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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Identity check. The specified human protein, UniProt Q9BW92, is the product of TARS2 (the supplied synonym is TARSL1). Primary research independently identifies human TARS2 as the nuclear gene encoding mitochondrial threonyl-tRNA synthetase (mtThrRS), a class-II aminoacyl-tRNA synthetase. This is not cytoplasmic TARS1, nor the separate threonyl-tRNA-synthetase-like gene TARSL2. The Q9BW92 accession and TARSL1 synonym are supplied identification metadata; the literature examined establishes the TARS2 protein identity but does not independently verify that accession–synonym mapping. (wang2016ahumandiseasecausing pages 4-5, zeng2023lossofthreonyltrna pages 1-2, barai2024beyondproteinsynthesis pages 1-2)
Primary reaction. TARS2 charges mitochondrial tRNA^Thr with L-threonine, using ATP. It first forms threonyl-AMP and pyrophosphate, then transfers threonine to the tRNA’s 3′-terminal adenosine: L-threonine + ATP + mitochondrial tRNA^Thr → L-threonyl–tRNA^Thr + AMP + PPi. The charged tRNA supplies threonine at Thr codons during mitochondrial protein synthesis. Purified human TARS2 performs threonine activation and mitochondrial tRNA^Thr aminoacylation directly; this assignment is therefore experimental, not merely inferred from its domain annotations. (wang2016ahumandiseasecausing pages 1-2, wang2016ahumandiseasecausing pages 4-5, zheng2020nitrosativestressinhibits pages 1-2)
Human mitochondrial tRNA^Thr has a UGU anticodon. In substrate-mutagenesis experiments, replacing either anticodon nucleotide G35 or U36 eliminated charging, whereas changing discriminator nucleotide A73 partially impaired it. Amino-acid selection favors threonine over the similar, noncognate amino acid serine by approximately 383-fold in the measured activation assay; measured Km values were 2.5 ± 0.1 mM for threonine and 180 ± 14 mM for serine. These are in-vitro activation parameters, not estimates of the cellular mistranslation rate. The study also found limited charging of some nonmitochondrial tRNAs in vitro, so physiological specificity is best stated as preferential charging of mitochondrial tRNA^Thr in its mitochondrial compartment, not absolute inability to recognize every other tRNA. (wang2016ahumandiseasecausing pages 5-6, wang2016ahumandiseasecausing media 18f44078)
TARS2 also proofreads serine misactivation and mischarging. Human enzyme assays detected both pre-transfer editing and hydrolysis of incorrectly formed Ser–tRNA^Thr. Substituting editing-site His133 and His137 abolished the latter, post-transfer deacylation and increased Ser–tRNA^Thr accumulation. Although tRNA-dependent pre-transfer editing contributed strongly to measured AMP production, post-transfer editing was the decisive final protection against detectable mischarged tRNA in these assays. (wang2016ahumandiseasecausing pages 1-2, wang2016ahumandiseasecausing pages 6-8)
The 718-residue precursor is made from a nuclear gene in the cytosol and imported into mitochondria using an N-terminal targeting sequence. Human-cell microscopy supports mitochondrial localization. Its organization comprises an N-terminal region, an N2 editing domain, a class-II aminoacylation catalytic core, and a C-terminal anticodon-binding/tRNA-binding domain; the catalytic-core and anticodon-binding annotations in the question align with this experimentally studied architecture. The N-terminal cleavage position has not been definitively established: a computational prediction and the N-terminal deletion yielding a soluble active recombinant enzyme gave different indications. (wang2016ahumandiseasecausing pages 4-5, wang2016ahumandiseasecausing pages 9-11, zhang2024tars2c.470c pages 1-2)
Within mitochondria, native mtThrRS forms foci that colocalize with the GRSF1-marked mitochondrial RNA granules. Deleting its C-terminal tRNA-binding region markedly reduced enrichment at those granules, consistent with local organization of tRNA charging near mitochondrial RNA metabolism; colocalization does not prove that every charging event occurs inside a granule. A 2022 interaction study also identified mitochondrial ArgRS among TARS2-associated synthetases, without establishing that this interaction is required for TARS2 catalysis. (peng2022rnagranuleclusteredmitochondrial pages 5-6, peng2022rnagranuleclusteredmitochondrial pages 6-7, peng2022rnagranuleclusteredmitochondrial pages 1-2)
The principal biochemical pathway is mitochondrial gene expression → translation of mitochondrially encoded respiratory-chain subunits → oxidative phosphorylation (OXPHOS). Human mitochondrial DNA specifies 13 proteins; insufficient correctly charged mitochondrial tRNA^Thr or defective proofreading can consequently compromise respiratory-chain production and function. In a 2023 mouse Tars2 editing-deficiency model, Ser–tRNA^Thr and Thr-to-Ser substitutions accumulated, mitochondrial translation and OXPHOS declined, and reactive oxygen species increased. Heart-restricted editing deficiency caused impaired cardiomyocyte proliferation, contractile dysfunction, dilated cardiomyopathy and fibrosis. This model establishes the importance of editing fidelity in vivo, but a mouse editing-site mutation should not be treated as the measured effect of every human TARS2 allele. (zheng2023mammalianmitochondrialtranslation pages 1-2, accogli2023clinicalneuroradiologicaland pages 1-3)
Additional signaling role. Research reviewed in 2024 reports that TARS2 participates in threonine-sensitive mTORC1 signaling, physically engaging the Rag amino-acid-sensing machinery and favoring RagA GTP loading, lysosomal mTORC1 recruitment and activation after threonine stimulation. This is a function distinct from supplying mitochondrial ribosomes with threonyl–tRNA^Thr; how TARS2 drives RagA nucleotide exchange remains unresolved. A 2023 disease study found that TARS2 residues 301–381 are important for Rag interaction. Four variants in this region had diminished protein abundance and reduced co-immunoprecipitation with RagA and RagC, so impaired signaling is plausible, although reduced stability complicates attributing each binding defect solely to an altered interface. A review reports a cytosolic TARS2 fraction of roughly 10–15%; that figure must not be interpreted as a measured lysosomal fraction. The review also cautions that the precise mechanistic link between Rag binding and nucleotide loading is unknown. (barai2024beyondproteinsynthesis pages 4-6, accogli2023clinicalneuroradiologicaland pages 10-11, tyynismaa2023diseasemodelsof pages 2-3)
Inherited disease and variant interpretation. Biallelic pathogenic TARS2 variants cause the recessive mitochondrial encephalomyopathy termed combined oxidative phosphorylation deficiency 21 (COXPD21). In a 2023 Genetics in Medicine study, 18 newly identified individuals from 15 families were assessed using sequencing, clinical evaluation, protein-interaction assays and zebrafish experiments. Across its expanded case series, axial hypotonia was reported in 24/27, elevated blood lactate in 17/20, and seizures in 14/28 individuals assessed for those features; denominators vary because observations were incomplete. In the newly described cohort, cerebellar atrophy occurred in 12/16 with evaluated imaging. These findings support TARS2 sequencing and careful variant assessment in compatible early-onset neurodevelopmental or mitochondrial presentations, rather than making any single feature diagnostic. (accogli2023clinicalneuroradiologicaland pages 1-3, accogli2023clinicalneuroradiologicaland pages 11-12, accogli2023clinicalneuroradiologicaland pages 8-10)
The same 2023 study found that zebrafish tars2 knockdown disrupted brain, heart, myelin and muscle development; supplying wild-type human TARS2 mRNA rescued major phenotypes. The fish also showed changes in mTORC1-associated readouts, while tested human variants often failed to rescue or rescued only partially. These assays strengthen pathogenicity assessments but do not, by themselves, determine whether each human allele primarily damages tRNA charging, editing, protein stability or Rag signaling. (accogli2023clinicalneuroradiologicaland pages 10-11)
A 2024 Orphanet Journal of Rare Diseases report added four affected individuals from three unrelated Chinese families and two previously unreported TARS2 variants. The recurrent c.470C>G, p.Thr157Arg allele was reported in six Chinese affected individuals overall; the authors proposed a Chinese-specific founder mutation and its relevance to population-aware carrier screening. The report principally supplies genetic and clinical evidence, not direct enzyme assays proving what that allele does to TARS2 catalysis. (zhang2024tars2c.470c pages 2-4, zhang2024tars2c.470c pages 4-6, zhang2024tars2c.470c pages 1-2)
Other experimental implications. In human cells, S-nitrosation of mtThrRS was detectable, and experimental nitrosative stress reduced its aminoacylation and editing activities; this identifies a potential regulatory mechanism, not an established treatment target. A lung-adenocarcinoma study associated higher TARS2 expression with poorer survival and found that knockdown suppressed proliferation and xenograft growth. The 2024 expert review explicitly notes that the lung-cancer experiments did not test whether mTORC1 signaling mediated those effects. Neither observation changes mitochondrial tRNA charging and proofreading as the best-established primary function. (zheng2020nitrosativestressinhibits pages 1-2, barai2024beyondproteinsynthesis pages 6-8)
The following evidence map separates direct biochemical findings, disease-model results and more qualified interpretations:
| Process/site | TARS2-specific experimental result and representative data | Evidence level | Citation |
|---|---|---|---|
| Mitochondrial tRNA^Thr charging | Purified human mitochondrial ThrRS activated threonine and charged mitochondrial tRNA^Thr(UGU). It discriminated threonine over serine by 383-fold; G35C or U36C abolished charging, whereas A73C partially reduced it. | Direct human in-vitro biochemistry and tRNA identity-element mutagenesis | (wang2016ahumandiseasecausing pages 5-6, wang2016ahumandiseasecausing media 18f44078) |
| Translational proofreading | Human TARS2 can misactivate serine. Mutating editing-site His133/His137 eliminated deacylation of Ser-tRNA^Thr and increased mischarging, establishing post-transfer editing as the critical final safeguard. | Direct human enzyme mutagenesis and biochemical assays | (wang2016ahumandiseasecausing pages 6-8) |
| Editing fidelity in vivo | Disabling the corresponding mouse Tars2 editing residues caused Ser-tRNA^Thr accumulation and Thr→Ser mistranslation, impaired mitochondrial translation/OXPHOS, increased ROS, and induced G0/G1 arrest. Heart-restricted editing deficiency produced contractile dysfunction, dilated cardiomyopathy, and fibrosis. | 2023 primary study using mammalian cells and a genetically engineered mouse model | (zheng2023mammalianmitochondrialtranslation pages 1-2) |
| Mitochondrial localization and RNA granules | TARS2 is synthesized as a nuclear-encoded precursor with an N-terminal targeting sequence and imported into mitochondria. Native mitochondrial ThrRS formed foci that colocalized with the mitochondrial RNA-granule marker GRSF1; deleting its C-terminal tRNA-binding region markedly reduced enrichment at GRSF1 foci. | Human-cell localization, microscopy, and domain-deletion evidence | (wang2016ahumandiseasecausing pages 4-5, peng2022rnagranuleclusteredmitochondrial pages 5-6, peng2022rnagranuleclusteredmitochondrial pages 6-7) |
| Cytosolic pool | A 2023 review reports that approximately 10–15% of TARS2 is cytosolic. This estimate should not be interpreted as showing that 10–15% is lysosomal; no quantitative lysosome-versus-mitochondrion partition was established in the cited excerpt. | Secondary-source estimate; compartmental interpretation limited | (tyynismaa2023diseasemodelsof pages 2-3) |
| Threonine-sensitive Rag–mTORC1 signaling | TARS2 residues 301–381 mediate Rag interaction. Four disease variants in this region had reduced abundance (38.9–65.6% of wild type) and reduced normalized binding to RagA (41.3–48.2%) and RagC (20.4–50.5%), supporting impaired amino-acid-dependent mTORC1 activation. | 2023 human-cell co-immunoprecipitation and disease-variant analysis; lower protein stability is a potential confounder | (accogli2023clinicalneuroradiologicaland pages 10-11) |
| Developmental and mTORC1-related effects | Zebrafish tars2 knockdown caused reduced head/cerebellar size, cardiac edema, apoptosis, impaired myelination, and muscle abnormalities; wild-type human TARS2 mRNA rescued major phenotypes. PGC1α decreased and PPARα increased, consistent with altered mTORC1-regulated signaling. | 2023 in-vivo morpholino/rescue model; supportive rather than definitive human-pathway proof | (accogli2023clinicalneuroradiologicaland pages 10-11) |
| Human recessive disease burden | In a 2023 cohort, 18 new individuals from 15 families carried biallelic TARS2 variants. Across the expanded series, axial hypotonia occurred in 24/27, elevated lactate in 17/20, seizures in 14/28, and cerebellar atrophy in 75% of those assessed. | Multicenter human genetic/clinical study with functional variant testing | (accogli2023clinicalneuroradiologicaland pages 11-12, accogli2023clinicalneuroradiologicaland pages 1-3) |
| 2024 founder-allele development | Four affected individuals from three unrelated Chinese families carried biallelic TARS2 variants. c.470C>G (p.Thr157Arg) recurred in six Chinese cases; its estimated frequency was 3/251,430 East-Asian gnomAD alleles and 1.8 per 10,000 in a Chinese testing database. Direct functional testing of this allele was not reported. | 2024 clinical-genetic founder study; recurrence and population evidence, not biochemical validation | (zhang2024tars2c.470c pages 2-4, zhang2024tars2c.470c pages 4-6, zhang2024tars2c.470c pages 1-2) |
Table: Concise evidence map for human TARS2 covering mitochondrial tRNA charging and proofreading, subcellular localization, Rag–mTORC1 signaling, animal models, and recent human genetic findings. It distinguishes direct experiments from secondary interpretations and clinical association evidence.
Functional-annotation conclusion: Human TARS2/Q9BW92 is primarily a mitochondrial, class-II threonyl-tRNA synthetase that uses threonine and ATP to charge mitochondrial tRNA^Thr and edits erroneous serine charging. Its experimentally supported consequences are accurate mitochondrial translation and maintenance of OXPHOS; threonine-responsive Rag–mTORC1 signaling is an additional, mechanistically less fully resolved role. (wang2016ahumandiseasecausing pages 1-2, wang2016ahumandiseasecausing pages 5-6, zheng2023mammalianmitochondrialtranslation pages 1-2, barai2024beyondproteinsynthesis pages 4-6)
References
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(wang2016ahumandiseasecausing pages 5-6): Yong Wang, Xiao-Long Zhou, Zhi-Rong Ruan, Ru-Juan Liu, Gilbert Eriani, and En-Duo Wang. A human disease-causing point mutation in mitochondrial threonyl-trna synthetase induces both structural and functional defects. Journal of Biological Chemistry, 291:6507-6520, Mar 2016. URL: https://doi.org/10.1074/jbc.m115.700849, doi:10.1074/jbc.m115.700849. This article has 52 citations and is from a domain leading peer-reviewed journal.
(wang2016ahumandiseasecausing media 18f44078): Yong Wang, Xiao-Long Zhou, Zhi-Rong Ruan, Ru-Juan Liu, Gilbert Eriani, and En-Duo Wang. A human disease-causing point mutation in mitochondrial threonyl-trna synthetase induces both structural and functional defects. Journal of Biological Chemistry, 291:6507-6520, Mar 2016. URL: https://doi.org/10.1074/jbc.m115.700849, doi:10.1074/jbc.m115.700849. This article has 52 citations and is from a domain leading peer-reviewed journal.
(wang2016ahumandiseasecausing pages 6-8): Yong Wang, Xiao-Long Zhou, Zhi-Rong Ruan, Ru-Juan Liu, Gilbert Eriani, and En-Duo Wang. A human disease-causing point mutation in mitochondrial threonyl-trna synthetase induces both structural and functional defects. Journal of Biological Chemistry, 291:6507-6520, Mar 2016. URL: https://doi.org/10.1074/jbc.m115.700849, doi:10.1074/jbc.m115.700849. This article has 52 citations and is from a domain leading peer-reviewed journal.
(wang2016ahumandiseasecausing pages 9-11): Yong Wang, Xiao-Long Zhou, Zhi-Rong Ruan, Ru-Juan Liu, Gilbert Eriani, and En-Duo Wang. A human disease-causing point mutation in mitochondrial threonyl-trna synthetase induces both structural and functional defects. Journal of Biological Chemistry, 291:6507-6520, Mar 2016. URL: https://doi.org/10.1074/jbc.m115.700849, doi:10.1074/jbc.m115.700849. This article has 52 citations and is from a domain leading peer-reviewed journal.
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(zheng2023mammalianmitochondrialtranslation pages 1-2): Wen-Qiang Zheng, Jian-Hui Zhang, Zi-Han Li, Xiuxiu Liu, Yong Zhang, Shuo Huang, Jinsong Li, Bin Zhou, Gilbert Eriani, En-Duo Wang, and Xiao-Long Zhou. Mammalian mitochondrial translation infidelity leads to oxidative stress–induced cell cycle arrest and cardiomyopathy. Proceedings of the National Academy of Sciences of the United States of America, Sep 2023. URL: https://doi.org/10.1073/pnas.2309714120, doi:10.1073/pnas.2309714120. This article has 40 citations and is from a highest quality peer-reviewed journal.
(accogli2023clinicalneuroradiologicaland pages 1-3): Andrea Accogli, Sheng-Jia Lin, Mariasavina Severino, Sung-Hoon Kim, Kevin Huang, Clarissa Rocca, Megan Landsverk, Maha S. Zaki, Almundher Al-Maawali, Varunvenkat M. Srinivasan, Khalid Al-Thihli, G. Bradly Schaefer, Monica Davis, Davide Tonduti, Chiara Doneda, Lara M. Marten, Chris Mühlhausen, Maria Gomez, Eleonora Lamantea, Rafael Mena, Mathilde Nizon, Vincent Procaccio, Amber Begtrup, Aida Telegrafi, Hong Cui, Heidi L. Schulz, Julia Mohr, Saskia Biskup, Mariana Amina Loos, Hilda Verónica Aráoz, Vincenzo Salpietro, Laura Davis Keppen, Manali Chitre, Cassidy Petree, Lucy Raymond, Julie Vogt, Lindsey B. Sawyer, Alice A. Basinger, Signe Vandal Pedersen, Toni S. Pearson, Dorothy K. Grange, Lokesh Lingappa, Paige McDunnah, Rita Horvath, Benjamin Cognè, Bertrand Isidor, Andreas Hahn, Karen W. Gripp, Seyed Mehdi Jafarnejad, Elsebet Østergaard, Carlos E. Prada, Daniele Ghezzi, Vykuntaraju K. Gowda, Robert W. Taylor, Nahum Sonenberg, Henry Houlden, Marie Sissler, Gaurav K. Varshney, and Reza Maroofian. Clinical, neuroradiological, and molecular characterization of mitochondrial threonyl-trna-synthetase (tars2)-related disorder. Genetics in Medicine, 25:100938, Nov 2023. URL: https://doi.org/10.1016/j.gim.2023.100938, doi:10.1016/j.gim.2023.100938. This article has 16 citations and is from a highest quality peer-reviewed journal.
(barai2024beyondproteinsynthesis pages 4-6): Pallob Barai and Jie Chen. Beyond protein synthesis: non-translational functions of threonyl-trna synthetases. Biochemical Society Transactions, 52:661-670, Mar 2024. URL: https://doi.org/10.1042/bst20230506, doi:10.1042/bst20230506. This article has 15 citations and is from a peer-reviewed journal.
(accogli2023clinicalneuroradiologicaland pages 10-11): Andrea Accogli, Sheng-Jia Lin, Mariasavina Severino, Sung-Hoon Kim, Kevin Huang, Clarissa Rocca, Megan Landsverk, Maha S. Zaki, Almundher Al-Maawali, Varunvenkat M. Srinivasan, Khalid Al-Thihli, G. Bradly Schaefer, Monica Davis, Davide Tonduti, Chiara Doneda, Lara M. Marten, Chris Mühlhausen, Maria Gomez, Eleonora Lamantea, Rafael Mena, Mathilde Nizon, Vincent Procaccio, Amber Begtrup, Aida Telegrafi, Hong Cui, Heidi L. Schulz, Julia Mohr, Saskia Biskup, Mariana Amina Loos, Hilda Verónica Aráoz, Vincenzo Salpietro, Laura Davis Keppen, Manali Chitre, Cassidy Petree, Lucy Raymond, Julie Vogt, Lindsey B. Sawyer, Alice A. Basinger, Signe Vandal Pedersen, Toni S. Pearson, Dorothy K. Grange, Lokesh Lingappa, Paige McDunnah, Rita Horvath, Benjamin Cognè, Bertrand Isidor, Andreas Hahn, Karen W. Gripp, Seyed Mehdi Jafarnejad, Elsebet Østergaard, Carlos E. Prada, Daniele Ghezzi, Vykuntaraju K. Gowda, Robert W. Taylor, Nahum Sonenberg, Henry Houlden, Marie Sissler, Gaurav K. Varshney, and Reza Maroofian. Clinical, neuroradiological, and molecular characterization of mitochondrial threonyl-trna-synthetase (tars2)-related disorder. Genetics in Medicine, 25:100938, Nov 2023. URL: https://doi.org/10.1016/j.gim.2023.100938, doi:10.1016/j.gim.2023.100938. This article has 16 citations and is from a highest quality peer-reviewed journal.
(tyynismaa2023diseasemodelsof pages 2-3): Henna Tyynismaa. Disease models of mitochondrial aminoacyl‐
(accogli2023clinicalneuroradiologicaland pages 11-12): Andrea Accogli, Sheng-Jia Lin, Mariasavina Severino, Sung-Hoon Kim, Kevin Huang, Clarissa Rocca, Megan Landsverk, Maha S. Zaki, Almundher Al-Maawali, Varunvenkat M. Srinivasan, Khalid Al-Thihli, G. Bradly Schaefer, Monica Davis, Davide Tonduti, Chiara Doneda, Lara M. Marten, Chris Mühlhausen, Maria Gomez, Eleonora Lamantea, Rafael Mena, Mathilde Nizon, Vincent Procaccio, Amber Begtrup, Aida Telegrafi, Hong Cui, Heidi L. Schulz, Julia Mohr, Saskia Biskup, Mariana Amina Loos, Hilda Verónica Aráoz, Vincenzo Salpietro, Laura Davis Keppen, Manali Chitre, Cassidy Petree, Lucy Raymond, Julie Vogt, Lindsey B. Sawyer, Alice A. Basinger, Signe Vandal Pedersen, Toni S. Pearson, Dorothy K. Grange, Lokesh Lingappa, Paige McDunnah, Rita Horvath, Benjamin Cognè, Bertrand Isidor, Andreas Hahn, Karen W. Gripp, Seyed Mehdi Jafarnejad, Elsebet Østergaard, Carlos E. Prada, Daniele Ghezzi, Vykuntaraju K. Gowda, Robert W. Taylor, Nahum Sonenberg, Henry Houlden, Marie Sissler, Gaurav K. Varshney, and Reza Maroofian. Clinical, neuroradiological, and molecular characterization of mitochondrial threonyl-trna-synthetase (tars2)-related disorder. Genetics in Medicine, 25:100938, Nov 2023. URL: https://doi.org/10.1016/j.gim.2023.100938, doi:10.1016/j.gim.2023.100938. This article has 16 citations and is from a highest quality peer-reviewed journal.
(accogli2023clinicalneuroradiologicaland pages 8-10): Andrea Accogli, Sheng-Jia Lin, Mariasavina Severino, Sung-Hoon Kim, Kevin Huang, Clarissa Rocca, Megan Landsverk, Maha S. Zaki, Almundher Al-Maawali, Varunvenkat M. Srinivasan, Khalid Al-Thihli, G. Bradly Schaefer, Monica Davis, Davide Tonduti, Chiara Doneda, Lara M. Marten, Chris Mühlhausen, Maria Gomez, Eleonora Lamantea, Rafael Mena, Mathilde Nizon, Vincent Procaccio, Amber Begtrup, Aida Telegrafi, Hong Cui, Heidi L. Schulz, Julia Mohr, Saskia Biskup, Mariana Amina Loos, Hilda Verónica Aráoz, Vincenzo Salpietro, Laura Davis Keppen, Manali Chitre, Cassidy Petree, Lucy Raymond, Julie Vogt, Lindsey B. Sawyer, Alice A. Basinger, Signe Vandal Pedersen, Toni S. Pearson, Dorothy K. Grange, Lokesh Lingappa, Paige McDunnah, Rita Horvath, Benjamin Cognè, Bertrand Isidor, Andreas Hahn, Karen W. Gripp, Seyed Mehdi Jafarnejad, Elsebet Østergaard, Carlos E. Prada, Daniele Ghezzi, Vykuntaraju K. Gowda, Robert W. Taylor, Nahum Sonenberg, Henry Houlden, Marie Sissler, Gaurav K. Varshney, and Reza Maroofian. Clinical, neuroradiological, and molecular characterization of mitochondrial threonyl-trna-synthetase (tars2)-related disorder. Genetics in Medicine, 25:100938, Nov 2023. URL: https://doi.org/10.1016/j.gim.2023.100938, doi:10.1016/j.gim.2023.100938. This article has 16 citations and is from a highest quality peer-reviewed journal.
(zhang2024tars2c.470c pages 2-4): Shujie Zhang, Haisong Qin, Qingming Wang, Yingfei Wang, Yanhui Liu, Qi Yang, Jingsi Luo, Zailong Qin, Xiang Ji, Lijuan Kan, Guoxing Geng, Jing Huang, Shengkai Wei, Qiuli Chen, Yiping Shen, Haiming Yuan, and Baoling Lai. Tars2 c.470 c > g is a chinese-specific founder mutation in three unrelated families with mitochondrial encephalomyopathy. Orphanet Journal of Rare Diseases, Oct 2024. URL: https://doi.org/10.1186/s13023-024-03365-w, doi:10.1186/s13023-024-03365-w. This article has 3 citations and is from a peer-reviewed journal.
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