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Question

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: P00447
• Protein Description: RecName: Full=Superoxide dismutase [Mn], mitochondrial; EC=1.15.1.1 {ECO:0000250|UniProtKB:P0A0J3}; Flags: Precursor;
• Gene Information: Name=SOD2; OrderedLocusNames=YHR008C;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the iron/manganese superoxide dismutase family.
• Key Domains: Fe/Mn_Superoxide_Dismutase. (IPR050265); Mn/Fe_SOD. (IPR001189); Mn/Fe_SOD_BS. (IPR019833); Mn/Fe_SOD_C. (IPR019832); Mn/Fe_SOD_N. (IPR019831)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "SOD2" matches the protein description above
2. Verify the organism is correct: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'SOD2' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene SOD2 (gene ID: SOD2, UniProt: P00447) in yeast.

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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.

Output

Question: You are an expert researcher providing comprehensive, well-cited information.

Provide detailed information focusing on:
1. Key concepts and definitions with current understanding
2. Recent developments and latest research (prioritize 2023-2024 sources)
3. Current applications and real-world implementations
4. Expert opinions and analysis from authoritative sources
5. Relevant statistics and data from recent studies

Format as a comprehensive research report with proper citations. Include URLs and publication dates where available.
Always prioritize recent, authoritative sources and provide specific citations for all major claims.

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: P00447
• Protein Description: RecName: Full=Superoxide dismutase [Mn], mitochondrial; EC=1.15.1.1 {ECO:0000250|UniProtKB:P0A0J3}; Flags: Precursor;
• Gene Information: Name=SOD2; OrderedLocusNames=YHR008C;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the iron/manganese superoxide dismutase family.
• Key Domains: Fe/Mn_Superoxide_Dismutase. (IPR050265); Mn/Fe_SOD. (IPR001189); Mn/Fe_SOD_BS. (IPR019833); Mn/Fe_SOD_C. (IPR019832); Mn/Fe_SOD_N. (IPR019831)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "SOD2" matches the protein description above
2. Verify the organism is correct: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'SOD2' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene SOD2 (gene ID: SOD2, UniProt: P00447) in yeast.

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.

Research Report: Functional Annotation of Saccharomyces cerevisiae SOD2 (YHR008C; UniProt P00447)

Executive summary

Saccharomyces cerevisiae SOD2 (YHR008C; UniProt P00447) encodes the mitochondrial matrix manganese superoxide dismutase (MnSOD/Sod2p) that catalyzes superoxide dismutation to hydrogen peroxide and oxygen and is essential for mitochondrial redox homeostasis and multiple downstream stress-adaptation processes (gupta2023mitochondrialsuperoxidedismutase pages 1-2, grujicic2025manganesesuperoxidedismutase pages 1-3). Beyond detoxification, yeast Sod2p can act upstream of redox signaling (e.g., via H2O2-dependent activation of Yap1 during ethanol stress) and, in recent work, suppresses nuclear genome instability during paraquat-induced oxidative stress, connecting mitochondrial redox state to nuclear DNA integrity (zyrina2017mitochondrialsuperoxidedismutase pages 11-13, gupta2023mitochondrialsuperoxidedismutase pages 1-2).

1) Mandatory verification of gene/protein identity (avoid symbol ambiguity)

Verified identity

The target described by UniProt P00447 corresponds to SOD2 / YHR008C in S. cerevisiae (S288c) and is explicitly described in multiple sources as:
- a mitochondrial matrix protein (gupta2023mitochondrialsuperoxidedismutase pages 1-2, maslanka2020linkagebetweencarbon pages 1-3)
- the manganese-dependent superoxide dismutase (MnSOD) (gupta2023mitochondrialsuperoxidedismutase pages 1-2, stepien2020impactofcurcumin pages 1-3)
- distinct from yeast SOD1, which is primarily cytosolic and also present in the mitochondrial intermembrane space (gupta2023mitochondrialsuperoxidedismutase pages 1-2, maslanka2020linkagebetweencarbon pages 1-3)

These statements match the UniProt description “Superoxide dismutase [Mn], mitochondrial; precursor” and the Fe/Mn SOD family/domain assignment.

2) Key concepts and definitions (current understanding)

Reactive oxygen species (ROS) and superoxide

Mitochondrial respiration is a major endogenous source of superoxide (O2•−), a reactive oxygen species that can initiate oxidative damage and redox signaling (zyrina2017mitochondrialsuperoxidedismutase pages 7-9).

Superoxide dismutase (SOD) reaction and substrate specificity

The core SOD reaction is the dismutation of superoxide:
2 O2•− + 2 H+ → H2O2 + O2.
For yeast Sod2p, this is described directly as conversion of superoxide to H2O2 and oxygen (gupta2023mitochondrialsuperoxidedismutase pages 1-2), and is also summarized in MnSOD-focused reviews (grujicic2025manganesesuperoxidedismutase pages 1-3, grujicic2024mnsodmimeticsin pages 2-4). Substrate specificity is thus for the superoxide radical/anionic species, not ROS in general.

MnSOD cofactors and mechanism

Sod2p is a metalloenzyme requiring manganese at the active site; Mn cycles between Mn2+/Mn3+ redox states during catalysis (grujicic2025manganesesuperoxidedismutase pages 1-3). MnSOD structural/mechanistic summaries describe canonical coordination by histidines/aspartate plus a water ligand (His26/His74/His163/Asp159/WAT1 in a common numbering scheme) and outline the Mn redox cycle producing H2O2 from superoxide (grujicic2025manganesesuperoxidedismutase pages 3-5).

Mitochondrial targeting and matrix localization

MnSOD is nuclear-encoded and imported into the mitochondrial matrix, where it is described as the only mitochondrial SOD (grujicic2025manganesesuperoxidedismutase pages 1-3). In yeast, Sod2 is explicitly called “the mitochondrial matrix protein Sod2” (gupta2023mitochondrialsuperoxidedismutase pages 1-2).

3) Core functional annotation: molecular function, localization, and pathway roles

3.1 Molecular function

Sod2p’s primary biochemical role is to eliminate mitochondrial superoxide radicals by converting them to H2O2 and O2 (gupta2023mitochondrialsuperoxidedismutase pages 1-2). This supports mitochondrial redox balance and limits downstream formation of more reactive oxidants derived from superoxide chemistry (gupta2023mitochondrialsuperoxidedismutase pages 11-12).

3.2 Subcellular localization and supporting evidence

Matrix-localized enzyme distributed across mitochondrial networks

In a 2023 study, Sod2-RFP was reported as distributed throughout mitochondrial networks and showed minimal overlap with DAPI-stained nuclei (only 1.6% ± 0.5 of cells) during oxidative stress conditions, arguing against stress-induced nuclear relocalization and supporting persistent mitochondrial localization (gupta2023mitochondrialsuperoxidedismutase pages 4-5). Corresponding figure evidence is shown in the cropped images (gupta2023mitochondrialsuperoxidedismutase media f9107816).

3.3 Biological processes/pathways in which Sod2p participates

A. Oxidative stress defense (canonical)

Sod2p protects cells against oxygen toxicity and oxidative stress and limits oxidative damage (stepien2020impactofcurcumin pages 1-3, zyrina2017mitochondrialsuperoxidedismutase pages 7-9). Loss of Sod2 is associated with reduced resistance to pro-oxidants such as menadione and paraquat in ethanol-tolerance studies (zyrina2017mitochondrialsuperoxidedismutase pages 7-9).

B. Mitochondria-to-nucleus redox signaling via Yap1 in ethanol stress

A key mechanistic model in yeast is that Sod2p-generated H2O2 serves as a signaling molecule that activates/relocalizes the transcription factor Yap1p under ethanol stress (zyrina2017mitochondrialsuperoxidedismutase pages 11-13, zyrina2017mitochondrialsuperoxidedismutase pages 7-9). Ethanol (12–16%) induces Yap1 relocalization, and repression of SOD2 prevents this relocalization while H2O2 can still activate Yap1 in Sod2-repressed cells—supporting the role of Sod2-produced H2O2 specifically in ethanol-triggered signaling (zyrina2017mitochondrialsuperoxidedismutase pages 7-9).

C. Genome stability under oxidative stress (recent primary research)

A 2023 GENETICS study identified a role for Sod2 in suppressing nuclear chromosomal rearrangements under paraquat-induced oxidative stress, particularly in genetic interaction with the RecQ helicase Sgs1 (gupta2023mitochondrialsuperoxidedismutase pages 1-2). The authors propose that mitochondrial superoxide/derived oxidants can leak/redox-signal to the nucleus and generate oxidative DNA lesions; in PQ-treated sod2Δ cells, genome instability is promoted by HR/TLS factors including Rad51, Pol32, and the Rev1/Pol ζ mutasome (gupta2023mitochondrialsuperoxidedismutase pages 11-12).

D. Mitochondrial morphology/homeostasis (quantitative)

The same 2023 study quantified mitochondrial morphology categories and showed that sod2Δ cells exhibited increased mitochondrial fragmentation (41% ± 5.8 fragmented), while sgs1Δ cells showed increased branching (47% ± 1.7 branched); the double mutant resembled sgs1Δ more than sod2Δ (branched 32% ± 5.8; fragmented 8% ± 1.7) (gupta2023mitochondrialsuperoxidedismutase pages 4-5). Figure evidence for these morphology categories and quantification is shown in the cropped figure set (gupta2023mitochondrialsuperoxidedismutase media f9107816).

4) Recent developments and latest research (prioritizing 2023–2024)

4.1 2023: Sod2 links mitochondrial ROS to nuclear genome integrity

Gupta et al. (GENETICS; published Aug 2023; https://doi.org/10.1093/genetics/iyad147) provided multiple lines of evidence that Sod2 protects against nuclear genome instability under oxidative stress without major relocalization to nuclei, including:
- Sod2-RFP localization primarily to mitochondria with only 1.6% ± 0.5 nuclear overlap (gupta2023mitochondrialsuperoxidedismutase pages 4-5)
- Quantified mitochondrial morphology shifts in sod2Δ and sgs1Δ (above) (gupta2023mitochondrialsuperoxidedismutase pages 4-5)
- Mechanistic genetic dependencies on HR and TLS pathways for rearrangements in oxidatively stressed sod2Δ cells (gupta2023mitochondrialsuperoxidedismutase pages 11-12)

4.2 2024: Δsod2 phenotypes in xenobiotic stress (DMSO)

Święciło et al. (Scientific Reports; published Sep 2024; https://doi.org/10.1038/s41598-024-72400-4) explicitly tested Δsod2 strains under short-term and long-term DMSO exposure and reported concentration-dependent outcomes:
- In 1-hour exposures, Δsod2 viability did not significantly decrease until 20% (v/v) DMSO, where viability dropped by ~36.3% versus control (swieciło2024theeffectof pages 4-5).
- In long-term exposure spot assays, 4% DMSO completely inhibited growth of both Δsod1 and Δsod2 mutants (swieciło2024theeffectof pages 5-6).
- Superoxide levels increased with DMSO concentration and increases were stronger in sod mutants, consistent with DMSO provoking oxidative stress; oxygen limitation (hypoxia/anoxia) improved growth under DMSO, consistent with a respiration/ROS contribution (swieciło2024theeffectof pages 6-7, swieciło2024theeffectof pages 7-8).

4.3 2024: Systems-level regulation of oxidative stress defenses (context for Sod2)

Hsu et al. (FEMS Yeast Research; published Jan 2024; https://doi.org/10.1093/femsyr/foae005) reported that ribosomal protein gene mutants exhibit increased oxidative stress (higher H2O2) and increased antioxidant enzyme activity at stationary phase, with catalase especially elevated, and show translational reprogramming of oxidative-stress transcripts (hsu2024mutationsofribosomal pages 1-2, hsu2024mutationsofribosomal pages 7-9). While the accessible excerpts did not provide Sod2-specific quantitative changes, the study provides authoritative recent context that yeast oxidative-stress defenses are co-regulated at transcriptional and translational levels during stress and stationary phase (hsu2024mutationsofribosomal pages 7-9).

5) Current applications and real-world implementations

5.1 Ethanol tolerance in yeast biotechnology/fermentation

A direct application-relevant implication is ethanol tolerance. Zyrina et al. (Applied and Environmental Microbiology; published Feb 2017; https://doi.org/10.1128/AEM.02759-16) explicitly state their findings “could be useful for the improvements of ethanol tolerance in the industrial strains,” based on a proposed Sod2p–Yap1p signaling module and its interaction with retrograde signaling (zyrina2017mitochondrialsuperoxidedismutase pages 11-13). Specific experimentally supported levers include:
- Mild H2O2 pretreatment (0.05 mM) to restore ethanol tolerance in SOD2-repressed cells (zyrina2017mitochondrialsuperoxidedismutase pages 11-13)
- Genetic or signaling interventions affecting retrograde signaling (e.g., activation by 2 mM methionine-sulfoximine or deletion of the negative regulator MKS1) that restore/improve ethanol resistance in SOD2-repressed contexts (zyrina2017mitochondrialsuperoxidedismutase pages 9-11)

These are laboratory demonstrations rather than deployed industrial protocols, but they map directly onto strain engineering and process conditioning concepts.

5.2 Oxidative-stress engineering strategies in yeast cell factories

A 2025 engineering-focused review (Feng et al.; Chem & Bio Engineering; published May 2025; https://doi.org/10.1021/cbe.5c00021) provides expert recommendations relevant to Sod2-centered engineering:
- Prefer dynamic, stress-responsive expression of antioxidant genes (to reduce metabolic burden of constitutive overexpression) (feng2025mechanismsandstrategies pages 7-9).
- Consider pathway-level modulation (e.g., TOR downregulation), which can be accompanied by Sod2p upregulation and reduced ROS during stationary phase (feng2025mechanismsandstrategies pages 7-9).

Although this review is outside 2023–2024, it synthesizes engineering practice and cautions that upstream pathway manipulation can have growth-phase-dependent effects on mitochondrial ROS (feng2025mechanismsandstrategies pages 7-9).

6) Expert opinions and analysis (authoritative sources)

6.1 MnSOD as a central mitochondrial redox node

MnSOD reviews emphasize that MnSOD is localized to the mitochondrial matrix, uses manganese redox cycling, and sits at a key control point where mitochondrial superoxide is converted into H2O2, a species that is both less reactive than superoxide and capable of acting in redox signaling (grujicic2025manganesesuperoxidedismutase pages 1-3, grujicic2025manganesesuperoxidedismutase pages 3-5). This conceptual framing supports interpretation of yeast results where Sod2-derived H2O2 functions as an upstream signal (e.g., Yap1 activation) (zyrina2017mitochondrialsuperoxidedismutase pages 11-13).

6.2 Yeast-specific expert interpretation: dual roles (protection and signaling)

Zyrina et al. explicitly argue that Sod2 has a signaling role in ethanol tolerance in addition to antioxidant protection, proposing a mitochondria-to-nucleus module (Sod2→H2O2→Yap1) that interacts with retrograde signaling (zyrina2017mitochondrialsuperoxidedismutase pages 11-13). This is an expert mechanistic interpretation grounded in genetic and physiological epistasis experiments (zyrina2017mitochondrialsuperoxidedismutase pages 7-9).

7) Relevant statistics and data points (recent studies emphasized)

Quantitative (2023)

• Sod2-RFP nuclear overlap under oxidative stress: 1.6% ± 0.5 (gupta2023mitochondrialsuperoxidedismutase pages 4-5)
• Mitochondrial morphology fractions:
• sod2Δ fragmented: 41% ± 5.8
• sgs1Δ branched: 47% ± 1.7
• sgs1Δ sod2Δ branched: 32% ± 5.8; fragmented: 8% ± 1.7 (gupta2023mitochondrialsuperoxidedismutase pages 4-5)

Quantitative (2024)

• Short-term DMSO sensitivity: Δsod2 viability drops by ~36.3% at 20% (v/v) DMSO (swieciło2024theeffectof pages 4-5)
• Long-term DMSO growth: 4% DMSO completely inhibited growth of Δsod2 (and Δsod1) mutants (swieciło2024theeffectof pages 5-6)

Quantitative experimental conditions supporting pathway claims

• Ethanol stress conditions used to demonstrate Sod2→Yap1 signaling: 12–16% ethanol for Yap1 relocalization assays and 12–18% ethanol for survival effects in SOD2 repression (zyrina2017mitochondrialsuperoxidedismutase pages 7-9).
• Rescue/conditioning: 0.05 mM H2O2 pretreatment rescues ethanol tolerance under SOD2 repression (zyrina2017mitochondrialsuperoxidedismutase pages 11-13).

Evidence summary table

The following table consolidates the functional annotation and key evidence into a compact map.

Table: This table summarizes verified identity, core biochemical function, localization, pathway roles, mutant phenotypes, and engineering relevance for Saccharomyces cerevisiae SOD2/YHR008C. It is useful as a compact evidence map linking classic function to recent 2023 findings on genome stability and mitochondrial morphology.

Visual evidence (figures)

Cropped figures from Gupta et al. (2023) provide direct visual support for (i) Sod2-RFP mitochondrial localization vs DAPI and (ii) mitochondrial morphology categories and their quantification across genotypes/stresses (gupta2023mitochondrialsuperoxidedismutase media f9107816).

Limitations and evidence gaps

• 2023–2024 literature directly focused on yeast Sod2 is more limited than for mammalian SOD2; several recent sources are broader oxidative-stress studies where Sod2 is one component. Where Sod2-specific quantitative values were not available in retrieved excerpts (e.g., certain 2024 systems studies), this report avoids inferring missing numbers.
• Post-translational modifications (e.g., acetylation) are well established for mammalian MnSOD but were not supported by yeast Sod2-specific primary evidence in the retrieved 2023–2024 sources; thus PTM claims were not emphasized.

References (URLs and publication dates)

• Gupta SV, Campos L, Schmidt KH. Mitochondrial superoxide dismutase Sod2 suppresses nuclear genome instability during oxidative stress. GENETICS. Aug 2023. https://doi.org/10.1093/genetics/iyad147 (gupta2023mitochondrialsuperoxidedismutase pages 1-2)
• Święciło A, Januś E, Krzepiłko A, Skowrońska M. The effect of DMSO on Saccharomyces cerevisiae yeast with different energy metabolism and antioxidant status. Scientific Reports. Sep 2024. https://doi.org/10.1038/s41598-024-72400-4 (swieciło2024theeffectof pages 4-5)
• Hsu C-H, Liu C-Y, Lo K-Y. Mutations of ribosomal protein genes induce overexpression of catalase in Saccharomyces cerevisiae. FEMS Yeast Research. Jan 2024. https://doi.org/10.1093/femsyr/foae005 (hsu2024mutationsofribosomal pages 1-2)
• Zyrina AN, Smirnova EA, Markova OV, Severin FF, Knorre DA. Mitochondrial superoxide dismutase and Yap1p act as a signaling module contributing to ethanol tolerance of the yeast Saccharomyces cerevisiae. Applied and Environmental Microbiology. Feb 2017. https://doi.org/10.1128/AEM.02759-16 (zyrina2017mitochondrialsuperoxidedismutase pages 1-3)
• Grujicic J, Allen AR. MnSOD mimetics in therapy: exploring their role in combating oxidative stress-related diseases. Antioxidants. Nov 2024. https://doi.org/10.3390/antiox13121444 (grujicic2024mnsodmimeticsin pages 2-4)
• Grujicic J, Allen AR. Manganese superoxide dismutase: structure, function, and implications in human disease. Antioxidants. Jul 2025. https://doi.org/10.3390/antiox14070848 (grujicic2025manganesesuperoxidedismutase pages 1-3)
• Feng T, Yu H, Ye L. Mechanisms and strategies for engineering oxidative stress resistance in Saccharomyces cerevisiae. Chem & Bio Engineering. May 2025. https://doi.org/10.1021/cbe.5c00021 (feng2025mechanismsandstrategies pages 7-9)

References

1. (gupta2023mitochondrialsuperoxidedismutase pages 1-2): Sonia Vidushi Gupta, Lillian Campos, and Kristina Hildegard Schmidt. Mitochondrial superoxide dismutase sod2 suppresses nuclear genome instability during oxidative stress. GENETICS, Aug 2023. URL: https://doi.org/10.1093/genetics/iyad147, doi:10.1093/genetics/iyad147. This article has 20 citations and is from a domain leading peer-reviewed journal.

2. (grujicic2025manganesesuperoxidedismutase pages 1-3): Jovan Grujicic and Antiño R. Allen. Manganese superoxide dismutase: structure, function, and implications in human disease. Antioxidants, 14:848, Jul 2025. URL: https://doi.org/10.3390/antiox14070848, doi:10.3390/antiox14070848. This article has 34 citations.

3. (zyrina2017mitochondrialsuperoxidedismutase pages 11-13): Anna N. Zyrina, Ekaterina A. Smirnova, Olga V. Markova, Fedor F. Severin, and Dmitry A. Knorre. Mitochondrial superoxide dismutase and yap1p act as a signaling module contributing to ethanol tolerance of the yeast saccharomyces cerevisiae. Applied and Environmental Microbiology, Feb 2017. URL: https://doi.org/10.1128/aem.02759-16, doi:10.1128/aem.02759-16. This article has 39 citations and is from a peer-reviewed journal.

4. (maslanka2020linkagebetweencarbon pages 1-3): Roman Maslanka, Renata Zadrag-Tecza, and Magdalena Kwolek-Mirek. Linkage between carbon metabolism, redox status and cellular physiology in the yeast saccharomyces cerevisiae devoid of sod1 or sod2 gene. Genes, 11:780, Jul 2020. URL: https://doi.org/10.3390/genes11070780, doi:10.3390/genes11070780. This article has 46 citations.

5. (stepien2020impactofcurcumin pages 1-3): Karolina Stępień, Dominik Wojdyła, Katarzyna Nowak, and Mateusz Mołoń. Impact of curcumin on replicative and chronological aging in the saccharomyces cerevisiae yeast. Biogerontology, 21:109-123, Oct 2020. URL: https://doi.org/10.1007/s10522-019-09846-x, doi:10.1007/s10522-019-09846-x. This article has 58 citations and is from a peer-reviewed journal.

6. (zyrina2017mitochondrialsuperoxidedismutase pages 7-9): Anna N. Zyrina, Ekaterina A. Smirnova, Olga V. Markova, Fedor F. Severin, and Dmitry A. Knorre. Mitochondrial superoxide dismutase and yap1p act as a signaling module contributing to ethanol tolerance of the yeast saccharomyces cerevisiae. Applied and Environmental Microbiology, Feb 2017. URL: https://doi.org/10.1128/aem.02759-16, doi:10.1128/aem.02759-16. This article has 39 citations and is from a peer-reviewed journal.

7. (grujicic2024mnsodmimeticsin pages 2-4): Jovan Grujicic and Antiño R. Allen. Mnsod mimetics in therapy: exploring their role in combating oxidative stress-related diseases. Antioxidants, 13:1444, Nov 2024. URL: https://doi.org/10.3390/antiox13121444, doi:10.3390/antiox13121444. This article has 21 citations.

8. (grujicic2025manganesesuperoxidedismutase pages 3-5): Jovan Grujicic and Antiño R. Allen. Manganese superoxide dismutase: structure, function, and implications in human disease. Antioxidants, 14:848, Jul 2025. URL: https://doi.org/10.3390/antiox14070848, doi:10.3390/antiox14070848. This article has 34 citations.

9. (gupta2023mitochondrialsuperoxidedismutase pages 11-12): Sonia Vidushi Gupta, Lillian Campos, and Kristina Hildegard Schmidt. Mitochondrial superoxide dismutase sod2 suppresses nuclear genome instability during oxidative stress. GENETICS, Aug 2023. URL: https://doi.org/10.1093/genetics/iyad147, doi:10.1093/genetics/iyad147. This article has 20 citations and is from a domain leading peer-reviewed journal.

10. (gupta2023mitochondrialsuperoxidedismutase pages 4-5): Sonia Vidushi Gupta, Lillian Campos, and Kristina Hildegard Schmidt. Mitochondrial superoxide dismutase sod2 suppresses nuclear genome instability during oxidative stress. GENETICS, Aug 2023. URL: https://doi.org/10.1093/genetics/iyad147, doi:10.1093/genetics/iyad147. This article has 20 citations and is from a domain leading peer-reviewed journal.

11. (gupta2023mitochondrialsuperoxidedismutase media f9107816): Sonia Vidushi Gupta, Lillian Campos, and Kristina Hildegard Schmidt. Mitochondrial superoxide dismutase sod2 suppresses nuclear genome instability during oxidative stress. GENETICS, Aug 2023. URL: https://doi.org/10.1093/genetics/iyad147, doi:10.1093/genetics/iyad147. This article has 20 citations and is from a domain leading peer-reviewed journal.

12. (swieciło2024theeffectof pages 4-5): Agata Święciło, Ewa Januś, Anna Krzepiłko, and Monika Skowrońska. The effect of dmso on saccharomyces cerevisiae yeast with different energy metabolism and antioxidant status. Scientific Reports, Sep 2024. URL: https://doi.org/10.1038/s41598-024-72400-4, doi:10.1038/s41598-024-72400-4. This article has 8 citations and is from a peer-reviewed journal.

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14. (swieciło2024theeffectof pages 6-7): Agata Święciło, Ewa Januś, Anna Krzepiłko, and Monika Skowrońska. The effect of dmso on saccharomyces cerevisiae yeast with different energy metabolism and antioxidant status. Scientific Reports, Sep 2024. URL: https://doi.org/10.1038/s41598-024-72400-4, doi:10.1038/s41598-024-72400-4. This article has 8 citations and is from a peer-reviewed journal.

15. (swieciło2024theeffectof pages 7-8): Agata Święciło, Ewa Januś, Anna Krzepiłko, and Monika Skowrońska. The effect of dmso on saccharomyces cerevisiae yeast with different energy metabolism and antioxidant status. Scientific Reports, Sep 2024. URL: https://doi.org/10.1038/s41598-024-72400-4, doi:10.1038/s41598-024-72400-4. This article has 8 citations and is from a peer-reviewed journal.

16. (hsu2024mutationsofribosomal pages 1-2): Ching-Hsiang Hsu, Ching-Yu Liu, and Kai-Yin Lo. Mutations of ribosomal protein genes induce overexpression of catalase in saccharomyces cerevisiae. FEMS Yeast Research, Jan 2024. URL: https://doi.org/10.1093/femsyr/foae005, doi:10.1093/femsyr/foae005. This article has 5 citations and is from a peer-reviewed journal.

17. (hsu2024mutationsofribosomal pages 7-9): Ching-Hsiang Hsu, Ching-Yu Liu, and Kai-Yin Lo. Mutations of ribosomal protein genes induce overexpression of catalase in saccharomyces cerevisiae. FEMS Yeast Research, Jan 2024. URL: https://doi.org/10.1093/femsyr/foae005, doi:10.1093/femsyr/foae005. This article has 5 citations and is from a peer-reviewed journal.

18. (zyrina2017mitochondrialsuperoxidedismutase pages 9-11): Anna N. Zyrina, Ekaterina A. Smirnova, Olga V. Markova, Fedor F. Severin, and Dmitry A. Knorre. Mitochondrial superoxide dismutase and yap1p act as a signaling module contributing to ethanol tolerance of the yeast saccharomyces cerevisiae. Applied and Environmental Microbiology, Feb 2017. URL: https://doi.org/10.1128/aem.02759-16, doi:10.1128/aem.02759-16. This article has 39 citations and is from a peer-reviewed journal.

19. (feng2025mechanismsandstrategies pages 7-9): Taotao Feng, Hongwei Yu, and Lidan Ye. Mechanisms and strategies for engineering oxidative stress resistance in saccharomyces cerevisiae. Chem & Bio Engineering, 2:409-422, May 2025. URL: https://doi.org/10.1021/cbe.5c00021, doi:10.1021/cbe.5c00021. This article has 15 citations.

20. (zyrina2017mitochondrialsuperoxidedismutase pages 1-3): Anna N. Zyrina, Ekaterina A. Smirnova, Olga V. Markova, Fedor F. Severin, and Dmitry A. Knorre. Mitochondrial superoxide dismutase and yap1p act as a signaling module contributing to ethanol tolerance of the yeast saccharomyces cerevisiae. Applied and Environmental Microbiology, Feb 2017. URL: https://doi.org/10.1128/aem.02759-16, doi:10.1128/aem.02759-16. This article has 39 citations and is from a peer-reviewed journal.

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