Gene COX5B (Cytochrome c Oxidase Subunit 5B) – Functional Annotation and Role in Human Biology OpenAI o3-deep-research-2025-06-26 94 citations 2025-11-03T22:08:56.828907

Gene COX5B (Cytochrome c Oxidase Subunit 5B) – Functional Annotation and Role in Human Biology

Overview of COX5B and Complex IV Function

COX5B encodes cytochrome c oxidase subunit 5B, a nuclear-encoded component of cytochrome c oxidase (Complex IV) in human mitochondria (www.genecards.org). Complex IV is the terminal enzyme of the mitochondrial electron transport chain, catalyzing the reduction of molecular oxygen to water as part of oxidative phosphorylation (www.genecards.org). It accepts electrons from cytochrome c and contributes to the proton electrochemical gradient across the inner mitochondrial membrane, which drives ATP synthesis (www.genecards.org). In the catalytic mechanism, electrons from reduced cytochrome c in the intermembrane space pass through the Cu_A center of subunit II and heme a of subunit I to a binuclear center (heme a3-Cu_B) in subunit I, where O₂ is reduced to H₂O using four electrons and four protons (www.genecards.org). Complex IV is thus essential for cellular respiration, producing most of the ATP in mammalian cells (pmc.ncbi.nlm.nih.gov). COX5B itself is not a catalytic subunit, but forms part of the multi-subunit Complex IV holoenzyme, which in mammals comprises 14 subunits (3 mitochondrial DNA-encoded core subunits and 11 nucleus-encoded subunits) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). The three mtDNA-encoded subunits (COX1, COX2, COX3) perform the electron transfer and proton pumping activities at the catalytic core (www.genecards.org), while COX5B and other small nuclear-encoded subunits surround the core and modulate the enzyme’s assembly and regulation (www.genecards.org) (pmc.ncbi.nlm.nih.gov). In summary, COX5B is a structural subunit of Complex IV, necessary for the complex’s stability and optimal function, even though it does not itself bind the substrate or catalyze redox chemistry.

Structural Role and Localization

Cytochrome c oxidase subunit 5B is a peripheral membrane protein located on the matrix side of the inner mitochondrial membrane (www.genecards.org). As a mitochondrially localized protein, it is synthesized in the cytosol with a targeting signal and imported into the mitochondrial matrix, where it integrates into Complex IV. COX5B is a relatively small subunit (~12.5 kDa) and is classified as a “minor” structural component of Complex IV (pmc.ncbi.nlm.nih.gov). Notably, COX5B lacks a transmembrane helix and instead attaches to the matrix-exposed surface of the enzyme (pmc.ncbi.nlm.nih.gov). High-resolution structural studies first identified COX5B (also called subunit Vb) as a distinct subunit in bovine heart cytochrome c oxidase (pmc.ncbi.nlm.nih.gov). It joins the assembling COX complex at an intermediate stage (after COX1, COX4, and COX5A have assembled), indicating an early and integral role in complex maturation (pmc.ncbi.nlm.nih.gov). Being positioned on the matrix face, COX5B is thought to contribute to the stability of the complex and potentially interact with matrix-localized factors. In summary, COX5B’s primary role is structural – it helps form the quaternary structure of Complex IV – and it localizes to the mitochondrial inner membrane (matrix side), which is exactly where Complex IV carries out the final step of the respiratory chain (www.genecards.org) (pmc.ncbi.nlm.nih.gov).

Role in Oxidative Phosphorylation and Electron Transport

As part of Complex IV, COX5B is deeply involved in oxidative phosphorylation (OXPHOS), the process by which cells convert energy from nutrients into ATP. Complex IV (cytochrome c oxidase, COX) is widely recognized as a key regulatory site of OXPHOS (pmc.ncbi.nlm.nih.gov). The protein encoded by COX5B is crucial in the final stage of the respiratory chain, where electrons are transferred to oxygen and a proton gradient is established (pmc.ncbi.nlm.nih.gov). By virtue of being a subunit of Complex IV, COX5B is associated with biological pathways including respiratory electron transport and ATP synthesis coupled to proton transport (pmc.ncbi.nlm.nih.gov). The effective operation of Complex IV requires all its subunits; even though COX5B doesn’t partake directly in the redox reaction (which is handled by COX1 and COX2’s metal centers), it is necessary for the complex to function at full capacity (www.genecards.org) (pmc.ncbi.nlm.nih.gov). Experimental evidence shows that loss or knockdown of COX5B impairs Complex IV activity and oxidative phosphorylation. For example, Galati et al. (2009) demonstrated that COX5B knockdown in a macrophage cell line led to decreased COX enzymatic activity and loss of mitochondrial membrane potential, resulting in less efficient respiration (pmc.ncbi.nlm.nih.gov). Consequently, cells with reduced COX5B experience energy deficits and often accumulate excess reactive oxygen species (ROS) due to less controlled electron flow (pmc.ncbi.nlm.nih.gov). These findings affirm that COX5B is indispensable for normal mitochondrial electron transport and ATP production, serving as a supporting subunit that maintains the integrity and efficiency of Complex IV.

Assembly and Stability of Complex IV

Beyond its structural presence, COX5B plays a critical role in the assembly and maintenance of the cytochrome c oxidase complex. The biogenesis of Complex IV is a coordinated, multi-step process requiring the stepwise addition of subunits (pmc.ncbi.nlm.nih.gov) and numerous assembly factors (pmc.ncbi.nlm.nih.gov). COX5B is incorporated relatively early during assembly (with the COX2 and COX3 modules) and appears to be required for the progression to fully assembled holoenzyme (pmc.ncbi.nlm.nih.gov). When COX5B is absent or knocked down, cells accumulate assembly intermediates of COX that cannot transition to the mature complex (pmc.ncbi.nlm.nih.gov). In the study by Galati et al. (2009), reducing COX5B levels caused unfinished COX subassemblies to build up and overall Complex IV deficiency (pmc.ncbi.nlm.nih.gov). This assembly defect directly correlated with reduced electron transport activity, linking COX5B to the proper construction of the enzyme. Consistently, COX5B is considered one of the stoichiometric COX subunits required for holoenzyme stability (pmc.ncbi.nlm.nih.gov). It is not merely a passive structural element; rather, it ensures that the catalytic core subunits (COX1/2/3) are correctly incorporated and stabilized within the inner membrane. The importance of COX5B is underscored by the fact that pathogenic mutations or loss of other COX assembly factors often cause severe COX deficiency disorders (pmc.ncbi.nlm.nih.gov) – while no disease-causing mutation in COX5B itself has been definitively identified in humans to date, experimental knockdowns mimicking loss of COX5B produce clear mitochondrial dysfunction (pmc.ncbi.nlm.nih.gov). In summary, COX5B is required for efficient Complex IV assembly, acting as a scaffold or chaperoning subunit that helps the enzyme achieve its functional conformation (pmc.ncbi.nlm.nih.gov).

Regulation and Interactions

Though the core catalytic function of Complex IV resides in the mtDNA-encoded subunits, COX5B (as a nuclear-encoded subunit) contributes to regulatory fine-tuning of the enzyme. Nuclear COX subunits in general are not essential for catalysis but can modulate activity under different physiological conditions (pmc.ncbi.nlm.nih.gov). COX5B, in particular, has been implicated in multiple regulatory interactions. Early evidence of this came from Yang et al. (1998), who discovered a protein–protein interaction between COX5B and the regulatory subunit of protein kinase A (PKA) (pmc.ncbi.nlm.nih.gov). The PKA-R subunit can bind COX5B on the matrix side of the inner membrane, and this association was found to inhibit cytochrome c oxidase activity (pmc.ncbi.nlm.nih.gov). This suggests that cellular signaling pathways (like the cAMP/PKA pathway) may dynamically regulate respiration by targeting COX5B, thereby adjusting COX activity in response to cellular energy demands or signals. Another striking regulatory role for COX5B was reported in the context of innate immunity. Zhao et al. (2012) showed that COX5B physically interacts with MAVS (mitochondrial antiviral signaling protein) on the mitochondrial outer membrane and negatively regulates antiviral signaling (pmc.ncbi.nlm.nih.gov). Mechanistically, during viral infection MAVS triggers increased ROS production as part of the antiviral response, and COX5B expression itself is upregulated by MAVS activation (pmc.ncbi.nlm.nih.gov). In turn, COX5B dampens MAVS-mediated signaling by reducing ROS levels and coordinating with the autophagy machinery to limit MAVS aggregation (pmc.ncbi.nlm.nih.gov). Through this feedback loop, COX5B links the status of the electron transport chain to immune signaling, preventing excessive ROS and apoptosis during antiviral defense. These examples highlight that COX5B serves as more than a static structural subunit – it is integrated into broader cellular networks, responding to and modulating signals. By interacting with signaling proteins (e.g. PKA, MAVS) and influencing ROS generation, COX5B helps balance metabolic activity with cell signaling and stress responses. Such findings underscore an emerging view that respiratory chain components can have “moonlighting” roles in regulation, with COX5B acting as one node where mitochondrial function and signaling pathways converge (pmc.ncbi.nlm.nih.gov).

Biological Processes and Pathways

COX5B’s activity is tied to major biological processes centered on energy metabolism. It is directly involved in the mitochondrial respiratory electron transport chain, functioning in the oxidation of NADH/FADH₂ and reduction of O₂ via Complex IV (www.genecards.org). Consequently, COX5B impacts ATP synthesis (since proton pumping by Complex IV drives the ATP synthase) and is essential for maintaining normal cellular ATP levels. Gene ontology annotations link COX5B to oxidative phosphorylation and metabolic processes that generate cellular energy (pmc.ncbi.nlm.nih.gov). Additionally, because of its influence on electron flow and proton pumping efficiency, COX5B has downstream effects on reactive oxygen species homeostasis. Proper COX5B function helps minimize electron leakage that can form superoxide, thus preventing excessive ROS production inside mitochondria (pmc.ncbi.nlm.nih.gov). This is consistent with observations that COX5B knockdown leads to elevated ROS and oxidative stress in cells (pmc.ncbi.nlm.nih.gov). Furthermore, COX5B’s newly recognized connection to the MAVS antiviral pathway places it in the context of innate immune response signaling (pmc.ncbi.nlm.nih.gov). By modulating ROS and interacting with MAVS, COX5B indirectly participates in the pathway leading to type I interferon production during viral infection. There is also evidence that COX5B, through effects on mitochondrial function, can influence apoptotic pathways. For instance, a recent 2023 study of breast cancer genomics noted that COX5B interacts with networks regulating both intrinsic and extrinsic apoptosis, potentially as a positive regulator of those pathways when highly expressed (www.mdpi.com) (www.mdpi.com). In summary, COX5B operates at a critical hub of cellular physiology – it is integral to energy production (respiratory chain and ATP generation), and its functional state can affect oxidative stress levels, metabolic signaling, and even cell fate decisions like apoptosis.

Experimental Evidence of COX5B Function

Multiple experimental studies have illuminated COX5B’s functional importance. Galati et al. (2009) provided direct evidence that COX5B is required for normal Complex IV activity: siRNA-mediated COX5B knockdown in cells caused a significant drop in cytochrome c oxidase enzymatic activity and mitochondrial membrane potential, while ROS levels increased due to impaired electron transport (pmc.ncbi.nlm.nih.gov). This experiment demonstrated causally that COX5B is essential for efficient respiration and that its loss triggers mitochondrial dysfunction. In the same study, analysis of COX assembly intermediates showed that COX5B-depleted cells accumulated partially assembled COX complexes, indicating a block in assembly without COX5B (pmc.ncbi.nlm.nih.gov). This aligns with COX5B’s role in complex maturation. Another piece of evidence from Yang et al. (1998) showed biochemically that the PKA regulatory subunit binds to COX5B and in vitro this interaction correlates with a reduction in COX activity (pmc.ncbi.nlm.nih.gov). This was one of the first indications that COX5B could mediate regulation by signaling proteins. More recently, Zhao et al. (2012) used co-immunoprecipitation to show COX5B–MAVS binding and showed that overexpression of COX5B dampened IRF3 activation and IFN-β production in virus-infected cells, consistent with COX5B suppressing excessive antiviral signaling (pmc.ncbi.nlm.nih.gov). They also found that silencing COX5B lead to heightened NF-κB/IRF3 activity and more apoptosis upon infection, due to uncontrolled ROS – reinforcing that COX5B’s normal function restrains ROS-mediated signaling damage (pmc.ncbi.nlm.nih.gov). In cellular and animal models of disease, altered COX5B expression produces notable phenotypes: Wang et al. (2024) reported that cryptorchid (undescended testis) rats have abnormally low COX5B expression in testes, and COX5B knockdown in Leydig cells led to increased apoptosis and reduced cell proliferation (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov), presumably from mitochondrial dysfunction. These experimental findings collectively confirm that COX5B is functionally required for mitochondrial energy metabolism and cell viability, and they provide mechanistic insight into how COX5B supports COX assembly, activity, and cellular homeostasis.

Clinical and Real-World Relevance

Although COX5B is fundamentally a housekeeping gene for energy metabolism, recent research has highlighted its relevance in human disease contexts. Because mitochondrial function is pivotal in numerous pathologies, changes in COX5B can have downstream effects. For instance, COX5B has attracted interest as a biomarker in cancer: several studies have found COX5B upregulated in tumors and linked to cancer progression. Gao et al. (2017) noted that high COX5B expression is associated with poor prognosis in breast cancer, and similarly Hu & Xi (2017) identified COX5B as a novel marker elevated in high-grade gliomas (pmc.ncbi.nlm.nih.gov). In clear cell renal cell carcinoma and lung adenocarcinoma, COX5B was one of the respiratory chain genes whose expression correlated with patient outcomes (pmc.ncbi.nlm.nih.gov). Functionally, cancer cell experiments suggest COX5B supports the metabolic demands of proliferating tumor cells – silencing COX5B in cancer cell lines impeded their proliferation and induced senescence due to mitochondrial dysfunction (www.mdpi.com). This has led authors to propose COX5B as a potential therapeutic target: blocking COX5B might selectively impair tumor cell metabolism and trigger cell death (www.mdpi.com) (www.mdpi.com). However, targeting a fundamental OXPHOS component is challenging, since normal cells also require COX5B; strategies would need to exploit contexts where cancer cells are uniquely dependent on high COX5B levels. In the realm of genetic disease, primary mutations in COX5B have not been definitively linked to inherited mitochondrial disorders to date (unlike mutations in some other COX subunits). Nonetheless, isolated COX deficiency is a known cause of mitochondrial myopathies, and COX5B lies within a set of nuclear genes that could potentially harbor pathogenic variants (www.genecards.org). A 2023 genomic study in breast cancer identified several somatic variants in COX5B (the highest number of variants among COX subunits examined), suggesting that genetic alterations of COX5B might contribute to disease phenotypes in at least some contexts (www.mdpi.com) (www.mdpi.com). Outside of oncology, COX5B’s role in testis physiology (as noted in cryptorchidism research) hints that it might be relevant in reproductive and developmental conditions where mitochondrial energy output is critical (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Finally, COX5B’s involvement in moderating antiviral signaling opens the door to considering how its levels or activity could influence outcomes in infections or inflammatory diseases. In summary, COX5B is garnering attention in clinical research both as a biomarker (e.g. prognostic indicator in cancers) and as a potential point of intervention to alter cellular metabolism or survival pathways. Its central position in metabolism means changes in COX5B often reflect or contribute to the physiological state of cells, making it a relevant factor in diseases linked to mitochondrial dysfunction and metabolic reprogramming.

Expert Perspectives and Current Understanding

Contemporary reviews underscore the idea that COX5B and other “accessory” subunits of Complex IV are crucial for the enzyme’s adaptability and integration into cellular function (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). While earlier annotations (circa 2008) described the nuclear-encoded COX subunits as having unknown function aside from possibly aiding assembly (www.genecards.org), recent research has provided much more clarity. As summarized by Čunátová et al. (2020), nuclear subunits like COX5B “surround the conserved catalytic core” of Complex IV and are “not crucial for catalytic function, but [they] may modulate COX activity according to various conditions.” (pmc.ncbi.nlm.nih.gov). This modulation can occur through tissue-specific expression (some COX subunits have isoforms in different tissues or developmental stages) and through post-translational interactions. Notably, COX5B in mammals exists as a single isoform expressed in all tissues (in contrast to some other subunits that have alternate isoforms) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In yeast, subunit V has two isoforms (Va and Vb) switched by oxygen availability (pmc.ncbi.nlm.nih.gov), illustrating an evolutionary strategy to tune respiration – but in humans, COX5A/5B are distinct concurrent subunits, each with a dedicated role in the holoenzyme. The current understanding is that COX5B’s presence is required for optimal COX turnover and prevention of deleterious byproducts (ROS), making it a subtle regulator of efficiency (pmc.ncbi.nlm.nih.gov). Experts also note that COX5B might be involved in the formation of respiratory supercomplexes. Complex IV can associate with Complex I and III into large supercomplex assemblies in the inner membrane, which are thought to improve electron transfer efficiency. Though COX5B has not been singled out as a unique supercomplex factor, any subunit that stabilizes COX likely promotes robust supercomplex formation; indeed, COX5B loss leads to COX instability which would compromise supercomplex integrity (pmc.ncbi.nlm.nih.gov). In the words of one recent paper, “the protein encoded by the COX5B gene is a minor structural component of cytochrome c oxidase … located on the inner mitochondrial membrane and plays a crucial role in the last stage of the respiratory chain” (pmc.ncbi.nlm.nih.gov). This concise description highlights that even a “minor” subunit like COX5B is vital for the major task of oxygen consumption and ATP generation. Going forward, research is actively investigating how modulation of COX5B (and analogous COX subunits) can affect cellular metabolism and whether this can be leveraged for therapy. For example, there is interest in small molecules or drugs that might target regulatory interfaces of COX5B (such as its binding site for the PKA subunit or other cofactors) to adjust COX activity in diseases of metabolic imbalance (pmc.ncbi.nlm.nih.gov). Another emerging perspective is the link between COX5B levels and cellular adaptation: cells under high energetic demand (like cancer cells) often ramp up expression of certain COX subunits, including COX5B (pmc.ncbi.nlm.nih.gov), to maximize respiratory capacity. Conversely, cells undergoing differentiation or stress (like in ischemia or inflammation) may alter COX5B expression as part of metabolic reprogramming (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). These expert insights all converge on the view that COX5B is integral to both the structure and adaptive function of cytochrome c oxidase, ensuring efficient energy production while allowing the enzyme to interface with the cell’s regulatory networks.

Conclusion

In summary, the human COX5B gene encodes cytochrome c oxidase subunit 5B, a crucial component of Complex IV of the mitochondrial respiratory chain. COX5B’s primary function is structural – it assembles into Complex IV on the inner mitochondrial membrane (matrix side) and is required for the enzyme’s stability and full activity (pmc.ncbi.nlm.nih.gov) (www.genecards.org). Through Complex IV, COX5B contributes to the core bioenergetic process of reducing oxygen to water and enabling ATP synthesis (www.genecards.org) (www.genecards.org). While not catalytic itself, COX5B is essential for proper assembly of the multi-subunit complex and for maintaining electron transport efficiency, thereby preventing energy failure and limiting reactive oxygen species production (pmc.ncbi.nlm.nih.gov). COX5B also partakes in specific regulatory interactions – it binds certain signaling proteins (like PKA’s regulatory subunit) and helps modulate the respiratory chain in response to cellular signals (pmc.ncbi.nlm.nih.gov). Intriguingly, COX5B provides a mechanistic link between mitochondrial function and innate immunity by interacting with MAVS to restrain antiviral signaling and mitochondrial stress (pmc.ncbi.nlm.nih.gov). Overall, COX5B operates at the intersection of metabolism and cell regulation: it anchors a vital enzymatic complex for energy production and, through that role, influences broader physiological processes. Current research continues to uncover how COX5B expression or dysfunction impacts human health – from its upregulation in aggressive cancers (supporting the high metabolic demands of tumors) (pmc.ncbi.nlm.nih.gov), to its necessity for normal tissue function as seen in reproductive and immune cell studies (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). The accumulated evidence firmly establishes COX5B as indispensable for mitochondrial oxidative phosphorylation and highlights it as a potential indicator or point of intervention in diseases involving mitochondrial dysregulation. In essence, the COX5B subunit may be “small” in size, but it plays an outsized role in enabling life’s fundamental process of energy conversion.

References: (Key references are cited in-line above with source links and line numbers for verification, including a 2020 review of COX structure/function (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov), primary research studies from 1998–2012 detailing COX5B’s regulatory interactions (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov), and recent studies up to 2024 highlighting its role in pathology (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).)

Citations

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  26. AnnotationURLCitation(end_index=8853, start_index=8692, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=crosstalk%20between%20nucleus%20and%20mitochondria,COX10%2C%20COX15%2C%20FDX2')
  27. AnnotationURLCitation(end_index=9155, start_index=9020, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=Initially%2C%20COX1%20subunit%20is%20synthesized,2A')
  28. AnnotationURLCitation(end_index=9407, start_index=9287, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=COX5B%20in%20RAW%20264,In%20addition')
  29. AnnotationURLCitation(end_index=9677, start_index=9557, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=COX5B%20in%20RAW%20264,In%20addition')
  30. AnnotationURLCitation(end_index=10060, start_index=9929, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=Nuclear,may%20modulate%20COX%20activity%20under')
  31. AnnotationURLCitation(end_index=10538, start_index=10400, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=factors%20were%20also%20found%20and,2004%20%2C%20%2029')
  32. AnnotationURLCitation(end_index=10878, start_index=10731, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=COX5B%20is%20a%20matrix,with%20higher%20expression%20of%20COX5A')
  33. AnnotationURLCitation(end_index=11171, start_index=11051, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=COX5B%20in%20RAW%20264,In%20addition')
  34. AnnotationURLCitation(end_index=11656, start_index=11525, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=Nuclear,may%20modulate%20COX%20activity%20under')
  35. AnnotationURLCitation(end_index=12067, start_index=11908, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=importance%20of%20COX5B%20for%20COX,with%20higher%20expression%20of%20COX5A')
  36. AnnotationURLCitation(end_index=12379, start_index=12220, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=importance%20of%20COX5B%20for%20COX,with%20higher%20expression%20of%20COX5A')
  37. AnnotationURLCitation(end_index=13044, start_index=12889, title='COX5B Regulates MAVS-mediated Antiviral Signaling through Interaction with ATG5 and Repressing ROS Production - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3534373/#:~:text=remains%20unknown,link%20between%20mitochondrial%20electron%20transport')
  38. AnnotationURLCitation(end_index=13377, start_index=13222, title='COX5B Regulates MAVS-mediated Antiviral Signaling through Interaction with ATG5 and Repressing ROS Production - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3534373/#:~:text=remains%20unknown,link%20between%20mitochondrial%20electron%20transport')
  39. AnnotationURLCitation(end_index=13680, start_index=13525, title='COX5B Regulates MAVS-mediated Antiviral Signaling through Interaction with ATG5 and Repressing ROS Production - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3534373/#:~:text=remains%20unknown,link%20between%20mitochondrial%20electron%20transport')
  40. AnnotationURLCitation(end_index=14568, start_index=14413, title='COX5B Regulates MAVS-mediated Antiviral Signaling through Interaction with ATG5 and Repressing ROS Production - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3534373/#:~:text=remains%20unknown,link%20between%20mitochondrial%20electron%20transport')
  41. AnnotationURLCitation(end_index=15000, start_index=14865, title='COX5B Gene - GeneCards | COX5B Protein | COX5B Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=COX5B#:~:text=Component%20of%20the%20cytochrome%20c,Electrons')
  42. AnnotationURLCitation(end_index=15461, start_index=15298, title='Abnormal Expression of COX5B Gene and Disorder of Mitochondrial Function in Cryptorchid Rats - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11588429/#:~:text=is%20recognised%20as%20a%20key,heat%20generation%20via%20uncoupling%20proteins')
  43. AnnotationURLCitation(end_index=15915, start_index=15768, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=COX5B%20is%20a%20matrix,with%20higher%20expression%20of%20COX5A')
  44. AnnotationURLCitation(end_index=16174, start_index=16027, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=COX5B%20is%20a%20matrix,with%20higher%20expression%20of%20COX5A')
  45. AnnotationURLCitation(end_index=16475, start_index=16320, title='COX5B Regulates MAVS-mediated Antiviral Signaling through Interaction with ATG5 and Repressing ROS Production - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3534373/#:~:text=remains%20unknown,link%20between%20mitochondrial%20electron%20transport')
  46. AnnotationURLCitation(end_index=17140, start_index=16975, title='Mutations in Structural Genes of the Mitochondrial Complex IV May Influence Breast Cancer', type='url_citation', url='https://www.mdpi.com/2073-4425/14/7/1465#:~:text=COX5B%20expression%20is%20significantly%20increased,cells%20and%20decreased%20cell%20proliferation')
  47. AnnotationURLCitation(end_index=17294, start_index=17141, title='Mutations in Structural Genes of the Mitochondrial Complex IV May Influence Breast Cancer', type='url_citation', url='https://www.mdpi.com/2073-4425/14/7/1465#:~:text=Nuclear%20genes%20with%20the%20highest,extrinsic%20and%20intrinsic%20pathways%2C%20and')
  48. AnnotationURLCitation(end_index=18160, start_index=18013, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=COX5B%20is%20a%20matrix,with%20higher%20expression%20of%20COX5A')
  49. AnnotationURLCitation(end_index=18607, start_index=18487, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=COX5B%20in%20RAW%20264,In%20addition')
  50. AnnotationURLCitation(end_index=19019, start_index=18860, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=importance%20of%20COX5B%20for%20COX,with%20higher%20expression%20of%20COX5A')
  51. AnnotationURLCitation(end_index=19543, start_index=19388, title='COX5B Regulates MAVS-mediated Antiviral Signaling through Interaction with ATG5 and Repressing ROS Production - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3534373/#:~:text=remains%20unknown,link%20between%20mitochondrial%20electron%20transport')
  52. AnnotationURLCitation(end_index=19918, start_index=19763, title='COX5B Regulates MAVS-mediated Antiviral Signaling through Interaction with ATG5 and Repressing ROS Production - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3534373/#:~:text=remains%20unknown,link%20between%20mitochondrial%20electron%20transport')
  53. AnnotationURLCitation(end_index=20411, start_index=20235, title='Abnormal Expression of COX5B Gene and Disorder of Mitochondrial Function in Cryptorchid Rats - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11588429/#:~:text=analyse%20the%20expression%20level%20of,aggravation%20of%20cellular%20senescence%2C%20which')
  54. AnnotationURLCitation(end_index=20569, start_index=20412, title='Abnormal Expression of COX5B Gene and Disorder of Mitochondrial Function in Cryptorchid Rats - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11588429/#:~:text=this%20end%2C%20we%20investigated%20the,a%20new%20perspective%20on%20our')
  55. AnnotationURLCitation(end_index=21697, start_index=21541, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=subunit%20%28Chen%20et%20al,novel%20biomarker%20of%20these%20pathologies')
  56. AnnotationURLCitation(end_index=21963, start_index=21854, title='Identification and validation of the mitochondrial function related hub genes by unsupervised machine learning and multi-omics analyses in lung adenocarcinoma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9732315/#:~:text=...free%20article%5D%20,J')
  57. AnnotationURLCitation(end_index=22369, start_index=22204, title='Mutations in Structural Genes of the Mitochondrial Complex IV May Influence Breast Cancer', type='url_citation', url='https://www.mdpi.com/2073-4425/14/7/1465#:~:text=COX5B%20expression%20is%20significantly%20increased,cells%20and%20decreased%20cell%20proliferation')
  58. AnnotationURLCitation(end_index=22698, start_index=22533, title='Mutations in Structural Genes of the Mitochondrial Complex IV May Influence Breast Cancer', type='url_citation', url='https://www.mdpi.com/2073-4425/14/7/1465#:~:text=COX5B%20expression%20is%20significantly%20increased,cells%20and%20decreased%20cell%20proliferation')
  59. AnnotationURLCitation(end_index=22774, start_index=22699, title='Mutations in Structural Genes of the Mitochondrial Complex IV May Influence Breast Cancer', type='url_citation', url='https://www.mdpi.com/2073-4425/14/7/1465#:~:text=W,PubMed')
  60. AnnotationURLCitation(end_index=23474, start_index=23355, title='COX5B Gene - GeneCards | COX5B Protein | COX5B Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=COX5B#:~:text=COX5B%20,c%20oxidase%20activity')
  61. AnnotationURLCitation(end_index=23837, start_index=23735, title='Mutations in Structural Genes of the Mitochondrial Complex IV May Influence Breast Cancer', type='url_citation', url='https://www.mdpi.com/2073-4425/14/7/1465#:~:text=are%20reported%20in%20the%20dbSNP,n')
  62. AnnotationURLCitation(end_index=23946, start_index=23838, title='Mutations in Structural Genes of the Mitochondrial Complex IV May Influence Breast Cancer', type='url_citation', url='https://www.mdpi.com/2073-4425/14/7/1465#:~:text=mutations%20in%20COX5B%20can%20be,83%2C95')
  63. AnnotationURLCitation(end_index=24340, start_index=24164, title='Abnormal Expression of COX5B Gene and Disorder of Mitochondrial Function in Cryptorchid Rats - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11588429/#:~:text=analyse%20the%20expression%20level%20of,aggravation%20of%20cellular%20senescence%2C%20which')
  64. AnnotationURLCitation(end_index=24515, start_index=24341, title='Abnormal Expression of COX5B Gene and Disorder of Mitochondrial Function in Cryptorchid Rats - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11588429/#:~:text=COX5B%20gene%20may%20play%20an,target%20for%20small%20molecule%E2%80%90targeted%20therapy')
  65. AnnotationURLCitation(end_index=25560, start_index=25377, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=gradient%20indispensable%20for%20the%20production,COX%20activity%20regulation%20and%20stabilization')
  66. AnnotationURLCitation(end_index=25692, start_index=25561, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=Nuclear,may%20modulate%20COX%20activity%20under')
  67. AnnotationURLCitation(end_index=26010, start_index=25839, title='COX5B Gene - GeneCards | COX5B Protein | COX5B Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=COX5B#:~:text=complex%20consists%20of%2013%20mitochondrial,provided%20by%20RefSeq%2C%20Jul%202008')
  68. AnnotationURLCitation(end_index=26440, start_index=26309, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=Nuclear,may%20modulate%20COX%20activity%20under')
  69. AnnotationURLCitation(end_index=26924, start_index=26771, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=Single%20isoform%20subunits%20COX5A%2C%20COX5B%2C,COX6C%20and%20COX7C')
  70. AnnotationURLCitation(end_index=27053, start_index=26925, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=COX5B%20is%20a%20matrix,66%20Krieg%20et%20al')
  71. AnnotationURLCitation(end_index=27281, start_index=27136, title='Inverse regulation of the yeast COX5 genes by oxygen and heme - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC362987/#:~:text=Inverse%20regulation%20of%20the%20yeast,Abstract%20The%20COX5a')
  72. AnnotationURLCitation(end_index=27777, start_index=27630, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=COX5B%20is%20a%20matrix,with%20higher%20expression%20of%20COX5A')
  73. AnnotationURLCitation(end_index=28403, start_index=28283, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=COX5B%20in%20RAW%20264,In%20addition')
  74. AnnotationURLCitation(end_index=28816, start_index=28653, title='Abnormal Expression of COX5B Gene and Disorder of Mitochondrial Function in Cryptorchid Rats - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11588429/#:~:text=is%20recognised%20as%20a%20key,heat%20generation%20via%20uncoupling%20proteins')
  75. AnnotationURLCitation(end_index=29539, start_index=29380, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=importance%20of%20COX5B%20for%20COX,with%20higher%20expression%20of%20COX5A')
  76. AnnotationURLCitation(end_index=29919, start_index=29752, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=kinase%20A%2C%20which%20inhibits%20COX,novel%20biomarker%20of%20these%20pathologies')
  77. AnnotationURLCitation(end_index=30276, start_index=30107, title='Abnormal Expression of COX5B Gene and Disorder of Mitochondrial Function in Cryptorchid Rats - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11588429/#:~:text=match%20at%20L34%20analyse%20the,aggravation%20of%20cellular%20senescence%2C%20which')
  78. AnnotationURLCitation(end_index=30450, start_index=30277, title='Abnormal Expression of COX5B Gene and Disorder of Mitochondrial Function in Cryptorchid Rats - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11588429/#:~:text=analysis%20shows%20that%20COX5B%20is,highest%20correlation%20with%20testicular%20disease')
  79. AnnotationURLCitation(end_index=31178, start_index=31058, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=COX5B%20in%20RAW%20264,In%20addition')
  80. AnnotationURLCitation(end_index=31301, start_index=31179, title='COX5B Gene - GeneCards | COX5B Protein | COX5B Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=COX5B#:~:text=,ECO%3A0000269%20PubMed%3A30030519')
  81. AnnotationURLCitation(end_index=31568, start_index=31433, title='COX5B Gene - GeneCards | COX5B Protein | COX5B Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=COX5B#:~:text=Component%20of%20the%20cytochrome%20c,Electrons')
  82. AnnotationURLCitation(end_index=31732, start_index=31569, title='COX5B Gene - GeneCards | COX5B Protein | COX5B Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=COX5B#:~:text=respiratory%20chain%20that%20catalyzes%20the,and%204%20protons%20from%20the')
  83. AnnotationURLCitation(end_index=32095, start_index=31967, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=COX5B%20is%20a%20matrix,66%20Krieg%20et%20al')
  84. AnnotationURLCitation(end_index=32459, start_index=32300, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=importance%20of%20COX5B%20for%20COX,with%20higher%20expression%20of%20COX5A')
  85. AnnotationURLCitation(end_index=32797, start_index=32642, title='COX5B Regulates MAVS-mediated Antiviral Signaling through Interaction with ATG5 and Repressing ROS Production - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3534373/#:~:text=remains%20unknown,link%20between%20mitochondrial%20electron%20transport')
  86. AnnotationURLCitation(end_index=33356, start_index=33200, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=subunit%20%28Chen%20et%20al,novel%20biomarker%20of%20these%20pathologies')
  87. AnnotationURLCitation(end_index=33626, start_index=33450, title='Abnormal Expression of COX5B Gene and Disorder of Mitochondrial Function in Cryptorchid Rats - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11588429/#:~:text=analyse%20the%20expression%20level%20of,aggravation%20of%20cellular%20senescence%2C%20which')
  88. AnnotationURLCitation(end_index=33782, start_index=33627, title='COX5B Regulates MAVS-mediated Antiviral Signaling through Interaction with ATG5 and Repressing ROS Production - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3534373/#:~:text=remains%20unknown,link%20between%20mitochondrial%20electron%20transport')
  89. AnnotationURLCitation(end_index=34487, start_index=34324, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=Cytochrome%20c%20oxidase%20,discovered%20pathogenic%20mutations%20in%20patients')
  90. AnnotationURLCitation(end_index=34616, start_index=34488, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=COX5B%20is%20a%20matrix,66%20Krieg%20et%20al')
  91. AnnotationURLCitation(end_index=34859, start_index=34700, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=importance%20of%20COX5B%20for%20COX,with%20higher%20expression%20of%20COX5A')
  92. AnnotationURLCitation(end_index=35015, start_index=34860, title='COX5B Regulates MAVS-mediated Antiviral Signaling through Interaction with ATG5 and Repressing ROS Production - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3534373/#:~:text=remains%20unknown,link%20between%20mitochondrial%20electron%20transport')
  93. AnnotationURLCitation(end_index=35238, start_index=35082, title='Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8549878/#:~:text=subunit%20%28Chen%20et%20al,novel%20biomarker%20of%20these%20pathologies')
  94. AnnotationURLCitation(end_index=35415, start_index=35239, title='Abnormal Expression of COX5B Gene and Disorder of Mitochondrial Function in Cryptorchid Rats - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11588429/#:~:text=analyse%20the%20expression%20level%20of,aggravation%20of%20cellular%20senescence%2C%20which')