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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: J7M3T1
• Protein Description: RecName: Full=Cytosolic-abundant heat soluble protein 3 {ECO:0000303|PubMed:22937162}; Short=CAHS3 {ECO:0000303|PubMed:22937162}; AltName: Full=Tardigrade-specific intrinsically disordered protein CAHS3 {ECO:0000305}; Short=TDP CAHS3 {ECO:0000305};
• Gene Information: Name=CAHS3 {ECO:0000303|PubMed:22937162}; ORFNames=RvY_16236;
• 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 "CAHS3" 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 'CAHS3' 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 CAHS3 (gene ID: CAHS3, UniProt: J7M3T1) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: J7M3T1
• Protein Description: RecName: Full=Cytosolic-abundant heat soluble protein 3 {ECO:0000303|PubMed:22937162}; Short=CAHS3 {ECO:0000303|PubMed:22937162}; AltName: Full=Tardigrade-specific intrinsically disordered protein CAHS3 {ECO:0000305}; Short=TDP CAHS3 {ECO:0000305};
• Gene Information: Name=CAHS3 {ECO:0000303|PubMed:22937162}; ORFNames=RvY_16236;
• 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 "CAHS3" 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 'CAHS3' 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 CAHS3 (gene ID: CAHS3, UniProt: J7M3T1) 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: Functional Annotation of CAHS3 (UniProt J7M3T1) from Ramazzottius varieornatus

1) Target verification (gene/protein identity)

The research target here is CAHS3 (cytosolic-abundant heat soluble protein 3; UniProt J7M3T1) from the eutardigrade Ramazzottius varieornatus, a tardigrade-specific, heat-soluble, stress-responsive protein belonging to the CAHS family (tanaka2022stressdependentcellstiffening pages 13-14, ishikawa2024searchforputative pages 1-2). All CAHS3-specific claims below are restricted to R. varieornatus CAHS3 (RvCAHS3) and are not inferred from unrelated “CAHS3” symbols in other organisms.

2) Key concepts and definitions (current understanding)

Anhydrobiosis is a reversible ametabolic state induced by extreme dehydration, allowing organisms such as tardigrades to survive near-complete water loss and resume activity upon rehydration (tanaka2022stressdependentcellstiffening pages 13-14). In R. varieornatus, a major component of the anhydrobiosis toolkit is a set of tardigrade-unique, highly hydrophilic, heat-soluble proteins—particularly CAHS (Cytosolic-Abundant Heat Soluble) proteins—that are enriched in the cytosol and have stress-dependent self-assembly behavior (olgenblum2024protectingproteinsfrom pages 2-3, tanaka2022stressdependentcellstiffening pages 13-14).

A central conceptual model emerging from recent work is that CAHS proteins function as stress-inducible, reversible physical stabilizers: they can convert from a dispersed cytosolic state to more solid-like assemblies (filaments/hydrogels) under dehydration-like conditions (hyperosmotic stress, desolvating agents), thereby increasing mechanical robustness of the cytoplasm and helping cells resist deformation during water loss (tanaka2022stressdependentcellstiffening pages 13-14, tanaka2021stressdependentcellstiffening pages 12-15, tanaka2022stressdependentcellstiffening media e7bc2dfb).

3) CAHS3: primary function and mechanism (what CAHS3 does)

3.1 Stress-dependent reversible filamentation and gelation

A high-confidence, CAHS3-specific mechanistic conclusion is that CAHS3 reversibly polymerizes into cytoskeleton-like filaments under stress and can undergo sol–gel transitions.

• Filament formation in cells (stress-dependent, reversible): CAHS3 forms filamentous networks in response to hyperosmotic/dehydration-like stress, and fluorescence recovery after photobleaching (FRAP) indicates CAHS assemblies become immobile specifically in the filament state, consistent with regulated polymerization rather than irreversible aggregation (tanaka2022stressdependentcellstiffening pages 13-14, tanaka2022stressdependentcellstiffening media 2119c462).
• Gel-transition in vitro: purified CAHS3 undergoes a reversible sol–gel transition at approximately ~4 mg/mL under desolvating conditions (e.g., trifluoroethanol, TFE), and high salt (2 M NaCl) can also induce a gel-transition (tanaka2021stressdependentcellstiffening pages 12-15, tanaka2021stressdependentcellstiffening pages 10-12, tanaka2022stressdependentcellstiffening media e7bc2dfb).

3.2 Sequence/structural determinants: CR1/CR2 motifs are required

CAHS3 filamentation/gelation depends strongly on a conserved C-terminal region (CR1/CR2), predicted to form helical/coiled-coil structure.

• The C-terminal CR1 and CR2 motifs are essential and sufficient for CAHS3 filament formation; point substitutions that disrupt secondary structure (e.g., proline substitutions) impair filamentation and gelation (tanaka2022stressdependentcellstiffening pages 13-14, tanaka2021stressdependentcellstiffening pages 10-12).
• A filament-deficient mutant (e.g., CAHS3-L207P) fails to form gels in vitro, linking filament formation to gelation (tanaka2021stressdependentcellstiffening pages 12-15, tanaka2021stressdependentcellstiffening pages 10-12).

These data support a model in which CAHS3’s primary biophysical “activity” is stress-triggered polymerization into a filamentous network, with macroscopic gel behavior emerging at sufficient concentration/ionic conditions (tanaka2022stressdependentcellstiffening pages 13-14, tanaka2021stressdependentcellstiffening pages 12-15).

3.3 Mechanistic role during dehydration: physical stabilization of cells

CAHS3 appears to provide on-demand mechanical reinforcement to cells under dehydration-like stress:

• In cell-like microdroplets, CAHS3 transitions from a liquid-like state to a stiffer state upon stress-induced filament formation, reaching an elasticity characterized by Young’s modulus ~2.0 kPa under conditions inducing filamentation/gelation (tanaka2021stressdependentcellstiffening pages 12-15, tanaka2021stressdependentdynamicanda pages 12-16, tanaka2022stressdependentcellstiffening media e7bc2dfb).
• In insect cells, CAHS3 expression increases stiffness/elasticity under hyperosmotic stress (reported as significant, p < 0.05) and improves resistance to stress-induced shrinkage (volume retention p < 0.001), consistent with mechanical stabilization against osmotic deformation (tanaka2021stressdependentcellstiffening pages 12-15, tanaka2022stressdependentcellstiffening media 0b15f4fb).

Collectively, these experiments support the hypothesis that a principal role of CAHS3 in anhydrobiosis is mechanical/structural stabilization of the cytoplasm, likely limiting deformation and damage during dehydration and rehydration cycles (tanaka2022stressdependentcellstiffening pages 13-14, tanaka2021stressdependentcellstiffening pages 12-15).

4) Localization: where CAHS3 acts

4.1 Subcellular localization

CAHS3 is reported to be cytosolic, not nuclear and not extracellular, consistent with its designation as “cytosolic-abundant” and with the idea that it stabilizes the cytoplasm during dehydration-like stress (tanaka2022stressdependentcellstiffening pages 13-14, tanaka2021stressdependentcellstiffening pages 12-15).

4.2 Tissue-level expression in tardigrades (in vivo)

A major 2023 advance was the development of the TardiVec in vivo expression system using R. varieornatus promoters to drive tissue-specific expression and live imaging (published Jan 2023). Using a CAHS3 promoter construct (pRvCAHS3), GFP signal was observed most strongly in the epidermal tissue (tanaka2023invivoexpression pages 3-4). This tissue bias was also emphasized in a 2024 promoter/motif study (published Sep 2024) that described CAHS3 as among the most highly expressed CAHS paralogs and noted pronounced epidermal expression in vivo (ishikawa2024searchforputative pages 1-2).

This is conceptually important: it suggests that even “core” anhydrobiosis proteins may be deployed non-uniformly across cell types, implying cell-type-specific anhydrobiosis machinery and possibly distinct mechanical requirements in different tissues (tanaka2023invivoexpression pages 3-4).

5) Expression and regulation (2023–2024 progress)

5.1 Promoter mapping and conserved motifs upstream of CAHS3

A 2024 study (Ishikawa et al., Genes to Cells, Sep 2024) performed in vivo promoter truncation assays and in silico motif discovery for RvCAHS3.

• A ~300–350 bp upstream region of RvCAHS3 was identified as critical for regulating expression in tardigrade vector experiments (ishikawa2024searchforputative pages 1-2).
• Three conserved motifs were described in the upstream region: MRv-6 (−440 to −433), MRv-7 (−191 to −184), and MRv-39 (sequence ACGGCAAAAC; at −307 to −298 on the negative strand; reported across 1032 sites (12.9%) genome-wide and present in multiple CAHS genes) (ishikawa2024searchforputative pages 4-5).

The conservation of these motifs across multiple CAHS genes supports the existence of shared cis-regulatory logic for parts of the CAHS gene family and potentially other anhydrobiosis-related genes (ishikawa2024searchforputative pages 4-5).

6) Quantitative and statistical data from recent/primary studies

Key quantitative findings that directly constrain CAHS3 functional hypotheses are:

• Endogenous CAHS3 amount: ~3.8 ng per animal (immunoblot-based), with wet mass ~1.84 µg, implying a rough cytosolic concentration of ~2 mg/mL in hydrated animals (tanaka2022stressdependentcellstiffening pages 13-14).
• Gel threshold concentration: in vitro sol–gel transition at ~4 mg/mL, close to the above estimate; dehydration-associated volume reduction could increase effective intracellular CAHS3 concentration and ionic strength, favoring gelation in vivo (tanaka2022stressdependentcellstiffening pages 13-14, tanaka2021stressdependentcellstiffening pages 12-15).
• Mechanical property (microdroplets): stress-induced assembly produces a material response measured as Young’s modulus ~2.0 kPa (tanaka2021stressdependentcellstiffening pages 12-15, tanaka2021stressdependentdynamicanda pages 12-16).
• Heterologous cell mechanics/volume: CAHS3 increases elasticity under stress (p < 0.05) and improves volume retention (p < 0.001) in an osmotic stress paradigm (tanaka2021stressdependentcellstiffening pages 12-15).

A compact, citation-linked quantitative summary is provided below.

Table: This table summarizes experimentally supported properties of Ramazzottius varieornatus CAHS3 (UniProt J7M3T1), including localization, stress-induced assembly, biophysical effects, and promoter regulation. It is useful as a compact evidence map linking quantitative observations to specific assays and sources.

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

7.1 2023–2024: moving from “protective protein” to “regulated material state”

Across the desiccation-tolerance field, CAHS proteins are increasingly treated as stress-responsive biomaterials (gels/glasses/condensates) rather than conventional enzymes or receptors.

• A 2024 Chemical Reviews article synthesizes evidence that CAHS proteins are cytosolically abundant, heat-soluble proteins linked to desiccation survival, can form reversible hydrogels/aerogels, and can protect enzymes/membranes in vitro comparably to (or better than) protective sugars; however, it emphasizes that mechanistic details remain incompletely resolved (Apr 2024) (olgenblum2024protectingproteinsfrom pages 2-3).
• 2024 work in eLife emphasizes that protective IDPs (including CAHS family members) can show functional synergy with endogenous cosolutes during drying and that, for CAHS proteins, synergy relates to self-assembly/gel formation (Nov 2024) (kc2024disorderedproteinsinteract pages 26-27).

7.2 2023–2024: separating hypotheses (water retention vs water interaction; gelation vs protection)

Although not CAHS3-specific, recent CAHS-family work has refined several mechanistic hypotheses relevant to CAHS3 interpretation.

• Thermogravimetric and cellular assays for CAHS D suggest CAHS gels do not simply protect by increasing total water retained in dried systems; rather, CAHS can interact with residual water without increasing bulk retention, arguing against “water retention” as a sole explanation (Jun 2023) (sanchezmartinez2023thetardigradeprotein pages 6-7).
• Work on CAHS D gel/fibril networking links assembly to protective phenotypes and to reversible physiological changes (e.g., reduced metabolic activity during osmotic shock), framing gelation as a potentially causal, tunable state in stress survival and “biostasis” (Mar 2024) (sanchezmartinez2024labileassemblyof pages 1-2).

These studies reinforce that CAHS-family proteins can protect via state changes and biophysical interactions rather than classical catalytic activity; CAHS3 likely shares this logic but with CAHS3-specific assembly rules documented above (tanaka2022stressdependentcellstiffening pages 13-14, tanaka2021stressdependentcellstiffening pages 12-15).

8) Current applications and real-world implementations

Direct real-world deployment of CAHS3 specifically is still limited in the literature retrieved here; most translational work uses other CAHS paralogs as model excipients. However, the CAHS-family concept is already being explored for dry biostabilization and engineering stress tolerance, which provides a plausible application pathway for CAHS3-like proteins.

• A 2024 Chemical Reviews article highlights efforts to exploit molecular glasses and gels (including protein gels) to protect proteins in dry/highly desiccated states, explicitly including tardigrade CAHS proteins among the best-studied protein-based mediators (Apr 2024) (olgenblum2024protectingproteinsfrom pages 2-3).
• 2024 mechanistic work suggests that solution chemistry (cosolutes) can tune protective function of desiccation-related IDPs and that CAHS self-assembly is important for synergy with cosolutes, supporting future formulation/engineering strategies (Nov 2024) (kc2024disorderedproteinsinteract pages 26-27).

9) Expert synthesis and interpretation (evidence-based analysis)

Most supported CAHS3 functional annotation: CAHS3 is a cytosolic, stress-inducible, reversible filament-/gel-forming protein that likely contributes to anhydrobiosis by providing on-demand mechanical stabilization of cells as water loss increases cytoplasmic crowding and ionic strength (tanaka2022stressdependentcellstiffening pages 13-14, tanaka2021stressdependentcellstiffening pages 12-15).

Why this interpretation is strong: (i) CAHS3 assembly is conditional (stress-dependent), reversible, and sequence-specific (CR1/CR2 helix integrity required), indicating regulated material behavior rather than nonspecific aggregation; (ii) assembly has measurable mechanical consequences (kPa-scale stiffness) and improves hyperosmotic stress phenotypes in heterologous systems (tanaka2022stressdependentcellstiffening pages 13-14, tanaka2021stressdependentcellstiffening pages 12-15, tanaka2022stressdependentcellstiffening media e7bc2dfb).

What remains uncertain: CAHS3 is often discussed in the same conceptual space as “vitrification” and enzyme protection in broader CAHS literature, but the most direct CAHS3 evidence currently emphasizes cytoskeletal/gel-like mechanical stabilization rather than a demonstrated, CAHS3-specific, client-enzyme stabilization mechanism (tanaka2022stressdependentcellstiffening pages 13-14, olgenblum2024protectingproteinsfrom pages 2-3). Accordingly, enzyme-protection claims should be treated as family-level plausibility unless directly tested for CAHS3.

10) Visual evidence (key experimental phenotypes)

Stress-induced filament formation, in vitro gel transition, and stiffness-related phenotypes for CAHS3 are shown in extracted figure panels from Tanaka et al. 2022 (tanaka2022stressdependentcellstiffening media 2119c462, tanaka2022stressdependentcellstiffening media e7bc2dfb, tanaka2022stressdependentcellstiffening media 0b15f4fb).

Key sources (with publication date and URL)

• Tanaka A. et al. Stress-dependent cell stiffening by tardigrade tolerance proteins that reversibly form a filamentous network and gel. PLOS Biology. 2022-09. https://doi.org/10.1371/journal.pbio.3001780 (tanaka2022stressdependentcellstiffening pages 13-14)
• Tanaka S. et al. In vivo expression vector derived from anhydrobiotic tardigrade genome enables live imaging in Eutardigrada. PNAS. 2023-01. https://doi.org/10.1073/pnas.2216739120 (tanaka2023invivoexpression pages 3-4)
• Ishikawa S. et al. Search for putative gene regulatory motifs in cahs3… Genes to Cells. 2024-09. https://doi.org/10.1111/gtc.13168 (ishikawa2024searchforputative pages 1-2, ishikawa2024searchforputative pages 4-5)
• Olgenblum G.I. et al. Protecting proteins from desiccation stress using molecular glasses and gels. Chemical Reviews. 2024-04. https://doi.org/10.1021/acs.chemrev.3c00752 (olgenblum2024protectingproteinsfrom pages 2-3)
• KC S. et al. Disordered proteins interact with the chemical environment to tune their protective function during drying. eLife. 2024-11. https://doi.org/10.7554/elife.97231 (kc2024disorderedproteinsinteract pages 26-27)

References

1. (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.

2. (ishikawa2024searchforputative pages 1-2): Sora Ishikawa, Sae Tanaka, and Kazuharu Arakawa. Search for putative gene regulatory motifs in cahs3, linked to anhydrobiosis in a tardigrade ramazzottius varieornatus, in vivo and in silico. Genes to Cells, 29:1144-1153, Sep 2024. URL: https://doi.org/10.1111/gtc.13168, doi:10.1111/gtc.13168. This article has 0 citations and is from a peer-reviewed journal.

3. (olgenblum2024protectingproteinsfrom pages 2-3): Gil I. Olgenblum, Brent O. Hutcheson, Gary J. Pielak, and Daniel Harries. Protecting proteins from desiccation stress using molecular glasses and gels. Chemical Reviews, 124:5668-5694, Apr 2024. URL: https://doi.org/10.1021/acs.chemrev.3c00752, doi:10.1021/acs.chemrev.3c00752. This article has 29 citations and is from a highest quality peer-reviewed journal.

4. (tanaka2021stressdependentcellstiffening pages 12-15): 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 through reversible formation of cytoskeleton-like filamentous network and gel-transition. bioRxiv, Oct 2021. URL: https://doi.org/10.1101/2021.10.02.462891, doi:10.1101/2021.10.02.462891. This article has 6 citations.

5. (tanaka2022stressdependentcellstiffening media e7bc2dfb): 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.

6. (tanaka2022stressdependentcellstiffening media 2119c462): 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.

7. (tanaka2021stressdependentcellstiffening pages 10-12): 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 through reversible formation of cytoskeleton-like filamentous network and gel-transition. bioRxiv, Oct 2021. URL: https://doi.org/10.1101/2021.10.02.462891, doi:10.1101/2021.10.02.462891. This article has 6 citations.

8. (tanaka2021stressdependentdynamicanda pages 12-16): A Tanaka, T Nakano, K Watanabe, and K Masuda. Stress-dependent dynamic and reversible formation of cytoskeleton-like filaments and gel-transition by tardigrade tolerance proteins. Unknown journal, 2021.

9. (tanaka2022stressdependentcellstiffening media 0b15f4fb): 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.

10. (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.

11. (ishikawa2024searchforputative pages 4-5): Sora Ishikawa, Sae Tanaka, and Kazuharu Arakawa. Search for putative gene regulatory motifs in cahs3, linked to anhydrobiosis in a tardigrade ramazzottius varieornatus, in vivo and in silico. Genes to Cells, 29:1144-1153, Sep 2024. URL: https://doi.org/10.1111/gtc.13168, doi:10.1111/gtc.13168. This article has 0 citations and is from a peer-reviewed journal.

12. (tanaka2021stressdependentdynamicand pages 12-16): A Tanaka, T Nakano, K Watanabe, and K Masuda. Stress-dependent dynamic and reversible formation of cytoskeleton-like filaments and gel-transition by tardigrade tolerance proteins. Unknown journal, 2021.

13. (kc2024disorderedproteinsinteract pages 26-27): 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.

14. (sanchezmartinez2023thetardigradeprotein pages 6-7): 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.

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