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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: Q53S33
• Protein Description: RecName: Full=BolA-like protein 3 {ECO:0000305};
• Gene Information: Name=BOLA3 {ECO:0000312|HGNC:HGNC:24415};
• Organism (full): Homo sapiens (Human).
• Protein Family: Belongs to the BolA/IbaG family. .
• Key Domains: BolA. (IPR002634); BolA-like_sf. (IPR036065); Mt_Fe-S_assembly_factor. (IPR052275); BolA (PF01722)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "BOLA3" 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 'BOLA3' 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 BOLA3 (gene ID: BOLA3, UniProt: Q53S33) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: Q53S33
• Protein Description: RecName: Full=BolA-like protein 3 {ECO:0000305};
• Gene Information: Name=BOLA3 {ECO:0000312|HGNC:HGNC:24415};
• Organism (full): Homo sapiens (Human).
• Protein Family: Belongs to the BolA/IbaG family. .
• Key Domains: BolA. (IPR002634); BolA-like_sf. (IPR036065); Mt_Fe-S_assembly_factor. (IPR052275); BolA (PF01722)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "BOLA3" 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 'BOLA3' 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 BOLA3 (gene ID: BOLA3, UniProt: Q53S33) 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 report: Human BOLA3 (UniProt Q53S33)

Plan and verification
- Verified identity: BOLA3 encodes human BolA-like protein 3, a member of the BolA/IbaG family with roles in mitochondrial iron–sulfur (Fe–S) protein biogenesis; recent biochemical and review literature discuss human BOLA3’s function and pathogenic variants, consistent with the UniProt entry (human; BolA family/domain) (bargagna2023understandingthemolecular pages 1-2, bargagna2024molecularpathwaysfor pages 40-44).
- Verified localization: BOLA3 functions within the mitochondrial Fe–S assembly (ISC) pathway, i.e., in mitochondria (zhong2023bola3andnfu1 pages 1-2, sheftel2012thehumanmitochondrial pages 1-2).

Key concepts and current definitions
- BOLA3 is a late-acting mitochondrial ISC accessory factor that partners with GLRX5 to form a heterocomplex bridged by a [2Fe–2S] cluster. In this complex, GLRX5 ligates via Cys67 and a glutathione cysteine, and BOLA3 contributes Cys59 and His96 ligands (human numbering). This complex acts as a [2Fe–2S] carrier/chaperone toward late ISC clients, notably NFU1 (bargagna2024molecularpathwaysfora pages 40-44, bargagna2024molecularpathwaysfor pages 40-44).
- Late ISC network architecture: the GLRX5–BOLA3 node supplies [2Fe–2S] clusters, whereas the ISCA1/ISCA2–IBA57 system and NFU1 are required to assemble and/or deliver [4Fe–4S] clusters to client proteins in mitochondria (zhong2023bola3andnfu1 pages 1-2, sheftel2012thehumanmitochondrial pages 1-2).
- Downstream processes: Proper BOLA3 function supports maturation of [4Fe–4S] enzymes, including lipoyl synthase (LIAS), thereby enabling protein lipoylation of pyruvate dehydrogenase (PDH), α‑ketoglutarate dehydrogenase (KGDH), and the glycine cleavage system H-protein; BOLA3 also contributes to mitochondrial respiratory complex activities and mitoribosomal Fe–S cluster insertion required for organellar translation (sheftel2012thehumanmitochondrial pages 1-2, zhong2023bola3andnfu1 pages 1-2, baker2014variantnonketotic pages 10-11).

Recent developments and latest research (emphasis 2023–2024)
- Mitoribosome Fe–S assembly: Zhong et al. demonstrated that human mitoribosomes contain three [2Fe–2S] clusters and receive them from the GLRX5–BOLA3 node; BOLA3 or NFU1 deficiency attenuates mitochondrial protein synthesis and contributes to the pathophysiology of MMDS (Multiple Mitochondrial Dysfunctions Syndromes). They also propose the ISCA1→NFU1 route inserts a [4Fe–4S] cluster into METTL17, a mitoribosome assembly factor (Nucleic Acids Research; advance access 12 Oct 2023; https://doi.org/10.1093/nar/gkad842) (zhong2023bola3andnfu1 pages 1-2).
- Variant-level mechanism for MMDS2: Bargagna et al. (2023 IJMS; 2024 review) dissected the pathogenic BOLA3 His96Arg (H96R) mutation. H96R preserves GLRX5 binding but produces an aberrant BOLA3–[2Fe–2S]–GLRX5 complex unable to transfer its cluster to NFU1 to assemble the NFU1 [4Fe–4S] cluster; this mechanistically explains the severe MMDS2 phenotype with impaired respiratory complexes and lipoylation defects. The review also catalogues BOLA3 variants, including Cys59Tyr (ligand site) with partial residual function (2023: https://doi.org/10.3390/ijms241411734) (bargagna2023understandingthemolecular pages 1-2, bargagna2024molecularpathwaysfor pages 55-56, bargagna2024molecularpathwaysfora pages 55-56, bargagna2023understandingthemolecular pages 11-12).
- Consolidation of late ISC roles: Earlier foundational work (Sheftel et al., 2012) established that ISCA1/ISCA2/IBA57 are required for mitochondrial [4Fe–4S] protein maturation and linked these factors to LIAS and lipoylation, a framework into which the GLRX5–BOLA3 node integrates (Mol Biol Cell; Apr 2012; https://doi.org/10.1091/mbc.e11-09-0772) (sheftel2012thehumanmitochondrial pages 1-2).

Current applications and real-world implementations
- Diagnostics: In variant nonketotic hyperglycinemia (vNKH) workups, sequencing of LIAS, BOLA3 and GLRX5 identifies etiologies; functional confirmation often uses western blot for lipoylated E2 subunits of PDH/KGDH and PDH enzyme assays. Baker et al. reported deficient protein lipoylation in 8/10 families and used complementation in fibroblasts to prove causality (Brain; Feb 2014; https://doi.org/10.1093/brain/awt328) (baker2014variantnonketotic pages 10-11, baker2014variantnonketotic pages 7-8, baker2014variantnonketotic pages 9-10).
- Mechanistic cell models: Zhong et al. used patient fibroblasts and gene knockdown to relate BOLA3/NFU1 deficiency to mitoribosome Fe–S cluster insertion and mitochondrial translation, now a platform for assessing pathogenic variants (zhong2023bola3andnfu1 pages 1-2).
- Gene/variant interpretation: Structural-biochemical assays (SEC, NMR, EPR, UV–vis/CD) of BOLA3 variants (H96R, C59Y) quantify effects on GLRX5 heterocomplex formation and NFU1 [4Fe–4S] assembly, informing pathogenicity classification (bargagna2023understandingthemolecular pages 1-2, bargagna2024molecularpathwaysfor pages 55-56, bargagna2024molecularpathwaysfora pages 55-56, bargagna2023understandingthemolecular pages 11-12).

Expert opinions and analyses from authoritative sources
- NAR 2023 (Zhong et al.) proposes a partitioned late ISC map: GLRX5–BOLA3 provides [2Fe–2S] to the mitoribosome, while ISCA1→NFU1 provides [4Fe–4S] to METTL17, arguing that impaired BOLA3 or NFU1 causes combined defects in electron transport chain enzymes and mitochondrial translation (zhong2023bola3andnfu1 pages 1-2).
- 2023–2024 expert reviews emphasize that BOLA3’s conserved His96 and Cys59 residues coordinate the [2Fe–2S] bridge within the GLRX5–BOLA3 complex, and that pathogenic substitution of these ligands explains loss of downstream [4Fe–4S] maturation and lipoylation (bargagna2024molecularpathwaysfora pages 40-44, bargagna2024molecularpathwaysfor pages 55-56, bargagna2024molecularpathwaysfor pages 40-44).

Relevant statistics and recent clinical data
- Variant NKH cohort: Baker et al. studied 11 patients from 10 families; genetic etiologies were defined for 8 patients with mutations in LIAS, BOLA3, or GLRX5. In that series, protein lipoylation defects were shown in 8 of 10 families tested (Brain; 2014) (baker2014variantnonketotic pages 2-3, baker2014variantnonketotic pages 10-11).
- BOLA3 clinical course: BOLA3-associated vNKH/MMDS2 is typically infantile and often fatal in the first year of life; recurrent truncating BOLA3 variant c.136C>T (p.R46X) occurred homozygously in multiple families (baker2014variantnonketotic pages 2-3, baker2014variantnonketotic pages 7-8).
- GLRX5 context for the node: A 2024 case report of GLRX5-mediated NKH presented with early-onset severe disease and death by ~4 months, underscoring the GLRX5–BOLA3–LIAS functional axis in lipoylation and glycine cleavage (Frontiers in Genetics; Sep 2024; https://doi.org/10.3389/fgene.2024.1432272) (marin2024casereportunveiling pages 3-4).

Mechanistic pathway synthesis
- Early ISC steps produce [2Fe–2S] clusters that are transferred to GLRX5. The GLRX5–BOLA3 heterocomplex binds a bridged [2Fe–2S] cluster via GLRX5 Cys67/glutathione and BOLA3 Cys59/His96, forming a mobile chaperone unit. Two such [2Fe–2S] equivalents can be delivered to NFU1, where reductive coupling yields a [4Fe–4S] cluster for late clients including LIAS and additional [4Fe–4S] assembly factors; in parallel, ISCA1/ISCA2/IBA57 function in [4Fe–4S] biogenesis/delivery, and GLRX5–BOLA3 supplies [2Fe–2S] to the mitoribosome (bargagna2024molecularpathwaysfora pages 40-44, bargagna2024molecularpathwaysfor pages 40-44, zhong2023bola3andnfu1 pages 1-2, sheftel2012thehumanmitochondrial pages 1-2).
- Pathogenic H96R disrupts BOLA3’s histidine ligand, generating an aberrant GLRX5–BOLA3 complex that cannot complete [2Fe–2S] → [4Fe–4S] transfer on NFU1, mechanistically explaining combined defects in respiratory complexes and lipoylation (bargagna2023understandingthemolecular pages 1-2, bargagna2023understandingthemolecular pages 11-12). C59Y produces partial loss consistent with milder phenotypes (bargagna2024molecularpathwaysfora pages 55-56).

Clinical phenotypes and disease links
- Multiple Mitochondrial Dysfunctions Syndrome type 2 (MMDS2): Biallelic BOLA3 variants cause leukodystrophy/encephalopathy with lactic acidosis and hyperglycinemia; biochemical findings include reduced activities of respiratory complexes and decreased activity of lipoyl-dependent enzymes (PDH, KGDH, glycine cleavage H-protein). Infantile lethality is common (bargagna2023understandingthemolecular pages 1-2, baker2014variantnonketotic pages 2-3).
- Variant nonketotic hyperglycinemia (vNKH): Mutations in LIAS, BOLA3, or GLRX5 lead to vNKH characterized by elevated plasma (and milder CSF) glycine and defective protein lipoylation; diagnostic lipoylation blotting was abnormal in most studied families (baker2014variantnonketotic pages 10-11, baker2014variantnonketotic pages 3-3, baker2014variantnonketotic pages 11-12).

URLs and publication dates (where available)
- Zhong et al., Nucleic Acids Research, advance access 12 Oct 2023: https://doi.org/10.1093/nar/gkad842 (zhong2023bola3andnfu1 pages 1-2).
- Bargagna et al., IJMS, 21 Jul 2023: https://doi.org/10.3390/ijms241411734 (bargagna2023understandingthemolecular pages 1-2).
- Sheftel et al., Mol Biol Cell, Apr 2012: https://doi.org/10.1091/mbc.e11-09-0772 (sheftel2012thehumanmitochondrial pages 1-2).
- Baker et al., Brain, Feb 2014: https://doi.org/10.1093/brain/awt328 (baker2014variantnonketotic pages 10-11, baker2014variantnonketotic pages 2-3, baker2014variantnonketotic pages 7-8, baker2014variantnonketotic pages 9-10, baker2014variantnonketotic pages 11-11, baker2014variantnonketotic pages 11-12, baker2014variantnonketotic pages 3-3).
- Marin et al., Frontiers in Genetics, Sep 2024: https://doi.org/10.3389/fgene.2024.1432272 (marin2024casereportunveiling pages 3-4).

Embedded summary table
| Category | Key points (compact) | Evidence |
|---|---|---|
| Identity / verification | Human gene BOLA3 (UniProt Q53S33). Member of BolA family with BolA/BolA-like and Mt_Fe-S_assembly_factor domains (BolA, BolA-like_sf, IPR052275). | (bargagna2023understandingthemolecular pages 1-2, bargagna2024molecularpathwaysfor pages 40-44) |
| Cellular localization | Mitochondrial matrix/mitochondrial ISC system (mitochondrial targeting; functions in mitochondrial Fe–S biogenesis). | (zhong2023bola3andnfu1 pages 1-2, sheftel2012thehumanmitochondrial pages 1-2) |
| Mechanistic role & primary interactors | Forms a heterocomplex with mitochondrial GLRX5 that binds a bridged [2Fe-2S] cluster; functions as a late-acting ISC accessory/chaperone delivering cluster equivalents toward NFU1 and clients. Interacts functionally with NFU1; works in network with ISCA1/2 and IBA57. | (bargagna2023understandingthemolecular pages 1-2, bargagna2024molecularpathwaysfor pages 40-44, zhong2023bola3andnfu1 pages 1-2, sheftel2012thehumanmitochondrial pages 1-2) |
| ISC pathway nodes (who supplies which) | GLRX5–BOLA3 node: supplies/hosts [2Fe-2S] bridged clusters (donor node). ISCA1/2–IBA57 (and ISCA1/2→NFU1) route: late [4Fe-4S] assembly/delivery to mitochondrial clients; NFU1 receives/converts two [2Fe-2S] inputs to a [4Fe-4S] on NFU1. | (zhong2023bola3andnfu1 pages 1-2, bargagna2023understandingthemolecular pages 1-2, sheftel2012thehumanmitochondrial pages 1-2) |
| Downstream processes affected | LIAS (lipoyl synthase) maturation and protein lipoylation (PDH, KGDH, GCS H-protein), respiratory complex activities, and mitoribosome [2Fe-2S] insertion/assembly → impacts mitochondrial protein synthesis. | (sheftel2012thehumanmitochondrial pages 1-2, zhong2023bola3andnfu1 pages 1-2, baker2014variantnonketotic pages 10-11) |
| Key 2023–2024 advances | 2023: Zhong et al. linked GLRX5–BOLA3 node to mitoribosomal [2Fe-2S] clusters and showed BOLA3/NFU1 loss attenuates mitochondrial translation (mitoribosome stability) (zhong2023bola3andnfu1 pages 1-2). 2023–2024: Bargagna et al. biochemical/structural dissection of H96R and C59Y variants showed H96R forms aberrant GLRX5–BOLA3 heterocomplex that cannot assemble [4Fe-4S] on NFU1 (mechanistic basis for MMDS2); reviews (2024) consolidate late-ISC pathway roles. | (zhong2023bola3andnfu1 pages 1-2, bargagna2023understandingthemolecular pages 1-2, bargagna2024molecularpathwaysfor pages 40-44, bargagna2024molecularpathwaysfor pages 55-56) |
| Disease links & clinical phenotype | Biallelic BOLA3 mutations → MMDS2 (multiple mitochondrial dysfunctions syndrome type 2): leukodystrophy/encephalopathy, lactic acidosis, hyperglycinemia, early lethal neonatal/infantile course. BOLA3 (with LIAS, GLRX5) implicated in variant non‑ketotic hyperglycinemia (vNKH) with lipoylation defects. | (bargagna2023understandingthemolecular pages 1-2, baker2014variantnonketotic pages 10-11, baker2014variantnonketotic pages 2-3) |
| Variants (functional effects) & selected statistics | Functionally characterized: H96R (c.287A>G) — preserves GLRX5 binding but yields nonfunctional BOLA3–[2Fe-2S]–GLRX5 unable to transfer/assemble [4Fe-4S] on NFU1; associated with severe MMDS2 and death in infancy (reported fatal <1 yr) (bargagna2023understandingthemolecular pages 1-2, bargagna2023understandingthemolecular pages 11-12). C59Y — perturbs cluster ligand, retains partial activity → milder phenotype (bargagna2024molecularpathwaysfor pages 40-44). R46X (c.136C>T) recurrent truncation seen homozygous in multiple families (baker2014variantnonketotic pages 7-8). Reported counts: Baker et al. cohort = 11 patients (10 families) with vNKH; genetic diagnosis in 8/11 (LIAS, BOLA3, GLRX5) and several pathogenic BOLA3 alleles reported (~8 described in literature excerpt). Typical BOLA3 cases often fatal in first year (cohort-level note). | (bargagna2023understandingthemolecular pages 11-12, bargagna2024molecularpathwaysfor pages 40-44, baker2014variantnonketotic pages 7-8, baker2014variantnonketotic pages 2-3, baker2014variantnonketotic pages 9-10) |

Table: Compact summary table of human BOLA3 (Q53S33) covering identity, localization, mechanistic role in Fe–S biogenesis, downstream processes, 2023–2024 advances, disease links, key variants and available cohort statistics with primary evidence citations.

Conclusion
Human BOLA3 is a mitochondrial BolA-family factor that forms a [2Fe–2S]-bridged heterocomplex with GLRX5, acting at a late ISC node to support NFU1-dependent [4Fe–4S] maturation, lipoyl synthase function and mitoribosomal Fe–S insertion. 2023–2024 work clarified that GLRX5–BOLA3 supplies mitoribosomal [2Fe–2S] clusters and that specific BOLA3 ligand-site variants (H96R, C59Y) explain MMDS2 mechanistically. Clinically, BOLA3 deficiency underlies MMDS2 and contributes to variant NKH with characteristic lipoylation defects, often with infantile lethality. These insights guide molecular diagnostics (sequencing of LIAS/BOLA3/GLRX5; lipoylation assays) and functional variant assessment strategies (zhong2023bola3andnfu1 pages 1-2, bargagna2023understandingthemolecular pages 1-2, baker2014variantnonketotic pages 10-11).

References

1. (bargagna2023understandingthemolecular pages 1-2): Beatrice Bargagna, Lucia Banci, and Francesca Camponeschi. Understanding the molecular basis of the multiple mitochondrial dysfunctions syndrome 2: the disease-causing his96arg mutation of bola3. International Journal of Molecular Sciences, 24:11734, Jul 2023. URL: https://doi.org/10.3390/ijms241411734, doi:10.3390/ijms241411734. This article has 1 citations and is from a poor quality or predatory journal.

2. (bargagna2024molecularpathwaysfor pages 40-44): B Bargagna. Molecular pathways for the maturation of mitochondrial and cytosolic human fe-s proteins. Unknown journal, 2024.

3. (zhong2023bola3andnfu1 pages 1-2): Hui Zhong, Alexandre Janer, Oleh Khalimonchuk, Hana Antonicka, Eric A Shoubridge, and Antoni Barrientos. Bola3 and nfu1 link mitoribosome iron–sulfur cluster assembly to multiple mitochondrial dysfunctions syndrome. Nucleic Acids Research, 51:11797-11812, Oct 2023. URL: https://doi.org/10.1093/nar/gkad842, doi:10.1093/nar/gkad842. This article has 31 citations and is from a highest quality peer-reviewed journal.

4. (sheftel2012thehumanmitochondrial pages 1-2): Alex D. Sheftel, Claudia Wilbrecht, Oliver Stehling, Brigitte Niggemeyer, Hans-Peter Elsässer, Ulrich Mühlenhoff, and Roland Lill. The human mitochondrial isca1, isca2, and iba57 proteins are required for [4fe-4s] protein maturation. Molecular Biology of the Cell, 23:1157-1166, Apr 2012. URL: https://doi.org/10.1091/mbc.e11-09-0772, doi:10.1091/mbc.e11-09-0772. This article has 250 citations and is from a domain leading peer-reviewed journal.

5. (bargagna2024molecularpathwaysfora pages 40-44): B Bargagna. Molecular pathways for the maturation of mitochondrial and cytosolic human fe-s proteins. Unknown journal, 2024.

6. (baker2014variantnonketotic pages 10-11): Peter R. Baker, Marisa W. Friederich, Michael A. Swanson, Tamim Shaikh, Kaustuv Bhattacharya, Gunter H. Scharer, Joseph Aicher, Geralyn Creadon-Swindell, Elizabeth Geiger, Kenneth N. MacLean, Wang-Tso Lee, Charu Deshpande, Mary-Louise Freckmann, Ling-Yu Shih, Melissa Wasserstein, Malene B. Rasmussen, Allan M. Lund, Peter Procopis, Jessie M. Cameron, Brian H. Robinson, Garry K. Brown, Ruth M. Brown, Alison G. Compton, Carol L. Dieckmann, Renata Collard, Curtis R. Coughlin, Elaine Spector, Michael F. Wempe, and Johan L.K. Van Hove. Variant non ketotic hyperglycinemia is caused by mutations in lias, bola3 and the novel gene glrx5. Brain : a journal of neurology, 137 Pt 2:366-79, Feb 2014. URL: https://doi.org/10.1093/brain/awt328, doi:10.1093/brain/awt328. This article has 258 citations.

7. (bargagna2024molecularpathwaysfor pages 55-56): B Bargagna. Molecular pathways for the maturation of mitochondrial and cytosolic human fe-s proteins. Unknown journal, 2024.

8. (bargagna2024molecularpathwaysfora pages 55-56): B Bargagna. Molecular pathways for the maturation of mitochondrial and cytosolic human fe-s proteins. Unknown journal, 2024.

9. (bargagna2023understandingthemolecular pages 11-12): Beatrice Bargagna, Lucia Banci, and Francesca Camponeschi. Understanding the molecular basis of the multiple mitochondrial dysfunctions syndrome 2: the disease-causing his96arg mutation of bola3. International Journal of Molecular Sciences, 24:11734, Jul 2023. URL: https://doi.org/10.3390/ijms241411734, doi:10.3390/ijms241411734. This article has 1 citations and is from a poor quality or predatory journal.

10. (baker2014variantnonketotic pages 7-8): Peter R. Baker, Marisa W. Friederich, Michael A. Swanson, Tamim Shaikh, Kaustuv Bhattacharya, Gunter H. Scharer, Joseph Aicher, Geralyn Creadon-Swindell, Elizabeth Geiger, Kenneth N. MacLean, Wang-Tso Lee, Charu Deshpande, Mary-Louise Freckmann, Ling-Yu Shih, Melissa Wasserstein, Malene B. Rasmussen, Allan M. Lund, Peter Procopis, Jessie M. Cameron, Brian H. Robinson, Garry K. Brown, Ruth M. Brown, Alison G. Compton, Carol L. Dieckmann, Renata Collard, Curtis R. Coughlin, Elaine Spector, Michael F. Wempe, and Johan L.K. Van Hove. Variant non ketotic hyperglycinemia is caused by mutations in lias, bola3 and the novel gene glrx5. Brain : a journal of neurology, 137 Pt 2:366-79, Feb 2014. URL: https://doi.org/10.1093/brain/awt328, doi:10.1093/brain/awt328. This article has 258 citations.

11. (baker2014variantnonketotic pages 9-10): Peter R. Baker, Marisa W. Friederich, Michael A. Swanson, Tamim Shaikh, Kaustuv Bhattacharya, Gunter H. Scharer, Joseph Aicher, Geralyn Creadon-Swindell, Elizabeth Geiger, Kenneth N. MacLean, Wang-Tso Lee, Charu Deshpande, Mary-Louise Freckmann, Ling-Yu Shih, Melissa Wasserstein, Malene B. Rasmussen, Allan M. Lund, Peter Procopis, Jessie M. Cameron, Brian H. Robinson, Garry K. Brown, Ruth M. Brown, Alison G. Compton, Carol L. Dieckmann, Renata Collard, Curtis R. Coughlin, Elaine Spector, Michael F. Wempe, and Johan L.K. Van Hove. Variant non ketotic hyperglycinemia is caused by mutations in lias, bola3 and the novel gene glrx5. Brain : a journal of neurology, 137 Pt 2:366-79, Feb 2014. URL: https://doi.org/10.1093/brain/awt328, doi:10.1093/brain/awt328. This article has 258 citations.

12. (baker2014variantnonketotic pages 2-3): Peter R. Baker, Marisa W. Friederich, Michael A. Swanson, Tamim Shaikh, Kaustuv Bhattacharya, Gunter H. Scharer, Joseph Aicher, Geralyn Creadon-Swindell, Elizabeth Geiger, Kenneth N. MacLean, Wang-Tso Lee, Charu Deshpande, Mary-Louise Freckmann, Ling-Yu Shih, Melissa Wasserstein, Malene B. Rasmussen, Allan M. Lund, Peter Procopis, Jessie M. Cameron, Brian H. Robinson, Garry K. Brown, Ruth M. Brown, Alison G. Compton, Carol L. Dieckmann, Renata Collard, Curtis R. Coughlin, Elaine Spector, Michael F. Wempe, and Johan L.K. Van Hove. Variant non ketotic hyperglycinemia is caused by mutations in lias, bola3 and the novel gene glrx5. Brain : a journal of neurology, 137 Pt 2:366-79, Feb 2014. URL: https://doi.org/10.1093/brain/awt328, doi:10.1093/brain/awt328. This article has 258 citations.

13. (marin2024casereportunveiling pages 3-4): Victor Marin, Louis Lebreton, Claire Guibet, Samir Mesli, Isabelle Redonnet-Vernhet, Mathurin Dexant, Delphine Lamireau, Sandrine Roche, Margaux Gaschignard, Jean Delmas, Henri Margot, and Claire Bar. Case report: unveiling genetic and phenotypic variability in nonketotic hyperglycinemia: an atypical early onset case associated with a novel glrx5 variant. Frontiers in Genetics, Sep 2024. URL: https://doi.org/10.3389/fgene.2024.1432272, doi:10.3389/fgene.2024.1432272. This article has 1 citations and is from a peer-reviewed journal.

14. (baker2014variantnonketotic pages 3-3): Peter R. Baker, Marisa W. Friederich, Michael A. Swanson, Tamim Shaikh, Kaustuv Bhattacharya, Gunter H. Scharer, Joseph Aicher, Geralyn Creadon-Swindell, Elizabeth Geiger, Kenneth N. MacLean, Wang-Tso Lee, Charu Deshpande, Mary-Louise Freckmann, Ling-Yu Shih, Melissa Wasserstein, Malene B. Rasmussen, Allan M. Lund, Peter Procopis, Jessie M. Cameron, Brian H. Robinson, Garry K. Brown, Ruth M. Brown, Alison G. Compton, Carol L. Dieckmann, Renata Collard, Curtis R. Coughlin, Elaine Spector, Michael F. Wempe, and Johan L.K. Van Hove. Variant non ketotic hyperglycinemia is caused by mutations in lias, bola3 and the novel gene glrx5. Brain : a journal of neurology, 137 Pt 2:366-79, Feb 2014. URL: https://doi.org/10.1093/brain/awt328, doi:10.1093/brain/awt328. This article has 258 citations.

15. (baker2014variantnonketotic pages 11-12): Peter R. Baker, Marisa W. Friederich, Michael A. Swanson, Tamim Shaikh, Kaustuv Bhattacharya, Gunter H. Scharer, Joseph Aicher, Geralyn Creadon-Swindell, Elizabeth Geiger, Kenneth N. MacLean, Wang-Tso Lee, Charu Deshpande, Mary-Louise Freckmann, Ling-Yu Shih, Melissa Wasserstein, Malene B. Rasmussen, Allan M. Lund, Peter Procopis, Jessie M. Cameron, Brian H. Robinson, Garry K. Brown, Ruth M. Brown, Alison G. Compton, Carol L. Dieckmann, Renata Collard, Curtis R. Coughlin, Elaine Spector, Michael F. Wempe, and Johan L.K. Van Hove. Variant non ketotic hyperglycinemia is caused by mutations in lias, bola3 and the novel gene glrx5. Brain : a journal of neurology, 137 Pt 2:366-79, Feb 2014. URL: https://doi.org/10.1093/brain/awt328, doi:10.1093/brain/awt328. This article has 258 citations.

16. (baker2014variantnonketotic pages 11-11): Peter R. Baker, Marisa W. Friederich, Michael A. Swanson, Tamim Shaikh, Kaustuv Bhattacharya, Gunter H. Scharer, Joseph Aicher, Geralyn Creadon-Swindell, Elizabeth Geiger, Kenneth N. MacLean, Wang-Tso Lee, Charu Deshpande, Mary-Louise Freckmann, Ling-Yu Shih, Melissa Wasserstein, Malene B. Rasmussen, Allan M. Lund, Peter Procopis, Jessie M. Cameron, Brian H. Robinson, Garry K. Brown, Ruth M. Brown, Alison G. Compton, Carol L. Dieckmann, Renata Collard, Curtis R. Coughlin, Elaine Spector, Michael F. Wempe, and Johan L.K. Van Hove. Variant non ketotic hyperglycinemia is caused by mutations in lias, bola3 and the novel gene glrx5. Brain : a journal of neurology, 137 Pt 2:366-79, Feb 2014. URL: https://doi.org/10.1093/brain/awt328, doi:10.1093/brain/awt328. This article has 258 citations.

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