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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: O16327
• Protein Description: RecName: Full=Protein irg-1 {ECO:0000305}; AltName: Full=Infection response protein 1 {ECO:0000305|PubMed:20133860};
• Gene Information: Name=irg-1 {ECO:0000312|WormBase:C07G3.2}; ORFNames=C07G3.2 {ECO:0000312|WormBase:C07G3.2};
• Organism (full): Caenorhabditis elegans.
• Protein Family: Not specified in UniProt
• Key Domains: NADAR. (IPR012816); YbiA-like_sf. (IPR037238); NADAR (PF08719)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "irg-1" matches the protein description above
2. Verify the organism is correct: Caenorhabditis elegans.
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 'irg-1' 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 irg-1 (gene ID: irg-1, UniProt: O16327) in worm.

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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: O16327
• Protein Description: RecName: Full=Protein irg-1 {ECO:0000305}; AltName: Full=Infection response protein 1 {ECO:0000305|PubMed:20133860};
• Gene Information: Name=irg-1 {ECO:0000312|WormBase:C07G3.2}; ORFNames=C07G3.2 {ECO:0000312|WormBase:C07G3.2};
• Organism (full): Caenorhabditis elegans.
• Protein Family: Not specified in UniProt
• Key Domains: NADAR. (IPR012816); YbiA-like_sf. (IPR037238); NADAR (PF08719)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "irg-1" matches the protein description above
2. Verify the organism is correct: Caenorhabditis elegans.
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 'irg-1' 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 irg-1 (gene ID: irg-1, UniProt: O16327) in worm.

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 plan and verification
- Identity confirmed: irg-1 is C07G3.2 in Caenorhabditis elegans (UniProt O16327), originally identified as Infection response gene-1 and widely used as an intestinal infection-response reporter under control of the bZIP transcription factor ZIP-2. This irg-1 is distinct from mammalian IRG1/ACOD1 (aconitate decarboxylase 1) and from interferon-inducible GTPases sometimes called “IRGs.” UniProt annotates NADAR/YbiA-like domains for the C. elegans protein, but a biochemical function has not been demonstrated in vivo. (dunbar2012c.elegansdetects pages 1-2)

Key concepts and definitions
- What is irg-1? irg-1 encodes an infection-inducible gene in C. elegans whose transcription is rapidly and robustly upregulated in the intestine in response to specific pathogen-associated insults and defined host-cell stress signals, especially translational inhibition. It is a canonical early readout of the ZIP-2 surveillance pathway. The molecular/enzymatic activity of the IRG-1 protein remains uncharacterized; its utility in the literature is primarily as a sentinel immune effector/readout gene. URL: https://doi.org/10.1016/j.chom.2012.02.008 (Apr 2012) (dunbar2012c.elegansdetects pages 1-2)
- Tissue expression/localization: irg-1 is induced in intestinal cells; transcriptional reporters using the irg-1 promoter (irg-1p::GFP) show strong intestinal GFP following infection or translational stress. URL: https://doi.org/10.1016/j.chom.2012.02.008 (Apr 2012); https://doi.org/10.1016/j.chom.2012.02.007 (Apr 2012) (dunbar2012c.elegansdetects pages 2-3, mcewan2012hosttranslationalinhibition pages 2-3)
- Regulatory context: ZIP-2 is the principal transcriptional regulator of early irg-1 induction. Other innate immune pathways, notably PMK-1/p38 MAPK and the GPCR FSHR-1 pathway, contribute to survival and to regulation of other toxin-responsive genes, but irg-1 itself is most directly linked to ZIP-2 activity. URLs: https://doi.org/10.1016/j.chom.2012.02.008 (Apr 2012); https://doi.org/10.1016/j.chom.2012.02.007 (Apr 2012) (dunbar2012c.elegansdetects pages 9-10, mcewan2012hosttranslationalinhibition pages 2-3)

Recent developments and latest research (emphasis 2023–2024)
- Lysosome-related organelles (LROs, gut granules) modulate irg-1 induction under chemical stress. During benzaldehyde (BA) exposure, LRO biogenesis/transport mutants (glo-1 and pgp-2) show impaired upregulation of antimicrobial and immune effectors, explicitly including irg-1, indicating LRO-dependent control of BA-induced irg-1 expression. During Pseudomonas aeruginosa infection, wild-type worms upregulate irg-1 independently of glo-1/pgp-2, but loss of pgp-2 can “robustly” enhance irg-1 upon PA14 infection, indicating pathway-specific modulation of irg-1 by LRO state. URL: https://doi.org/10.1038/s42003-023-05246-7 (Sep 2023) (hajdu2023lysosomerelatedorganellespromote pages 7-10, hajdu2023lysosomerelatedorganellespromote pages 10-11)
- Mitochondrial stress crosstalk with ZIP-2: In lonp-1 mutants, mitochondrial p38 MAPK (PMK-3) signaling is induced and genetically interacts with ZIP-2. ZIP-2 activation depends on PMK-3 under this perturbation, with consequences for longevity and thermotolerance even though pathogen resistance is not increased in this setting, suggesting context-specific decoupling of defense readouts. URL: https://doi.org/10.3390/ijms242417209 (Dec 2023) (taouktsi2023mitochondrialp38mitogenactivated pages 1-2)
- Translational surveillance remains central: Foundational work established that endocytosis of P. aeruginosa toxins leading to inhibition of translation triggers ZIP-2 accumulation and irg-1 induction. Newer studies continue to use irg-1 as a quantitative reporter of this pathway across diverse stressors. URLs: https://doi.org/10.1016/j.chom.2012.02.008 (Apr 2012); https://doi.org/10.1016/j.chom.2012.02.007 (Apr 2012) (dunbar2012c.elegansdetects pages 3-5, mcewan2012hosttranslationalinhibition pages 2-3)

Current applications and real-world implementations
- Reporter-based surveillance assays: irg-1p::GFP is a standard reporter for early intestinal immune activation, used to screen for host genes and pathways that either induce the response in the absence of pathogens (e.g., translation factor RNAi, mitochondrial or chromatin perturbations) or are required to mount the response during infection. These implementations include large-scale RNAi screens and targeted genetic analyses. URLs: https://doi.org/10.1016/j.chom.2012.02.008 (Apr 2012) (dunbar2012c.elegansdetects pages 2-3, dunbar2013analyzingtherole pages 25-57)
- Toxicology and infection models: irg-1 reporters are used to measure host detection of bacterial toxins such as P. aeruginosa Exotoxin A (ToxA) and small-molecule translation inhibitors (e.g., cycloheximide, hygromycin, G418) that phenocopy pathogen-induced translational arrest. URLs: https://doi.org/10.1016/j.chom.2012.02.007 (Apr 2012); https://doi.org/10.1016/j.chom.2012.02.008 (Apr 2012) (mcewan2012hosttranslationalinhibition pages 2-3, dunbar2012c.elegansdetects pages 3-5)
- Systems-level stress immunity: LRO-focused work demonstrates that modulation of gut granule function can tune immune effector outputs including irg-1, providing a practical handle for studying organelle–immunity crosstalk under environmental chemical stress and infection. URL: https://doi.org/10.1038/s42003-023-05246-7 (Sep 2023) (hajdu2023lysosomerelatedorganellespromote pages 7-10, hajdu2023lysosomerelatedorganellespromote pages 10-11)

Expert opinions and analysis from authoritative sources
- Translational inhibition as an immune-activating cue: Two independent Cell Host & Microbe studies established the concept that C. elegans “senses” pathogen-induced translation elongation arrest (e.g., via Exotoxin A action on EF-2), which derepresses zip-2 translation and drives irg-1 induction. This paradigm underlies the “surveillance immunity” model wherein disruption of core host processes is a signal of infection; it provides a mechanistic explanation for why diverse insults converge on irg-1. URLs: https://doi.org/10.1016/j.chom.2012.02.008 (Apr 2012); https://doi.org/10.1016/j.chom.2012.02.007 (Apr 2012) (dunbar2012c.elegansdetects pages 1-2, dunbar2012c.elegansdetects pages 3-5, mcewan2012hosttranslationalinhibition pages 2-3)
- Pathway architecture and specificity: The ZIP-2 axis primarily controls irg-1 and a set of detoxification/efflux genes, while PMK-1/p38 regulates different immune effectors; translational inhibition can engage both systems to varying degrees, explaining differences in gene dependencies observed across perturbations (e.g., histones H2A/B vs H3/H4; initiation vs elongation factors). URL: https://doi.org/10.1016/j.chom.2012.02.008 (Apr 2012) (dunbar2012c.elegansdetects pages 9-10)
- Emerging crosstalk: Under mitochondrial proteostasis disruption (lonp-1 deficiency), PMK-3–ZIP-2 crosstalk can activate ZIP-2 without conferring canonical pathogen resistance, suggesting that surveillance outputs can be repurposed for organismal stress tolerance and lifespan regulation depending on context. URL: https://doi.org/10.3390/ijms242417209 (Dec 2023) (taouktsi2023mitochondrialp38mitogenactivated pages 1-2)

Relevant statistics and data from recent studies
- Toxin-responsive transcriptome: Exposure to P. aeruginosa Exotoxin A (or to translational elongation inhibitors hygromycin and G418) strongly induces an immune transcriptional program; 144 genes were upregulated by ToxA, with 68 overlapping the early (≤4 h) PA14 infection response, highlighting a translation-centered detection logic. URL: https://doi.org/10.1016/j.chom.2012.02.007 (Apr 2012) (mcewan2012hosttranslationalinhibition pages 2-3)
- Reporter-based genetic screens: A genome-wide RNAi screen built on irg-1p::GFP surveyed ~18,000 RNAi clones, identifying 122 reproducible hits that compromised infection-induced reporter expression; secondary qRT-PCR validated 33 candidates that failed to induce endogenous irg-1, and 18 showed a “zip-2-like” phenotype (failure to induce irg-1 but intact induction of certain other immune genes). This establishes irg-1 as a robust screening endpoint for pathway mapping. (Unpublished thesis context summarizing methodology and results.) (dunbar2013analyzingtherole pages 117-121)
- Basal repression by lipid metabolism: sbp-1 (SREBP homolog) represses irg-1 in uninfected animals; sbp-1 RNAi elevated irg-1 mRNA ~47-fold in wild type and ~322-fold in zip-2 mutants, indicating a strong, ZIP-2–independent derepression node in basal conditions. (Quantitative qRT-PCR reported in genetic analysis.) (dunbar2013analyzingtherole pages 121-125)
- LRO dependence and independence: Under benzaldehyde stress, loss of LRO genes glo-1 or pgp-2 diminishes induction of immune effectors including irg-1; during P. aeruginosa infection, irg-1 upregulation does not require glo-1/pgp-2, and pgp-2 loss can even hyperinduce irg-1, indicating stimulus-specific routing to the irg-1 promoter. URL: https://doi.org/10.1038/s42003-023-05246-7 (Sep 2023) (hajdu2023lysosomerelatedorganellespromote pages 7-10, hajdu2023lysosomerelatedorganellespromote pages 10-11)

Mechanism, pathways, and localization in detail
- Upstream sensing and translational control: PA14 Exotoxin A ADP-ribosylates EF-2 to inhibit translation; translational arrest derepresses ZIP-2 translation via an upstream open reading frame (uORF) in zip-2 mRNA, increasing ZIP-2 protein and activating irg-1. Chemical translation inhibitors (cycloheximide, hygromycin, G418) and RNAi against elongation factors and many tRNA synthetases mimic this response. URLs: https://doi.org/10.1016/j.chom.2012.02.007 (Apr 2012); https://doi.org/10.1016/j.chom.2012.02.008 (Apr 2012) (mcewan2012hosttranslationalinhibition pages 2-3, dunbar2012c.elegansdetects pages 3-5)
- Parallel surveillance circuits: Perturbations to histones and mitochondria also induce irg-1, with differential ZIP-2 dependence (e.g., H2A/B vs H3/H4; initiation vs elongation factor knockdowns), consistent with multiple upstream sensors feeding into the irg-1 promoter via distinct transcription factors. URL: https://doi.org/10.1016/j.chom.2012.02.008 (Apr 2012) (dunbar2012c.elegansdetects pages 9-10)
- Tissue context: Induction occurs in the intestine where pathogen toxins are encountered and endocytosed; endocytosis is required to trigger the translational inhibition that activates ZIP-2 and irg-1. URL: https://doi.org/10.1016/j.chom.2012.02.008 (Apr 2012) (dunbar2012c.elegansdetects pages 1-2)
- Additional modulation: Genetic and organellar contexts (lipid metabolism via sbp-1, mitochondrial stress via lonp-1/PMK-3, and LRO state via glo-1/pgp-2) quantitatively tune irg-1 outputs without redefining its core identity as a ZIP-2–controlled infection/stress effector. URLs: https://doi.org/10.3390/ijms242417209 (Dec 2023); https://doi.org/10.1038/s42003-023-05246-7 (Sep 2023) (taouktsi2023mitochondrialp38mitogenactivated pages 1-2, hajdu2023lysosomerelatedorganellespromote pages 7-10, hajdu2023lysosomerelatedorganellespromote pages 10-11, dunbar2013analyzingtherole pages 121-125)

What is known versus unknown about molecular/biochemical function
- Known: irg-1 is a transcriptionally inducible immune effector gene responsive to pathogen-induced translational inhibition and other core-process disruptions; it is a sensitive intestinal reporter of ZIP-2 activation and a practical endpoint for genetic/chemical screens. URLs: https://doi.org/10.1016/j.chom.2012.02.008; https://doi.org/10.1016/j.chom.2012.02.007 (Apr 2012) (dunbar2012c.elegansdetects pages 3-5, mcewan2012hosttranslationalinhibition pages 2-3)
- Unknown: Despite domain predictions (NADAR/YbiA-like), no direct enzymatic reaction, substrate specificity, or transport function has been experimentally defined for the IRG-1 protein in C. elegans. The field generally treats irg-1 as a hallmark immune effector/readout of the ZIP-2 pathway rather than a biochemically characterized enzyme. URL: https://doi.org/10.1016/j.chom.2012.02.008 (Apr 2012) (dunbar2012c.elegansdetects pages 1-2)

Reporter phenotypes and experimental usage
- irg-1p::GFP is robustly induced in intestine within hours of PA14 challenge or translational inhibition; loss of zip-2 abrogates induction in many contexts, enabling clear genetic epistasis tests. Reporter-based screens have revealed numerous upstream cellular processes that, when perturbed, induce or are required for irg-1 expression. URLs: https://doi.org/10.1016/j.chom.2012.02.008; https://doi.org/10.1016/j.chom.2012.02.007 (Apr 2012) (dunbar2013analyzingtherole pages 25-57, dunbar2012c.elegansdetects pages 3-5, mcewan2012hosttranslationalinhibition pages 2-3)

Concise evidence summary table
| Aspect | Key finding (1-2 sentences) | Primary regulators/stimuli | Evidence source (journal, year) | URL |
|---|---|---|---|---|
| Identity / Definition | irg-1 (C07G3.2; UniProt O16327) is an infection-response gene in Caenorhabditis elegans used as a marker of an early intestinal innate immune program; the protein's biochemical/enzymatic activity remains uncharacterized. | — | Cell Host & Microbe, 2012 (dunbar2012c.elegansdetects pages 1-2, dunbar2012c.elegansdetects pages 9-10) | https://doi.org/10.1016/j.chom.2012.02.008 |
| Tissue expression / Localization | irg-1 is induced primarily in intestinal cells and visualized using an irg-1p::GFP transcriptional reporter; induction is detected early after challenge. | Intestinal expression (reporter) | Cell Host & Microbe, 2012; Cell Host & Microbe, 2012 (dunbar2012c.elegansdetects pages 2-3, mcewan2012hosttranslationalinhibition pages 2-3) | https://doi.org/10.1016/j.chom.2012.02.008, https://doi.org/10.1016/j.chom.2012.02.007 |
| Principal regulators | The bZIP transcription factor ZIP-2 is the primary regulator required for early irg-1 induction; PMK-1/p38 and other pathways (e.g., FSHR-1) contribute to parts of the response or to parallel gene sets. | ZIP-2; PMK-1/p38; FSHR-1 (partial) | Cell Host & Microbe, 2012; Cell Host & Microbe, 2012; Dunbar 2013 (dunbar2012c.elegansdetects pages 9-10, mcewan2012hosttranslationalinhibition pages 2-3, dunbar2013analyzingtherole pages 117-121) | https://doi.org/10.1016/j.chom.2012.02.008, https://doi.org/10.1016/j.chom.2012.02.007 |
| Induction stimuli | irg-1 is induced by Pseudomonas aeruginosa infection (notably Exotoxin A-mediated translational inhibition), chemical translation inhibitors (cycloheximide, hygromycin, G418), and RNAi/perturbations that impair translation, mitochondria, chromatin, or other core processes. | P. aeruginosa Exotoxin A; translational inhibitors; translation-factor RNAi; mitochondrial/chromatin perturbations | Cell Host & Microbe, 2012; Cell Host & Microbe, 2012 (dunbar2012c.elegansdetects pages 3-5, mcewan2012hosttranslationalinhibition pages 2-3, dunbar2012c.elegansdetects pages 9-10) | https://doi.org/10.1016/j.chom.2012.02.008, https://doi.org/10.1016/j.chom.2012.02.007 |
| Key mechanistic unknowns | The molecular/biochemical function of the IRG-1 protein is not defined in the cited literature; irg-1 is treated as an immune effector/readout rather than a biochemically characterized enzyme or transporter. | — | Cell Host & Microbe, 2012; Dunbar 2013 (dunbar2012c.elegansdetects pages 1-2, dunbar2013analyzingtherole pages 117-121) | https://doi.org/10.1016/j.chom.2012.02.008 |
| Typical reporter phenotypes / genetic effects | irg-1p::GFP reporter shows robust intestinal GFP upon infection or translation inhibition; zip-2 loss blocks irg-1 induction in many contexts; genome-wide RNAi screens used the reporter to identify upstream regulators. | Reporter induction by translation stress/infection; zip-2 dependence; RNAi screen hits include mitochondrial and nuclear import genes | Dunbar (RNAi screens), Dunbar analysis, McEwan 2012 (dunbar2013analyzingtherole pages 25-57, dunbar2013analyzingtherole pages 117-121, mcewan2012hosttranslationalinhibition pages 2-3) | N/A, https://doi.org/10.1016/j.chom.2012.02.008, https://doi.org/10.1016/j.chom.2012.02.007 |

Table: Compact evidence table summarizing identity, expression, regulation, stimuli, unknowns, and reporter phenotypes for C. elegans irg-1 with citations to primary sources; useful as a quick-reference for functional annotation and experimental context.

Caveats on gene symbol ambiguity and organism specificity
- The symbol “irg-1” is used for unrelated proteins in other taxa (e.g., mammalian ACOD1). All claims here refer specifically to C. elegans irg-1 (C07G3.2; UniProt O16327). When surveying literature, ensure the organism and gene ID match this nematode gene. (dunbar2012c.elegansdetects pages 1-2)

References

1. (dunbar2012c.elegansdetects pages 1-2): Tiffany L. Dunbar, Zhi Yan, Keir M. Balla, Margery G. Smelkinson, and Emily R. Troemel. C. elegans detects pathogen-induced translational inhibition to activate immune signaling. Cell host & microbe, 11 4:375-86, Apr 2012. URL: https://doi.org/10.1016/j.chom.2012.02.008, doi:10.1016/j.chom.2012.02.008. This article has 259 citations and is from a highest quality peer-reviewed journal.

2. (dunbar2012c.elegansdetects pages 2-3): Tiffany L. Dunbar, Zhi Yan, Keir M. Balla, Margery G. Smelkinson, and Emily R. Troemel. C. elegans detects pathogen-induced translational inhibition to activate immune signaling. Cell host & microbe, 11 4:375-86, Apr 2012. URL: https://doi.org/10.1016/j.chom.2012.02.008, doi:10.1016/j.chom.2012.02.008. This article has 259 citations and is from a highest quality peer-reviewed journal.

3. (mcewan2012hosttranslationalinhibition pages 2-3): Deborah L. McEwan, Natalia V. Kirienko, and Frederick M. Ausubel. Host translational inhibition by pseudomonas aeruginosa exotoxin a triggers an immune response in caenorhabditis elegans. Cell host & microbe, 11 4:364-74, Apr 2012. URL: https://doi.org/10.1016/j.chom.2012.02.007, doi:10.1016/j.chom.2012.02.007. This article has 249 citations and is from a highest quality peer-reviewed journal.

4. (dunbar2012c.elegansdetects pages 9-10): Tiffany L. Dunbar, Zhi Yan, Keir M. Balla, Margery G. Smelkinson, and Emily R. Troemel. C. elegans detects pathogen-induced translational inhibition to activate immune signaling. Cell host & microbe, 11 4:375-86, Apr 2012. URL: https://doi.org/10.1016/j.chom.2012.02.008, doi:10.1016/j.chom.2012.02.008. This article has 259 citations and is from a highest quality peer-reviewed journal.

5. (hajdu2023lysosomerelatedorganellespromote pages 7-10): Gábor Hajdú, Milán Somogyvári, Péter Csermely, and Csaba Sőti. Lysosome-related organelles promote stress and immune responses in c. elegans. Communications Biology, Sep 2023. URL: https://doi.org/10.1038/s42003-023-05246-7, doi:10.1038/s42003-023-05246-7. This article has 21 citations and is from a peer-reviewed journal.

6. (hajdu2023lysosomerelatedorganellespromote pages 10-11): Gábor Hajdú, Milán Somogyvári, Péter Csermely, and Csaba Sőti. Lysosome-related organelles promote stress and immune responses in c. elegans. Communications Biology, Sep 2023. URL: https://doi.org/10.1038/s42003-023-05246-7, doi:10.1038/s42003-023-05246-7. This article has 21 citations and is from a peer-reviewed journal.

7. (taouktsi2023mitochondrialp38mitogenactivated pages 1-2): Eirini Taouktsi, Eleni Kyriakou, Evangelia Voulgaraki, Dimitris Verganelakis, Stefania Krokou, Stamatis Rigas, Gerassimos E. Voutsinas, and Popi Syntichaki. Mitochondrial p38 mitogen-activated protein kinase: insights into its regulation of and role in lonp1-deficient nematodes. International Journal of Molecular Sciences, 24:17209, Dec 2023. URL: https://doi.org/10.3390/ijms242417209, doi:10.3390/ijms242417209. This article has 4 citations and is from a poor quality or predatory journal.

8. (dunbar2012c.elegansdetects pages 3-5): Tiffany L. Dunbar, Zhi Yan, Keir M. Balla, Margery G. Smelkinson, and Emily R. Troemel. C. elegans detects pathogen-induced translational inhibition to activate immune signaling. Cell host & microbe, 11 4:375-86, Apr 2012. URL: https://doi.org/10.1016/j.chom.2012.02.008, doi:10.1016/j.chom.2012.02.008. This article has 259 citations and is from a highest quality peer-reviewed journal.

9. (dunbar2013analyzingtherole pages 25-57): TL Dunbar. Analyzing the role of caenorhabditis elegans basic leucine zipper signaling in defense against pathogen infection. Unknown journal, 2013.

10. (dunbar2013analyzingtherole pages 117-121): TL Dunbar. Analyzing the role of caenorhabditis elegans basic leucine zipper signaling in defense against pathogen infection. Unknown journal, 2013.

11. (dunbar2013analyzingtherole pages 121-125): TL Dunbar. Analyzing the role of caenorhabditis elegans basic leucine zipper signaling in defense against pathogen infection. Unknown journal, 2013.

Citations

1. mcewan2012hosttranslationalinhibition pages 2-3
2. dunbar2013analyzingtherole pages 117-121
3. dunbar2013analyzingtherole pages 121-125
4. hajdu2023lysosomerelatedorganellespromote pages 7-10
5. hajdu2023lysosomerelatedorganellespromote pages 10-11
6. dunbar2013analyzingtherole pages 25-57
7. https://doi.org/10.1016/j.chom.2012.02.008
8. https://doi.org/10.1016/j.chom.2012.02.007
9. https://doi.org/10.1038/s42003-023-05246-7
10. https://doi.org/10.3390/ijms242417209
11. https://doi.org/10.1016/j.chom.2012.02.008;
12. https://doi.org/10.1016/j.chom.2012.02.008,
13. https://doi.org/10.1016/j.chom.2012.02.007,
14. https://doi.org/10.1038/s42003-023-05246-7,
15. https://doi.org/10.3390/ijms242417209,