5xti: Difference between revisions

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Cryo-EM architecture of human respiratory chain megacomplex-I2III2IV2

Structural highlights

5xti is a 138 chain structure with sequence from Bos taurus and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	8Q1, CDL, CU, FES, FMN, HEA, HEC, HEM, MG, NDP, PEE, PLX, SF4, ZN
Activity:	NADH:ubiquinone reductase (H(+)-translocating), with EC number 1.6.5.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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Disease

[QCR7_HUMAN] Isolated CoQ-cytochrome C reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [NDUAD_HUMAN] Papillary or follicular thyroid carcinoma. Disease susceptibility is associated with variations affecting the gene represented in this entry. Defects in NDUFA13 are a cause of a mitochondrial complex I deficiency characterized by early onset hypotonia, dyskinesia and sensorial deficiencies, as well as a severe optic neuropathy.^[1] [NDUS6_HUMAN] Isolated NADH-CoQ reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [NDUAA_HUMAN] Leigh syndrome with leukodystrophy. The disease is caused by mutations affecting the gene represented in this entry. [NDUAB_HUMAN] Isolated NADH-CoQ reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [NDUS4_HUMAN] Isolated NADH-CoQ reductase deficiency;Leigh syndrome with leukodystrophy. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. [CY1_HUMAN] Isolated CoQ-cytochrome C reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [NDUB9_HUMAN] Isolated NADH-CoQ reductase deficiency. [QCR8_HUMAN] Isolated CoQ-cytochrome C reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [NDUS1_HUMAN] Isolated NADH-CoQ reductase deficiency;Leigh syndrome with leukodystrophy. The disease is caused by mutations affecting the gene represented in this entry. [NDUS3_HUMAN] Isolated NADH-CoQ reductase deficiency;Leigh syndrome with leukodystrophy. [CYB_HUMAN] Histiocytoid cardiomyopathy;Leber hereditary optic neuropathy;Isolated CoQ-cytochrome C reductase deficiency. Defects in MT-CYB are a rare cause of mitochondrial dysfunction underlying different myopathies. They include mitochondrial encephalomyopathy, hypertrophic cardiomyopathy (HCM), and sporadic mitochondrial myopathy (MM). In mitochondrial myopathy, exercise intolerance is the predominant symptom. Additional features include lactic acidosis, muscle weakness and/or myoglobinuria. Defects in MTCYB are also found in cases of exercise intolerance accompanied by deafness, mental retardation, retinitis pigmentosa, cataract, growth retardation, epilepsy (multisystem disorder).^[2] ^[3] The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. [QCR2_HUMAN] Isolated CoQ-cytochrome C reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [NDUS8_HUMAN] Isolated NADH-CoQ reductase deficiency;Leigh syndrome with leukodystrophy. The disease is caused by mutations affecting the gene represented in this entry. [NDUA1_HUMAN] Isolated NADH-CoQ reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [NDUV1_HUMAN] Isolated NADH-CoQ reductase deficiency;Leigh syndrome with leukodystrophy. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. [NDUBB_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease may be caused by mutations affecting the gene represented in this entry. [NDUV2_HUMAN] Isolated NADH-CoQ reductase deficiency. [NDUB3_HUMAN] Isolated NADH-CoQ reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [NDUAC_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. [NDUS7_HUMAN] Isolated NADH-CoQ reductase deficiency;Leigh syndrome with leukodystrophy. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. [NDUA9_HUMAN] Isolated NADH-CoQ reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry.

Function

[B9EE38_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[SAAS:SAAS00136983] [Q4GRX1_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[SAAS:SAAS00093760] [QCR7_HUMAN] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This component is involved in redox-linked proton pumping. [NDUAD_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis (PubMed:27626371). Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (PubMed:27626371). Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes (PubMed:15753091).^[4] ^[5] ^[6] ^[7] [NDUA5_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[8] [NDUB8_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[9] [NDUS6_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[10] [NDUAA_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[11] [COX7B_BOVIN] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [NDUBA_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[12] [COX8B_BOVIN] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [QCR9_HUMAN] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This subunit interacts with cytochrome c1 (By similarity). [NDUAB_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[13] [NDUV3_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. May be the terminally assembled subunit of Complex I.^[14] [NDUS5_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[15] [X5BVZ3_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[SAAS:SAAS00061107] [NDUS4_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[16] ^[17] [COX41_BOVIN] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [CY1_HUMAN] This is the heme-containing component of the cytochrome b-c1 complex, which accepts electrons from Rieske protein and transfers electrons to cytochrome c in the mitochondrial respiratory chain. [NDUC1_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[18] [COX5B_BOVIN] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [NDUB9_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[19] [QCR10_HUMAN] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may be closely linked to the iron-sulfur protein in the complex and function as an iron-sulfur protein binding factor. [QCR8_HUMAN] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This subunit, together with cytochrome b, binds to ubiquinone. [NDUS1_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized. [NDUS3_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). [CX6B1_BOVIN] Connects the two COX monomers into the physiological dimeric form. [UCRI_HUMAN] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The transit peptide of the Rieske protein seems to form part of the bc1 complex and is considered to be the subunit 11/IX of that complex. [COX7C_BOVIN] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [CYB_HUMAN] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.[UniProtKB:P00157] [COX1_BOVIN] Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. [NDUA3_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[20] [QCR6_HUMAN] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1. [CX7A1_BOVIN] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [QCR2_HUMAN] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. The core protein 2 is required for the assembly of the complex. [QCR1_HUMAN] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1. [NDUS8_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). May donate electrons to ubiquinone. [NDUA1_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[21] [NDUV1_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). [NDUC2_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[22] [NDUB6_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[23] [NDUBB_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[24] [NDUV2_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). [COX5A_BOVIN] This is the heme A-containing chain of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [NDUB5_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[25] [COX6C_BOVIN] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [NDUB2_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[26] [COX2_BOVIN] Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1. [NDUB3_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[27] [NDUAC_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[28] [ACPM_HUMAN] Carrier of the growing fatty acid chain in fatty acid biosynthesis in mitochondria. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity). [NDUS7_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[29] [NDUA9_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[30] ^[31] [CX6A2_BOVIN] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [COX3_BOVIN] Subunits I, II and III form the functional core of the enzyme complex. [NDUA7_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[32] [NDUB4_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[33] [NDUA6_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[34] [V9JN72_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[RuleBase:RU004419] [NDUB1_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[35] [NDUB7_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[36] [NDUA2_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.

Publication Abstract from PubMed

The respiratory megacomplex represents the highest-order assembly of respiratory chain complexes, and it allows mitochondria to respond to energy-requiring conditions. To understand its architecture, we examined the human respiratory chain megacomplex-I2III2IV2 (MCI2III2IV2) with 140 subunits and a subset of associated cofactors using cryo-electron microscopy. The MCI2III2IV2 forms a circular structure with the dimeric CIII located in the center, where it is surrounded by two copies each of CI and CIV. Two cytochrome c (Cyt.c) molecules are positioned to accept electrons on the surface of the c1 state CIII dimer. Analyses indicate that CII could insert into the gaps between CI and CIV to form a closed ring, which we termed the electron transport chain supercomplex. The structure not only reveals the precise assignment of individual subunits of human CI and CIII, but also enables future in-depth analysis of the electron transport chain as a whole.

Architecture of Human Mitochondrial Respiratory Megacomplex I2III2IV2.,Guo R, Zong S, Wu M, Gu J, Yang M Cell. 2017 Sep 7;170(6):1247-1257.e12. doi: 10.1016/j.cell.2017.07.050. Epub 2017, Aug 24. PMID:28844695^[37]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Angebault C, Charif M, Guegen N, Piro-Megy C, Mousson de Camaret B, Procaccio V, Guichet PO, Hebrard M, Manes G, Leboucq N, Rivier F, Hamel CP, Lenaers G, Roubertie A. Mutation in NDUFA13/GRIM19 leads to early onset hypotonia, dyskinesia and sensorial deficiencies, and mitochondrial complex I instability. Hum Mol Genet. 2015 Jul 15;24(14):3948-55. doi: 10.1093/hmg/ddv133. Epub 2015 Apr, 21. PMID:25901006 doi:https://dx.doi.org/10.1093/hmg/ddv133
↑ Keightley JA, Anitori R, Burton MD, Quan F, Buist NR, Kennaway NG. Mitochondrial encephalomyopathy and complex III deficiency associated with a stop-codon mutation in the cytochrome b gene. Am J Hum Genet. 2000 Dec;67(6):1400-10. Epub 2000 Oct 20. PMID:11047755 doi:https://dx.doi.org/10.1086/316900
↑ Wibrand F, Ravn K, Schwartz M, Rosenberg T, Horn N, Vissing J. Multisystem disorder associated with a missense mutation in the mitochondrial cytochrome b gene. Ann Neurol. 2001 Oct;50(4):540-3. PMID:11601507
↑ Lufei C, Ma J, Huang G, Zhang T, Novotny-Diermayr V, Ong CT, Cao X. GRIM-19, a death-regulatory gene product, suppresses Stat3 activity via functional interaction. EMBO J. 2003 Mar 17;22(6):1325-35. PMID:12628925 doi:https://dx.doi.org/10.1093/emboj/cdg135
↑ Zhang J, Yang J, Roy SK, Tininini S, Hu J, Bromberg JF, Poli V, Stark GR, Kalvakolanu DV. The cell death regulator GRIM-19 is an inhibitor of signal transducer and activator of transcription 3. Proc Natl Acad Sci U S A. 2003 Aug 5;100(16):9342-7. Epub 2003 Jul 16. PMID:12867595 doi:https://dx.doi.org/10.1073/pnas.1633516100
↑ Barnich N, Hisamatsu T, Aguirre JE, Xavier R, Reinecker HC, Podolsky DK. GRIM-19 interacts with nucleotide oligomerization domain 2 and serves as downstream effector of anti-bacterial function in intestinal epithelial cells. J Biol Chem. 2005 May 13;280(19):19021-6. Epub 2005 Mar 7. PMID:15753091 doi:https://dx.doi.org/10.1074/jbc.M413776200
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Murray J, Zhang B, Taylor SW, Oglesbee D, Fahy E, Marusich MF, Ghosh SS, Capaldi RA. The subunit composition of the human NADH dehydrogenase obtained by rapid one-step immunopurification. J Biol Chem. 2003 Apr 18;278(16):13619-22. Epub 2003 Feb 28. PMID:12611891 doi:https://dx.doi.org/10.1074/jbc.C300064200
↑ van den Heuvel L, Ruitenbeek W, Smeets R, Gelman-Kohan Z, Elpeleg O, Loeffen J, Trijbels F, Mariman E, de Bruijn D, Smeitink J. Demonstration of a new pathogenic mutation in human complex I deficiency: a 5-bp duplication in the nuclear gene encoding the 18-kD (AQDQ) subunit. Am J Hum Genet. 1998 Feb;62(2):262-8. PMID:9463323 doi:https://dx.doi.org/10.1086/301716
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Murray J, Zhang B, Taylor SW, Oglesbee D, Fahy E, Marusich MF, Ghosh SS, Capaldi RA. The subunit composition of the human NADH dehydrogenase obtained by rapid one-step immunopurification. J Biol Chem. 2003 Apr 18;278(16):13619-22. Epub 2003 Feb 28. PMID:12611891 doi:https://dx.doi.org/10.1074/jbc.C300064200
↑ van den Bosch BJ, Gerards M, Sluiter W, Stegmann AP, Jongen EL, Hellebrekers DM, Oegema R, Lambrichs EH, Prokisch H, Danhauser K, Schoonderwoerd K, de Coo IF, Smeets HJ. Defective NDUFA9 as a novel cause of neonatally fatal complex I disease. J Med Genet. 2012 Jan;49(1):10-5. doi: 10.1136/jmedgenet-2011-100466. Epub 2011, Nov 23. PMID:22114105 doi:https://dx.doi.org/10.1136/jmedgenet-2011-100466
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754
↑ Guo R, Zong S, Wu M, Gu J, Yang M. Architecture of Human Mitochondrial Respiratory Megacomplex I2III2IV2. Cell. 2017 Sep 7;170(6):1247-1257.e12. doi: 10.1016/j.cell.2017.07.050. Epub 2017, Aug 24. PMID:28844695 doi:https://dx.doi.org/10.1016/j.cell.2017.07.050

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[1] Angebault C, Charif M, Guegen N, Piro-Megy C, Mousson de Camaret B, Procaccio V, Guichet PO, Hebrard M, Manes G, Leboucq N, Rivier F, Hamel CP, Lenaers G, Roubertie A. Mutation in NDUFA13/GRIM19 leads to early onset hypotonia, dyskinesia and sensorial deficiencies, and mitochondrial complex I instability. Hum Mol Genet. 2015 Jul 15;24(14):3948-55. doi: 10.1093/hmg/ddv133. Epub 2015 Apr, 21. PMID:25901006 doi:https://dx.doi.org/10.1093/hmg/ddv133

[2] Keightley JA, Anitori R, Burton MD, Quan F, Buist NR, Kennaway NG. Mitochondrial encephalomyopathy and complex III deficiency associated with a stop-codon mutation in the cytochrome b gene. Am J Hum Genet. 2000 Dec;67(6):1400-10. Epub 2000 Oct 20. PMID:11047755 doi:https://dx.doi.org/10.1086/316900

[3] Wibrand F, Ravn K, Schwartz M, Rosenberg T, Horn N, Vissing J. Multisystem disorder associated with a missense mutation in the mitochondrial cytochrome b gene. Ann Neurol. 2001 Oct;50(4):540-3. PMID:11601507

[4] Lufei C, Ma J, Huang G, Zhang T, Novotny-Diermayr V, Ong CT, Cao X. GRIM-19, a death-regulatory gene product, suppresses Stat3 activity via functional interaction. EMBO J. 2003 Mar 17;22(6):1325-35. PMID:12628925 doi:https://dx.doi.org/10.1093/emboj/cdg135

[5] Zhang J, Yang J, Roy SK, Tininini S, Hu J, Bromberg JF, Poli V, Stark GR, Kalvakolanu DV. The cell death regulator GRIM-19 is an inhibitor of signal transducer and activator of transcription 3. Proc Natl Acad Sci U S A. 2003 Aug 5;100(16):9342-7. Epub 2003 Jul 16. PMID:12867595 doi:https://dx.doi.org/10.1073/pnas.1633516100

[6] Barnich N, Hisamatsu T, Aguirre JE, Xavier R, Reinecker HC, Podolsky DK. GRIM-19 interacts with nucleotide oligomerization domain 2 and serves as downstream effector of anti-bacterial function in intestinal epithelial cells. J Biol Chem. 2005 May 13;280(19):19021-6. Epub 2005 Mar 7. PMID:15753091 doi:https://dx.doi.org/10.1074/jbc.M413776200

[7] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[8] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[9] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[10] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[11] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[12] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[13] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[14] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[15] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[16] Murray J, Zhang B, Taylor SW, Oglesbee D, Fahy E, Marusich MF, Ghosh SS, Capaldi RA. The subunit composition of the human NADH dehydrogenase obtained by rapid one-step immunopurification. J Biol Chem. 2003 Apr 18;278(16):13619-22. Epub 2003 Feb 28. PMID:12611891 doi:https://dx.doi.org/10.1074/jbc.C300064200

[17] van den Heuvel L, Ruitenbeek W, Smeets R, Gelman-Kohan Z, Elpeleg O, Loeffen J, Trijbels F, Mariman E, de Bruijn D, Smeitink J. Demonstration of a new pathogenic mutation in human complex I deficiency: a 5-bp duplication in the nuclear gene encoding the 18-kD (AQDQ) subunit. Am J Hum Genet. 1998 Feb;62(2):262-8. PMID:9463323 doi:https://dx.doi.org/10.1086/301716

[18] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[19] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[20] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[21] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[22] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[23] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[24] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[25] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[26] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[27] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[28] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[29] Murray J, Zhang B, Taylor SW, Oglesbee D, Fahy E, Marusich MF, Ghosh SS, Capaldi RA. The subunit composition of the human NADH dehydrogenase obtained by rapid one-step immunopurification. J Biol Chem. 2003 Apr 18;278(16):13619-22. Epub 2003 Feb 28. PMID:12611891 doi:https://dx.doi.org/10.1074/jbc.C300064200

[30] van den Bosch BJ, Gerards M, Sluiter W, Stegmann AP, Jongen EL, Hellebrekers DM, Oegema R, Lambrichs EH, Prokisch H, Danhauser K, Schoonderwoerd K, de Coo IF, Smeets HJ. Defective NDUFA9 as a novel cause of neonatally fatal complex I disease. J Med Genet. 2012 Jan;49(1):10-5. doi: 10.1136/jmedgenet-2011-100466. Epub 2011, Nov 23. PMID:22114105 doi:https://dx.doi.org/10.1136/jmedgenet-2011-100466

[31] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[32] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[33] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[34] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[35] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[36] Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:https://dx.doi.org/10.1038/nature19754

[37] Guo R, Zong S, Wu M, Gu J, Yang M. Architecture of Human Mitochondrial Respiratory Megacomplex I2III2IV2. Cell. 2017 Sep 7;170(6):1247-1257.e12. doi: 10.1016/j.cell.2017.07.050. Epub 2017, Aug 24. PMID:28844695 doi:https://dx.doi.org/10.1016/j.cell.2017.07.050

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[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

[16]

[17]

[18]

[19]

[20]

[21]

[22]

[23]

[24]

[25]

[26]

[27]

[28]

[29]

[30]

[31]

[32]

[33]

[34]

[35]

[36]

[37]

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