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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:** Q99437
- **Protein Description:** RecName: Full=V-type proton ATPase 21 kDa proteolipid subunit c'' {ECO:0000305}; Short=V-ATPase 21 kDa proteolipid subunit c'' {ECO:0000305}; AltName: Full=Vacuolar proton pump 21 kDa proteolipid subunit c'' {ECO:0000305}; AltName: Full=hATPL;
- **Gene Information:** Name=ATP6V0B; Synonyms=ATP6F;
- **Organism (full):** Homo sapiens (Human).
- **Protein Family:** Belongs to the V-ATPase proteolipid subunit family.
- **Key Domains:** ATPase_proteolipid_c-like_dom. (IPR002379); ATPase_proteolipid_csu. (IPR000245); F/V-ATP_Csub_sf. (IPR035921); ATP-synt_C (PF00137)

### MANDATORY VERIFICATION STEPS:

1. **Check if the gene symbol "ATP6V0B" matches the protein description above**
2. **Verify the organism is correct:** Homo sapiens (Human).
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 'ATP6V0B' 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 **ATP6V0B** (gene ID: ATP6V0B, UniProt: Q99437) in human.

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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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:** Q99437
- **Protein Description:** RecName: Full=V-type proton ATPase 21 kDa proteolipid subunit c'' {ECO:0000305}; Short=V-ATPase 21 kDa proteolipid subunit c'' {ECO:0000305}; AltName: Full=Vacuolar proton pump 21 kDa proteolipid subunit c'' {ECO:0000305}; AltName: Full=hATPL;
- **Gene Information:** Name=ATP6V0B; Synonyms=ATP6F;
- **Organism (full):** Homo sapiens (Human).
- **Protein Family:** Belongs to the V-ATPase proteolipid subunit family.
- **Key Domains:** ATPase_proteolipid_c-like_dom. (IPR002379); ATPase_proteolipid_csu. (IPR000245); F/V-ATP_Csub_sf. (IPR035921); ATP-synt_C (PF00137)

### MANDATORY VERIFICATION STEPS:

1. **Check if the gene symbol "ATP6V0B" matches the protein description above**
2. **Verify the organism is correct:** Homo sapiens (Human).
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 'ATP6V0B' 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 **ATP6V0B** (gene ID: ATP6V0B, UniProt: Q99437) in human.

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 plan and verification
Objective 1: Verify identity, organism, family, domains. The target is human ATP6V0B (UniProt Q99437), encoding the V-ATPase V0 21 kDa proteolipid subunit c'' (also called c-double-prime), a member of the V-ATPase proteolipid subunit family. Literature identifies ATP6V0B as the V0 c'' proteolipid subunit in mammals, consistent with the UniProt description and human organism context (Homo sapiens). V-ATPase proteolipids (c, c', c'') are homologous to F-type ATP synthase c subunits and form the membrane c-ring of the Vo sector (ion-conducting rotor), validating the protein family and domain expectations (ATPase proteolipid c-like) (holliday2014vacuolarh+atpasean pages 2-3, cipriano2008structureandregulation pages 2-4, forgac1999structureandproperties pages 3-3).

Objective 2: Summarize key concepts and definitions
- V-ATPase architecture and function: Eukaryotic V-ATPases acidify intracellular organelles and, in specialized cells, the extracellular milieu. They consist of a cytosolic catalytic V1 sector (ATP hydrolysis) and a membrane-embedded Vo sector (H+ translocation). ATP hydrolysis in V1 drives rotation of the central stalk (D/F) and subunit d, which rotates the proteolipid c-ring of Vo past the stationary a-subunit to move protons across the membrane (rotary mechanism) (cipriano2008structureandregulation pages 2-4, holliday2014vacuolarh+atpasean pages 2-3).
- Proteolipid subunits: The Vo proteolipids include c (4 transmembrane helices), c' (4 TM), and c'' (5 TM; ATP6V0B). Each harbors a single buried, protonatable carboxyl essential for H+ translocation: in TM4 of c (and c') and TM3 of c'' (c'') (cipriano2008structureandregulation pages 2-4, forgac1999structureandproperties pages 3-3).
- Compartmental roles: V-ATPases acidify endosomes, lysosomes, Golgi, and secretory/synaptic vesicles; plasma membrane V-ATPases occur in specialized cells (e.g., renal intercalated cells, epididymal clear cells, osteoclast ruffled border), where extracellular acidification supports physiological functions (holliday2014vacuolarh+atpasean pages 2-3, chu2021thevatpasea3 pages 2-3).

Objective 3: ATP6V0B-specific function and structural/biochemical details
- Identity and synonyms: ATP6V0B encodes the Vo proteolipid subunit c'' (c-double-prime), a ~20–23 kDa hydrophobic subunit with five transmembrane helices; it is homologous to other proteolipids and to the F-type c subunit (holliday2014vacuolarh+atpasean pages 2-3, forgac1999structureandproperties pages 3-3).
- Conserved catalytic residue: c'' contains a buried acidic residue in TM3 required for proton translocation; mutational/chemical modification studies demonstrate that neutralizing the essential carboxyl of a single proteolipid subunit can abolish transport, underscoring the functional necessity of each proteolipid’s conserved carboxyl (cipriano2008structureandregulation pages 2-4, forgac1999structureandproperties pages 3-3).
- c-ring composition and stoichiometry: In yeast, the Vo ring contains multiple c copies plus single copies of c' and c'' (a1 d1 e n c4–5 c'1 c''1), establishing a general principle of mixed proteolipid rings. Mammalian summaries similarly describe a c-ring that includes a single c'' together with multiple c subunits; some overviews denote a c9 + c'' ring, implying one ATP6V0B per ring in mammals (cipriano2008structureandregulation pages 2-4, chu2021thevatpasea3 pages 2-3, yang2025vatpaseandlysosomal pages 6-7).
- Placement and interactions: Cross-linking places the a-subunit TM7 adjacent to TM4 of c' and TM3 of c'', consistent with a direct interface between a and proteolipid helices where proton exchange occurs during rotation. Potent macrolide inhibitors (bafilomycin/concanamycin) bind within helical interfaces of the proteolipid ring, indicating druggable grooves near c/c'' interfaces (cipriano2008structureandregulation pages 2-4).

Objective 4: Localization and pathways
- Subcellular localization: ATP6V0B-containing V-ATPases populate the acidifying pumps of the endo-lysosomal system, Golgi, and secretory/synaptic vesicles; in certain polarized or specialized cell types, V-ATPase is targeted to the plasma membrane for extracellular acidification (kidney intercalated cells, epididymis clear cells, osteoclasts). Targeting is largely determined by the isoform of the a-subunit (e.g., a3 targeting in osteoclasts), but the proteolipid ring that includes ATP6V0B is integral to Vo in all locations (holliday2014vacuolarh+atpasean pages 2-3, chu2021thevatpasea3 pages 2-3).
- Pathways: V-ATPases are central for endocytic trafficking, receptor–ligand dissociation, lysosomal hydrolase activation, neurotransmitter loading into synaptic vesicles, autophagy and mTORC1 nutrient/energy sensing at lysosomes. By contributing to luminal acidification, the ATP6V0B-containing c-ring is required for these processes (cipriano2008structureandregulation pages 2-4, holliday2014vacuolarh+atpasean pages 2-3).

Objective 5: Recent developments (priority to 2023–2024) and latest research context
- Although few 2023–2024 primary data directly isolate ATP6V0B-specific effects, contemporary reviews and updates reinforce mechanistic placement of the proteolipid ring and its regulation within emerging V-ATPase biology, including lysosomal energy-sensing platforms and accessory subunits embedded near the c-ring in mammalian brain V-ATPases (e.g., AC45/ATP6AP1, ATP6AP2) (chen2025theemergingroles pages 22-23, yang2025vatpaseandlysosomal pages 6-7). These updates contextualize ATP6V0B as the unique c'' proteolipid in a mammalian c-ring whose stability, interactions, and regulation are relevant to disease pathways.

Objective 6: Regulation and interaction partners
- Transcriptional regulation: The transcription factor E2F1 upregulates ATP6V0B expression and V-ATPase activity; E2F1 activation drives lysosome peripheral trafficking and mTORC1 activation, which is suppressed by V-ATPase inhibition. Reporter assays and mRNA measurements confirm E2F1-induced ATP6V0B transcription (meoevoli2015vatpaseamaster pages 5-8).
- Protein interactions and assembly environment: Mammalian V-ATPases incorporate accessory proteins (ATP6AP1/AC45 and ATP6AP2) within or adjacent to the proteolipid ring in brain complexes, and these proteins interface with mTORC1 energy-sensing machinery, linking Vo ring composition to signaling. Although not specific to ATP6V0B alone, they are positioned in the ring neighborhood where c'' resides (yang2025vatpaseandlysosomal pages 6-7).

Objective 7: Disease associations and phenotypes
- V-ATPase subunits and disease: Multiple V-ATPase subunit mutations cause human disease, particularly neurological disorders (e.g., ATP6V1A variants causing developmental epileptic encephalopathy), emphasizing that disruption of V-ATPase function leads to organelle acidification defects and neurodevelopmental phenotypes. While direct human genetic disease caused by ATP6V0B has not been clearly established, the essential role of the proteolipid ring (including c'') in proton translocation supports the plausibility that perturbation would be deleterious (groszer2022rarehumanatp6v1a pages 7-9, cipriano2008structureandregulation pages 2-4, forgac1999structureandproperties pages 3-3).
- Cancer and tissue remodeling: V-ATPase localization to the plasma membrane in tumor cells and osteoclasts drives extracellular acidification for invasion/metastasis and bone resorption, respectively. ATP6V0B participates as the c'' subunit of the proton-translocating rotor required for these activities (holliday2014vacuolarh+atpasean pages 2-3, chu2021thevatpasea3 pages 2-3).

Objective 8: Applications and implementations
- Pharmacology and tool compounds: Bafilomycin and concanamycin are classical macrolide inhibitors that target interfaces within the proteolipid ring of Vo, inhibiting rotation and H+ translocation. These compounds are widely used as research tools to block organelle acidification, interrogate autophagy (late-stage flux), and inhibit mTORC1 activation dependent on lysosomal acidification (cipriano2008structureandregulation pages 2-4).
- Translational contexts: Accessory subunit interactions near the proteolipid ring (e.g., ATP6AP1/ATP6AP2) link V-ATPase to nutrient/energy sensing (mTORC1), suggesting V-ATPase modulators—and, by extension, the stability/interaction profile of the c-ring that includes ATP6V0B—may have therapeutic implications in cancer and metabolic/inflammatory diseases (yang2025vatpaseandlysosomal pages 6-7, chen2025theemergingroles pages 22-23).

Objective 9: Quantitative/statistical details
- Proteolipid ring stoichiometry: Yeast Vo contains 4–5 copies of c plus single copies of c' and c'' in the ring (a1 d1 e n c4–5 c'1 c''1). Mammalian summaries suggest a similar principle with multiple c-subunits and one c'' per ring (often summarized as c9 + c'') (cipriano2008structureandregulation pages 2-4, chu2021thevatpasea3 pages 2-3, yang2025vatpaseandlysosomal pages 6-7).
- Essential residues: The essential protonatable carboxylates are located in TM4 of c (and c') and TM3 of c''; neutralization or chemical modification of a single proteolipid’s essential carboxyl can abolish proton transport, underscoring the dependence on every proteolipid site within the ring (cipriano2008structureandregulation pages 2-4, forgac1999structureandproperties pages 3-3).

Expert analysis
- Specificity and unique role of ATP6V0B: Among the proteolipid family, ATP6V0B provides the sole c'' subunit in the mammalian ring, adding a fifth helix and distinct topology compared with c/c'. The unique TM3-carboxyl position and proximity to a-subunit TM7 (from cross-linking) suggest c'' contributes specialized interfaces critical for torque transmission and proton exchange. Given the inferred one-per-ring stoichiometry, ATP6V0B is structurally nonredundant: damage to c'' would be expected to compromise the rotor’s integrity and the proton pathway for the entire complex (cipriano2008structureandregulation pages 2-4, forgac1999structureandproperties pages 3-3).
- Regulatory integration: E2F1-driven induction of ATP6V0B places this subunit under cell-cycle and growth control, aligning V-ATPase acidification capacity with anabolic signaling (mTORC1). This supports a model wherein proteolipid ring capacity (including ATP6V0B levels) is tuned to proliferative cues to modulate lysosomal signaling hubs (meoevoli2015vatpaseamaster pages 5-8).
- Evidence limitations and 2023–2024 gap: Direct 2023–2024 cryo-EM placement of c'' within human complexes and human genetics directly implicating ATP6V0B remain sparse in the accessible evidence compiled here. Nonetheless, long-standing biochemical and cross-linking evidence establish the topology, essential residue, and a–c'' proximities, and recent reviews reinforce the mammalian ring organization and accessory subunits near the ring (cipriano2008structureandregulation pages 2-4, yang2025vatpaseandlysosomal pages 6-7, chen2025theemergingroles pages 22-23).

Key sources with URLs and dates
- Forgac M. Structure and Properties of the Vacuolar (H+)-ATPases. J Biol Chem. 1999 May 14;274(19):12951–12954. https://doi.org/10.1074/jbc.274.19.12951 (mechanism; proteolipid subunits; essential carboxyl; early stoichiometry) (forgac1999structureandproperties pages 3-3).
- Cipriano DJ et al. Structure and regulation of the vacuolar ATPases. Biochim Biophys Acta. 2008 Jul–Aug;1777(7–8):599–604. https://doi.org/10.1016/j.bbabio.2008.03.013 (rotary mechanism; c/c'/c'' helices and essential residues; a–ring interactions; inhibitor binding site) (cipriano2008structureandregulation pages 2-4).
- Holliday LS. Vacuolar H+-ATPase: An Essential Multitasking Enzyme in Physiology and Pathophysiology. New J Sci. 2014;2014:675430. https://doi.org/10.1155/2014/675430 (subunit catalog including ATP6V0B as c''; physiological localizations) (holliday2014vacuolarh+atpasean pages 2-3).
- Chu A, Zirngibl RA, Manolson MF. The V-ATPase a3 Subunit. Int J Mol Sci. 2021 Jun;22(13):6934. https://doi.org/10.3390/ijms22136934 (membrane ring composition summarized as c9+c''; essential E98 in c'') (chu2021thevatpasea3 pages 2-3).
- Meo-Evoli N et al. V-ATPase: a master effector of E2F1-mediated lysosomal trafficking, mTORC1 activation and autophagy. Oncotarget. 2015 Aug;6(29):28057–28070. https://doi.org/10.18632/oncotarget.4812 (E2F1 directly induces ATP6V0B; coupling to mTORC1) (meoevoli2015vatpaseamaster pages 5-8).
- Groszer M. Rare human ATP6V1A variants provide unique insights into V-ATPase functions. Brain. 2022 Jul;145(8):2626–2628. https://doi.org/10.1093/brain/awac255 (context: subunit mutations cause neurological disease; lysosomal V-ATPase overview) (groszer2022rarehumanatp6v1a pages 7-9).
- Chen Y-Y et al. The Emerging Roles of V-ATPase-Dependent Lysosomal Acidification in Cardiovascular Disease. Biomolecules. 2025 Apr;15(4):525. https://doi.org/10.3390/biom15040525 (recent review summarizing assembly factors, localization, signaling links) (chen2025theemergingroles pages 22-23).
- Yang X, Holliday LS. V-ATPase and Lysosomal Energy Sensing in Periodontitis and MRONJ. Biomolecules. 2025 Jul;15(7):997. https://doi.org/10.3390/biom15070997 (mammalian ring organization including c''/ATP6V0B; accessory subunits within ring) (yang2025vatpaseandlysosomal pages 6-7).

Conclusions
Human ATP6V0B encodes the Vo proteolipid c'' subunit, a five-helix rotor component containing an essential buried carboxyl in TM3. It assembles with multiple c subunits to form the proteolipid c-ring that rotates against the a-subunit to translocate H+ during ATP-driven catalysis. ATP6V0B-containing V-ATPases acidify lysosomes, endosomes, Golgi, and secretory/synaptic vesicles and can localize to plasma membranes in specialized cells. Transcriptional upregulation by E2F1 links ATP6V0B to growth signaling, while accessory proteins embedded near the ring connect Vo composition to mTORC1 energy sensing. Although direct 2023–2024 ATP6V0B-specific structures and genetics remain limited in this evidence set, foundational biochemical and cross-linking work, supported by recent reviews, define ATP6V0B’s identity, essential residues, ring stoichiometry, and functional placement in mammalian V-ATPase biology (cipriano2008structureandregulation pages 2-4, holliday2014vacuolarh+atpasean pages 2-3, chu2021thevatpasea3 pages 2-3, forgac1999structureandproperties pages 3-3, yang2025vatpaseandlysosomal pages 6-7, meoevoli2015vatpaseamaster pages 5-8).

References

1. (holliday2014vacuolarh+atpasean pages 2-3): L. Shannon Holliday. Vacuolar h+-atpase: an essential multitasking enzyme in physiology and pathophysiology. New Journal of Science, 2014:1-21, Jan 2014. URL: https://doi.org/10.1155/2014/675430, doi:10.1155/2014/675430. This article has 59 citations.

2. (cipriano2008structureandregulation pages 2-4): Daniel J. Cipriano, Yanru Wang, Sarah Bond, Ayana Hinton, Kevin C. Jefferies, Jie Qi, and Michael Forgac. Structure and regulation of the vacuolar atpases. Biochimica et biophysica acta, 1777 7-8:599-604, Jul 2008. URL: https://doi.org/10.1016/j.bbabio.2008.03.013, doi:10.1016/j.bbabio.2008.03.013. This article has 226 citations.

3. (forgac1999structureandproperties pages 3-3): Michael Forgac. Structure and properties of the vacuolar (h+)-atpases*. The Journal of Biological Chemistry, 274:12951-12954, May 1999. URL: https://doi.org/10.1074/jbc.274.19.12951, doi:10.1074/jbc.274.19.12951. This article has 414 citations.

4. (chu2021thevatpasea3 pages 2-3): Anh Chu, Ralph A. Zirngibl, and Morris F. Manolson. The v-atpase a3 subunit: structure, function and therapeutic potential of an essential biomolecule in osteoclastic bone resorption. International Journal of Molecular Sciences, 22:6934, Jun 2021. URL: https://doi.org/10.3390/ijms22136934, doi:10.3390/ijms22136934. This article has 31 citations and is from a poor quality or predatory journal.

5. (yang2025vatpaseandlysosomal pages 6-7): Xianrui Yang and Lexie Shannon Holliday. V-atpase and lysosomal energy sensing in periodontitis and medicine-related osteonecrosis of the jaw. Biomolecules, 15:997, Jul 2025. URL: https://doi.org/10.3390/biom15070997, doi:10.3390/biom15070997. This article has 0 citations and is from a poor quality or predatory journal.

6. (chen2025theemergingroles pages 22-23): Yan-Yan Chen, Cai-Xia Liu, Hai-Xin Liu, and Shi-Yuan Wen. The emerging roles of vacuolar-type atpase-dependent lysosomal acidification in cardiovascular disease. Biomolecules, 15:525, Apr 2025. URL: https://doi.org/10.3390/biom15040525, doi:10.3390/biom15040525. This article has 7 citations and is from a poor quality or predatory journal.

7. (meoevoli2015vatpaseamaster pages 5-8): Nathalie Meo-Evoli, Eugènia Almacellas, Francesco Alessandro Massucci, Antonio Gentilella, Santiago Ambrosio, Sara C. Kozma, George Thomas, and Albert Tauler. V-atpase: a master effector of e2f1-mediated lysosomal trafficking, mtorc1 activation and autophagy. Oncotarget, 6:28057-28070, Aug 2015. URL: https://doi.org/10.18632/oncotarget.4812, doi:10.18632/oncotarget.4812. This article has 53 citations and is from a poor quality or predatory journal.

8. (groszer2022rarehumanatp6v1a pages 7-9): Matthias Groszer. Rare human atp6v1a variants provide unique insights into v-atpase functions. Brain : a journal of neurology, 145:2626-2628, Jul 2022. URL: https://doi.org/10.1093/brain/awac255, doi:10.1093/brain/awac255. This article has 5 citations.

## Citations

1. cipriano2008structureandregulation pages 2-4
2. meoevoli2015vatpaseamaster pages 5-8
3. yang2025vatpaseandlysosomal pages 6-7
4. forgac1999structureandproperties pages 3-3
5. chen2025theemergingroles pages 22-23
6. https://doi.org/10.1074/jbc.274.19.12951
7. https://doi.org/10.1016/j.bbabio.2008.03.013
8. https://doi.org/10.1155/2014/675430
9. https://doi.org/10.3390/ijms22136934
10. https://doi.org/10.18632/oncotarget.4812
11. https://doi.org/10.1093/brain/awac255
12. https://doi.org/10.3390/biom15040525
13. https://doi.org/10.3390/biom15070997
14. https://doi.org/10.1155/2014/675430,
15. https://doi.org/10.1016/j.bbabio.2008.03.013,
16. https://doi.org/10.1074/jbc.274.19.12951,
17. https://doi.org/10.3390/ijms22136934,
18. https://doi.org/10.3390/biom15070997,
19. https://doi.org/10.3390/biom15040525,
20. https://doi.org/10.18632/oncotarget.4812,
21. https://doi.org/10.1093/brain/awac255,