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Relevant bibliographies by topics / Coenzyme Q

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Academic literature on the topic 'Coenzyme Q'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Coenzyme Q"

1

Matthews, P. M., and D. L. Arnold. "Coenzyme Q." Neurology 43, no. 3, Part 1 (March 1, 1993): 628. http://dx.doi.org/10.1212/wnl.43.3_part_1.628.

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Bendahan, D., G. K. Ribbens, and P. J. Cozzone. "Coenzyme Q." Neurology 43, no. 3, Part 1 (March 1, 1993): 628. http://dx.doi.org/10.1212/wnl.43.3_part_1.628-a.

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Mortensen, Svend Aage. "Coenzyme Q 10." JACC: Heart Failure 3, no. 3 (March 2015): 270–71. http://dx.doi.org/10.1016/j.jchf.2014.12.006.

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Comhair, Suzy A. A., Deepa Grandon, Anam Khan, Renliang Zhang, Stanley L. Hazen, and Serpil C. Erzurum. "Coenzyme Q in Asthma." American Journal of Respiratory and Critical Care Medicine 191, no. 11 (June 2015): 1336–38. http://dx.doi.org/10.1164/rccm.201412-2259le.

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Morré, D. James, and Dorothy M. Morré. "Non-mitochondrial coenzyme Q." BioFactors 37, no. 5 (June 14, 2011): 355–60. http://dx.doi.org/10.1002/biof.156.

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Finsterer, Josef, and Sinda Zarrouk-Mahjoub. "Causes of low muscle coenzyme-Q levels beyond primary coenzyme-Q-deficiency." Molecular Genetics and Metabolism Reports 15 (June 2018): 96–97. http://dx.doi.org/10.1016/j.ymgmr.2018.03.006.

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Enriquez, José Antonio, and Giorgio Lenaz. "Coenzyme Q and the Respiratory Chain: Coenzyme Q Pool and Mitochondrial Supercomplexes." Molecular Syndromology 5, no. 3-4 (2014): 119–40. http://dx.doi.org/10.1159/000363364.

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Arroyo, Antonio, Carlos Santos-Ocaña, Macarena Ruiz-Ferrer, Sergio Padilla, Ángela Gavilán, Juan C. Rodríguez-Aguilera, and Plácido Navas. "Coenzyme Q is irreplaceable by demethoxy-coenzyme Q in plasma membrane ofCaenorhabditis elegans." FEBS Letters 580, no. 7 (February 20, 2006): 1740–46. http://dx.doi.org/10.1016/j.febslet.2006.02.025.

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Beyer, Robert E. "An analysis of the role of coenzyme Q in free radical generation and as an antioxidant." Biochemistry and Cell Biology 70, no. 6 (June 1, 1992): 390–403. http://dx.doi.org/10.1139/o92-061.

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The vital role of coenzyme Q in mitochondrial electron transfer and its regulation, and in energy conservation, is well established. However, the role of coenzyme Q in free oxyradical formation and as an antioxidant remains controversial. Demonstration of the existence of the semiquinone form of coenzyme Q during electron transport, coupled with recent evidence that hydrogen peroxide (but not molecular oxygen) may act as an oxidant of the semiquinone, suggests that the highly reactive OH∙ radical may be formed from the semiquinone. On the other hand, data exist implicating the Fe–S species as the source of electron transfer chain, free radical production. Additional data exist suggesting instead that the unpaired electron of the coenzyme Q semiquinone most likely dismutates superoxide radicals. These concepts and those arising from observations at several levels of organization including subcellular systems, intact animals, and human subjects in the clinical setting, supporting the concept of reduced coenzyme Q as an antioxidant, will be presented. The results of recent studies on the interaction between the two-electron quinone reductase – DT diaphorase and coenzyme Q10 will be presented. The possibility that superoxide dismutase may interact with reduced coenzyme Q, in conjunction with DT diaphorase inhibiting its autoxidation, will be described. The regulation of cellular coenzyme Q concentrations during oxidative stress accompanying aerobic exercise, resulting in increased protection from free radical damage, will also be presented.Key words: coenzyme Q, ubiquinone, free radicals, lipid peroxidation, antioxidant, DT diaphorase, superoxide dismutase, review.

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Liancai, Zhu, Wang Bochu ., Tan Jun ., and Luo Min . "Coenzyme Q in Cancer Therapy." International Journal of Cancer Research 2, no. 3 (June 15, 2006): 290–98. http://dx.doi.org/10.3923/ijcr.2006.290.298.

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Dissertations / Theses on the topic "Coenzyme Q"

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Lunceford, Adam Lee. "The effect of coenzyme Q₁₀ supplementation on aging and disease." Diss., Restricted to subscribing institutions, 2008. http://proquest.umi.com/pqdweb?did=1692119651&sid=4&Fmt=2&clientId=1564&RQT=309&VName=PQD.

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Osonkie, Odi Christian. "Investigation of the role of monooxygenases in coenzyme q biosynthesis." Diss., Restricted to subscribing institutions, 2009. http://proquest.umi.com/pqdweb?did=1872149541&sid=12&Fmt=2&clientId=1564&RQT=309&VName=PQD.

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Ozeir, Mohammad. "Etude de la voie du coenzyme Q¦ chez la levure Saccharomyces cerevisiae." Phd thesis, Université de Grenoble, 2012. http://tel.archives-ouvertes.fr/tel-00859892.

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Le coenzyme Q (ubiquinone ou Q) est une molécule organique lipophile composée d'une benzoquinone substituée et d'une chaîne polyisoprényle contenant 6 unités chez Saccharomyces cerevisiae (Q6), 8 chez Escherichia coli (Q8) et 10 chez l'homme (Q10). Q a un rôle bien connu de transporteur d'électrons dans les chaînes respiratoires et fonctionne également comme un antioxydant membranaire. La déficience primaire en Q10 a maintenant été attribuée à des mutations dans 6 gènes de la biosynthèse de Q10 et cause des pathologies sévères. La biosynthèse de Q6 est mitochondriale et nécessite au moins 9 protéines organisées au sein d'un complexe multiprotéique chez la levure (Coq1-Coq9). L'acide 4-hydroxybenzoique (4-HB) et l'acide para-aminobenzoique (pABA) sont les deux précurseurs connus du noyau aromatique de Q6. Malgré de nombreuses recherches et l'importance cruciale de Q dans le métabolisme eucaryote, certaines étapes de la voie de biosynthèse de Q ne sont pas connues. L'étude présentée dans ce manuscrit a permis de montrer l'implication de la protéine Coq6, proposée comme étant une mono-oxygénase à flavine, dans une seule des trois réactions d'hydroxylation que compte la voie de biosynthèse de Q6: l'hydroxylation en C5. De plus, notre étude sur Coq8, une protéine kinase dont sa surexpression stabilise le complexe multiprotéique, nous a permis de confirmer les fonctions de certaines protéines Coq (Coq5, Coq7), de découvrir la fonction de Coq6 et d'éclaircir le rôle des autres (Coq4, Coq9). Nous rapportons également que des analogues hydroxylés ou méthoxylés de 4-HB et du pABA peuvent court-circuiter des étapes déficientes des mutants particuliers conduisant ainsi à la synthèse du coenzyme Q6 dans ces derniers. Ce résultat ouvre de nouvelles perspectives pour traiter les déficiences en coenzyme Q10 qui jusqu'à présent sont traitées par supplémentation en Q. Finalement, la réaction de déamination, essentielle à la biosynthèse de Q6 à partir du pABA, reste incomprise mais nos résultats suggèrent fortement l'implication de Coq6 dans cette étape.

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Billon-Grand, Geneviève. "Contribution à la taxonomie et à la phylogénie des levures apport du critère "coenzyme Q /." Grenoble 2 : ANRT, 1988. http://catalogue.bnf.fr/ark:/12148/cb376120033.

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Canh, Tran UyenPhuong. "Characterization of Coq2 and Coq7 proteins, dual function polypeptides in Saccharomyces cerevisiae coenzyme Q biosynthesis." Diss., Restricted to subscribing institutions, 2007. http://proquest.umi.com/pqdweb?did=1320942011&sid=1&Fmt=2&clientId=1564&RQT=309&VName=PQD.

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Billon-Grand, Geneviève. "Contribution à la taxonomie et à la phylogénie des levures : apport du critère "coenzyme Q"." Lyon 1, 1988. http://www.theses.fr/1988LYO10141.

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Etude taxonomique et phylogenetique des levures et plus particulierement du genre pichia. La mise au point d'une technique colorimetrique permettant la mise en evidence des nitrites et nitrates reductases demontre que l'attribution d'une valeur generique au critere assimilation des nitrates est erronee tout en lui conservant cependant une valeur interspecifique. L'utilisation de la chromatographie hplc des ubiquinones permet une approche plus fine de la taxonomie des levures

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Gomes, Fernando. "A síntese de coenzima Q e a estabilidade de DNA mitocondrial em Saccharomyces cerevisiae." Universidade de São Paulo, 2012. http://www.teses.usp.br/teses/disponiveis/42/42132/tde-19092012-103914/.

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Mutantes respiratórios de Saccharomyces cerevisiae podem apresentar uma ampla variedade de instabilidade do mtDNA. Nós analisamos diferentes classes de mutantes e observamos uma elevada instabilidade nos mutantes que não possuem a coenzima Q (CoQ) funcional. O objetivo desse trabalho foi avaliar os efeitos das alterações no estado redox da coenzima Q sobre a estabilidade do mtDNA de diferentes linhagens de S. cerevisiae. No mutante Dcoq10, que sintetiza CoQ não funcional, a inativação das NADH desidrogenases individuais Ndi1p e Nde1p, resultou numa menor instabilidade do mtDNA, acompanhada por uma diminuição na taxa de liberação de peróxido de hidrogênio (H2O2). Por outro lado, a super-expressão de Nde1p aumentou a instabilidade do mutante Dcoq10. A inativação das NADH desidrogenases na linhagem Dcoq4, deficiente na síntese da CoQ, não reduziu a instabilidade do mtDNA. Juntos, os resultados indicam que alterações no estado de oxido-redução da coenzima Q influenciam a estabilidade do mtDNA, provavelmente através da produção de espécies reativas de oxigênio.
Saccharomyces cerevisiae respiratory mutants can show a wide range of mtDNA instability. We analyze different classes of mutants and observed a higher instability among mutants lacking a functional coenzyme Q (CoQ). The aim of this study was to evaluate the effects of alterations in the redox state of coenzyme Q on the stability of mtDNA mitochondrial in different strains of Saccharomyces cerevisiae. In Dcoq10 mutant, which synthesizes CoQ nonfunctional, inactivation of individual NADH dehydrogenases Ndi1p Nde1p has shown a decreased mtDNA instability, which was accompanied by a decrement in the rate of hydrogen peroxide (H2O2) release. Moreover, overexpression of Nde1p increased instability Dcoq10 mutant. The inactivation of individual NADH dehydrogenases in Dcoq4 strain which is deficient in the synthesis of CoQ, did not reduce the instability of the mtDNA. All the results indicate that changes in the redox state of coenzyme Q influence the stability of mtDNA, probably by the production of reactive oxygen species.

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Dhanasettakorn, Khwankaew Grün Ingolf Lin Mengshi. "Coenzyme Q₁₀ content, composition, texture and physiochemical characteristics of pasta fortified with freeze-dried beef heart." Diss., Columbia, Mo. : University of Missouri--Columbia, 2008. http://hdl.handle.net/10355/6636.

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Title from PDF of title page (University of Missouri--Columbia, viewed on Mar. 15, 2010). The entire thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file; a non-technical public abstract appears in the public.pdf file. Dissertation advisors: Dr. Ingolf U. Grün, Dr. Mengshi Lin. Vita. Includes bibliographical references.

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Galinier, Anne. "Etat redox des tissus adipeux : implication dans l'obésité." Toulouse 3, 2006. http://www.theses.fr/2006TOU30038.

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Les changements de mode de vie et d'alimentation ont entraîné un développement considérable de l'obésité et des complications métaboliques tels que diabète et/ou athérosclérose. Ces désordres touchant les systèmes endocrinien, immunitaire s'accompagnent de phénomènes inflammatoires et sont associés à une obésité aux dépends du tissu adipeux viscéral. En effet, au-delà de son rôle connu de stockage énergétique sous forme de triglycérides, le tissu adipeux, infiltré de cellules de type macrophagique, est apparu comme un tissu endocrine capable de sécréter hormones et cytokines pro inflammatoires. Le rôle de la mitochondrie et plus généralement le métabolisme d'oxydo-réduction dans le tissu adipeux blanc ont été longtemps négligé mais apparaissent de plus en plus prépondérants. Le but de notre travail a été tout d'abord de développer une technique permettant le dosage de l'état redox du coenzyme Q, seul antioxydant lipophile synthétisé chez l'Homme et présent de manière obligatoire dans la chaîne respiratoire. La technique chromatographique couplée à une détection électrochimique a été validée biologiquement grâce à une approche pharmacologique permettant de moduler le flux électronique de la chaîne respiratoire mitochondriale sur des cellules en culture en augmentant (roténone, carbonyl cyanide chlorophenylhydrazone) ou en diminuant (antimycine) l'oxydation du coenzyme Q. Les modifications du statut tissulaire en coenzyme Q dans des modèles animaux, montre qu'il est un élément régulateur clef de la biologie adipocytaire, nécessaire au métabolisme oxydatif des lipides et à la dépense énergétique. .
The recent evolution of way of life and modifications of food intake involved a considerable development of obesity and associated metabolic complications, which results in co-morbid diseases such as diabetes and/or atherosclerosis. These disorders are generally associated a visceral obesity and related to the endocrine and immune systems but also to inflammatory phenomena. Indeed, beyond its well-known role as energy storage in the form of triglycerides, adipose tissues have endocrine function by secreting hormones and pro-inflammatory cytokines and contained macrophagic cells. The role of mitochondria and the redox metabolism in white adipose tissues was neglected a long time but are now emerging as crucial. To evaluate this, we first set up and validate a technique to measure coenzyme Q, the alone lipophilic antioxidant synthesized by human and an obligatory component of the respiratory chain. To achieve this goal, we used a high performance liquid chromatography-electrochemical technique and we controlled changes in redox state using various inhibitors of mitochondrial respiratory chain

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Hajj, Chehade Mahmoud. "Élucidation du rôle de nouveaux acteurs de la biosynthèse de Q8 chez Escherichia coli et caractérisation du complexe protéique de biosynthèse de Q8." Thesis, Université Grenoble Alpes (ComUE), 2015. http://www.theses.fr/2015GREAV010/document.

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Le coenzyme Q est une molécule lipophile rédox rencontrée chez les eucaryotes et chez la plupart des procaryotes. La structure de Q correspond à une benzoquinone substituée par une chaîne polyisoprényle dont la longueur varie selon les organismes. Q joue le rôle de transporteur d'électrons dans les chaînes respiratoires d'où provient la plupart de l'énergie de la cellule. La biosynthèse de Q chez la bactérie Escherichia coli comporte huit étapes et implique au moins neuf protéines (UbiA-UbiH et UbiX). Trois réactions d'hydroxylation sont nécessaires pour la biosynthèse de Q8 en conditions aérobies. Alors que les protéines UbiH et UbiF présentent des homologies de séquence avec des monooxygénases à flavine connues pour catalyser des réactions d'hydroxylation, UbiB qui a été proposée comme étant la troisième hydroxylase, présente uniquement une homologie de séquence avec des kinases. Nous rapportons dans ce travail que la protéine VisC, renommée UbiI, catalyse la réaction d'hydroxylation auparavant attribuée à UbiB. Nous avons également identifié deux nouvelles protéines (YigP et YqiC, renommées respectivement UbiJ et UbiK) importantes pour le métabolisme de Q chez Escherichia coli puisque leur mutation diminue fortement le contenu en Q des souches mutantes. Ces protéines interagissent avec la plupart des protéines connues pour participer à la biosynthèse de Q ce qui implique l'existence d'un complexe de biosynthèse de Q. En utilisant des approches biochimiques et protéomiques, nous avons pu mettre en évidence un complexe impliquant plusieurs protéines Ubi et notamment UbiJ et UbiK. Ces deux protéines semblent avoir un rôle dans l'assemblage et/ou la stabilisation de ce complexe multiprotéique. Enfin, nous nous sommes intéressés à la biosynthèse de Q dans des conditions de cultures anaérobies. Nos résultats montrent l'existence « d'hydroxylases anaérobies », inconnues à ce jour, qui remplaçent les hydroxylases aérobies UbiH, UbiI et UbiF. Grâce à une approche phylogénétique, nous identifions un gène important pour la biosynthèse de Q uniquement en conditions anaérobies suggérant une réorganisation de la biosynthèse de Q entre ces deux environnements fréquemment rencontrés par E. coli. L'ensemble de nos résultats a permis d'améliorer notre connaissance de la voie de biosynthèse procaryote de Q grâce à la découverte de nouveaux gènes impliqués dans ce processus et grâce à l'identification de la fonction moléculaire de certaines protéines
Ubiquinone (Q) is a lipophilic compound that plays an important role in electron and proton transport in the respiratory chains of Escherichia coli. Besides this important role in energy production, Q also functions as a membrane soluble antioxidant. The biosynthesis of Q8 requires eight reactions and involves at least nine proteins (UbiA-UbiH and UbiX) in Escherichia coli. Three of these reactions are hydroxylations resulting in the introduction of a hydroxyl group on carbon atoms at position 1, 5 and 6 of the aromatic ring. The C1 and C6 hydroxylation are well characterized whereas the C5 hydroxylation has been proposed to involve UbiB, a protein kinase without any sequence homology with monooxygenase. In this work, by genetic and biochemical methods we provide evidence that VisC which we renamed UbiI, displays sequence homology with monooxygenases and catalyzes the C5 hydroxylation, not UbiB. We have identified two new genes, yqiC and yigP (renammed UbiJ and UbiK) which are required only for Q8 biosynthesis in aerobic conditions. The exact role of the corresponding proteins, renamed UbiJ and UbiK, remains unknown. These proteins are able to interact with other Ubi proteins to be able to produce Q supporting the protein complex hypothesis. Our progress on the characterization of an Ubi-complex regrouping several Ubi proteins suggest that UbiJ and UbiK may fulfill functions related to the Ubi-complex stability. Mutants affected in hydroxylation steps are deficient for Q8 in aerobic conditions but recover a wild type Q8 content when grown in anaerobic conditions. This intriguing observation supports the existence of an alternative hydroxylation system independent from dioxygen which has not been characterized so far. By phylogenetic studies, we have identified a new gene in which the deletion affect the biosynthesis of Q only in anaerobic conditions suggesting a reorganization of Q biosynthesis in these two conditions. Our results has improved our knowledge of the prokaryotic Q biosynthetic pathway through the discovery of new genes involved in this process and through the identification of the molecular function of some proteins

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Books on the topic "Coenzyme Q"

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López Lluch, Guillermo, ed. Coenzyme Q in Aging. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-45642-9.

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L, Hunt Gerald, ed. The miracle nutrient: Coenzyme Q₁₀. Toronto: Bantam, 1987.

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Bliznakov, Emile G. The Miracle nutrient: Coenzyme Q subscript 10. New York: Bantam Books, 1986.

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International, Symposium on the Biomedical and Clinical Aspects of Coenzyme Q. (5th 1985 Tokyo Japan). Biomedical and clinical aspects of coenzyme Q: Volume 5 : proceedings of the Fifth International Symposium on the Biomedical and Clinical Aspects of Coenzyme Q, held in Tokyo, Japan, 24-26 October 1985. Amsterdam: Elsevier Science Publishers, 1986.

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International Symposium on the Biomedical and Clinical Aspects of Coenzyme Q. (6th 1990 Rome, Italy). Biomedical and clinical aspects of coenzyme Q, volume 6: Proceedings of the sixth International Symposium on the Biomedical and Clinical Aspects of Coenzyme Q, held in Rome, Italy, 22-24 January, 1990. Edited by Folkers Karl August, Littarru G. P, and Yamagami T. Amsterdam: Elsevier Science Publishers, 1991.

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Kagan, Valerian E., and Peter J. Quinn, eds. Coenzyme Q. CRC Press, 2000. http://dx.doi.org/10.1201/9781420036701.

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Lluch, Guillermo López. Coenzyme Q in Aging. Springer, 2020.

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Folkers, K., and T. Yamagami. Biomedical and Clinical Aspects of Coenzyme Q: Proceedings (Biomedical & Clinical Aspects of Coenzyme Q). Elsevier Science Publishing Company, 1991.

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Coenzyme Q-10 (Woodland Health Ser). Woodland Publishing, 1999.

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Biomedical & Clinical Aspects of Coenzyme Q. Elsevier Science Publishing Company, 1987.

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Book chapters on the topic "Coenzyme Q"

1

Hatefi, Youssef. "Coenzyme Q (Ubiquinone)." In Advances in Enzymology - and Related Areas of Molecular Biology, 275–328. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122709.ch5.

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Brea-Calvo, Gloria, María Alcázar-Fabra, Eva Trevisson, and Plácido Navas. "Coenzyme Q Biosynthesis Disorders." In Mitochondrial Diseases, 143–90. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-70147-5_6.

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Navas, Plácido. "The Current Coenzyme Q Science and Knowledge." In Coenzyme Q in Aging, 3–9. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-45642-9_1.

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Quiles, José L., Alfonso Varela-López, María D. Navarro-Hortal, and Maurizio Battino. "Coenzyme Q, mtDNA and Mitochondrial Dysfunction During Aging." In Coenzyme Q in Aging, 191–225. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-45642-9_10.

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Hernández-Camacho, Juan Diego. "Coenzyme Q10 and Metabolic Syndrome." In Coenzyme Q in Aging, 227–40. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-45642-9_11.

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Alcaín, Francisco J., Javier Domínguez, Mario Durán-Prado, and Julia Vaamonde. "Coenzyme Q and Age-Related Neurodegenerative Disorders: Parkinson and Alzheimer Diseases." In Coenzyme Q in Aging, 241–68. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-45642-9_12.

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Hernández-Camacho, Juan Diego, Catherine Meza-Torres, and Guillermo López-Lluch. "Immunosenescence and CoQ10." In Coenzyme Q in Aging, 269–82. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-45642-9_13.

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Vaamonde, Diana, Anthony C. Hackney, Carolina Algar-Santacruz, María José Garcia-Moreno, and Juan Manuel García-Manso. "Coenzyme Q10 in Fertility and Reproduction." In Coenzyme Q in Aging, 283–308. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-45642-9_14.

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Burón, María Isabel, Cristina Parrado, José Antonio González-Reyes, Lucía Fernández del Río, Elena Gutiérrez-Casado, Miguel Calvo-Rubio, Sandra Rodríguez-López, and José Manuel Villalba. "Caloric Restriction, Longevity and Coenzyme Q." In Coenzyme Q in Aging, 311–28. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-45642-9_15.

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Bentinger, Magnus, Gustav Dallner, Kerstin Brismar, Ewa Swiezewska, and Michael Tekle. "Age Dependent Changes of Coenzyme Q Levels and its Induction in Experimental Systems." In Coenzyme Q in Aging, 329–46. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-45642-9_16.

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Conference papers on the topic "Coenzyme Q"

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Sharp, Jacqueline, Margaret Park, Erika L. Lundgrin, Wilson Tang, James Thomas, Kewal Asosingh, Suzy Comhair, et al. "Coenzyme Q Affects Cardiac Function And Erythropoiesis In Pulmonary Arterial Hypertension." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a6738.

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Awate, Pallavi, Tulin Dadali, Ryan Ng, Saie Mogre, Anne R. Diers, Hannah Rockwell, Justice McDaniel, et al. "Abstract 3530: Coenzyme Q10 (BPM31510-IV in clinical trials) increases mitochondrial Q-pool and modulates electron transport chain function to elicit cell death in pancreatic cancer cells." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3530.

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