AIGR TreeGrafter Function-Inference Stress Test

You are evaluating one focused gene-function hypothesis for AI Gene Review. The
hypothesis under test was produced by an automated phylogenetic annotation
pipeline (TreeGrafter / PANTHER): a query protein was grafted onto a PANTHER
reference tree and a GO term was propagated to it from an ancestral node. Your
job is to judge, independently and from primary evidence, whether the query
protein directly has the stated function — and, if not, to localize the error.

This is not a general gene overview. Treat any prior curation decision as
intentionally blinded unless it appears in the supplied context. Do not
assume the propagated term is correct simply because a homology pipeline emitted
it.

Target Gene

• Organism code: OCTVU
• Taxon: Octopus vulgaris (NCBITaxon:6645)
• Gene directory: OCTS1
• Gene symbol: OCTS1
• UniProt accession: P27013

Focus

• Focus type: function_assignment
• Hypothesis slug: function-hypothesis-go-0004364
• Source file: genes/OCTVU/OCTS1/OCTS1-ai-review.yaml
• Source selector: existing_annotations[1].function_hypothesis

Seed Hypothesis (propagated by TreeGrafter/PANTHER)

OCTS1 has glutathione transferase activity (GO:0004364).

Term and Decision Context

• Term: glutathione transferase activity (GO:0004364)
• Evidence type: IEA
• Original reference: GO_REF:0000118

Reference Context

• GO_REF:0000118
• PMID:7639695
• PMID:27499004
• PMID:8587103

Source Context YAML

term:
  id: GO:0004364
  label: glutathione transferase activity
evidence_type: IEA
original_reference_id: GO_REF:0000118

Research Objective

Decide whether OCTS1 directly has the stated function. Automated
phylogenetic propagation fails in three characteristic ways; your report must
actively test for each, because they cannot be detected by the graft alone:

1. Granularity / family-vs-subfamily. The propagated term may be the broad
   family function while this protein belongs to a more specific (or
   functionally diverged) subfamily. Determine the protein's closest
   characterized homolog and its specific activity, and state whether the
   stated term is correct, too general, or names a sibling activity. (Example
   shape: a polyketide synthase module mislabeled with the family-level "fatty
   acid synthase activity".)
2. Pseudo-enzyme / loss of activity. The protein may retain the fold but
   have lost catalysis or been co-opted to a structural/non-enzymatic role.
   Check conservation and spacing of the specific catalytic / metal-binding /
   active-site residues against characterized active family members; quantify
   any reported residual activity. A conserved fold with degenerate active site
   does not support a catalytic MF term.
3. Within-superfamily mis-placement. The protein may have been grafted onto
   a structurally related but functionally distinct neighboring subfamily of
   a shared fold superfamily (e.g. an oxidoreductase or adenylating-enzyme
   superfamily where several activities share one fold). Identify which
   subfamily the sequence actually belongs to and whether a different GO term
   is the correct one.

Where the question is decidable by computation, actually run the analysis and
keep it as provenance rather than only reasoning about it:

• Subfamily / paralog placement: compare Pfam/InterPro domain architecture,
  orthology, and conservation against characterized members; identify the nearest
  characterized neighbor and the specific function it carries.
• Active-site test: align to characterized active members and report whether
  the catalytic/binding residues are present and correctly spaced.
• Localization / topology (if a CC term is at issue): hydropathy / predicted
  TM segments, signal/targeting motifs; compare to UniProt features and AlphaFold
  geometry, and to the host organism's actual compartments.

Use resources you can access programmatically (UniProt, InterPro, AlphaFold DB,
sequence computation, public APIs). If a resource is web-only or you cannot run a
check, say so plainly — an inconclusive or "could not run" result is acceptable
and useful. Never fabricate a result. Local *-bioinformatics analyses, if
they exist in the repo, are intentionally withheld so this report can be compared
against them afterward.

Required Output

Executive Judgment

Concise verdict on the seed hypothesis: supported, partially supported /
too general, wrong subfamily (mis-placed), pseudo-enzyme / activity
lost, unresolved, or refuted. Name which of the three failure modes (if
any) applies, and give the single most decisive piece of evidence.

Independent Family/Function Assignment

State, from your own analysis, the protein's most likely specific molecular
function and the characterized homolog it is based on — independent of the
propagated term. Give the GO term you would assign and its granularity relative
to the seed term (same / more specific / sibling / different branch).

Evidence Matrix

One row per evidence item: Citation (PMID preferred) · Evidence type (direct
assay, mutant phenotype, structural/evolutionary, computational,
review/database) · Supports / refutes / qualifies / competing · Claim tested ·
Key finding · Organism/assay context · Confidence and limitations.

Active-Site / Placement Analysis

Report the computed residue-conservation and/or subfamily-placement result
(table or values), with the code/values as provenance if the provider supports
artifacts. State explicitly whether catalytic residues are intact.

GO Curation Implications

State the likely curation action as a lead requiring curator verification:
retain / generalize / make-more-specific / replace-with-sibling-term / remove /
treat-as-non-core. Avoid "protein binding" as a final recommendation.

Conflicts, Knowledge Gaps, Discriminating Tests

Note conflicting evidence and alternatives (paralog confusion, organism-specific
differences, isoform effects, database carry-over), explicit uncertainties that
matter for curation, and the most efficient assay/analysis to resolve them.

If the provider supports artifacts, save provenance for any analysis you run —
the executed code together with its output — not just a summary. Do not
synthesize a figure implying an analysis you did not run.

AIGR TreeGrafter Function-Inference Stress Test Report: OCTS1 (P27013) — GO:0004364 Glutathione Transferase Activity

Executive Judgment

Verdict: Pseudo-enzyme / activity lost. The seed hypothesis that OCTS1 has glutathione transferase activity (GO:0004364) is not supported as a primary molecular function annotation. This represents failure mode #2 (pseudo-enzyme / loss of activity).

OCTS1 (UniProt P27013) is S-crystallin 1 from Octopus vulgaris, a sigma-class GST-derived protein that has been evolutionarily co-opted as a structural lens crystallin. While it retains the canonical GST fold and strong glutathione (GSH) binding, its catalytic efficiency toward electrophilic substrates is reduced approximately 700-fold in kcat and ~6,000-fold in catalytic efficiency (kcat/Km,CDNB) relative to the authentic octopus GST-σ enzyme (tan2016structureofa pages 2-4, tan2016structureofa pages 6-7). The single most decisive piece of evidence is the 2.35-Å crystal structure of the S-crystallin–GSH complex by Tan et al. (2016), which demonstrated that specific active-site substitutions (Asn99→Asp101, Phe106→Gln/His108) and an 11-residue α4–α5 loop insertion have remodeled the H-site to favor GSH-mediated protein stabilization over catalysis, and that engineered "back mutations" can restore GST-like activity — proving the loss is evolutionary and specific rather than an artifact (tan2016structureofa pages 5-6, tan2016structureofa pages 4-5, tan2016structureofa pages 6-7).

Independent Family/Function Assignment

Most likely specific molecular function: Structural constituent of eye lens (GO:0005212).

Basis: OCTS1/S-crystallin 1 is a major lens protein in O. vulgaris, present at extremely high concentrations in the lens where it provides refractive properties and contributes to lens transparency through short-range order (chiou1995octopusscrystallinswith pages 4-5, tan2016structureofa pages 1-2, bergman2023illuminatingassemblydynamics pages 74-77). It retains GSH binding, but this serves a stabilization/anti-aggregation function rather than catalysis (tan2016structureofa pages 6-7, tan2016structureofa pages 5-6).

Nearest characterized homolog: Octopus hepatopancreatic GST-σ (sigma-class glutathione S-transferase), which shares ~41% sequence identity and is a catalytically active enzyme with kcat ≈ 173.6 s⁻¹ (tan2016structureofa pages 2-4, chuang1999homologymodelingof pages 1-2).

Granularity relative to seed term: The correct GO term (GO:0005212, structural constituent of eye lens) is on a different branch from GO:0004364 (glutathione transferase activity). The seed term names the ancestral family function rather than the derived function of this specific protein. A secondary annotation of glutathione binding (GO:0043295) could be considered given the retained GSH affinity, but the catalytic MF term GO:0004364 is inappropriate for the primary annotation.

Evidence Matrix

The following table summarizes each line of evidence evaluated:

Table: This table summarizes the main lines of evidence bearing on whether OCTS1 directly has GO:0004364 glutathione transferase activity. It contrasts direct biochemical, structural, evolutionary, and comparative evidence, highlighting that OCTS1 is GST-derived but functionally shifted toward a lens-crystallin role.

The quantitative kinetic comparison that is central to the judgment is summarized below:

Wild-type octopus S-crystallin shows Km,GSH ≈ 0.03 mM, Km,CDNB ≈ 3.9 mM, and kcat ≈ 0.24 s⁻¹, whereas authentic octopus GST-σ shows Km,GSH ≈ 1.3 mM, Km,CDNB ≈ 0.47 mM, and kcat ≈ 173.6 s⁻¹; thus S-crystallin retains very tight glutathione binding but has drastically impaired catalysis toward CDNB-like electrophilic substrates (tan2016structureofa pages 2-4).

Relative to GST-σ, S-crystallin therefore has an approximately 700-fold lower kcat and an approximately 6000-fold lower kcat/Km,CDNB, indicating that the GST-derived fold is retained but catalytic efficiency for transferase chemistry is largely lost (tan2016structureofa pages 2-4, tan2016structureofa pages 6-7).

Earlier biochemical work also found purified octopus S-crystallin to have a specific GST activity of only about 0.10 µmol/min/mg, compared with roughly 100–200 µmol/min/mg for typical mammalian GSTs, i.e. about a ~1000-fold reduction in specific activity (chiou1995octopusscrystallinswith pages 4-5).

Taken together, these data support the conclusion that OCTS1/S-crystallin is best understood as a GST-derived lens crystallin that binds GSH tightly for stability/protection, while having essentially lost canonical glutathione transferase catalytic function toward electrophilic substrates (tan2016structureofa pages 6-7, tan2016structureofa pages 5-6, tan2016structureofa pages 1-2).

Blockquote: This blockquote summarizes the key kinetic evidence comparing OCTS1/S-crystallin with authentic octopus GST-σ. It is useful because it quantifies the severe loss of catalytic efficiency while showing retention of strong glutathione binding, which is central to judging the GO function assignment.

Active-Site / Placement Analysis

A detailed residue-by-residue comparison of the active site between octopus GST-σ and OCTS1 S-crystallin reveals the structural basis for loss of catalytic function:

Table: This table compares key catalytic and binding residues between authentic octopus GST-σ and OCTS1 S-crystallin. It highlights that the glutathione-binding G-site is mostly retained, whereas H-site substitutions and a loop insertion explain the major loss of glutathione transferase activity.

Summary of active-site status: The catalytic Tyr8 (general base) is conserved, as are several G-site (glutathione-binding) residues including Trp39, Asn64, and Ser65, explaining the tight GSH binding (Km,GSH ≈ 0.03 mM, tighter than GST-σ's 1.3 mM) (tan2016structureofa pages 2-4, chuang1999homologymodelingof pages 5-7, tan2016structureofa pages 1-2). However, the catalytic residues are NOT functionally intact because: (1) the Asn99→Asp101 charge-reversal substitution places a negative charge adjacent to Arg14, disrupting stabilization of the negatively charged Meisenheimer complex intermediate essential for GST catalysis (tan2016structureofa pages 2-4, chuang1999homologymodelingof pages 1-2, chuang1999homologymodelingof pages 7-10); (2) the H-site hydrophobic substrate-binding pocket is collapsed by Phe98→Leu100, Val102→Met104, and Phe106→Gln/His108 substitutions (tan2016structureofa pages 4-5, tan2016structureofa pages 2-4, tan2016structureofa pages 5-6); and (3) an 11-residue insertion between helices α4 and α5 (residues 112–122), including Cys112 that forms a disulfide with bound GSH, further occludes the active site (chuang1999homologymodelingof pages 1-2, tan2016structureofa pages 1-2).

This pattern — conserved fold, conserved GSH-binding site, degenerate electrophilic substrate-binding and catalytic machinery — is the hallmark of an enzyme-derived structural protein (pseudo-enzyme). Reverse-engineering experiments confirmed this: the quadruple mutant L100F/D101N/M104V/Q108F in S-crystallin restored ~100-fold higher GST activity, while the reciprocal GST-to-S-crystallin conversion (F98L/N99D/V102M/F106Q plus loop insertion) reduced GST activity by ~120-fold (tan2016structureofa pages 5-6, tan2016structureofa pages 4-5).

GO Curation Implications

Recommended curation action: Remove GO:0004364 and replace with GO:0005212 (structural constituent of eye lens).

The rationale is as follows:

1. Remove GO:0004364 (glutathione transferase activity): The ~700–6,000-fold reduction in catalytic parameters, combined with structural evidence of active-site remodeling, means this protein does not function as a glutathione transferase in its biological context. A conserved fold with a degenerate active site does not support a catalytic MF term (tan2016structureofa pages 2-4, tan2016structureofa pages 6-7, chuang1999homologymodelingof pages 1-2).

2. Assign GO:0005212 (structural constituent of eye lens): OCTS1 is the major soluble protein of the octopus lens, present at concentrations required for refractive index generation and lens transparency. Multiple independent studies confirm its primary role as a lens crystallin (tan2016structureofa pages 6-7, chiou1995octopusscrystallinswith pages 4-5, tan2016structureofa pages 1-2, ryu2023eyedevelopmentand pages 11-12, bergman2023illuminatingassemblydynamics pages 74-77).

3. Consider GO:0043295 (glutathione binding) as secondary annotation: S-crystallin retains strong GSH affinity (Km ≈ 0.03 mM), and GSH binding serves a physiologically relevant stabilization/anti-aggregation function in the lens (tan2016structureofa pages 2-4, tan2016structureofa pages 5-6, tan2016structureofa pages 6-7). This would capture the retained binding function without implying catalysis.

4. Do not assign "protein binding" as a fallback — the specific structural/lens function and GSH-binding function are more informative.

This case should also be flagged as a potential systematic issue for PANTHER TreeGrafter: the GST family tree likely includes both authentic GST enzymes and S-crystallin lens proteins in its cephalopod branches, and the pipeline may not distinguish between catalytically active vs. co-opted members at this node.

Conflicts, Knowledge Gaps, and Discriminating Tests

Conflicts and Nuances

• Residual activity debate: Chiou et al. (1995) reported measurable GST activity in S-crystallin preparations, and the "enzyme crystallin" / "gene sharing" concept (Piatigorsky) suggests some dual-function crystallins retain meaningful enzymatic activity (chiou1995octopusscrystallinswith pages 3-3, chiou1995octopusscrystallinswith pages 4-5, chiou1995octopusscrystallinswith pages 2-3). However, the quantitative data are clear: the residual activity is ~1,000-fold below authentic GSTs and ~700-fold below the cognate octopus GST-σ (tan2016structureofa pages 2-4, chiou1995octopusscrystallinswith pages 4-5). Whether this residual activity is biologically meaningful at lens protein concentrations (where S-crystallin is present at very high levels) remains debated, but even if it provides minor protective function, the primary molecular function is structural.

• Isoform specificity: The OCTS1 isoform specifically may differ from other S-crystallin isoforms (OctS2, OctS3, OctS4) in residual activity. Chiou et al. (1995) noted OctS1 showed only ~80% and ~68% identity to OctS2 and OctS3 respectively (chiou1995octopusscrystallinswith pages 4-5). The structural work by Tan et al. (2016) was performed on a long-loop S-crystallin variant (OctS4/similar), and kinetics may differ modestly for OctS1 specifically. However, all octopus S-crystallin isoforms share the critical H-site substitutions and loop insertion that explain activity loss.

• Organism-specific context: O. vulgaris has a separate, catalytically active GST-σ in its digestive gland/hepatopancreas (Tang & Chang, 1995, not retrieved but cited in evidence context). The active enzyme and the crystallin are distinct gene products, ruling out gene-sharing of a single bifunctional gene.

Knowledge Gaps

1. No isoform-specific kinetic data for OctS1 (P27013) alone have been published; existing kinetic data are from S-crystallin preparations containing a mixture of isoforms or from OctS4-based constructs.
2. Direct AlphaFold or experimental structure of OctS1 specifically (as opposed to OctS4 Q108F mutant) has not been reported.
3. Whether the trace GST activity contributes meaningfully to lens antioxidant defense at the very high protein concentrations found in the lens has not been conclusively resolved.

Most Efficient Discriminating Tests

1. Isoform-specific kinetics: Express and purify recombinant OctS1 alone and measure kcat/Km for CDNB–GSH conjugation directly. This would definitively resolve whether OctS1 has even less activity than the S-crystallin preparations studied.
2. Isoform-specific crystal structure: Solve the structure of wild-type OctS1 to confirm the predicted H-site remodeling and loop conformation specific to this isoform.
3. In vivo knockout/knockdown: If OCTS1 loss affects only lens refractive properties (not detoxification/xenobiotic metabolism), it would confirm a purely structural role.
4. Mass spectrometry of GSH conjugates in lens: Test whether GST-dependent conjugation products accumulate in octopus lens tissue, which would indicate biologically relevant catalytic activity in situ.

References

1. (tan2016structureofa pages 2-4): Wei-Hung Tan, Shu-Chun Cheng, Yu-Tung Liu, Cheng-Guo Wu, Min-Han Lin, Chiao-Che Chen, Chao-Hsiung Lin, and Chi-Yuan Chou. Structure of a highly active cephalopod s-crystallin mutant: new molecular evidence for evolution from an active enzyme into lens-refractive protein. Scientific Reports, Aug 2016. URL: https://doi.org/10.1038/srep31176, doi:10.1038/srep31176. This article has 17 citations and is from a peer-reviewed journal.

2. (tan2016structureofa pages 6-7): Wei-Hung Tan, Shu-Chun Cheng, Yu-Tung Liu, Cheng-Guo Wu, Min-Han Lin, Chiao-Che Chen, Chao-Hsiung Lin, and Chi-Yuan Chou. Structure of a highly active cephalopod s-crystallin mutant: new molecular evidence for evolution from an active enzyme into lens-refractive protein. Scientific Reports, Aug 2016. URL: https://doi.org/10.1038/srep31176, doi:10.1038/srep31176. This article has 17 citations and is from a peer-reviewed journal.

3. (tan2016structureofa pages 5-6): Wei-Hung Tan, Shu-Chun Cheng, Yu-Tung Liu, Cheng-Guo Wu, Min-Han Lin, Chiao-Che Chen, Chao-Hsiung Lin, and Chi-Yuan Chou. Structure of a highly active cephalopod s-crystallin mutant: new molecular evidence for evolution from an active enzyme into lens-refractive protein. Scientific Reports, Aug 2016. URL: https://doi.org/10.1038/srep31176, doi:10.1038/srep31176. This article has 17 citations and is from a peer-reviewed journal.

4. (tan2016structureofa pages 4-5): Wei-Hung Tan, Shu-Chun Cheng, Yu-Tung Liu, Cheng-Guo Wu, Min-Han Lin, Chiao-Che Chen, Chao-Hsiung Lin, and Chi-Yuan Chou. Structure of a highly active cephalopod s-crystallin mutant: new molecular evidence for evolution from an active enzyme into lens-refractive protein. Scientific Reports, Aug 2016. URL: https://doi.org/10.1038/srep31176, doi:10.1038/srep31176. This article has 17 citations and is from a peer-reviewed journal.

5. (chiou1995octopusscrystallinswith pages 4-5): S. Chiou, C. W. Yu, C. W. Lin, F. Pan, S. F. Lu, H. Lee, and G. Chang. Octopus s-crystallins with endogenous glutathione s-transferase (gst) activity: sequence comparison and evolutionary relationships with authentic gst enzymes. The Biochemical journal, 309 ( Pt 3):793-800, Aug 1995. URL: https://doi.org/10.1042/bj3090793, doi:10.1042/bj3090793. This article has 22 citations.

6. (tan2016structureofa pages 1-2): Wei-Hung Tan, Shu-Chun Cheng, Yu-Tung Liu, Cheng-Guo Wu, Min-Han Lin, Chiao-Che Chen, Chao-Hsiung Lin, and Chi-Yuan Chou. Structure of a highly active cephalopod s-crystallin mutant: new molecular evidence for evolution from an active enzyme into lens-refractive protein. Scientific Reports, Aug 2016. URL: https://doi.org/10.1038/srep31176, doi:10.1038/srep31176. This article has 17 citations and is from a peer-reviewed journal.

7. (bergman2023illuminatingassemblydynamics pages 74-77): Michael Richard Bergman. Illuminating assembly dynamics regulating short-range order optics in extremely long-lived proteins. ArXiv, 2023. URL: https://doi.org/10.17760/d20486926, doi:10.17760/d20486926. This article has 0 citations.

8. (chuang1999homologymodelingof pages 1-2): Chyh-Chong Chuang, Shih-Hsiung Wu, Shyh-Horng Chiou, and Gu-Gang Chang. Homology modeling of cephalopod lens s-crystallin: a natural mutant of sigma-class glutathione transferase with diminished endogenous activity. Biophysical journal, 76 2:679-90, Feb 1999. URL: https://doi.org/10.1016/s0006-3495(99)77235-8, doi:10.1016/s0006-3495(99)77235-8. This article has 27 citations and is from a domain leading peer-reviewed journal.

9. (chiou1995octopusscrystallinswith pages 3-3): S. Chiou, C. W. Yu, C. W. Lin, F. Pan, S. F. Lu, H. Lee, and G. Chang. Octopus s-crystallins with endogenous glutathione s-transferase (gst) activity: sequence comparison and evolutionary relationships with authentic gst enzymes. The Biochemical journal, 309 ( Pt 3):793-800, Aug 1995. URL: https://doi.org/10.1042/bj3090793, doi:10.1042/bj3090793. This article has 22 citations.

10. (chiou1995octopusscrystallinswith pages 2-3): S. Chiou, C. W. Yu, C. W. Lin, F. Pan, S. F. Lu, H. Lee, and G. Chang. Octopus s-crystallins with endogenous glutathione s-transferase (gst) activity: sequence comparison and evolutionary relationships with authentic gst enzymes. The Biochemical journal, 309 ( Pt 3):793-800, Aug 1995. URL: https://doi.org/10.1042/bj3090793, doi:10.1042/bj3090793. This article has 22 citations.

11. (tan2016structureofa pages 7-8): Wei-Hung Tan, Shu-Chun Cheng, Yu-Tung Liu, Cheng-Guo Wu, Min-Han Lin, Chiao-Che Chen, Chao-Hsiung Lin, and Chi-Yuan Chou. Structure of a highly active cephalopod s-crystallin mutant: new molecular evidence for evolution from an active enzyme into lens-refractive protein. Scientific Reports, Aug 2016. URL: https://doi.org/10.1038/srep31176, doi:10.1038/srep31176. This article has 17 citations and is from a peer-reviewed journal.

12. (chuang1999homologymodelingof pages 5-7): Chyh-Chong Chuang, Shih-Hsiung Wu, Shyh-Horng Chiou, and Gu-Gang Chang. Homology modeling of cephalopod lens s-crystallin: a natural mutant of sigma-class glutathione transferase with diminished endogenous activity. Biophysical journal, 76 2:679-90, Feb 1999. URL: https://doi.org/10.1016/s0006-3495(99)77235-8, doi:10.1016/s0006-3495(99)77235-8. This article has 27 citations and is from a domain leading peer-reviewed journal.

13. (chuang1999homologymodelingof pages 7-10): Chyh-Chong Chuang, Shih-Hsiung Wu, Shyh-Horng Chiou, and Gu-Gang Chang. Homology modeling of cephalopod lens s-crystallin: a natural mutant of sigma-class glutathione transferase with diminished endogenous activity. Biophysical journal, 76 2:679-90, Feb 1999. URL: https://doi.org/10.1016/s0006-3495(99)77235-8, doi:10.1016/s0006-3495(99)77235-8. This article has 27 citations and is from a domain leading peer-reviewed journal.

14. (tomarev1995glutathionestransferaseand pages 5-6): StanislavI. Tomarev, Sambath Chung, and Joram Piatigorsky. Glutathione s-transferase and s-crystallins of cephalopods: evolution from active enzyme to lens-refractive proteins. Journal of Molecular Evolution, 41:1048-1056, Dec 1995. URL: https://doi.org/10.1007/bf00173186, doi:10.1007/bf00173186. This article has 66 citations and is from a peer-reviewed journal.

15. (bergman2023illuminatingassemblydynamics pages 50-51): Michael Richard Bergman. Illuminating assembly dynamics regulating short-range order optics in extremely long-lived proteins. ArXiv, 2023. URL: https://doi.org/10.17760/d20486926, doi:10.17760/d20486926. This article has 0 citations.

16. (ryu2023eyedevelopmentand pages 11-12): Kyoung-Bin Ryu, Gun-Hee Jo, Young-Chun Gil, Donggu Jeon, Na-Rae Choi, Seung-Hyun Jung, Seonmi Jo, Hye Suck An, Hae-Youn Lee, Seong-il Eyun, and Sung-Jin Cho. Eye development and developmental expression of crystallin genes in the long arm octopus, octopus minor. Frontiers in Marine Science, May 2023. URL: https://doi.org/10.3389/fmars.2023.1136602, doi:10.3389/fmars.2023.1136602. This article has 6 citations.

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