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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.

Comprehensive Research Report: Arabidopsis thaliana HSP17.6A (At1g59860; UniProt Q9XIE3)

Executive summary

HSP17.6A (At1g59860; UniProt Q9XIE3; also referenced as AtHsp17.6A-CI) encodes a 17.6 kDa class I cytosolic small heat shock protein (sHSP/HSP20 family) characterized by an α-crystallin domain and ATP-independent “holdase” chaperone activity. The protein is part of a plant-expanded, highly redundant cytosolic sHSP set that is transcriptionally induced by canonical heat shock factor (HSF) pathways and is regulated in broader stress and developmental contexts. Current evidence supports predominant action in cytosolic proteostasis during heat stress, with distribution between cytosol and nucleus and possible roles in stress acclimation; direct single-gene loss-of-function phenotypes are expected to be subtle due to redundancy. Quantitatively, At1g59860 is strongly HSF-dependent (log2FC 4.24 under HsfA1d overexpression; fold change −9 in an HsfA1 triple knockout), and HSP17.6A expression is modulated by miRNA160/ARF regulatory circuitry during heat stress. (higashi2013hsfa1daprotein pages 5-7, eisenhardt2013smallheatshock pages 1-2, eisenhardt2013smallheatshock pages 2-4, eisenhardt2013smallheatshock pages 4-6, lin2018microrna160modulatesplant pages 1-2, lin2018microrna160modulatesplant pages 12-14)

1. Gene/protein identity verification (critical disambiguation)

Target identity confirmed. A peer-reviewed review explicitly lists AtHsp17.6A-CI from Arabidopsis thaliana with UniProt Q9XIE3, length ~155 aa, mass ~17.6 kDa, and localization annotation c/n (cytosol/nucleus). This matches the user-provided UniProt record and supports that the intended protein is a class I cytosolic sHSP rather than organellar (chloroplast/mitochondrial/ER/peroxisomal) sHSPs. (Eisenhardt, 2013-12; https://doi.org/10.1515/bmc-2013-0028) (eisenhardt2013smallheatshock pages 4-6)

Ambiguity and paralogs. The same review highlights that plants contain multiple highly similar cytosolic sHSPs in the same compartment and lists closely related AtHsp17.6B-CI and AtHsp17.6C-CI alongside AtHsp17.6A-CI, emphasizing that paralogy complicates assigning unique in vivo functions to a single gene. (Eisenhardt, 2013-12; https://doi.org/10.1515/bmc-2013-0028) (eisenhardt2013smallheatshock pages 2-4, eisenhardt2013smallheatshock pages 4-6)

2. Key concepts and definitions (current understanding)

2.1 What are small heat shock proteins (sHSPs/HSP20)?

Small heat shock proteins are α-crystallin domain (ACD)-type chaperones. They bind non-native (unfolded or partially unfolded) client proteins in an ATP-independent manner, keeping clients soluble so that other ATP-dependent systems (e.g., HSP70/HSP100) can later refold them. Because they do not actively refold proteins themselves, sHSPs are described as “holdases.” (Eisenhardt, 2013-12; https://doi.org/10.1515/bmc-2013-0028) (eisenhardt2013smallheatshock pages 1-2)

Domain architecture. A defining feature is a conserved ACD (~80–100 residues) flanked by a variable N-terminal region and a short C-terminal extension; the N-terminus is often implicated in substrate binding and in the structural plasticity that makes full-length sHSPs challenging to crystallize. (Eisenhardt, 2013-12; https://doi.org/10.1515/bmc-2013-0028) (eisenhardt2013smallheatshock pages 1-2, eisenhardt2013smallheatshock pages 4-6)

2.2 Oligomerization and mechanism

ACD-type sHSPs form large oligomers (reported in the review as commonly ~150–800 kDa), and these oligomers are dynamic and can rearrange with temperature or other conditions. In many cases dimers serve as basic structural subunits that assemble into higher-order oligomers (e.g., 12-, 24-, 36-mers). This dynamic oligomerization underpins their holdase function and stress responsiveness. (Eisenhardt, 2013-12; https://doi.org/10.1515/bmc-2013-0028) (eisenhardt2013smallheatshock pages 4-6)

2.3 Cytosolic class I sHSPs in plants and nuclear distribution

Plants are unusual in having many closely related sHSP paralogs in the same compartment, particularly in the cytosol. Although cytosolic sHSPs often lack canonical nuclear localization signals, experimental studies (summarized by Eisenhardt) indicate they can be distributed between cytoplasm and nucleus, with functional significance of nuclear pools not fully resolved. (Eisenhardt, 2013-12; https://doi.org/10.1515/bmc-2013-0028) (eisenhardt2013smallheatshock pages 2-4)

3. HSP17.6A: functional annotation (gene-specific where possible)

3.1 Primary molecular function

Likely primary function: ATP-independent molecular chaperone/holdase contributing to proteostasis under conditions that increase protein misfolding (especially heat stress). This is inferred from its family membership, ACD-type architecture, and class I cytosolic identity, all of which are strongly linked to holdase chaperone activity in the reviewed literature. (Eisenhardt, 2013-12; https://doi.org/10.1515/bmc-2013-0028) (eisenhardt2013smallheatshock pages 1-2, eisenhardt2013smallheatshock pages 4-6)

Not an enzyme/transporter. No evidence in the retrieved texts indicates catalytic activity or substrate transport; its functional substrate is best described as misfolded/non-native proteins (client proteins) under stress conditions. (eisenhardt2013smallheatshock pages 1-2)

3.2 Subcellular localization

Cytosol/nucleus annotation. AtHsp17.6A-CI (Q9XIE3) is annotated as c/n in a curated sHSP overview table, consistent with cytosolic class I sHSP behavior in plants. (Eisenhardt, 2013-12; https://doi.org/10.1515/bmc-2013-0028) (eisenhardt2013smallheatshock pages 4-6)

Implication: HSP17.6A is expected to operate primarily in cytosolic proteostasis, with potential nuclear presence during heat stress or recovery phases, consistent with broader reports that cytosolic sHSPs partition between compartments. (eisenhardt2013smallheatshock pages 2-4, eisenhardt2013smallheatshock pages 4-6)

3.3 Regulation: heat shock transcription factors and promoter HSEs

A key quantitative dataset directly implicates HSF-A1 regulon control:

• In a study of Thellungiella/Arabidopsis HsfA1d, AT1G59860 (HSP17.6A-CI) is among genes upregulated by TsHsfA1d overexpression, with log2(fold change) = 4.24 relative to WT.
• In contrast, in an athsfa1a/b/d triple knockout, AT1G59860 shows a reported fold change of −9 relative to WT in the same table.
• The gene is marked with a “Perfect HSE” indicator in the table, consistent with direct HSF binding sites in its promoter.

These observations support that HSP17.6A is a canonical heat shock response gene under strong positive control by HsfA1 family activity. (Higashi et al., 2013-03; https://doi.org/10.1093/mp/sst024) (higashi2013hsfa1daprotein pages 5-7)

3.4 Regulation: RNA-based circuitry (miR160/ARF module)

A 2018 study reports that heat stress increases miR160 and that manipulating the miR160 pathway affects thermotolerance-associated phenotypes (seed germination, survival, hypocotyl elongation), accompanied by changes in HSP gene expression including HSP17.6A:

• The authors report that transcriptome and qRT-PCR analyses show HSP17.6A (along with HSP17.6II, HSP21, and HSP70B) is regulated by heat across genetic backgrounds (miR160 overexpression 160OE; miR160 inhibition MIM160; arf mutants). (Lin et al., 2018-02-01; https://doi.org/10.3389/fpls.2018.00068) (lin2018microrna160modulatesplant pages 1-2)
• They further state that miR160 overexpression enhanced HSP17.6A expression under heat stress, while reduction of miR160 decreased HSP17.6A (and other HSPs). (Lin et al., 2018-02-01; https://doi.org/10.3389/fpls.2018.00068) (lin2018microrna160modulatesplant pages 12-14)

Interpretation: HSP17.6A is embedded not only in the canonical HSF transcriptional network, but also in broader regulatory circuits involving developmental regulators (ARFs) and miRNA-mediated stress responses, consistent with multilayer control of heat tolerance traits. (lin2018microrna160modulatesplant pages 1-2, lin2018microrna160modulatesplant pages 12-14)

4. Phenotypes and functional evidence

4.1 Heat tolerance: indirect evidence through regulatory activation

In the HsfA1d study, Arabidopsis lines overexpressing AtHsfA1d show markedly greater heat tolerance than WT after 42°C for 80 min followed by recovery at 22°C for 10 days; these lines also show higher expression of “Hsp17” in expression profiling, linking increased HSP17-family expression (including class I small HSPs) to improved thermotolerance. (Higashi et al., 2013-03; https://doi.org/10.1093/mp/sst024) (higashi2013hsfa1daprotein pages 5-7)

This is not a single-gene HSP17.6A perturbation, but it provides experimentally grounded support that increasing the HSF→HSP17 axis can improve thermotolerance, and AT1G59860 is one quantified member of that axis. (higashi2013hsfa1daprotein pages 5-7)

4.2 Osmotolerance: direct overexpression claim (secondary-cited)

A 2014 peer-reviewed article explicitly cites earlier work stating: “At-HSP17.6A… can enhance osmotolerance upon overexpression.” This supports practical relevance of manipulating HSP17.6A expression for abiotic stress tolerance, but the primary study (Sun et al., 2001) full text was not retrievable in the current tool context, so the quantitative strength and experimental design cannot be assessed here. (Reddy et al., 2014-03; https://doi.org/10.1371/journal.pone.0089125) (reddy2014unravelingregulationof pages 16-16)

4.3 Redundancy and expected subtle knockout phenotypes

A thesis source discussing Arabidopsis class I sHSPs notes that knockout phenotypes can be weak, consistent with extensive redundancy among closely related sHSP paralogs. It also describes HSP17.6 and HSP17.6A as genetic duplicates and highlights that paralogs differ mainly in the N-terminal region, which is functionally important for chaperone activity. While this is not a peer-reviewed primary research article, it aligns with the paralog redundancy perspective emphasized in the 2013 review. (Ramsay, 2014) (ramsay2014studiesonan pages 220-225)

5. Pathways and biological processes

5.1 Heat shock response (HSR) pathway

HSP17.6A participates in the heat shock response as an HSF-regulated HSP gene with heat shock elements in its promoter and strong dependency on HsfA1 activity (quantitative transcript upregulation under HsfA1d overexpression and downregulation under HsfA1 triple knockout). (Higashi et al., 2013-03; https://doi.org/10.1093/mp/sst024) (higashi2013hsfa1daprotein pages 5-7)

5.2 Proteostasis and aggregation management

The family-level mechanism indicates HSP17.6A most plausibly contributes to proteostasis by binding unfolding proteins and preventing aggregation during stress, acting upstream of ATP-dependent refolding systems. In plants, such chaperone networks are considered key components of stress survival and recovery. (Eisenhardt, 2013-12; https://doi.org/10.1515/bmc-2013-0028) (eisenhardt2013smallheatshock pages 1-2)

6. Recent developments (prioritizing 2023–2024)

6.1 2023 community-scale proteomics resource: Arabidopsis PeptideAtlas build 2023–10

A major 2023/2024 resource update provides a broad experimental framework for protein-level support and PTM mapping in Arabidopsis:

• The 2023 PeptideAtlas build (published online 2023-11-21) matched ~70 million MS/MS spectra to Araport11 and identified 18,267 proteins at the highest confidence level, representing 78.6% of the predicted proteome.
• The release maps multiple PTM categories, including 5198 phosphorylated proteins, 668 ubiquitinated proteins, 3050 N-terminally acetylated proteins, and 864 lysine-acetylated proteins.

While this paper does not in the provided snippet confirm HSP17.6A specifically, it is a key enabling resource for validating protein accumulation and modifications for genes like HSP17.6A under diverse conditions and tissues. (van Wijk et al., 2023-11-21; https://doi.org/10.1021/acs.jproteome.3c00536) (wijk2023detectionofthe pages 1-2)

6.2 2024 heat stress nuclear proteomics kinetics study (Arabidopsis)

A 2024 study in Scientific Reports performs quantitative LC–MS/MS of nuclear proteomes at 22°C, after heat stress at 37°C for 4 h and 24 h, and during recovery, defining multiple kinetic clusters (“Early”, “Late”, “Transient”, etc.). The retrieved text chunks did not include the detailed gene-level paragraph for HSP17.6A, but the search metadata indicated that HSP17.6A (At1g59860) is mentioned in the work, implying continued interest in mapping heat-stress-responsive nuclear proteome components that may include cytosol/nucleus-distributed sHSPs. (Sáez-Vásquez et al., 2024-08; https://doi.org/10.1038/s41598-024-65558-4) (saezvasquez2024proteomicprofilingofa pages 13-14, saezvasquez2024proteomicprofilingofa pages 12-13)

7. Current applications and real-world implementations

7.1 Trait engineering and molecular markers

Within the available evidence base, the most direct application claim for HSP17.6A is enhanced osmotolerance upon overexpression (cited secondary). This supports its candidacy as a genetic engineering target for abiotic stress tolerance—particularly osmotic and potentially heat stress—though validation and trade-off analysis require the original overexpression study details. (Reddy et al., 2014-03; https://doi.org/10.1371/journal.pone.0089125) (reddy2014unravelingregulationof pages 16-16)

7.2 Thermotolerance improvement via upstream regulators

HsfA1d overexpression improves heat tolerance and increases Hsp17 expression levels, suggesting a practical strategy where manipulating regulators of HSP17.6A (HSFs) can elevate the chaperone network and yield thermotolerance phenotypes. This approach is already used as a conceptual route in plant stress biology and biotechnology studies of heat tolerance. (Higashi et al., 2013-03; https://doi.org/10.1093/mp/sst024) (higashi2013hsfa1daprotein pages 5-7)

8. Expert opinions and authoritative synthesis

A key expert-level synthesis emphasizes that while sHSPs are clearly beneficial in preventing aggregation under stress, plants’ multiplicity of highly similar sHSPs in the same compartment makes it challenging to define the in vivo relevance of each single paralog, supporting cautious interpretation of single-gene annotations and phenotypes without gene-specific perturbation data. (Eisenhardt, 2013-12; https://doi.org/10.1515/bmc-2013-0028) (eisenhardt2013smallheatshock pages 1-2, eisenhardt2013smallheatshock pages 2-4)

9. Quantitative statistics and data (from retrieved sources)

• AT1G59860 (HSP17.6A-CI): log2 fold change 4.24 in TsHsfA1d overexpression vs WT; fold change −9 in athsfa1a/b/d triple knockout vs WT; gene marked with perfect HSE in promoter annotation (Table 2). (Higashi et al., 2013-03; https://doi.org/10.1093/mp/sst024) (higashi2013hsfa1daprotein pages 5-7)
• PeptideAtlas 2023–10: 18,267 high-confidence proteins; 78.6% predicted proteome coverage; PTM counts: 5198 phosphorylated, 668 ubiquitinated, 3050 N-terminal acetylated, 864 lysine-acetylated proteins. (van Wijk et al., 2023-11-21; https://doi.org/10.1021/acs.jproteome.3c00536) (wijk2023detectionofthe pages 1-2)

10. Evidence summary table

The following table compiles the main annotation-relevant claims with publication dates and URLs.

Table: This table compiles the most directly supported evidence found for Arabidopsis HSP17.6A (At1g59860; UniProt Q9XIE3), covering identity, mechanism, regulation, localization, functional evidence, and recent proteomics updates. It is useful as a compact annotation aid because each claim is tied to a specific source, date, URL, and context ID.

11. Limitations of the current evidence retrieval

• The primary paper most directly asserting At-HSP17.6A overexpression enhances osmotolerance (Sun et al., 2001) was not accessible in the retrieved full-text corpus; therefore, the experimental design and effect sizes cannot be verified here beyond the secondary citation. (reddy2014unravelingregulationof pages 16-16)
• The 2024 nuclear proteomics study was retrieved, but the available text chunks did not include the specific sentence(s) about HSP17.6A/At1g59860 needed to extract detailed kinetic cluster membership or abundance trajectories. (saezvasquez2024proteomicprofilingofa pages 13-14)
• Direct biochemical assays of AtHsp17.6A client proteins, interactors, and high-resolution localization experiments were not present in the retrieved primary literature set; the most robust mechanistic detail is therefore at the family level (sHSP/ACD holdase model). (eisenhardt2013smallheatshock pages 1-2, eisenhardt2013smallheatshock pages 4-6)

12. Functional annotation statement (recommended)

HSP17.6A (At1g59860; UniProt Q9XIE3) encodes a class I cytosolic small heat shock protein (ACD-type sHSP/HSP20) that acts as an ATP-independent holdase chaperone, binding non-native proteins to prevent aggregation under heat and other stresses. It is HSF-regulated with strong HsfA1 dependence and is additionally modulated by RNA-based regulatory pathways (miR160/ARF). The protein is annotated to localize to cytosol and nucleus, and gene-level phenotypes may be masked by redundancy with other cytosolic sHSP paralogs. (higashi2013hsfa1daprotein pages 5-7, eisenhardt2013smallheatshock pages 1-2, eisenhardt2013smallheatshock pages 2-4, eisenhardt2013smallheatshock pages 4-6, lin2018microrna160modulatesplant pages 1-2, lin2018microrna160modulatesplant pages 12-14)

References

1. (higashi2013hsfa1daprotein pages 5-7): Yukari Higashi, Naohiko Ohama, Tomoko Ishikawa, Taku Katori, Ayaka Shimura, Kazuya Kusakabe, Kazuko Yamaguchi-Shinozaki, Junko Ishida, Maho Tanaka, Motoaki Seki, Kazuo Shinozaki, Yoichi Sakata, Takahisa Hayashi, and Teruaki Taji. Hsfa1d, a protein identified via fox hunting using thellungiella salsuginea cdnas improves heat tolerance by regulating heat-stress-responsive gene expression. Molecular plant, 6 2:411-22, Mar 2013. URL: https://doi.org/10.1093/mp/sst024, doi:10.1093/mp/sst024. This article has 65 citations and is from a highest quality peer-reviewed journal.

2. (eisenhardt2013smallheatshock pages 1-2): Benjamin Dennis Eisenhardt. Small heat shock proteins: recent developments. BioMolecular Concepts, 4:583-595, Dec 2013. URL: https://doi.org/10.1515/bmc-2013-0028, doi:10.1515/bmc-2013-0028. This article has 23 citations and is from a peer-reviewed journal.

3. (eisenhardt2013smallheatshock pages 2-4): Benjamin Dennis Eisenhardt. Small heat shock proteins: recent developments. BioMolecular Concepts, 4:583-595, Dec 2013. URL: https://doi.org/10.1515/bmc-2013-0028, doi:10.1515/bmc-2013-0028. This article has 23 citations and is from a peer-reviewed journal.

4. (eisenhardt2013smallheatshock pages 4-6): Benjamin Dennis Eisenhardt. Small heat shock proteins: recent developments. BioMolecular Concepts, 4:583-595, Dec 2013. URL: https://doi.org/10.1515/bmc-2013-0028, doi:10.1515/bmc-2013-0028. This article has 23 citations and is from a peer-reviewed journal.

5. (lin2018microrna160modulatesplant pages 1-2): Jeng-Shane Lin, Chia-Chia Kuo, I-Chu Yang, Wei-An Tsai, Yu-Hsing Shen, Chih-Ching Lin, Yi-Chen Liang, Yu-Chi Li, Yun-Wei Kuo, Yu-Chi King, Hsi-Mei Lai, and Shih-Tong Jeng. Microrna160 modulates plant development and heat shock protein gene expression to mediate heat tolerance in arabidopsis. Frontiers in Plant Science, Feb 2018. URL: https://doi.org/10.3389/fpls.2018.00068, doi:10.3389/fpls.2018.00068. This article has 170 citations.

6. (lin2018microrna160modulatesplant pages 12-14): Jeng-Shane Lin, Chia-Chia Kuo, I-Chu Yang, Wei-An Tsai, Yu-Hsing Shen, Chih-Ching Lin, Yi-Chen Liang, Yu-Chi Li, Yun-Wei Kuo, Yu-Chi King, Hsi-Mei Lai, and Shih-Tong Jeng. Microrna160 modulates plant development and heat shock protein gene expression to mediate heat tolerance in arabidopsis. Frontiers in Plant Science, Feb 2018. URL: https://doi.org/10.3389/fpls.2018.00068, doi:10.3389/fpls.2018.00068. This article has 170 citations.

7. (reddy2014unravelingregulationof pages 16-16): Palakolanu Sudhakar Reddy, Polavarapu B. Kavi Kishor, Christiane Seiler, Markus Kuhlmann, Lennart Eschen-Lippold, Justin Lee, Malireddy K. Reddy, and Nese Sreenivasulu. Unraveling regulation of the small heat shock proteins by the heat shock factor hvhsfb2c in barley: its implications in drought stress response and seed development. PLoS ONE, 9:e89125, Mar 2014. URL: https://doi.org/10.1371/journal.pone.0089125, doi:10.1371/journal.pone.0089125. This article has 117 citations and is from a peer-reviewed journal.

8. (ramsay2014studiesonan pages 220-225): SW Ramsay. Studies on an arabidopsis myb transcription factor involved in heat and salt tolerance. Unknown journal, 2014.

9. (wijk2023detectionofthe pages 1-2): Klaas J. van Wijk, Tami Leppert, Zhi Sun, Alyssa Kearly, Margaret Li, Luis Mendoza, Isabell Guzchenko, Erica Debley, Georgia Sauermann, Pratyush Routray, Sagunya Malhotra, Andrew Nelson, Qi Sun, and Eric W. Deutsch. Detection of the arabidopsis proteome and its post-translational modifications and the nature of the unobserved (dark) proteome in peptideatlas. Journal of proteome research, 23:185-214, Nov 2023. URL: https://doi.org/10.1021/acs.jproteome.3c00536, doi:10.1021/acs.jproteome.3c00536. This article has 31 citations and is from a peer-reviewed journal.

10. (saezvasquez2024proteomicprofilingofa pages 13-14): Julio Saez-Vasquez, Eduardo Muñoz-Diaz, Isabel Fuenzalida-Valdivia, Tommy Darriere, DeBures Anne, Francisca Blanco-Herrera, Magali Rompais, and Christine Carapito. Proteomic profiling of arabidopsis nuclei reveals distinct protein accumulation kinetics upon heat stress. Scientific Reports, Aug 2024. URL: https://doi.org/10.1038/s41598-024-65558-4, doi:10.1038/s41598-024-65558-4. This article has 7 citations and is from a peer-reviewed journal.

11. (saezvasquez2024proteomicprofilingofa pages 12-13): Julio Saez-Vasquez, Eduardo Muñoz-Diaz, Isabel Fuenzalida-Valdivia, Tommy Darriere, DeBures Anne, Francisca Blanco-Herrera, Magali Rompais, and Christine Carapito. Proteomic profiling of arabidopsis nuclei reveals distinct protein accumulation kinetics upon heat stress. Scientific Reports, Aug 2024. URL: https://doi.org/10.1038/s41598-024-65558-4, doi:10.1038/s41598-024-65558-4. This article has 7 citations and is from a peer-reviewed journal.

Artifacts

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Citations

1. eisenhardt2013smallheatshock pages 4-6
2. eisenhardt2013smallheatshock pages 1-2
3. eisenhardt2013smallheatshock pages 2-4
4. reddy2014unravelingregulationof pages 16-16
5. ramsay2014studiesonan pages 220-225
6. wijk2023detectionofthe pages 1-2
7. saezvasquez2024proteomicprofilingofa pages 13-14
8. saezvasquez2024proteomicprofilingofa pages 12-13
9. https://doi.org/10.1515/bmc-2013-0028
10. https://doi.org/10.1093/mp/sst024
11. https://doi.org/10.3389/fpls.2018.00068
12. https://doi.org/10.1371/journal.pone.0089125
13. https://doi.org/10.1021/acs.jproteome.3c00536
14. https://doi.org/10.1038/s41598-024-65558-4
15. https://doi.org/10.1093/mp/sst024,
16. https://doi.org/10.1515/bmc-2013-0028,
17. https://doi.org/10.3389/fpls.2018.00068,
18. https://doi.org/10.1371/journal.pone.0089125,
19. https://doi.org/10.1021/acs.jproteome.3c00536,
20. https://doi.org/10.1038/s41598-024-65558-4,