Cited by 1,026Coenzyme Q10 studies and effectsMitochondrial Function and PathologyBioactive Compounds and Antitumor Agents

The DOI matches its Crossref record; 321 of the 323 references it cites were found in a registry or an index.

Metabolism and function of coenzyme Q

Open access

Turunen, Mikael, Olsson, Jerker, Dallner, Gustav·2004·Biochimica et Biophysica Acta (BBA) - Biomembranes

DOI 10.1016/j.bbamem.2003.11.012

Open this paper in CoChat — free account Open PDF

Abstract

Coenzyme Q (CoQ) is present in all cells and membranes and in addition to be a member of the mitochondrial respiratory chain it has also several other functions of great importance for the cellular metabolism. This review summarizes the findings available to day concerning CoQ distribution, biosynthesis, regulatory modifications and its participation in cellular metabolism. There are a number of indications that this lipid is not always functioning by its direct presence at the site of action but also using e.g. receptor expression modifications, signal transduction mechanisms and action through its metabolites. The biosynthesis of CoQ is studied in great detail in bacteria and yeast but only to a limited extent in animal tissues and therefore the informations available is restricted. However, it is known that the CoQ is compartmentalized in the cell with multiple sites of biosynthesis, breakdown and regulation which is the basis of functional specialization. Some regulatory mechanisms concerning amount and biosynthesis are established and nuclear transcription factors are partly identified in this process. Using appropriate ligands of nuclear receptors the biosynthetic rate can be increased in experimental system which raises the possibility of drug-induced upregulation of the lipid in deficiency. During aging and pathophysiological conditions the tissue concentration of CoQ is modified which influences cellular functions. In this case the extent of disturbances is dependent on the localization and the modified distribution of the lipid at cellular and membrane levels.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/j.bbamem.2003.11.012

Cites

321 of 321 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
Mitochondria and Apoptosis
Green, D. R., & Reed, J. C. (1998) · Science · doi:10.1126/science.281.5381.1309 · Cited by 9,051
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827
A Receptor-Mediated Pathway for Cholesterol Homeostasis
Brown, M. S., & Goldstein, J. L. (1986) · Science · doi:10.1126/science.3513311 · Cited by 5,703
Regulation of the mevalonate pathway
Goldstein, J. L., & Brown, M. S. (1990) · Nature · doi:10.1038/343425a0 · Cited by 5,394
Prions
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Oxygen toxicity, oxygen radicals, transition metals and disease
Halliwell, B., & Gutteridge, J. M. C. (1984) · Biochemical Journal · doi:10.1042/bj2190001 · Cited by 5,330
Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators
Issemann, I., & Green, S. (1990) · Nature · doi:10.1038/347645a0 · Cited by 3,519
Mitochondrial free radical generation, oxidative stress, and aging
Cadenas, E., & Davies, K. J. A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00317-8 · Cited by 3,010
Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor
Hörlein, A., Näär, A. M., Heinzel, T., Torchia, J., Gloss, B. R., Kurokawa, R., Ryan, A. K., Kamei, Y., Söderström, M., Glass, C. K., et al. (1995) · Nature · doi:10.1038/377397a0 · Cited by 2,072
Cellular energy utilization and molecular origin of standard metabolic rate in mammals
Rolfe, D. F., & Brown, G. C. (1997) · Physiological Reviews · doi:10.1152/physrev.1997.77.3.731 · Cited by 2,021
Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors
Kliewer, S. A., Umesono, K., Noonan, D. J., Heyman, R. A., & Evans, R. M. (1992) · Nature · doi:10.1038/358771a0 · Cited by 1,746
Direct repeats as selective response elements for the thyroid hormone, retinoic acid, and vitamin D3 receptors
Umesono, K., Murakami, K. K., Thompson, C. C., & Evans, R. M. (1991) · Cell · doi:10.1016/0092-8674(91)90020-y · Cited by 1,688
Targeted Disruption of the α Isoform of the Peroxisome Proliferator-Activated Receptor Gene in Mice Results in Abolishment of the Pleiotropic Effects of Peroxisome Proliferators
Lee, S. S. T., Pineau, T., Drago, J., Lee, E. J., Owens, J. W., Kroetz, D. L., Fernández‐Salguero, P. M., Westphal, H., & Gonzalez, F. J. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.6.3012 · Cited by 1,652
Thermogenic mechanisms in brown fat.
Nicholls, D. G., & Locke, R. M. (1984) · Physiological Reviews · doi:10.1152/physrev.1984.64.1.1 · Cited by 1,602
DNA damage by oxygen‐derived species Its mechanism and measurement in mammalian systems
Halliwell, B. B., & Aruoma, O. I. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80347-6 · Cited by 1,537
Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signalling
Kliewer, S. A., Umesono, K., Mangelsdorf, D. J., & Evans, R. M. (1992) · Nature · doi:10.1038/355446a0 · Cited by 1,489
Peroxiredoxin Evolution and the Regulation of Hydrogen Peroxide Signaling
Wood, Z. A., Poole, L. B., & Karplus, P. A. (2003) · Science · doi:10.1126/science.1080405 · Cited by 1,369
Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
Schägger, H., & Pfeiffer, K. (2000) · The EMBO Journal · doi:10.1093/emboj/19.8.1777 · Cited by 1,356
Biochemical, physiological and medical aspects of ubiquinone function
Ernster, L., & Dallner, G. (1995) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/0925-4439(95)00028-3 · Cited by 1,246
Self-citation
RXRβ: A coregulator that enhances binding of retinoic acid, thyroid hormone, and vitamin D receptors to their cognate response elements
Yu, V. C. K., Delsert, C., D, B. A. M., Holloway, J. M., Devary, O. V., Näär, A. M., Kim, S. Y., Boutin, J., Glass, C. K., & Rosenfeld, M. G. (1991) · Cell · doi:10.1016/0092-8674(91)90301-e · Cited by 1,188
Metal ion-catalyzed oxidation of proteins: Biochemical mechanism and biological consequences
Stadtman, E. R. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90006-5 · Cited by 1,160
Tissue-specific functions of individual glutathione peroxidases
Brigelius-Flohé, R. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00173-2 · Cited by 1,114
Effects of Coenzyme Q10 in Early Parkinson Disease: Evidence of Slowing of the Functional Decline
Shults, C. W. (2002) · Archives of Neurology · doi:10.1001/archneur.59.10.1541 · Cited by 984
[21] Thioredoxin and thioredoxin reductase
Holmgren, A., & Björnstedt, M. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)52023-6 · Cited by 941
Uncoupling: new approaches to an old problem of bioenergetics
Skulachev, V. P. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(97)00091-1 · Cited by 893
BIOCHEMISTRY OF PEROXISOMES
van den BOSCH, H., Schutgens, R. B. H., Wanders, R. J. A., & Tager, J. M. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.61.070192.001105 · Cited by 844
Degradation of oxidized proteins in mammalian cells
Grune, T., Reinheckel, T., & Davies, K. J. A. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.7.9212076 · Cited by 835
Ubiquinol-10 protects human low density lipoprotein more efficiently against lipid peroxidation than does alpha-tocopherol.
Stocker, R., Bowry, V. W., & Frei, B. B. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.5.1646 · Cited by 797
Mitochondria Are Excitable Organelles Capable of Generating and Conveying Electrical and Calcium Signals
Ichas, F., Jouaville, L. S., & Mazat, J. (1997) · Cell · doi:10.1016/s0092-8674(00)80301-3 · Cited by 748
The genetics and pathology of oxidative phosphorylation
Smeitink, J. A. M., van den Heuvel, L., & DiMauro, S. (2001) · Nature Reviews Genetics · doi:10.1038/35072063 · Cited by 733
Decreased atherosclerosis in mice deficient in both macrophage colony-stimulating factor (op) and apolipoprotein E.
Smith, J. D., Trogan, E., Ginsberg, M., Grigaux, C., Tian, J., & Miyata, M. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.18.8264 · Cited by 721
Transient and Long-Lasting Openings of the Mitochondrial Permeability Transition Pore Can Be Monitored Directly in Intact Cells by Changes in Mitochondrial Calcein Fluorescence
Petronilli, V., Miotto, G., Canton, M., Brini, M., Colonna, R., Bernardi, P., & Lisa, F. D. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77239-5 · Cited by 677
DNA REPAIR IN EUKARYOTES
Wood, R. D. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.001031 · Cited by 669
Diabetes and Endothelial Dysfunction: A Clinical Perspective
Calles-Escandón, J., & Cipolla, M. J. (2001) · Endocrine Reviews · doi:10.1210/edrv.22.1.0417 · Cited by 657
Unique response pathways are established by allosteric interactions among nuclear hormone receptors
FORMAN, B. M., Umesono, K., Chen, J., & Evans, R. M. (1995) · Cell · doi:10.1016/0092-8674(95)90075-6 · Cited by 629
Ubiquinol-10 is an effective lipid-soluble antioxidant at physiological concentrations.
Frei, B. B., Kim, M. C., & Ames, B. N. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.12.4879 · Cited by 623
UCP1: The only protein able to mediate adaptive non-shivering thermogenesis and metabolic inefficiency
Nedergaard, J., Golozoubova, V., Matthias, A., Asadi, A., Jacobsson, A., & Cannon, B. (2001) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00247-4 · Cited by 615
Intercellular adhesion molecule-1 (ICAM-1) expression and cell signaling cascades
Hubbard, A. K., & Rothlein, R. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00223-9 · Cited by 594
Isolation of a quinone from beef heart mitochondria
Crane, F. L., Hatefi, Y., Lester, R. L., & Widmer, C. (1957) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(57)90457-2 · Cited by 588
Leucocyte-endothelial interactions and regulation of leucocyte migration
Adams, D., & Shaw, S. (1994) · The Lancet · doi:10.1016/s0140-6736(94)92029-x · Cited by 580
Coenzyme Q 10 administration increases brain mitochondrial concentrations and exerts neuroprotective effects
Matthews, R. T., Yang, L., Browne, S., Baik, M., & Beal, M. F. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.15.8892 · Cited by 557
Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence
Zhong, L., Arnér, E. S. J., & Holmgren, A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.100114897 · Cited by 528
PET genes of Saccharomyces cerevisiae
Tzagoloff, A., & Dieckmann, C. L. (1990) · Microbiological Reviews · doi:10.1128/mr.54.3.211-225.1990 · Cited by 520
Role of Mitochondria in Oxidative Stress and Aging
Lenaz, G., Bovina, C., D’Aurelio, M., Fato, R., Formiggini, G., Genova, M. L., GIULIANO, G., Pich, M. M., Paolucci, U., Castelli, G. P., et al. (2002) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2002.tb02094.x · Cited by 494
Widespread Occurrence of Three Sequence Motifs in Diverse S-Adenosylmethionine-Dependent Methyltransferases Suggests a Common Structure for These Enzymes
Kagan, R. M., & Clarke, S. G. (1994) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1994.1187 · Cited by 472
Reactive oxygen species, mitochondria, apoptosis and aging
Papa, S., & Skulachev, V. P. (1997) · Springer eBooks · doi:10.1007/978-1-4615-6111-8_47 · Cited by 467
Protonmotive redox mechanism of the cytochrome b‐c1 complex in the respiratory chain: Protonmotive ubiquinone cycle
Mitchell, P. D. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)80098-6 · Cited by 448
Transplasma-membrane redox systems in growth and development
Crane, F. L., SUN, I. L., Clark, M. G., Grebing, C., & Löw, H. (1985) · Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics · doi:10.1016/0304-4173(85)90013-8 · Cited by 446
The Inhibition of Mitochondrial Peroxidation by Ubiquinone and Ubiquinol
Mellors, A., & Tappel, A. L. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99728-0 · Cited by 432
A new role for phospholipase A2: protection of membranes from lipid peroxidation damage
van Kuijk, F. J. G. M., Sevanian, A., Handelman, G. J., & Dratz, E. A. (1987) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(87)90014-4 · Cited by 428
Lovastatin decreases coenzyme Q levels in humans.
Folkers, K., Langsjoen, P. H., Willis, R. A., Richardson, P. C., Xia, L., Ye, C. Q., & Tamagawa, H. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.22.8931 · Cited by 426
Age‐related changes in the lipid compositions of rat and human tissues
Kalén, A., Appelkvist, E., & Dallner, G. (1989) · Lipids · doi:10.1007/bf02535072 · Cited by 425
Self-citation
Mutations in the clk-1 gene of Caenorhabditis elegans affect developmental and behavioral timing
Wong, A., Boutis, P., & Hekimi, S. (1995) · Genetics · doi:10.1093/genetics/139.3.1247 · Cited by 416
M ECHANISM AND R EGULATION OF S ELENOPROTEIN S YNTHESIS
Driscoll, D. M., & Copeland, P. R. (2003) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.23.011702.073318 · Cited by 409
Energy metabolism defects in Huntington's disease and effects of coenzyme Q10
Koroshetz, W. J., Jenkins, B. G., Rosen, B. R., & Beal, M. F. (1997) · Annals of Neurology · doi:10.1002/ana.410410206 · Cited by 405
Reactive oxygen species, mitochondria, apoptosis and aging
Papa, S., & Скулачев, В. П. (1997) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006873518427 · Cited by 389
Muscle coenzyme Q deficiency in familial mitochondrial encephalomyopathy.
Ogasahara, S., Engel, A. G., Frens, D. B., & Mack, D. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.7.2379 · Cited by 365
Structure and function of the uncoupling protein from brown adipose tissue
Klingenberg, M., & Huang, S. (1999) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(98)00232-6 · Cited by 359
Discovery, biochemistry and biology of lovastatin
Alberts, A. W. (1988) · The American Journal of Cardiology · doi:10.1016/0002-9149(88)90002-1 · Cited by 358
Quinone-responsive multiple respiratory-chain dysfunction due to widespread coenzyme Q10 deficiency
Rötig, A., Appelkvist, E., Géromel, V., Chrétien, D., Kadhom, N., Edery, P., Bideau, M. L., Dallner, G., Münnich, A., Ernster, L., et al. (2000) · The Lancet · doi:10.1016/s0140-6736(00)02531-9 · Cited by 354
Self-citation
Enzymatic Aspects of Isoprenoid Chain Elongation
Ogura, K., & Koyama, T. (1998) · Chemical Reviews · doi:10.1021/cr9600464 · Cited by 347
UDP-glucuronosyltransferases
Burchell, B., & Coughtrie, M. W. H. (1989) · Pharmacology & Therapeutics · doi:10.1016/0163-7258(89)90122-8 · Cited by 346
The preference of cholesterol for phosphatidylcholine in mixed phosphatidylcholine-phosphatidylethanolamine bilayers
van Dijck, P. W. M., KRUIJFF, B. D., Deenen, L. L. M. V., de Gier, J., & DEMEL, R. A. (1976) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(76)90326-6 · Cited by 340
Coenzyme Q is an obligatory cofactor for uncoupling protein function
Echtay, K. S., Winkler, E., & Klingenberg, M. (2000) · Nature · doi:10.1038/35046114 · Cited by 334
Role of macrophage colony-stimulating factor in atherosclerosis: studies of osteopetrotic mice.
Qiao, J. H., Tripathi, J., Mishra, N. K., Cai, Y., Tripathi, S., Wang, X. P., Imes, S., Fishbein, M. C., Clinton, S. K., Libby, P., et al. (1997) · Europe PMC (PubMed Central) · Cited by 327
The role of DT-diaphorase in the maintenance of the reduced antioxidant form of coenzyme Q in membrane systems.
Beyer, R. E., Segura‐Aguilar, J., Bernardo, S. D., Cavazzoni, M., Fato, R., Fiorentini, D., Galli, M. C., Setti, M., Landi, L., & Lenaz, G. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.6.2528 · Cited by 327
Coenzyme Q10 levels correlate with the activities of complexes I and II/III in mitochondria from parkinsonian and nonparkinsonian subjects
Shults, C. W., Haas, R. H., Passov, D., & Beal, M. F. (1997) · Annals of Neurology · doi:10.1002/ana.410420221 · Cited by 326
Evidence of Plasma CoQ10‐Lowering Effect by HMG‐CoA Reductase Inhibitors: A Double‐Blind, Placebo‐Controlled Study
Ghirlanda, G., Oradei, A., Manto, A., Lippa, S., Uccioli, L., Caputo, S., Greco, A. V., & Littarru, G. P. (1993) · The Journal of Clinical Pharmacology · doi:10.1002/j.1552-4604.1993.tb03948.x · Cited by 324
Regulation of HMG‐CoA reductase: identification of the site phosphorylated by the AMP‐activated protein kinase in vitro and in intact rat liver.
Clarke, P. R., & Hardie, D. G. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07420.x · Cited by 322
[30] DT-diaphorase: Purification, properties, and function
Lind, C., Cadenas, E., Hochstein, P., & Ernster, L. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)86122-c · Cited by 321
Structural and Functional Conservation of the Caenorhabditis elegans Timing Gene clk-1
Ewbank, J. J., Barnes, T. M., Lakowski, B., Lussier, M., Bussey, H., & Hekimi, S. (1997) · Science · doi:10.1126/science.275.5302.980 · Cited by 319
Distribution and redox state of ubiquinones in rat and human tissues
Åberg, F. O., Appelkvist, E., Dallner, G., & Ernster, L. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90511-t · Cited by 319
Self-citation
Uncoupling proteins 2 and 3 are highly active H + transporters and highly nucleotide sensitive when activated by coenzyme Q (ubiquinone)
Echtay, K. S., Winkler, E., Frischmuth, K., & Klingenberg, M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1416 · Cited by 313
Genetic and functional changes in mitochondria associated with aging
Ozawa, T. (1997) · Physiological Reviews · doi:10.1152/physrev.1997.77.2.425 · Cited by 312 · cited 12×
“The free radicals formed in the cell are able to damage lipids, proteins and DNA, a concept known as oxidative stress.”
BackgroundInfluential
Biomedical and clinical aspects of coenzyme Q
Littarru, G. P. (1993) · Journal of Molecular Medicine · doi:10.1007/bf00184478 · Cited by 310
Coenzyme Q10 Prevents Apoptosis by Inhibiting Mitochondrial Depolarization Independently of Its Free Radical Scavenging Property
Papucci, L., Schiavone, N., Witort, E. J., Donnini, M., Lapucci, A., Tempestini, A., Formigli, L., Zecchi‐Orlandini, S., Orlandini, G., Carella, G., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302297200 · Cited by 308
The biological role of dolichol
Chojnacki, T., & Dallner, G. (1988) · Biochemical Journal · doi:10.1042/bj2510001 · Cited by 300
Self-citation
Structures and Proton-Pumping Strategies of Mitochondrial Respiratory Enzymes
Schultz, B. E., & Chan, S. I. (2001) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.30.1.23 · Cited by 299
Lipophilic HMG-CoA reductase inhibitor has an anti-inflammatory effect
Inoue, I., Goto, S.-I., Mizotani, K., Awata, T., Mastunaga, T., Kawai, S.-I., Nakajima, T., Hokari, S., Komoda, T., & Katayama, S. (2000) · Life Sciences · doi:10.1016/s0024-3205(00)00680-9 · Cited by 298
Peroxisome proliferator activated receptors: transcriptional regulators of adipogenesis, lipid metabolism and more…
Wahli, W., Braissant, O., & Desvergne, B. (1995) · Chemistry & Biology · doi:10.1016/1074-5521(95)90045-4 · Cited by 297
Nuclear-receptor interactions on DNA-response elements
Khorasanizadeh, S., & Rastinejad, F. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01800-x · Cited by 288
Ubiquinol: an endogenous antioxidant in aerobic organisms
Ernster, L., & Forsmark-Andrée, P. (1993) · Journal of Molecular Medicine · doi:10.1007/bf00226842 · Cited by 286
Fenton chemistry. Amino acid oxidation.
Stadtman, E. R., & Berlett, B. S. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47359-6 · Cited by 285
Elucidation of the deficiency in two yeast coenzyme Q mutants. Characterization of the structural gene encoding hexaprenyl pyrophosphate synthetase.
Ashby, M. N., & Edwards, P. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38280-8 · Cited by 282
A Ubiquinone-binding Site Regulates the Mitochondrial Permeability Transition Pore
Fontaine, E. M., Ichas, F., & Bernardi, P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.40.25734 · Cited by 273
Hepatic peroxisome proliferation in rodents and its significance for humans
Bentley, P., Calder, I. C., Elcombe, C. R., GRASSO, P., Stringer, D. A., & Wiegand, H.-J. (1993) · Food and Chemical Toxicology · doi:10.1016/0278-6915(93)90225-n · Cited by 271
The influence of dolichol, dolichol esters, and dolichyl phosphate on phospholipid polymorphism and fluidity in model membranes.
Valtersson, C., van Duÿn, G., Verkleij, A. J., Chojnacki, T., KRUIJFF, B. D., & Dallner, G. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89424-8 · Cited by 270
Self-citation
Mitochondrial oxidative phosphorylation changes in the life span. Molecular aspects and physiopathological implications
Papa, S. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00077-1 · Cited by 266
Identification of a Functional Peroxisome Proliferator-responsive Element in the Murine Fatty Acid Transport Protein Gene
Frohnert, B. I., Hui, T. Y., & Bernlohr, D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.7.3970 · Cited by 265
Branch-point reactions in the biosynthesis of cholesterol, dolichol, ubiquinone and prenylated proteins
Grünler, J., Ericsson, J., & Dallner, G. (1994) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(94)90200-3 · Cited by 259
Self-citation
Coenzyme Q10 improves blood pressure and glycaemic control: a controlled trial in subjects with type 2 diabetes
Hodgson, J., Watts, G. F., Playford, D. A., Burke, V., & Croft, K. D. (2002) · European Journal of Clinical Nutrition · doi:10.1038/sj.ejcn.1601464 · Cited by 253
Extension of Life-Span in Caenorhabditis elegans by a Diet Lacking Coenzyme Q
Larsen, P. L., & Clarke, C. F. (2002) · Science · doi:10.1126/science.1064653 · Cited by 249
Biochemical rationale and myocardial tissue data on the effective therapy of cardiomyopathy with coenzyme Q10.
Folkers, K., Vadhanavikit, S., & Mortensen, S. A. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.3.901 · Cited by 246
Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones
Ullrich, O., Reinheckel, T., Sitte, N., Hass, R., Grune, T., & Davies, K. J. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.11.6223 · Cited by 229
S-Adenosylmethionine-dependent Methylation inSaccharomyces cerevisiae
Niewmierzycka, A., & Clarke, S. G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.2.814 · Cited by 226
Hepatocyte-Specific Mutation Establishes Retinoid X Receptor α as a Heterodimeric Integrator of Multiple Physiological Processes in the Liver
Wan, Y. Y., An, D., Cai, Y., Repa, J. J., Chen, T. H.-P., Flores, M., Postic, C., Magnuson, M. A., Chen, J., Chien, K. R., et al. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.12.4436-4444.2000 · Cited by 226
Simultaneous Detection of Ubiquinol and Ubiquinone in Human Plasma as a Marker of Oxidative Stress
Yamashita, S., & Yamamoto, Y. (1997) · Analytical Biochemistry · doi:10.1006/abio.1997.2187 · Cited by 220
Requirement for coenzyme Q in plasma membrane electron transport.
SUN, I. L., Sun, E. E., Crane, F. L., Morré, D. J., Lindgren, A., & Löw, H. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.23.11126 · Cited by 220
Lipid Composition in Different Regions of the Brain in Alzheimer's Disease/Senile Dementia of Alzheimer's Type
SoOderberg, M., Edlund, C., Alafuzoff, I., Kristensson, K., & Dallner, G. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb10994.x · Cited by 215
Self-citation
Control of transcription activation by steroid hormone receptors
Gronemeyer, H. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.8.1592204 · Cited by 215
Ubiquinone biosynthesis by the microsomal fraction from rat liver
Kalén, A., Norling, B., Appelkvist, E. L., & Dallner, G. (1987) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(87)90183-8 · Cited by 211
Self-citation
The Mammalian Cytosolic Selenoenzyme Thioredoxin Reductase Reduces Ubiquinone
Xia, L., Nordman, T., Olsson, J. M., Damdimopoulos, A. E., Björkhem‐Bergman, L., Nalvarte, I., Eriksson, L. C., Arnér, E. S. J., Spyrou, G., & Björnstedt, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210456200 · Cited by 209
Self-citation
Inhibition of selenoprotein synthesis by selenocysteine tRNA[Ser]Sec lacking isopentenyladenosine
Warner, G. J., Berry, M. J., Moustafa, M. E., Carlson, B. A., Hatfield, D. L., & Faust, J. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001280200 · Cited by 207
NADH- and NADPH-dependent lipid peroxidation in bovine heart submitochondrial particles. Dependence on the rate of electron flow in the respiratory chain and an antioxidant role of ubiquinol
Takayanagi, R., Takeshige, K., & Minakami, S. (1980) · Biochemical Journal · doi:10.1042/bj1920853 · Cited by 202
Dose-related decrease of serum coenzyme Q10 during treatment with HMG-CoA reductase inhibitors
Mortensen, S. A., Leth, A., Agner, E., & Rohde, M. (1997) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(97)00014-9 · Cited by 199
Effects of coenzyme Q10 administration on its tissue concentrations, mitochondrial oxidant generation, and oxidative stress in the rat
Kwong, L. K., Kamzalov, S., Rebrin, I., Bayne, A.-C. V., Jana, C. K., Morris, P., Forster, M. J., & Sohal, R. S. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00916-4 · Cited by 199
A dietary source of coenzyme Q is essential for growth of long-lived Caenorhabditis elegans clk-1 mutants
Jonassen, T., Larsen, P. L., & Clarke, C. F. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.2.421 · Cited by 197
Chain-length determination mechanism of isoprenyl diphosphate synthases and implications for molecular evolution
Wang, K., & Ohnuma, S. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01464-4 · Cited by 196
Coenzyme Q10 improves endothelial dysfunction of the brachial artery in Type II diabetes mellitus
Watts, G. F., Playford, D. A., Croft, K. D., Ward, N. C., Mori, T. A., & Burke, V. (2002) · Diabetologia · doi:10.1007/s00125-001-0760-y · Cited by 193
Uptake of Dietary Coenzyme Q Supplement is Limited in Rats
Zhang, Y., Åberg, F. O., Appelkvist, E., Dallner, G., & Ernster, L. (1995) · Journal of Nutrition · doi:10.1093/jn/125.3.446 · Cited by 192
Self-citation
Effect of micronutrient status on natural killer cell immune function in healthy free-living subjects aged ≥90 y
Ravaglia, G., Forti, P., Maioli, F., Bastagli, L., Facchini, A., Mariani, E., Savarino, L., Sassi, S., Cucinotta, D., & Lenaz, G. (2000) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/71.2.590 · Cited by 189
COQ2 is a candidate for the structural gene encoding para-hydroxybenzoate:polyprenyltransferase.
Ashby, M. N., Kutsunai, S. Y., Ackerman, S. H., Tzagoloff, A., & Edwards, P. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50638-x · Cited by 188
Comparative study on dynamics of antioxidative action of α-tocopheryl hydroquinone, ubiquinol, and α-tocopherol against lipid peroxidation
Shi, H., Noguchi, N., & Niki, E. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00053-2 · Cited by 188
The COQ7 Gene Encodes a Protein in Saccharomyces cerevisiae Necessary for Ubiquinone Biosynthesis
Marbois, B. N., & Clarke, C. F. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.6.2995 · Cited by 182
Divalent cation and prenyl pyrophosphate specificities of the protein farnesyltransferase from rat brain, a zinc metalloenzyme.
Reiss, Y., Brown, M. S., & Goldstein, J. L. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42709-3 · Cited by 173
Uncoupling proteins: the issues from a biochemist point of view
Klingenberg, M., & Echtay, K. S. (2001) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00242-5 · Cited by 172
Identification of farnesol as the non-sterol derivative of mevalonic acid required for the accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Correll, C. C., Ng, L., & Edwards, P. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32450-x · Cited by 171
Glutathione Reductase from Human Erythrocytes
Krohne‐Ehrich, G., Schirmer, R. H., & Untucht‐Grau, R. (1977) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1977.tb11856.x · Cited by 170
Studies with Ubiquinone‐Depleted Submitochondrial Particles
Ernster, L., Lee, I.-Y., Norling, B., & Persson, B. (1969) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1969.tb00609.x · Cited by 168
Biosynthesis of Ubiquinone
Olson, R. E., & Rudney, H. (1983) · Vitamins and hormones · doi:10.1016/s0083-6729(08)60431-8 · Cited by 165
PET genes of Saccharomyces cerevisiae.
Tzagoloff, A., & Dieckmann, C. L. (1990) · Microbiological Reviews · doi:10.1128/mmbr.54.3.211-225.1990 · Cited by 161
Up-regulation of the plasma membrane oxidoreductase as a prerequisite for the viability of human Namalwa rho 0 cells.
Larm, J. A., Vaillant, F., Linnane, A. W., & Lawen, A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43779-9 · Cited by 156
PPAR Tissue Distribution and Interactions with Other Hormone‐Signaling Pathwaysa
Lemberger, T., Braissant, O., Juge-Aubry, C. E., KELLER, H., Saladin, R., Staels, B., Auwerx, J. H., Burger, A., Meier, C. A., & Wahli, W. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb18619.x · Cited by 156
The Peroxisome Proliferator-activated Receptor α (PPARα) Regulates Bile Acid Biosynthesis
Hunt, M. C., Yang, Y., Eggertsen, G., Carneheim, C., Gåfvels, M. E., Einarsson, C., & Alexson, S. E. H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002782200 · Cited by 155
Progress on the Mitochondrial Permeability Transition Pore: Regulation by Complex I and Ubiquinone Analogs
Fontaine, E. M., & Bernardi, P. (1999) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005475802350 · Cited by 149
Effects of coenzyme Q10 and α-tocopherol administration on their tissue levels in the mouse: elevation of mitochondrial α-tocopherol by coenzyme Q10
Lass, A., Forster, M. J., & Sohal, R. S. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00330-x · Cited by 148
Three Classes of Ubiquinone Analogs Regulate the Mitochondrial Permeability Transition Pore through a Common Site
Walter, L., Nogueira, V., Leverve, X. M., Heitz, M., Bernardi, P., & Fontaine, E. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004128200 · Cited by 148
Overview of the use of CoQ10 in cardiovascular disease
Langsjoen, P. H., & Langsjoen, A. M. (1999) · BioFactors · doi:10.1002/biof.5520090224 · Cited by 147
Oxidative Stress in Patients with Hepatitis, Cirrhosis, and Hepatoma Evaluated by Plasma Antioxidants
Yamamoto, Y., Yamashita, S., Fujisawa, A., Kokura, S., & Yoshikawa, T. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8752 · Cited by 147
Antioxidant action of ubiquinol homologues with different isoprenoid chain length in biomembranes
Kagan, V. E., Serbinova, E. A., Koynova, G. M., Kitanova, S., Tyurin, V. A., Stoytchev, T., Quinn, P. J., & Packer, L. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90114-x · Cited by 147
Distribution and breakdown of labeled coenzyme Q10 in rat
Bentinger, M., Dallner, G., Chojnacki, T., & Świeżewska, E. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01357-6 · Cited by 146
Self-citation
Lipid peroxidation and changes in the ubiquinone content and the respiratory chain enzymes of submitochondrial particles
Forsmark-Andrée, P., Lee, C.-P., Dallner, G., & Ernster, L. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00330-9 · Cited by 145
Self-citation
A C-methyltransferase involved in both ubiquinone and menaquinone biosynthesis: isolation and identification of the Escherichia coli ubiE gene
Lee, P. T., Hsu, A. Y., Ha, H. T., & Clarke, C. F. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.5.1748-1754.1997 · Cited by 139
Identification of Escherichia coli ubiB , a Gene Required for the First Monooxygenase Step in Ubiquinone Biosynthesis
Poon, W. W., Davis, D. E., Ha, H. T., Jonassen, T., Rather, P. N., & Clarke, C. F. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.18.5139-5146.2000 · Cited by 139
Stimulation by hydrogen peroxide of DNA synthesis, competence family gene expression and phosphorylation of a specific protein in quiescent Balb/3T3 cells.
Shibanuma, M., Kuroki, T., & Nose, K. (1990) · PubMed · Cited by 139
A growth factor- and hormone-stimulated NADH oxidase from rat liver plasma membrane
Brightman, A. O., Wang, J., Miu, R. K.-M., SUN, I. L., Barr, R., Crane, F. L., & Morré, D. J. (1992) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(92)90168-l · Cited by 138
Dietary Cosupplementation With Vitamin E and Coenzyme Q 10 Inhibits Atherosclerosis in Apolipoprotein E Gene Knockout Mice
Thomas, S. R., Leichtweis, S. B., Pettersson, K. S., Croft, K. D., Mori, T. A., Brown, A. J., & Stocker, R. (2001) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.21.4.585 · Cited by 138
Conversion from Farnesyl Diphosphate Synthase to Geranylgeranyl Diphosphate Synthase by Random Chemical Mutagenesis
Ohnuma, S., Nakazawa, T., Hemmi, H., Hallberg, A.-M., Koyama, T., Ogura, K., & Nishino, T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.17.10087 · Cited by 136
Lovastatin decreases coenzyme Q levels in rats.
Willis, R. A., Folkers, K., Tucker, J. L., Ye, C. Q., Xia, L., & Tamagawa, H. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.22.8928 · Cited by 135
Yeast Clk-1 Homologue (Coq7/Cat5) Is a Mitochondrial Protein in Coenzyme Q Synthesis
Jonassen, T., Proft, M., Rández‐Gil, F., Schultz, J. R., Marbois, B. N., Entian, K., & Clarke, C. F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3351 · Cited by 134
Coantioxidants make alpha-tocopherol an efficient antioxidant for low-density lipoprotein
Thomas, S. R., Neužil, J., Mohr, D., & Stocker, R. (1995) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/62.6.1357s · Cited by 133
COENZYME Q. I. STRUCTURE STUDIES ON THE COENZYME Q GROUP
Wolf, D. E., Hoffman, C. H., Trenner, N. R., Arison, B. H., Shunk, C. H., Linn, B. O., McPherson, J. F., & Folkers, K. (1958) · Journal of the American Chemical Society · doi:10.1021/ja01550a096 · Cited by 130
Vitamin E and selenium deficiency induces expression of the ubiquinone‐dependent antioxidant system at the plasma membrane
Navarro, F., Navas, P., Burgess, J. R., Bello, R. I., de Cabo, R., Arroyo, A., & Villalba, J. M. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.15.1665 · Cited by 128
Surface Oxidase and Oxidative Stress Propagation in Aging
Morré, D. M., Lenaz, G., & Morré, D. J. (2000) · Journal of Experimental Biology · doi:10.1242/jeb.203.10.1513 · Cited by 128
ABC1, a novel yeast nuclear gene has a dual function in mitochondria: it suppresses a cytochrome b mRNA translation defect and is essential for the electron transfer in the bc 1 complex.
Bousquet, I., Dujardin, G., & Słonimski, P. P. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07732.x · Cited by 126
A Defect in Coenzyme Q Biosynthesis Is Responsible for the Respiratory Deficiency in Saccharomyces cerevisiae abc1Mutants
Do, T. Q., Hsu, A. Y., Jonassen, T., Lee, P. T., & Clarke, C. F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100952200 · Cited by 126
Inhibition of lipid peroxidation by ubiquinol in submitochondrial particles in the absence of vitamin E
Forsmark-Andrée, P., Åberg, F. O., Norling, B., Nordenbrand, K., Dallner, G., & Ernster, L. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80720-n · Cited by 124
Self-citation
Polyprenyl diphosphate synthase essentially defines the length of the side chain of ubiquinone
Okada, K., Suzuki, K., Kamiya, Y., Xufen, Z., Fujisaki, S., Nishimura, Y., Nishino, T., Nakagawad, T., Kawamukai, M., & Matsuda, H. (1996) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(96)00064-1 · Cited by 123
Adaptation of Escherichia coli to respiratory conditions: Regulation of gene expression
Iuchi, S., & Lin, E. C. C. (1991) · Cell · doi:10.1016/0092-8674(91)90130-q · Cited by 122
Nonaprenyl-4-hydroxybenzoate transferase, an enzyme involved in ubiquinone biosynthesis, in the endoplasmic reticulum-Golgi system of rat liver.
Kalén, A., Appelkvist, E. L., Chojnacki, T., & Dallner, G. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40172-5 · Cited by 121
Self-citation
In vivo supplementation with coenzyme Q 10 enhances the recovery of human lymphocytes from oxidative DNA damage
Tomasetti, M., Alleva, R., & Collins, A. R. (2001) · The FASEB Journal · doi:10.1096/fj.00-0694fje · Cited by 121
Identification, purification, and immunochemical characterization of a tocopherol-binding protein in rat liver cytosol.
Yoshida, H., Yusin, M., REN, I., Kuhlenkamp, J., Hirano, T., Stolz, A., & Kaplowitz, N. (1992) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)41524-x · Cited by 121
Biosynthesis of Ubiquinone in Escherichia coli K-12: Location of Genes Affecting the Metabolism of 3-Octaprenyl-4-hydroxybenzoic Acid and 2-Octaprenylphenol
Cox, G. B., Young, I. G., McCann, L. M., & Gibson, F. (1969) · Journal of Bacteriology · doi:10.1128/jb.99.2.450-458.1969 · Cited by 120
Characterization of Polyprenyldiphosphate: 4-Hydroxybenzoate Polyprenyltransferase from Escherichia coli
Melzer, M., & Heide, L. E. (1994) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(94)90193-7 · Cited by 119
The roles of coenzyme Q10 and vitamin E on the peroxidation of human low density lipoprotein subfractions.
Alleva, R., Tomasetti, M., Battino, M. A., CURATOLA, G., Littarru, G. P., & Folkers, K. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.20.9388 · Cited by 118
Alterations in the rates of synthesis and degradation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A reductase produced by cholestyramine and mevinolin.
Edwards, P. A., Lan, S. F., & Fogelman, A. M. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44444-9 · Cited by 117
Mitochondrial Ubiquinone Homologues, Superoxide Radical Generation, and Longevity in Different Mammalian Species
Lass, A., Agarwal, S., & Sohal, R. S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.31.19199 · Cited by 117
Conversion of Product Specificity of Archaebacterial Geranylgeranyl-diphosphate Synthase
Ohnuma, S., Hirooka, K., Hemmi, H., Ishida, C., Ohto, C., & Nishino, T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.31.18831 · Cited by 117
Cholesterol synthesis in rat liver peroxisomes. Conversion of mevalonic acid to cholesterol.
Thompson, S. L., Burrows, R., Laub, R. J., & Krisans, S. K. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45395-1 · Cited by 116
Restricted Uptake of Dietary Coenzyme Q Is in Contrast to the Unrestricted Uptake of α-Tocopherol into Rat Organs and Cells
Zhang, Y., Turunen, M., & Appelkvist, E. (1996) · Journal of Nutrition · doi:10.1093/jn/126.9.2089 · Cited by 116
Self-citation
The Existence of a Lysosomal Redox Chain and the Role of Ubiquinone
Gille, L., & Nohl, H. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1649 · Cited by 116
Yeast and Rat Coq3 and Escherichia coli UbiG Polypeptides Catalyze Both O-Methyltransferase Steps in Coenzyme Q Biosynthesis
Poon, W. W., Barkovich, R. J., Hsu, A. Y., Frankel, A., Lee, P. T., Shepherd, J. N., Myles, D. C., & Clarke, C. F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.21665 · Cited by 116
Complementation of coq3 Mutant Yeast by Mitochondrial Targeting of the Escherichia coli UbiG Polypeptide: Evidence That UbiG Catalyzes Both O-Methylation Steps in Ubiquinone Biosynthesis
Hsu, A. Y., Poon, W. W., Shepherd, J. A., Myles, D. C., & Clarke, C. F. (1996) · Biochemistry · doi:10.1021/bi9602932 · Cited by 114
3-Polyprenyl-4-hydroxybenzoate Synthesis in the Inner Membrane of Mitochondria from p-Hydroxybenzoate and Isopentenylpyrophosphate
Momose, K., & Rudney, H. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45124-7 · Cited by 111
Peroxisome Proliferator–induced Pleiotropic Responses: Pursuit of a Phenomenona
Reddy, J. K., & Chu, R. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb18616.x · Cited by 110
Distribution of antioxidants among blood components and lipoproteins: Significance of lipids/CoQ10 ratio as a possible marker of increased risk for atherosclerosis
Tomasetti, M., Alleva, R., Solenghi, M. D., & Littarru, G. P. (1999) · BioFactors · doi:10.1002/biof.5520090218 · Cited by 109
Endogenous ubiquinol prevents protein modification accompanying lipid peroxidation in beef heart submitochondrial particles
Forsmark-Andrée, P., Dallner, G., & Ernster, L. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)00076-a · Cited by 107
Self-citation
Dihydrolipoic Acid Maintains Ubiquinone in the Antioxidant Active Form by Two-Electron Reduction of Ubiquinone and One-Electron Reduction of Ubisemiquinone
Kozlov, A. V., Gille, L., Staniek, K., & Nohl, H. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.1064 · Cited by 106
The NADPH-dependent O-.2-generating oxidase from human neutrophils.
Gabig, T. G. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32416-5 · Cited by 105
Synthesis of delta 2-isopentenyl tRNA from mevalonate in cultured human fibroblasts.
Faust, J. R., Brown, M. S., & Goldstein, J. L. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43600-9 · Cited by 104
Anti-atherogenic effect of coenzyme Q10 in apolipoprotein E gene knockout mice
Witting, P. K., Pettersson, K. S., Letters, J., & Stocker, R. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00311-7 · Cited by 104
DT-Diaphorase Maintains the Reduced State of Ubiquinones in Lipid Vesicles thereby Promoting their Antioxidant Function
Landi, L., Fiorentini, D., Galli, M. C., Segura‐Aguilar, J., & Beyer, R. E. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00294-8 · Cited by 104
Rates of cholesterol, ubiquinone, dolichol and dolichyl‐P biosynthesis in rat brain slices
Andersson, M., Elmberger, P. G., Edlund, C., Kristensson, K., & Dallner, G. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)81107-y · Cited by 104
Self-citation
Rapid Nonvesicular Transport of Sterol between the Plasma Membrane Domains of Polarized Hepatic Cells
Wüstner, D., Herrmann, A., Hao, M., & Maxfield, F. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202626200 · Cited by 104
Uptake of Exogenous Coenzyme Q and Transport to Mitochondria Is Required for bc1 Complex Stability in Yeast coq Mutants
Santos‐Ocaña, C., Do, T. Q., Clarke, C. F., Padilla, S., & Navas, P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112222200 · Cited by 104
In vitro and in vivo synthesis of dolichol and other main mevalonate products in various organs of the rat
Elmberger, P. G., Kalén, A., Appelkvist, E., & Dallner, G. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb13379.x · Cited by 102
Self-citation
The plasma membrane NADH oxidase of HeLa cells has hydroquinone oxidase activity
Kishi, T., Morré, D. M., & Morré, D. J. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00049-3 · Cited by 102
Biosynthesis of ubiquinone and plastoquinone in the endoplasmic reticulum-Golgi membranes of spinach leaves.
Świeżewska, E., Dallner, G., Andersson, B., & Ernster, L. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54102-8 · Cited by 101
Self-citation
The lipid compositions of different regions of rat brain during development and aging
Zhang, Y., Appelkvist, E., Kristensson, K., & Dallner, G. (1996) · Neurobiology of Aging · doi:10.1016/s0197-4580(96)00076-0 · Cited by 101
Self-citation
A constituent of the unsaponifiable portion of animal tissue lipids (λmax. 272mμ.)
Festenstein, G. N., Heaton, F. W., Lowe, J. S., & Morton, R. A. (1955) · Biochemical Journal · doi:10.1042/bj0590558 · Cited by 101
Mammalian α-Keto Acid Dehydrogenase Complexes
Hayakawa, T., Kanzaki, T., Kitamura, T., Fukuyoshi, Y., Sakurai, Y., Koike, K., Suematsu, T., & Koike, M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83420-2 · Cited by 99
Coenzyme Q10 enrichment decreases oxidative DNA damage in human lymphocytes
Tomasetti, M., Littarru, G. P., Stocker, R., & Alleva, R. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00132-x · Cited by 99
Characterization of the COQ5 Gene from Saccharomyces cerevisiae EVIDENCE FOR A C-METHYLTRANSFERASE IN UBIQUINONE BIOSYNTHESIS
Barkovich, R. J., Shtanko, A., Shepherd, J. A., Lee, P. T., Myles, D. C., Tzagoloff, A., & Clarke, C. F. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.14.9182 · Cited by 97
Discharge of newly‐synthesized dolichol and ubiquinone with lipoproteins to rat liver perfusate and to the bile
Elmberger, P. G., Kalén, A., Brunk, U. T., & Dallner, G. (1989) · Lipids · doi:10.1007/bf02544535 · Cited by 97
Self-citation
Diurnal rhythm of rat liver mRNAs encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase. Correlation of functional and total mRNA levels with enzyme activity and protein.
Clarke, C. F., Fogelman, A. M., & Edwards, P. A. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90983-x · Cited by 96
Comparison of free α‐tocopherol and α‐tocopheryl acetate as sources of vitamin E in rats and humans
Burton, G. W., Ingold, K. U., Foster, D. O., Cheng, S. C., Webb, A. C., & Hughes, L. (1988) · Lipids · doi:10.1007/bf02536201 · Cited by 96
Regulation of the Mitochondrial Permeability Transition Pore by Ubiquinone Analogs. A Progress Report
Walter, L., Miyoshi, H., Leverve, X. M., Bernardi, P., & Fontaine, E. M. (2002) · Free Radical Research · doi:10.1080/10715760290021252 · Cited by 94
Quinone specificity of Complex I
Lenaz, G. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00028-0 · Cited by 93
Dietary Coenzyme Q10 and Vitamin E Alter the Status of These Compounds in Rat Tissues and Mitochondria
Ibrahim, W. H., Chow, C. K., Bhagavan, H. N., & Chopra, R. K. (2000) · Journal of Nutrition · doi:10.1093/jn/130.9.2343 · Cited by 91
Major changes in complex I activity in mitochondria from aged rats may not be detected by direct assay of NADH:coenzyme Q reductase
Genova, M. L., Castelluccio, C., Fato, R., Castelli, G. P., Pich, M. M., Formiggini, G., Bovina, C., Marchetti, M., & Lenaz, G. (1995) · Biochemical Journal · doi:10.1042/bj3110105 · Cited by 91
The Identification of Escherichia Coli ispB (CEL) Gene Encoding the Octaprenyl Diphosphate Synthase
Asai, K., Fujisaki, S., Nishimura, Y., Nishino, T., Okada, K., Nakagawa, T., Kawamukai, M., & Matsuda, H. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1933 · Cited by 90
Effect of exercise training on tissue vitamin E and ubiquinone content
Gohil, K., Rothfuss, L., Lang, J., & Packer, L. (1987) · Journal of Applied Physiology · doi:10.1152/jappl.1987.63.4.1638 · Cited by 90
Isolation and Functional Expression of Human COQ3, a Gene Encoding a Methyltransferase Required for Ubiquinone Biosynthesis
Jonassen, T., & Clarke, C. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.17.12381 · Cited by 89
Mitochondrial coenzyme Q content and aging
Lass, A., Kwong, L. K., & Sohal, R. S. (1999) · BioFactors · doi:10.1002/biof.5520090215 · Cited by 88
Genetic and physiological analysis of the role of uncoupling proteins in human energy homeostasis
Pecqueur, C., Couplan, E., Bouillaud, F., & Ricquier, D. (2000) · Journal of Molecular Medicine · doi:10.1007/s001090000150 · Cited by 88
The molecular and cellular pathology of solar ultraviolet radiation.
Tyrrell, R. M. (1994) · PubMed · Cited by 87
Analysis of the Decaprenyl Diphosphate Synthase (dps) Gene in Fission Yeast Suggests a Role of Ubiquinone as an Antioxidant
Suzuki, K., Okada, K., Kamiya, Y., Zhu, X. F., Nakagawa, T., Kawamukai, M., & Matsuda, H. (1997) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a021614 · Cited by 86
Farnesol-induced growth inhibition in Saccharomyces cerevisiae by a cell cycle mechanism
Machida, K., Tanaka, T., Yano, Y., Otani, S., & Taniguchi, M. (1999) · Microbiology · doi:10.1099/13500872-145-2-293 · Cited by 85
Pro‐ and Antioxidant Functions of Quinones and Quinone Reductases in Mammalian Cells
Cadenas, E., Hochstein, P., & Ernster, L. (1992) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123119.ch3 · Cited by 83

Flagged first, then by citations

2 of the 323 references couldn’t be matched to a known paper.

Research works printed but not linked: 4

van Duijn, 1987, Influence of dolichols on lipid polymorphism in model membranes and the consequences for phospholipid flip-flop and vesicle fusion, Chem. Scr., 27, 95
Nobuyoshi, 1984, Levels of coenzyme Q10 in biopsies of left ventricular muscle and influence of administration of coenzyme Q10, vol. 4, 221
Kitamura, 1984, Myocardial tissue level of coenzyme Q10 in patients with cardiac failure, vol. 4, 243
J. Grünler, Compartmentalization of lipid metabolism in rat liver, PhD thesis. Stockholm University, 2000.

Sorted by citations

Targeting Ferroptosis as a Vulnerability in Cancer
Lei, G., Zhuang, L., & Gan, B. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-022-00459-0 · Cited by 2,252
A review on antioxidants, prooxidants and related controversy: Natural and synthetic compounds, screening and analysis methodologies and future perspectives
Carocho, M., & Ferreira, I. C. F. R. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2012.09.021 · Cited by 1,661
Studies on free radicals, antioxidants, and co-factors.
Rahman, K. (2007) · PubMed Central · Cited by 983
Mitochondrial Dysfunction in Diabetes: From Molecular Mechanisms to Functional Significance and Therapeutic Opportunities
Sivitz, W. I., & Yorek, M. A. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2531 · Cited by 742
mTORC1 couples cyst(e)ine availability with GPX4 protein synthesis and ferroptosis regulation
Zhang, Y., Swanda, R. V., Nie, L., Liu, X., Wang, C., Lee, H., Lei, G., Mao, C., Koppula, P., Cheng, W., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21841-w · Cited by 724

See all 1,026

Authors: Turunen, M., Olsson, J., & Dallner, G.
Affiliations: Karolinska University Hospital (SE)
Karolinska Institutet (SE)
Stockholm University (SE)
Corresponding author: Dallner, Gustav
Venue: Biochimica et Biophysica Acta (BBA) - Biomembranes
Publisher: Elsevier BV
Published: 2004-01
Volume: 1660
Issue: 1-2
Pages: 171-199
ISSN: 0005-2736 (ISSN-L)
DOI: 10.1016/j.bbamem.2003.11.012
OpenAlex: W1971714188
Cited by: 1,026
References: 323
Citations by year: 2026: 20 · 2025: 36 · 2024: 34 · 2023: 47 · 2022: 63 · 2021: 61 · 2020: 71 · 2019: 49 · 2018: 46 · 2017: 47 · 2016: 49 · 2015: 72 · 2014: 55 · 2013: 44 · 2012: 43
FWCI: 8.73
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3486 d)
Locations: Biochimica et Biophysica Acta (BBA) - Biomembranes (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
Keywords: coenzyme Q10, mitochondrial respiratory chain, coenzyme Q biosynthesis, cellular metabolism, nuclear transcription factors, nuclear receptors, signal transduction, aging, membrane localization
MeSH terms: Aging, Animals, Biological Transport, Diet, Escherichia coli, Half-Life, Humans, Mevalonic Acid, Oxidation-Reduction, Terpenes, Tissue Distribution, Ubiquinone, Models, Animal

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

Metabolism and function of coenzyme Q

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks