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Artículos de revistas sobre el tema "COQ4"

Autor: Grafiati

Publicado: 10 de marzo de 2023

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1

Yen, Hsiu-Chuan, Bing-Shian Chen, Si-Ling Yang, et al. "Levels of Coenzyme Q10 and Several COQ Proteins in Human Astrocytoma Tissues Are Inversely Correlated with Malignancy." Biomolecules 12, no. 2 (2022): 336. http://dx.doi.org/10.3390/biom12020336.

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In a previous study, we reported the alterations of primary antioxidant enzymes and decreased citrate synthase (CS) activities in different grades of human astrocytoma tissues. Here, we further investigated coenzyme Q10 (CoQ10) levels and protein levels of polyprenyl diphosphate synthase subunit (PDSS2) and several COQ proteins required for CoQ10 biosynthesis in these tissues. We found that the level of endogenous CoQ10, but not of exogenous α-tocopherol, was higher in nontumor controls than in all grades of astrocytoma tissues. The levels of COQ3, COQ5, COQ6, COQ7, COQ8A, and COQ9, but not of

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2

Gomes, Fernando, Erich B. Tahara, Cleverson Busso, Alicia J. Kowaltowski, and Mario H. Barros. "nde1 deletion improves mitochondrial DNA maintenance in Saccharomyces cerevisiae coenzyme Q mutants." Biochemical Journal 449, no. 3 (2013): 595–603. http://dx.doi.org/10.1042/bj20121432.

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Saccharomyces cerevisiae has three distinct inner mitochondrial membrane NADH dehydrogenases mediating the transfer of electrons from NADH to CoQ (coenzyme Q): Nde1p, Nde2p and Ndi1p. The active site of Ndi1p faces the matrix side, whereas the enzymatic activities of Nde1p and Nde2p are restricted to the intermembrane space side, where they are responsible for cytosolic NADH oxidation. In the present study we genetically manipulated yeast strains in order to alter the redox state of CoQ and NADH dehydrogenases to evaluate the consequences on mtDNA (mitochondrial DNA) maintenance. Interestingly

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3

Chen, Fengxiang, and Lei Yang. "The Transition Metal and Non-metal co-Doping Graphene for Oxygen Reduction Reaction Electrocatalysis: a Density Functional Theory Study." Bulletin of Science and Practice 7, no. 2 (2021): 197–207. http://dx.doi.org/10.33619/2414-2948/63/18.

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Proton exchange membrane fuel cells (PEMFCs) are vital energy-conversion devices in a hydrogen-fueled economic. In this study, we performed density functional theory (DFT) calculations to study 4e− oxygen reduction reaction process on transition metal embedded in single and double vacancies (SV and DV) in a graphene. We calculated bonding energy and adsorption energy on CoX3 (X = B, C, N, Si, P and S) and CoX4 (X = B, C, N, Si, P and S) embedded in graphene. Our DFT results indicate that formation of CoX3 is unfeasible and the formation of CoX4 is feasible. In addition, the crucial role of lig

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4

Finsterer, Josef, and Sinda Zarrouk-Mahjoub. "Mitochondrial cardioencephalopathy due to a COQ4 mutation." Molecular Genetics and Metabolism Reports 13 (December 2017): 7–8. http://dx.doi.org/10.1016/j.ymgmr.2017.07.003.

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5

Marbois, Beth, Peter Gin, Kym F. Faull, et al. "Coq3 and Coq4 Define a Polypeptide Complex in Yeast Mitochondria for the Biosynthesis of Coenzyme Q." Journal of Biological Chemistry 280, no. 21 (2005): 20231–38. http://dx.doi.org/10.1074/jbc.m501315200.

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6

Wang, Sining, Akash Jain, Noelle Alexa Novales, Audrey N. Nashner, Fiona Tran, and Catherine F. Clarke. "Predicting and Understanding the Pathology of Single Nucleotide Variants in Human COQ Genes." Antioxidants 11, no. 12 (2022): 2308. http://dx.doi.org/10.3390/antiox11122308.

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Coenzyme Q (CoQ) is a vital lipid that functions as an electron carrier in the mitochondrial electron transport chain and as a membrane-soluble antioxidant. Deficiencies in CoQ lead to metabolic diseases with a wide range of clinical manifestations. There are currently few treatments that can slow or stop disease progression. Primary CoQ10 deficiency can arise from mutations in any of the COQ genes responsible for CoQ biosynthesis. While many mutations in these genes have been identified, the clinical significance of most of them remains unclear. Here we analyzed the structural and functional

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7

Basselin, Mireille, Shannon M. Hunt, Hiam Abdala-Valencia, and Edna S. Kaneshiro. "Ubiquinone Synthesis in Mitochondrial and Microsomal Subcellular Fractions of Pneumocystis spp.: Differential Sensitivities to Atovaquone." Eukaryotic Cell 4, no. 8 (2005): 1483–92. http://dx.doi.org/10.1128/ec.4.8.1483-1492.2005.

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ABSTRACT The lung pathogen Pneumocystis spp. is the causative agent of a type of pneumonia that can be fatal in people with defective immune systems, such as AIDS patients. Atovaquone, an analog of ubiquinone (coenzyme Q [CoQ]), inhibits mitochondrial electron transport and is effective in clearing mild to moderate cases of the infection. Purified rat-derived intact Pneumocystis carinii cells synthesize de novo four CoQ homologs, CoQ7, CoQ8, CoQ9, and CoQ10, as demonstrated by the incorporation of radiolabeled precursors of both the benzoquinone ring and the polyprenyl chain. A central step in

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8

Spinazzi, Marco, Enrico Radaelli, Katrien Horré, et al. "PARL deficiency in mouse causes Complex III defects, coenzyme Q depletion, and Leigh-like syndrome." Proceedings of the National Academy of Sciences 116, no. 1 (2018): 277–86. http://dx.doi.org/10.1073/pnas.1811938116.

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The mitochondrial intramembrane rhomboid protease PARL has been implicated in diverse functions in vitro, but its physiological role in vivo remains unclear. Here we show that Parl ablation in mouse causes a necrotizing encephalomyelopathy similar to Leigh syndrome, a mitochondrial disease characterized by disrupted energy production. Mice with conditional PARL deficiency in the nervous system, but not in muscle, develop a similar phenotype as germline Parl KOs, demonstrating the vital role of PARL in neurological homeostasis. Genetic modification of two major PARL substrates, PINK1 and PGAM5,

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9

Sondheimer, Neal, Stacy Hewson, Jessie M. Cameron, et al. "Novel recessive mutations in COQ4 cause severe infantile cardiomyopathy and encephalopathy associated with CoQ 10 deficiency." Molecular Genetics and Metabolism Reports 12 (September 2017): 23–27. http://dx.doi.org/10.1016/j.ymgmr.2017.05.001.

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10

Caglayan, Ahmet Okay, Hakan Gumus, Erin Sandford, et al. "COQ4 Mutation Leads to Childhood-Onset Ataxia Improved by CoQ10 Administration." Cerebellum 18, no. 3 (2019): 665–69. http://dx.doi.org/10.1007/s12311-019-01011-x.

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11

Belogrudov, Grigory I., Peter T. Lee, Tanya Jonassen, Adam Y. Hsu, Peter Gin, and Catherine F. Clarke. "Yeast COQ4 Encodes a Mitochondrial Protein Required for Coenzyme Q Synthesis." Archives of Biochemistry and Biophysics 392, no. 1 (2001): 48–58. http://dx.doi.org/10.1006/abbi.2001.2448.

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12

Meza-Torres, Catherine, Juan Diego Hernández-Camacho, Ana Belén Cortés-Rodríguez, et al. "Resveratrol Regulates the Expression of Genes Involved in CoQ Synthesis in Liver in Mice Fed with High Fat Diet." Antioxidants 9, no. 5 (2020): 431. http://dx.doi.org/10.3390/antiox9050431.

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Resveratrol (RSV) is a bioactive natural molecule that induces antioxidant activity and increases protection against oxidative damage. RSV could be used to mitigate damages associated to metabolic diseases and aging. Particularly, RSV regulates different aspects of mitochondrial metabolism. However, no information is available about the effects of RSV on Coenzyme Q (CoQ), a central component in the mitochondrial electron transport chain. Here, we report for the first time that RSV modulates COQ genes and parameters associated to metabolic syndrome in mice. Mice fed with high fat diet (HFD) pre

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13

Ling, Tsz-ki, Chun-yiu Law, Chun-hung Ko, et al. "A common COQ4 mutation in undiagnosed mitochondrial disease: a local case series." Pathology 51 (February 2019): S112—S113. http://dx.doi.org/10.1016/j.pathol.2018.12.317.

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14

Casarin, Alberto, Jose Carlos Jimenez-Ortega, Eva Trevisson, et al. "Functional characterization of human COQ4, a gene required for Coenzyme Q10 biosynthesis." Biochemical and Biophysical Research Communications 372, no. 1 (2008): 35–39. http://dx.doi.org/10.1016/j.bbrc.2008.04.172.

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15

Brea-Calvo, Gloria, Tobias B. Haack, Daniela Karall, et al. "COQ4 Mutations Cause a Broad Spectrum of Mitochondrial Disorders Associated with CoQ10 Deficiency." American Journal of Human Genetics 96, no. 2 (2015): 309–17. http://dx.doi.org/10.1016/j.ajhg.2014.12.023.

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16

Marbois, Beth, Peter Gin, Melissa Gulmezian, and Catherine F. Clarke. "The yeast Coq4 polypeptide organizes a mitochondrial protein complex essential for coenzyme Q biosynthesis." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1791, no. 1 (2009): 69–75. http://dx.doi.org/10.1016/j.bbalip.2008.10.006.

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17

FORSGREN, Margareta, Anneli ATTERSAND, Staffan LAKE, et al. "Isolation and functional expression of human COQ2, a gene encoding a polyprenyl transferase involved in the synthesis of CoQ." Biochemical Journal 382, no. 2 (2004): 519–26. http://dx.doi.org/10.1042/bj20040261.

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The COQ2 gene in Saccharomyces cerevisiae encodes a Coq2 (p-hydroxybenzoate:polyprenyl transferase), which is required in the biosynthetic pathway of CoQ (ubiquinone). This enzyme catalyses the prenylation of p-hydroxybenzoate with an all-trans polyprenyl group. We have isolated cDNA which we believe encodes the human homologue of COQ2 from a human muscle and liver cDNA library. The clone contained an open reading frame of length 1263 bp, which encodes a polypeptide that has sequence homology with the Coq2 homologues in yeast, bacteria and mammals. The human COQ2 gene, when expressed in yeast

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18

Martín-Montalvo, Alejandro, Isabel González-Mariscal, Sergio Padilla, et al. "Respiratory-induced coenzyme Q biosynthesis is regulated by a phosphorylation cycle of Cat5p/Coq7p." Biochemical Journal 440, no. 1 (2011): 107–14. http://dx.doi.org/10.1042/bj20101422.

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CoQ6 (coenzyme Q6) biosynthesis in yeast is a well-regulated process that requires the final conversion of the late intermediate DMQ6 (demethoxy-CoQ6) into CoQ6 in order to support respiratory metabolism in yeast. The gene CAT5/COQ7 encodes the Cat5/Coq7 protein that catalyses the hydroxylation step of DMQ6 conversion into CoQ6. In the present study, we demonstrated that yeast Coq7 recombinant protein purified in bacteria can be phosphorylated in vitro using commercial PKA (protein kinase A) or PKC (protein kinase C) at the predicted amino acids Ser20, Ser28 and Thr32. The total absence of pho

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19

Bosch, Annet M., Erik-Jan Kamsteeg, Richard J. Rodenburg, et al. "Coenzyme Q10 deficiency due to a COQ4 gene defect causes childhood-onset spinocerebellar ataxia and stroke-like episodes." Molecular Genetics and Metabolism Reports 17 (December 2018): 19–21. http://dx.doi.org/10.1016/j.ymgmr.2018.09.002.

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20

Acosta Lopez, Manuel J., Eva Trevisson, Marcella Canton, et al. "Vanillic Acid Restores Coenzyme Q Biosynthesis and ATP Production in Human Cells Lacking COQ6." Oxidative Medicine and Cellular Longevity 2019 (July 10, 2019): 1–11. http://dx.doi.org/10.1155/2019/3904905.

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Coenzyme Q (CoQ), a redox-active lipid, is comprised of a quinone group and a polyisoprenoid tail. It is an electron carrier in the mitochondrial respiratory chain, a cofactor of other mitochondrial dehydrogenases, and an essential antioxidant. CoQ requires a large set of enzymes for its biosynthesis; mutations in genes encoding these proteins cause primary CoQ deficiency, a clinically and genetically heterogeneous group of diseases. Patients with CoQ deficiency often respond to oral CoQ10 supplementation. Treatment is however problematic because of the low bioavailability of CoQ10 and the poo

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21

Nishida, Ikuhisa, Ryota Yanai, Yasuhiro Matsuo, Tomohiro Kaino, and Makoto Kawamukai. "Benzoic acid inhibits Coenzyme Q biosynthesis in Schizosaccharomyces pombe." PLOS ONE 15, no. 11 (2020): e0242616. http://dx.doi.org/10.1371/journal.pone.0242616.

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Coenzyme Q (CoQ, ubiquinone) is an essential component of the electron transport system in aerobic organisms. Human type CoQ10, which has 10 units of isoprene in its quinone structure, is especially valuable as a food supplement. Therefore, studying the biosynthesis of CoQ10 is important not only for increasing metabolic knowledge, but also for improving biotechnological production. Herein, we show that Schizosaccharomyces pombe utilizes p-aminobenzoate (PABA) in addition to p-hydroxybenzoate (PHB) as a precursor for CoQ10 synthesis. We explored compounds that affect the synthesis of CoQ10 and

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22

Burgardt, Arthur, Ludovic Pelosi, Mahmoud Hajj Chehade, Volker F. Wendisch, and Fabien Pierrel. "Rational Engineering of Non-Ubiquinone Containing Corynebacterium glutamicum for Enhanced Coenzyme Q10 Production." Metabolites 12, no. 5 (2022): 428. http://dx.doi.org/10.3390/metabo12050428.

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Coenzyme Q10 (CoQ10) is a lipid-soluble compound with important physiological functions and is sought after in the food and cosmetic industries owing to its antioxidant properties. In our previous proof of concept, we engineered for CoQ10 biosynthesis the industrially relevant Corynebacterium glutamicum, which does not naturally synthesize any CoQ. Here, liquid chromatography–mass spectrometry (LC–MS) analysis identified two metabolic bottlenecks in the CoQ10 production, i.e., low conversion of the intermediate 10-prenylphenol (10P-Ph) to CoQ10 and the accumulation of isoprenologs with prenyl

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23

Eisenberg-Bord, Michal, Hui S. Tsui, Diana Antunes, et al. "The Endoplasmic Reticulum-Mitochondria Encounter Structure Complex Coordinates Coenzyme Q Biosynthesis." Contact 2 (January 2019): 251525641882540. http://dx.doi.org/10.1177/2515256418825409.

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Loss of the endoplasmic reticulum (ER)-mitochondria encounter structure (ERMES) complex that resides in contact sites between the yeast ER and mitochondria leads to impaired respiration; however, the reason for that is not clear. We find that in ERMES null mutants, there is an increase in the level of mRNAs encoding for biosynthetic enzymes of coenzyme Q6 (CoQ6), an essential electron carrier of the mitochondrial respiratory chain. We show that the mega complexes involved in CoQ6 biosynthesis (CoQ synthomes) are destabilized in ERMES mutants. This, in turn, affects the level and distribution o

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24

Awad, Agape M., Michelle C. Bradley, Lucía Fernández-del-Río, Anish Nag, Hui S. Tsui, and Catherine F. Clarke. "Coenzyme Q10 deficiencies: pathways in yeast and humans." Essays in Biochemistry 62, no. 3 (2018): 361–76. http://dx.doi.org/10.1042/ebc20170106.

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Coenzyme Q (ubiquinone or CoQ) is an essential lipid that plays a role in mitochondrial respiratory electron transport and serves as an important antioxidant. In human and yeast cells, CoQ synthesis derives from aromatic ring precursors and the isoprene biosynthetic pathway. Saccharomyces cerevisiae coq mutants provide a powerful model for our understanding of CoQ biosynthesis. This review focusses on the biosynthesis of CoQ in yeast and the relevance of this model to CoQ biosynthesis in human cells. The COQ1–COQ11 yeast genes are required for efficient biosynthesis of yeast CoQ. Expression of

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25

Widmeier, Eugen, Merlin Airik, Hannah Hugo, et al. "Treatment with 2,4-Dihydroxybenzoic Acid Prevents FSGS Progression and Renal Fibrosis in Podocyte-Specific Coq6 Knockout Mice." Journal of the American Society of Nephrology 30, no. 3 (2019): 393–405. http://dx.doi.org/10.1681/asn.2018060625.

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BackgroundAlthough studies have identified >55 genes as causing steroid-resistant nephrotic syndrome (SRNS) and localized its pathogenesis to glomerular podocytes, the disease mechanisms of SRNS remain largely enigmatic. We recently reported that individuals with mutations in COQ6, a coenzyme Q (also called CoQ10, CoQ, or ubiquinone) biosynthesis pathway enzyme, develop SRNS with sensorineural deafness, and demonstrated the beneficial effect of CoQ for maintenace of kidney function.MethodsTo study COQ6 function in podocytes, we generated a podocyte-specific Coq6 knockout mouse (Coq6podKO) m

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Dai, Ya-Nan, Kang Zhou, Dong-Dong Cao, et al. "Crystal structures and catalytic mechanism of theC-methyltransferase Coq5 provide insights into a key step of the yeast coenzyme Q synthesis pathway." Acta Crystallographica Section D Biological Crystallography 70, no. 8 (2014): 2085–92. http://dx.doi.org/10.1107/s1399004714011559.

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Saccharomyces cerevisiaeCoq5 is anS-adenosyl methionine (SAM)-dependent methyltransferase (SAM-MTase) that catalyzes the onlyC-methylation step in the coenzyme Q (CoQ) biosynthesis pathway, in which 2-methoxy-6-polyprenyl-1,4-benzoquinone (DDMQH2) is converted to 2-methoxy-5-methyl-6-polyprenyl-1,4-benzoquinone (DMQH2). Crystal structures of Coq5 were determined in the apo form (Coq5-apo) at 2.2 Å resolution and in the SAM-bound form (Coq5-SAM) at 2.4 Å resolution, representing the first pair of structures for the yeast CoQ biosynthetic enzymes. Coq5 displays a typical class I SAM-MTase struct

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27

Berenguel Hernández, Aida M., Mercedes de la Cruz, María Alcázar-Fabra, et al. "Design of High-Throughput Screening of Natural Extracts to Identify Molecules Bypassing Primary Coenzyme Q Deficiency in Saccharomyces cerevisiae." SLAS DISCOVERY: Advancing the Science of Drug Discovery 25, no. 3 (2019): 299–309. http://dx.doi.org/10.1177/2472555219877185.

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Coenzyme Q10 (CoQ10) deficiency syndrome is a rare disease included in the family of mitochondrial diseases, which is a heterogeneous group of genetic disorders characterized by defective energy production. CoQ10 biosynthesis in humans requires at least 11 gene products acting in a multiprotein complex within mitochondria. The high-throughput screening (HTS) method based on the stabilization of the CoQ biosynthesis complex (Q-synthome) produced by the COQ8 gene overexpression is proven here to be a successful method for identifying new molecules from natural extracts that are able to bypass th

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28

MacDonald, Michael J. "Stimulation of insulin release from pancreatic islets by quinones." Bioscience Reports 11, no. 3 (1991): 165–70. http://dx.doi.org/10.1007/bf01182485.

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Coenzyme Q (CoQ0) and other quinones were shown to be potent insulin secretagogues in the isolated pancreatic islet. The order of potency was CoQ0≅benzoquinone≅hydroquinonemenadione. CoQ6 and CoQ10 (ubiquinone), duroquinone and durohydroquinone did not stimulate insulin release. CoQ0's insulinotropism was enhanced in calcium-free medium and CoQ0 appeared to stimulate only the second phase of insulin release. CoQ0 inhibited inositol mono-, bis- and trisphosphate formation. Inhibitors of mitochondrial respiration (rotenone, antimycin A, FCCP and cyanide) and the calcium channel blocker verapamil

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29

Zhou, Li, Gilles Barthe, Pierre-Yves Strub, Junyi Liu, and Mingsheng Ying. "CoqQ: Foundational Verification of Quantum Programs." Proceedings of the ACM on Programming Languages 7, POPL (2023): 833–65. http://dx.doi.org/10.1145/3571222.

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CoqQ is a framework for reasoning about quantum programs in the Coq proof assistant. Its main components are: a deeply embedded quantum programming language, in which classic quantum algorithms are easily expressed, and an expressive program logic for proving properties of programs. CoqQ is foundational: the program logic is formally proved sound with respect to a denotational semantics based on state-of-art mathematical libraries (MathComp and MathComp Analysis). CoqQ is also practical: assertions can use Dirac expressions, which eases concise specifications, and proofs can exploit local and

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Bradley, Michelle C., Krista Yang, Lucía Fernández-del-Río, et al. "COQ11 deletion mitigates respiratory deficiency caused by mutations in the gene encoding the coenzyme Q chaperone protein Coq10." Journal of Biological Chemistry 295, no. 18 (2020): 6023–42. http://dx.doi.org/10.1074/jbc.ra119.012420.

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Coenzyme Q (Qn) is a vital lipid component of the electron transport chain that functions in cellular energy metabolism and as a membrane antioxidant. In the yeast Saccharomyces cerevisiae, coq1–coq9 deletion mutants are respiratory-incompetent, sensitive to lipid peroxidation stress, and unable to synthesize Q6. The yeast coq10 deletion mutant is also respiratory-deficient and sensitive to lipid peroxidation, yet it continues to produce Q6 at an impaired rate. Thus, Coq10 is required for the function of Q6 in respiration and as an antioxidant and is believed to chaperone Q6 from its site of s

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31

Zhou, Lian, Ming Li, Xing-Yu Wang, et al. "Biosynthesis of Coenzyme Q in the Phytopathogen Xanthomonas campestris via a Yeast-Like Pathway." Molecular Plant-Microbe Interactions® 32, no. 2 (2019): 217–26. http://dx.doi.org/10.1094/mpmi-07-18-0183-r.

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Coenzyme Q (CoQ) is a lipid-soluble membrane component found in organisms ranging from bacteria to mammals. The biosynthesis of CoQ has been intensively studied in Escherichia coli, where 12 genes (ubiA, -B, -C, -D, -E, -F, -G, -H, -I, -J, -K, and -X) are involved. In this study, we first investigated the putative genes for CoQ8 biosynthesis in the phytopathogen Xanthomonas campestris pv. campestris using a combination of bioinformatic, genetic, and biochemical methods. We showed that Xc_0489 (coq7Xc) encodes a di-iron carboxylate monooxygenase filling the E. coli UbiF role for hydroxylation a

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Romero-Moya, Damià, Julio Castaño, Carlos Santos-Ocaña, Plácido Navas, and Pablo Menendez. "Generation, genome edition and characterization of iPSC lines from a patient with coenzyme Q 10 deficiency harboring a heterozygous mutation in COQ4 gene." Stem Cell Research 24 (October 2017): 144–47. http://dx.doi.org/10.1016/j.scr.2016.09.007.

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Walker, Emma C., Elizabeth M. Todd, Rashmi Ramani, et al. "A novel variant in CoQ biosynthesis highly prevalent in Papua New Guinea children increases mortality following bacterial pneumonia." Journal of Immunology 206, no. 1_Supplement (2021): 52.20. http://dx.doi.org/10.4049/jimmunol.206.supp.52.20.

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Abstract To identify immune variants predisposing to severe pneumonia, we performed whole exome sequencing in a pediatric population highly susceptible to acute lower respiratory infections, identifying a candidate novel variant in the CoQ biosynthetic pathway. To evaluate the effect of this variant on immune function during bacterial pneumonia, we generated a mouse line using CRISPR-Cas9 that expresses the homologous variant in the enzyme COQ6. Interestingly, we found that the variant does not result in CoQ deficiency, as other known variants in biosynthetic proteins do, however intra-trachea

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Lapointe, Jérôme, Ying Wang, Eve Bigras, and Siegfried Hekimi. "The submitochondrial distribution of ubiquinone affects respiration in long-lived Mclk1+/− mice." Journal of Cell Biology 199, no. 2 (2012): 215–24. http://dx.doi.org/10.1083/jcb.201203090.

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Mclk1 (also known as Coq7) and Coq3 code for mitochondrial enzymes implicated in the biosynthetic pathway of ubiquinone (coenzyme Q or UQ). Mclk1+/− mice are long-lived but have dysfunctional mitochondria. This phenotype remains unexplained, as no changes in UQ content were observed in these mutants. By producing highly purified submitochondrial fractions, we report here that Mclk1+/− mice present a unique mitochondrial UQ profile that was characterized by decreased UQ levels in the inner membrane coupled with increased UQ in the outer membrane. Dietary-supplemented UQ10 was actively incorpora

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Finsterer, Josef, FulvioA Scorza, AnaC Fiorini, CarlaA Scorza, and AntonioCarlos de Almeida. "Lethal neonatal CoQ deficiency due to a COQ9 variant." Journal of Pediatric Neurosciences 13, no. 2 (2018): 286. http://dx.doi.org/10.4103/jpn.jpn_37_18.

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36

Hseu, You-Cheng, Yu-Fang Tseng, Sudhir Pandey, et al. "Coenzyme Q0 Inhibits NLRP3 Inflammasome Activation through Mitophagy Induction in LPS/ATP-Stimulated Macrophages." Oxidative Medicine and Cellular Longevity 2022 (January 7, 2022): 1–15. http://dx.doi.org/10.1155/2022/4266214.

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Coenzyme Q (CoQ) analogs with a variable number of isoprenoid units have exhibited as anti-inflammatory as well as antioxidant molecules. Using novel quinone derivative CoQ0 (2,3-dimethoxy-5-methyl-1,4-benzoquinone, zero side chain isoprenoid), we studied its molecular activities against LPS/ATP-induced inflammation and redox imbalance in murine RAW264.7 macrophages. CoQ0’s non- or subcytotoxic concentration suppressed the NLRP3 inflammasome and procaspase-1 activation, followed by downregulation of IL1β expression in LPS/ATP-stimulated RAW264.7 macrophages. Similarly, treatment of CoQ0 led to

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37

Garcia-Corzo, L., M. Luna-Sanchez, C. Doerrier, et al. "Dysfunctional Coq9 protein causes predominant encephalomyopathy associated with CoQ deficiency." Human Molecular Genetics 22, no. 6 (2012): 1233–48. http://dx.doi.org/10.1093/hmg/dds530.

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38

Wang, Wenping, Irene Liparulo, Nicola Rizzardi, et al. "Coenzyme Q Depletion Reshapes MCF-7 Cells Metabolism." International Journal of Molecular Sciences 22, no. 1 (2020): 198. http://dx.doi.org/10.3390/ijms22010198.

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Mitochondrial dysfunction plays a significant role in the metabolic flexibility of cancer cells. This study aimed to investigate the metabolic alterations due to Coenzyme Q depletion in MCF-7 cells. Method: The Coenzyme Q depletion was induced by competitively inhibiting with 4-nitrobenzoate the coq2 enzyme, which catalyzes one of the final reactions in the biosynthetic pathway of CoQ. The bioenergetic and metabolic characteristics of control and coenzyme Q depleted cells were investigated using polarographic and spectroscopic assays. The effect of CoQ depletion on cell growth was analyzed in

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Taguchi, Hideki. "Behavior of Co4+ ion in K2NiF4-type (Ca1+xSm1−x)CoO4." Solid State Sciences 9, no. 9 (2007): 869–73. http://dx.doi.org/10.1016/j.solidstatesciences.2007.01.009.

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40

Lee, Szu-Hsien, and Hsiu-Chuan Yen. "Comparison on the Roles of COQ3 and COQ7 Proteins in Maintaining Coenzyme Q 10 Levels, the Stability of Other COQ Proteins, and Mitochondrial Functions in Human Cells." Free Radical Biology and Medicine 112 (November 2017): 169–70. http://dx.doi.org/10.1016/j.freeradbiomed.2017.10.264.

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41

Yu, Yanan, Zhao Wang, Ziping Li, Xinxin Hang, and Yanfeng Bi. "Assembly of {Co14} nanoclusters from adenine-modified Co4-thiacalix[4]arene units." CrystEngComm 23, no. 24 (2021): 4382–88. http://dx.doi.org/10.1039/d1ce00440a.

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42

Mano, T., R. Sinohara, Y. Sawai, et al. "Effects of thyroid hormone on coenzyme Q and other free radical scavengers in rat heart muscle." Journal of Endocrinology 145, no. 1 (1995): 131–36. http://dx.doi.org/10.1677/joe.0.1450131.

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Abstract Active oxygen species are reported to cause organ damage. This study was therefore designed to determine the behaviour of antioxidants and free radical scavengers so as to reveal changes in animals in the hyper- and hypothyroid state. Levels of antioxidant factors (i.e. coenzyme Q (CoQ)10, CoQ9 and vitamin E) and free radical scavengers (catalase, glutathione peroxidase (GSH-PX) and superoxide dismutase (SOD)) were measured in the heart muscles of rats rendered hyper- or hypothyroid by 4 weeks of thyroxine (T4) or methimazol treatment. Serum levels of CoQ9 and total SOD were also meas

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43

Lu, Mei, Yulin Zhou, Zengge Wang, Zhongmin Xia, Jun Ren, and Qiwei Guo. "Clinical phenotype, in silico and biomedical analyses, and intervention for an East Asian population-specific c.370G>A (p.G124S) COQ4 mutation in a Chinese family with CoQ10 deficiency-associated Leigh syndrome." Journal of Human Genetics 64, no. 4 (2019): 297–304. http://dx.doi.org/10.1038/s10038-019-0563-y.

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44

De REVIERS, M. "Photopériodisme, développement testiculaire et production de spermatozoïdes chez les oiseaux domestiques." INRAE Productions Animales 9, no. 1 (1996): 35–44. http://dx.doi.org/10.20870/productions-animales.1996.9.1.4033.

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La reproduction du Coq peut être dans une large mesure contrôlée par la durée quotidienne d’éclairement. Ce sont les variations de cette durée qui permettent le mieux de maîtriser la précocité de la production de spermatozoïdes, tandis que la persistance de cette production peut, sauf cas particulier, être la plus satisfaisante en jours courts. Cette condition est donc contradictoire à la fois avec une production de spermatozoïdes précoce, qui nécessite des jours croissants, et avec le maintien d’une intensité de ponte élevée, car on ne sait l’obtenir qu’en jours longs. Comme palliatif,

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45

Lohman, D. C., F. Forouhar, E. T. Beebe, et al. "Mitochondrial COQ9 is a lipid-binding protein that associates with COQ7 to enable coenzyme Q biosynthesis." Proceedings of the National Academy of Sciences 111, no. 44 (2014): E4697—E4705. http://dx.doi.org/10.1073/pnas.1413128111.

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46

He, Cuiwen H., Letian X. Xie, Christopher M. Allan, UyenPhuong C. Tran, and Catherine F. Clarke. "Coenzyme Q supplementation or over-expression of the yeast Coq8 putative kinase stabilizes multi-subunit Coq polypeptide complexes in yeast coq null mutants." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1841, no. 4 (2014): 630–44. http://dx.doi.org/10.1016/j.bbalip.2013.12.017.

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47

He, Cuiwen, Letian Xie, Christophe Allan, UyenPhuong Tran, and Catherine Clarke. "Coenzyme Q supplementation or Over-Expression of the Yeast Coq8 Putative Kinase Stabilizes Multi-Subunit Coq Polypeptide Complexes in Yeast Coq Null Mutants." Free Radical Biology and Medicine 65 (November 2013): S125. http://dx.doi.org/10.1016/j.freeradbiomed.2013.10.705.

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48

Aydin, Deniz, Danielle C. Lohman, David J. Pagliarini, and Matteo Dal Peraro. "A Combined Computational and Experimental Study to Investigate the Role of COQ9 in Promoting COQ Biosynthesis." Biophysical Journal 114, no. 3 (2018): 460a. http://dx.doi.org/10.1016/j.bpj.2017.11.2541.

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49

Gigante, M., S. Diella, L. Santangelo, et al. "Further phenotypic heterogeneity of CoQ10 deficiency associated with steroid resistant nephrotic syndrome and novel COQ2 and COQ6 variants." Clinical Genetics 92, no. 2 (2017): 224–26. http://dx.doi.org/10.1111/cge.12960.

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50

Porplycia, Danielle, Gigi Y. Lau, Jared McDonald, Zhilin Chen, Jeffrey G. Richards, and Christopher D. Moyes. "Subfunctionalization of COX4 paralogs in fish." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 312, no. 5 (2017): R671—R680. http://dx.doi.org/10.1152/ajpregu.00479.2016.

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Cytochrome c oxidase (COX) subunit 4 has two paralogs in most vertebrates. The mammalian COX4-2 gene is hypoxia responsive, and the protein has a disrupted ATP-binding site that confers kinetic properties on COX that distinguish it from COX4-1. The structure-function of COX4-2 orthologs in other vertebrates remains uncertain. Phylogenetic analyses suggest the two paralogs arose in basal vertebrates, but COX4-2 orthologs diverged faster than COX4-1 orthologs. COX4-1/4-2 protein levels in tilapia tracked mRNA levels across tissues, and did not change in hypoxia, arguing against a role for differ

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