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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Plan and verification
- Target identity verification: ATP5MC1 (synonym ATP5G1) encodes the mitochondrial ATP synthase Fo subunit c1; UniProt P05496; organism: Homo sapiens. It belongs to the ATPase C chain family and carries the conserved proteolipid c-subunit domains consistent with Fo rotor subunits. This matches the requested protein description and domains and is human-specific, so no symbol ambiguity is apparent (chau2025smallscaleprotocolsto pages 1-2, tauchmannova2024variabilityofclinical pages 1-3).
| Category | Key facts | Primary sources (with year) | URL |
|---|---|---|---|
| Identity / synonyms / organism | Human gene ATP5MC1 (syn. ATP5G1); UniProt P05496; encodes the mitochondrial ATP synthase Fo subunit c1 precursor. | Chau et al., 2025 (chau2025smallscaleprotocolsto pages 1-2); Tauchmannová et al., 2024 (tauchmannova2024variabilityofclinical pages 1-3) | https://doi.org/10.1371/journal.pone.0323136, https://doi.org/10.33549/physiolres.935407 |
| Complex membership & localization | Member of F1Fo-ATP synthase (Complex V); membrane-embedded Fo domain; localizes to inner mitochondrial membrane and assembles into the rotor c-ring. | Chau et al., 2025 (chau2025smallscaleprotocolsto pages 1-2); Tauchmannová et al., 2024 (tauchmannova2024variabilityofclinical pages 1-3) | https://doi.org/10.1371/journal.pone.0323136, https://doi.org/10.33549/physiolres.935407 |
| Molecular function | Proteolipid c subunit that contributes proton-binding sites in the Fo rotor; mediates proton translocation that drives rotation of the central stalk and ATP synthesis. Conserved protonatable Glu/Asp in c-subunits (e.g., c-Glu in modeled systems) is key for proton binding. | Luo et al., 2020 (luo2020bedaquilineinhibitsthe pages 8-9); Tauchmannová et al., 2024 (tauchmannova2024variabilityofclinical pages 1-3) | https://doi.org/10.1038/s42003-020-01173-z, https://doi.org/10.33549/physiolres.935407 |
| Structural notes | Mammalian c-ring stoichiometry reported as eight c copies (c8 ring) in human/vertebrate ATP synthase; proton translocation occurs at the c-ring / subunit a interface. | Tauchmannová et al., 2024 (tauchmannova2024variabilityofclinical pages 1-3); Tauchmannová refs (tauchmannova2024variabilityofclinical pages 24-26) | https://doi.org/10.33549/physiolres.935407 |
| Inhibitors & binding region | Oligomycin A specifically inhibits Fo proton transfer (oligomycin-sensitivity conferring protein/OSCP context); diarylquinoline bedaquiline (BDQ) can bind the c-ring and inhibit mitochondrial ATP synthase with a binding site overlapping canonical Fo inhibitor pockets. | Luo et al., 2020 (luo2020bedaquilineinhibitsthe pages 8-9); Tauchmannová et al., 2024 (tauchmannova2024variabilityofclinical pages 1-3) | https://doi.org/10.1038/s42003-020-01173-z, https://doi.org/10.33549/physiolres.935407 |
| Assembly / biogenesis | Nuclear-encoded assembly factors (TMEM70, TMEM242 and others) assist rotor/c-ring assembly and incorporation of subunit c into mature Complex V; TMEM70 is a well-documented pathogenic assembly factor. | Chau et al., 2025 (chau2025smallscaleprotocolsto pages 1-2); Tauchmannová et al., 2024 (tauchmannova2024variabilityofclinical pages 1-3, tauchmannova2024variabilityofclinical pages 24-26) | https://doi.org/10.1371/journal.pone.0323136, https://doi.org/10.33549/physiolres.935407 |
| Disease relevance | Pathogenic variants in Complex V subunits/assembly factors cause variable mitochondrial encephalo-cardiomyopathies and metabolic disease; SARS-CoV-2 infection coordinately suppresses nuclear-encoded OXPHOS modules and the ATP5MC1 module was reported as down-regulated in infected human samples. | Tauchmannová et al., 2024 (tauchmannova2024variabilityofclinical pages 1-3); Guarnieri et al., 2023 (guarnieri2023coremitochondrialgenes pages 4-6) | https://doi.org/10.33549/physiolres.935407, https://doi.org/10.1126/scitranslmed.abq1533 |
| Assays / applications | Small-scale human PBMC protocols exist to measure Complex V: spectrophotometric and in-gel activities, clear-native western for assembly, and ΔΨm (TMRM) with oligomycin challenge to determine forward versus reverse operation — suitable for patient-derived samples. | Chau et al., 2025 (chau2025smallscaleprotocolsto pages 1-2) | https://doi.org/10.1371/journal.pone.0323136 |
Table: Concise reference table summarizing identity, function, structure, inhibitors, assembly factors, disease relevance (including SARS‑CoV‑2 effects), and practical assays for human ATP5MC1 (UniProt P05496), with primary sources cited for each entry.
Comprehensive research report
1) Key concepts and definitions
- Protein and complex: ATP5MC1 encodes the Fo c-subunit 1 of mitochondrial F1Fo-ATP synthase (Complex V), a multi-subunit rotary enzyme in the inner mitochondrial membrane that synthesizes ATP using the proton motive force. Human Complex V comprises 18 subunits; MT-ATP6 and MT-ATP8 are mtDNA-encoded and the remainder, including ATP5MC1, are nuclear-encoded (chau2025smallscaleprotocolsto pages 1-2, tauchmannova2024variabilityofclinical pages 1-3).
- Localization and assembly: ATP5MC1 is an integral membrane proteolipid of the Fo sector that assembles into the rotor c-ring embedded in the inner mitochondrial membrane; proton translocation occurs at the interface of the c-ring and subunit a (tauchmannova2024variabilityofclinical pages 1-3).
- Mammalian c-ring stoichiometry: In human/vertebrate ATP synthase, the c-ring contains eight copies of the c-subunit (c8 ring), a key architectural determinant of the H+/ATP coupling ratio (tauchmannova2024variabilityofclinical pages 1-3).
- Catalytic coupling: Protonation/deprotonation of a conserved acidic residue in each c-subunit (canonical Glu/Asp) drives rotation of the c-ring; rotation is mechanically coupled via the central stalk (γ, δ, ε) to conformational changes in F1 that synthesize ATP (luo2020bedaquilineinhibitsthe pages 8-9, tauchmannova2024variabilityofclinical pages 1-3).
2) Recent developments and latest research (prioritize 2023–2024)
- Structural-mechanistic updates: Recent reviews and structural syntheses emphasize a human c8 c-ring and the a–c interface as the proton conduction path; OSCP is the oligomycin sensitivity-conferring protein interacting with inhibitor-sensitive regions of Complex V (2024 review) (tauchmannova2024variabilityofclinical pages 1-3). Molecular dynamics and structural analyses modeling the acidic residue (e.g., cGlu) in the c-subunit clarify proton-binding states during inhibitor engagement and rotation (Luo 2020; provides mechanistic specifics used widely in recent analyses) (luo2020bedaquilineinhibitsthe pages 8-9).
- Disease spectrum synthesis: A 2024 systematic review catalogues variability of clinical phenotypes from isolated ATP synthase defects, spanning encephalo-cardiomyopathies and neurometabolic disease; it highlights that both mtDNA (e.g., MT-ATP6/8) and nuclear genes (including structural subunits and assembly factors such as TMEM70) are implicated (Aug 2024) (tauchmannova2024variabilityofclinical pages 1-3, tauchmannova2024variabilityofclinical pages 31-32).
- COVID-19–linked regulation: Human omics during SARS-CoV-2 infection show coordinated suppression of nuclear-encoded OXPHOS transcripts; the “ATP5MC1 module” of Complex V was reported down-regulated in human nasopharyngeal samples as viral load rose, with broader and persistent suppression of OXPHOS nuclear transcripts in heart, kidney, and liver autopsies. Some lung autopsy samples showed recovery/induction of structural Complex V genes (including ATP5MC1) post-clearance, indicating tissue- and stage-specific dynamics (Aug 2023) (guarnieri2023coremitochondrialgenes pages 4-6, guarnieri2023coremitochondrialgenes pages 6-7, guarnieri2023coremitochondrialgenes pages 1-2).
3) Current applications and real-world implementations
- Clinical/biomarker assays for Complex V in human PBMCs: A 2025 protocol suite enables small-scale measurement of Complex V activity and assembly in human peripheral blood mononuclear cells using as little as ~2×10^6 PBMCs (~2 ml blood). It combines spectrophotometric and in-gel activities, clear-native gel westerns for assembly, and ΔΨm cytochemistry with TMRM plus oligomycin challenge to infer forward (ATP synthase) versus reverse (ATPase) operation in intact cells (May 2025; methods are readily transferrable to clinical research) (chau2025smallscaleprotocolsto pages 1-2). These assays directly probe Fo function targeted by ATP5MC1 and its inhibitor sensitivity.
- Inhibitor mapping and safety pharmacology: Bedaquiline, a diarylquinoline TB drug, inhibits yeast and human mitochondrial ATP synthase by binding the Fo/c-ring region with a site that overlaps canonical Fo inhibitor pockets framed by oligomycin. This informs off-target risk and medicinal chemistry strategies to improve selectivity (Aug 2020; used in ongoing 2023–2024 analyses) (luo2020bedaquilineinhibitsthe pages 8-9).
4) Expert opinions and analysis from authoritative sources
- Assembly factors and c-ring incorporation: Authoritative methodological and clinical reviews emphasize TMEM70 as a central assembly factor whose pathogenic variants cause isolated ATP synthase deficiency; recent complex V method papers add TMEM242 among nuclear factors assisting rotor/c-ring biogenesis and incorporation of subunit c. Together they support a modular assembly model in which proper c-ring integration is rate-limiting and clinically relevant (2024–2025) (tauchmannova2024variabilityofclinical pages 1-3, tauchmannova2024variabilityofclinical pages 24-26, chau2025smallscaleprotocolsto pages 1-2).
- Clinical variability and genotype–phenotype: The 2024 Physiol Res review concludes that ATP synthase defects present with broad neurologic and cardiometabolic spectra, and that both structural subunits and assembly components contribute; IF1 regulation and OSCP interactions modulate hydrolytic activity and apoptosis susceptibility, adding layers to disease mechanisms (Aug 2024) (tauchmannova2024variabilityofclinical pages 1-3, tauchmannova2024variabilityofclinical pages 31-32).
- Infection and metabolism interface: The 2023 Sci Transl Med study provides expert synthesis that viral suppression of nuclear-encoded mitochondrial genes shifts metabolism toward glycolysis with organ-specific persistence; the inclusion of ATP5MC1 in regulated modules underscores Complex V as part of the antiviral metabolic program (Aug 2023) (guarnieri2023coremitochondrialgenes pages 4-6, guarnieri2023coremitochondrialgenes pages 1-2).
5) Relevant statistics and data from recent studies
- Composition: Human Complex V contains 18 subunits; two are mtDNA-encoded (MT-ATP6, MT-ATP8), with ATP5MC1 among the nuclear-encoded Fo subunits (chau2025smallscaleprotocolsto pages 1-2).
- Stoichiometry: Human/vertebrate c-ring stoichiometry is reported as c8 (eight copies of ATP5MC1/ATP5MC2/ATP5MC3-type c subunits per ring) (tauchmannova2024variabilityofclinical pages 1-3).
- Assay throughput: PBMC Complex V assessments can be performed from ~2×10^6 cells (~2 ml blood), enabling minimally invasive patient studies (chau2025smallscaleprotocolsto pages 1-2).
- COVID-19 transcriptional regulation: SARS-CoV-2 infection down-regulates clusters of nuclear-encoded OXPHOS genes, including an ATP5MC1 gene module in human nasopharyngeal samples; suppression in autopsy heart encompassed “virtually all OXPHOS mRNAs,” while lung showed recovery with viral clearance (Aug 2023; Sci Transl Med; URL: https://doi.org/10.1126/scitranslmed.abq1533) (guarnieri2023coremitochondrialgenes pages 4-6, guarnieri2023coremitochondrialgenes pages 6-7, guarnieri2023coremitochondrialgenes pages 1-2).
Mechanistic details specific to ATP5MC1
- Substrate/transport: The c-subunit forms part of the proton-conducting rotor; each protomer provides a conserved protonatable acidic side chain (modeled as cGlu in mechanistic studies) that transiently binds a proton from the intermembrane space, enabling rotation relative to subunit a and release toward the matrix at the a–c interface (luo2020bedaquilineinhibitsthe pages 8-9, tauchmannova2024variabilityofclinical pages 1-3).
- Inhibitors: Oligomycin A inhibits Fo proton transfer; in cell-based ΔΨm assays, oligomycin typically hyperpolarizes mitochondria when Complex V is in ATP synthase mode and depolarizes when it is operating in reverse ATPase mode. Bedaquiline can occupy overlapping c-ring inhibitor pockets analogous to oligomycin-sensitive sites, explaining mitochondrial off-target effects (chau2025smallscaleprotocolsto pages 1-2, luo2020bedaquilineinhibitsthe pages 8-9).
- Assembly and quality control: TMEM70 and TMEM242 are implicated in the assembly of the rotor and incorporation of subunit c into mature Complex V; defects in these factors compromise c-ring biogenesis and Complex V stability (chau2025smallscaleprotocolsto pages 1-2, tauchmannova2024variabilityofclinical pages 1-3, tauchmannova2024variabilityofclinical pages 24-26).
Disease relevance
- Primary ATP synthase disorders: Variants across Complex V—including mtDNA MT-ATP6/8 and nuclear-encoded structural subunits/assembly factors (e.g., TMEM70)—produce severe pediatric encephalo‑cardiomyopathy and broader neurometabolic presentations. Reviews synthesize genotype–phenotype variability and highlight diagnostic value of targeted exome/genome sequencing and functional Complex V assays (Aug 2024) (tauchmannova2024variabilityofclinical pages 1-3, tauchmannova2024variabilityofclinical pages 31-32).
- Infection-induced bioenergetic remodeling: SARS-CoV-2 induces suppression of nuclear-encoded OXPHOS genes, including ATP5MC1-module genes in human nasopharyngeal tissue, with tissue-specific persistence or recovery in autopsy organs; these data link ATP synthase subunits to systemic infection responses (Aug 2023) (guarnieri2023coremitochondrialgenes pages 4-6, guarnieri2023coremitochondrialgenes pages 6-7, guarnieri2023coremitochondrialgenes pages 1-2).
Data and source list (URLs and dates)
- Chau KY, Taanman JW, Schapira AHV. Small-scale protocols to characterize mitochondrial Complex V… PLoS One, 2025-05. https://doi.org/10.1371/journal.pone.0323136 (assays, oligomycin response, assembly factors including TMEM70/TMEM242) (chau2025smallscaleprotocolsto pages 1-2).
- Tauchmannová K et al. Variability of Clinical Phenotypes… Physiological Research, 2024-08. https://doi.org/10.33549/physiolres.935407 (human c8 ring; a–c interface; disease spectrum; TMEM70) (tauchmannova2024variabilityofclinical pages 1-3, tauchmannova2024variabilityofclinical pages 31-32).
- Guarnieri JW et al. Core mitochondrial genes are down-regulated during SARS-CoV-2 infection… Sci Transl Med, 2023-08. https://doi.org/10.1126/scitranslmed.abq1533 (ATP5MC1 module down-regulation; tissue-specific patterns) (guarnieri2023coremitochondrialgenes pages 4-6, guarnieri2023coremitochondrialgenes pages 6-7, guarnieri2023coremitochondrialgenes pages 1-2).
- Luo M et al. Bedaquiline inhibits the yeast and human mitochondrial ATP synthases. Commun Biol, 2020-08. https://doi.org/10.1038/s42003-020-01173-z (c-ring inhibitor site overlap; modeled c-subunit acidic residue; human off-target) (luo2020bedaquilineinhibitsthe pages 8-9).
- Del Dotto V et al. Variants in Human ATP Synthase Mitochondrial Genes… IJMS, 2024-02. https://doi.org/10.3390/ijms25042239 (expert review on MT-ATP6/8 variants, therapeutic outlook) (dotto2024variantsinhuman pages 24-26).
Conclusion
ATP5MC1 encodes a core proteolipid of the Fo motor that forms the human c8 rotor ring, provides the proton-binding site essential for rotary catalysis, and is a locus of inhibition by classical Fo inhibitors. Up-to-date structural, clinical, and systems-biology evidence converges on the centrality of Fo/c-ring biogenesis and regulation—via assembly factors like TMEM70/TMEM242 and context-dependent transcriptional programs (e.g., during SARS-CoV-2 infection)—in determining Complex V function in health and disease. Practical PBMC assays now permit minimally invasive assessment of Complex V activity and assembly in human samples, facilitating translational applications in ATP synthase–related disorders (chau2025smallscaleprotocolsto pages 1-2, tauchmannova2024variabilityofclinical pages 1-3, guarnieri2023coremitochondrialgenes pages 4-6).
References
(chau2025smallscaleprotocolsto pages 1-2): Kai-Yin Chau, Jan-Willem Taanman, and Anthony H.V. Schapira. Small-scale protocols to characterize mitochondrial complex v activity and assembly in peripheral blood mononuclear cells. PLOS One, 20:e0323136, May 2025. URL: https://doi.org/10.1371/journal.pone.0323136, doi:10.1371/journal.pone.0323136. This article has 2 citations and is from a peer-reviewed journal.
(tauchmannova2024variabilityofclinical pages 1-3): K. Tauchmannová, A. Pecinová, J. Houštěk, and T. Mrázek. Variability of clinical phenotypes caused by isolated defects of mitochondrial atp synthase. Physiological Research, pages S243-S278, Aug 2024. URL: https://doi.org/10.33549/physiolres.935407, doi:10.33549/physiolres.935407. This article has 9 citations and is from a peer-reviewed journal.
(luo2020bedaquilineinhibitsthe pages 8-9): Min Luo, Wenchang Zhou, Hiral Patel, Anurag P. Srivastava, Jindrich Symersky, Michał M. Bonar, José D. Faraldo-Gómez, Maofu Liao, and David M. Mueller. Bedaquiline inhibits the yeast and human mitochondrial atp synthases. Communications Biology, Aug 2020. URL: https://doi.org/10.1038/s42003-020-01173-z, doi:10.1038/s42003-020-01173-z. This article has 68 citations and is from a peer-reviewed journal.
(tauchmannova2024variabilityofclinical pages 24-26): K. Tauchmannová, A. Pecinová, J. Houštěk, and T. Mrázek. Variability of clinical phenotypes caused by isolated defects of mitochondrial atp synthase. Physiological Research, pages S243-S278, Aug 2024. URL: https://doi.org/10.33549/physiolres.935407, doi:10.33549/physiolres.935407. This article has 9 citations and is from a peer-reviewed journal.
(guarnieri2023coremitochondrialgenes pages 4-6): Joseph W. Guarnieri, Joseph M. Dybas, Hossein Fazelinia, Man S. Kim, Justin Frere, Yuanchao Zhang, Yentli Soto Albrecht, Deborah G. Murdock, Alessia Angelin, Larry N. Singh, Scott L. Weiss, Sonja M. Best, Marie T. Lott, Shiping Zhang, Henry Cope, Victoria Zaksas, Amanda Saravia-Butler, Cem Meydan, Jonathan Foox, Christopher Mozsary, Yaron Bram, Yared Kidane, Waldemar Priebe, Mark R. Emmett, Robert Meller, Sam Demharter, Valdemar Stentoft-Hansen, Marco Salvatore, Diego Galeano, Francisco J. Enguita, Peter Grabham, Nidia S. Trovao, Urminder Singh, Jeffrey Haltom, Mark T. Heise, Nathaniel J. Moorman, Victoria K. Baxter, Emily A. Madden, Sharon A. Taft-Benz, Elizabeth J. Anderson, Wes A. Sanders, Rebekah J. Dickmander, Stephen B. Baylin, Eve Syrkin Wurtele, Pedro M. Moraes-Vieira, Deanne Taylor, Christopher E. Mason, Jonathan C. Schisler, Robert E. Schwartz, Afshin Beheshti, and Douglas C. Wallace. Core mitochondrial genes are down-regulated during sars-cov-2 infection of rodent and human hosts. Science Translational Medicine, Aug 2023. URL: https://doi.org/10.1126/scitranslmed.abq1533, doi:10.1126/scitranslmed.abq1533. This article has 177 citations and is from a highest quality peer-reviewed journal.
(tauchmannova2024variabilityofclinical pages 31-32): K. Tauchmannová, A. Pecinová, J. Houštěk, and T. Mrázek. Variability of clinical phenotypes caused by isolated defects of mitochondrial atp synthase. Physiological Research, pages S243-S278, Aug 2024. URL: https://doi.org/10.33549/physiolres.935407, doi:10.33549/physiolres.935407. This article has 9 citations and is from a peer-reviewed journal.
(guarnieri2023coremitochondrialgenes pages 6-7): Joseph W. Guarnieri, Joseph M. Dybas, Hossein Fazelinia, Man S. Kim, Justin Frere, Yuanchao Zhang, Yentli Soto Albrecht, Deborah G. Murdock, Alessia Angelin, Larry N. Singh, Scott L. Weiss, Sonja M. Best, Marie T. Lott, Shiping Zhang, Henry Cope, Victoria Zaksas, Amanda Saravia-Butler, Cem Meydan, Jonathan Foox, Christopher Mozsary, Yaron Bram, Yared Kidane, Waldemar Priebe, Mark R. Emmett, Robert Meller, Sam Demharter, Valdemar Stentoft-Hansen, Marco Salvatore, Diego Galeano, Francisco J. Enguita, Peter Grabham, Nidia S. Trovao, Urminder Singh, Jeffrey Haltom, Mark T. Heise, Nathaniel J. Moorman, Victoria K. Baxter, Emily A. Madden, Sharon A. Taft-Benz, Elizabeth J. Anderson, Wes A. Sanders, Rebekah J. Dickmander, Stephen B. Baylin, Eve Syrkin Wurtele, Pedro M. Moraes-Vieira, Deanne Taylor, Christopher E. Mason, Jonathan C. Schisler, Robert E. Schwartz, Afshin Beheshti, and Douglas C. Wallace. Core mitochondrial genes are down-regulated during sars-cov-2 infection of rodent and human hosts. Science Translational Medicine, Aug 2023. URL: https://doi.org/10.1126/scitranslmed.abq1533, doi:10.1126/scitranslmed.abq1533. This article has 177 citations and is from a highest quality peer-reviewed journal.
(guarnieri2023coremitochondrialgenes pages 1-2): Joseph W. Guarnieri, Joseph M. Dybas, Hossein Fazelinia, Man S. Kim, Justin Frere, Yuanchao Zhang, Yentli Soto Albrecht, Deborah G. Murdock, Alessia Angelin, Larry N. Singh, Scott L. Weiss, Sonja M. Best, Marie T. Lott, Shiping Zhang, Henry Cope, Victoria Zaksas, Amanda Saravia-Butler, Cem Meydan, Jonathan Foox, Christopher Mozsary, Yaron Bram, Yared Kidane, Waldemar Priebe, Mark R. Emmett, Robert Meller, Sam Demharter, Valdemar Stentoft-Hansen, Marco Salvatore, Diego Galeano, Francisco J. Enguita, Peter Grabham, Nidia S. Trovao, Urminder Singh, Jeffrey Haltom, Mark T. Heise, Nathaniel J. Moorman, Victoria K. Baxter, Emily A. Madden, Sharon A. Taft-Benz, Elizabeth J. Anderson, Wes A. Sanders, Rebekah J. Dickmander, Stephen B. Baylin, Eve Syrkin Wurtele, Pedro M. Moraes-Vieira, Deanne Taylor, Christopher E. Mason, Jonathan C. Schisler, Robert E. Schwartz, Afshin Beheshti, and Douglas C. Wallace. Core mitochondrial genes are down-regulated during sars-cov-2 infection of rodent and human hosts. Science Translational Medicine, Aug 2023. URL: https://doi.org/10.1126/scitranslmed.abq1533, doi:10.1126/scitranslmed.abq1533. This article has 177 citations and is from a highest quality peer-reviewed journal.
(dotto2024variantsinhuman pages 24-26): Valentina Del Dotto, Francesco Musiani, Alessandra Baracca, and Giancarlo Solaini. Variants in human atp synthase mitochondrial genes: biochemical dysfunctions, associated diseases, and therapies. International Journal of Molecular Sciences, 25:2239, Feb 2024. URL: https://doi.org/10.3390/ijms25042239, doi:10.3390/ijms25042239. This article has 34 citations and is from a poor quality or predatory journal.