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gene_id: RvLEAM
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gene_info: Name=RvLEAM {ECO:0000303|PubMed:25675104}; ORFNames=RvY_15023;
organism_full: Ramazzottius varieornatus (Water bear) (Tardigrade).
protein_family: Belongs to the LEA type 4 family. .
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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: A0A0E4AVP3
• Protein Description: RecName: Full=Group 3 late-embryogenesis abundant protein, mitochondrial {ECO:0000303|PubMed:25675104}; Short=LEAM {ECO:0000303|PubMed:25675104}; Flags: Precursor;
• Gene Information: Name=RvLEAM {ECO:0000303|PubMed:25675104}; ORFNames=RvY_15023;
• Organism (full): Ramazzottius varieornatus (Water bear) (Tardigrade).
• Protein Family: Belongs to the LEA type 4 family. .
• Key Domains: Not specified in UniProt

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "RvLEAM" 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 'RvLEAM' 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 RvLEAM (gene ID: RvLEAM, UniProt: A0A0E4AVP3) 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: A0A0E4AVP3
• Protein Description: RecName: Full=Group 3 late-embryogenesis abundant protein, mitochondrial {ECO:0000303|PubMed:25675104}; Short=LEAM {ECO:0000303|PubMed:25675104}; Flags: Precursor;
• Gene Information: Name=RvLEAM {ECO:0000303|PubMed:25675104}; ORFNames=RvY_15023;
• Organism (full): Ramazzottius varieornatus (Water bear) (Tardigrade).
• Protein Family: Belongs to the LEA type 4 family. .
• Key Domains: Not specified in UniProt

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "RvLEAM" 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 'RvLEAM' 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 RvLEAM (gene ID: RvLEAM, UniProt: A0A0E4AVP3) 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 RvLEAM (UniProt A0A0E4AVP3) from Ramazzottius varieornatus

1) Target verification (mandatory disambiguation)

The target gene/protein in this report is RvLEAM from the tardigrade Ramazzottius varieornatus (water bear), matching the UniProt entry A0A0E4AVP3, described as a mitochondrial Group 3 late-embryogenesis abundant (LEA) protein (often referred to as LEAM) (tanaka2015novelmitochondriatargetedheatsoluble pages 2-4). The defining primary paper (peer-reviewed) explicitly names and characterizes RvLEAM as a mitochondrial LEA protein from R. varieornatus and provides both native-organism and heterologous localization experiments (tanaka2015novelmitochondriatargetedheatsoluble pages 5-7, tanaka2015novelmitochondriatargetedheatsoluble pages 2-4). No evidence in the retrieved corpus suggests an alternative gene with the same symbol in another organism; thus, the symbol is treated as unambiguous in this context (tanaka2015novelmitochondriatargetedheatsoluble pages 2-4).

2) Key concepts and definitions (current understanding)

2.1 Late Embryogenesis Abundant (LEA) proteins and “group 3 LEA/LEAM”

LEA proteins are classically described as highly hydrophilic, stress-associated proteins that are typically intrinsically disordered in aqueous conditions but can acquire α-helical structure under water deficit. Mechanistic models emphasize protection of other macromolecules through molecular shielding/anti-aggregation, membrane stabilization, and contributions to vitrification/glass-like states in the dry cytoplasm (hand2018challengesduringdiapause pages 8-8, romeroperez2023whenphasedwithout pages 22-23). A recent high-authority synthesis (Chemical Reviews, 2023) also frames LEA/hydrophilin protection in terms of hydration-dependent phase/material properties, including effects on vitrification and protective assemblies (romeroperez2023whenphasedwithout pages 11-12, romeroperez2023whenphasedwithout pages 22-23).

Group 3 LEA proteins are commonly enriched for repeated short motifs and are frequently predicted to form amphipathic α-helices under dehydration-like conditions, consistent with “molecular shield” and membrane-protective models (yoshida2022decipheringthebiological pages 4-6, romeroperez2023whenphasedwithout pages 22-23).

2.2 Mitochondrial LEA proteins

Mitochondria are major sites of stress vulnerability during dehydration/rehydration (bioenergetic collapse, membrane perturbation, ROS). Mitochondria-targeted LEA proteins are therefore hypothesized to provide organelle-localized protection via the same physical-chemical modes (shielding, membrane stabilization, glass modulation) but focused on mitochondrial matrices and membranes (hand2018challengesduringdiapause pages 8-8). In tardigrades, mitochondrial-localized heat-soluble proteins including RvLEAM were described as candidate mitochondrial protectants (schill2019environmentaladaptationsdesiccation pages 10-13).

3) RvLEAM: sequence/family features and inferred molecular properties

Tanaka et al. (2015) report that RvLEAM shows sequence similarity to nematode LEA proteins (e-value < 1e−05) and matches a LEA-related motif (PTHR23241), supporting its assignment as a canonical LEA-family protein rather than a tardigrade-unique disordered protein family (tanaka2015novelmitochondriatargetedheatsoluble pages 4-5). They identify nine LEA-like 11-mer motifs, consistent with group 3 LEA architecture and predicted helical repeats (tanaka2015novelmitochondriatargetedheatsoluble pages 4-5).

Physicochemical predictions show RvLEAM is highly hydrophilic (GRAVY −0.94) with no strong hydrophobic segment, consistent with a soluble protein. The absence of a transmembrane region led the authors to infer mitochondrial matrix localization rather than membrane insertion (tanaka2015novelmitochondriatargetedheatsoluble pages 4-5). Secondary-structure prediction suggested long helical regions and putative amphipathic helices (tanaka2015novelmitochondriatargetedheatsoluble pages 4-5), aligning with prevailing LEA models in which amphipathic helices interact with protein or membrane surfaces during dehydration/osmotic stress (yoshida2022decipheringthebiological pages 4-6, romeroperez2023whenphasedwithout pages 22-23).

4) Subcellular localization: direct experimental evidence

4.1 Computational targeting predictions

Multiple predictors (TargetP, WoLF PSORT, MitoProt2) supported mitochondrial targeting; TargetP predicted a 31-aa N-terminal mitochondrial targeting peptide (tanaka2015novelmitochondriatargetedheatsoluble pages 5-7, tanaka2015novelmitochondriatargetedheatsoluble pages 4-5).

4.2 Heterologous localization (human cells)

In human HEp-2 cells, an RvLEAM–GFP fusion co-localized with mitochondria stained by MitoTracker, while GFP alone was diffuse (tanaka2015novelmitochondriatargetedheatsoluble pages 5-7). A cropped figure region showing this co-localization (Figure 1d in the original paper) was retrieved (tanaka2015novelmitochondriatargetedheatsoluble media 470ae241).

4.3 Native localization (tardigrade embryos)

Immunohistochemistry in R. varieornatus embryos detected RvLEAM signal broadly across cells and mostly merged with ATP5A, a mitochondrial marker, providing direct evidence that RvLEAM localizes to mitochondria in the native organism (tanaka2015novelmitochondriatargetedheatsoluble pages 5-7).

5) Biochemical properties: heat solubility and implications

A defining biochemical feature reported for RvLEAM is heat solubility. Recombinant RvLEAM expressed in bacteria remained largely in the soluble fraction after high-temperature treatment, and purified RvLEAM alone was also heat-soluble (tanaka2015novelmitochondriatargetedheatsoluble pages 5-7). Heat-solubility is consistent with LEA proteins being enriched in disorder and resistant to aggregation during stress, enabling them to function under extreme physicochemical conditions (romeroperez2023whenphasedwithout pages 22-23).

6) Primary functional evidence: stress tolerance phenotypes (heterologous system)

6.1 Hyperosmotic stress tolerance in human cells

Tanaka et al. used stable HEp-2 lines expressing RvLEAM and challenged cells with 100–350 mM sucrose for 48 h, using a PrestoBlue reducing-power assay to quantify relative metabolic activity (normalized to 0 mM sucrose; n=3, SEM; Dunnett’s test) (tanaka2015novelmitochondriatargetedheatsoluble pages 10-11, tanaka2015novelmitochondriatargetedheatsoluble pages 4-5). RvLEAM-expressing cells exhibited significantly improved tolerance across conditions, including an approximately two-fold increase in metabolic activity at 300 mM sucrose and at least ~10% improvement across tested concentrations (tanaka2015novelmitochondriatargetedheatsoluble pages 10-11). A cropped region containing the hyperosmotic tolerance plot (Figure 5) was retrieved (tanaka2015novelmitochondriatargetedheatsoluble media 129a06d0).

Interpretation: This experiment provides direct functional evidence that RvLEAM can enhance cellular performance under osmotic/water stress when targeted to mitochondria, consistent with mitochondrial protection being a key bottleneck in anhydrobiotic/cryptobiotic survival (tanaka2015novelmitochondriatargetedheatsoluble pages 10-11, hand2018challengesduringdiapause pages 8-8).

7) Pathways and biological role (evidence-based + inference)

No enzymatic catalytic activity is reported for RvLEAM; instead, evidence supports RvLEAM as a non-enzymatic, stress-protective, organelle-localized protein. The best-supported functional model is that RvLEAM contributes to tolerance of water/osmotic stress by protecting mitochondrial components (proteins and/or membranes) via LEA-like physical mechanisms (molecular shielding, stabilization of macromolecular assemblies, modulation of dry-state material properties) (hand2018challengesduringdiapause pages 8-8, yoshida2022decipheringthebiological pages 4-6, romeroperez2023whenphasedwithout pages 22-23).

While RvLEAM itself was not demonstrated to induce gels/condensates (those observations are stronger for tardigrade CAHS-family proteins), broader desiccation biology emphasizes that protective IDPs/LEA proteins can influence vitrification/glass transition behavior and hydration-dependent phase/material transitions, which may be central to survival in dry states (romeroperez2023whenphasedwithout pages 11-12, romeroperez2023whenphasedwithout pages 22-23). Thus, RvLEAM’s predicted amphipathic helical segments and heat-solubility are consistent with canonical LEA modes of action (tanaka2015novelmitochondriatargetedheatsoluble pages 4-5, romeroperez2023whenphasedwithout pages 22-23).

8) Recent developments (prioritizing 2023–2024)

8.1 2023: Updated mechanistic framing (biophysics/condensates)

A 2023 Chemical Reviews article synthesized modern understanding of desiccation tolerance across biomolecules and condensate/material-state changes, discussing how IDPs (including LEA/hydrophilins and tardigrade disordered proteins) can protect through molecular shielding, gelation/solidification, and effects on vitrification and diffusion in drying cells (romeroperez2023whenphasedwithout pages 11-12, romeroperez2023whenphasedwithout pages 22-23). This provides up-to-date conceptual scaffolding for interpreting RvLEAM as a mitochondrial-localized component of a broader stress-protective material strategy.

8.2 2024: RvLEAM becomes a structural biology reagent (cryo-EM implementation)

A major 2024 development is the repurposing of RvLEAM as a practical additive for cryo-electron microscopy sample preparation. Abe et al. (Nature Communications, 2024-09-xx) used a truncated construct RvLEAMshort (~15 kDa) derived from R. varieornatus RvLEAM to mitigate air–water interface (AWI) damage during plunge freezing (abe2024smallleaproteinsa pages 2-3). In reported datasets, adding RvLEAMshort at 1:6 sample:RvLEAMshort enabled reconstructions at 4.5 Å (polymerase α-primase) and 3.7 Å (PRC2) (abe2024smallleaproteinsa pages 2-3, abe2024smallleaproteinsa pages 4-5).

Quantitatively, in a crosslinked PRC2 control without RvLEAMshort only ~3% of ~1.7 million picked particles contributed to the final map, whereas with RvLEAMshort ~14% of ~2.5 million picked particles contributed, indicating higher particle usability/retention (abe2024smallleaproteinsa pages 4-5). Orientation isotropy improved substantially (sphericity up to 0.97 with crosslinking + RvLEAMshort) and a 3.1 Å map was obtained under a 10-min crosslink condition (abe2024smallleaproteinsa pages 5-6, abe2024smallleaproteinsa pages 3-4).

Relevance to functional annotation: Although this is an ex vivo application, it strongly supports the concept that LEA proteins (including a tardigrade mitochondrial LEA) can act as surface-active protective agents under extreme interfacial stress—consistent with “molecular shielding” and stress stabilization frameworks (abe2024smallleaproteinsa pages 2-3, romeroperez2023whenphasedwithout pages 22-23).

9) Current applications and real-world implementations

1) Cell stress-engineering concept: RvLEAM expression in human cells improves survival/metabolic activity under hyperosmotic stress (tanaka2015novelmitochondriatargetedheatsoluble pages 10-11). While not yet a deployed clinical/industrial product in the retrieved sources, this is a concrete demonstration of translational potential (engineering mitochondrial protectants for cell preservation or stress resilience).

2) Structural biology workflow additive (implemented in practice): RvLEAMshort is used as an AWI protectant in cryo-EM grid preparation to enable/accelerate high-resolution structure determination for fragile complexes, with explicit workflow parameters and quantitative improvements in particle retention and orientation distribution (abe2024smallleaproteinsa pages 2-3, abe2024smallleaproteinsa pages 4-5).

10) Expert opinions / authoritative analysis

A tardigrade-focused review of anhydrobiosis genomics emphasizes that LEA proteins are typically hydrophilic and unstructured, can form amphipathic helices under water deficit, and that mitochondrial-localized examples (including RvLEAM) can improve hyperosmotic tolerance in human cells—supporting the view of RvLEAM as a mitochondria-targeted protectant (yoshida2022decipheringthebiological pages 4-6). More broadly, the Chemical Reviews synthesis highlights that while multiple protective IDP families exist, the molecular rules remain incompletely resolved, and dry-state biology likely involves coupled effects on diffusion, glass transitions, and biomolecular phase behavior (romeroperez2023whenphasedwithout pages 11-12).

11) Key statistics and quantitative data (from recent studies)

• Human-cell hyperosmotic tolerance (2015 primary study): 100–350 mM sucrose exposure for 48 h; RvLEAM expression yields ~2× higher metabolic activity at 300 mM sucrose, with ≥~10% improvement across tested conditions (tanaka2015novelmitochondriatargetedheatsoluble pages 10-11, tanaka2015novelmitochondriatargetedheatsoluble media 129a06d0).
• Cryo-EM AWI protection (2024 Nature Communications): with RvLEAMshort at 1:6 sample:LEA, maps at 4.5 Å (PP) and 3.7 Å (PRC2) (abe2024smallleaproteinsa pages 2-3, abe2024smallleaproteinsa pages 4-5). With crosslinking + RvLEAMshort: PRC2 sphericity 0.97 and 3.1 Å map (abe2024smallleaproteinsa pages 5-6, abe2024smallleaproteinsa pages 3-4). Particle contribution improves from ~3% of 1.7M (no RvLEAMshort control) to ~14% of 2.5M (with RvLEAMshort) (abe2024smallleaproteinsa pages 4-5).

12) Limitations and evidence gaps

• Direct loss-of-function or knockdown/knockout evidence in R. varieornatus demonstrating RvLEAM necessity for anhydrobiosis was not present in the retrieved sources; current functional support is strongest for localization and heterologous protective effects (tanaka2015novelmitochondriatargetedheatsoluble pages 5-7, tanaka2015novelmitochondriatargetedheatsoluble pages 10-11).
• No direct measurements were retrieved for RvLEAM structural transitions during dehydration (e.g., CD/FTIR of RvLEAM itself), nor direct identification of specific mitochondrial binding partners or substrates.

13) Evidence summary table

The following table consolidates major claims, evidence types, quantitative outcomes, and metadata.

Table: This table compiles the main experimentally supported and inferred findings for RvLEAM from Ramazzottius varieornatus, including identity verification, mitochondrial localization, structural and biochemical properties, stress-tolerance effects, and recent biotechnology applications.

Key source URLs (with publication dates)

• Tanaka S. et al. “Novel Mitochondria-Targeted Heat-Soluble Proteins Identified in the Anhydrobiotic Tardigrade Improve Osmotic Tolerance of Human Cells.” PLoS ONE (2015-02). https://doi.org/10.1371/journal.pone.0118272 (tanaka2015novelmitochondriatargetedheatsoluble pages 5-7, tanaka2015novelmitochondriatargetedheatsoluble pages 10-11)
• Abe K.M. et al. “Small LEA proteins mitigate air-water interface damage to fragile cryo-EM samples during plunge freezing.” Nature Communications (2024-09). https://doi.org/10.1038/s41467-024-52091-1 (abe2024smallleaproteinsa pages 2-3, abe2024smallleaproteinsa pages 4-5)
• Romero-Perez P.S. et al. “When Phased without Water: Biophysics of Cellular Desiccation, from Biomolecules to Condensates.” Chemical Reviews (2023-05). https://doi.org/10.1021/acs.chemrev.2c00659 (romeroperez2023whenphasedwithout pages 11-12, romeroperez2023whenphasedwithout pages 22-23)

References

1. (tanaka2015novelmitochondriatargetedheatsoluble pages 2-4): Sae Tanaka, Junko Tanaka, Yoshihiro Miwa, Daiki D. Horikawa, Toshiaki Katayama, Kazuharu Arakawa, Atsushi Toyoda, Takeo Kubo, and Takekazu Kunieda. Novel mitochondria-targeted heat-soluble proteins identified in the anhydrobiotic tardigrade improve osmotic tolerance of human cells. PLoS ONE, 10:e0118272, Feb 2015. URL: https://doi.org/10.1371/journal.pone.0118272, doi:10.1371/journal.pone.0118272. This article has 143 citations and is from a peer-reviewed journal.

2. (tanaka2015novelmitochondriatargetedheatsoluble pages 5-7): Sae Tanaka, Junko Tanaka, Yoshihiro Miwa, Daiki D. Horikawa, Toshiaki Katayama, Kazuharu Arakawa, Atsushi Toyoda, Takeo Kubo, and Takekazu Kunieda. Novel mitochondria-targeted heat-soluble proteins identified in the anhydrobiotic tardigrade improve osmotic tolerance of human cells. PLoS ONE, 10:e0118272, Feb 2015. URL: https://doi.org/10.1371/journal.pone.0118272, doi:10.1371/journal.pone.0118272. This article has 143 citations and is from a peer-reviewed journal.

3. (hand2018challengesduringdiapause pages 8-8): Steven C. Hand, Daniel S. Moore, and Yuvraj Patil. Challenges during diapause and anhydrobiosis: mitochondrial bioenergetics and desiccation tolerance. IUBMB Life, 70:1251-1259, Oct 2018. URL: https://doi.org/10.1002/iub.1953, doi:10.1002/iub.1953. This article has 28 citations and is from a peer-reviewed journal.

4. (romeroperez2023whenphasedwithout pages 22-23): Paulette Sofia Romero-Perez, Yanniv Dorone, Eduardo Flores, Shahar Sukenik, and Steven Boeynaems. When phased without water: biophysics of cellular desiccation, from biomolecules to condensates. Chemical Reviews, 123:9010-9035, May 2023. URL: https://doi.org/10.1021/acs.chemrev.2c00659, doi:10.1021/acs.chemrev.2c00659. This article has 75 citations and is from a highest quality peer-reviewed journal.

5. (romeroperez2023whenphasedwithout pages 11-12): Paulette Sofia Romero-Perez, Yanniv Dorone, Eduardo Flores, Shahar Sukenik, and Steven Boeynaems. When phased without water: biophysics of cellular desiccation, from biomolecules to condensates. Chemical Reviews, 123:9010-9035, May 2023. URL: https://doi.org/10.1021/acs.chemrev.2c00659, doi:10.1021/acs.chemrev.2c00659. This article has 75 citations and is from a highest quality peer-reviewed journal.

6. (yoshida2022decipheringthebiological pages 4-6): Yuki Yoshida and Sae Tanaka. Deciphering the biological enigma—genomic evolution underlying anhydrobiosis in the phylum tardigrada and the chironomid polypedilum vanderplanki. Insects, 13:557, Jun 2022. URL: https://doi.org/10.3390/insects13060557, doi:10.3390/insects13060557. This article has 10 citations.

7. (schill2019environmentaladaptationsdesiccation pages 10-13): Ralph O. Schill and Steffen Hengherr. Environmental adaptations: desiccation tolerance. ArXiv, pages 273-293, Jan 2019. URL: https://doi.org/10.1007/978-3-319-95702-9_10, doi:10.1007/978-3-319-95702-9_10. This article has 50 citations.

8. (tanaka2015novelmitochondriatargetedheatsoluble pages 4-5): Sae Tanaka, Junko Tanaka, Yoshihiro Miwa, Daiki D. Horikawa, Toshiaki Katayama, Kazuharu Arakawa, Atsushi Toyoda, Takeo Kubo, and Takekazu Kunieda. Novel mitochondria-targeted heat-soluble proteins identified in the anhydrobiotic tardigrade improve osmotic tolerance of human cells. PLoS ONE, 10:e0118272, Feb 2015. URL: https://doi.org/10.1371/journal.pone.0118272, doi:10.1371/journal.pone.0118272. This article has 143 citations and is from a peer-reviewed journal.

9. (tanaka2015novelmitochondriatargetedheatsoluble media 470ae241): Sae Tanaka, Junko Tanaka, Yoshihiro Miwa, Daiki D. Horikawa, Toshiaki Katayama, Kazuharu Arakawa, Atsushi Toyoda, Takeo Kubo, and Takekazu Kunieda. Novel mitochondria-targeted heat-soluble proteins identified in the anhydrobiotic tardigrade improve osmotic tolerance of human cells. PLoS ONE, 10:e0118272, Feb 2015. URL: https://doi.org/10.1371/journal.pone.0118272, doi:10.1371/journal.pone.0118272. This article has 143 citations and is from a peer-reviewed journal.

10. (tanaka2015novelmitochondriatargetedheatsoluble pages 10-11): Sae Tanaka, Junko Tanaka, Yoshihiro Miwa, Daiki D. Horikawa, Toshiaki Katayama, Kazuharu Arakawa, Atsushi Toyoda, Takeo Kubo, and Takekazu Kunieda. Novel mitochondria-targeted heat-soluble proteins identified in the anhydrobiotic tardigrade improve osmotic tolerance of human cells. PLoS ONE, 10:e0118272, Feb 2015. URL: https://doi.org/10.1371/journal.pone.0118272, doi:10.1371/journal.pone.0118272. This article has 143 citations and is from a peer-reviewed journal.

11. (tanaka2015novelmitochondriatargetedheatsoluble media 129a06d0): Sae Tanaka, Junko Tanaka, Yoshihiro Miwa, Daiki D. Horikawa, Toshiaki Katayama, Kazuharu Arakawa, Atsushi Toyoda, Takeo Kubo, and Takekazu Kunieda. Novel mitochondria-targeted heat-soluble proteins identified in the anhydrobiotic tardigrade improve osmotic tolerance of human cells. PLoS ONE, 10:e0118272, Feb 2015. URL: https://doi.org/10.1371/journal.pone.0118272, doi:10.1371/journal.pone.0118272. This article has 143 citations and is from a peer-reviewed journal.

12. (abe2024smallleaproteinsa pages 2-3): Kaitlyn M. Abe, Gan Li, Qixiang He, Timothy Grant, and Ci Ji Lim. Small lea proteins mitigate air-water interface damage to fragile cryo-em samples during plunge freezing. Nature Communications, Sep 2024. URL: https://doi.org/10.1038/s41467-024-52091-1, doi:10.1038/s41467-024-52091-1. This article has 17 citations and is from a highest quality peer-reviewed journal.

13. (abe2024smallleaproteinsa pages 4-5): Kaitlyn M. Abe, Gan Li, Qixiang He, Timothy Grant, and Ci Ji Lim. Small lea proteins mitigate air-water interface damage to fragile cryo-em samples during plunge freezing. Nature Communications, Sep 2024. URL: https://doi.org/10.1038/s41467-024-52091-1, doi:10.1038/s41467-024-52091-1. This article has 17 citations and is from a highest quality peer-reviewed journal.

14. (abe2024smallleaproteinsa pages 5-6): Kaitlyn M. Abe, Gan Li, Qixiang He, Timothy Grant, and Ci Ji Lim. Small lea proteins mitigate air-water interface damage to fragile cryo-em samples during plunge freezing. Nature Communications, Sep 2024. URL: https://doi.org/10.1038/s41467-024-52091-1, doi:10.1038/s41467-024-52091-1. This article has 17 citations and is from a highest quality peer-reviewed journal.

15. (abe2024smallleaproteinsa pages 3-4): Kaitlyn M. Abe, Gan Li, Qixiang He, Timothy Grant, and Ci Ji Lim. Small lea proteins mitigate air-water interface damage to fragile cryo-em samples during plunge freezing. Nature Communications, Sep 2024. URL: https://doi.org/10.1038/s41467-024-52091-1, doi:10.1038/s41467-024-52091-1. This article has 17 citations and is from a highest quality peer-reviewed journal.

Citations

1. tanaka2015novelmitochondriatargetedheatsoluble pages 2-4
2. hand2018challengesduringdiapause pages 8-8
3. schill2019environmentaladaptationsdesiccation pages 10-13
4. tanaka2015novelmitochondriatargetedheatsoluble pages 4-5
5. tanaka2015novelmitochondriatargetedheatsoluble pages 5-7
6. romeroperez2023whenphasedwithout pages 22-23
7. tanaka2015novelmitochondriatargetedheatsoluble pages 10-11
8. abe2024smallleaproteinsa pages 2-3
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10. yoshida2022decipheringthebiological pages 4-6
11. romeroperez2023whenphasedwithout pages 11-12
12. abe2024smallleaproteinsa pages 5-6
13. abe2024smallleaproteinsa pages 3-4
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