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gene_id: ocr-2
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gene_info: Name=ocr-2 {ECO:0000313|EMBL:CCD63561.1, ECO:0000313|WormBase:T09A12.3a};
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organism_full: Caenorhabditis elegans.
protein_family: Not specified in UniProt
protein_domains: Ankyrin_rpt. (IPR002110); Ankyrin_rpt-contain_sf. (IPR036770);
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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: O61220
• Protein Description: SubName: Full=Ion transport domain-containing protein {ECO:0000313|EMBL:CCD63561.1};
• Gene Information: Name=ocr-2 {ECO:0000313|EMBL:CCD63561.1, ECO:0000313|WormBase:T09A12.3a}; ORFNames=CELE_T09A12.3 {ECO:0000313|EMBL:CCD63561.1}, T09A12.3 {ECO:0000313|WormBase:T09A12.3a};
• Organism (full): Caenorhabditis elegans.
• Protein Family: Not specified in UniProt
• Key Domains: Ankyrin_rpt. (IPR002110); Ankyrin_rpt-contain_sf. (IPR036770); Ion_trans_dom. (IPR005821); TRPV. (IPR024862); Ank_2 (PF12796)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "ocr-2" 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 'ocr-2' 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 ocr-2 (gene ID: ocr-2, UniProt: O61220) 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: O61220
• Protein Description: SubName: Full=Ion transport domain-containing protein {ECO:0000313|EMBL:CCD63561.1};
• Gene Information: Name=ocr-2 {ECO:0000313|EMBL:CCD63561.1, ECO:0000313|WormBase:T09A12.3a}; ORFNames=CELE_T09A12.3 {ECO:0000313|EMBL:CCD63561.1}, T09A12.3 {ECO:0000313|WormBase:T09A12.3a};
• Organism (full): Caenorhabditis elegans.
• Protein Family: Not specified in UniProt
• Key Domains: Ankyrin_rpt. (IPR002110); Ankyrin_rpt-contain_sf. (IPR036770); Ion_trans_dom. (IPR005821); TRPV. (IPR024862); Ank_2 (PF12796)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "ocr-2" 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 'ocr-2' 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 ocr-2 (gene ID: ocr-2, UniProt: O61220) 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
We verified that the target is Caenorhabditis elegans ocr-2, a TRPV-subfamily ion channel subunit that functions with OSM-9; the organism and functional identity are consistent with experimental studies demonstrating OSM-9/OCR-2 as a heteromeric, warmth-responsive TRPV channel in C. elegans sensory neurons (particularly ADL) (ohnishi2020osm9andocr2 pages 1-2, ohnishi2020osm9andocr2 pages 8-9). The literature below focuses strictly on C. elegans OCR-2/OSM-9 biology per the mandate to avoid cross-organism symbol ambiguity.

1) Key concepts and definitions
- Molecular identity and family: ocr-2 encodes a transient receptor potential vanilloid (TRPV)-like channel subunit. Together with OSM-9, it forms a functional TRPV channel required for thermosensory signaling and multiple chemosensory modalities in C. elegans (ohnishi2020osm9andocr2 pages 1-2, ohnishi2020osm9andocr2 pages 8-9).
- Channel assembly: OSM-9 and OCR-2 act cooperatively; single subunits alone do not confer warming-evoked currents, whereas co-expression yields a functional, heat-responsive channel, consistent with heteromeric TRPV assembly (ohnishi2020osm9andocr2 pages 7-8, ohnishi2020osm9andocr2 pages 11-12).
- Sensory cilia context: OCR-2/OSM-9 signals in sensory cilia. TRPV-family channels require intraflagellar transport (IFT) for vectorial movement within cilia, and the ciliary transition zone (TZ) functions as a diffusion/gating barrier controlling membrane protein entry/exit (burght2019signalingcompartmentat pages 19-22).

2) Recent developments and latest research (emphasis 2023–2024)
- Cilia trafficking controls response dynamics: A 2024 study dissected the roles of cilia structure and IFT in shaping chemosensory responses. Acute or prolonged IFT inhibition can generate ectopic periciliary membrane compartment (PCMC) branches that mislocalize ciliary signaling proteins including OSM-9, altering odorant response desensitization despite preserved primary responses in some contexts (AWA). These data highlight how trafficking/localization of TRPV components modulate sensory coding, even without gross cilia loss (PLOS Biology, Nov 26, 2024; https://doi.org/10.1371/journal.pbio.3002892) (philbrook2024ciliastructureand pages 10-11, philbrook2024ciliastructureand pages 16-18).
- Osmolarity and egg-laying inhibition: A 2024 preprint reported that hyperosmotic conditions inhibit egg-laying via both sensory and biophysical mechanisms; under their conditions, ocr-2(vs29) mutants were still inhibited, suggesting OCR-2 is not solely required for this form of inhibition (bioRxiv, Dec 31, 2024; https://doi.org/10.1101/2024.12.30.630790) (medrano2024osmolarityregulatesc. pages 28-33).

3) Current applications and real-world implementations
- Reconstitution of TRPV thermosensitivity: Co-expression of OSM-9 and OCR-2 in Xenopus oocytes demonstrated warming-evoked inward currents with outward-rectifying I–V relationships, establishing a tractable heterologous system to probe TRPV gating and ion conduction for the worm channel complex (Scientific Reports, Oct 2020; https://doi.org/10.1038/s41598-020-75302-3) (ohnishi2020osm9andocr2 pages 7-8, ohnishi2020osm9andocr2 pages 11-12).
- Behavioral neurogenetics in C. elegans: Genetic rescue and neuron-specific expression were used to link OSM-9/OCR-2 function in ADL to warmth responses and temperature acclimatisation; ectopic expression in a non-warmth-sensing neuron (ASER) conferred warming responsiveness, a powerful application of in vivo functional reconstitution (ohnishi2020osm9andocr2 pages 5-6, ohnishi2020osm9andocr2 pages 1-2).
- Endocannabinoid modulation of TRP-dependent behaviors: In vivo pharmacology and genetics showed that 2-AG engages TRP channel–dependent pathways to stimulate monoamine (5-HT and DA) release and modulate locomotory behavior, demonstrating utility of C. elegans as a model for TRP-linked neuromodulation (J. Neurosci., May 2019; https://doi.org/10.1523/JNEUROSCI.2371-18.2019) (oakes2019cannabinoidsstimulatethe pages 3-4, oakes2019cannabinoidsstimulatethe pages 9-10).

4) Expert opinions and analyses from authoritative sources
- Ciliary transport and gating as a framework: A 2019 synthesis on ciliary signaling and IFT emphasizes that intraflagellar transport is required for vectorial movement of TRPV channels in the ciliary membrane and that the transition zone establishes a selective barrier controlling receptor/cargo trafficking—principles that frame OCR-2/OSM-9 localization and signaling in cilia (bioRxiv, 2020 posting of 2019 study; https://doi.org/10.1101/861955) (burght2019signalingcompartmentat pages 19-22).

5) Relevant statistics and data from recent studies
- Thermosensory currents and temperature range: Co-expression of OSM-9 and OCR-2 in oocytes produced warming-evoked inward currents upon heating to approximately 35–36°C, with outward-rectifying I–V curves; neither subunit alone was heat-responsive (Scientific Reports, 2020; https://doi.org/10.1038/s41598-020-75302-3) (ohnishi2020osm9andocr2 pages 7-8, ohnishi2020osm9andocr2 pages 11-12).
- In vivo thermosensory phenotypes: osm-9 and ocr-2 single mutants exhibit reduced warming-evoked Ca2+ responses in ADL over ~13–27°C, rescued by cell-specific cDNA expression, supporting cell-autonomous roles; double/triple mutant responses suggest compensatory mechanisms (Scientific Reports, 2020; https://doi.org/10.1038/s41598-020-75302-3) (ohnishi2020osm9andocr2 pages 7-8, ohnishi2020osm9andocr2 pages 5-6).
- Endocannabinoid dose–response: 2-AG inhibited locomotion dose-dependently with an IC50 near 3 μM; inhibition required serotonergic and dopaminergic signaling and involved TRP-channel–dependent monoamine release, establishing quantitative neuromodulatory impact (J. Neurosci., 2019; https://doi.org/10.1523/JNEUROSCI.2371-18.2019) (oakes2019cannabinoidsstimulatethe pages 3-4, oakes2019cannabinoidsstimulatethe pages 9-10).

Detailed functional annotation of ocr-2
Primary molecular function and substrates
- Channel class: OCR-2 is a TRPV-subfamily ion channel subunit. In heteromer with OSM-9, it forms an ion channel that is directly heat-activated in both heterologous expression (oocytes) and in vivo reconstitution, with properties resembling vertebrate TRPVs (outward-rectifying I–V) (ohnishi2020osm9andocr2 pages 7-8, ohnishi2020osm9andocr2 pages 11-12).
- Stimuli: Heat is a direct stimulus for the OSM-9/OCR-2 channel; OSM-9/OCR-2 acts as an accessorial warmth receptor in ADL neurons contributing to temperature acclimatisation (ohnishi2020osm9andocr2 pages 1-2, ohnishi2020osm9andocr2 pages 8-9). Genetic literature also supports roles in chemosensation and mechanosensation across neuron types, consistent with polymodal TRPV function (ohnishi2020osm9andocr2 pages 8-9).
- Ion selectivity: The oocyte recordings demonstrate macroscopic currents and outward rectification; specific ionic selectivity ratios were not provided in the excerpts, but the behavior and I–V features are consistent with cation-permeable TRPV channels (ohnishi2020osm9andocr2 pages 7-8, ohnishi2020osm9andocr2 pages 11-12).

Subunit composition and codependence
- Heteromerization: Functional heat responses require co-expression of OSM-9 and OCR-2; each alone is insufficient. In vivo, ciliary colocalization is reported to be codependent, and single-mutant phenotypes/rescues support heteromeric channel function (ohnishi2020osm9andocr2 pages 8-9, ohnishi2020osm9andocr2 pages 5-6).

Cellular/subcellular localization and trafficking
- Sensory cilia localization: OCR-2/OSM-9 localize to sensory cilia, where TRPV channels are trafficked by IFT; a transition zone barrier modulates ciliary entry/exit (burght2019signalingcompartmentat pages 19-22).
- IFT dependence and mislocalization under trafficking stress: Conditional IFT inhibition or IFT mutants cause formation of PCMC branches and mislocalization of OSM-9 and other ciliary signaling proteins from cilia to PCMC branches in AWA, altering desensitization kinetics while sometimes sparing primary responses, highlighting the importance of precise localization for response dynamics (PLOS Biology, 2024; https://doi.org/10.1371/journal.pbio.3002892) (philbrook2024ciliastructureand pages 10-11, philbrook2024ciliastructureand pages 16-18).

Neuronal expression and organismal roles
- Neuron types and behaviors: OCR-2 functions with OSM-9 in multiple sensory neurons. In ADL, OSM-9/OCR-2 mediate warmth responses and contribute to temperature acclimatisation (ohnishi2020osm9andocr2 pages 1-2, ohnishi2020osm9andocr2 pages 5-6). In nociceptive contexts, a heteromeric OSM-9/OCR-2 channel is required for aversive chemical responses such as to 1-octanol, consistent with roles in ASH nociceptors (J. Neurosci., 2019; https://doi.org/10.1523/JNEUROSCI.2371-18.2019) (oakes2019cannabinoidsstimulatethe pages 9-10). More broadly, modeling and synthesis works list OCR-2 as a TRPV nociceptor subunit with roles in chemosensation and thermosensation across amphid neurons, though some of these are preprints (castano2025modelingtrpvlikereceptors pages 13-17, pieroni2025identificationofmolecular pages 27-29).
- Osmosensation and egg-laying context: Hyperosmotic environments inhibit egg-laying via sensory and mechanical pathways; one 2024 study reported that ocr-2(vs29) mutants remained inhibited under high osmolarity, suggesting that OCR-2 is not alone sufficient to mediate this inhibition (bioRxiv, 2024; https://doi.org/10.1101/2024.12.30.630790) (medrano2024osmolarityregulatesc. pages 28-33).

Modulation by endogenous and exogenous ligands
- Endocannabinoids: 2-AG engages TRP channel–dependent mechanisms to stimulate serotonin and dopamine release and modulate locomotory behavior. Although this work did not isolate OCR-2 specifically, it implicates TRPV-like channels in cannabinoid-dependent neuromodulation in C. elegans, intersecting with OCR-2/OSM-9–dependent aversive responses (J. Neurosci., 2019; https://doi.org/10.1523/JNEUROSCI.2371-18.2019) (oakes2019cannabinoidsstimulatethe pages 3-4, oakes2019cannabinoidsstimulatethe pages 9-10).
- Vanilloids/terpenes: Preprint and synthesis studies suggest vanilloid-like ligands (e.g., capsaicin analogues) and certain terpenes can modulate C. elegans nociceptive behaviors via TRPV-like channels including OCR-2/OSM-9; structural modeling favors OCR-2 as a primary vanilloid target in C. elegans (ChemRxiv, 2025; https://doi.org/10.26434/chemrxiv-2025-bhspb) (castano2025modelingtrpvlikereceptors pages 13-17). These insights are preliminary and should be interpreted cautiously pending peer review.
- Octopamine: Within the cannabinoid-modulation study, octopamine signaling components are discussed in the broader monoaminergic modulation of aversive behaviors; however, direct OCR-2 modulation by octopamine was not supported by the provided excerpts (oakes2019cannabinoidsstimulatethe pages 9-10, oakes2019cannabinoidsstimulatethe pages 3-4).

Embedded summary table of key findings
| Topic | Key finding | Neuron / Cells | Subcellular localization | Evidence type | Year & Source (URL) |
|---|---|---|---|---|---|
| Thermosensation: OSM-9/OCR-2 heteromeric warm receptor | OSM-9 and OCR-2 act cooperatively as an accessorial warmth-sensing TRPV complex required for temperature acclimatisation and ADL warming-evoked Ca2+ responses. | ADL (and sufficiency shown in reconstituted ASER) | Sensory cilia; codependent ciliary colocalisation | Genetic mutants, Ca2+ imaging, rescue, behavioral assays | 2020, Scientific Reports — https://doi.org/10.1038/s41598-020-75302-3 (ohnishi2020osm9andocr2 pages 8-9, ohnishi2020osm9andocr2 pages 5-6) |
| Heterologous electrophysiology: Xenopus oocyte currents require co-expression | Neither OSM-9 nor OCR-2 alone produced heat-evoked currents; co-expression yields warming-induced inward currents with outward-rectifying I–V, supporting heteromeric channel function. | Xenopus oocytes; ectopic expression in ASER | Heterologous membrane (oocyte) / reconstituted neuronal membrane | Two-electrode voltage-clamp electrophysiology; reconstitution experiments | 2020, Scientific Reports — https://doi.org/10.1038/s41598-020-75302-3 (ohnishi2020osm9andocr2 pages 7-8, ohnishi2020osm9andocr2 pages 11-12) |
| Ciliary localization & IFT dependence; mislocalization to PCMC branches (Philbrook 2024) | Acute inhibition of IFT or IFT mutants cause ectopic periciliary membrane compartment (PCMC) branches that mislocalize OSM-9 (and some OCR-2) away from cilia, altering response dynamics and desensitization. | AWA (also effects seen across chemosensory neurons such as ASH) | Cilia base/tip and ectopic PCMC branches; ciliary vs periciliary redistribution | Live imaging (tagged receptors), Ca2+ imaging, genetic IFT perturbation | 2024, PLOS Biology — https://doi.org/10.1371/journal.pbio.3002892 (philbrook2024ciliastructureand pages 10-11, philbrook2024ciliastructureand pages 16-18) |
| IFT & transition-zone (TZ) gating of TRPV channels (van der Burght 2019) | Intraflagellar transport is required for vectorial movement and enrichment of TRPV-type channels in cilia; transition zone acts as a diffusion/gating barrier controlling ciliary entry. | Ciliated sensory neurons broadly | Transition zone and ciliary axoneme (tip/middle) | IFT perturbation, localization studies, review/bioRxiv synthesis citing Qin 2005 and others | 2019, bioRxiv — https://doi.org/10.1101/861955 (burght2019signalingcompartmentat pages 19-22) |
| Aversive chemical sensitivity & cannabinoid-linked modulation (1-octanol, etc.) | Aversive chemical (e.g., 1-octanol) nocifensive responses require a heteromeric OSM-9/OCR-2 TRPV channel in sensory neurons; cannabinoids/endocannabinoid signaling can engage TRP channels to modulate monoamine release and behavior. | ASH nociceptors; monoaminergic neurons (serotonin/dopamine release) | Sensory cilia (TRPV localization in cilia) and monoaminergic terminals | Behavioral assays, pharmacology, genetic mutants, neurochemical assays | 2019, J. Neurosci. — https://doi.org/10.1523/JNEUROSCI.2371-18.2019 (oakes2019cannabinoidsstimulatethe pages 9-10, oakes2019cannabinoidsstimulatethe pages 3-4) |
| Osmolarity & egg‑laying inhibition; ocr-2 mutants (Medrano 2024) | Hyperosmotic conditions inhibit egg-laying via sensory and biophysical mechanisms; reported ocr-2(vs29) mutants remained inhibited in high osmolarity, suggesting OCR-2 is not solely required for this inhibition (possible brood-size/confound noted). | HSNs, uv1s and chemosensory neurons; broader egg‑laying circuit | Sensory cilia (uv1/other chemosensory neuron localization implicated) | Behavioral assays, optogenetics, mutant analysis (bioRxiv preprint) | 2024, bioRxiv — https://doi.org/10.1101/2024.12.30.630790 (medrano2024osmolarityregulatesc. pages 28-33) |
| TRPV structural/modeling & vanilloid interactions (preprint summary) | Structural modeling and MD docking suggest OCR-2 (and OSM-9) may interact with vanilloid-like ligands (capsaicin analogues) and support OCR-2 as a relevant antinociceptive target in C. elegans (preprint synthesis). | Nociceptive sensory neurons (general TRPV-expressing cells) | Predicted pore/ankyrin-repeat and ligand-interaction regions (modeled) | In silico modeling (AlphaFold3, docking, MD) and literature synthesis — preprint | 2025, ChemRxiv (preprint) — https://doi.org/10.26434/chemrxiv-2025-bhspb (castano2025modelingtrpvlikereceptors pages 13-17) |
| Neuron expression spectrum & alleles (functional characterization preprint) | OCR-2 is reported expressed in many amphid sensory neurons (ASH, AWA, AWC, ASE, ADF, ASI, ASJ, ASK, IL2s) with characterized loss‑of‑function/deletion alleles linked to altered nociceptive and chemosensory behaviors (preprint). | ASH, AWA, AWC, ASE, ADF, ASI, ASJ, ASK, IL2s (amphid neurons) | Sensory cilia (amphid channel localization) | Genetic alleles, behavioral phenotyping, functional assays — preprint | 2025, bioRxiv (preprint) — https://doi.org/10.1101/2025.08.19.670888 (pieroni2025identificationofmolecular pages 27-29, pieroni2025identificationofmolecular pages 19-20) |

Table: Compact table summarizing experimental and modeling evidence for C. elegans OCR-2 (TRPV) covering function, localization, neurons, evidence types and citations for rapid reference.

Synthesis and outlook
The strongest evidence defines OCR-2 as a TRPV-family subunit that, together with OSM-9, forms a heat-responsive cation channel in sensory cilia, shaping thermosensory signaling in ADL and contributing to chemosensory and nociceptive behaviors across neuron types. Recent work (2024) emphasizes that continuous IFT and precise spatial organization of ciliary signaling components—including TRPV subunits—critically tune sensory response dynamics, particularly desensitization and adaptation. Endocannabinoid-dependent modulation of TRP pathways provides a tractable entry point to dissect neuromodulatory control of TRPV-dependent behaviors in vivo. Open questions include precise ionic selectivity and pharmacology of native OSM-9/OCR-2 channels, neuron-by-neuron contributions in polymodal nociception and osmosensation, and the molecular logic by which the ciliary transition zone and IFT adaptively regulate TRPV trafficking and signaling.

Citations (URLs and dates provided above): (ohnishi2020osm9andocr2 pages 1-2, ohnishi2020osm9andocr2 pages 8-9, ohnishi2020osm9andocr2 pages 7-8, ohnishi2020osm9andocr2 pages 11-12, burght2019signalingcompartmentat pages 19-22, philbrook2024ciliastructureand pages 10-11, philbrook2024ciliastructureand pages 16-18, medrano2024osmolarityregulatesc. pages 28-33, ohnishi2020osm9andocr2 pages 5-6, oakes2019cannabinoidsstimulatethe pages 3-4, oakes2019cannabinoidsstimulatethe pages 9-10, castano2025modelingtrpvlikereceptors pages 13-17, pieroni2025identificationofmolecular pages 27-29)

References

1. (ohnishi2020osm9andocr2 pages 1-2): Kohei Ohnishi, Shigeru Saito, Toru Miura, Akane Ohta, Makoto Tominaga, Takaaki Sokabe, and Atsushi Kuhara. Osm-9 and ocr-2 trpv channels are accessorial warm receptors in caenorhabditis elegans temperature acclimatisation. Scientific Reports, Oct 2020. URL: https://doi.org/10.1038/s41598-020-75302-3, doi:10.1038/s41598-020-75302-3. This article has 42 citations and is from a peer-reviewed journal.

2. (ohnishi2020osm9andocr2 pages 8-9): Kohei Ohnishi, Shigeru Saito, Toru Miura, Akane Ohta, Makoto Tominaga, Takaaki Sokabe, and Atsushi Kuhara. Osm-9 and ocr-2 trpv channels are accessorial warm receptors in caenorhabditis elegans temperature acclimatisation. Scientific Reports, Oct 2020. URL: https://doi.org/10.1038/s41598-020-75302-3, doi:10.1038/s41598-020-75302-3. This article has 42 citations and is from a peer-reviewed journal.

3. (ohnishi2020osm9andocr2 pages 7-8): Kohei Ohnishi, Shigeru Saito, Toru Miura, Akane Ohta, Makoto Tominaga, Takaaki Sokabe, and Atsushi Kuhara. Osm-9 and ocr-2 trpv channels are accessorial warm receptors in caenorhabditis elegans temperature acclimatisation. Scientific Reports, Oct 2020. URL: https://doi.org/10.1038/s41598-020-75302-3, doi:10.1038/s41598-020-75302-3. This article has 42 citations and is from a peer-reviewed journal.

4. (ohnishi2020osm9andocr2 pages 11-12): Kohei Ohnishi, Shigeru Saito, Toru Miura, Akane Ohta, Makoto Tominaga, Takaaki Sokabe, and Atsushi Kuhara. Osm-9 and ocr-2 trpv channels are accessorial warm receptors in caenorhabditis elegans temperature acclimatisation. Scientific Reports, Oct 2020. URL: https://doi.org/10.1038/s41598-020-75302-3, doi:10.1038/s41598-020-75302-3. This article has 42 citations and is from a peer-reviewed journal.

5. (burght2019signalingcompartmentat pages 19-22): Servaas N. van der Burght, Suzanne Rademakers, Jacque-Lynne Johnson, Chunmei Li, Gert-Jan Kremers, Adriaan B. Houtsmuller, Michel R. Leroux, and Gert Jansen. Signaling compartment at the ciliary tip is formed and maintained by intraflagellar transport and functions as sensitive salt detector. bioRxiv, Dec 2019. URL: https://doi.org/10.1101/861955, doi:10.1101/861955. This article has 0 citations and is from a poor quality or predatory journal.

6. (philbrook2024ciliastructureand pages 10-11): Alison Philbrook, Michael P. O’Donnell, Laura Grunenkovaite, and Piali Sengupta. Cilia structure and intraflagellar transport differentially regulate sensory response dynamics within and between c. elegans chemosensory neurons. PLOS Biology, 22:e3002892, Nov 2024. URL: https://doi.org/10.1371/journal.pbio.3002892, doi:10.1371/journal.pbio.3002892. This article has 8 citations and is from a highest quality peer-reviewed journal.

7. (philbrook2024ciliastructureand pages 16-18): Alison Philbrook, Michael P. O’Donnell, Laura Grunenkovaite, and Piali Sengupta. Cilia structure and intraflagellar transport differentially regulate sensory response dynamics within and between c. elegans chemosensory neurons. PLOS Biology, 22:e3002892, Nov 2024. URL: https://doi.org/10.1371/journal.pbio.3002892, doi:10.1371/journal.pbio.3002892. This article has 8 citations and is from a highest quality peer-reviewed journal.

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Citations

1. burght2019signalingcompartmentat pages 19-22
2. oakes2019cannabinoidsstimulatethe pages 9-10
3. castano2025modelingtrpvlikereceptors pages 13-17
4. philbrook2024ciliastructureand pages 10-11
5. philbrook2024ciliastructureand pages 16-18
6. oakes2019cannabinoidsstimulatethe pages 3-4
7. pieroni2025identificationofmolecular pages 27-29
8. pieroni2025identificationofmolecular pages 19-20
9. https://doi.org/10.1371/journal.pbio.3002892
10. https://doi.org/10.1101/2024.12.30.630790
11. https://doi.org/10.1038/s41598-020-75302-3
12. https://doi.org/10.1523/JNEUROSCI.2371-18.2019
13. https://doi.org/10.1101/861955
14. https://doi.org/10.26434/chemrxiv-2025-bhspb
15. https://doi.org/10.1101/2025.08.19.670888
16. https://doi.org/10.1038/s41598-020-75302-3,
17. https://doi.org/10.1101/861955,
18. https://doi.org/10.1371/journal.pbio.3002892,
19. https://doi.org/10.1101/2024.12.30.630790,
20. https://doi.org/10.1523/jneurosci.2371-18.2019,
21. https://doi.org/10.26434/chemrxiv-2025-bhspb,
22. https://doi.org/10.1101/2025.08.19.670888,