vitro.	Disulfides	83-92	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	51-56
26085103-9	2015	Therefore, these studies support that Mia40 functions as an electron sink to facilitate the insertion of two disulfide bonds into substrates.	Disulfides	109-118	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	38-43
26214018-8	2015	The introduction of disulfides in the IMS is catalyzed by Mia40 that functions as a chaperone inducing their folding.	Disulfides	20-30	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	58-63
26214018-10	2015	The solution NMR structure of Mia40 (and supporting biochemical experiments) showed that Mia40 is a novel type of disulfide donor whose recognition capacity for its substrates relies on a hydrophobic binding cleft found adjacent to a thiol active CPC motif.	Disulfides	114-123	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	30-35
26214018-10	2015	The solution NMR structure of Mia40 (and supporting biochemical experiments) showed that Mia40 is a novel type of disulfide donor whose recognition capacity for its substrates relies on a hydrophobic binding cleft found adjacent to a thiol active CPC motif.	Disulfides	114-123	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	89-94
26214018-10	2015	The solution NMR structure of Mia40 (and supporting biochemical experiments) showed that Mia40 is a novel type of disulfide donor whose recognition capacity for its substrates relies on a hydrophobic binding cleft found adjacent to a thiol active CPC motif.	Sulfhydryl Compounds	234-239	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	30-35
26214018-10	2015	The solution NMR structure of Mia40 (and supporting biochemical experiments) showed that Mia40 is a novel type of disulfide donor whose recognition capacity for its substrates relies on a hydrophobic binding cleft found adjacent to a thiol active CPC motif.	Sulfhydryl Compounds	234-239	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	89-94
26214018-12	2015	This consists of only 9 amino acids, found upstream or downstream of a unique Cys that is primed for docking to Mia40 when the substrate is accommodated in the Mia40 binding cleft.	Cysteine	78-81	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	112-117
26214018-12	2015	This consists of only 9 amino acids, found upstream or downstream of a unique Cys that is primed for docking to Mia40 when the substrate is accommodated in the Mia40 binding cleft.	Cysteine	78-81	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	160-165
26214018-14	2015	Identification of new Mia40 substrates (some even without the requirement of their cysteines) reveals an expanded chaperone-like activity of this protein in the IMS.	Cysteine	83-92	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	22-27
26275620-0	2015	Human mitochondrial MIA40 (CHCHD4) is a component of the Fe-S cluster export machinery.	Iron	57-61	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	20-25
26275620-0	2015	Human mitochondrial MIA40 (CHCHD4) is a component of the Fe-S cluster export machinery.	Iron	57-61	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	27-33
26275620-4	2015	hMIA40 is an iron-binding protein with the ability to bind iron in vivo and in vitro.	Iron	13-17	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-6
26275620-4	2015	hMIA40 is an iron-binding protein with the ability to bind iron in vivo and in vitro.	Iron	59-63	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-6
26275620-5	2015	hMIA40 harbours CPC (Cys-Pro-Cys) motif-dependent Fe-S clusters that are sensitive to oxidation.	cpc	16-19	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-6
26275620-5	2015	hMIA40 harbours CPC (Cys-Pro-Cys) motif-dependent Fe-S clusters that are sensitive to oxidation.	Cys-Pro-Cys	21-32	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-6
26275620-5	2015	hMIA40 harbours CPC (Cys-Pro-Cys) motif-dependent Fe-S clusters that are sensitive to oxidation.	Iron	50-54	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-6
26275620-6	2015	Depletion of hMIA40 results in accumulation of iron in mitochondria concomitant with decreases in the activity and stability of Fe-S-containing cytosolic enzymes.	Iron	47-51	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	13-19
26275620-6	2015	Depletion of hMIA40 results in accumulation of iron in mitochondria concomitant with decreases in the activity and stability of Fe-S-containing cytosolic enzymes.	Iron	128-132	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	13-19
26275620-8	2015	Taken together, our results demonstrate an indispensable role for hMIA40 for the export of Fe-S clusters from mitochondria.	Iron	91-95	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	66-72
26387864-1	2015	The essential oxidoreductase Mia40/CHCHD4 mediates disulfide bond formation and protein folding in the mitochondrial intermembrane space.	Disulfides	51-60	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	29-34
26387864-1	2015	The essential oxidoreductase Mia40/CHCHD4 mediates disulfide bond formation and protein folding in the mitochondrial intermembrane space.	Disulfides	51-60	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	35-41
26387864-2	2015	Here, we investigated the interactome of Mia40 thereby revealing links between thiol-oxidation and apoptosis, energy metabolism, and Ca(2+) signaling.	Sulfhydryl Compounds	79-84	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	41-46
26387864-4	2015	We examined the biogenesis of MICU1 and find that Mia40 introduces an intermolecular disulfide bond that links MICU1 and its inhibitory paralog MICU2 in a heterodimer.	Disulfides	85-94	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	50-55
26371297-6	2015	Our new assignments include two CHCH-domain containing subunits that contain disulfide bridges between CX9C motifs; they are processed by the Mia40 oxidative-folding pathway in the intermembrane space and probably stabilize the membrane domain.	Disulfides	77-86	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	142-147
26014136-3	2015	Reduced pancreatic ribonuclease A (rRNase), avian lysozyme, and riboflavin binding protein are all competent substrates of the Mia40/lfALR system, although they lack those sequence features previously thought to direct disulfide bond formation in cognate IMS substrates.	Riboflavin	64-74	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	127-132
26014136-3	2015	Reduced pancreatic ribonuclease A (rRNase), avian lysozyme, and riboflavin binding protein are all competent substrates of the Mia40/lfALR system, although they lack those sequence features previously thought to direct disulfide bond formation in cognate IMS substrates.	Disulfides	219-228	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	127-132
25956655-5	2015	It is composed by two main proteins: Mia40 is the oxidoreductase that catalyzes the formation of the disulfide bonds in the substrate, while ALR reoxidizes Mia40 after the import.	Disulfides	101-110	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	37-42
25956655-6	2015	In this study, we demonstrated that: (i) APE1 and Mia40 interact through disulfide bond formation; and (ii) Mia40 expression levels directly affect APE1"s mitochondrial translocation and, consequently, play a role in the maintenance of mitochondrial DNA integrity.	Disulfides	73-82	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	50-55
25956655-6	2015	In this study, we demonstrated that: (i) APE1 and Mia40 interact through disulfide bond formation; and (ii) Mia40 expression levels directly affect APE1"s mitochondrial translocation and, consequently, play a role in the maintenance of mitochondrial DNA integrity.	Disulfides	73-82	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	108-113
24569988-1	2014	Mia40-catalyzed disulfide formation drives the import of many proteins into the mitochondria.	Disulfides	16-25	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
25451030-1	2014	Mia40 (a mitochondrial import and assembly protein) catalyzes disulfide bond formation in proteins in the mitochondrial intermembrane space.	Disulfides	62-71	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
25451030-2	2014	By using Cox17 (a mitochondrial copper-binding protein) as a natural substrate, we discovered that, in the presence of Mia40, the formation of native disulfides is strongly favored.	Copper	32-38	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	119-124
25451030-2	2014	By using Cox17 (a mitochondrial copper-binding protein) as a natural substrate, we discovered that, in the presence of Mia40, the formation of native disulfides is strongly favored.	Disulfides	150-160	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	119-124
25451030-3	2014	The catalytic mechanism of Mia40 involves a functional interplay between the chaperone site and the catalytic disulfide.	Disulfides	110-119	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	27-32
25451030-4	2014	Mia40 forms a specific native disulfide in Cox17 much more rapidly than other disulfides, in particular, non-native ones, which originates from the recently described high affinity for hydrophobic regions near target cysteines and the long lifetime of the mixed disulfide.	Disulfides	30-39	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
25451030-4	2014	Mia40 forms a specific native disulfide in Cox17 much more rapidly than other disulfides, in particular, non-native ones, which originates from the recently described high affinity for hydrophobic regions near target cysteines and the long lifetime of the mixed disulfide.	Disulfides	78-88	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
25451030-4	2014	Mia40 forms a specific native disulfide in Cox17 much more rapidly than other disulfides, in particular, non-native ones, which originates from the recently described high affinity for hydrophobic regions near target cysteines and the long lifetime of the mixed disulfide.	Disulfides	78-87	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
25451030-6	2014	We found that species with inadvertently formed incorrect disulfides are rebound by Mia40 and reshuffled, revealing a proofreading mechanism that is steered by the conformational folding of the substrate protein.	Disulfides	58-68	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	84-89
24983157-4	2014	The catalytic cysteines of Mia40 display unusually low chemical reactivity, as expressed in conventional pK values and reduction potentials.	Cysteine	14-23	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	27-32
24983157-5	2014	The stability of the mixed disulfide intermediate is coupled energetically with hydrophobic interactions between Mia40 and the substrate.	Disulfides	27-36	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	113-118
24983157-6	2014	Based on these properties, we suggest a mechanism for Mia40, where the hydrophobic binding site is employed to select a substrate thiol for forming the initial mixed disulfide.	Sulfhydryl Compounds	130-135	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	54-59
24983157-6	2014	Based on these properties, we suggest a mechanism for Mia40, where the hydrophobic binding site is employed to select a substrate thiol for forming the initial mixed disulfide.	Disulfides	166-175	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	54-59
25392302-2	2015	The main component of this pathway is the oxidoreductase Mia40, which introduces disulfides into its substrates.	Disulfides	81-91	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	57-62
25392302-5	2015	Here we demonstrate the presence of glutaredoxins in the IMS and show that limiting amounts of these glutaredoxins provide a kinetic barrier to prevent the thermodynamically feasible reduction of Mia40 substrates by the IMS glutathione pool.	Glutathione	224-235	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	196-201
24569988-4	2014	Mia40 accelerates Cox19 folding through the specific recognition of the third Cys in the second helical CX9C motif and the subsequent oxidation of the inner disulfide bond.	Cysteine	78-81	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
24569988-4	2014	Mia40 accelerates Cox19 folding through the specific recognition of the third Cys in the second helical CX9C motif and the subsequent oxidation of the inner disulfide bond.	Disulfides	157-166	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
24569988-6	2014	The same intermediate dominates the pathway in the absence of Mia40, and chemical induction of an alpha-helical structure by trifluoroethanol suffices to accelerate productive folding and mimic the Mia40 folding template mechanism.	Trifluoroethanol	125-141	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	198-203
24382809-7	2014	Insertion of nuclear-encoded mitochondrial proteins requires specific import pathways; we show that specific cysteine motifs, part of the Mia40/Erv1 mitochondrial import pathway, are present in PLP and are required for its insertion into mitochondria.	Cysteine	109-117	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	138-143
24382809-10	2014	These physiological abnormalities are preventable by mutations in PLP cysteine motifs, a hallmark of the Mia40/Erv1 pathway.	Cysteine	70-78	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	105-110
24407114-0	2014	Mia40 targets cysteines in a hydrophobic environment to direct oxidative protein folding in the mitochondria.	Cysteine	14-23	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
24360785-5	2014	Mrp10 contains an unconventional proline-rich matrix-targeting sequence that renders import intermediates accessible to Mia40.	Proline	33-40	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	120-125
24407114-1	2014	Mia40 catalyses the oxidative folding of disulphide-containing proteins in the mitochondria.	disulphide	41-51	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
24407114-2	2014	The folding pathway is directed by the formation of the first mixed disulphide between Mia40 and its substrate.	disulphide	68-78	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	87-92
24407114-5	2014	Cys36 of Cox17 forms the mixed disulphide in an extremely rapid reaction that is limited by the preceding complex formation with Mia40.	disulphide	31-41	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	129-134
24407114-7	2014	Mia40 binds preferentially to hydrophobic regions and the dynamic nature of the non-covalent complex allows rapid reorientation for an optimal positioning of the reactive cysteine.	Cysteine	171-179	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
24407114-8	2014	Mia40 thus uses the unique proximity between its substrate-binding site and the catalytic disulphide to select a particular cysteine for forming the critical initial mixed disulphide.	disulphide	90-100	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
24407114-8	2014	Mia40 thus uses the unique proximity between its substrate-binding site and the catalytic disulphide to select a particular cysteine for forming the critical initial mixed disulphide.	Cysteine	124-132	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
24407114-8	2014	Mia40 thus uses the unique proximity between its substrate-binding site and the catalytic disulphide to select a particular cysteine for forming the critical initial mixed disulphide.	disulphide	172-182	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
24101517-2	2013	Here we report that the mammalian homolog of the yeast mitochondrial disulfide relay protein Mia40 (CHCHD4) is necessary for the respiratory-dependent translocation of p53 into the mitochondria.	Disulfides	69-78	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	100-106
23834247-2	2013	Mia40 uses its redox active CPC motif to shuttle disulfides between its client proteins (newly imported proteins) and the thiol oxidase Erv1.	Disulfides	49-59	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
23834247-5	2013	We show that Mia40 binds a [2Fe-2S] cluster in a dimer form with the cluster co-ordinated by the cysteine residues of the CPC motifs.	Cysteine	97-105	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	13-18
23834247-6	2013	The biological relevance of the cofactor binding was confirmed in vivo by cysteine redox state and iron uptake analyses, which showed that a significant amount of cellular Mia40 binds iron in vivo.	Cysteine	74-82	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	172-177
23834247-6	2013	The biological relevance of the cofactor binding was confirmed in vivo by cysteine redox state and iron uptake analyses, which showed that a significant amount of cellular Mia40 binds iron in vivo.	Iron	99-103	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	172-177
23834247-6	2013	The biological relevance of the cofactor binding was confirmed in vivo by cysteine redox state and iron uptake analyses, which showed that a significant amount of cellular Mia40 binds iron in vivo.	Iron	184-188	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	172-177
23834247-7	2013	Furthermore, our oxygen consumption results suggested that the Fe-S-containing Mia40 is not an electron donor for Erv1.	Oxygen	17-23	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	79-84
23834247-7	2013	Furthermore, our oxygen consumption results suggested that the Fe-S-containing Mia40 is not an electron donor for Erv1.	Iron	63-67	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	79-84
22901034-2	2013	This oxidative folding process depends on the disulfide donor/import receptor Mia40 and the flavin adenine dinucleotide oxidase Erv1 and concerns proteins involved in mitochondrial biogenesis, respiratory complex assembly, and metal transfer.	Disulfides	46-55	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	78-83
22901034-7	2013	Furthermore, a more general role for Mia40 in recognizing substrates targeted to other compartments, or even without specific cysteine motifs, remains an intriguing possibility.	Cysteine	126-134	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	37-42
23676665-3	2013	We developed assays to follow protein oxidation in living mammalian cells, which reveal that import and oxidative folding of proteins are kinetically and functionally coupled and depend on the oxidoreductase Mia40, the sulfhydryl oxidase augmenter of liver regeneration (ALR), and the intracellular glutathione pool.	Glutathione	299-310	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	208-213
23790485-2	2013	Several proteins of the intermembrane space (IMS) are imported and localized through an oxidative process, being folded through the formation of structural disulfide bonds catalyzed by Mia40, and trapped in the IMS.	Disulfides	156-165	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	185-190
22910915-2	2012	This process requires disulfide bond transfer from oxidized Mia40 to a substrate protein.	Disulfides	22-31	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	60-65
23197653-3	2013	This system (consisting of two proteins, Gfer and Mia40) is involved in the mitochondrial import of Cys-rich proteins.	Cysteine	100-103	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	50-55
23283984-2	2013	The oxidoreductase Mia40 is a central component of the pathway responsible for the transfer of disulfide bonds to intermembrane space precursor proteins, causing their oxidative folding.	Disulfides	95-104	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	19-24
23283984-6	2013	Tim22 forms a disulfide-bonded intermediate with Mia40 upon import into mitochondria.	Disulfides	14-23	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	49-54
23283984-8	2013	We propose that Mia40 not only is responsible for disulfide bond formation, but also assists the Tim22 protein in its integration into the inner membrane of mitochondria.	Disulfides	50-59	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	16-21
24348563-2	2013	The main components of this disulfide relay machinery are the oxidoreductase Mia40 and the sulfhydryl oxidase Erv1/ALR.	Disulfides	28-37	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	77-82
23019327-4	2012	The CHCH domain proteins are traditionally imported and trapped in the IMS by using a disulfide relay system mediated by Mia40 and Erv1.	Disulfides	86-95	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	121-126
23019327-7	2012	By analysis of the CHCH domain cysteine mutants, we further show that they have distinct roles in binding to Mia40 in the IMS and proper folding of the protein.	Cysteine	31-39	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	109-114
23019327-8	2012	The transient disulfide-bonded intermediate with Mia40 is formed preferentially between the second cysteine in helix 1, Cys(193), and the active site cysteine in Mia40, Cys(55).	Disulfides	14-23	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	49-54
23019327-8	2012	The transient disulfide-bonded intermediate with Mia40 is formed preferentially between the second cysteine in helix 1, Cys(193), and the active site cysteine in Mia40, Cys(55).	Disulfides	14-23	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	162-167
23019327-8	2012	The transient disulfide-bonded intermediate with Mia40 is formed preferentially between the second cysteine in helix 1, Cys(193), and the active site cysteine in Mia40, Cys(55).	Cysteine	99-107	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	49-54
23019327-8	2012	The transient disulfide-bonded intermediate with Mia40 is formed preferentially between the second cysteine in helix 1, Cys(193), and the active site cysteine in Mia40, Cys(55).	Cysteine	99-107	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	162-167
23019327-8	2012	The transient disulfide-bonded intermediate with Mia40 is formed preferentially between the second cysteine in helix 1, Cys(193), and the active site cysteine in Mia40, Cys(55).	Cysteine	120-123	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	49-54
23019327-8	2012	The transient disulfide-bonded intermediate with Mia40 is formed preferentially between the second cysteine in helix 1, Cys(193), and the active site cysteine in Mia40, Cys(55).	Cysteine	120-123	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	162-167
23019327-8	2012	The transient disulfide-bonded intermediate with Mia40 is formed preferentially between the second cysteine in helix 1, Cys(193), and the active site cysteine in Mia40, Cys(55).	Cysteine	150-158	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	49-54
23019327-8	2012	The transient disulfide-bonded intermediate with Mia40 is formed preferentially between the second cysteine in helix 1, Cys(193), and the active site cysteine in Mia40, Cys(55).	Cysteine	150-158	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	162-167
23019327-8	2012	The transient disulfide-bonded intermediate with Mia40 is formed preferentially between the second cysteine in helix 1, Cys(193), and the active site cysteine in Mia40, Cys(55).	Cysteine	169-172	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	49-54
23186364-0	2013	Disulfide bond formation: sulfhydryl oxidase ALR controls mitochondrial biogenesis of human MIA40.	Disulfides	0-9	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	92-97
22990235-2	2012	Substrates of Mia40 that were identified so far are of simple structure and receive one or two disulphide bonds.	disulphide	95-105	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	14-19
22990235-4	2012	Atp23 contains ten cysteine residues which are oxidized during several rounds of interaction with Mia40.	Cysteine	19-27	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	98-103
22990235-8	2012	Thus, Mia40 plays a much broader role in import and folding of polypeptides than previously expected and can serve as folding factor for proteins with complex disulphide patterns as well as for cysteine-free polypeptides.	disulphide	159-169	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	6-11
22990235-8	2012	Thus, Mia40 plays a much broader role in import and folding of polypeptides than previously expected and can serve as folding factor for proteins with complex disulphide patterns as well as for cysteine-free polypeptides.	Cysteine	194-202	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	6-11
22705944-0	2012	Glutathione redox potential in the mitochondrial intermembrane space is linked to the cytosol and impacts the Mia40 redox state.	Glutathione	0-11	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	110-115
22842048-6	2012	These results suggest a model where the molecular interactions guiding the protein recognition between Mia40 and the disulfide-reduced CHCHD5 and CHCHD7 substrates occurs in vivo when the latter proteins are partially embedded in the protein import pore of the outer membrane of mitochondria.	Disulfides	117-126	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	103-108
22918950-2	2012	The disulfide bond formation pathway is based on a relay of reactions involving disulfide transfer from the sulfhydryl oxidase Erv1 to Mia40 and from Mia40 to substrate proteins.	Disulfides	4-13	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	135-140
22918950-2	2012	The disulfide bond formation pathway is based on a relay of reactions involving disulfide transfer from the sulfhydryl oxidase Erv1 to Mia40 and from Mia40 to substrate proteins.	Disulfides	4-13	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	150-155
22918950-2	2012	The disulfide bond formation pathway is based on a relay of reactions involving disulfide transfer from the sulfhydryl oxidase Erv1 to Mia40 and from Mia40 to substrate proteins.	Disulfides	80-89	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	135-140
22918950-2	2012	The disulfide bond formation pathway is based on a relay of reactions involving disulfide transfer from the sulfhydryl oxidase Erv1 to Mia40 and from Mia40 to substrate proteins.	Disulfides	80-89	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	150-155
22918950-8	2012	Thus Mia40 in cooperation with Erv1 promotes the formation of two disulfide bonds in the substrate protein, ensuring the efficiency of oxidative folding in the intermembrane space of mitochondria.	Disulfides	66-75	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	5-10
22705944-7	2012	Moreover, we show that the local E(GSH) contributes to the partially reduced redox state of the IMS oxidoreductase Mia40 in vivo.	Glutathione	35-38	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	115-120
22612783-2	2012	Contrary to the endoplasmatic reticulum ER where several chaperones of the disulfide isomerase family exist, oxidative folding in the IMS is exclusively catalyzed by the oxoreductase Mia40 that recognizes a group of proteins with characteristic cysteine motifs organized in twin CX(3)C, twin CX(9)C or CX(2)C motifs.	Cysteine	245-253	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	183-188
22296668-3	2012	The C-terminal FAD-binding domain of Erv1/ALR has an essential role in the import process by creating a transient  intermolecular disulfide bond with Mia40.	Disulfides	130-139	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	150-155
22296668-4	2012	The action of Mia40 is selective for the formation of both intra and intersubunit structural disulfide bonds of Erv1/ALR, but the complete maturation process requires additional binding of FAD.	Disulfides	93-102	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	14-19
21700214-2	2011	Here, the structural and metal-binding properties of anamorsin and its interaction with Mia40, a well-known oxidoreductase involved in protein trapping in the mitochondrial intermembrane space (IMS), were characterized.	Metals	25-30	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	88-93
22224850-1	2012	The oxidative folding mechanism in the intermembrane space of human mitochondria underpins a disulfide relay system consisting of the import receptor Mia40 and the homodimeric FAD-dependent thiol oxidase ALR.	Disulfides	93-102	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	150-155
22224850-4	2012	The intermediate critical for the electron-transfer process implies the formation of a specific inter-subunit disulfide which exclusively allows electron flow from Mia40 to FAD.	Disulfides	110-119	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	164-169
21865594-0	2011	Mia40-dependent oxidation of cysteines in domain I of Ccs1 controls its distribution between mitochondria and the cytosol.	Cysteine	29-38	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
21865594-7	2011	In this study we detail the import and folding pathway of Ccs1 and characterize its interaction with the oxidoreductase of the mitochondrial disulfide relay Mia40.	Disulfides	141-150	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	157-162
21865594-8	2011	We identify cysteines at positions 27 and 64 in domain I of Ccs1 as critical for mitochondrial import and interaction with Mia40.	Cysteine	12-21	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	123-128
21865594-9	2011	On interaction with Mia40, these cysteines form a structural disulfide bond that stabilizes the overall fold of domain I.	Cysteine	33-42	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	20-25
21865594-9	2011	On interaction with Mia40, these cysteines form a structural disulfide bond that stabilizes the overall fold of domain I.	Disulfides	61-70	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	20-25
20849374-3	2011	Pathways that form disulfide bonds have now been unraveled in the bacterial periplasm (disulfide bond protein A [DsbA], DsbB, DsbC, DsbG, and DsbD), the endoplasmic reticulum (protein disulfide isomerase and Ero1), and the mitochondrial intermembrane space (Mia40 and Erv1).	Disulfides	19-28	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	258-263
22214851-0	2012	Human CHCHD4 mitochondrial proteins regulate cellular oxygen consumption rate and metabolism and provide a critical role in hypoxia signaling and tumor progression.	Oxygen	54-60	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	6-12
22214851-6	2012	CHCHD4.1 is identical to MIA40, the homolog of yeast Mia40, a key component of the mitochondrial disulfide relay system that regulates electron transfer to cytochrome c. Further analysis revealed that CHCHD4 proteins contain an evolutionarily conserved coiled-coil-helix-coiled-coil-helix (CHCH) domain important for mitochondrial localization.	Disulfides	97-106	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-6
22214851-6	2012	CHCHD4.1 is identical to MIA40, the homolog of yeast Mia40, a key component of the mitochondrial disulfide relay system that regulates electron transfer to cytochrome c. Further analysis revealed that CHCHD4 proteins contain an evolutionarily conserved coiled-coil-helix-coiled-coil-helix (CHCH) domain important for mitochondrial localization.	Disulfides	97-106	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	201-207
22214851-7	2012	Modulation of CHCHD4 protein expression in tumor cells regulated cellular oxygen consumption rate and metabolism.	Oxygen	74-80	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	14-20
23091723-6	2012	Finally, the protein CHCHD4, which modulates cellular HIF-1alpha concentrations by promoting mitochondrial electron transport chain activity, has been proposed to exert its regulatory effect by affecting cellular oxygen availability.	Oxygen	213-219	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	21-27
21383138-1	2011	Oxidative protein folding in the mitochondrial intermembrane space requires the transfer of a disulfide bond from MIA40 to the substrate.	Disulfides	94-103	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	114-119
21383138-2	2011	During this process MIA40 is reduced and regenerated to a functional state through the interaction with the flavin-dependent sulfhydryl oxidase ALR.	4,6-dinitro-o-cresol	108-114	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	20-25
21383138-3	2011	Here we present the mechanistic basis of ALR-MIA40 interaction at atomic resolution by biochemical and structural analyses of the mitochondrial ALR isoform and its covalent mixed disulfide intermediate with MIA40.	Disulfides	179-188	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	45-50
21383138-3	2011	Here we present the mechanistic basis of ALR-MIA40 interaction at atomic resolution by biochemical and structural analyses of the mitochondrial ALR isoform and its covalent mixed disulfide intermediate with MIA40.	Disulfides	179-188	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	207-212
20537978-4	2011	Mia40 is maintained in an oxidized, active conformation by the sulfhydryl oxidase Erv1, a homodimeric flavoenzyme, which can form disulfide bonds de novo.	Disulfides	130-139	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
20136511-4	2010	Tim40/Mia40 transfers disulfide bonds to newly imported IMS proteins by dithiol/disulfide exchange reactions involving mixed disulfide intermediates.	Disulfides	22-31	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	6-11
21059946-2	2010	A class of such proteins with alpha-helical hairpin structure bridged by two intramolecular disulfides is trapped by a Mia40-dependent oxidative process.	Disulfides	92-102	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	119-124
20367259-4	2010	IMS import of SOD1 involves its copper chaperone, CCS, whose mitochondrial distribution is regulated by the Mia40/Erv1 disulfide relay system in a redox-dependent manner: CCS promotes SOD1 maturation and retention in the IMS.	Disulfides	119-128	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	108-113
20136511-4	2010	Tim40/Mia40 transfers disulfide bonds to newly imported IMS proteins by dithiol/disulfide exchange reactions involving mixed disulfide intermediates.	dithiol	72-79	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	6-11
20136511-4	2010	Tim40/Mia40 transfers disulfide bonds to newly imported IMS proteins by dithiol/disulfide exchange reactions involving mixed disulfide intermediates.	Disulfides	80-89	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	6-11
20136511-4	2010	Tim40/Mia40 transfers disulfide bonds to newly imported IMS proteins by dithiol/disulfide exchange reactions involving mixed disulfide intermediates.	Disulfides	80-89	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	6-11
20136511-6	2010	After disulfide transfer from Tim40/Mia40 to substrate proteins, Tim40/Mia40 is reoxidized again by Erv1, which is then oxidized by electron transfer to either cytochrome c or molecular oxygen.	Disulfides	6-15	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	36-41
20136511-6	2010	After disulfide transfer from Tim40/Mia40 to substrate proteins, Tim40/Mia40 is reoxidized again by Erv1, which is then oxidized by electron transfer to either cytochrome c or molecular oxygen.	Disulfides	6-15	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	71-76
20136511-6	2010	After disulfide transfer from Tim40/Mia40 to substrate proteins, Tim40/Mia40 is reoxidized again by Erv1, which is then oxidized by electron transfer to either cytochrome c or molecular oxygen.	Oxygen	186-192	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	36-41
20136511-6	2010	After disulfide transfer from Tim40/Mia40 to substrate proteins, Tim40/Mia40 is reoxidized again by Erv1, which is then oxidized by electron transfer to either cytochrome c or molecular oxygen.	Oxygen	186-192	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	71-76
20367259-4	2010	IMS import of SOD1 involves its copper chaperone, CCS, whose mitochondrial distribution is regulated by the Mia40/Erv1 disulfide relay system in a redox-dependent manner: CCS promotes SOD1 maturation and retention in the IMS.	Copper	32-38	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	108-113
20026652-0	2009	A novel intermembrane space-targeting signal docks cysteines onto Mia40 during mitochondrial oxidative folding.	Cysteine	51-60	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	66-71
20214493-5	2010	Proteins destined to the intermembrane space are trapped by a disulfide relay mechanism that involves an electron cascade from the incoming substrate to Mia40, then on to Erv1, and finally to molecular oxygen via cytochrome c.	Disulfides	62-71	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	153-158
20026652-1	2009	Mia40 imports Cys-containing proteins into the mitochondrial intermembrane space (IMS) by ensuring their Cys-dependent oxidative folding.	Cysteine	14-17	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
20026652-1	2009	Mia40 imports Cys-containing proteins into the mitochondrial intermembrane space (IMS) by ensuring their Cys-dependent oxidative folding.	Cysteine	105-108	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
20026652-2	2009	In this study, we show that the specific Cys of the substrate involved in docking with Mia40 is substrate dependent, the process being guided by an IMS-targeting signal (ITS) present in Mia40 substrates.	Cysteine	41-44	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	87-92
20026652-2	2009	In this study, we show that the specific Cys of the substrate involved in docking with Mia40 is substrate dependent, the process being guided by an IMS-targeting signal (ITS) present in Mia40 substrates.	Cysteine	41-44	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	186-191
20026652-4	2009	We rationalize the dual function of Mia40 as a receptor and an oxidase in a two step-specific mechanism: an ITS-guided sliding step orients the substrate noncovalently, followed by docking of the substrate Cys now juxtaposed to pair with the Mia40 active Cys.	Cysteine	206-209	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	36-41
20026652-4	2009	We rationalize the dual function of Mia40 as a receptor and an oxidase in a two step-specific mechanism: an ITS-guided sliding step orients the substrate noncovalently, followed by docking of the substrate Cys now juxtaposed to pair with the Mia40 active Cys.	Cysteine	206-209	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	242-247
20026652-4	2009	We rationalize the dual function of Mia40 as a receptor and an oxidase in a two step-specific mechanism: an ITS-guided sliding step orients the substrate noncovalently, followed by docking of the substrate Cys now juxtaposed to pair with the Mia40 active Cys.	Cysteine	255-258	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	36-41
19679655-8	2009	To understand the functional role of each disulfide, small molecules and the physiological substrate protein Mia40 were used as electron donors in oxygen consumption assays.	Disulfides	42-51	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	109-114
19720617-4	2009	For their import into the IMS, they employ a disulphide relay system, made up of two essential proteins, Mia40/Tim40 and the flavin-dependent sulfhydryl-electron transferase Erv1.	disulphide	45-55	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	105-110
19679655-8	2009	To understand the functional role of each disulfide, small molecules and the physiological substrate protein Mia40 were used as electron donors in oxygen consumption assays.	Oxygen	147-153	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	109-114
18761382-5	2009	Substrates are imported via a disulfide exchange relay with two components Mia40 and Erv1.	Disulfides	30-39	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	75-80
19477928-1	2009	Mia40 and Erv1 execute a disulfide relay to import the small Tim proteins into the mitochondrial intermembrane space.	Disulfides	25-34	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
19182799-3	2009	MIA40 has a 66-residue folded domain made of an alpha-helical hairpin core stabilized by two structural disulfides and a rigid N-terminal lid, with a characteristic CPC motif that can donate its disulfide bond to substrates.	Disulfides	104-114	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
19182799-3	2009	MIA40 has a 66-residue folded domain made of an alpha-helical hairpin core stabilized by two structural disulfides and a rigid N-terminal lid, with a characteristic CPC motif that can donate its disulfide bond to substrates.	Disulfides	104-113	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
19397338-8	2009	An N-terminal His-tagged version of human Mia40, a resident oxidoreductase of the IMS and a putative physiological reductant of lfALR, was subcloned and expressed in Escherichia coli BL21 DE3 cells.	Histidine	14-17	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	42-47
19397338-9	2009	Mia40, as isolated, shows a visible spectrum characteristic of an Fe-S center and contains 0.56 +/- 0.02 atom of iron per subunit.	Iron	66-70	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
19397338-9	2009	Mia40, as isolated, shows a visible spectrum characteristic of an Fe-S center and contains 0.56 +/- 0.02 atom of iron per subunit.	Iron	113-117	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
19397338-10	2009	Treatment of Mia40 with guanidine hydrochloride and triscarboxyethylphosphine hydrochloride during purification removed this chromophore.	Guanidine	24-47	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	13-18
19397338-10	2009	Treatment of Mia40 with guanidine hydrochloride and triscarboxyethylphosphine hydrochloride during purification removed this chromophore.	triscarboxyethylphosphine hydrochloride	52-91	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	13-18
19397338-13	2009	Thus, catalysis involves a flow of reducing equivalents from the reduced CxC motif of Mia40 to distal and then proximal CxxC motifs of lfALR to the flavin ring and, finally, to cytochrome c or molecular oxygen.	4,6-dinitro-o-cresol	148-154	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	86-91
19397338-13	2009	Thus, catalysis involves a flow of reducing equivalents from the reduced CxC motif of Mia40 to distal and then proximal CxxC motifs of lfALR to the flavin ring and, finally, to cytochrome c or molecular oxygen.	Oxygen	203-209	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	86-91
18179776-3	2008	Recently, a disulfide relay system in the IMS has been identified which consists of two essential components, the sulfhydryl oxidase Erv1 and the redox-regulated import receptor Mia40/Tim40.	Disulfides	12-21	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	178-183
18852299-6	2008	The ternary complex represents a transient and intermediate step in the oxidation of intermembrane space precursors, where the oxidase Erv1 promotes disulfide transfer to the precursor while both oxidase and precursor are associated with the disulfide carrier Mia40.	Disulfides	242-251	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	260-265
19076451-4	2008	Mia40 is a protein in the intermembrane space that directly binds newly imported proteins via disulfide bonds.	Disulfides	94-103	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
19076451-5	2008	By reorganization of these bonds, intramolecular disulfide bonds are formed in the imported proteins, which are thereby released from Mia40 into the intermembrane space.	Disulfides	49-58	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	134-139
19076451-8	2008	Oxidation of Mia40 is carried out by Erv1, a conserved flavine adenine dinucleotide (FAD)-binding sulfhydryl oxidase.	Flavin-Adenine Dinucleotide	55-83	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	13-18
19076451-8	2008	Oxidation of Mia40 is carried out by Erv1, a conserved flavine adenine dinucleotide (FAD)-binding sulfhydryl oxidase.	Flavin-Adenine Dinucleotide	85-88	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	13-18
19076451-9	2008	Erv1 directly interacts with Mia40 and shuttles electrons from reduced Mia40 to oxidized cytochrome c, from whence they flow through cytochrome oxidase to molecular oxygen.	Oxygen	165-171	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	29-34
18787558-2	2008	This system consists of two essential proteins, Mia40 and Erv1, which bind to newly imported proteins by disulphide transfer.	disulphide	105-115	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	48-53
18179776-5	2008	In order to enable Mia40 to perform the oxidation of substrate proteins, the sulfhydryl oxidase Erv1 mediates the oxidation of Mia40 in a disulfide transfer reaction.	Disulfides	138-147	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	19-24
18179776-5	2008	In order to enable Mia40 to perform the oxidation of substrate proteins, the sulfhydryl oxidase Erv1 mediates the oxidation of Mia40 in a disulfide transfer reaction.	Disulfides	138-147	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	127-132
17680986-5	2007	Here we show that interaction with Mia40 is a site-specific event: (i) the N-terminal first cysteine of the precursor is crucial for docking onto Mia40 via a mixed disulphide; (ii) release is triggered by disulphide pairing of the C-terminal cysteine onto the N-terminal one; and (iii) formation of the inner disulphide between the second and third cysteines apparently precedes the release reaction and is critical for assembly with Tim9.	Cysteine	92-100	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	35-40
17978092-4	2008	Import of the precursors requires the essential intermembrane space proteins Mia40 and Erv1 that were proposed to form a relay for disulfide formation in the precursor proteins.	Disulfides	131-140	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	77-82
17959605-0	2007	Functional characterization of Mia40p, the central component of the disulfide relay system of the mitochondrial intermembrane space.	Disulfides	68-77	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	31-37
17959605-1	2007	Mia40p and Erv1p are components of a translocation pathway for the import of cysteine-rich proteins into the intermembrane space of mitochondria.	Cysteine	77-85	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-6
17959605-2	2007	We have characterized the redox behavior of Mia40p and reconstituted the disulfide transfer system of Mia40p by using recombinant functional C-terminal fragment of Mia40p, Mia40C, and Erv1p.	Disulfides	73-82	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	102-108
17959605-2	2007	We have characterized the redox behavior of Mia40p and reconstituted the disulfide transfer system of Mia40p by using recombinant functional C-terminal fragment of Mia40p, Mia40C, and Erv1p.	Disulfides	73-82	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	102-108
17959605-3	2007	Oxidized Mia40p contains three intramolecular disulfide bonds.	Disulfides	46-55	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	9-15
17680986-5	2007	Here we show that interaction with Mia40 is a site-specific event: (i) the N-terminal first cysteine of the precursor is crucial for docking onto Mia40 via a mixed disulphide; (ii) release is triggered by disulphide pairing of the C-terminal cysteine onto the N-terminal one; and (iii) formation of the inner disulphide between the second and third cysteines apparently precedes the release reaction and is critical for assembly with Tim9.	Cysteine	92-100	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	146-151
17680986-5	2007	Here we show that interaction with Mia40 is a site-specific event: (i) the N-terminal first cysteine of the precursor is crucial for docking onto Mia40 via a mixed disulphide; (ii) release is triggered by disulphide pairing of the C-terminal cysteine onto the N-terminal one; and (iii) formation of the inner disulphide between the second and third cysteines apparently precedes the release reaction and is critical for assembly with Tim9.	disulphide	164-174	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	35-40
17967948-3	2007	Both factors form a disulfide relay system in which Mia40 functions as a receptor that transiently interacts with incoming polypeptides via disulfide bonds.	Disulfides	20-29	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	52-57
17967948-3	2007	Both factors form a disulfide relay system in which Mia40 functions as a receptor that transiently interacts with incoming polypeptides via disulfide bonds.	Disulfides	140-149	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	52-57
17680986-5	2007	Here we show that interaction with Mia40 is a site-specific event: (i) the N-terminal first cysteine of the precursor is crucial for docking onto Mia40 via a mixed disulphide; (ii) release is triggered by disulphide pairing of the C-terminal cysteine onto the N-terminal one; and (iii) formation of the inner disulphide between the second and third cysteines apparently precedes the release reaction and is critical for assembly with Tim9.	disulphide	164-174	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	146-151
15989945-1	2005	In this issue of Cell, show that there is a disulfide relay system in the intermembrane space (IMS) of mitochondria that is comprised of the proteins Mia40 and Erv1.	Disulfides	44-53	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	150-155
17680986-5	2007	Here we show that interaction with Mia40 is a site-specific event: (i) the N-terminal first cysteine of the precursor is crucial for docking onto Mia40 via a mixed disulphide; (ii) release is triggered by disulphide pairing of the C-terminal cysteine onto the N-terminal one; and (iii) formation of the inner disulphide between the second and third cysteines apparently precedes the release reaction and is critical for assembly with Tim9.	disulphide	205-215	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	35-40
17680986-5	2007	Here we show that interaction with Mia40 is a site-specific event: (i) the N-terminal first cysteine of the precursor is crucial for docking onto Mia40 via a mixed disulphide; (ii) release is triggered by disulphide pairing of the C-terminal cysteine onto the N-terminal one; and (iii) formation of the inner disulphide between the second and third cysteines apparently precedes the release reaction and is critical for assembly with Tim9.	Cysteine	242-250	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	35-40
17680986-5	2007	Here we show that interaction with Mia40 is a site-specific event: (i) the N-terminal first cysteine of the precursor is crucial for docking onto Mia40 via a mixed disulphide; (ii) release is triggered by disulphide pairing of the C-terminal cysteine onto the N-terminal one; and (iii) formation of the inner disulphide between the second and third cysteines apparently precedes the release reaction and is critical for assembly with Tim9.	disulphide	205-215	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	35-40
17680986-5	2007	Here we show that interaction with Mia40 is a site-specific event: (i) the N-terminal first cysteine of the precursor is crucial for docking onto Mia40 via a mixed disulphide; (ii) release is triggered by disulphide pairing of the C-terminal cysteine onto the N-terminal one; and (iii) formation of the inner disulphide between the second and third cysteines apparently precedes the release reaction and is critical for assembly with Tim9.	Cysteine	349-358	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	35-40
16185709-6	2005	Depletion of MIA40 in human cells by RNA interference specifically affected steady-state levels of small and cysteine-containing intermembrane space proteins like DDP1 and TIM10A, suggesting that MIA40 acts along the import pathway into the intermembrane space.	Cysteine	109-117	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	13-18
16185709-6	2005	Depletion of MIA40 in human cells by RNA interference specifically affected steady-state levels of small and cysteine-containing intermembrane space proteins like DDP1 and TIM10A, suggesting that MIA40 acts along the import pathway into the intermembrane space.	Cysteine	109-117	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	196-201
16185709-7	2005	Studies on the in vivo redox state of human MIA40 demonstrated that it contains intramolecular disulfide bonds.	Disulfides	95-104	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	44-49
16185709-8	2005	Thiol-trapping assays revealed the co-existence of different oxidation states of human MIA40 within the cell.	Sulfhydryl Compounds	0-5	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	87-92
16185709-11	2005	Taken together, we conclude that the biogenesis and function of MIA40 in the mitochondrial intermembrane space is dependent on redox processes involving conserved cysteine residues.	Cysteine	163-171	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	64-69
17553782-0	2007	Biogenesis of the essential Tim9-Tim10 chaperone complex of mitochondria: site-specific recognition of cysteine residues by the intermembrane space receptor Mia40.	Cysteine	103-111	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	157-162
17553782-6	2007	Mia40 selectively recognizes cysteine-containing IMS proteins in a site-specific manner in organello and in vitro.	Cysteine	29-37	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
17336303-1	2007	The thiol oxidase Erv1 and the redox-regulated receptor Mia40/Tim40 are components of a disulfide relay system which mediates import of proteins into the intermembrane space (IMS) of mitochondria.	Disulfides	88-97	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	56-61
17336303-3	2007	After passage across the translocase of the mitochondrial outer membrane Erv1 interacts via disulfide bonds with Mia40.	Disulfides	92-101	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	113-118
16771672-5	2006	A redox pathway (Mia40p and Erv1p) mediates the import of intermembrane space proteins such as the small Tim proteins, Cox17p, and Cox19p, which have disulfide bonds.	Disulfides	150-159	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	17-23
15989955-3	2005	After passage through the TOM channel, these proteins are covalently trapped by Mia40 via disulfide bridges.	Disulfides	90-99	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	80-85
15989955-4	2005	Mia40 contains cysteine residues, which are oxidized by the sulfhydryl oxidase Erv1.	Cysteine	15-23	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
15989955-6	2005	We propose that Erv1 and Mia40 function as a disulfide relay system that catalyzes the import of proteins into the IMS by an oxidative folding mechanism.	Disulfides	45-54	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	25-30
15989945-3	2005	Oxidized Mia40 traps newly imported proteins through mixed disulfide bridges.	Disulfides	59-68	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	9-14
15989945-5	2005	The reduced Mia40 generated is then reoxidized by the sulfhydryl oxidase Erv1, promoting the next round of disulfide exchange.	Disulfides	107-116	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	12-17
33818502-0	2021	Exploring the contribution of the mitochondrial disulfide relay system to Parkinson"s disease: the PINK1/CHCHD4 interplay.	Disulfides	48-57	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	105-111
15620710-0	2005	Mia40, a novel factor for protein import into the intermembrane space of mitochondria is able to bind metal ions.	Metals	102-107	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
15620710-3	2005	We have identified an essential component, Mia40/Tim40/Ykl195w, with a highly conserved domain in the IMS that is able to bind zinc and copper ions.	Copper	136-142	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	43-48
15620710-4	2005	In cells lacking Mia40, the endogenous levels of Tim13 and other metal-binding IMS proteins are strongly reduced due to the impaired import of these proteins.	Metals	65-70	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	17-22
15620710-6	2005	We conclude that Mia40 is the first essential component of a specific translocation pathway of metal-binding IMS proteins.	Metals	95-100	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	17-22
34557489-5	2021	The intermembrane space (IMS) contains a high number of cysteine-rich proteins, which are mostly imported via the MIA40 oxidative folding system, dependent on the reduction, and oxidation of key Cys residues.	Cysteine	56-64	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	114-119
34557489-5	2021	The intermembrane space (IMS) contains a high number of cysteine-rich proteins, which are mostly imported via the MIA40 oxidative folding system, dependent on the reduction, and oxidation of key Cys residues.	Cysteine	195-198	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	114-119
35204825-9	2022	Redox sensitivity of p53 functions is supported by (i) thioredoxin-dependent reduction of p53 disulfides, (ii) inhibition of the thioredoxin-dependent deoxyribonucleotide synthesis by p53 binding to RRM2B and (iii) changed intracellular distribution of p53 through its oxidation by CHCHD4 in the mitochondrial intermembrane space.	Deoxyribonucleotides	151-170	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	282-288