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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: J7MDG6
• Protein Description: RecName: Full=Cytosolic-abundant heat soluble protein 2 {ECO:0000303|PubMed:22937162}; Short=CAHS2 {ECO:0000303|PubMed:22937162}; AltName: Full=Tardigrade-specific intrinsically disordered protein CAHS2 {ECO:0000305}; Short=TDP CAHS2 {ECO:0000305};
• Gene Information: Name=CAHS2 {ECO:0000303|PubMed:22937162}; ORFNames=RvY_00946;
• 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 "CAHS2" 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 'CAHS2' 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 CAHS2 (gene ID: CAHS2, UniProt: J7MDG6) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: J7MDG6
• Protein Description: RecName: Full=Cytosolic-abundant heat soluble protein 2 {ECO:0000303|PubMed:22937162}; Short=CAHS2 {ECO:0000303|PubMed:22937162}; AltName: Full=Tardigrade-specific intrinsically disordered protein CAHS2 {ECO:0000305}; Short=TDP CAHS2 {ECO:0000305};
• Gene Information: Name=CAHS2 {ECO:0000303|PubMed:22937162}; ORFNames=RvY_00946;
• 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 "CAHS2" 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 'CAHS2' 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 CAHS2 (gene ID: CAHS2, UniProt: J7MDG6) 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 CAHS2 (UniProt J7MDG6) in Ramazzottius varieornatus

Executive summary

CAHS2 (cytosolic-abundant heat soluble protein 2) is a tardigrade-specific, highly hydrophilic, heat-soluble, intrinsically disordered protein (IDP) discovered as a major heat-soluble component of Ramazzottius varieornatus extracts and classified in the CAHS family on the basis of cytoplasmic localization. The strongest CAHS2-specific evidence supports: (i) identity in R. varieornatus, (ii) cytoplasmic localization, and (iii) family-level biophysics (disorder-to-helix transitions; conserved amphipathic repeat motifs) suggesting a stress-protection “molecular shield” concept during dehydration. However, direct CAHS2-specific functional assays (e.g., knockout, client protection assays, gelation thresholds) are currently scarce in the accessible literature; most mechanistic and quantitative evidence is derived from other CAHS paralogs (e.g., CAHS3) or CAHS proteins from related tardigrades (e.g., CAHS D). (yamaguchi2012twonovelheatsoluble pages 3-5, yamaguchi2012twonovelheatsoluble pages 1-2, yamaguchi2012twonovelheatsoluble pages 5-6)

Table: This table summarizes what is directly supported for Ramazzottius varieornatus CAHS2 (UniProt J7MDG6) versus what must currently be inferred from the CAHS family. It is useful for distinguishing firm CAHS2-specific annotation from broader mechanistic and application evidence derived from closely related CAHS proteins.

1) Key concepts and definitions (current understanding)

1.1 Anhydrobiosis and tardigrade stress-tolerance proteins

Anhydrobiosis is a reversible, near-complete dehydration state associated with profound reduction of metabolism and remarkable tolerance to temperature, radiation, and other extremes (conceptual background in CAHS-focused literature). CAHS proteins are highlighted as a tardigrade-unique class of protective proteins that contribute to coping with water loss in eutardigrades. (tanaka2022stressdependentcellstiffening pages 1-2, bino2024possiblerolesof pages 1-2)

1.2 CAHS proteins and what “heat-soluble” means

CAHS proteins were defined operationally by remaining soluble after extreme heating of cell lysates, analogous to how LEA proteins were historically studied for desiccation tolerance. In the foundational discovery workflow, the soluble fraction of R. varieornatus lysate was heated at 92°C for 15 minutes, and heat-soluble bands were isolated and sequenced; CAHS proteins were abundant among the recovered heat-soluble components. (yamaguchi2012twonovelheatsoluble pages 2-3)

1.3 Intrinsically disordered proteins (IDPs) and disorder–to–helix transitions

A central concept for CAHS proteins is intrinsic disorder in hydrated conditions and stress-triggered structural change. In the defining CAHS/SAHS study, CAHS proteins were described as intrinsically unstructured when hydrated, and as undergoing conformational change toward α-helical structure under water-deficient conditions (mimicked by desolvating agents such as TFE). Conserved CAHS repeat motifs were proposed to form amphiphilic α-helices, supporting a “molecular shield” model under dehydration. (yamaguchi2012twonovelheatsoluble pages 1-2, yamaguchi2012twonovelheatsoluble pages 3-5)

2) Gene/protein identity verification (mandatory)

CAHS2 in this report refers specifically to:
- Organism: Ramazzottius varieornatus (tardigrade)
- Family: Cytosolic-abundant heat soluble (CAHS)
- Localization class: cytoplasmic

This mapping is supported because the discovery paper explicitly states “CAHS1 and CAHS2 are cytoplasmic” and defines CAHS proteins as newly identified major heat-soluble proteins from R. varieornatus. (yamaguchi2012twonovelheatsoluble pages 3-5, yamaguchi2012twonovelheatsoluble pages 1-2)

3) Foundational experimental evidence for CAHS2 (2012 primary literature)

3.1 How CAHS2 was identified/defined

The CAHS/SAHS families were defined by heat-soluble proteomics in R. varieornatus, which:
- heated soluble lysate (92°C, 15 min) to enrich heat-soluble proteins;
- excised heat-soluble gel bands and identified peptides by mass spectrometry against a draft genome;
- obtained full-length cDNAs by RACE for a set of five abundant heat-soluble proteins; and
- named the families according to distinct subcellular localization classes: CAHS (cytoplasmic) versus SAHS (secretory). (yamaguchi2012twonovelheatsoluble pages 2-3)

3.2 Subcellular localization of CAHS2

CAHS2 is assigned to the cytoplasm (“CAHS1 and CAHS2 are cytoplasmic”), which is consistent with the UniProt description “cytosolic-abundant.” (yamaguchi2012twonovelheatsoluble pages 3-5)

3.3 Structural/biophysical properties inferred for CAHS2 from its family definition

The CAHS family is characterized by:
- intrinsic disorder in hydrated state;
- secondary-structure gain (α-helix) under water-deficient conditions;
- conserved 19-mer repeats capable of forming amphiphilic stripes in α-helices, proposed to function as a molecular shield under dehydration.

While these were established using representative CAHS proteins in the discovery study (not necessarily CAHS2 alone), CAHS2 is part of this family definition and shares these characteristic motifs/behavior by inference. (yamaguchi2012twonovelheatsoluble pages 1-2, yamaguchi2012twonovelheatsoluble pages 5-6)

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

4.1 CAHS proteins: protection is not simply “water retention” (2023)

A detailed thermogravimetric analysis study of CAHS D (a CAHS-family model protein from a different tardigrade) found that dried CAHS D retained ~4.03% water, comparable to gelatin (4.62%) and lysozyme (5.07%), while a different non-gelling protein retained 6.77%. This supports a modern view that CAHS-mediated tolerance is not explained by increasing bulk water retention, though CAHS can interact with residual water (shifted water-loss onset/offset temperatures). This family-level mechanistic clarification shapes how CAHS2 should be interpreted (CAHS2 is unlikely to be a simple “water sponge”). (sanchezmartinez2023thetardigradeprotein pages 3-4)

4.2 Gelation/fibrillization and reversible “biostasis” (2024)

A 2024 mechanistic study of CAHS D reports a gelation/fibrillization mechanism with features likened to intermediate filament assembly and links fibrillar networking to reversible biostasis (including metabolic suppression during osmotic shock). Quantitatively, gelation was strong at ~20 g/L (~0.8 mM), with thermal behavior (gel melt) near ~40°C in DSC experiments. This strengthens the field’s current emphasis on stress-induced self-assembly (filaments/gels) as a functional principle within the CAHS family, which may apply to CAHS2 if it shares similar assembly-prone sequence features. (sanchezmartinez2024labileassemblyof pages 5-6)

4.3 Shared regulatory motifs across CAHS genes (2024)

A 2024 regulatory study centered on CAHS3 reports that motifs identified upstream of CAHS3 were also found upstream of other CAHS genes, suggesting a shared cis-regulatory architecture among CAHS-family loci. Although CAHS2 was not functionally dissected in this text, it supports the concept that CAHS genes may be coordinately regulated as part of an anhydrobiosis-related program. (ishikawa2024searchforputative pages 1-2)

4.4 Evolutionary context and nomenclature complexity (2024)

A 2024 phylogenetic analysis of desiccation/temperature-related protein families in Tardigrada generates CAHS family phylogenies and notes nomenclature drift (homology-group numbering and genus-specific letters). This implies that mapping CAHS2 across datasets requires care, especially when older studies used different naming conventions for paralogs. (fleming2024theevolutionof pages 2-5)

4.5 CAHS proteins in mammalian cells (2024)

A 2024 study expressed codon-optimized R. varieornatus CAHS paralogs (CAHS1/3/8/12) in HeLa cells and used live imaging under hyperosmotic stress; expression of CAHS1/3/8 tended to enhance resilience to hyperosmotic conditions. While CAHS2 itself was not included, the study demonstrates real-world feasibility of deploying R. varieornatus CAHS proteins in mammalian systems and frames them as potential cryo/osmo-protectants. (bino2024possiblerolesof pages 1-2)

5) Functional interpretation: what CAHS2 likely does (and does not do)

5.1 Primary functional role (best-supported)

CAHS2 is best annotated as a non-enzymatic, cytosolic stress-protection protein. The primary evidence supports a model in which CAHS proteins (including CAHS2 by family membership) contribute to tolerance of dehydration-like conditions through stress-responsive structural transitions (disorder→α-helix) and potentially amphipathic helical shielding of vulnerable cellular macromolecules during water loss. (yamaguchi2012twonovelheatsoluble pages 1-2, yamaguchi2012twonovelheatsoluble pages 5-6)

5.2 Mechanistic models under active refinement (expert synthesis)

Two broad, not mutually exclusive, CAHS-family mechanisms are emphasized in authoritative sources:
- Self-assembly into networks/gels/condensates that change cell material properties and can reduce molecular motion (supported by CAHS3 and CAHS D mechanistic work). (tanaka2022stressdependentcellstiffening pages 11-13, sanchezmartinez2024labileassemblyof pages 5-6)
- Vitrification/glass-like states in dried conditions, debated and nuanced by later data showing the mechanism is not simply bulk water retention and may depend on chemical environment and assembly behavior. (sanchezmartinez2023thetardigradeprotein pages 3-4, sanchezmartinez2024labileassemblyof pages 5-6)

CAHS2 itself has not been shown in the retrieved sources to form a particular material state (gel/filament) under defined conditions, so this remains a hypothesis by analogy.

5.3 Cellular localization and pathways

The most direct localization evidence for CAHS2 is cytoplasmic (and by implication part of cytosolic stress-protection rather than secretory or mitochondrial pathways). No CAHS2-specific binding partners or canonical signaling pathway membership were found in retrieved sources; CAHS proteins are generally treated as biophysical effectors rather than enzymes in a defined metabolic pathway. (yamaguchi2012twonovelheatsoluble pages 3-5)

6) Quantitative data and statistics from recent studies (relevant to CAHS-family; CAHS2-specific gaps noted)

6.1 Cell/material mechanics (CAHS3 exemplar)

In CAHS3 experiments (a R. varieornatus CAHS paralog), salt-induced filament formation in protein-containing droplets produced gel-like elasticity with average Young’s modulus ~2.0 kPa; hyperosmotic conditions included 0.4 M trehalose. In vitro gel transition was reported at roughly ~4 mg/mL CAHS protein in that system. Additionally, endogenous CAHS3 abundance was estimated at ~3.81 ng per tardigrade. These quantitative benchmarks support the “mechanical stabilization” hypothesis for CAHS proteins. (tanaka2022stressdependentcellstiffening pages 11-13, tanaka2022stressdependentcellstiffening pages 20-22)

6.2 Water retention versus water interaction (CAHS D exemplar)

Dried CAHS D contained 4.03% water, similar to common proteins; a non-gelling control retained 6.77%. This argues against CAHS protection being explained by exceptional total water retention. (sanchezmartinez2023thetardigradeprotein pages 3-4)

6.3 CAHS-based dry preservation of a therapeutic protein (FVIII)

A key translational demonstration used engineered CAHS D variants as excipients for FVIII:
- A CAHS D Linker Region formulation used 10 mg/mL CAHS with FVIII and stored samples at ambient ~22°C, with assays at weekly intervals; this formulation stabilized dried FVIII for ≥10 weeks with no statistically significant loss of function in the excerpted results. (packebush2023naturalandengineered pages 14-14, packebush2023naturalandengineered pages 8-10)
- Under severe dry heat stress (95°C for 48 h), engineered CAHS (2X Linker) provided robust protection across 0.1–20 mg/mL. Sugar benchmarks: sucrose protected FVIII across 0.1–20 mg/mL, trehalose gave full protection at 1–20 mg/mL. (packebush2023naturalandengineered pages 7-8)

These data are not CAHS2-specific but demonstrate the practical potential of CAHS-family proteins as cold-chain-breaking excipients.

7) Current applications and real-world implementations

1. Dry biologics stabilization / pharmaceutical excipients: engineered CAHS variants enabling weeks-long dry storage of FVIII at ambient temperature and resistance to extreme dry heat. (packebush2023naturalandengineered pages 8-10, packebush2023naturalandengineered pages 7-8)
2. Engineering stress-tolerant mammalian cells: heterologous expression of R. varieornatus CAHS paralogs in HeLa cells with improved hyperosmotic resilience (qualitative in retrieved text). (bino2024possiblerolesof pages 1-2)
3. Synthetic biology / cell protection paradigms: CAHS2 is used as a representative tardigrade extremotolerance protein in a large-scale screen showing that some extremotolerance-associated proteins can form condensates and attenuate apoptosis in human cells, linking condensate formation to cellular protection concepts. (veling2022naturalanddesigned pages 1-3)

8) Expert opinions and authoritative synthesis

Authoritative review-level framing (Chemical Reviews 2023) emphasizes two converging themes in desiccation biology: (i) IDPs (including CAHS/LEA) as protective agents, and (ii) condensates/self-assembly as an organizing principle during water loss. This provides expert-context support for interpreting CAHS2 as a biophysical protectant rather than a classical pathway enzyme. (bino2024possiblerolesof pages 1-2)

9) Evidence gaps and recommended annotation confidence

9.1 What can be annotated with high confidence for CAHS2 (J7MDG6)

• Protein class: tardigrade-specific CAHS family, heat-soluble, hydrophilic IDP (family definition). (yamaguchi2012twonovelheatsoluble pages 1-2)
• Localization: cytoplasm. (yamaguchi2012twonovelheatsoluble pages 3-5)
• Likely function: contributes to desiccation/anhydrobiosis tolerance via biophysical stabilization under water-deficient stress (family-level inference consistent with CAHS mechanisms). (tanaka2022stressdependentcellstiffening pages 1-2, yamaguchi2012twonovelheatsoluble pages 1-2)

9.2 What cannot yet be stated specifically for CAHS2 from retrieved sources

• A CAHS2-specific gelation threshold, filament formation behavior, or phase behavior.
• A CAHS2-specific client protection assay (enzyme/biologic stabilization).
• A CAHS2-specific in vivo phenotype (knockout/knockdown) in R. varieornatus.
• Direct CAHS2 interaction partners or participation in a defined biochemical pathway.

10) Conclusion

CAHS2 (UniProt J7MDG6) from R. varieornatus is best interpreted as a cytosolic, tardigrade-specific intrinsically disordered stress-protection protein initially defined by extreme heat-solubility and cytoplasmic localization, with a plausible mechanism involving dehydration-triggered formation of amphipathic helices and, by family analogy, stress-induced self-assembly that stabilizes intracellular structures. The most significant 2023–2024 advances refine mechanistic models for CAHS proteins (especially CAHS D) and demonstrate compelling applications (dry preservation of FVIII, mammalian osmotic tolerance engineering), but direct CAHS2-specific experimental mechanistic data remain limited, making CAHS2 annotation partly reliant on CAHS family inference. (yamaguchi2012twonovelheatsoluble pages 3-5, sanchezmartinez2023thetardigradeprotein pages 3-4, sanchezmartinez2024labileassemblyof pages 5-6, packebush2023naturalandengineered pages 8-10, bino2024possiblerolesof pages 1-2)

References

1. (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.

2. (yamaguchi2012twonovelheatsoluble pages 1-2): 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.

3. (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.

4. (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.

5. (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.

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8. (tanaka2022stressdependentcellstiffening pages 1-2): 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.

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11. (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.

12. (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.

13. (sanchezmartinez2024labileassemblyof pages 5-6): 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.

14. (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.

15. (packebush2023naturalandengineered pages 2-3): 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.

16. (packebush2023naturalandengineered pages 10-13): 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.

17. (packebush2023naturalandengineered pages 14-14): 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.

18. (packebush2023naturalandengineered pages 8-10): 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.

19. (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.

20. (veling2022naturalanddesigned pages 1-3): Mike T. Veling, Dan T. Nguyen, Nicole N. Thadani, Michela E. Oster, Nathan J. Rollins, Kelly P. Brock, Neville P. Bethel, Samuel Lim, David Baker, Jeffrey C. Way, Debora S. Marks, Roger L. Chang, and Pamela A. Silver. Natural and designed proteins inspired by extremotolerant organisms can form condensates and attenuate apoptosis in human cells. ACS Synthetic Biology, 11:1292-1302, Feb 2022. URL: https://doi.org/10.1021/acssynbio.1c00572, doi:10.1021/acssynbio.1c00572. This article has 25 citations and is from a domain leading peer-reviewed journal.

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