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1

Schägger, Hermann. "Respiratory Chain Supercomplexes." IUBMB Life (International Union of Biochemistry and Molecular Biology: Life) 52, no. 3-5 (2001): 119–28. http://dx.doi.org/10.1080/15216540152845911.

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2

Ameyama, Minoru, Kazunobu Matsushita, Emiko Shinagawa, and Osao Adachi. "Sugar-oxidizing Respiratory Chain ofGluconobacter suboxydans. Evidence for a Branched Respiratory Chain and Characterization of Respiratory Chain-Linked Cytochromes." Agricultural and Biological Chemistry 51, no. 11 (1987): 2943–50. http://dx.doi.org/10.1080/00021369.1987.10868527.

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3

DiMauro, Salvatore, and Eric A. Schon. "Mitochondrial Respiratory-Chain Diseases." New England Journal of Medicine 348, no. 26 (2003): 2656–68. http://dx.doi.org/10.1056/nejmra022567.

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4

Rich, Peter R., and Amandine Maréchal. "The mitochondrial respiratory chain." Essays in Biochemistry 47 (June 14, 2010): 1–23. http://dx.doi.org/10.1042/bse0470001.

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Abstract (sommario):
In the present chapter, the structures and mechanisms of the major components of mammalian mitochondrial respiratory chains are reviewed. Particular emphasis is placed on the four protein complexes and their cofactors that catalyse the electron transfer pathway between oxidation of NADH and succinate and the reduction of oxygen to water. Current ideas are reviewed of how these electron transfer reactions are coupled to formation of the proton and charge gradient across the inner mitochondrial membrane that is used to drive ATP synthesis. Additional respiratory components that are found in mamm
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5

AMEYAMA, Minoru, Kazunobu MATSUSHITA, Emiko SHINAGAWA, and Osao ADACHI. "Sugar-oxidizing respiratory chain of Gluconobacter suboxydans. Evidence for a branched respiratory chain and characterization of respiratory chain-linked cytochromes." Agricultural and Biological Chemistry 51, no. 11 (1987): 2943–50. http://dx.doi.org/10.1271/bbb1961.51.2943.

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6

MBBS, Joannie Hui, Denise M. Kirby, David R. Thorburn, and A. vihu Boneh. "Decreased activities of mitochondrial respiratory chain complexes in non-mitochondrial respiratory chain diseases." Developmental Medicine & Child Neurology 48, no. 2 (2006): 132–36. http://dx.doi.org/10.1017/s0012162206000284.

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7

Meuric, Vincent, Astrid Rouillon, Fatiha Chandad, and Martine Bonnaure-Mallet. "Putative respiratory chain ofPorphyromonas gingivalis." Future Microbiology 5, no. 5 (2010): 717–34. http://dx.doi.org/10.2217/fmb.10.32.

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8

Shoubridge, Eric A. "Supersizing the Mitochondrial Respiratory Chain." Cell Metabolism 15, no. 3 (2012): 271–72. http://dx.doi.org/10.1016/j.cmet.2012.02.009.

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9

Pfeiffer, Kathy, Vishal Gohil, Rosemary A. Stuart, et al. "Cardiolipin Stabilizes Respiratory Chain Supercomplexes." Journal of Biological Chemistry 278, no. 52 (2003): 52873–80. http://dx.doi.org/10.1074/jbc.m308366200.

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10

Zhang, Mei, Eugenia Mileykovskaya, and William Dowhan. "Gluing the Respiratory Chain Together." Journal of Biological Chemistry 277, no. 46 (2002): 43553–56. http://dx.doi.org/10.1074/jbc.c200551200.

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11

Guenthard, J., F. Wyler, B. Fowler, and R. Baumgartner. "Cardiomyopathy in respiratory chain disorders." Archives of Disease in Childhood 72, no. 3 (1995): 223–26. http://dx.doi.org/10.1136/adc.72.3.223.

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12

Triepels, R. H., L. P. Van Den Heuvel, J. M. Trijbels, and J. A. Smeitink. "Respiratory chain complex I deficiency." American Journal of Medical Genetics 106, no. 1 (2001): 37–45. http://dx.doi.org/10.1002/ajmg.1397.

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13

Wang, Yi, Jing Yang, Yu Zhang, and Jianhua Zhou. "Focus on Mitochondrial Respiratory Chain: Potential Therapeutic Target for Chronic Renal Failure." International Journal of Molecular Sciences 25, no. 2 (2024): 949. http://dx.doi.org/10.3390/ijms25020949.

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The function of the respiratory chain is closely associated with kidney function, and the dysfunction of the respiratory chain is a primary pathophysiological change in chronic kidney failure. The incidence of chronic kidney failure caused by defects in respiratory-chain-related genes has frequently been overlooked. Correcting abnormal metabolic reprogramming, rescuing the “toxic respiratory chain”, and targeting the clearance of mitochondrial reactive oxygen species are potential therapies for treating chronic kidney failure. These treatments have shown promising results in slowing fibrosis a
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14

Pyle, Angela, Helen J. Nightingale, Helen Griffin, et al. "Respiratory chain deficiency in nonmitochondrial disease." Neurology Genetics 1, no. 1 (2015): e6. http://dx.doi.org/10.1212/nxg.0000000000000006.

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15

Esteitie, N., and N.-G. Larsson. "Defective assembly of the respiratory chain." Acta Paediatrica 93, no. 10 (2007): 1268–70. http://dx.doi.org/10.1111/j.1651-2227.2004.tb02920.x.

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16

Walker, Ulrich A., Steven Collins, and Edward Byrne. "Respiratory Chain Encephalomyopathies: A Diagnostic Classification." European Neurology 36, no. 5 (1996): 260–67. http://dx.doi.org/10.1159/000117269.

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17

Enriquez, José Antonio, Paula Fernandez-Montes, Jose Luis Cabrera-Alarcon, and Carolina García-Poyatos. "Respiratory chain heterogeneity for healthy metabolism." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1865 (September 2024): 149136. http://dx.doi.org/10.1016/j.bbabio.2024.149136.

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18

Ädelroth, Pia, Jóhanna Vilhjálmsdóttir, Mateusz Janczak, and Olga Stah. "The respiratory chain of Mycobacterium smegmatis." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1865 (September 2024): 149134. http://dx.doi.org/10.1016/j.bbabio.2024.149134.

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19

Eubel, Holger, Jesco Heinemeyer, Stephanie Sunderhaus, and Hans-Peter Braun. "Respiratory chain supercomplexes in plant mitochondria." Plant Physiology and Biochemistry 42, no. 12 (2004): 937–42. http://dx.doi.org/10.1016/j.plaphy.2004.09.010.

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20

Bott, Michael, and Axel Niebisch. "The respiratory chain of Corynebacterium glutamicum." Journal of Biotechnology 104, no. 1-3 (2003): 129–53. http://dx.doi.org/10.1016/s0168-1656(03)00144-5.

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21

Bindoff, L. A., and D. M. Turnbull. "8 Defects of the respiratory chain." Baillière's Clinical Endocrinology and Metabolism 4, no. 3 (1990): 583–619. http://dx.doi.org/10.1016/s0950-351x(05)80069-2.

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22

Larsson, Nils-Göran, and Pierre Rustin. "Animal models for respiratory chain disease." Trends in Molecular Medicine 7, no. 12 (2001): 578–81. http://dx.doi.org/10.1016/s1471-4914(01)02167-0.

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23

Hicks, David B., and Terry A. Krulwich. "The respiratory chain of alkaliphilic bacteria." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1229, no. 3 (1995): 303–14. http://dx.doi.org/10.1016/0005-2728(95)00024-d.

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24

Higgins, D. S., M. Garcia-Osuna, and J. T. Greenamyre. "Neuroleptic effects on the respiratory chain." Biological Psychiatry 39, no. 7 (1996): 553. http://dx.doi.org/10.1016/0006-3223(96)84132-1.

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25

Rötig, A. "Genetics of mitochondrial respiratory chain deficiencies." Revue Neurologique 170, no. 5 (2014): 309–22. http://dx.doi.org/10.1016/j.neurol.2013.11.006.

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26

Winge, Dennis R., and Alex Tzagoloff. "Assembly of the Mitochondrial Respiratory Chain." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1793, no. 1 (2009): 1. http://dx.doi.org/10.1016/j.bbamcr.2008.11.002.

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27

Slater, E. C. "Keilin, Cytochrome, and the Respiratory Chain." Journal of Biological Chemistry 278, no. 19 (2003): 16455–61. http://dx.doi.org/10.1074/jbc.x200011200.

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28

Rustin, Pierre, Dominique Chretien, Thomas Bourgeron, et al. "Assessment of the mitochondrial respiratory chain." Lancet 338, no. 8758 (1991): 60. http://dx.doi.org/10.1016/0140-6736(91)90057-v.

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29

Lincke, C., C. van den Bogert, L. Nijtmans, R. Wanders, P. Tamminga, and P. Barth. "Cerebellar Hypoplasia in Respiratory Chain Dysfunction." Neuropediatrics 27, no. 04 (1996): 216–18. http://dx.doi.org/10.1055/s-2007-973792.

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30

Gauthier-Villars, Marion, P. Landrieu, Valérie Cormier-Daire, et al. "Respiratory Chain Deficiency in Alpers Syndrome." Neuropediatrics 32, no. 3 (2001): 150–52. http://dx.doi.org/10.1055/s-2001-16614.

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31

Suomalainen, Anu. "Biomarkers for mitochondrial respiratory chain disorders." Journal of Inherited Metabolic Disease 34, no. 2 (2010): 277–82. http://dx.doi.org/10.1007/s10545-010-9222-3.

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32

Mayr, Johannes A., Tobias B. Haack, Peter Freisinger, et al. "Spectrum of combined respiratory chain defects." Journal of Inherited Metabolic Disease 38, no. 4 (2015): 629–40. http://dx.doi.org/10.1007/s10545-015-9831-y.

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33

Alvarez, Cristina Uribe, Natalia Chiquete-Félix, Salvador Uribe-Carvajal, and Antonio Peña. "Exploring the Staphylococcus Epidermidis Respiratory Chain." Biophysical Journal 108, no. 2 (2015): 602a. http://dx.doi.org/10.1016/j.bpj.2014.11.3280.

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34

Brzezinski, Peter. "Regulatory Interactions within the Respiratory Chain." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1859 (September 2018): e13. http://dx.doi.org/10.1016/j.bbabio.2018.09.040.

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35

Capaldi, Roderick A. "Mitochondrial myopathies and respiratory chain proteins." Trends in Biochemical Sciences 13, no. 4 (1988): 144–48. http://dx.doi.org/10.1016/0968-0004(88)90073-4.

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36

Wolvetang, Ernst J., Karina L. Johnson, Kenia Krauer, Steve J. Ralph, and Anthony W. Linnane. "Mitochondrial respiratory chain inhibitors induce apoptosis." FEBS Letters 339, no. 1-2 (1994): 40–44. http://dx.doi.org/10.1016/0014-5793(94)80380-3.

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37

Kogot-Levin, Aviram, and Ann Saada. "Ceramide and the mitochondrial respiratory chain." Biochimie 100 (May 2014): 88–94. http://dx.doi.org/10.1016/j.biochi.2013.07.027.

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38

Herzig, R. P., U. Andersson, and R. C. Scarpulla. "Dynein light chain interacts with NRF-1 and EWG, structurally and functionally related transcription factors from humans and drosophila." Journal of Cell Science 113, no. 23 (2000): 4263–73. http://dx.doi.org/10.1242/jcs.113.23.4263.

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Abstract (sommario):
Nuclear respiratory factor-1 is a transcriptional activator that has been implicated in the nuclear control of respiratory chain expression. Yeast two-hybrid screens were performed to identify proteins that physically interact with nuclear respiratory factor-1. Saturation screening of both mouse embryo and mouse testis libraries yielded 14 independent clones, all of which represented two different isoforms of dynein light chain. In addition to using the two-hybrid method, the specificity of the nuclear respiratory factor-1/dynein light chain interaction was established by chemical crosslinking
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39

Cogliati, Sara, Christian Frezza, Maria Eugenia Soriano, et al. "Mitochondrial Cristae Shape Determines Respiratory Chain Supercomplexes Assembly and Respiratory Efficiency." Cell 155, no. 1 (2013): 160–71. http://dx.doi.org/10.1016/j.cell.2013.08.032.

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40

Lehmann, Diana, Helen A. L. Tuppen, Georgia E. Campbell, et al. "Understanding mitochondrial DNA maintenance disorders at the single muscle fibre level." Nucleic Acids Research 47, no. 14 (2019): 7430–43. http://dx.doi.org/10.1093/nar/gkz472.

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Abstract Clonal expansion of mitochondrial DNA (mtDNA) deletions is an important pathological mechanism in adults with mtDNA maintenance disorders, leading to a mosaic mitochondrial respiratory chain deficiency in skeletal muscle. This study had two aims: (i) to determine if different Mendelian mtDNA maintenance disorders showed similar pattern of mtDNA deletions and respiratory chain deficiency and (ii) to investigate the correlation between the mitochondrial genetic defect and corresponding respiratory chain deficiency. We performed a quantitative analysis of respiratory chain deficiency, at
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41

Altinterim, Basar. "The Effect in respiratory chain of CoQ10." Sakarya Medical Journal 3, no. 2 (2013): 51–54. http://dx.doi.org/10.5505/sakaryamj.2013.35220.

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42

Oexle, Konrad, and Angelika Zwirner. "Advanced Telomere Shortening in Respiratory Chain Disorders." Human Molecular Genetics 6, no. 6 (1997): 905–8. http://dx.doi.org/10.1093/hmg/6.6.905.

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43

Fernandez-Mosquera, Lorena, King Faisal Yambire, Renata Couto, et al. "Mitochondrial respiratory chain deficiency inhibits lysosomal hydrolysis." Autophagy 15, no. 9 (2019): 1572–91. http://dx.doi.org/10.1080/15548627.2019.1586256.

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44

Chen, Ming, Leif P. Andersen, Lin Zhai, and Arsalan Kharazmi. "Characterization of the respiratory chain ofHelicobacter pylori." FEMS Immunology & Medical Microbiology 24, no. 2 (1999): 169–74. http://dx.doi.org/10.1111/j.1574-695x.1999.tb01278.x.

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45

Rich, P. R. "The molecular machinery of Keilin's respiratory chain." Biochemical Society Transactions 31, no. 6 (2003): 1095–105. http://dx.doi.org/10.1042/bst0311095.

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Abstract (sommario):
Keilin's classic paper of 1925 [Keilin (1925) Proc. R. Soc. London Ser. B 100, 129–151], achieved with simple, but elegant, techniques, describes the cytochrome components of the respiratory chain and their roles in intracellular respiration and oxygen consumption. Since that time, a tremendous amount of work has clarified the intricate details of the prosthetic groups, cofactors and proteins that comprise the respiratory chain and associated machinery for ATP synthesis. The work has culminated in advanced crystallographic and spectroscopic methods that provide structural and mechanistic detai
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46

Finsterer, Josef, Georg Pelzl, Max Zartl, Elisabeth Unger, and Bruno Mamoli. "Video-EEG Monitoring in Respiratory Chain Disorders." Clinical Electroencephalography 32, no. 1 (2001): 24–27. http://dx.doi.org/10.1177/155005940103200107.

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47

Turrens, Julio F. "Superoxide Production by the Mitochondrial Respiratory Chain." Bioscience Reports 17, no. 1 (1997): 3–8. http://dx.doi.org/10.1023/a:1027374931887.

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This mini-review describes the role of different mitochondrial components in the formation of reactive oxygen species under normal and pathological conditions and the effect of inhibitors and uncouplers on superoxide formation.
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48

Cholley, Florence, P. Edery, D. Ricquier, S. Peudenier, A. Slama, and M. Tardieu. "Mitochondrial Respiratory Chain Deficiency Revealed by Hypothermia." Neuropediatrics 32, no. 2 (2001): 104–6. http://dx.doi.org/10.1055/s-2001-13878.

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49

Rötig, Agnès. "Genetic bases of mitochondrial respiratory chain disorders." Diabetes & Metabolism 36, no. 2 (2010): 97–107. http://dx.doi.org/10.1016/j.diabet.2009.11.002.

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50

Castro-Gago, M., M. O. Blanco-Barca, and J. Eirís-Puñal. "Epilepsy and Respiratory Chain Defects in Children." Neuropediatrics 40, no. 03 (2009): 152. http://dx.doi.org/10.1055/s-0029-1243186.

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