The mitochondrial-encoded subunits of respiratory complex I (NADH:ubiquinone oxidoreductase): identifying residues important in mechanism and disease

Structure of the Hydrophilic Domain of Respiratory Complex I from <i>Thermus thermophilus</i>

Sazanov, L. A., & Hinchliffe, P. (2006) · Science · doi:10.1126/science.1123809 · Cited by 763 · see citing works

The architecture of respiratory complex I

Efremov, R. G., Baradaran, R., & Sazanov, L. A. (2010) · Nature · doi:10.1038/nature09066 · Cited by 616 · see citing works

MITOMAP: a human mitochondrial genome database--2004 update

Brandon, M. (2004) · Nucleic Acids Research · doi:10.1093/nar/gki079 · Cited by 568 · see citing works

Bovine Complex I Is a Complex of 45 Different Subunits

Carroll, J., Fearnley, I. M., Skehel, M. J., Shannon, R. J., Hirst, J., & Walker, J. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607135200 · Cited by 486 · see citing works

The nuclear encoded subunits of complex I from bovine heart mitochondria

Hirst, J., Carroll, J., Fearnley, I. M., Shannon, R. J., & Walker, J. E. (2003) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(03)00059-8 · Cited by 384 · see citing works

Functional Modules and Structural Basis of Conformational Coupling in Mitochondrial Complex I

Hunte, C., Zickermann, V., & Brandt, U. (2010) · Science · doi:10.1126/science.1191046 · Cited by 370 · see citing works

URF6, Last Unidentified Reading Frame of Human mtDNA, Codes for an NADH Dehydrogenase Subunit

Chomyn, A., Cleeter, M. W. J., Ragan, C., Riley, M., Doolittle, R. F., & Attardi, G. M. (1986) · Science · doi:10.1126/science.3764430 · Cited by 348 · see citing works

Mitochondrial introns: a critical view.

Lang, B., Laforest, M., & Burger, G. (2007) · Trends in Genetics · doi:10.1016/j.tig.2007.01.006 · Cited by 334 · see citing works

Transmembrane topology of the NuoL, M and N subunits of NADH:quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters

Mathiesen, C., & Hägerhäll, C. (2002) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(02)00343-2 · Cited by 203 · see citing works

Towards the molecular mechanism of respiratory complex I

Hirst, J. (2009) · Biochemical Journal · doi:10.1042/bj20091382 · Cited by 173 · see citing works

OligoWiz 2.0--integrating sequence feature annotation into the design of microarray probes

Wernersson, R., & Nielsen, H. B. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki399 · Cited by 149 · see citing works

Novel mutations of ND genes in complex I deficiency associated with mitochondrial encephalopathy

Malfatti, E., Bugiani, M., Invernizzi, F., de Souza, C. F. M., Farina, L., Carrara, F., Lamantea, E., Antozzi, C. G., Confalonieri, P. A., Sanseverino, M. T. V., et al. (2007) · Brain · doi:10.1093/brain/awm114 · Cited by 145 · see citing works

Unique domain anchoring of Src to synaptic NMDA receptors via the mitochondrial protein NADH dehydrogenase subunit 2

Gingrich, J. R., Pelkey, K. A., Fam, S. R., Huang, Y., Petralia, R. S., Wenthold, R. J., & Salter, M. W. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401413101 · Cited by 128 · see citing works

Sequence variation in mitochondrial complex I genes: mutation or polymorphism?

Mitchell, A. L., Elson, J. L., Howell, N., et al. (2005) · Journal of Medical Genetics · doi:10.1136/jmg.2005.032474 · Cited by 126 · see citing works

The G13513A mutation in the ND5 gene of mitochondrial DNA as a common cause of MELAS or Leigh syndrome: evidence from 12 cases.

Shanske, S., Çoku, J., Lu, J., et al. (2008) · PubMed · doi:10.1001/archneurol.2007.67 · Cited by 124 · see citing works

Conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH:ubiquinone oxidoreductase (Complex I)

Euro, L., Belevich, G., Verkhovsky, M. I., Wikström, M. K. F., & Verkhovskaya, M. L. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.06.001 · Cited by 106 · see citing works

A novel recurrent mitochondrial DNA mutation in ND3 gene is associated with isolated complex I deficiency causing Leigh syndrome and dystonia

Sarzi, E., Brown, M. D., Lebon, S., Chrétien, D., Münnich, A., Rötig, A., & Procaccio, V. (2006) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.31565 · Cited by 104 · see citing works

Identification of novel mutations in five patients with mitochondrial encephalomyopathy

Valente, L., Piga, D., Lamantea, E., Carrara, F., Uziel, G., Cudia, P., Zani, A., Farina, L., Morandi, L. O., Mora, M., et al. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.10.001 · Cited by 102 · see citing works

The Membrane Subunit NuoL(ND5) Is Involved in the Indirect Proton Pumping Mechanism of Escherichia coli Complex I

Nakamaru‐Ogiso, E., Kao, M., Chen, H., Sinha, S. C., Yagi, T., & Ohnishi, T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.157826 · Cited by 93 · see citing works

Characterization of the NuoM (ND4) Subunit in Escherichia coli NDH-1

Torres‐Bacete, J., Nakamaru‐Ogiso, E., Matsuno‐Yagi, A., & Yagi, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707855200 · Cited by 92 · see citing works

Mutagenesis of Subunit N of theEscherichia coliComplex I. Identification of the Initiation Codon and the Sensitivity of Mutants to Decylubiquinone

Amarneh, B., & Vik, S. B. (2003) · Biochemistry · doi:10.1021/bi0340346 · Cited by 84 · see citing works

Mutated ND2 impairs mitochondrial complex I assembly and leads to Leigh Syndrome

Ugalde, C., Hinttala, R., Timal, S., Smeets, R., Rodenburg, R. J., Uusimaa, J., van den Heuvel, L. P., Nijtmans, L. G. J., Majamaa, K., & Smeitink, J. A. M. (2006) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2006.08.003 · Cited by 82 · see citing works

A new mitochondrial DNA mutation at 14577 T/C is probably a major pathogenic mutation for maternally inherited type 2 diabetes.

Tawata, M., Hayashi, J. I., Isobe, K., Ohkubo, E., Ohtaka, M., Chen, J., Aida, K., & Onaya, T. (2000) · Diabetes · doi:10.2337/diabetes.49.7.1269 · Cited by 69 · see citing works

Critical Roles of Subunit NuoH (ND1) in the Assembly of Peripheral Subunits with the Membrane Domain of Escherichia coli NDH-1

Sinha, P. K., Torres‐Bacete, J., Nakamaru‐Ogiso, E., Castro‐Guerrero, N. A., Matsuno‐Yagi, A., & Yagi, T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809468200 · Cited by 65 · see citing works

Characterization of the Membrane Domain Subunit NuoK (ND4L) of the NADH-Quinone Oxidoreductase fromEscherichia coli,

Kao, M., Nakamaru‐Ogiso, E., Matsuno‐Yagi, A., et al. (2005) · Biochemistry · doi:10.1021/bi050708w · Cited by 64 · see citing works

Species-specific and Mutant MWFE Proteins

Yadava, N., Potluri, P., Smith, E. N., Bisevac, A., & Scheffler, I. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202016200 · Cited by 64 · see citing works

Functional Roles of Four Conserved Charged Residues in the Membrane Domain Subunit NuoA of the Proton-translocating NADH-Quinone Oxidoreductase from Escherichia coli

Kao, M., Bernardo, S. D., Perego, M., Nakamaru‐Ogiso, E., Matsuno‐Yagi, A., & Yagi, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403885200 · Cited by 60 · see citing works

Identification of membrane proteins by tandem mass spectrometry of protein ions

Carroll, J., Altman, M. C., Fearnley, I., & Walker, J. (2007) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0706817104 · Cited by 60 · see citing works

Characterization of the Membrane Domain Subunit NuoJ (ND6) of the NADH-Quinone Oxidoreductase fromEscherichia coliby Chromosomal DNA Manipulation

Kao, M., Bernardo, S. D., Nakamaru‐Ogiso, E., et al. (2005) · Biochemistry · doi:10.1021/bi0476477 · Cited by 59 · see citing works

Analysis of the Pathogenic Human Mitochondrial Mutation ND1/3460, and Mutations of Strictly Conserved Residues in Its Vicinity, Using the Bacterium Paracoccus denitrificans

Zickermann, V., Barquera, B., Wikström, M. K. F., et al. (1998) · Biochemistry · doi:10.1021/bi9810555 · Cited by 55 · see citing works

A Pair of Membrane-Embedded Acidic Residues in the NuoK Subunit of Escherichia coli NDH-1, a Counterpart of the ND4L Subunit of the Mitochondrial Complex I, Are Required for High Ubiquinone Reductase Activity

Kervinen, M., Pätsi, J., Finel, M., et al. (2003) · Biochemistry · doi:10.1021/bi0355903 · Cited by 55 · see citing works

The C-terminally Truncated NuoL Subunit (ND5 Homologue) of the Na+-dependent Complex I from Escherichia coli Transports Na+

Steuber, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301682200 · Cited by 54 · see citing works

Single particle analysis confirms distal location of subunits NuoL and NuoM in Escherichia coli complex I

Baranova, E. A., Morgan, D. J., & Sazanov, L. A. (2007) · Journal of Structural Biology · doi:10.1016/j.jsb.2007.01.009 · Cited by 54 · see citing works

ND3 and ND4L Subunits of Mitochondrial Complex I, Both Nucleus Encoded in Chlamydomonas reinhardtii , Are Required for Activity and Assembly of the Enzyme

Cardol, P., Lapaille, M., Minet, P., et al. (2006) · Eukaryotic Cell · doi:10.1128/ec.00118-06 · Cited by 50 · see citing works

Mutagenesis of Three Conserved Glu Residues in a Bacterial Homologue of the ND1 Subunit of Complex I Affects Ubiquinone Reduction Kinetics but Not Inhibition by Dicyclohexylcarbodiimide

Kurki, S., Zickermann, V., Kervinen, M., et al. (2000) · Biochemistry · doi:10.1021/bi001134s · Cited by 49 · see citing works

Truncation of subunit ND2 disrupts the threefold symmetry of the antiporter‐like subunits in complex I from higher metazoans

Birrell, J. A., & Hirst, J. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.09.017 · Cited by 43 · see citing works

Transmembrane orientation and topology of the NADH:quinone oxidoreductase putative quinone binding subunit NuoH

Roth, R. G., & Hägerhäll, C. (2001) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00265-6 · Cited by 39 · see citing works

The MELAS mutations 3946 and 3949 perturb the critical structure in a conserved loop of the ND1 subunit of mitochondrial complex I

Kervinen, M., Hinttala, R., Helander, H. M., Kurki, S., Uusimaa, J., Finel, M., Majamaa, K., & Hassinen, I. E. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl176 · Cited by 39 · see citing works

Features of Subunit NuoM (ND4) in Escherichia coli NDH-1

Torres‐Bacete, J., Sinha, P. K., Castro‐Guerrero, N. A., Matsuno‐Yagi, A., & Yagi, T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.059154 · Cited by 37 · see citing works

Leber hereditary optic neuropathy mutations in the ND6 subunit of mitochondrial complex I affect ubiquinone reduction kinetics in a bacterial model of the enzyme

Pätsi, J., Kervinen, M., Finel, M., & Hassinen, I. E. (2007) · Biochemical Journal · doi:10.1042/bj20070866 · Cited by 36 · see citing works

Mitochondrial complex I activity is significantly decreased in a patient with maternally inherited type 2 diabetes mellitus and hypertrophic cardiomyopathy associated with mitochondrial DNA C3310T mutation: A cybrid study

Chen, J., Hattori, Y., Nakajima, K., Eizawa, T., Ehara, T., Koyama, M., Hirai, T., Fukuda, Y., Kinoshita, M., Sugiyama, A., et al. (2006) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2006.03.024 · Cited by 29 · see citing works

Characterization and Topology of the Membrane Domain Nqo10 Subunit of the Proton-Translocating NADH-Quinone Oxidoreductase of Paracoccus denitrificans

Kao, M., Bernardo, S. D., Matsuno‐Yagi, A., et al. (2003) · Biochemistry · doi:10.1021/bi034166z · Cited by 27 · see citing works

Exploring the Membrane Domain of the Reduced Nicotinamide Adenine Dinucleotide−Quinone Oxidoreductase of Paracoccus denitrificans: Characterization of the NQO7 Subunit

Bernardo, S. D., Yano, T., & Yagi, T. (2000) · Biochemistry · doi:10.1021/bi0006619 · Cited by 25 · see citing works

A Patient with Type 2 Diabetes Mellitus Associated with Mutations in Calcium Sensing Receptor Gene and Mitochondrial DNA

Ohkubo, E., Aida, K., Chen, J., Hayashi, J., Isobe, K., Tawata, M., & Onaya, T. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3867 · Cited by 23 · see citing works

Characterization of the Membrane Domain Nqo11 Subunit of the Proton-Translocating NADH-Quinone Oxidoreductase of Paracoccus denitrificans

Kao, M., Bernardo, S. D., Matsuno‐Yagi, A., et al. (2002) · Biochemistry · doi:10.1021/bi025525d · Cited by 15 · see citing works

Untitled work

(1996) · doi:10.1002/(sici)1098-1004(1996)7:4

Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I

Chouchani, E. T., Methner, C., Nadtochiy, S. M., Logan, A., Pell, V. R., Ding, S., James, A. M., Cochemé, H. M., Reinhold, J., Lilley, K. S., et al. (2013) · Nature Medicine · doi:10.1038/nm.3212 · Cited by 619 · see citing works

Correlation in species, cofactor, oligomerization and substrate specificity in short‐chain oxidoreductase enzymes

Huether, R., & Duax, W. L. (2010) · The FASEB Journal · doi:10.1096/fasebj.24.1_supplement.lb163

Oxidoreductase mimicking activity of Ru(edta) complexes in conversion of NAD coenzymes

Chrzanowska, M., Katafias, A., van Eldik, R., et al. (2022) · Polyhedron · doi:10.1016/j.poly.2022.115872 · Cited by 4 · see citing works

[Strategy to solve cofactor issues in oxidoreductase catalyzed biocatalytic applications].

Jiang, J., Wu, X., & Chen, Y. (2012) · PubMed · Cited by 2 · see citing works

Cofactor requirements of microsomal 3β-hydroxy-steroid oxidoreductase, 5-ene-isomerase from human placenta

Weidenfeld, J., Ben-Uzilio, R., & Ne'eman, Y. (1975) · Journal of Steroid Biochemistry · doi:10.1016/0022-4731(75)90113-2 · Cited by 5 · see citing works

Human mitochondrial respiratory chain deficiencies.

Morgan-Hughes, J. A., Schapira, A. H. V., Jm, C., et al. (1988) · PubMed