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protein_description: 'RecName: Full=Cytosolic-abundant heat soluble protein 1 {ECO:0000303|PubMed:22937162};
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gene_info: Name=CAHS1 {ECO:0000303|PubMed:22937162}; ORFNames=RvY_00944;
organism_full: Ramazzottius varieornatus (Water bear) (Tardigrade).
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protein_domains: Not specified in UniProt
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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: J7M799
• Protein Description: RecName: Full=Cytosolic-abundant heat soluble protein 1 {ECO:0000303|PubMed:22937162}; Short=CAHS1 {ECO:0000303|PubMed:22937162}; AltName: Full=Tardigrade-specific intrinsically disordered protein CAHS1 {ECO:0000305}; Short=TDP CAHS1 {ECO:0000305};
• Gene Information: Name=CAHS1 {ECO:0000303|PubMed:22937162}; ORFNames=RvY_00944;
• Organism (full): Ramazzottius varieornatus (Water bear) (Tardigrade).
• Protein Family: Belongs to the Cytosolic-abundant heat soluble protein
• Key Domains: Not specified in UniProt

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "CAHS1" matches the protein description above
2. Verify the organism is correct: Ramazzottius varieornatus (Water bear) (Tardigrade).
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 'CAHS1' 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 CAHS1 (gene ID: CAHS1, UniProt: J7M799) in RAMVA.

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: J7M799
• Protein Description: RecName: Full=Cytosolic-abundant heat soluble protein 1 {ECO:0000303|PubMed:22937162}; Short=CAHS1 {ECO:0000303|PubMed:22937162}; AltName: Full=Tardigrade-specific intrinsically disordered protein CAHS1 {ECO:0000305}; Short=TDP CAHS1 {ECO:0000305};
• Gene Information: Name=CAHS1 {ECO:0000303|PubMed:22937162}; ORFNames=RvY_00944;
• Organism (full): Ramazzottius varieornatus (Water bear) (Tardigrade).
• Protein Family: Belongs to the Cytosolic-abundant heat soluble protein
• Key Domains: Not specified in UniProt

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "CAHS1" matches the protein description above
2. Verify the organism is correct: Ramazzottius varieornatus (Water bear) (Tardigrade).
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 'CAHS1' 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 CAHS1 (gene ID: CAHS1, UniProt: J7M799) in RAMVA.

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: CAHS1 (UniProt J7M799) from Ramazzottius varieornatus (tardigrade)

0) Scope and identity verification (critical)

Target verified: The gene symbol CAHS1 in this report refers specifically to cytosolic abundant heat-soluble protein 1 from the eutardigrade Ramazzottius varieornatus (water bear), UniProt accession J7M799, consistent with the UniProt entry supplied by the user. A multiomics study explicitly states that recombinant CAHS1 from R. varieornatus used in their assays corresponds to “UniProt ID: J7M799” (publication date: 2020-10-27, bioRxiv; URL: https://doi.org/10.1101/2020.10.27.358333) (murai2020multiomicsstudyof pages 13-16).

Important nomenclature caveat (avoid misannotation): CAHS proteins were historically named “in discovery order,” so the label “CAHS1” does not guarantee orthology across genera; even within Ramazzottius, at least one CAHS protein formerly called Ramazzottius CAHS1 was later renamed (Ramazzottius CAHS2a) in a phylogeny-aware nomenclature (publication date: 2024-11, Genome Biology and Evolution; URL: https://doi.org/10.1093/gbe/evad217) (fleming2024theevolutionof pages 2-5, fleming2024theevolutionof pages 5-6, fleming2024theevolutionof pages 1-2). Therefore, accession-anchored identity (J7M799) is the safest way to track CAHS1 across studies.

1) Key concepts and definitions (current understanding)

1.1 Anhydrobiosis and “tardigrade disordered proteins”

Anhydrobiosis is an ametabolic, reversible state induced by extreme desiccation. In many organisms, LEA proteins and sugars (e.g., trehalose) contribute to drying tolerance. Tardigrades additionally possess lineage-specific, highly hydrophilic, stress-related proteins often discussed as tardigrade-specific intrinsically disordered proteins (IDPs) or “tardigrade disordered proteins,” including the CAHS family (yamaguchi2012twonovelheatsoluble pages 2-3, murai2021multiomicsstudyof pages 1-2, kc2024disorderedproteinsinteract pages 1-2).

1.2 CAHS proteins and CAHS1

The CAHS acronym was introduced as “Cytoplasmic Abundant Heat Soluble” proteins based on heat-soluble proteomics and subcellular localization (publication date: 2012-08, PLoS ONE; URL: https://doi.org/10.1371/journal.pone.0044209) (yamaguchi2012twonovelheatsoluble pages 2-3, yamaguchi2012twonovelheatsoluble pages 3-5). In this foundational work, CAHS1 was categorized as a cytoplasmic abundant heat-soluble protein, distinct from SAHS (secretory) proteins (yamaguchi2012twonovelheatsoluble pages 2-3).

Biophysical definition relevant to function: CAHS1 (and CAHS proteins generally) behave as hydration-sensitive IDPs that can undergo disorder → α-helix transitions under water-deficient or desolvating conditions, and can further self-assemble into higher-order states (fibrils/hydrogels/condensates) under dehydration-like stresses (yamaguchi2012twonovelheatsoluble pages 3-5, yagiutsumi2021desiccationinducedfibrouscondensation pages 2-3, yagiutsumi2021desiccationinducedfibrouscondensation pages 3-4).

2) Functional annotation of CAHS1 (J7M799): primary function, mechanism, and pathways

2.1 Primary function (best-supported)

CAHS1 is not an enzyme and no catalytic reaction or substrate specificity has been demonstrated in the cited primary literature. Instead, the best-supported primary function is physical/biophysical stabilization of the cytosol (and partially nucleus) during dehydration-like stress, via stress-induced, reversible self-assembly into condensates/fibrous networks and gels that can increase mechanical stability and reduce damage to cellular components (yamaguchi2012twonovelheatsoluble pages 3-5, yagiutsumi2021desiccationinducedfibrouscondensation pages 2-3, yagiutsumi2021desiccationinducedfibrouscondensation pages 3-4).

This functional framing is consistent with:
* The original hypothesis that CAHS proteins act as “molecular shield”–like protectants analogous to (but sequence-distinct from) LEA proteins (yamaguchi2012twonovelheatsoluble pages 2-3, yamaguchi2012twonovelheatsoluble pages 3-5).
* Direct evidence that CAHS1 forms dehydration-induced fibrous condensates and undergoes sol–gel transitions (yagiutsumi2021desiccationinducedfibrouscondensation pages 2-3, yagiutsumi2021desiccationinducedfibrouscondensation pages 3-4).

2.2 Mechanistic model: hydration-triggered structural switching and self-assembly

(i) Intrinsic disorder in hydrated conditions. The discovery study predicted CAHS proteins are intrinsically unstructured (FoldIndex) and showed CAHS1 CD signatures consistent with disorder in hydrated conditions (yamaguchi2012twonovelheatsoluble pages 3-5).

(ii) Disorder-to-α-helix transition under water deficit. CAHS1 adopts α-helical structure under water-deficient mimicry (e.g., TFE), with CAHS1 responding at relatively low TFE (~10%), indicating high sensitivity to water availability (yamaguchi2012twonovelheatsoluble pages 3-5). In the later CAHS1-focused study, dehydration produced IR amide I peaks (~1655 and 1650 cm−1) consistent with α-helical structure, which reversed upon rehydration (yagiutsumi2021desiccationinducedfibrouscondensation pages 2-3).

(iii) C-terminal helical region drives oligomerization/fibrils/gels. Detailed biophysical work indicates CAHS1 contains an intrinsically disordered N-terminus and a C-terminal α-helical region that mediates homo-oligomerization and assembly; as concentration increases, CAHS1 forms fibrils and eventually hydrogels, and these transitions are reversible and salt-sensitive (yagiutsumi2021desiccationinducedfibrouscondensation pages 3-4, yagiutsumi2021desiccationinducedfibrouscondensation pages 2-3).

(iv) Stress-induced condensation and gelation as a protective phase transition. In cell-based assays, CAHS1 forms reversible condensates under osmotic shock (dehydration-mimicking), consistent with a protective phase transition concept (yagiutsumi2021desiccationinducedfibrouscondensation pages 4-6, yagiutsumi2021desiccationinducedfibrouscondensation pages 3-4).

2.3 “Pathways” context (interpretation)

CAHS1’s role is best described as part of a stress tolerance module supporting anhydrobiosis rather than a classic biochemical signaling pathway.

Recent synthesis work on disordered protectants supports that CAHS-family proteins can synergize with cosolutes present during drying. In a 2024 eLife study on desiccation-related IDPs, synergy between CAHS proteins and endogenous cosolutes was reported, and for CAHS (in contrast to LEA), synergy correlated with self-assembly and gel formation (publication date: 2024-11, eLife; URL: https://doi.org/10.7554/elife.97231) (kc2024disorderedproteinsinteract pages 1-2). This supports the idea that CAHS self-assembly is functionally relevant in the chemically changing intracellular environment during desiccation.

3) Localization: where CAHS1 acts

3.1 Subcellular localization (cellular systems)

Human cell expression systems (HeLa): CAHS1-mEGFP localizes broadly to cytosol and nucleus under unstressed conditions and forms mainly granule-like aggregates under hyperosmotic stress (0.5 M sorbitol or 0.2 M NaCl), with rapid reversibility after stress release (publication date: 2024-11, Cell Structure and Function; URL: https://doi.org/10.1247/csf.24035) (bino2024possiblerolesof pages 7-8, bino2024possiblerolesof pages 6-7).

Earlier localization consistent with cytosol/nucleus protection: The 2012 discovery work found CAHS1-GFP predominantly in the cytoplasm with weak nuclear signal and proposed that CAHS proteins contribute to protection of the cytoplasm and nucleus (yamaguchi2012twonovelheatsoluble pages 3-5, yamaguchi2012twonovelheatsoluble pages 5-6).

3.2 In vivo tardigrade context (tissue-level)

A genetic tool development paper (TardiVec) reported that promoters from CAHS genes drive tissue-specific expression in vivo. Notably, the CAHS1 promoter (pRvCAHS1) produced an epidermal expression pattern similar to CAHS3 promoter-driven expression, implying CAHS1 and CAHS3 subfamilies are active in similar tissues (publication date: 2023-01, PNAS; URL: https://doi.org/10.1073/pnas.2216739120) (tanaka2023invivoexpression pages 3-4). This suggests that in the animal, CAHS proteins may contribute strongly to epidermal protection during dehydration.

4) Recent developments (prioritizing 2023–2024)

4.1 2024: CAHS1 increases osmotic-stress tolerance in mammalian cells (quantitative)

Bino et al. (2024) tested CAHS paralogs in HeLa cells and measured sorbitol tolerance using viability (WST-1) and cytotoxicity (LDH) assays. In a CAHS1 inducible system, increasing CAHS1 expression shifted sorbitol dose–response curves:
* IC50 (viability) increased from ~0.06 M sorbitol (no doxycycline) to ~0.16 M (100 ng/mL doxycycline). (bino2024possiblerolesof media b6ad5a04)
* EC50 (cell death) increased from ~0.18 M to ~0.40 M with induction. (bino2024possiblerolesof media b6ad5a04)

In a comparison across paralogs, mean viability IC50 values increased modestly upon induction for CAHS1, CAHS3, and CAHS8 (ratios ~1.12–1.20×), whereas CAHS12 did not improve relative to control (publication date: 2024-11; URL: https://doi.org/10.1247/csf.24035) (bino2024possiblerolesof media b6ad5a04, bino2024possiblerolesof pages 7-8).

Interpretation: These data support that CAHS1 can act as a broadly acting physical protectant in heterologous mammalian cells under dehydration-like osmotic stress, consistent with a conserved biophysical mechanism rather than reliance on tardigrade-specific cofactors.

4.2 2024: In vivo imaging indicates tissue specificity and stress-responsive dynamics

TardiVec-based live imaging indicated CAHS expression in tardigrades is not uniform; CAHS3 expression was frequently observed in epidermal cells, and CAHS promoters (including CAHS1) can drive similar tissue patterns. During dehydration, CAHS-tagged proteins showed “LLPS-like dynamics,” although fluorescence was difficult to image in fully dehydrated samples (publication date: 2023-01; URL: https://doi.org/10.1073/pnas.2216739120) (tanaka2023invivoexpression pages 6-7, tanaka2023invivoexpression pages 3-4).

4.3 2024: Evolution/nomenclature reanalysis impacts annotation practice

The 2024 Genome Biology and Evolution analysis provides expert-level guidance that “CAHS1” naming can be misleading across taxa and that standardized phylogeny-aware nomenclature is needed. For functional annotation pipelines, this means that direct mapping to accessions (e.g., J7M799) and careful orthology inference are essential to avoid transferring function from non-orthologous CAHS proteins (publication date: 2024-11; URL: https://doi.org/10.1093/gbe/evad217) (fleming2024theevolutionof pages 2-5, fleming2024theevolutionof pages 5-6).

5) Applications and real-world implementations

5.1 Engineering stress-tolerant cells (osmotic stress)

The HeLa-cell work demonstrates an engineered, inducible CAHS1 system can improve tolerance to hyperosmotic stress with measurable IC50/EC50 shifts (bino2024possiblerolesof media b6ad5a04). This supports CAHS proteins as potential molecular tools/excipients for cell stabilization in biotechnology contexts where osmotic stress is limiting.

5.2 Microbial engineering for industrial stresses (biofuels)

A 2023 study expressed three CAHS proteins in the cyanobacterium Synechocystis and reported altered tolerance to biofuels (1.5% ethanol; 0.25% butanol), with measurable growth phenotype differences and extensive transcriptomic remodeling in engineered strains (publication date: 2023-01, Frontiers in Microbiology; URL: https://doi.org/10.3389/fmicb.2022.1091502) (zhang2023expressionoftardigrade pages 1-2, zhang2023expressionoftardigrade pages 6-7). Although the CAHS proteins used are not explicitly tied to J7M799 in the excerpted text, this provides proof-of-principle that CAHS-family IDPs can be deployed for stress tolerance engineering.

5.3 Biopreservation (cold-chain–independent stabilization) — CAHS family context

While CAHS1-specific excipient use was not directly evidenced in the retrieved texts, CAHS-family proteins (especially CAHS D) are being developed as dry-state protectants for labile biologics.

A 2023 Scientific Reports study tested CAHS-based mediators for stabilizing human clotting factor VIII (FVIII) under repeated desiccation cycles and thermal stress, demonstrating that protective capacity depends on sequence-controlled phase behavior (publication date: 2023-11; URL: https://doi.org/10.1038/s41598-023-31586-9) (packebush2023naturalandengineered pages 3-4, packebush2023naturalandengineered pages 5-7). Key quantitative examples from the excerpts:
* CAHS D samples are fluid from 0.1–7.5 mg/mL and form a hydrogel at ~10 mg/mL; an engineered 2X Linker variant gels at ~5 mg/mL (packebush2023naturalandengineered pages 4-5).
* A non-gelling “Linker Region” (LR) excipient showed robust and complete protection of FVIII at ≥1 mg/mL in repeated desiccation assays (packebush2023naturalandengineered pages 5-7).
* Under certain thermal-stress conditions, protective performance differed across CAHS variants in a concentration-dependent manner (packebush2023naturalandengineered pages 7-8).

Relevance to CAHS1 annotation: These applied studies reinforce the mechanistic interpretation that CAHS proteins function as tunable, environmentally responsive materials (gels/vitrified solids) rather than as classical biochemical catalysts.

6) Statistics and quantitative data highlights

6.1 CAHS1 self-assembly thresholds and structural readouts

From CAHS1 biophysical characterization (publication date: 2021-11, Scientific Reports; URL: https://doi.org/10.1038/s41598-021-00724-6):
* Turbidity/condensation increases abruptly above ~0.3 mM CAHS1; macroscopic gelation above ~0.6 mM; hydrogel demonstrated at 1.2 mM (yagiutsumi2021desiccationinducedfibrouscondensation pages 2-3).
* Dehydration-induced α-helical IR features at amide I ~1655 and 1650 cm−1, reversible upon rehydration (yagiutsumi2021desiccationinducedfibrouscondensation pages 2-3).
* HS-AFM visualization: fibrils observed when concentration increased from 0.4 μM to 3.3 μM (yagiutsumi2021desiccationinducedfibrouscondensation pages 6-7).

6.2 CAHS1-induced hyperosmotic tolerance in mammalian cells

From Bino et al. 2024 figure-derived values (publication date: 2024-11; URL: https://doi.org/10.1247/csf.24035):
* CAHS1 inducible clone: viability IC50 increased from ~0.06 M to ~0.16 M sorbitol, and LDH EC50 increased from ~0.18 M to ~0.40 M with CAHS1 induction (bino2024possiblerolesof media b6ad5a04).

6.3 Quantitative constraints on “water retention” mechanism (CAHS D context)

A 2023 study using thermogravimetric analysis concluded CAHS D does not increase total water retention in dry systems, but interacts differently with residual water. Quantitative excerpted values:
* Dried CAHS D contained 4.03% water (not significantly different from gelatin 4.62% or lysozyme 5.07%), while a non-gelling variant (FL_Pro) retained 6.77% water (p < 0.05) (publication date: 2023-06; URL: https://doi.org/10.1038/s41598-023-37485-3) (sanchezmartinez2023thetardigradeprotein pages 3-4, sanchezmartinez2023thetardigradeprotein pages 4-6).

Implication for CAHS1: CAHS-family protection should not be assumed to be primarily via bulk water retention; instead, phase behavior and interactions with residual water are currently better-supported mechanistic drivers.

7) Expert opinions and authoritative analysis (interpretive synthesis)

1. CAHS proteins as materials-like protectants: Across primary CAHS1 work and broader CAHS literature, an emerging consensus is that CAHS proteins act as hydration-sensitive, reversible assemblies (condensates/fibers/gels) that stabilize cell structure and macromolecules during dehydration-like stress (yagiutsumi2021desiccationinducedfibrouscondensation pages 3-4, kc2024disorderedproteinsinteract pages 1-2, sanchezmartinez2024labileassemblyof pages 1-2).

2. Functional diversity within CAHS paralogs: Comparative studies (e.g., Bino 2024) show paralogs differ in localization/assembly morphology and protective effect, suggesting CAHS1 is part of a diversified protective repertoire rather than a single redundant protein (bino2024possiblerolesof pages 6-7, bino2024possiblerolesof media b6ad5a04).

3. Annotation caution from evolutionary work: Fleming et al. (2024) emphasize that past naming conventions can confound cross-study inference. For functional annotation of CAHS1 (J7M799), this means do not transfer function from “CAHS1” in other genera without orthology checks, and prefer accession-based mapping and phylogeny-aware grouping (fleming2024theevolutionof pages 2-5, fleming2024theevolutionof pages 5-6).

8) Summary: functional annotation statement (recommended)

CAHS1 (UniProt J7M799) in Ramazzottius varieornatus is a tardigrade-specific, cytosolic abundant heat-soluble intrinsically disordered protein that undergoes hydration-dependent disorder-to-α-helix transitions and reversible self-assembly (condensates/fibrils/hydrogels), likely providing physical stabilization of cytosol (and partly nucleus) during dehydration-like stresses associated with anhydrobiosis. (yamaguchi2012twonovelheatsoluble pages 3-5, yagiutsumi2021desiccationinducedfibrouscondensation pages 2-3, bino2024possiblerolesof pages 7-8)

Embedded evidence summary table

Table: This table summarizes the most relevant primary and review-like studies for functional annotation of CAHS1 in Ramazzottius varieornatus, including identity verification, mechanism, localization, and quantitative findings. It is useful for distinguishing direct CAHS1 evidence from broader CAHS-family context and recent nomenclature revisions.

Key source URLs (with publication dates)

• Yamaguchi et al., 2012-08, PLoS ONE: https://doi.org/10.1371/journal.pone.0044209 (yamaguchi2012twonovelheatsoluble pages 3-5)
• Yagi-Utsumi et al., 2021-11, Scientific Reports: https://doi.org/10.1038/s41598-021-00724-6 (yagiutsumi2021desiccationinducedfibrouscondensation pages 2-3)
• Tanaka et al., 2023-01, PNAS: https://doi.org/10.1073/pnas.2216739120 (tanaka2023invivoexpression pages 3-4)
• Bino et al., 2024-11, Cell Structure and Function: https://doi.org/10.1247/csf.24035 (bino2024possiblerolesof media b6ad5a04)
• Fleming et al., 2024-11, Genome Biology and Evolution: https://doi.org/10.1093/gbe/evad217 (fleming2024theevolutionof pages 2-5)
• KC et al., 2024-11, eLife: https://doi.org/10.7554/elife.97231 (kc2024disorderedproteinsinteract pages 1-2)
• Sanchez-Martinez et al., 2023-06, Scientific Reports: https://doi.org/10.1038/s41598-023-37485-3 (sanchezmartinez2023thetardigradeprotein pages 3-4)
• Packebush et al., 2023-11, Scientific Reports: https://doi.org/10.1038/s41598-023-31586-9 (packebush2023naturalandengineered pages 5-7)

References

1. (murai2020multiomicsstudyof pages 13-16): Yumi Murai, Maho Yagi-Utsumi, Masayuki Fujiwara, Masaru Tomita, Koichi Kato, and Kazuharu Arakawa. Multiomics study of a heterotardigrade, echinisicus testudo, suggests convergent evolution of anhydrobiosis-related proteins in tardigrada. bioRxiv, Oct 2020. URL: https://doi.org/10.1101/2020.10.27.358333, doi:10.1101/2020.10.27.358333. This article has 4 citations.

2. (fleming2024theevolutionof pages 2-5): James F Fleming, Davide Pisani, and Kazuharu Arakawa. The evolution of temperature and desiccation-related protein families in tardigrada reveals a complex acquisition of extremotolerance. Genome Biology and Evolution, Nov 2024. URL: https://doi.org/10.1093/gbe/evad217, doi:10.1093/gbe/evad217. This article has 21 citations and is from a domain leading peer-reviewed journal.

3. (fleming2024theevolutionof pages 5-6): James F Fleming, Davide Pisani, and Kazuharu Arakawa. The evolution of temperature and desiccation-related protein families in tardigrada reveals a complex acquisition of extremotolerance. Genome Biology and Evolution, Nov 2024. URL: https://doi.org/10.1093/gbe/evad217, doi:10.1093/gbe/evad217. This article has 21 citations and is from a domain leading peer-reviewed journal.

4. (fleming2024theevolutionof pages 1-2): James F Fleming, Davide Pisani, and Kazuharu Arakawa. The evolution of temperature and desiccation-related protein families in tardigrada reveals a complex acquisition of extremotolerance. Genome Biology and Evolution, Nov 2024. URL: https://doi.org/10.1093/gbe/evad217, doi:10.1093/gbe/evad217. This article has 21 citations and is from a domain leading peer-reviewed journal.

5. (yamaguchi2012twonovelheatsoluble pages 2-3): Ayami Yamaguchi, Sae Tanaka, Shiho Yamaguchi, Hirokazu Kuwahara, Chizuko Takamura, Shinobu Imajoh-Ohmi, Daiki D. Horikawa, Atsushi Toyoda, Toshiaki Katayama, Kazuharu Arakawa, Asao Fujiyama, Takeo Kubo, and Takekazu Kunieda. Two novel heat-soluble protein families abundantly expressed in an anhydrobiotic tardigrade. PLoS ONE, 7:e44209, Aug 2012. URL: https://doi.org/10.1371/journal.pone.0044209, doi:10.1371/journal.pone.0044209. This article has 195 citations and is from a peer-reviewed journal.

6. (murai2021multiomicsstudyof pages 1-2): Yumi Murai, Maho Yagi-Utsumi, Masayuki Fujiwara, Sae Tanaka, Masaru Tomita, Koichi Kato, and Kazuharu Arakawa. Multiomics study of a heterotardigrade, echinisicus testudo, suggests the possibility of convergent evolution of abundant heat-soluble proteins in tardigrada. BMC Genomics, Nov 2021. URL: https://doi.org/10.1186/s12864-021-08131-x, doi:10.1186/s12864-021-08131-x. This article has 42 citations and is from a peer-reviewed journal.

7. (kc2024disorderedproteinsinteract pages 1-2): Shraddha KC, Kenny H Nguyen, Vincent Nicholson, Annie Walgren, Tony Trent, Edith Gollub, Paulette Sofia Romero-Perez, Alex S Holehouse, Shahar Sukenik, and Thomas C Boothby. Disordered proteins interact with the chemical environment to tune their protective function during drying. eLife, Nov 2024. URL: https://doi.org/10.7554/elife.97231, doi:10.7554/elife.97231. This article has 20 citations and is from a domain leading peer-reviewed journal.

8. (yamaguchi2012twonovelheatsoluble pages 3-5): Ayami Yamaguchi, Sae Tanaka, Shiho Yamaguchi, Hirokazu Kuwahara, Chizuko Takamura, Shinobu Imajoh-Ohmi, Daiki D. Horikawa, Atsushi Toyoda, Toshiaki Katayama, Kazuharu Arakawa, Asao Fujiyama, Takeo Kubo, and Takekazu Kunieda. Two novel heat-soluble protein families abundantly expressed in an anhydrobiotic tardigrade. PLoS ONE, 7:e44209, Aug 2012. URL: https://doi.org/10.1371/journal.pone.0044209, doi:10.1371/journal.pone.0044209. This article has 195 citations and is from a peer-reviewed journal.

9. (yagiutsumi2021desiccationinducedfibrouscondensation pages 2-3): Maho Yagi-Utsumi, Kazuhiro Aoki, Hiroki Watanabe, Chihong Song, Seiji Nishimura, Tadashi Satoh, Saeko Yanaka, Christian Ganser, Sae Tanaka, Vincent Schnapka, Ean Wai Goh, Yuji Furutani, Kazuyoshi Murata, Takayuki Uchihashi, Kazuharu Arakawa, and Koichi Kato. Desiccation-induced fibrous condensation of cahs protein from an anhydrobiotic tardigrade. Scientific Reports, Nov 2021. URL: https://doi.org/10.1038/s41598-021-00724-6, doi:10.1038/s41598-021-00724-6. This article has 74 citations and is from a peer-reviewed journal.

10. (yagiutsumi2021desiccationinducedfibrouscondensation pages 3-4): Maho Yagi-Utsumi, Kazuhiro Aoki, Hiroki Watanabe, Chihong Song, Seiji Nishimura, Tadashi Satoh, Saeko Yanaka, Christian Ganser, Sae Tanaka, Vincent Schnapka, Ean Wai Goh, Yuji Furutani, Kazuyoshi Murata, Takayuki Uchihashi, Kazuharu Arakawa, and Koichi Kato. Desiccation-induced fibrous condensation of cahs protein from an anhydrobiotic tardigrade. Scientific Reports, Nov 2021. URL: https://doi.org/10.1038/s41598-021-00724-6, doi:10.1038/s41598-021-00724-6. This article has 74 citations and is from a peer-reviewed journal.

11. (yagiutsumi2021desiccationinducedfibrouscondensation pages 4-6): Maho Yagi-Utsumi, Kazuhiro Aoki, Hiroki Watanabe, Chihong Song, Seiji Nishimura, Tadashi Satoh, Saeko Yanaka, Christian Ganser, Sae Tanaka, Vincent Schnapka, Ean Wai Goh, Yuji Furutani, Kazuyoshi Murata, Takayuki Uchihashi, Kazuharu Arakawa, and Koichi Kato. Desiccation-induced fibrous condensation of cahs protein from an anhydrobiotic tardigrade. Scientific Reports, Nov 2021. URL: https://doi.org/10.1038/s41598-021-00724-6, doi:10.1038/s41598-021-00724-6. This article has 74 citations and is from a peer-reviewed journal.

12. (bino2024possiblerolesof pages 7-8): Takahiro Bino, Yuhei Goto, Gembu Maryu, Kazuharu Arakawa, and Kazuhiro Aoki. Possible roles of cahs proteins from tardigrade in osmotic stress tolerance in mammalian cells. Cell Structure and Function, 49:123-133, Nov 2024. URL: https://doi.org/10.1247/csf.24035, doi:10.1247/csf.24035. This article has 5 citations and is from a peer-reviewed journal.

13. (bino2024possiblerolesof pages 6-7): Takahiro Bino, Yuhei Goto, Gembu Maryu, Kazuharu Arakawa, and Kazuhiro Aoki. Possible roles of cahs proteins from tardigrade in osmotic stress tolerance in mammalian cells. Cell Structure and Function, 49:123-133, Nov 2024. URL: https://doi.org/10.1247/csf.24035, doi:10.1247/csf.24035. This article has 5 citations and is from a peer-reviewed journal.

14. (yamaguchi2012twonovelheatsoluble pages 5-6): Ayami Yamaguchi, Sae Tanaka, Shiho Yamaguchi, Hirokazu Kuwahara, Chizuko Takamura, Shinobu Imajoh-Ohmi, Daiki D. Horikawa, Atsushi Toyoda, Toshiaki Katayama, Kazuharu Arakawa, Asao Fujiyama, Takeo Kubo, and Takekazu Kunieda. Two novel heat-soluble protein families abundantly expressed in an anhydrobiotic tardigrade. PLoS ONE, 7:e44209, Aug 2012. URL: https://doi.org/10.1371/journal.pone.0044209, doi:10.1371/journal.pone.0044209. This article has 195 citations and is from a peer-reviewed journal.

15. (tanaka2023invivoexpression pages 3-4): Sae Tanaka, Kazuhiro Aoki, and Kazuharu Arakawa. In vivo expression vector derived from anhydrobiotic tardigrade genome enables live imaging in eutardigrada. Proceedings of the National Academy of Sciences, Jan 2023. URL: https://doi.org/10.1073/pnas.2216739120, doi:10.1073/pnas.2216739120. This article has 27 citations and is from a highest quality peer-reviewed journal.

16. (bino2024possiblerolesof media b6ad5a04): Takahiro Bino, Yuhei Goto, Gembu Maryu, Kazuharu Arakawa, and Kazuhiro Aoki. Possible roles of cahs proteins from tardigrade in osmotic stress tolerance in mammalian cells. Cell Structure and Function, 49:123-133, Nov 2024. URL: https://doi.org/10.1247/csf.24035, doi:10.1247/csf.24035. This article has 5 citations and is from a peer-reviewed journal.

17. (tanaka2023invivoexpression pages 6-7): Sae Tanaka, Kazuhiro Aoki, and Kazuharu Arakawa. In vivo expression vector derived from anhydrobiotic tardigrade genome enables live imaging in eutardigrada. Proceedings of the National Academy of Sciences, Jan 2023. URL: https://doi.org/10.1073/pnas.2216739120, doi:10.1073/pnas.2216739120. This article has 27 citations and is from a highest quality peer-reviewed journal.

18. (zhang2023expressionoftardigrade pages 1-2): Heao Zhang, Qingyang Liu, Qing Liang, Boxiang Wang, Zixi Chen, and Jiangxin Wang. Expression of tardigrade disordered proteins impacts the tolerance to biofuels in a model cyanobacterium synechocystis sp. pcc 6803. Frontiers in Microbiology, Jan 2023. URL: https://doi.org/10.3389/fmicb.2022.1091502, doi:10.3389/fmicb.2022.1091502. This article has 3 citations and is from a peer-reviewed journal.

19. (zhang2023expressionoftardigrade pages 6-7): Heao Zhang, Qingyang Liu, Qing Liang, Boxiang Wang, Zixi Chen, and Jiangxin Wang. Expression of tardigrade disordered proteins impacts the tolerance to biofuels in a model cyanobacterium synechocystis sp. pcc 6803. Frontiers in Microbiology, Jan 2023. URL: https://doi.org/10.3389/fmicb.2022.1091502, doi:10.3389/fmicb.2022.1091502. This article has 3 citations and is from a peer-reviewed journal.

20. (packebush2023naturalandengineered pages 3-4): Maxwell H. Packebush, Silvia Sánchez-Martínez, Sourav Biswas, S. Kc, K. Nguyen, J. Ramirez, V. Nicholson, and T. Boothby. Natural and engineered mediators of desiccation tolerance stabilize human blood clotting factor viii in a dry state. Scientific Reports, Nov 2023. URL: https://doi.org/10.1038/s41598-023-31586-9, doi:10.1038/s41598-023-31586-9. This article has 30 citations and is from a peer-reviewed journal.

21. (packebush2023naturalandengineered pages 5-7): Maxwell H. Packebush, Silvia Sánchez-Martínez, Sourav Biswas, S. Kc, K. Nguyen, J. Ramirez, V. Nicholson, and T. Boothby. Natural and engineered mediators of desiccation tolerance stabilize human blood clotting factor viii in a dry state. Scientific Reports, Nov 2023. URL: https://doi.org/10.1038/s41598-023-31586-9, doi:10.1038/s41598-023-31586-9. This article has 30 citations and is from a peer-reviewed journal.

22. (packebush2023naturalandengineered pages 4-5): Maxwell H. Packebush, Silvia Sánchez-Martínez, Sourav Biswas, S. Kc, K. Nguyen, J. Ramirez, V. Nicholson, and T. Boothby. Natural and engineered mediators of desiccation tolerance stabilize human blood clotting factor viii in a dry state. Scientific Reports, Nov 2023. URL: https://doi.org/10.1038/s41598-023-31586-9, doi:10.1038/s41598-023-31586-9. This article has 30 citations and is from a peer-reviewed journal.

23. (packebush2023naturalandengineered pages 7-8): Maxwell H. Packebush, Silvia Sánchez-Martínez, Sourav Biswas, S. Kc, K. Nguyen, J. Ramirez, V. Nicholson, and T. Boothby. Natural and engineered mediators of desiccation tolerance stabilize human blood clotting factor viii in a dry state. Scientific Reports, Nov 2023. URL: https://doi.org/10.1038/s41598-023-31586-9, doi:10.1038/s41598-023-31586-9. This article has 30 citations and is from a peer-reviewed journal.

24. (yagiutsumi2021desiccationinducedfibrouscondensation pages 6-7): Maho Yagi-Utsumi, Kazuhiro Aoki, Hiroki Watanabe, Chihong Song, Seiji Nishimura, Tadashi Satoh, Saeko Yanaka, Christian Ganser, Sae Tanaka, Vincent Schnapka, Ean Wai Goh, Yuji Furutani, Kazuyoshi Murata, Takayuki Uchihashi, Kazuharu Arakawa, and Koichi Kato. Desiccation-induced fibrous condensation of cahs protein from an anhydrobiotic tardigrade. Scientific Reports, Nov 2021. URL: https://doi.org/10.1038/s41598-021-00724-6, doi:10.1038/s41598-021-00724-6. This article has 74 citations and is from a peer-reviewed journal.

25. (sanchezmartinez2023thetardigradeprotein pages 3-4): Silvia Sanchez-Martinez, John F. Ramirez, Emma K. Meese, Charles A. Childs, and Thomas C. Boothby. The tardigrade protein cahs d interacts with, but does not retain, water in hydrated and desiccated systems. Scientific Reports, Jun 2023. URL: https://doi.org/10.1038/s41598-023-37485-3, doi:10.1038/s41598-023-37485-3. This article has 26 citations and is from a peer-reviewed journal.

26. (sanchezmartinez2023thetardigradeprotein pages 4-6): Silvia Sanchez-Martinez, John F. Ramirez, Emma K. Meese, Charles A. Childs, and Thomas C. Boothby. The tardigrade protein cahs d interacts with, but does not retain, water in hydrated and desiccated systems. Scientific Reports, Jun 2023. URL: https://doi.org/10.1038/s41598-023-37485-3, doi:10.1038/s41598-023-37485-3. This article has 26 citations and is from a peer-reviewed journal.

27. (sanchezmartinez2024labileassemblyof pages 1-2): S. Sanchez-Martinez, K. Nguyen, S. Biswas, V. Nicholson, A. V. Romanyuk, J. Ramirez, S. Kc, A. Akter, C. Childs, E. Meese, E. T. Usher, G. Ginell, F. Yu, E. Gollub, M. Malferrari, F. Francia, G. Venturoli, E. W. Martin, F. Caporaletti, G. Giubertoni, S. Woutersen, S. Sukenik, D. N. Woolfson, A. Holehouse, T. Boothby, VI.Veni, and A. Cortajarena. Labile assembly of a tardigrade protein induces biostasis. Protein Science : A Publication of the Protein Society, Mar 2024. URL: https://doi.org/10.1002/pro.4941, doi:10.1002/pro.4941. This article has 27 citations.

28. (yagiutsumi2021desiccationinducedfibrouscondensation pages 1-2): Maho Yagi-Utsumi, Kazuhiro Aoki, Hiroki Watanabe, Chihong Song, Seiji Nishimura, Tadashi Satoh, Saeko Yanaka, Christian Ganser, Sae Tanaka, Vincent Schnapka, Ean Wai Goh, Yuji Furutani, Kazuyoshi Murata, Takayuki Uchihashi, Kazuharu Arakawa, and Koichi Kato. Desiccation-induced fibrous condensation of cahs protein from an anhydrobiotic tardigrade. Scientific Reports, Nov 2021. URL: https://doi.org/10.1038/s41598-021-00724-6, doi:10.1038/s41598-021-00724-6. This article has 74 citations and is from a peer-reviewed journal.

29. (murai2020multiomicsstudyof pages 7-9): Yumi Murai, Maho Yagi-Utsumi, Masayuki Fujiwara, Masaru Tomita, Koichi Kato, and Kazuharu Arakawa. Multiomics study of a heterotardigrade, echinisicus testudo, suggests convergent evolution of anhydrobiosis-related proteins in tardigrada. bioRxiv, Oct 2020. URL: https://doi.org/10.1101/2020.10.27.358333, doi:10.1101/2020.10.27.358333. This article has 4 citations.

30. (tanaka2022stressdependentcellstiffening pages 13-14): Akihiro Tanaka, Tomomi Nakano, Kento Watanabe, Kazutoshi Masuda, Gen Honda, Shuichi Kamata, Reitaro Yasui, Hiroko Kozuka-Hata, Chiho Watanabe, Takumi Chinen, Daiju Kitagawa, Satoshi Sawai, Masaaki Oyama, Miho Yanagisawa, and Takekazu Kunieda. Stress-dependent cell stiffening by tardigrade tolerance proteins that reversibly form a filamentous network and gel. PLOS Biology, 20:e3001780, Sep 2022. URL: https://doi.org/10.1371/journal.pbio.3001780, doi:10.1371/journal.pbio.3001780. This article has 59 citations and is from a highest quality peer-reviewed journal.

31. (bino2024possiblerolesof pages 1-2): Takahiro Bino, Yuhei Goto, Gembu Maryu, Kazuharu Arakawa, and Kazuhiro Aoki. Possible roles of cahs proteins from tardigrade in osmotic stress tolerance in mammalian cells. Cell Structure and Function, 49:123-133, Nov 2024. URL: https://doi.org/10.1247/csf.24035, doi:10.1247/csf.24035. This article has 5 citations and is from a peer-reviewed journal.

32. (bino2024possiblerolesof pages 2-5): Takahiro Bino, Yuhei Goto, Gembu Maryu, Kazuharu Arakawa, and Kazuhiro Aoki. Possible roles of cahs proteins from tardigrade in osmotic stress tolerance in mammalian cells. Cell Structure and Function, 49:123-133, Nov 2024. URL: https://doi.org/10.1247/csf.24035, doi:10.1247/csf.24035. This article has 5 citations and is from a peer-reviewed journal.

33. (bino2024possiblerolesof media 437c27e1): Takahiro Bino, Yuhei Goto, Gembu Maryu, Kazuharu Arakawa, and Kazuhiro Aoki. Possible roles of cahs proteins from tardigrade in osmotic stress tolerance in mammalian cells. Cell Structure and Function, 49:123-133, Nov 2024. URL: https://doi.org/10.1247/csf.24035, doi:10.1247/csf.24035. This article has 5 citations and is from a peer-reviewed journal.

34. (sanchezmartinez2024labileassemblyof pages 2-5): S. Sanchez-Martinez, K. Nguyen, S. Biswas, V. Nicholson, A. V. Romanyuk, J. Ramirez, S. Kc, A. Akter, C. Childs, E. Meese, E. T. Usher, G. Ginell, F. Yu, E. Gollub, M. Malferrari, F. Francia, G. Venturoli, E. W. Martin, F. Caporaletti, G. Giubertoni, S. Woutersen, S. Sukenik, D. N. Woolfson, A. Holehouse, T. Boothby, VI.Veni, and A. Cortajarena. Labile assembly of a tardigrade protein induces biostasis. Protein Science : A Publication of the Protein Society, Mar 2024. URL: https://doi.org/10.1002/pro.4941, doi:10.1002/pro.4941. This article has 27 citations.

35. (sanchezmartinez2024labileassemblyof pages 12-14): S. Sanchez-Martinez, K. Nguyen, S. Biswas, V. Nicholson, A. V. Romanyuk, J. Ramirez, S. Kc, A. Akter, C. Childs, E. Meese, E. T. Usher, G. Ginell, F. Yu, E. Gollub, M. Malferrari, F. Francia, G. Venturoli, E. W. Martin, F. Caporaletti, G. Giubertoni, S. Woutersen, S. Sukenik, D. N. Woolfson, A. Holehouse, T. Boothby, VI.Veni, and A. Cortajarena. Labile assembly of a tardigrade protein induces biostasis. Protein Science : A Publication of the Protein Society, Mar 2024. URL: https://doi.org/10.1002/pro.4941, doi:10.1002/pro.4941. This article has 27 citations.

36. (sanchezmartinez2024labileassemblyof pages 14-17): S. Sanchez-Martinez, K. Nguyen, S. Biswas, V. Nicholson, A. V. Romanyuk, J. Ramirez, S. Kc, A. Akter, C. Childs, E. Meese, E. T. Usher, G. Ginell, F. Yu, E. Gollub, M. Malferrari, F. Francia, G. Venturoli, E. W. Martin, F. Caporaletti, G. Giubertoni, S. Woutersen, S. Sukenik, D. N. Woolfson, A. Holehouse, T. Boothby, VI.Veni, and A. Cortajarena. Labile assembly of a tardigrade protein induces biostasis. Protein Science : A Publication of the Protein Society, Mar 2024. URL: https://doi.org/10.1002/pro.4941, doi:10.1002/pro.4941. This article has 27 citations.

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