The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus
Abstract
Respiratory complex I plays a central role in cellular energy production in bacteria and mitochondria. Its dysfunction is implicated in many human neurodegenerative diseases, as well as in aging. The crystal structure of the hydrophilic domain (peripheral arm) of complex I from Thermus thermophilus has been solved at 3.3 angstrom resolution. This subcomplex consists of eight subunits and contains all the redox centers of the enzyme, including nine iron-sulfur clusters. The primary electron acceptor, flavin-mononucleotide, is within electron transfer distance of cluster N3, leading to the main redox pathway, and of the distal cluster N1a, a possible antioxidant. The structure reveals new aspects of the mechanism and evolution of the enzyme. The terminal cluster N2 is coordinated, uniquely, by two consecutive cysteines. The novel subunit Nqo15 has a similar fold to the mitochondrial iron chaperone frataxin, and it may be involved in iron-sulfur cluster regeneration in the complex.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“We modeled the location of ND3 Cys39 using structures of prokaryotic complex I (refs. 32–34). This modeling led to an orthologous mammalian core structure containing ND3 Cys39 (Fig. 3f,g and Supplementary Figs. 14 and 15).”
From Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I (2013) · cites this paper as [32]
Citations
Cites
Murzin, A. G., Brenner, S. E., Hubbard, T., & Chothia, C. (1995) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80134-2 · Cited by 6,435
Mitochondria, Oxidants, and Aging
Balaban, R. S., Nemoto, S., & Finkel, T. (2005) · Cell · doi:10.1016/j.cell.2005.02.001 · Cited by 4,388
Krissinel, E., & Henrick, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904026460 · Cited by 3,788
Peters, J. W. (1998) · Science · doi:10.1126/science.282.5395.1853 · Cited by 1,891
Natural engineering principles of electron tunnelling in biological oxidation–reduction
Page, C. C., Moser, C. C., Chen, X., & Dutton, P. L. (1999) · Nature · doi:10.1038/46972 · Cited by 1,866
Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas
Volbeda, A., Charon, M., Piras, C., Hatchikian, E. C., Frey, M., & Fontecilla-Camps, J. C. (1995) · Nature · doi:10.1038/373580a0 · Cited by 1,573
Holm, L., & Sander, C. (1996) · Science · doi:10.1126/science.273.5275.595 · Cited by 1,497
Classification and phylogeny of hydrogenases
Vignais, P. M., Billoud, B., & Meyer, J. (2001) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2001.tb00587.x · Cited by 1,209
The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains
Walker, J. E. (1992) · Quarterly Reviews of Biophysics · doi:10.1017/s003358350000425x · Cited by 777
Characterization of Superoxide-producing Sites in Isolated Brain Mitochondria
Kudin, A. P., Bimpong‐Buta, N., Vielhaber, S., Elger, C. E., & Kunz, W. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310341200 · Cited by 514
Flagged first, then by citations
Research works printed but not linked: 1
- 10.1016/S0168-6445(01)00063-8 · DOI
Cited by
Sorted by citations
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207
Lubitz, W., Ogata, H., Rüdiger, O., & Reijerse, E. J. (2014) · Chemical Reviews · doi:10.1021/cr4005814 · Cited by 2,067
The mononuclear molybdenum enzymes
Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738
Occurrence, Classification, and Biological Function of Hydrogenases: An Overview
Vignais, P. M., & Billoud, B. (2007) · Chemical Reviews · doi:10.1021/cr050196r · Cited by 1,617
Mitochondrial electron transport chain, ROS generation and uncoupling (Review)
Zhao, R., Jiang, S., Zhang, L., & Yu, Z. (2019) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2019.4188 · Cited by 1,511
Structure/Function Relationships of [NiFe]- and [FeFe]-Hydrogenases
Fontecilla-Camps, J. C., Volbeda, A., Cavazza, C., & Nicolet, Y. (2007) · Chemical Reviews · doi:10.1021/cr050195z · Cited by 1,365
Brand, M. D. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.001 · Cited by 1,063
The assembly, regulation and function of the mitochondrial respiratory chain
Vercellino, I., & Sazanov, L. A. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00415-0 · Cited by 1,015
Self-citationMetalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers
Liu, J., Chakraborty, S., Hosseinzadeh, P., Yu, Y., Tian, S., Petrik, I. D., Bhagi, A., & Lu, Y. (2014) · Chemical Reviews · doi:10.1021/cr400479b · Cited by 905
Crystal structure of the entire respiratory complex I
Baradaran, R., Berrisford, J. M., Minhas, G. S., & Sazanov, L. A. (2013) · Nature · doi:10.1038/nature11871 · Cited by 797
Self-citationDirect Electrochemistry of Redox Enzymes as a Tool for Mechanistic Studies
Léger, C., & Bertrand, P. (2008) · Chemical Reviews · doi:10.1021/cr0680742 · Cited by 802
Hirst, J. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-070511-103700 · Cited by 779
Kußmaul, L., & Hirst, J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510977103 · Cited by 745
Microbial Ecology of the Dark Ocean above, at, and below the Seafloor
Orcutt, B. N., Sylvan, J. B., Knab, N. J., & Edwards, K. J. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00039-10 · Cited by 692
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
The architecture of respiratory complex I
Efremov, R. G., Baradaran, R., & Sazanov, L. A. (2010) · Nature · doi:10.1038/nature09066 · Cited by 634
Self-citationCardiac Mitochondria and Reactive Oxygen Species Generation
Chen, Y., & Zweier, J. L. (2014) · Circulation Research · doi:10.1161/circresaha.114.300559 · Cited by 618
Maturation of Iron-Sulfur Proteins in Eukaryotes: Mechanisms, Connected Processes, and Diseases
Lill, R., & Mühlenhoff, U. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052705.162653 · Cited by 605
How to make a living from anaerobic ammonium oxidation
Kartal, B., de Almeida, N. M., Maalcke, W. J., den Camp, H. J. M. O., Jetten, M. S. M., & Keltjens, J. T. (2012) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12014 · Cited by 602
Structure of mammalian respiratory complex I
Zhu, J., Vinothkumar, K. R., & Hirst, J. (2016) · Nature · doi:10.1038/nature19095 · Cited by 587
Reversible interconversion of carbon dioxide and formate by an electroactive enzyme
Reda, T., Plugge, C. M., Abram, N. J., & Hirst, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801290105 · Cited by 561
A giant molecular proton pump: structure and mechanism of respiratory complex I
Sazanov, L. A. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3997 · Cited by 579
Self-citationMolecular Mechanisms of Superoxide Production by the Mitochondrial Respiratory Chain
Dröse, S., & Brandt, U. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3573-0_6 · Cited by 537
Atomic structure of the entire mammalian mitochondrial complex I
Fiedorczuk, K., Letts, J. A., Degliesposti, G., Kaszuba, K., Skehel, M. J., & Sazanov, L. A. (2016) · Nature · doi:10.1038/nature19794 · Cited by 527
Self-citationThe architecture of respiratory supercomplexes
Letts, J. A., Fiedorczuk, K., & Sazanov, L. A. (2016) · Nature · doi:10.1038/nature19774 · Cited by 490
Self-citationLacey, A. L. D., Fernández, V. M., Rousset, M., & Cammack, R. (2007) · Chemical Reviews · doi:10.1021/cr0501947 · Cited by 465
Denitrification and aerobic respiration, hybrid electron transport chains and co-evolution
Chen, J., & Strous, M. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.10.002 · Cited by 468
Mitochondrial respiratory complex I: Structure, function and implication in human diseases
Sharma, L., Lu, J., & Bai, Y. (2009) · Current Medicinal Chemistry · doi:10.2174/092986709787846578 · Cited by 438
Understanding mitochondrial complex I assembly in health and disease
Mimaki, M., Wang, X., McKenzie, M., Thorburn, D. R., & Ryan, M. T. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2011.08.010 · Cited by 420
Mitochondria and Iron: current questions
Paul, B. T., Manz, D. H., Torti, F. M., & Torti, S. V. (2016) · Expert Review of Hematology · doi:10.1080/17474086.2016.1268047 · Cited by 445
Maranzana, E., Barbero, G., Falasca, A. I., Lenaz, G., & Genova, M. L. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4845 · Cited by 445
Mitochondrial iron–sulfur clusters: Structure, function, and an emerging role in vascular biology
Read, A. D., Bentley, R. E. T., Archer, S. L., & Dunham‐Snary, K. J. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102164 · Cited by 440
Architecture of mammalian respiratory complex I
Vinothkumar, K. R., Zhu, J., & Hirst, J. (2014) · Nature · doi:10.1038/nature13686 · Cited by 419
Mammalian Mitochondrial Complex I: Biogenesis, Regulation, and Reactive Oxygen Species Generation
Koopman, W. J. H., Nijtmans, L. G. J., Dieteren, C. E. J., Roestenberg, P., Valsecchi, F., Smeitink, J. A. M., & Willems, P. H. G. M. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2743 · Cited by 411
Structure of Mammalian Respiratory Supercomplex I 1 III 2 IV 1
Wu, M., Gu, J., Guo, R., Huang, Y., & Yang, M. (2016) · Cell · doi:10.1016/j.cell.2016.11.012 · Cited by 399
Generation of superoxide by the mitochondrial Complex I
Grivennikova, V. G., & Vinogradov, A. D. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.03.013 · Cited by 379
Structure of the membrane domain of respiratory complex I
Efremov, R. G., & Sazanov, L. A. (2011) · Nature · doi:10.1038/nature10330 · Cited by 370
Self-citationFunctional 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
The architecture of the mammalian respirasome
Gu, J., Wu, M., Guo, R., Yan, K., Lei, J., Gao, N., & Yang, M. (2016) · Nature · doi:10.1038/nature19359 · Cited by 372
Flavin-based Electron bifurcation, a new mechanism of biological energy coupling
Buckel, W., & Thauer, R. K. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00707 · Cited by 369
Mitochondrial function in hypoxic ischemic injury and influence of aging
Ham, P. B., & Raju, R. P. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.06.006 · Cited by 374
Why Do We Still Have a Maternally Inherited Mitochondrial DNA? Insights from Evolutionary Medicine
Wallace, D. C. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.081205.150955 · Cited by 372
Morais, V. A., Haddad, D., Craessaerts, K., Bock, P. D., Swerts, J., Vilain, S., Aerts, L., Overbergh, L., Grünewald, A., Seibler, P., et al. (2014) · Science · doi:10.1126/science.1249161 · Cited by 373
Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1
Althoff, T., Mills, D. J., Popot, J., & Kühlbrandt, W. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.324 · Cited by 334
Structure and function of mitochondrial complex I
Wirth, C., Brandt, U., Hunte, C., & Zickermann, V. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.02.013 · Cited by 346
Complex I deficiency: clinical features, biochemistry and molecular genetics
Fassone, E., & Rahman, S. (2012) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2012-101159 · Cited by 325
Glutathione—a review on its role and significance in Parkinson's disease
Martin, H. L., & Teismann, P. (2009) · The FASEB Journal · doi:10.1096/fj.08-125443 · Cited by 320
Electron Flow through Metalloproteins
Winkler, J. R., & Gray, H. B. (2013) · Chemical Reviews · doi:10.1021/cr4004715 · Cited by 317
The production of reactive oxygen species by complex I
Hirst, J., King, M. S., & Pryde, K. R. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360976 · Cited by 312
Proton-Coupled Electron Flow in Protein Redox Machines
Dempsey, J. L., Winkler, J. R., & Gray, H. B. (2010) · Chemical Reviews · doi:10.1021/cr100182b · Cited by 300
Mitochondrial Management of Reactive Oxygen Species
Napolitano, G., Fasciolo, G., & Venditti, P. (2021) · Antioxidants · doi:10.3390/antiox10111824 · Cited by 305
Bioenergetics and anaerobic respiratory chains of aceticlastic methanogens
Welte, C. U., & Deppenmeier, U. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.12.002 · Cited by 290
The Oxidative Phosphorylation System in Mammalian Mitochondria
Papa, S., Martino, P. L., Capitanio, G., Gaballo, A., Rasmo, D. D., Signorile, A., & Petruzzella, V. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2869-1_1 · Cited by 303
Mitochondrial complex I: structure, function and pathology
Janssen, R. J. R. J., Nijtmans, L. G., Heuvel, L. P. V. D., & Smeitink, J. A. M. (2006) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-006-0362-4 · Cited by 276
Lücker, S., Nowka, B., Rattei, T., Spieck, E., & Daims, H. (2013) · Frontiers in Microbiology · doi:10.3389/fmicb.2013.00027 · Cited by 274
The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum )
Pierce, E., Xie, G. G., Barabote, R. D., Saunders, E. H., Han, C. S., Detter, J. C., Richardson, P., Brettin, T. S., Das, A., Ljungdahl, L. G., et al. (2008) · Environmental Microbiology · doi:10.1111/j.1462-2920.2008.01679.x · Cited by 267
Iron–sulfur protein folds, iron–sulfur chemistry, and evolution
Meyer, J. (2007) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-007-0318-7 · Cited by 277
Regulation of mitochondrial oxidative phosphorylation through cell signaling
Hüttemann, M., Lee, I., Samavati, L., Yu, H., & Doan, J. W. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.10.001 · Cited by 277
A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase
Goris, T., Wait, A. F., Saggu, M., Fritsch, J., Heidary, N., Stein, M., Zebger, I., Lendzian, F., Armstrong, F. A., Friedrich, B., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.555 · Cited by 262
James, A. M., Sharpley, M. S., Manas, A.-R. B., Frerman, F. E., Hirst, J., Smith, R. A. J., & Murphy, M. P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611463200 · Cited by 262
Metagenome and mRNA expression analyses of anaerobic methanotrophic archaea of the ANME‐1 group
Meyerdierks, A., Kube, M., Kostadinov, I., Teeling, H., Glöckner, F. O., Reinhardt, R., & Amann, R. (2009) · Environmental Microbiology · doi:10.1111/j.1462-2920.2009.02083.x · Cited by 265
Mechanisms and Evolution of Oxidative Sulfur Metabolism in Green Sulfur Bacteria
Gregersen, L. H., Bryant, D. A., & Frigaard, N. (2011) · Frontiers in Microbiology · doi:10.3389/fmicb.2011.00116 · Cited by 258
New Perspectives on Proton Pumping in Cellular Respiration
Wikström, M. K. F., Sharma, V., Kaila, V. R. I., Hosler, J. P., & Hummer, G. (2015) · Chemical Reviews · doi:10.1021/cr500448t · Cited by 262
[NiFe] hydrogenases: A common active site for hydrogen metabolism under diverse conditions
Shafaat, H. S., Rüdiger, O., Ogata, H., & Lubitz, W. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.01.015 · Cited by 257
Analysis of the Assembly Profiles for Mitochondrial- and Nuclear-DNA-Encoded Subunits into Complex I
Lazarou, M., McKenzie, M., Ohtake, A., Thorburn, D. R., & Ryan, M. T. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00074-07 · Cited by 254
OXPHOS mutations and neurodegeneration
Koopman, W. J. H., Distelmaier, F., Smeitink, J. A. M., & Willems, P. H. G. M. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.300 · Cited by 270
Structural Basis for the Mechanism of Respiratory Complex I
Berrisford, J. M., & Sazanov, L. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.032144 · Cited by 253
Self-citationThe pathogenesis of Friedreich ataxia and the structure and function of frataxin
Pandolfo, M., & Pastore, A. (2009) · Journal of Neurology · doi:10.1007/s00415-009-1003-2 · Cited by 242
[FeFe] hydrogenases and their evolution: a genomic perspective
Meyer, J. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-6477-4 · Cited by 251
Hüttemann, M., Lee, I., Pecinová, A., Pecina, P., Przyklenk, K., & Doan, J. W. (2008) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-008-9169-3 · Cited by 241
Mitochondrial Respiratory Chain Complexes
Sousa, J. S., D’Imprima, E., & Vonck, J. (2018) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-981-10-7757-9_7 · Cited by 263
The mitochondrial respiratory chain
Rich, P. R., & Maréchal, A. (2010) · Essays in Biochemistry · doi:10.1042/bse0470001 · Cited by 237
Cyanobacterial NDH-1 complexes: Novel insights and remaining puzzles
Battchikova, N., Eisenhut, M., & Aro, E. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.10.017 · Cited by 246
Differential effects of mitochondrial Complex I inhibitors on production of reactive oxygen species
Fato, R., Bergamini, C., Bortolus, M., Maniero, A. L., Leoni, S., Ohnishi, T., & Lenaz, G. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.11.003 · Cited by 238
Electron flow through metalloproteins
Gray, H. B., & Winkler, J. R. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.05.001 · Cited by 232
Sazanov, L. A. (2007) · Biochemistry · doi:10.1021/bi602508x · Cited by 247
Self-citationHarvest and utilization of chemical energy in wastes by microbial fuel cells
Sun, M., Zhai, L., Li, W., & Yu, H. (2016) · Chemical Society Reviews · doi:10.1039/c5cs00903k · Cited by 231
Cryo-EM structures of complex I from mouse heart mitochondria in two biochemically defined states
Agip, A.-N. A., Blaza, J. N., Bridges, H. R., Viscomi, C. F., Rawson, S., Muench, S. P., & Hirst, J. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0073-1 · Cited by 223
The prokaryotic complex iron–sulfur molybdoenzyme family
Rothery, R. A., Workun, G. J., & Weiner, J. H. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.09.002 · Cited by 228
Supramolecular Structure of the Mitochondrial Oxidative Phosphorylation System
Boekema, E. J., & Braun, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.r600031200 · Cited by 224
Yamamoto, H., Peng, L., Fukao, Y., & Shikanai, T. (2011) · The Plant Cell · doi:10.1105/tpc.110.080291 · Cited by 223
Structure and function of mitochondrial supercomplexes
Dudkina, N. V., Kouřil, R., Peters, K., Braun, H., & Boekema, E. J. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.12.013 · Cited by 218
Maio, N., & Rouault, T. A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.09.009 · Cited by 222
Zhang, Z., Huang, Q., Zhao, D., Lian, F., Li, X., & Qi, W. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1112363 · Cited by 236
Assembly of mitochondrial complex I and defects in disease
Lazarou, M., Thorburn, D. R., Ryan, M. T., & McKenzie, M. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.04.015 · Cited by 217
Electron tunneling chains of mitochondria
Moser, C. C., Farid, T. A., Chobot, S. E., & Dutton, P. L. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.04.015 · Cited by 205
Zhang, J., Frerman, F. E., & Kim, J. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604567103 · Cited by 207
Human Ind1, an Iron-Sulfur Cluster Assembly Factor for Respiratory Complex I
Sheftel, A. D., Stehling, O., Pierik, A. J., Netz, D. J. A., Kerscher, S., Elsässer, H., Wittig, I., Balk, J., Brandt, U., & Lill, R. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00817-09 · Cited by 211
Structures of membrane proteins
Vinothkumar, K. R., & Henderson, R. A. (2010) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583510000041 · Cited by 205
Thermus thermophilus as biological model
Cava, F., Hidalgo, A., & Berenguer, J. (2009) · Extremophiles · doi:10.1007/s00792-009-0226-6 · Cited by 202
The role of iron in mitochondrial function
Levi, S., & Rovida, E. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.09.008 · Cited by 202
Unifying concepts in anaerobic respiration: Insights from dissimilatory sulfur metabolism
Grein, F., Ramos, A. R., Venceslau, S. S., & Pereira, I. A. C. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.09.001 · Cited by 200
Friedreich Ataxia: Molecular Mechanisms, Redox Considerations, and Therapeutic Opportunities
Santos, R., Lefevre, S. D., Sliwa, D., Seguin, A., Camadro, J., & Lesuisse, E. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3015 · Cited by 197
Protein co‐evolution, co‐adaptation and interactions
Pazos, F., & Valencia, A. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.189 · Cited by 191
Frataxin: a protein in search for a function
Pastore, A., & Puccio, H. M. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12220 · Cited by 191
Oliveira, T. F., Vonrhein, C., Matias, P. M., Venceslau, S. S., Pereira, I. A. C., & Archer, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805643200 · Cited by 190
Internal Architecture of Mitochondrial Complex I from Arabidopsis thaliana
Senkler, J., Sunderhaus, S., Nimtz, M., Jänsch, L., & Braun, H. (2010) · The Plant Cell · doi:10.1105/tpc.109.073726 · Cited by 187
Mechanisms of mitochondrial diseases
Ylikallio, E., & Suomalainen, A. (2011) · Annals of Medicine · doi:10.3109/07853890.2011.598547 · Cited by 197
Structure and biogenesis of the chloroplast NAD(P)H dehydrogenase complex
Peng, L., Yamamoto, H., & Shikanai, T. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.10.015 · Cited by 184
Hurd, T. R., Requejo, R., Filipovska, A., Brown, S., Prime, T. A., Robinson, A. J., Fearnley, I. M., & Murphy, M. P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803432200 · Cited by 182
Metadata
- Authors
- Sazanov, L. A., & Hinchliffe, P.
- Affiliations
- MRC Mitochondrial Biology Unit (GB)
- Corresponding author
- Sazanov, Leonid A.
- Venue
- Science
- Published
- 2006-03-10
- Volume
- 311
- Issue
- 5766
- Pages
- 1430-1436
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1983737836
- Cited by
- 763
- References
- 49
- Citations by year
- 2026: 7 · 2025: 15 · 2024: 28 · 2023: 14 · 2022: 20 · 2021: 22 · 2020: 26 · 2019: 24 · 2018: 29 · 2017: 28 · 2016: 35 · 2015: 34 · 2014: 41 · 2013: 51 · 2012: 60
- FWCI
- 40.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- mitochondrial complex I, NADH dehydrogenase, Thermus thermophilus, hydrophilic domains, iron-sulfur clusters, flavin mononucleotide, electron transfer, frataxin, crystal structure, enzyme evolution
- MeSH terms
- Frataxin, Animals, Bacterial Proteins, Binding Sites, Oxidation-Reduction, Protein Conformation, Thermus thermophilus, Protein Structure, Tertiary, Protein Folding, Crystallography, X-Ray, Protein Subunits, Iron-Binding Proteins, Electron Transport Complex I
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
