MTX2

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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 MTX2 / Metaxin-2 (UniProt O75431)—functional annotation and biomedical relevance

0) Target verification (gene/protein identity)

The target of this report is human MTX2 (Metaxin-2), corresponding to UniProt O75431, a 263–amino-acid mitochondrial protein localized to the outer mitochondrial membrane (OMM); the literature evidence used here explicitly matches this identity and organism context and does not refer to an unrelated “MTX2” symbol from another species. (elouej2020lossofmtx2 pages 1-2)

1) Key concepts and definitions (current understanding)

1.1 Metaxin family and “GST-like” fold (definition vs. enzyme function)

MTX2 is a member of the metaxin family and is described in recent clinical genetics literature as having two annotated regions: an N-terminal Sam37/metaxin_N domain (reported as aa 41–162) and a glutathione S-transferase (GST)-like domain. (dogan2023anovelmtx2 pages 5-5, fu2024casereporta pages 2-4)

Importantly, the “GST-like” designation in MTX2 is best interpreted as a structural fold similarity, not evidence that MTX2 catalyzes canonical GST conjugation reactions; the strongest experimental and genetic evidence supports a non-enzymatic role in mitochondrial outer membrane protein biogenesis/organization rather than a metabolic enzyme function. (elouej2020lossofmtx2 pages 1-2, elouej2020lossofmtx2 pages 2-4)

1.2 SAM (Sorting and Assembly Machinery) and β-barrel insertion (definition)

The mitochondrial Sorting and Assembly Machinery (SAM) is an OMM pathway that supports the correct integration of β-barrel proteins into the OMM. MTX2 and its partner Metaxin-1 (MTX1) are described as components of this machinery in the context of human disease genetics and functional studies. (elouej2020lossofmtx2 pages 1-2)

1.3 MICOS–SAM / MIB bridging (definition)

The SAM complex is described as a binding partner of Mic60, a core component of MICOS (mitochondrial contact site and cristae organizing system). These interactions form larger assemblies described as mitochondrial intermembrane space bridging complexes implicated in cristae junction organization and mitochondrial architecture. (elouej2020lossofmtx2 pages 1-2)

2) Molecular function, pathways, and subcellular localization

2.1 Subcellular localization and topology

MTX2 is localized to the outer mitochondrial membrane and is described as facing the cytosolic compartment. It is proposed to associate with the OMM through direct interaction with MTX1. (elouej2020lossofmtx2 pages 1-2, talarmingas2024validationofmetaxin2 pages 1-2)

2.2 Primary molecular function: OMM protein biogenesis/assembly and mitochondrial architecture

Multiple converging lines of evidence support MTX2’s primary function as a mitochondrial outer membrane protein biogenesis/assembly factor:

• Complex membership and partner interaction: MTX2 interacts directly with MTX1 and is positioned as part of the SAM machinery, supporting β-barrel protein integration in the OMM. (elouej2020lossofmtx2 pages 1-2)
• Systems/architecture linkage: SAM is described as interacting with Mic60/MICOS in higher-order bridging assemblies, linking MTX2’s SAM role to broader mitochondrial ultrastructure organization. (elouej2020lossofmtx2 pages 1-2)

2.3 Apoptosis and stress response linkage (secondary functional axis)

MTX1/MTX2 have also been discussed as contributing to TNF-α–induced apoptosis via interaction with the pro-apoptotic protein Bak, linking OMM composition to cell-death signaling. (elouej2020lossofmtx2 pages 1-2)

Consistent with this, patient fibroblasts lacking MTX2 show resistance to apoptosis induction (e.g., TNFα/CHX and staurosporine) and reduced caspase-3 activation. (elouej2020lossofmtx2 pages 6-7)

3) Human genetics and disease association (real-world relevance)

3.1 Disease: Mandibuloacral dysplasia associated with MTX2 (MADaM)

A key real-world “implementation” of MTX2 biology is in clinical genetics, where biallelic MTX2 loss-of-function variants cause a severe progeroid syndrome.

Discovery cohort (primary literature): Elouej et al. (Nature Communications; published Sep 2020; URL: https://doi.org/10.1038/s41467-020-18146-9) evaluated 7 patients from 5 consanguineous families and reported 5 homozygous null MTX2 variants, establishing MADaM. (elouej2020lossofmtx2 pages 1-2)

Clinical features included growth retardation and multisystem disease (e.g., renal involvement and severe hypertension), with cellular phenotypes implicating mitochondrial dysfunction. (elouej2020lossofmtx2 pages 1-2)

Variant spectrum expansion (recent):
* A 2023 clinical report (American Journal of Medical Genetics A; Oct 2023; URL: https://doi.org/10.1002/ajmg.a.63010) described a new splice-site variant c.543+1G>T causing exon 8 skipping (cDNA evidence) and noted that previously only five MTX2 pathogenic variants had been reported in the original discovery paper. (dogan2023anovelmtx2 pages 5-5)
* A 2024 case report (Frontiers in Endocrinology; published 13 Mar 2024; URL: https://doi.org/10.3389/fendo.2024.1345067) reported a novel homozygous splice-site mutation c.378+1G>A and summarized that 7 molecularly diagnosed MADaM cases had been reported worldwide prior to their report; they also describe deep sequencing coverage (99.80%, >100× depth) supporting diagnostic confidence. (fu2024casereporta pages 1-2, fu2024casereporta pages 2-4)

3.2 Mechanistic cellular consequences of MTX2 loss in human patient fibroblasts (quantitative)

Elouej et al. quantified mitochondrial morphology and function changes in MTX2-deficient fibroblasts:

(a) Secondary depletion of MTX1: Patient fibroblasts show loss of MTX2 and a complete secondary depletion of MTX1 protein, without reduction in MTX1 transcript levels (consistent with MTX1 instability when MTX2 is absent). (elouej2020lossofmtx2 pages 4-5)

(b) Mitochondrial network fragmentation / fission bias: Mitochondrial network analysis (MiNA macro) scored 53 (WT), 46 (MADM2), and 51 (MADM3) cells from n=5 independent experiments, showing significant reductions in network features (mitochondrial footprint, individuals, networks, branches per network). DRP1 was significantly increased (e.g., pMADM2 = 0.0015; pMADM3 = 0.042), consistent with increased fission. (elouej2020lossofmtx2 pages 4-5)

(c) Respiratory chain protein composition: Multiple respiratory chain subunits were significantly reduced (complex I/III/IV/V) while complex II SDHA was not. (elouej2020lossofmtx2 pages 5-6)

(d) Mitochondrial respiration: Respiration analyses showed a significant decrease in respiration dedicated to ATP synthesis (expressed as R–O/F) and decreased basal routine respiration (R/F) in patient fibroblasts; reported as n=4 independent experiments with p=0.015. (elouej2020lossofmtx2 pages 5-6, elouej2020lossofmtx2 media 62f590fd)

(e) Membrane potential: TMRM FACS showed increased mitochondrial membrane potential in at least one patient line (MADM2; reported p=0.015). (elouej2020lossofmtx2 pages 5-6, elouej2020lossofmtx2 media 1c141a95)

(f) Apoptosis resistance and mitophagy/autophagy: In patient fibroblasts, apoptosis induction was significantly blunted with strong p-values (e.g., TNFα/CHX pMADM2 = 4.0×10−5; pMADM3 = 2.1×10−7; staurosporine pMADM2 = 3.7×10−7; pMADM3 = 4.0×10−4). Autophagy markers (LC3B-II/LC3B-I) were increased (e.g., pMADM2 = 0.0002; pMADM3 = 0.026), and mitophagy was described as LC3C-associated rather than Parkin/ubiquitin-mediated. (elouej2020lossofmtx2 pages 6-7)

4) Recent developments (prioritizing 2023–2024)

4.1 2023: New splice-site pathogenic variant with functional transcript evidence

The 2023 splice-site variant report provides transcript-level evidence (exon skipping) strengthening the causal link between MTX2 splicing disruption and MADaM, and independently reiterates MTX2’s SAM/β-barrel insertion role as the mechanistic frame for disease. (dogan2023anovelmtx2 pages 5-5)

4.2 2024: Expanded global clinical reporting and molecular diagnostics rigor

The 2024 Frontiers case report contributes (i) a new likely pathogenic splice-site variant (c.378+1G>A), (ii) explicit clinical laboratory abnormalities (e.g., proteinuria, microhematuria, hypercholesterolemia, low IgG) in a pediatric presentation, and (iii) reporting of sequencing QC metrics (coverage/depth), illustrating how MTX2 is now used in real-world diagnostic workflows. (fu2024casereporta pages 2-4, fu2024casereporta pages 1-2)

4.3 2024: Model organism validation for mechanism and therapeutic discovery

Talarmin-Gas et al. (Communications Biology; Oct 2024; URL: https://doi.org/10.1038/s42003-024-06967-z) further validated mtx-2–deficient C. elegans as a MADaM model, using AFM, oxygen consumption rate analyses, and transcriptomics. They reported perturbations in aging, TOR, and WNT-signaling pathways and multiple quantitative phenotypes (e.g., body length reduction, pharyngeal pumping differences, and mitochondrial morphometrics). (talarmingas2024validationofmetaxin2 pages 1-2, talarmingas2024validationofmetaxin2 pages 8-10)

4.4 2024: Expert synthesis linking MTX2 to kinase interactomes and mitochondrial homeostasis

A 2024 expert review of Nek kinases and mitochondrial homeostasis (Cells; 7 Mar 2024; URL: https://doi.org/10.3390/cells13060473) summarizes that MTX2 appears among validated mitochondrial interactors emerging from Nek kinase interactome work, placing MTX2 in broader frameworks of mitochondrial composition/structure and stress-response networks. (basei2024themitochondrialconnection pages 1-3)

5) Current applications and real-world implementations

1. Molecular diagnosis and variant interpretation in progeroid syndromes: Reviews emphasize that overlapping phenotypes across premature-ageing syndromes motivate NGS gene panels and specialized clinical evaluation; MADaM (MTX2) is included among these syndromes in clinical genetics context. (coppede2021mutationsinvolvedin pages 1-2)
2. Functional assays to interpret variants: Patient fibroblast phenotyping (mitochondrial network quantification, respiration, apoptosis assays) provides a framework for validating candidate MTX2 variants beyond in silico prediction—especially for splice-site variants now being reported (2023–2024). (elouej2020lossofmtx2 pages 6-7, elouej2020lossofmtx2 pages 5-6, dogan2023anovelmtx2 pages 5-5)
3. Model-organism platforms for therapy discovery: The validated C. elegans model is explicitly positioned as enabling mechanistic dissection and scalable testing for therapeutics, leveraging measurable mitochondrial respiration and organismal phenotypes. (talarmingas2024validationofmetaxin2 pages 1-2)

6) Expert opinion and analysis (authoritative synthesis)

• “Functions remain largely unknown” but anchored by SAM context: The 2020 discovery paper explicitly notes that MTX2’s functions are “largely unknown” while anchoring its best-supported role in SAM-mediated β-barrel integration and interactions with MICOS/Mic60. This is a typical pattern for rare-disease gene discovery: genetic causality and robust cell phenotyping precede deep mechanistic dissection. (elouej2020lossofmtx2 pages 1-2)
• Mechanistic plausibility of pleiotropic phenotypes: The observed clinical syndrome (MADaM) includes nuclear morphological abnormalities, but the authors interpret these as downstream/secondary to mitochondrial dysfunction and altered mitochondrial composition, supporting an emerging view that mitochondrial architecture and signaling can drive “laminopathy-like” phenotypes without primary LMNA defects. (elouej2020lossofmtx2 pages 9-10, elouej2020lossofmtx2 pages 1-2)

7) Key statistics and data highlights (recent and foundational)

• Human cohort size (discovery): 7 patients, 5 families, 5 homozygous null MTX2 variants (Nature Communications, Sep 2020). (elouej2020lossofmtx2 pages 1-2)
• Mitochondrial network scoring: 53/46/51 cells (WT/MADM2/MADM3) across n=5 experiments; multiple network metrics significantly decreased. (elouej2020lossofmtx2 pages 4-5)
• Respiration functional deficit: Reduced ATP synthesis-linked respiration metric (R–O/F) and basal respiration ratios with n=4, p=0.015, visualized in Figure 3 panels. (elouej2020lossofmtx2 pages 5-6, elouej2020lossofmtx2 media 62f590fd)
• Apoptosis resistance: Strong significance for reduced death after TNFα/CHX and staurosporine exposure (p-values down to ~10−7). (elouej2020lossofmtx2 pages 6-7)
• 2024 diagnostic sequencing QC: 99.80% coverage and >100× depth in MTX2 region in a clinical exome workflow. (fu2024casereporta pages 2-4)

Evidence map (summary table)

Table: This table summarizes the core functional annotation of human MTX2/Metaxin-2 from the provided evidence, including identity, localization, molecular role, complex membership, disease relevance, and recent 2023-2024 updates. It is useful as a compact evidence map for building the full research report.

Visual evidence from primary literature

Quantitative mitochondrial respiration and membrane potential changes in MTX2-deficient human fibroblasts are shown in the cropped panels from Elouej et al. Figure 3 (respiration metrics and TMRM FACS). (elouej2020lossofmtx2 media 62f590fd, elouej2020lossofmtx2 media 1c141a95)

Limitations of the current evidence set

Within the retrieved 2023–2024 corpus available here, the most direct MTX2 updates are primarily clinical variant reports and model-organism validation rather than new high-resolution structural biology of human SAM-metaxin assemblies; therefore, this report emphasizes disease genetics, functional cell phenotyping, and validated pathway context (SAM–MICOS/MIB) over detailed atomic-level mechanism. (fu2024casereporta pages 1-2, talarmingas2024validationofmetaxin2 pages 1-2, elouej2020lossofmtx2 pages 1-2)

References

1. (elouej2020lossofmtx2 pages 1-2): Sahar Elouej, Karim Harhouri, Morgane Le Mao, Genevieve Baujat, Sheela Nampoothiri, Hϋlya Kayserili, Nihal Al Menabawy, Laila Selim, Arianne Llamos Paneque, Christian Kubisch, Davor Lessel, Robert Rubinsztajn, Chayki Charar, Catherine Bartoli, Coraline Airault, Jean-François Deleuze, Agnes Rötig, Peter Bauer, Catarina Pereira, Abigail Loh, Nathalie Escande-Beillard, Antoine Muchir, Lisa Martino, Yosef Gruenbaum, Song-Hua Lee, Philippe Manivet, Guy Lenaers, Bruno Reversade, Nicolas Lévy, and Annachiara De Sandre-Giovannoli. Loss of mtx2 causes mandibuloacral dysplasia and links mitochondrial dysfunction to altered nuclear morphology. Nature Communications, Sep 2020. URL: https://doi.org/10.1038/s41467-020-18146-9, doi:10.1038/s41467-020-18146-9. This article has 79 citations and is from a highest quality peer-reviewed journal.

2. (dogan2023anovelmtx2 pages 5-5): Burcu Yeter Doğan, Neslihan Günay, Yasin Ada, and Muhammet Ensar Doğan. A novel mtx2 gene splice site variant resulting in exon skipping, causing the recently described mandibuloacral dysplasia progeroid syndrome. American Journal of Medical Genetics Part A, 191:173-182, Oct 2023. URL: https://doi.org/10.1002/ajmg.a.63010, doi:10.1002/ajmg.a.63010. This article has 14 citations.

3. (fu2024casereporta pages 2-4): Xiaohui Fu, Shuli Chen, Xiao Huang, Qinghua Lu, Yunfei Cui, Weinan Lin, and Qin Yang. Case report: a novel splice-site mutation of mtx2 gene caused mandibuloacral dysplasia progeroid syndrome: the first report from china and literature review. Frontiers in Endocrinology, Mar 2024. URL: https://doi.org/10.3389/fendo.2024.1345067, doi:10.3389/fendo.2024.1345067. This article has 4 citations.

4. (elouej2020lossofmtx2 pages 2-4): Sahar Elouej, Karim Harhouri, Morgane Le Mao, Genevieve Baujat, Sheela Nampoothiri, Hϋlya Kayserili, Nihal Al Menabawy, Laila Selim, Arianne Llamos Paneque, Christian Kubisch, Davor Lessel, Robert Rubinsztajn, Chayki Charar, Catherine Bartoli, Coraline Airault, Jean-François Deleuze, Agnes Rötig, Peter Bauer, Catarina Pereira, Abigail Loh, Nathalie Escande-Beillard, Antoine Muchir, Lisa Martino, Yosef Gruenbaum, Song-Hua Lee, Philippe Manivet, Guy Lenaers, Bruno Reversade, Nicolas Lévy, and Annachiara De Sandre-Giovannoli. Loss of mtx2 causes mandibuloacral dysplasia and links mitochondrial dysfunction to altered nuclear morphology. Nature Communications, Sep 2020. URL: https://doi.org/10.1038/s41467-020-18146-9, doi:10.1038/s41467-020-18146-9. This article has 79 citations and is from a highest quality peer-reviewed journal.

5. (talarmingas2024validationofmetaxin2 pages 1-2): Chloé Talarmin-Gas, Georges Smolyakov, Cleo Parisi, Cyril Scandola, Valérie Andrianasolonirina, Cloé Lecoq, Valentine Houtart, Song-Hua Lee, Homa Adle-Biassette, Bénédicte Thiébot, Timothy Ganderton, and Philippe Manivet. Validation of metaxin-2 deficient c. elegans as a model for mandibuloacral dysplasia associated to mtx-2 (madam) syndrome. Communications Biology, Oct 2024. URL: https://doi.org/10.1038/s42003-024-06967-z, doi:10.1038/s42003-024-06967-z. This article has 5 citations and is from a peer-reviewed journal.

6. (elouej2020lossofmtx2 pages 6-7): Sahar Elouej, Karim Harhouri, Morgane Le Mao, Genevieve Baujat, Sheela Nampoothiri, Hϋlya Kayserili, Nihal Al Menabawy, Laila Selim, Arianne Llamos Paneque, Christian Kubisch, Davor Lessel, Robert Rubinsztajn, Chayki Charar, Catherine Bartoli, Coraline Airault, Jean-François Deleuze, Agnes Rötig, Peter Bauer, Catarina Pereira, Abigail Loh, Nathalie Escande-Beillard, Antoine Muchir, Lisa Martino, Yosef Gruenbaum, Song-Hua Lee, Philippe Manivet, Guy Lenaers, Bruno Reversade, Nicolas Lévy, and Annachiara De Sandre-Giovannoli. Loss of mtx2 causes mandibuloacral dysplasia and links mitochondrial dysfunction to altered nuclear morphology. Nature Communications, Sep 2020. URL: https://doi.org/10.1038/s41467-020-18146-9, doi:10.1038/s41467-020-18146-9. This article has 79 citations and is from a highest quality peer-reviewed journal.

7. (fu2024casereporta pages 1-2): Xiaohui Fu, Shuli Chen, Xiao Huang, Qinghua Lu, Yunfei Cui, Weinan Lin, and Qin Yang. Case report: a novel splice-site mutation of mtx2 gene caused mandibuloacral dysplasia progeroid syndrome: the first report from china and literature review. Frontiers in Endocrinology, Mar 2024. URL: https://doi.org/10.3389/fendo.2024.1345067, doi:10.3389/fendo.2024.1345067. This article has 4 citations.

8. (elouej2020lossofmtx2 pages 4-5): Sahar Elouej, Karim Harhouri, Morgane Le Mao, Genevieve Baujat, Sheela Nampoothiri, Hϋlya Kayserili, Nihal Al Menabawy, Laila Selim, Arianne Llamos Paneque, Christian Kubisch, Davor Lessel, Robert Rubinsztajn, Chayki Charar, Catherine Bartoli, Coraline Airault, Jean-François Deleuze, Agnes Rötig, Peter Bauer, Catarina Pereira, Abigail Loh, Nathalie Escande-Beillard, Antoine Muchir, Lisa Martino, Yosef Gruenbaum, Song-Hua Lee, Philippe Manivet, Guy Lenaers, Bruno Reversade, Nicolas Lévy, and Annachiara De Sandre-Giovannoli. Loss of mtx2 causes mandibuloacral dysplasia and links mitochondrial dysfunction to altered nuclear morphology. Nature Communications, Sep 2020. URL: https://doi.org/10.1038/s41467-020-18146-9, doi:10.1038/s41467-020-18146-9. This article has 79 citations and is from a highest quality peer-reviewed journal.

9. (elouej2020lossofmtx2 pages 5-6): Sahar Elouej, Karim Harhouri, Morgane Le Mao, Genevieve Baujat, Sheela Nampoothiri, Hϋlya Kayserili, Nihal Al Menabawy, Laila Selim, Arianne Llamos Paneque, Christian Kubisch, Davor Lessel, Robert Rubinsztajn, Chayki Charar, Catherine Bartoli, Coraline Airault, Jean-François Deleuze, Agnes Rötig, Peter Bauer, Catarina Pereira, Abigail Loh, Nathalie Escande-Beillard, Antoine Muchir, Lisa Martino, Yosef Gruenbaum, Song-Hua Lee, Philippe Manivet, Guy Lenaers, Bruno Reversade, Nicolas Lévy, and Annachiara De Sandre-Giovannoli. Loss of mtx2 causes mandibuloacral dysplasia and links mitochondrial dysfunction to altered nuclear morphology. Nature Communications, Sep 2020. URL: https://doi.org/10.1038/s41467-020-18146-9, doi:10.1038/s41467-020-18146-9. This article has 79 citations and is from a highest quality peer-reviewed journal.

10. (elouej2020lossofmtx2 media 62f590fd): Sahar Elouej, Karim Harhouri, Morgane Le Mao, Genevieve Baujat, Sheela Nampoothiri, Hϋlya Kayserili, Nihal Al Menabawy, Laila Selim, Arianne Llamos Paneque, Christian Kubisch, Davor Lessel, Robert Rubinsztajn, Chayki Charar, Catherine Bartoli, Coraline Airault, Jean-François Deleuze, Agnes Rötig, Peter Bauer, Catarina Pereira, Abigail Loh, Nathalie Escande-Beillard, Antoine Muchir, Lisa Martino, Yosef Gruenbaum, Song-Hua Lee, Philippe Manivet, Guy Lenaers, Bruno Reversade, Nicolas Lévy, and Annachiara De Sandre-Giovannoli. Loss of mtx2 causes mandibuloacral dysplasia and links mitochondrial dysfunction to altered nuclear morphology. Nature Communications, Sep 2020. URL: https://doi.org/10.1038/s41467-020-18146-9, doi:10.1038/s41467-020-18146-9. This article has 79 citations and is from a highest quality peer-reviewed journal.

11. (elouej2020lossofmtx2 media 1c141a95): Sahar Elouej, Karim Harhouri, Morgane Le Mao, Genevieve Baujat, Sheela Nampoothiri, Hϋlya Kayserili, Nihal Al Menabawy, Laila Selim, Arianne Llamos Paneque, Christian Kubisch, Davor Lessel, Robert Rubinsztajn, Chayki Charar, Catherine Bartoli, Coraline Airault, Jean-François Deleuze, Agnes Rötig, Peter Bauer, Catarina Pereira, Abigail Loh, Nathalie Escande-Beillard, Antoine Muchir, Lisa Martino, Yosef Gruenbaum, Song-Hua Lee, Philippe Manivet, Guy Lenaers, Bruno Reversade, Nicolas Lévy, and Annachiara De Sandre-Giovannoli. Loss of mtx2 causes mandibuloacral dysplasia and links mitochondrial dysfunction to altered nuclear morphology. Nature Communications, Sep 2020. URL: https://doi.org/10.1038/s41467-020-18146-9, doi:10.1038/s41467-020-18146-9. This article has 79 citations and is from a highest quality peer-reviewed journal.

12. (talarmingas2024validationofmetaxin2 pages 8-10): Chloé Talarmin-Gas, Georges Smolyakov, Cleo Parisi, Cyril Scandola, Valérie Andrianasolonirina, Cloé Lecoq, Valentine Houtart, Song-Hua Lee, Homa Adle-Biassette, Bénédicte Thiébot, Timothy Ganderton, and Philippe Manivet. Validation of metaxin-2 deficient c. elegans as a model for mandibuloacral dysplasia associated to mtx-2 (madam) syndrome. Communications Biology, Oct 2024. URL: https://doi.org/10.1038/s42003-024-06967-z, doi:10.1038/s42003-024-06967-z. This article has 5 citations and is from a peer-reviewed journal.

13. (basei2024themitochondrialconnection pages 1-3): Fernanda L. Basei, Ivan Rosa e Silva, Pedro R. Firmino Dias, Camila C. Ferezin, Andressa Peres de Oliveira, Luidy K. Issayama, Livia A. R. Moura, Fernando Riback da Silva, and Jörg Kobarg. The mitochondrial connection: the nek kinases’ new functional axis in mitochondrial homeostasis. Cells, 13:473, Mar 2024. URL: https://doi.org/10.3390/cells13060473, doi:10.3390/cells13060473. This article has 13 citations.

14. (coppede2021mutationsinvolvedin pages 1-2): Fabio Coppede. Mutations involved in premature-ageing syndromes. The Application of Clinical Genetics, 14:279-295, Jun 2021. URL: https://doi.org/10.2147/tacg.s273525, doi:10.2147/tacg.s273525. This article has 39 citations.

15. (elouej2020lossofmtx2 pages 9-10): Sahar Elouej, Karim Harhouri, Morgane Le Mao, Genevieve Baujat, Sheela Nampoothiri, Hϋlya Kayserili, Nihal Al Menabawy, Laila Selim, Arianne Llamos Paneque, Christian Kubisch, Davor Lessel, Robert Rubinsztajn, Chayki Charar, Catherine Bartoli, Coraline Airault, Jean-François Deleuze, Agnes Rötig, Peter Bauer, Catarina Pereira, Abigail Loh, Nathalie Escande-Beillard, Antoine Muchir, Lisa Martino, Yosef Gruenbaum, Song-Hua Lee, Philippe Manivet, Guy Lenaers, Bruno Reversade, Nicolas Lévy, and Annachiara De Sandre-Giovannoli. Loss of mtx2 causes mandibuloacral dysplasia and links mitochondrial dysfunction to altered nuclear morphology. Nature Communications, Sep 2020. URL: https://doi.org/10.1038/s41467-020-18146-9, doi:10.1038/s41467-020-18146-9. This article has 79 citations and is from a highest quality peer-reviewed journal.

16. (elouej2020lossofmtx2 pages 4-4): Sahar Elouej, Karim Harhouri, Morgane Le Mao, Genevieve Baujat, Sheela Nampoothiri, Hϋlya Kayserili, Nihal Al Menabawy, Laila Selim, Arianne Llamos Paneque, Christian Kubisch, Davor Lessel, Robert Rubinsztajn, Chayki Charar, Catherine Bartoli, Coraline Airault, Jean-François Deleuze, Agnes Rötig, Peter Bauer, Catarina Pereira, Abigail Loh, Nathalie Escande-Beillard, Antoine Muchir, Lisa Martino, Yosef Gruenbaum, Song-Hua Lee, Philippe Manivet, Guy Lenaers, Bruno Reversade, Nicolas Lévy, and Annachiara De Sandre-Giovannoli. Loss of mtx2 causes mandibuloacral dysplasia and links mitochondrial dysfunction to altered nuclear morphology. Nature Communications, Sep 2020. URL: https://doi.org/10.1038/s41467-020-18146-9, doi:10.1038/s41467-020-18146-9. This article has 79 citations and is from a highest quality peer-reviewed journal.

Citations

1. basei2024themitochondrialconnection pages 1-3
2. coppede2021mutationsinvolvedin pages 1-2
3. fu2024casereporta pages 2-4
4. fu2024casereporta pages 1-2
5. https://doi.org/10.1038/s41467-020-18146-9
6. https://doi.org/10.1002/ajmg.a.63010
7. https://doi.org/10.3389/fendo.2024.1345067
8. https://doi.org/10.1038/s42003-024-06967-z
9. https://doi.org/10.3390/cells13060473
10. https://doi.org/10.1038/s41467-020-18146-9,
11. https://doi.org/10.1002/ajmg.a.63010,
12. https://doi.org/10.3389/fendo.2024.1345067,
13. https://doi.org/10.1038/s42003-024-06967-z,
14. https://doi.org/10.3390/cells13060473,
15. https://doi.org/10.2147/tacg.s273525,