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Human GEMIN5 (UniProt Q8TEQ6): Functional Annotation Research Report

Executive summary

Identity is verified. The requested target is human GEMIN5, also called Gem-associated protein 5 or gem nuclear organelle-associated protein 5, corresponding to human gene ENSG00000082516 and the supplied UniProt accession Q8TEQ6. The literature consistently describes this protein as a large, predominantly cytoplasmic, multidomain RNA-binding component of the survival motor neuron (SMN) complex. No conflicting same-symbol protein was encountered. Its experimentally established tandem N-terminal WD40 β-propellers, central TPR-like oligomerization module, and C-terminal noncanonical RNA-binding region agree with the supplied WD-repeat Gemin-5 family and InterPro β-propeller/GEMIN5-RBS annotations (OpenTargets Search: -GEMIN5, jin2016structuralbasisfor pages 1-2, martinezsalas2020emergingrolesof pages 3-5, guo2022structuralbasisfor pages 7-8).

GEMIN5 is not an enzyme or transporter. Its primary biochemical role is that of an RNA-substrate receptor and ribonucleoprotein-assembly adaptor: it recognizes appropriate precursor small nuclear RNAs (pre-snRNAs), principally through the Sm-site region and cap-associated features, and delivers them to the SMN complex for Sm-core assembly. It also acts independently of the SMN complex as a ribosome-associated regulator that changes global translation and selectively promotes or represses translation according to mRNA structure and context (franciscovelilla2018thelandscapeof pages 13-14, jin2016structuralbasisfor pages 1-2, martinezsalas2020emergingrolesof pages 3-5).

1. Protein organization and correspondence to the supplied domain annotations

Table: Domain-resolved functional annotation of human GEMIN5 (UniProt Q8TEQ6), separating pre-snRNA selection and SMN-complex delivery from ribosome association and selective mRNA translation. Residue boundaries are approximate because experimental constructs and annotation schemes differ among studies.

The N-terminal half contains two juxtaposed seven-bladed WD40 β-propellers forming a rigid RNA-recognition surface. Structural studies found that aromatic residues stack with bases in the Sm-site RNA, while arginine-mediated hydrogen bonds contribute specificity. An adenine immediately 5′ of the Sm site is important for efficient recognition; studies differ somewhat on the contribution of the adjacent 3′ stem-loop, indicating that GEMIN5 reads a composite sequence-and-structure code rather than a single invariant short sequence (jin2016structuralbasisfor pages 1-2).

The middle region, experimentally mapped approximately to residues 807–1097, is an α-helical TPR-like module. SEC–MALS measured an approximately 64-kDa species for a construct whose monomer is approximately 32 kDa, establishing stable homodimerization. Crystal structures at 2.0–2.7 Å showed a canoe-shaped dimer composed of elongated α-solenoids. The A951E substitution disrupted dimerization, endogenous GEMIN5 recruitment, and translation-related activity, demonstrating that this region is an interaction hub rather than merely a spacer (morenomorcillo2020structuralbasisfor pages 3-4, morenomorcillo2020structuralbasisfor pages 4-5, morenomorcillo2020structuralbasisfor pages 10-11).

The C-terminal region contains overlapping noncanonical RNA-binding elements, usually termed RBS1 and RBS2. A 2022 cryo-EM analysis of residues 841–1508 found an all-α-helical homodecamer organized as a dimer of pentamers. Disrupting hydrophobic pentamer interfaces impaired both higher-order assembly and binding to the structured SL1 RNA. The data support coordinated RNA recognition by adjacent protomers and explain GEMIN5’s preference for extended stem-loop substrates. Structural models and maps are available as PDB 7XDT/7XGR and EMDB EMD-33152/EMD-33187 (published September 2022; https://doi.org/10.1038/s41467-022-32883-z) (guo2022structuralbasisfor pages 7-8, guo2022structuralbasisfor pages 8-9).

2. Primary molecular function: pre-snRNA selection and snRNP assembly

GEMIN5’s most firmly established primary role is to identify Sm-class pre-snRNAs and hand them to the SMN complex. The relevant RNA substrates are spliceosomal snRNA precursors bearing the U-rich Sm-site or “snRNP code,” with recognition additionally influenced by nearby nucleotides, RNA conformation, and the m7G cap. This substrate-selection step prevents indiscriminate Sm-protein assembly on unrelated RNAs (fortuna2023smnregulatesgemin5 pages 16-18, jin2016structuralbasisfor pages 1-2, martinezsalas2020emergingrolesof pages 3-5).

Mechanistically, the pathway is:

1. Sm proteins are initially organized by the PRMT5–pICln machinery.
2. GEMIN5 binds an appropriate pre-snRNA using its tandem WD40 domains.
3. GEMIN5 delivers the RNA to the SMN–Gemins complex, interacting with SMN and GEMIN2.
4. The complex assembles the Sm ring around the snRNA Sm site, producing the core snRNP required for spliceosome maturation.
5. Subsequent RNA remodeling and maturation involve other SMN-complex factors and nuclear Cajal-body-associated steps (fortuna2023smnregulatesgemin5 pages 1-3, martinezsalas2020emergingrolesof pages 3-5, martinezsalas2020emergingrolesof pages 1-3).

Recent work refines rather than replaces this model. A 2023 study showed that compact structures in human pre-snRNAs can occlude the Sm site and that the SMN-complex helicase Gemin3 drives remodeling needed to expose it. GEMIN5 therefore provides substrate capture/selection, whereas other complex members help remodel and assemble the selected RNA (Nature Communications, October 2023; https://doi.org/10.1038/s41467-023-42324-0).

Because mature Sm-class snRNPs are core spliceosomal components, GEMIN5 loss can produce downstream alternative-splicing abnormalities. Nevertheless, GEMIN5 should not be annotated as a spliceosomal catalytic factor: its precise upstream function is snRNA recognition and RNP-assembly chaperoning.

3. Ribosome binding and translation regulation

GEMIN5 also has an experimentally separable, SMN-complex-independent role in protein synthesis. Its N-terminal region binds native ribosomes and ribosomal proteins L3/L4 and occurs in polysome fractions. Mutations affecting the relevant N-terminal surface impair ribosome association. Depletion and overexpression produce opposite changes in global protein synthesis, supporting a role in translation regulation, possibly including elongation-level control (franciscovelilla2018thelandscapeof pages 13-14).

The protein’s effect is not uniformly repressive. Its outcome depends on the RNA target and oligomeric context:

• The C-terminal RBS1 region binds a structured H12/SL1 element within GEMIN5 mRNA and stimulates its translation. Destabilizing this stem-loop removes the stimulatory effect, forming an autoregulatory feedback circuit that maintains GEMIN5 abundance (franciscovelilla2018thelandscapeof pages 13-14).
• GEMIN5 promotes polysome association and translation of selected transcripts bearing 5′ terminal oligopyrimidine tracts, particularly ribosomal-protein mRNAs, and transcripts bearing the histone 3′ stem-loop. RIP, reporter, motif-disruption, and polysome analyses support direct, cis-element-dependent regulation (Embarc-Buh et al., Cellular and Molecular Life Sciences 79:490, 2022; https://doi.org/10.1007/s00018-022-04519-4) (martinez‐salas2025understandinggemin5interactions pages 14-15).
• Its C-terminal region also recognizes viral internal ribosome-entry-site RNAs. Different intact or proteolytically generated GEMIN5 fragments can repress or stimulate IRES-dependent translation, emphasizing that isolated-fragment behavior should not automatically be equated with the full-length protein’s physiological activity (pineiro2015gemin5amultitasking pages 1-4, martinezsalas2020emergingrolesof pages 3-5).

A key 2024 result was that native-ribosome association and negative translation regulation require both the WD40 region and oligomerization-competent TPR module. By contrast, loss of oligomerization did not eliminate the protein’s predominantly cytoplasmic distribution. Thus, oligomerization regulates functional complex formation rather than serving primarily as a localization signal (Cell Death Discovery, June 2024; https://doi.org/10.1038/s41420-024-02057-5) (franciscovelilla2024oligomerizationregulatesthe pages 12-13, martinez‐salas2025understandinggemin5interactions pages 14-15).

4. Cellular localization

Full-length GEMIN5 is predominantly cytoplasmic, consistent with the cytoplasmic phase of Sm-class snRNP assembly and with its ribosome/polysome functions. Reported cytoplasmic pools include SMN-related assembly compartments or U bodies, soluble mRNPs, ribosomal and polysomal fractions, and stress granules after arsenite or heat stress (pineiro2015gemin5amultitasking pages 1-4, martinezsalas2020emergingrolesof pages 3-5).

A smaller nuclear pool can colocalize with SMN in gems/Gemini of Cajal bodies, linked to later snRNP maturation and recycling. It is therefore misleading to infer from the historical term “gem-associated” that GEMIN5 is principally nuclear. Current evidence instead supports dynamic partitioning, with most functional protein in the cytoplasm and smaller regulated nuclear or stress-associated pools (pineiro2015gemin5amultitasking pages 1-4, martinezsalas2020emergingrolesof pages 1-3, franciscovelilla2024oligomerizationregulatesthe pages 12-13).

5. Recent developments, 2023–2024

SMN–GEMIN5 interdependence

Fortuna et al. showed that SMN abundance regulates GEMIN5 transcript level, protein stability, and disease phenotypes. SMA patient-derived motor neurons with greater than 75% loss of SMN had reduced GEMIN5. GEMIN5-mutant neurons showed approximately 70–80% reduction of GEMIN5; increasing SMN by lentiviral expression or splice-correcting antisense treatment raised GEMIN5 and partially restored snRNP-related defects (Acta Neuropathologica, June 2023; https://doi.org/10.1007/s00401-023-02607-8) (fortuna2023smnregulatesgemin5 pages 16-18, fortuna2023smnregulatesgemin5 pages 11-13).

In one quantitative experiment, 500 nM Nusinersen/ASO N1 reduced SMN2 exon-7 skipping from approximately 50% to 25%, raised SMN2 mRNA by approximately 25%, and raised GEMIN5 mRNA by approximately 25%. Cycloheximide-chase experiments indicated increased GEMIN5 stability for at least eight hours after SMN enhancement. These findings identify SMN as a biological modifier of GEMIN5 insufficiency, but they do not establish Nusinersen as a clinically validated treatment for GEMIN5-associated disease (fortuna2023smnregulatesgemin5 pages 11-13).

Oligomerization as a functional switch

The 2024 oligomerization study found that oligomerization-proficient regions preferentially recruited proteins associated with ribosomes, splicing, translation regulation, the SMN complex, and RNA stability. Binding of most tested SMN-complex partners—including SMN, GEMIN2, and GEMIN4—depended on the dimerization module, while ribosome-dependent translation repression required cooperation between that module and the WD40 region (franciscovelilla2024oligomerizationregulatesthe pages 12-13).

Coupling altered splicing to translation

A 2024 RNA Biology study reported that GEMIN5 upregulation changed steady-state mRNA profiles and increased alternative-splicing events; RNA-seq of polysome-associated RNA showed that a substantial subset of these alternatively spliced mRNAs entered translating polysomes. Exon-skipping events were especially likely to be polysome-associated, including events affecting cell-growth regulators. This supports the expert interpretation of GEMIN5 as a dosage-sensitive gene-expression balancer, rather than a factor whose biological output simply increases monotonically with abundance (published August 2024; https://doi.org/10.1080/15476286.2024.2394755) (martinez‐salas2025understandinggemin5interactions pages 14-15).

6. Human disease and real-world applications

The strongest human association is an autosomal-recessive neurodevelopmental disorder characterized by developmental delay, hypotonia, cerebellar ataxia/motor dysfunction, and frequently cerebellar atrophy. The foundational 2021 cohort comprised 30 affected individuals from 22 unrelated families with biallelic GEMIN5 variants. Patient iPSC-derived neurons showed altered protein abundance/distribution, disturbed interacting partners, and reduced snRNP assembly. The fly GEMIN5 homolog model showed developmental abnormalities, motor impairment, and shortened lifespan (Nature Communications, May 2021; https://doi.org/10.1038/s41467-021-22627-w). Open Targets accordingly reports strong associations with hereditary disease and neurodevelopmental disorder with cerebellar atrophy and motor dysfunction, but its numerical association scores are evidence-ranking metrics—not prevalence or penetrance estimates (OpenTargets Search: -GEMIN5).

Mechanistic work on neurological variants found at least two pathogenic classes: substitutions in the TPR-like module that impair dimerization and ribosome association, and C-terminal RBS1-region variants that destabilize the protein. Both perturb translation- and RNA-processing interaction networks, providing functional evidence that disease can arise from combined failure of snRNP biogenesis, protein stability, and translation regulation (Life Science Alliance, 2022; https://doi.org/10.26508/lsa.202201403).

Current real-world applications are principally:

• Molecular diagnosis: inclusion of GEMIN5 in sequencing and interpretation of recessive neurodevelopmental/ataxia phenotypes.
• Variant functionalization: mapping variants to WD40, TPR-like, or RBS regions and testing stability, oligomerization, ribosome binding, RNA binding, and snRNP assembly.
• Patient-derived models: iPSC neurons provide disease-relevant readouts for snRNP assembly, nuclear Sm accumulation, splicing, and protein stability.
• Preclinical modifier testing: SMN augmentation partially rescues molecular and organismal phenotypes, suggesting a pathway-level therapeutic hypothesis. There is presently no evidence in the retrieved literature for an approved GEMIN5-directed drug or a clinical trial establishing benefit in GEMIN5-associated neurodevelopmental disease (fortuna2023smnregulatesgemin5 pages 16-18, fortuna2023smnregulatesgemin5 pages 1-3, fortuna2023smnregulatesgemin5 pages 11-13).

7. Evidence assessment and expert interpretation

The highest-confidence annotation is pre-snRNA receptor/adaptor in SMN-mediated snRNP assembly, supported by recombinant binding, depletion/delivery experiments, patient neurons, and multiple independent crystal structures. Ribosome association and translation regulation are also well supported, although the exact step in translation and the determinants that switch between repression and activation remain less completely resolved (franciscovelilla2018thelandscapeof pages 13-14, jin2016structuralbasisfor pages 1-2, martinezsalas2020emergingrolesof pages 3-5).

The apparent complexity is best explained by modularity. The WD40 propellers recognize sequence-constrained snRNA features and bind ribosomes; the middle TPR-like region determines oligomerization and partner recruitment; and the C-terminal region recognizes structured RNAs through multivalent assemblies. Consequently, “GEMIN5 regulates translation” should always be qualified by transcript, RNA structure, cellular state, protein fragment, and oligomeric state (guo2022structuralbasisfor pages 7-8, morenomorcillo2020structuralbasisfor pages 3-4, franciscovelilla2024oligomerizationregulatesthe pages 12-13).

Finally, both reduced and excessive GEMIN5 can disturb gene expression. Loss-of-function compromises snRNP assembly and neuronal homeostasis, whereas experimentally elevated GEMIN5 can increase alternative-splicing events that reach polysomes. Therapeutic strategies will therefore probably require restoration toward a physiological range rather than unrestricted overexpression.

References

1. (OpenTargets Search: -GEMIN5): Open Targets Query (-GEMIN5, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.

2. (jin2016structuralbasisfor pages 1-2): Wenxing Jin, Yi Wang, Chao-Pei Liu, Na Yang, Mingliang Jin, Yao Cong, Mingzhu Wang, and Rui-Ming Xu. Structural basis for snrna recognition by the double-wd40 repeat domain of gemin5. Genes & Development, 30:2391-2403, Nov 2016. URL: https://doi.org/10.1101/gad.291377.116, doi:10.1101/gad.291377.116. This article has 65 citations and is from a highest quality peer-reviewed journal.

3. (martinezsalas2020emergingrolesof pages 3-5): Encarnacion Martinez-Salas, Azman Embarc-Buh, and Rosario Francisco-Velilla. Emerging roles of gemin5: from snrnps assembly to translation control. International Journal of Molecular Sciences, 21:3868, May 2020. URL: https://doi.org/10.3390/ijms21113868, doi:10.3390/ijms21113868. This article has 46 citations.

4. (guo2022structuralbasisfor pages 7-8): Qiong Guo, Shidong Zhao, Rosario Francisco-Velilla, Jiahai Zhang, Azman Embarc-Buh, Salvador Abellan, Mengqi Lv, Peiping Tang, Qingguo Gong, Huaizong Shen, Linfeng Sun, Xuebiao Yao, Jinrong Min, Yunyu Shi, Encarnacion Martínez-Salas, Kaiming Zhang, and Chao Xu. Structural basis for gemin5 decamer-mediated mrna binding. Nature Communications, Sep 2022. URL: https://doi.org/10.1038/s41467-022-32883-z, doi:10.1038/s41467-022-32883-z. This article has 13 citations and is from a highest quality peer-reviewed journal.

5. (franciscovelilla2018thelandscapeof pages 13-14): Rosario Francisco-Velilla, Javier Fernandez-Chamorro, Ivan Dotu, and Encarnación Martinez-Salas. The landscape of the non-canonical rna-binding site of gemin5 unveils a feedback loop counteracting the negative effect on translation. Nucleic Acids Research, 46:7339-7353, May 2018. URL: https://doi.org/10.1093/nar/gky361, doi:10.1093/nar/gky361. This article has 32 citations and is from a highest quality peer-reviewed journal.

6. (morenomorcillo2020structuralbasisfor pages 3-4): María Moreno-Morcillo, Rosario Francisco-Velilla, Azman Embarc-Buh, Javier Fernández-Chamorro, Santiago Ramón-Maiques, and Encarnacion Martinez-Salas. Structural basis for the dimerization of gemin5 and its role in protein recruitment and translation control. Nucleic Acids Research, 48:788-801, Dec 2020. URL: https://doi.org/10.1093/nar/gkz1126, doi:10.1093/nar/gkz1126. This article has 34 citations and is from a highest quality peer-reviewed journal.

7. (morenomorcillo2020structuralbasisfor pages 4-5): María Moreno-Morcillo, Rosario Francisco-Velilla, Azman Embarc-Buh, Javier Fernández-Chamorro, Santiago Ramón-Maiques, and Encarnacion Martinez-Salas. Structural basis for the dimerization of gemin5 and its role in protein recruitment and translation control. Nucleic Acids Research, 48:788-801, Dec 2020. URL: https://doi.org/10.1093/nar/gkz1126, doi:10.1093/nar/gkz1126. This article has 34 citations and is from a highest quality peer-reviewed journal.

8. (morenomorcillo2020structuralbasisfor pages 10-11): María Moreno-Morcillo, Rosario Francisco-Velilla, Azman Embarc-Buh, Javier Fernández-Chamorro, Santiago Ramón-Maiques, and Encarnacion Martinez-Salas. Structural basis for the dimerization of gemin5 and its role in protein recruitment and translation control. Nucleic Acids Research, 48:788-801, Dec 2020. URL: https://doi.org/10.1093/nar/gkz1126, doi:10.1093/nar/gkz1126. This article has 34 citations and is from a highest quality peer-reviewed journal.

9. (franciscovelilla2024oligomerizationregulatesthe pages 12-13): Rosario Francisco-Velilla, Salvador Abellan, Azman Embarc-Buh, and Encarnacion Martinez-Salas. Oligomerization regulates the interaction of gemin5 with members of the smn complex and the translation machinery. Cell Death Discovery, Jun 2024. URL: https://doi.org/10.1038/s41420-024-02057-5, doi:10.1038/s41420-024-02057-5. This article has 5 citations and is from a peer-reviewed journal.

10. (guo2022structuralbasisfor pages 8-9): Qiong Guo, Shidong Zhao, Rosario Francisco-Velilla, Jiahai Zhang, Azman Embarc-Buh, Salvador Abellan, Mengqi Lv, Peiping Tang, Qingguo Gong, Huaizong Shen, Linfeng Sun, Xuebiao Yao, Jinrong Min, Yunyu Shi, Encarnacion Martínez-Salas, Kaiming Zhang, and Chao Xu. Structural basis for gemin5 decamer-mediated mrna binding. Nature Communications, Sep 2022. URL: https://doi.org/10.1038/s41467-022-32883-z, doi:10.1038/s41467-022-32883-z. This article has 13 citations and is from a highest quality peer-reviewed journal.

11. (fortuna2023smnregulatesgemin5 pages 16-18): Tyler R. Fortuna, Sukhleen Kour, Anuradha Venkatakrishnan Chimata, Anixa Muiños-Bühl, Eric N. Anderson, Charlie H. Nelson IV, Caroline Ward, Om Chauhan, Casey O’Brien, Dhivyaa Rajasundaram, Deepa S. Rajan, Brunhilde Wirth, Amit Singh, and Udai Bhan Pandey. Smn regulates gemin5 expression and acts as a modifier of gemin5-mediated neurodegeneration. Acta Neuropathologica, 146:477-498, Jun 2023. URL: https://doi.org/10.1007/s00401-023-02607-8, doi:10.1007/s00401-023-02607-8. This article has 11 citations and is from a highest quality peer-reviewed journal.

12. (fortuna2023smnregulatesgemin5 pages 1-3): Tyler R. Fortuna, Sukhleen Kour, Anuradha Venkatakrishnan Chimata, Anixa Muiños-Bühl, Eric N. Anderson, Charlie H. Nelson IV, Caroline Ward, Om Chauhan, Casey O’Brien, Dhivyaa Rajasundaram, Deepa S. Rajan, Brunhilde Wirth, Amit Singh, and Udai Bhan Pandey. Smn regulates gemin5 expression and acts as a modifier of gemin5-mediated neurodegeneration. Acta Neuropathologica, 146:477-498, Jun 2023. URL: https://doi.org/10.1007/s00401-023-02607-8, doi:10.1007/s00401-023-02607-8. This article has 11 citations and is from a highest quality peer-reviewed journal.

13. (fortuna2023smnregulatesgemin5 pages 11-13): Tyler R. Fortuna, Sukhleen Kour, Anuradha Venkatakrishnan Chimata, Anixa Muiños-Bühl, Eric N. Anderson, Charlie H. Nelson IV, Caroline Ward, Om Chauhan, Casey O’Brien, Dhivyaa Rajasundaram, Deepa S. Rajan, Brunhilde Wirth, Amit Singh, and Udai Bhan Pandey. Smn regulates gemin5 expression and acts as a modifier of gemin5-mediated neurodegeneration. Acta Neuropathologica, 146:477-498, Jun 2023. URL: https://doi.org/10.1007/s00401-023-02607-8, doi:10.1007/s00401-023-02607-8. This article has 11 citations and is from a highest quality peer-reviewed journal.

14. (martinezsalas2020emergingrolesof pages 1-3): Encarnacion Martinez-Salas, Azman Embarc-Buh, and Rosario Francisco-Velilla. Emerging roles of gemin5: from snrnps assembly to translation control. International Journal of Molecular Sciences, 21:3868, May 2020. URL: https://doi.org/10.3390/ijms21113868, doi:10.3390/ijms21113868. This article has 46 citations.

15. (martinez‐salas2025understandinggemin5interactions pages 14-15): Encarnacion Martinez‐Salas, Salvador Abellan, and Rosario Francisco‐Velilla. Understanding gemin5 interactions: from structural and functional insights to selective translation. Wiley Interdisciplinary Reviews. RNA, Mar 2025. URL: https://doi.org/10.1002/wrna.70008, doi:10.1002/wrna.70008. This article has 4 citations and is from a peer-reviewed journal.

16. (pineiro2015gemin5amultitasking pages 1-4): David Piñeiro, Javier Fernandez-Chamorro, Rosario Francisco-Velilla, and Encarna Martinez-Salas. Gemin5: a multitasking rna-binding protein involved in translation control. Biomolecules, 5:528-544, Apr 2015. URL: https://doi.org/10.3390/biom5020528, doi:10.3390/biom5020528. This article has 50 citations.

Artifacts

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Citations

1. jin2016structuralbasisfor pages 1-2
2. franciscovelilla2018thelandscapeof pages 13-14
3. franciscovelilla2024oligomerizationregulatesthe pages 12-13
4. martinezsalas2020emergingrolesof pages 3-5
5. guo2022structuralbasisfor pages 7-8
6. morenomorcillo2020structuralbasisfor pages 3-4
7. morenomorcillo2020structuralbasisfor pages 4-5
8. morenomorcillo2020structuralbasisfor pages 10-11
9. guo2022structuralbasisfor pages 8-9
10. martinezsalas2020emergingrolesof pages 1-3
11. https://doi.org/10.1038/s41467-022-32883-z
12. https://doi.org/10.1038/s41467-023-42324-0
13. https://doi.org/10.1007/s00018-022-04519-4
14. https://doi.org/10.1038/s41420-024-02057-5
15. https://doi.org/10.1007/s00401-023-02607-8
16. https://doi.org/10.1080/15476286.2024.2394755
17. https://doi.org/10.1038/s41467-021-22627-w
18. https://doi.org/10.26508/lsa.202201403
19. https://doi.org/10.1101/gad.291377.116,
20. https://doi.org/10.3390/ijms21113868,
21. https://doi.org/10.1038/s41467-022-32883-z,
22. https://doi.org/10.1093/nar/gky361,
23. https://doi.org/10.1093/nar/gkz1126,
24. https://doi.org/10.1038/s41420-024-02057-5,
25. https://doi.org/10.1007/s00401-023-02607-8,
26. https://doi.org/10.1002/wrna.70008,
27. https://doi.org/10.3390/biom5020528,