The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The gene symbol clk-1 unambiguously corresponds to the Caenorhabditis elegans Clock abnormal protein 1, also known as ubiquinone biosynthesis monooxygenase COQ7 (UniProt: P48376). This protein belongs to the COQ7 family of diiron carboxylate hydroxylases and contains the expected Ferritin-like superfamily fold (IPR009078) and the Ubq_synth_Coq7 domain (IPR011566; PF03232). The gene is encoded at locus ZC395.2 and is orthologous to yeast COQ7/CAT5, mouse Mclk1, and human COQ7 (wang2013moleculargeneticsof pages 4-6, jonassen1998yeastclk1homologue pages 1-1).
The following table summarizes the core properties of CLK-1:
| Property | Details/Description |
|---|---|
| Gene name | clk-1 (C. elegans clock abnormal protein 1 / COQ7 ortholog) (wang2013moleculargeneticsof pages 4-6, jonassen1998yeastclk1homologue pages 1-1) |
| UniProt accession | P48376 |
| Protein name | NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial; also called protein CLK-1 or ubiquinone biosynthesis monooxygenase COQ7 (wang2013moleculargeneticsof pages 6-7, stefely2017biochemistryofmitochondrial pages 21-22) |
| Enzymatic function | Catalyzes hydroxylation of demethoxyubiquinone during coenzyme Q biosynthesis; in C. elegans, loss of clk-1 prevents endogenous UQ9 production and causes DMQ9 accumulation, establishing CLK-1 as the DMQ hydroxylase step in the pathway (wang2013moleculargeneticsof pages 6-7, haynes2022mitochondrialdysfunctionaging pages 1-2, haynes2022mitochondrialdysfunctionaging pages 12-12) |
| EC number | EC 1.14.13.253 |
| Substrate | DMQ9 / 5-demethoxyubiquinone-9 (demethoxyubiquinone precursor of ubiquinone-9) (wang2013moleculargeneticsof pages 6-7, haynes2022mitochondrialdysfunctionaging pages 1-2, wang2013moleculargeneticsof pages 12-14) |
| Product | UQ9 / ubiquinone-9 (coenzyme Q9); some descriptions also refer to formation of the hydroxylated intermediate en route to mature ubiquinone (haynes2022mitochondrialdysfunctionaging pages 1-2, haynes2022mitochondrialdysfunctionaging pages 12-12) |
| Cofactor / active site | Carboxylate-bridged diiron center that activates dioxygen for aromatic ring hydroxylation; catalytic activity is iron-sensitive and disrupted by manganese mismetallation (wang2013moleculargeneticsof pages 6-7, diessl2022manganesedrivencoqdeficiency pages 3-5, diessl2022manganesedrivencoqdeficiency pages 1-2) |
| Protein family | COQ7 family; conserved eukaryotic ubiquinone-biosynthetic hydroxylase family (wang2013moleculargeneticsof pages 4-6, jonassen1998yeastclk1homologue pages 1-1) |
| Structural features | Predicted/characterized four-helix bundle diiron protein with an additional membrane-associating helix; membrane-bound or peripherally membrane-associated hydroxylase (wang2022predictingandunderstanding pages 34-38, awad2018coenzymeq10deficiencies pages 7-8) |
| Subcellular localization | Primarily mitochondrial, associated with the inner mitochondrial membrane on the matrix side for CoQ biosynthesis; evidence also supports nuclear localization under stress/ROS conditions, where CLK-1/COQ7 may regulate gene expression (awad2018coenzymeq10deficiencies pages 7-8, lionaki2016differentialproteindistribution pages 8-9, jonassen2001adietarysource pages 5-6) |
| Pathway | Coenzyme Q (ubiquinone) biosynthesis; CLK-1/COQ7 functions in the late aromatic ring-modification steps and participates with COQ3/4/5/6/7/9 in the COQ metabolon / CoQ synthome (awad2018coenzymeq10deficiencies pages 8-10, nicoll2024invitroconstruction pages 1-2) |
| Organism | Caenorhabditis elegans (worm) |
| Orthologs | Conserved across eukaryotes: yeast Coq7p/Cat5p, mouse MCLK1, human COQ7; functional complementation data support strong conservation (haynes2022mitochondrialdysfunctionaging pages 12-12, wang2013moleculargeneticsof pages 4-6, diazcasado2019theparadoxof pages 7-9, jonassen1998yeastclk1homologue pages 1-1) |
Table: This table summarizes the core identity, enzymatic role, localization, structure, and pathway context of C. elegans CLK-1/COQ7. It is useful as a compact reference for functional annotation and for distinguishing clk-1 from unrelated similarly named genes.
CLK-1 is an NADH-dependent hydroxylase (EC 1.14.13.253) that catalyzes the hydroxylation of 5-demethoxyubiquinone-9 (DMQ9) to produce ubiquinone-9 (UQ9/coenzyme Q9) in C. elegans. This reaction represents the penultimate step in the coenzyme Q biosynthetic pathway, specifically the C5 hydroxylation of the quinone ring (wang2013moleculargeneticsof pages 6-7, stefely2017biochemistryofmitochondrial pages 21-22, haynes2022mitochondrialdysfunctionaging pages 1-2, haynes2022mitochondrialdysfunctionaging pages 12-12). Loss-of-function mutations in clk-1 (such as the qm30 null allele) abolish endogenous UQ9 production and lead to accumulation of DMQ9, the direct substrate of CLK-1, firmly establishing this enzymatic assignment (haynes2022mitochondrialdysfunctionaging pages 1-2, wang2013moleculargeneticsof pages 12-14, wang2013moleculargeneticsof pages 4-6).
CLK-1/COQ7 is a member of the carboxylate-bridged diiron protein family, which also includes methane monooxygenase, ribonucleotide reductase, and phenol hydroxylase (awad2018coenzymeq10deficiencies pages 7-8). The protein employs a diiron center to activate molecular oxygen (O₂) for the aromatic ring hydroxylation reaction. Spectroscopic characterization of the purified mouse ortholog MCLK1 confirmed the presence of this diiron center, which serves as the catalytic active site for dioxygen activation and subsequent demethoxyubiquinone hydroxylation (wang2013moleculargeneticsof pages 6-7). The enzymatic activity is sensitive to iron availability, and the diiron center can be reduced by substrate-mediated processes in the presence of NADH and oxygen. In vitro assays using substrate analogs DMQ0 and DMQ2 demonstrated binding to the diiron site and NADH-mediated reduction (stefely2017biochemistryofmitochondrial pages 21-22, awad2018coenzymeq10deficiencies pages 8-10).
COQ7 is predicted—and partially confirmed experimentally—to adopt a four-helix bundle architecture, with an additional α-helix mediating peripheral association with the mitochondrial inner membrane (wang2022predictingandunderstanding pages 34-38, awad2018coenzymeq10deficiencies pages 7-8). The iron-liganding motif has been refined as E–X₆–Y–X₂₂–E–X₂–H–X₄₈–E–X₆–Y–X₂₈–E–X₂–H, with key residues (E60, Y67, E90, H93, E142, Y149, E178, H181 in human COQ7 numbering) predicted to coordinate the two Fe(II) atoms within the bundle. However, experimentally determined structures have not yet captured metals in the active site, so the metal-liganding assignments remain based on structural analogy to other diiron proteins (wang2022predictingandunderstanding pages 34-38, wang2022predictingandunderstanding pages 38-41).
A particularly notable finding is that the diiron center of Coq7 is uniquely sensitive to manganese mismetallation. Under conditions of manganese overload, Mn²⁺ ions erroneously occupy the diiron binding sites, inactivating the enzyme and triggering its proteolytic degradation. This mismetallation selectively disrupts CoQ biosynthesis while leaving respiratory chain complexes intact, establishing Coq7 as the molecular target of manganese-induced bioenergetic failure (diessl2022manganesedrivencoqdeficiency pages 3-5, diessl2022manganesedrivencoqdeficiency pages 5-6, diessl2022manganesedrivencoqdeficiency pages 1-2, diessl2022manganesedrivencoqdeficiency pages 2-3).
The primary site of CLK-1 function is the mitochondria. CLK-1 contains a mitochondrial targeting sequence (MTS) and is peripherally associated with the inner mitochondrial membrane on the matrix side (awad2018coenzymeq10deficiencies pages 7-8, jonassen2001adietarysource pages 5-6). This localization is consistent with the established site of coenzyme Q biosynthesis in eukaryotic cells and with the mitochondrial localization of the yeast homolog Coq7p (jonassen2001adietarysource pages 5-6, jonassen1998yeastclk1homologue pages 1-1). CLK-1 is expressed ubiquitously throughout the worm, consistent with the observation that Q biosynthesis occurs in essentially all tissues (jonassen2001adietarysource pages 5-6).
Evidence supports a dual mitochondrial-nuclear distribution for CLK-1/COQ7. The protein contains nuclear localization signals in addition to its MTS, and nuclear accumulation has been observed under conditions of mitochondrial stress and elevated reactive oxygen species (ROS) (lionaki2016differentialproteindistribution pages 8-9, lionaki2016differentialproteindistribution pages 7-8). In the nucleus, CLK-1/COQ7 has been reported to bind chromatin and regulate oxidative stress response genes while suppressing genes associated with the mitochondrial unfolded protein response (UPRmt). Importantly, restricting CLK-1 exclusively to the nucleus inhibits ubiquinone biosynthesis, demonstrating that its nuclear role is distinct from its enzymatic function in the mitochondria (lionaki2016differentialproteindistribution pages 8-9). However, these nuclear "moonlighting" functions remain an area of active investigation and require further confirmation (haynes2022mitochondrialdysfunctionaging pages 12-13).
Coenzyme Q (ubiquinone) is an essential redox-active lipid composed of a benzoquinone ring and a polyisoprenyl tail. It functions primarily as a mobile electron carrier in the mitochondrial electron transport chain and as a membrane-soluble antioxidant (guerra2023coenzymeqbiochemistry pages 1-3). The biosynthesis of CoQ involves multiple enzymatic modifications of the aromatic ring, including decarboxylation, hydroxylation, and methylation reactions. CLK-1/COQ7 catalyzes the late-stage C5 hydroxylation that converts DMQ to UQ (haynes2022mitochondrialdysfunctionaging pages 12-12, guerra2023coenzymeqbiochemistry pages 3-4).
CLK-1/COQ7 does not function in isolation but rather as part of a multi-protein complex called the COQ metabolon (also termed the CoQ synthome or Complex Q). This complex comprises at least six core proteins: COQ3, COQ4, COQ5, COQ6, COQ7, and COQ9, all located at the matrix side of the inner mitochondrial membrane (awad2018coenzymeq10deficiencies pages 8-10, nicoll2024invitroconstruction pages 1-2). The metabolon coordinates sequential ring-modification reactions, facilitating substrate channeling among its component enzymes.
A landmark 2024 study by Nicoll et al. in Nature Catalysis achieved the first in vitro reconstitution of the complete COQ metabolon using ancestral sequence reconstruction, capturing the entire biosynthetic pathway in vitro and revealing enzymes responsible for previously uncharacterized steps (nicoll2024invitroconstruction pages 1-2, mattevi2023invitroconstruction pages 1-4). This work also demonstrated that COQ8, a kinase, increases and streamlines coenzyme Q production by phosphorylating metabolon components such as COQ3, thereby regulating metabolon assembly and disassembly (nicoll2024invitroconstruction pages 1-2, nicoll2024invitroconstruction pages 8-8).
A particularly well-characterized interaction within the metabolon is the COQ7:COQ9 complex. COQ9 is a lipid-binding auxiliary protein that physically associates with COQ7 and is essential for both the stability and catalytic activity of COQ7 (diazcasado2019theparadoxof pages 3-5, staiano2023biosynthesisdeficiencyand pages 4-5). The two proteins form a double heterodimer that reshapes the mitochondrial inner membrane to allow substrate accessibility to their lipid-binding sites (staiano2023biosynthesisdeficiencyand pages 4-5). COQ9 binds aromatic isoprene intermediates and is proposed to present these directly to COQ7 for hydroxylation (diazcasado2019theparadoxof pages 3-5). In COQ9-deficient cells and mice, COQ7 levels decrease and the COQ7 substrate DMQ accumulates, confirming the functional coupling of these two proteins (diazcasado2019theparadoxof pages 3-5).
clk-1 loss-of-function mutants in C. elegans display a constellation of pleiotropic phenotypes collectively described as the "Clock" (Clk) phenotype: slowed development, reduced rates of pharyngeal pumping, defecation, and swimming, as well as increased UV stress resistance and extended adult lifespan (jonassen2001adietarysource pages 5-6, jonassen1998yeastclk1homologue pages 1-1). The clk-1 mutant was among the first genetic demonstrations that mitochondrial dysfunction can paradoxically extend lifespan (haynes2022mitochondrialdysfunctionaging pages 1-1, haynes2022mitochondrialdysfunctionaging pages 12-12).
clk-1 null mutants lack endogenous UQ9 and instead accumulate its biosynthetic precursor DMQ9 (haynes2022mitochondrialdysfunctionaging pages 1-2, wang2013moleculargeneticsof pages 12-14). DMQ9 differs from UQ9 by lacking one methoxy group and appears to act as a non-functional competitor at CoQ-binding sites in mitochondrial respiratory complexes, particularly at Complex I, further reducing electron transport chain efficiency (diazcasado2019theparadoxof pages 7-9, wang2013moleculargeneticsof pages 12-14). Despite lacking endogenous UQ9, clk-1 mutants survive because they can absorb bacterial UQ8 from their E. coli food source, which partially substitutes for endogenous UQ9 but does not fully restore wild-type phenotypes (haynes2022mitochondrialdysfunctionaging pages 1-1, haynes2022mitochondrialdysfunctionaging pages 1-2). Critically, clk-1 mutant larvae die on CoQ-deficient diets, indicating that a minimum level of dietary CoQ is essential for development and fertility (diazcasado2019theparadoxof pages 7-9).
The lifespan extension in clk-1 mutants is intimately tied to deficient UQ synthesis. Treatment with 2,4-dihydroxybenzoic acid (2,4-DHB), a biosynthetic intermediate that bypasses the CLK-1 enzymatic step, rescues all clk-1 mutant phenotypes including the aging effect, even without any CLK-1 protein present (haynes2022mitochondrialdysfunctionaging pages 1-2, haynes2022mitochondrialdysfunctionaging pages 12-12). This demonstrates that all phenotypes result from the lack of UQ9 rather than from loss of any alternative CLK-1 function. The precise mechanism by which reduced UQ biosynthesis extends lifespan remains under investigation, but it is proposed to involve reduced electron flow through the respiratory chain, altered ROS production, and adaptive mitohormetic responses (diazcasado2019theparadoxof pages 7-9, haynes2022mitochondrialdysfunctionaging pages 12-12). Notably, the lifespan extension in clk-1 mutants is not suppressed by loss of the apoptotic pathway component CED-4, and in fact CED-4 loss further extends clk-1 mutant lifespan, distinguishing the clk-1 longevity mechanism from those of other mitochondrial mutants such as isp-1 and nuo-6 (haynes2022mitochondrialdysfunctionaging pages 12-13).
CLK-1/COQ7 is highly conserved across eukaryotes, from Saccharomyces cerevisiae (yeast Coq7p/Cat5p) to C. elegans (CLK-1), mouse (MCLK1), and human (COQ7) (wang2013moleculargeneticsof pages 4-6, diazcasado2019theparadoxof pages 7-9, jonassen1998yeastclk1homologue pages 1-1). Functional conservation has been demonstrated through cross-species complementation experiments: the rat and C. elegans CLK-1 homologs can rescue yeast coq7/cat5 mutants, restoring growth on nonfermentable carbon sources (jonassen1998yeastclk1homologue pages 1-1). Similarly, mammalian COQ7 cDNA can partially complement yeast coq7 mutations (wang2013moleculargeneticsof pages 4-6). Both yeast coq7 and C. elegans clk-1 mutants accumulate the same class of biosynthetic intermediate (DMQ6 and DMQ9, respectively), and heterozygous Mclk1 mice also display extended lifespan, paralleling the C. elegans phenotype (wang2013moleculargeneticsof pages 4-6, diazcasado2019theparadoxof pages 7-9). Treatment with 2,4-DHB restores UQ biosynthesis in CLK-1-deficient mouse cells and Mclk1 knockout mice, confirming conservation of the bypass mechanism (haynes2022mitochondrialdysfunctionaging pages 12-12).
Several important advances have furthered our understanding of COQ7/CLK-1:
In vitro reconstitution of the COQ metabolon (2024): Nicoll et al. used ancestral sequence reconstruction to create stable, experimentally tractable COQ proteins and achieved the first complete in vitro reconstitution of the CoQ biosynthetic metabolon, revealing the determinants of substrate channeling and the regulatory role of COQ8 kinase (nicoll2024invitroconstruction pages 1-2, mattevi2023invitroconstruction pages 1-4, nicoll2024invitroconstruction pages 8-8).
Manganese mismetallation of Coq7 (2022): Diessl et al. demonstrated that manganese overload selectively inactivates Coq7 through mismetallation of its diiron center, revealing a conserved molecular mechanism for manganese-induced bioenergetic failure (diessl2022manganesedrivencoqdeficiency pages 3-5, diessl2022manganesedrivencoqdeficiency pages 5-6, diessl2022manganesedrivencoqdeficiency pages 1-2).
COQ7:COQ9 double heterodimer characterization (2023): Staiano et al. described the COQ7–COQ9 complex as a double heterodimer that reshapes the mitochondrial inner membrane for substrate accessibility, advancing understanding of the lipid-binding and substrate delivery mechanisms (staiano2023biosynthesisdeficiencyand pages 4-5).
CoQ biochemistry review (2023): Guerra and Pagliarini provided a comprehensive review highlighting persisting knowledge gaps in CoQ biosynthesis, distribution, and transport, while emphasizing the central role of the COQ metabolon in which COQ7 participates (guerra2023coenzymeqbiochemistry pages 12-14, guerra2023coenzymeqbiochemistry pages 1-3).
C. elegans CLK-1 (UniProt P48376) is a mitochondrial diiron carboxylate hydroxylase that catalyzes the C5 hydroxylation of DMQ9 to produce UQ9, the penultimate step in coenzyme Q biosynthesis. It functions at the matrix face of the inner mitochondrial membrane as part of the COQ metabolon, in close partnership with the lipid-binding protein COQ9. Loss of CLK-1 abolishes endogenous UQ9 production, leading to pleiotropic phenotypes including slowed development and extended lifespan—effects that are entirely attributable to UQ deficiency and can be rescued by biosynthetic bypass compounds. CLK-1 is highly conserved across eukaryotes, and its diiron active site is uniquely vulnerable to manganese mismetallation. Evidence also supports a secondary, stress-responsive nuclear localization where CLK-1 may modulate gene expression, though this function requires further confirmation.
References
(wang2013moleculargeneticsof pages 4-6): Ying Wang and Siegfried Hekimi. Molecular genetics of ubiquinone biosynthesis in animals. Critical Reviews in Biochemistry and Molecular Biology, 48:69-88, Jan 2013. URL: https://doi.org/10.3109/10409238.2012.741564, doi:10.3109/10409238.2012.741564. This article has 90 citations and is from a peer-reviewed journal.
(jonassen1998yeastclk1homologue pages 1-1): Tanya Jonassen, Markus Proft, Francisca Randez-Gil, Jeffery R. Schultz, B. Noelle Marbois, Karl-Dieter Entian, and Catherine F. Clarke. Yeast clk-1 homologue (coq7/cat5) is a mitochondrial protein in coenzyme q synthesis*. The Journal of Biological Chemistry, 273:3351-3357, Feb 1998. URL: https://doi.org/10.1074/jbc.273.6.3351, doi:10.1074/jbc.273.6.3351. This article has 182 citations.
(wang2013moleculargeneticsof pages 6-7): Ying Wang and Siegfried Hekimi. Molecular genetics of ubiquinone biosynthesis in animals. Critical Reviews in Biochemistry and Molecular Biology, 48:69-88, Jan 2013. URL: https://doi.org/10.3109/10409238.2012.741564, doi:10.3109/10409238.2012.741564. This article has 90 citations and is from a peer-reviewed journal.
(stefely2017biochemistryofmitochondrial pages 21-22): Jonathan A. Stefely and David J. Pagliarini. Biochemistry of mitochondrial coenzyme q biosynthesis. Trends in biochemical sciences, 42 10:824-843, Oct 2017. URL: https://doi.org/10.1016/j.tibs.2017.06.008, doi:10.1016/j.tibs.2017.06.008. This article has 401 citations and is from a domain leading peer-reviewed journal.
(haynes2022mitochondrialdysfunctionaging pages 1-2): Cole M Haynes and Siegfried Hekimi. Mitochondrial dysfunction, aging, and the mitochondrial unfolded protein response in caenorhabditis elegans. Genetics, Nov 2022. URL: https://doi.org/10.1093/genetics/iyac160, doi:10.1093/genetics/iyac160. This article has 40 citations and is from a domain leading peer-reviewed journal.
(haynes2022mitochondrialdysfunctionaging pages 12-12): Cole M Haynes and Siegfried Hekimi. Mitochondrial dysfunction, aging, and the mitochondrial unfolded protein response in caenorhabditis elegans. Genetics, Nov 2022. URL: https://doi.org/10.1093/genetics/iyac160, doi:10.1093/genetics/iyac160. This article has 40 citations and is from a domain leading peer-reviewed journal.
(wang2013moleculargeneticsof pages 12-14): Ying Wang and Siegfried Hekimi. Molecular genetics of ubiquinone biosynthesis in animals. Critical Reviews in Biochemistry and Molecular Biology, 48:69-88, Jan 2013. URL: https://doi.org/10.3109/10409238.2012.741564, doi:10.3109/10409238.2012.741564. This article has 90 citations and is from a peer-reviewed journal.
(diessl2022manganesedrivencoqdeficiency pages 3-5): Jutta Diessl, Jens Berndtsson, Filomena Broeskamp, Lukas Habernig, Verena Kohler, Carmela Vazquez-Calvo, Arpita Nandy, Carlotta Peselj, Sofia Drobysheva, Ludovic Pelosi, F.-Nora Vögtle, Fabien Pierrel, Martin Ott, and Sabrina Büttner. Manganese-driven coq deficiency. Nature Communications, Oct 2022. URL: https://doi.org/10.1038/s41467-022-33641-x, doi:10.1038/s41467-022-33641-x. This article has 26 citations and is from a highest quality peer-reviewed journal.
(diessl2022manganesedrivencoqdeficiency pages 1-2): Jutta Diessl, Jens Berndtsson, Filomena Broeskamp, Lukas Habernig, Verena Kohler, Carmela Vazquez-Calvo, Arpita Nandy, Carlotta Peselj, Sofia Drobysheva, Ludovic Pelosi, F.-Nora Vögtle, Fabien Pierrel, Martin Ott, and Sabrina Büttner. Manganese-driven coq deficiency. Nature Communications, Oct 2022. URL: https://doi.org/10.1038/s41467-022-33641-x, doi:10.1038/s41467-022-33641-x. This article has 26 citations and is from a highest quality peer-reviewed journal.
(wang2022predictingandunderstanding pages 34-38): Sining Wang, 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, 11:2308, Nov 2022. URL: https://doi.org/10.3390/antiox11122308, doi:10.3390/antiox11122308. This article has 7 citations.
(awad2018coenzymeq10deficiencies pages 7-8): Agape M. Awad, 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, 62:361-376, Jul 2018. URL: https://doi.org/10.1042/ebc20170106, doi:10.1042/ebc20170106. This article has 185 citations and is from a peer-reviewed journal.
(lionaki2016differentialproteindistribution pages 8-9): Eirini Lionaki, Ilias Gkikas, and Nektarios Tavernarakis. Differential protein distribution between the nucleus and mitochondria: implications in aging. Frontiers in Genetics, Sep 2016. URL: https://doi.org/10.3389/fgene.2016.00162, doi:10.3389/fgene.2016.00162. This article has 57 citations and is from a peer-reviewed journal.
(jonassen2001adietarysource pages 5-6): Tanya Jonassen, Pamela L. Larsen, and Catherine F. Clarke. A dietary source of coenzyme q is essential for growth of long-lived caenorhabditis elegans clk-1 mutants. Proceedings of the National Academy of Sciences of the United States of America, 98 2:421-6, Jan 2001. URL: https://doi.org/10.1073/pnas.98.2.421, doi:10.1073/pnas.98.2.421. This article has 249 citations and is from a highest quality peer-reviewed journal.
(awad2018coenzymeq10deficiencies pages 8-10): Agape M. Awad, 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, 62:361-376, Jul 2018. URL: https://doi.org/10.1042/ebc20170106, doi:10.1042/ebc20170106. This article has 185 citations and is from a peer-reviewed journal.
(nicoll2024invitroconstruction pages 1-2): Callum R. Nicoll, Laura Alvigini, Andrea Gottinger, Domiziana Cecchini, Barbara Mannucci, Federica Corana, María Laura Mascotti, and Andrea Mattevi. In vitro construction of the coq metabolon unveils the molecular determinants of coenzyme q biosynthesis. Nature catalysis, 7:148-160, Jan 2024. URL: https://doi.org/10.1038/s41929-023-01087-z, doi:10.1038/s41929-023-01087-z. This article has 27 citations and is from a domain leading peer-reviewed journal.
(diazcasado2019theparadoxof pages 7-9): M. E. Díaz-Casado, J. Quiles, Eliana Barriocanal-Casado, Pilar González-García, Maurizio Battino, M. Battino, Maurizio Battino, L. López, and A. Varela-López. The paradox of coenzyme q10 in aging. Sep 2019. URL: https://doi.org/10.3390/nu11092221, doi:10.3390/nu11092221. This article has 105 citations.
(wang2022predictingandunderstanding pages 38-41): Sining Wang, 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, 11:2308, Nov 2022. URL: https://doi.org/10.3390/antiox11122308, doi:10.3390/antiox11122308. This article has 7 citations.
(diessl2022manganesedrivencoqdeficiency pages 5-6): Jutta Diessl, Jens Berndtsson, Filomena Broeskamp, Lukas Habernig, Verena Kohler, Carmela Vazquez-Calvo, Arpita Nandy, Carlotta Peselj, Sofia Drobysheva, Ludovic Pelosi, F.-Nora Vögtle, Fabien Pierrel, Martin Ott, and Sabrina Büttner. Manganese-driven coq deficiency. Nature Communications, Oct 2022. URL: https://doi.org/10.1038/s41467-022-33641-x, doi:10.1038/s41467-022-33641-x. This article has 26 citations and is from a highest quality peer-reviewed journal.
(diessl2022manganesedrivencoqdeficiency pages 2-3): Jutta Diessl, Jens Berndtsson, Filomena Broeskamp, Lukas Habernig, Verena Kohler, Carmela Vazquez-Calvo, Arpita Nandy, Carlotta Peselj, Sofia Drobysheva, Ludovic Pelosi, F.-Nora Vögtle, Fabien Pierrel, Martin Ott, and Sabrina Büttner. Manganese-driven coq deficiency. Nature Communications, Oct 2022. URL: https://doi.org/10.1038/s41467-022-33641-x, doi:10.1038/s41467-022-33641-x. This article has 26 citations and is from a highest quality peer-reviewed journal.
(lionaki2016differentialproteindistribution pages 7-8): Eirini Lionaki, Ilias Gkikas, and Nektarios Tavernarakis. Differential protein distribution between the nucleus and mitochondria: implications in aging. Frontiers in Genetics, Sep 2016. URL: https://doi.org/10.3389/fgene.2016.00162, doi:10.3389/fgene.2016.00162. This article has 57 citations and is from a peer-reviewed journal.
(haynes2022mitochondrialdysfunctionaging pages 12-13): Cole M Haynes and Siegfried Hekimi. Mitochondrial dysfunction, aging, and the mitochondrial unfolded protein response in caenorhabditis elegans. Genetics, Nov 2022. URL: https://doi.org/10.1093/genetics/iyac160, doi:10.1093/genetics/iyac160. This article has 40 citations and is from a domain leading peer-reviewed journal.
(guerra2023coenzymeqbiochemistry pages 1-3): Rachel M. Guerra and David J. Pagliarini. Coenzyme q biochemistry and biosynthesis. Trends in Biochemical Sciences, 48:463-476, May 2023. URL: https://doi.org/10.1016/j.tibs.2022.12.006, doi:10.1016/j.tibs.2022.12.006. This article has 142 citations and is from a domain leading peer-reviewed journal.
(guerra2023coenzymeqbiochemistry pages 3-4): Rachel M. Guerra and David J. Pagliarini. Coenzyme q biochemistry and biosynthesis. Trends in Biochemical Sciences, 48:463-476, May 2023. URL: https://doi.org/10.1016/j.tibs.2022.12.006, doi:10.1016/j.tibs.2022.12.006. This article has 142 citations and is from a domain leading peer-reviewed journal.
(mattevi2023invitroconstruction pages 1-4): Andrea Mattevi, Callum Nicoll, Laura Alvigini, Andrea Gottinger, Domiziana Cecchini, Barbara Mannucci, Federica Corana, and Maria Laura Mascotti. In vitro construction of the coq metabolon unveils the molecular determinants of coenzyme q biosynthesis. Nov 2023. URL: https://doi.org/10.21203/rs.3.rs-2845141/v1, doi:10.21203/rs.3.rs-2845141/v1.
(nicoll2024invitroconstruction pages 8-8): Callum R. Nicoll, Laura Alvigini, Andrea Gottinger, Domiziana Cecchini, Barbara Mannucci, Federica Corana, María Laura Mascotti, and Andrea Mattevi. In vitro construction of the coq metabolon unveils the molecular determinants of coenzyme q biosynthesis. Nature catalysis, 7:148-160, Jan 2024. URL: https://doi.org/10.1038/s41929-023-01087-z, doi:10.1038/s41929-023-01087-z. This article has 27 citations and is from a domain leading peer-reviewed journal.
(diazcasado2019theparadoxof pages 3-5): M. E. Díaz-Casado, J. Quiles, Eliana Barriocanal-Casado, Pilar González-García, Maurizio Battino, M. Battino, Maurizio Battino, L. López, and A. Varela-López. The paradox of coenzyme q10 in aging. Sep 2019. URL: https://doi.org/10.3390/nu11092221, doi:10.3390/nu11092221. This article has 105 citations.
(staiano2023biosynthesisdeficiencyand pages 4-5): Carmine Staiano, Laura García-Corzo, David Mantle, Nadia Turton, Lauren E. Millichap, Gloria Brea-Calvo, and Iain Hargreaves. Biosynthesis, deficiency, and supplementation of coenzyme q. Antioxidants, 12:1469, Jul 2023. URL: https://doi.org/10.3390/antiox12071469, doi:10.3390/antiox12071469. This article has 25 citations.
(haynes2022mitochondrialdysfunctionaging pages 1-1): Cole M Haynes and Siegfried Hekimi. Mitochondrial dysfunction, aging, and the mitochondrial unfolded protein response in caenorhabditis elegans. Genetics, Nov 2022. URL: https://doi.org/10.1093/genetics/iyac160, doi:10.1093/genetics/iyac160. This article has 40 citations and is from a domain leading peer-reviewed journal.
(guerra2023coenzymeqbiochemistry pages 12-14): Rachel M. Guerra and David J. Pagliarini. Coenzyme q biochemistry and biosynthesis. Trends in Biochemical Sciences, 48:463-476, May 2023. URL: https://doi.org/10.1016/j.tibs.2022.12.006, doi:10.1016/j.tibs.2022.12.006. This article has 142 citations and is from a domain leading peer-reviewed journal.