Affinage

TRMT10C

tRNA methyltransferase 10 homolog C · UniProt Q7L0Y3

Length
403 aa
Mass
47.3 kDa
Annotated
2026-06-10
48 papers in source corpus 24 papers cited in narrative 24 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

TRMT10C (MRPP1) is a SPOUT-domain methyltransferase that serves as the structural and catalytic core of mitochondrial tRNA maturation, partnering with SDR5C1 (MRPP2) to form a tRNA-binding subcomplex and, upon recruitment of the endonuclease PRORP (MRPP3), the three-subunit mitochondrial RNase P that processes the 5' ends of mt-tRNA precursors and is essential for mitochondrial translation and respiration (PMID:34489609, PMID:21857155). The TRMT10C C-terminal SPOUT fold binds SAM and catalyzes N1-methylation of purine 9 of mt-tRNAs, while its N-terminus mediates tRNA binding and self-association; the TRMT10C-SDR5C1 N1-methylation subcomplex assembles constitutively, but full RNase P assembles only in the presence of precursor tRNA (PMID:29880640). Cryo-EM and kinetic analyses establish that TRMT10C-SDR5C1 engages the entire tRNA, including the anticodon loop, and directs and activates PRORP's nuclease domain to the correct cleavage site through an induced-fit measuring mechanism, compensating for the eroded canonical features of structurally degenerate mt-tRNAs (PMID:34489609, PMID:37779095, PMID:41261864). Beyond 5'-processing, TRMT10C-SDR5C1 functions as a sequential maturation platform: it retains tRNA after RNase P cleavage to enhance ELAC2-catalyzed 3'-processing—especially for noncanonical mt-tRNAs whose maturation depends on direct ELAC2-TRMT10C protein-protein contacts rather than ELAC2-RNA contacts—thereby enforcing the 5'-to-3' processing order, and then presents the nascent tRNA to the CCA-adding enzyme (PMID:29040705, PMID:39516281, PMID:39747487). TRMT10C protein stability depends on SDR5C1, and disruption of the complex by mutations in TRMT10C or SDR5C1 impairs mt-tRNA processing and mitochondrial protein synthesis (PMID:27132592, PMID:24549042). Missense variants in TRMT10C cause a mitochondrial disorder, acting by destabilizing MRPP1 protein and impairing mt-RNA processing without affecting methyltransferase activity, a defect rescued by wild-type TRMT10C (PMID:27132592).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 2011 High

    Established that TRMT10C is functionally required for mitochondrial tRNA 5'-end processing and downstream translation, defining its essential role in mitochondrial gene expression.

    Evidence siRNA knockdown with deep sequencing of transcript ends, Northern blotting, and mitochondrial translation/respiration assays

    PMID:21857155 PMID:22028365

    Open questions at the time
    • Did not resolve the molecular architecture of the processing complex
    • Methyltransferase catalytic contribution not separated from processing role
  2. 2014 Medium

    Showed that TRMT10C protein levels depend on its partner SDR5C1, revealing an obligate stability dependence within the methylation subcomplex.

    Evidence HSD10/SDR5C1 siRNA knockdown plus ectopic rescue with Western blotting and precursor tRNA RT-PCR

    PMID:24549042

    Open questions at the time
    • Structural basis of the stabilizing interaction not defined
    • Whether stability loss fully accounts for processing defects unclear
  3. 2015 High

    Defined the reciprocal TRMT10C-SDR5C1 interaction and showed disease mutations in SDR5C1 disrupt tetramerization and complex formation, linking complex integrity to RNase P activity.

    Evidence Recombinant mutant protein biochemistry, co-immunoprecipitation, methyltransferase and processing assays; plus PRORP crystal structure showing a non-productive active site

    PMID:25925575 PMID:25953853

    Open questions at the time
    • Induced-fit activation of PRORP was structural inference, not directly visualized
    • Order of assembly events not fully resolved
  4. 2016 High

    Demonstrated TRMT10C is a human disease gene, with missense variants causing mitochondrial dysfunction via protein destabilization independent of methyltransferase activity.

    Evidence Patient fibroblast functional studies, lentiviral wild-type rescue, Northern blotting, mitochondrial protein synthesis assays; Drosophila ortholog Roswell loss-of-function in vivo

    PMID:27131785 PMID:27132592

    Open questions at the time
    • Phenotypic spectrum of TRMT10C mutations not fully mapped
    • Why methylation activity is dispensable for the disease mechanism not resolved
  5. 2017 High

    Reframed TRMT10C-SDR5C1 from a single-step enzyme to a sequential maturation platform that hands off tRNA between 5'-processing, 3'-processing, and CCA addition.

    Evidence In vitro reconstitution with purified proteins and 22 mitochondrial tRNA substrates, sequential enzyme assays

    PMID:29040705

    Open questions at the time
    • Structural basis for tRNA retention and handoff not yet defined
    • Why 5 of 22 tRNAs were not enhanced unexplained
  6. 2018 High

    Mapped TRMT10C domain functions, assigning tRNA binding and self-interaction to the N-terminus and SAM binding/N1-methylation to the C-terminal SPOUT fold, and showed full RNase P assembles only on precursor tRNA.

    Evidence X-ray crystallography, SAXS, interaction and activity assays

    PMID:29880640

    Open questions at the time
    • Conformational changes during PRORP recruitment not captured
    • Substrate-induced assembly mechanism not visualized at high resolution
  7. 2021 High

    Provided the high-resolution structural mechanism of substrate recognition, showing how TRMT10C-SDR5C1 binds the full tRNA and recruits/activates PRORP for precise cleavage.

    Evidence Cryo-EM structure of human mtRNase P bound to precursor tRNA with functional validation

    PMID:34489609

    Open questions at the time
    • Dynamics of the induced-fit transition not directly observed
    • Did not address 3'-processing handoff structurally
  8. 2023 High

    Quantitatively defined the division of labor, showing PRORP alone binds and cleaves some pre-tRNAs while TRMT10C-SDR5C1 chiefly enforces cleavage-site accuracy and rate, compensating for eroded mt-tRNA features.

    Evidence Kinetic analysis with 12 mitochondrial pre-tRNA substrates and multiple protein combinations

    PMID:31455609 PMID:33380464 PMID:37779095

    Open questions at the time
    • Determinants of substrate-specific dependence on the subcomplex incompletely defined
    • How disease-mutant tRNAs evade processing structurally unresolved
  9. 2024 High

    Extended TRMT10C-SDR5C1 into the 3'-processing complex, with cryo-EM structures of the ELAC2/SDR5C1/TRMT10C assembly explaining the 5'-to-3' processing order and noncanonical tRNA maturation via direct ELAC2-TRMT10C contacts.

    Evidence Cryo-EM of ELAC2/SDR5C1/TRMT10C-tRNA complexes plus biochemical processing assays; kinetic encasement analysis

    PMID:39516281 PMID:39747487 PMID:41261864

    Open questions at the time
    • How the platform coordinates the temporal transition between RNase P and ELAC2 not fully resolved
    • Coupling to CCA-adding enzyme not structurally captured
  10. 2024 Medium

    Identified upstream and regulatory inputs controlling TRMT10C abundance and complex assembly, including N6AMT1-dependent cytosolic translation and post-translational/micropeptide control of the subcomplex.

    Evidence N6AMT1 knockdown/translational profiling; MRPIP micropeptide interaction and mutagenesis; HSD17B10 succinylation proteomics and mutagenesis

    PMID:39038923 PMID:39503847 PMID:40513568

    Open questions at the time
    • Physiological conditions regulating these inputs unclear
    • Whether these regulatory layers operate in normal tissue not established
  11. 2025 Medium

    Reported context-dependent noncanonical roles for TRMT10C, including succinylation-controlled nuclear import driving m1A modification of nuclear-encoded mRNAs and elevated mitochondrial ND5 mRNA m1A in disease models.

    Evidence Subcellular fractionation, NLS mutagenesis, m1A-RIP, knockdown/overexpression rescue in coronary microembolization and Alzheimer's disease models

    PMID:38287100 PMID:40384859

    Open questions at the time
    • Nuclear/mRNA-modifying activity not independently confirmed beyond single disease-model studies
    • Relationship between canonical mitochondrial role and these moonlighting functions unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • How TRMT10C-SDR5C1 temporally coordinates the complete relay from 5'-processing through 3'-processing and CCA addition, and whether its reported nuclear mRNA-modifying functions occur under physiological conditions, remain open.
  • No integrated structural model spanning all sequential maturation steps
  • Nuclear localization and mRNA m1A roles rest on single-lab disease-model studies

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0016740 transferase activity 4 GO:0003723 RNA binding 3 GO:0098772 molecular function regulator activity 3 GO:0140098 catalytic activity, acting on RNA 3
Localization
GO:0005739 mitochondrion 2
Pathway
R-HSA-8953854 Metabolism of RNA 3 R-HSA-392499 Metabolism of proteins 2
Partners
ELAC2KPNA4N6AMT1P32PRORPSDR5C1
Complex memberships
TRMT10C-SDR5C1 N1-methylation subcomplexmitochondrial RNase P (TRMT10C-SDR5C1-PRORP)mitochondrial RNase Z complex (ELAC2-SDR5C1-TRMT10C)

Evidence

Reading pass · 24 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2021 Cryo-EM structure of human mtRNase P bound to precursor tRNA revealed that TRMT10C (MRPP1) and SDR5C1 (MRPP2) form a subcomplex that binds conserved mitochondrial tRNA elements including the anticodon loop, and positions the tRNA for methylation; PRORP (MRPP3) is then recruited and activated through interactions with its PPR and nuclease domains to ensure precise pre-tRNA cleavage. Cryo-EM structure determination with functional validation Nature structural & molecular biology High 34489609
2018 X-ray crystallography and SAXS analyses showed that the TRMT10C N-terminus is involved in tRNA binding and monomer-monomer self-interaction, while the C-terminal SPOUT fold contains key residues for SAM binding and N1-methylation. The entire TRMT10C interacts with MRPP2 (SDR5C1) to form the N1-methylation subcomplex, whereas the full MRPP1-MRPP2-MRPP3 RNase P complex assembles only in the presence of precursor tRNA. X-ray crystallography, SAXS, interaction assays, activity assays The Journal of biological chemistry High 29880640
2017 TRMT10C (MRPP1) and SDR5C1 (MRPP2) form a tRNA-maturation platform: the MRPP1/2 subcomplex retains the tRNA product after 5'-processing by RNase P, significantly enhances efficiency of ELAC2-catalyzed 3'-processing for 17 of 22 mitochondrial tRNAs, and then presents the nascent tRNA to the mitochondrial CCA-adding enzyme. In vitro reconstitution assays with purified proteins and mitochondrial tRNA substrates Nucleic acids research High 29040705
2016 Patients with TRMT10C missense variants (p.Arg181Leu and p.Thr272Ala) showed decreased MRPP1 protein levels and increased mt-RNA precursors indicative of impaired mt-RNA processing and defective mitochondrial protein synthesis; lentiviral transduction of wild-type TRMT10C rescued mt-RNA processing and mitochondrial protein synthesis defects. The variants affect MRPP1 protein stability and mt-tRNA processing without affecting m1R9 methyltransferase activity. Patient fibroblast functional studies, lentiviral rescue, Northern blotting, mitochondrial protein synthesis assay American journal of human genetics High 27132592
2015 TRMT10C interacts with SDR5C1 (MRPP2/HSD10); pathogenic SDR5C1 mutations disrupt homotetramerization of SDR5C1 and/or impair its interaction with TRMT10C, leading to impaired tRNA processing and methylation activities of the mtRNase P complex. Biochemical characterization of recombinant mutant proteins, co-immunoprecipitation, enzymatic activity assays Nucleic acids research High 25925575
2015 Crystal structure of the MRPP3 (PRORP) nuclease subunit showed a distorted, non-productive active site, leading to the proposed mechanism that PRORP switches to a productive state only upon association with MRPP1 (TRMT10C) and MRPP2 through an induced-fit process when pre-tRNA substrate is present. X-ray crystallography of MRPP3, structural analysis Nucleic acids research Medium 25953853
2011 MRPP1 (TRMT10C) is essential for mt-tRNA processing (5' end), RNA modification, translation, and mitochondrial respiration; MRPP1 and MRPP3 together process the 5' ends of tRNAs and the 5' non-tRNA-containing site of the CO1 transcript. Deep sequencing of transcript ends after siRNA knockdown, Northern blotting, mitochondrial translation assay Cell cycle High 21857155
2011 MRPP1 (TRMT10C) is required for the processing of mitochondrial long noncoding RNAs generated from the mitochondrial genome. Deep sequencing, Northern blotting, strand-specific qRT-PCR with MRPP1 knockdown RNA Medium 22028365
2014 HSD10 (SDR5C1/MRPP2) is required for maintaining normal MRPP1 (TRMT10C) protein levels; knockdown of HSD10 causes reduction in MRPP1 protein (but not MRPP3) and impairs processing of precursor tRNAs from the mitochondrial heavy strand. Ectopic expression of HSD10 restores MRPP1 levels and partially rescues RNA processing. siRNA knockdown, ectopic overexpression, Western blotting, patient fibroblast studies, RT-PCR of precursor tRNAs Human molecular genetics Medium 24549042
2019 Purified mtRNase P (TRMT10C/MRPP1, MRPP2, MRPP3) recognizes, cleaves, and methylates a subset but not all mitochondrial pre-tRNAs in vitro; addition of SAM (the TRMT10C cofactor) enhances binding and cleavage of some mitochondrial pre-tRNAs, and the presence of MRPP3 can enhance the methylation activity of the MRPP1/2 subcomplex. In vitro cleavage and methylation assays with purified recombinant mtRNase P components RNA Medium 31455609
2023 Kinetic analysis showed that PRORP (MRPP3) alone can bind pre-tRNAs with nanomolar affinity and cleave some at reduced efficiency without TRMT10C-SDR5C1. The main function of the TRMT10C-SDR5C1 subcomplex is to direct PRORP's nuclease domain to the correct cleavage site, increasing the rate and accuracy of cleavage, likely by compensating for structural erosion of canonical features in mitochondrial tRNAs. Kinetic analysis with purified recombinant proteins, 12 different mitochondrial pre-tRNA substrates Nucleic acids research High 37779095
2020 Disease-linked mutations in mitochondrial pre-tRNAIle, pre-tRNALeu(UUR), and pre-tRNAMet reduce MRPP1 (TRMT10C)-catalyzed methylation activity (up to ~90% reduction) and 5' end processing by mtRNase P; several mutations weaken pre-tRNA binding affinity (2- to 6-fold higher Ks than wild-type). In vitro methylation and cleavage assays with recombinant mtRNase P and disease-mutant pre-tRNA substrates, binding assays RNA Medium 33380464
2016 In Drosophila, the MRPP1 ortholog Roswell is essential for development, localizes to mitochondria, and its loss causes defective mitochondrial tRNA processing and mitochondrial dysfunction in vivo. Homology-based identification, genetic knockdown/overexpression, immunofluorescence localization, mitochondrial tRNA processing assays, lethality assay Nucleic acids research Medium 27131785
2017 Novel HSD17B10 missense mutations (p.V12L and p.V176M) reduce dehydrogenase, methyltransferase, and tRNA processing activities of the MRPP2-TRMT10C complex; p.V12L reduces SDR5C1 stability, while p.V176M impairs kinetics and complex formation with TRMT10C. Biochemical characterization of recombinant mutant proteins, enzymatic activity assays, complex formation assays Biochimica et biophysica acta. Molecular basis of disease Medium 28888424
2016 A novel HSD17B10 p.K212E mutation impairs SDR5C1-dependent mitochondrial RNase P activities (5'-processing and methylation of purine-9 of mitochondrial tRNAs), suggesting pathogenicity through general mitochondrial dysfunction caused by reduced maturation of mitochondrial tRNAs. Functional assays of mitochondrial RNase P activity in patient cells and in vitro with recombinant mutant protein RNA biology Medium 26950678
2024 Cryo-EM structures of the mitochondrial RNase Z complex (ELAC2/SDR5C1/TRMT10C) bound to mitochondrial tRNAHis revealed that TRMT10C-SDR5C1 participates in the 3'-processing complex and provides the molecular rationale for the 5'-to-3' tRNA processing order in mitochondria. Cryo-EM structure determination of the ELAC2/SDR5C1/TRMT10C complex with tRNA substrate The EMBO journal High 39516281
2025 TRMT10C and SDR5C1 specifically facilitate ELAC2-mediated 3'-end processing of structurally degenerate mitochondrial tRNAs lacking the canonical elbow; processing of noncanonical mt-tRNAs depends on direct protein-protein interactions between ELAC2 and TRMT10C rather than direct ELAC2-RNA contacts. This identifies TRMT10C-SDR5C1 as a mitochondrial tRNA maturation platform that compensates for structural erosion of mt-tRNAs. Cryo-EM structures of ELAC2 in complex with TRMT10C, SDR5C1, and divergent mt-tRNA substrates; biochemical processing assays Nature structural & molecular biology High 39747487
2025 Kinetic analysis showed that TRMT10C-SDR5C1 encases the entire tRNA substrate; mtRNase P processes pre-tRNAs more efficiently with longer 5' extensions and uses a rigid measuring mechanism for cleavage-site selection. Without interactions with the pre-tRNA, TRMT10C-SDR5C1 cannot stimulate cleavage by PRORP, explaining the complex's inability to process D-armless mitochondrial tRNASer(AGY). Kinetic analysis with substrate and protein variants, cleavage assays with multiple mitochondrial pre-tRNAs Nucleic acids research Medium 41261864
2024 N6AMT1 is required for cytosolic translation of TRMT10C (MRPP1) and PRORP (MRPP3); in the absence of N6AMT1, TRMT10C and PRORP protein levels decrease, RNA processing within mitochondria is impaired, leading to accumulation of unprocessed and double-stranded RNA, preventing mitochondrial protein synthesis. Translational profiling, N6AMT1 knockdown/knockout, Western blotting, mitochondrial RNA processing assays Proceedings of the National Academy of Sciences Medium 39503847
2013 MRPP1 (TRMT10C) co-immunoprecipitates with P32, a mitochondrial protein that also interacts with RNase H1, suggesting MRPP1 participates in a mitochondrial RNA processing complex. Co-immunoprecipitation PloS one Low 23990920
2025 A lncRNA-derived micropeptide MRPIP inhibits mtRNase P complex assembly by interacting with HSD17B10 (MRPP2/SDR5C1) at the R25 residue, disrupting HSD17B10 tetramerization and the subsequent HSD17B10-TRMT10C (MRPP1) subcomplex formation, leading to perturbed post-transcriptional RNA processing. Protein-protein interaction studies, site-directed mutagenesis, biochemical complex assembly assays Molecular cell Medium 40513568
2025 In the context of coronary microembolization, reduced succinylation of TRMT10C (at sites recognized by CPT1A) promotes KPNA4-mediated nuclear import via two NLS sequences (KAKR and KKK(X)10KVKK); nuclear TRMT10C then catalyzes m1A modifications on TAFAZZIN and NLRX1 mRNAs, leading to YTHDF2-mediated decay of these transcripts and consequent inflammation, ROS production, and suppression of mitophagy. Subcellular fractionation, nuclear localization signal mutagenesis, m1A-RIP, TRMT10C knockdown and CPT1A overexpression rescue experiments International journal of biological sciences Medium 40384859
2024 TRMT10C-mediated m1A methylation of ND5 mRNA is enhanced in an Alzheimer's disease cell model and in AD patients; increased TRMT10C protein levels cause m1A modification of ND5 mRNA leading to translation repression of ND5 and mitochondrial complex I dysfunction. m1A methylation mapping, TRMT10C overexpression, mitochondrial function assays, patient sample analysis Molecular psychiatry Medium 38287100
2024 HSD17B10 K99 succinylation (mediated by CPT1A) maintains mitochondrial RNase P stability; K99R mutation of HSD17B10 impairs its binding to TRMT10C (MRPP1), disrupts RNase P activity, and induces oxidative stress. ASIV treatment restores HSD17B10-TRMT10C interaction and RNase P activity. Succinylated proteomics, site-directed mutagenesis (K99R), co-immunoprecipitation, RNase P activity assay, molecular docking Phytotherapy research Medium 39038923

Source papers

Stage 0 corpus · 48 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2011 Long noncoding RNAs are generated from the mitochondrial genome and regulated by nuclear-encoded proteins. RNA (New York, N.Y.) 249 22028365
2011 RNA processing in human mitochondria. Cell cycle (Georgetown, Tex.) 201 21857155
2011 Involvement of human ELAC2 gene product in 3' end processing of mitochondrial tRNAs. RNA biology 168 21593607
2017 m1A Post-Transcriptional Modification in tRNAs. Biomolecules 152 28230814
2022 N1-methyladenosine modification in cancer biology: Current status and future perspectives. Computational and structural biotechnology journal 136 36467585
2016 Recessive Mutations in TRMT10C Cause Defects in Mitochondrial RNA Processing and Multiple Respiratory Chain Deficiencies. American journal of human genetics 86 27132592
2021 Structural basis of RNA processing by human mitochondrial RNase P. Nature structural & molecular biology 81 34489609
2017 The MRPP1/MRPP2 complex is a tRNA-maturation platform in human mitochondria. Nucleic acids research 62 29040705
2024 Research progress of N1-methyladenosine RNA modification in cancer. Cell communication and signaling : CCS 56 38291517
2022 Dysregulated mitochondrial and cytosolic tRNA m1A methylation in Alzheimer's disease. Human molecular genetics 56 34897434
2020 Functional characterization of the human tRNA methyltransferases TRMT10A and TRMT10B. Nucleic acids research 55 32392304
2015 Molecular insights into HSD10 disease: impact of SDR5C1 mutations on the human mitochondrial RNase P complex. Nucleic acids research 54 25925575
2014 Mutation or knock-down of 17β-hydroxysteroid dehydrogenase type 10 cause loss of MRPP1 and impaired processing of mitochondrial heavy strand transcripts. Human molecular genetics 53 24549042
2015 Structure of the nuclease subunit of human mitochondrial RNase P. Nucleic acids research 50 25953853
2021 Bi-allelic variants in the mitochondrial RNase P subunit PRORP cause mitochondrial tRNA processing defects and pleiotropic multisystem presentations. American journal of human genetics 46 34715011
2013 Human RNase H1 is associated with protein P32 and is involved in mitochondrial pre-rRNA processing. PloS one 45 23990920
2016 A novel HSD17B10 mutation impairing the activities of the mitochondrial RNase P complex causes X-linked intractable epilepsy and neurodevelopmental regression. RNA biology 40 26950678
2017 Novel patient missense mutations in the HSD17B10 gene affect dehydrogenase and mitochondrial tRNA modification functions of the encoded protein. Biochimica et biophysica acta. Molecular basis of disease 38 28888424
2024 N1-methylation of adenosine (m1A) in ND5 mRNA leads to complex I dysfunction in Alzheimer's disease. Molecular psychiatry 32 38287100
2018 Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. The Journal of biological chemistry 32 29880640
2024 Advances in the Structural and Functional Understanding of m1A RNA Modification. Accounts of chemical research 24 38331425
2016 Loss of the mitochondrial protein-only ribonuclease P complex causes aberrant tRNA processing and lethality in Drosophila. Nucleic acids research 23 27131785
2019 Interplay between substrate recognition, 5' end tRNA processing and methylation activity of human mitochondrial RNase P. RNA (New York, N.Y.) 21 31455609
2023 Cleavage kinetics of human mitochondrial RNase P and contribution of its non-nuclease subunits. Nucleic acids research 17 37779095
2024 Structural basis of 3'-tRNA maturation by the human mitochondrial RNase Z complex. The EMBO journal 15 39516281
2025 Molecular basis of human nuclear and mitochondrial tRNA 3' processing. Nature structural & molecular biology 14 39747487
2024 Astragaloside IV protects renal tubular epithelial cells against oxidative stress-induced injury by upregulating CPT1A-mediated HSD17B10 lysine succinylation in diabetic kidney disease. Phytotherapy research : PTR 14 39038923
2020 Disease-associated mutations in mitochondrial precursor tRNAs affect binding, m1R9 methylation, and tRNA processing by mtRNase P. RNA (New York, N.Y.) 14 33380464
2024 Mitochondrial S-adenosylmethionine deficiency induces mitochondrial unfolded protein response and extends lifespan in Caenorhabditis elegans. Aging cell 10 38361361
2024 TRMT10C-mediated m7G modification of circFAM126A inhibits lung cancer growth by regulating cellular glycolysis. Cell biology and toxicology 10 39289194
2025 De-succinylation-induced accumulation of TRMT10C in the nucleus plays a detrimental role in coronary microembolization via its m1A modification function. International journal of biological sciences 8 40384859
2024 Cytosolic N6AMT1-dependent translation supports mitochondrial RNA processing. Proceedings of the National Academy of Sciences of the United States of America 7 39503847
2025 Hepatic micropeptide modulates mitochondrial RNA processing machinery in hepatocellular carcinoma. Molecular cell 6 40513568
2025 Genetic variants of m1A modification genes and the risk of neuroblastoma: novel insights from a Chinese case-control study. Human genomics 5 40340897
2025 Increased S-adenosyl methionine strengthens the suppression in mitochondrial unfolded protein response induced by 6-PPD quinone at environmentally relevant concentrations in Caenorhabditis elegans. Environmental pollution (Barking, Essex : 1987) 4 41072709
2024 Single-cell transcriptomics reveals writers of RNA modification-mediated immune microenvironment and cardiac resident Macro-MYL2 macrophages in heart failure. BMC cardiovascular disorders 4 39152369
2024 Mitochondrial Genome-Encoded Long Noncoding RNA Cytochrome B (LncCytB) and Mitochondrial Ribonucleases in Diabetic Retinopathy. Biomedicines 4 39200102
2024 TRMT10C gene polymorphisms confer hepatoblastoma susceptibility: evidence from a seven-center case-control study. Journal of Cancer 4 39247598
2022 Reduction of Drosophila Mitochondrial RNase P in Skeletal and Heart Muscle Causes Muscle Degeneration, Cardiomyopathy, and Heart Arrhythmia. Frontiers in cell and developmental biology 4 35663400
2016 17β-Hydroxysteroid dehydrogenase type 10 predicts survival of patients with colorectal cancer and affects mitochondrial DNA content. Cancer letters 4 26884257
2025 Identification of mitochondrial-related causal genes for major depression disorder via integrating multi-omics. Journal of affective disorders 3 40274126
2026 Disulfiram-induced c-FOS influences lipid metabolism and angiogenesis in hepatocellular carcinoma. Science China. Life sciences 2 41557108
2024 The protein-only RNase Ps, endonucleases that cleave pre-tRNA: Biological relevance, molecular architectures, substrate recognition and specificity, and protein interactomes. Wiley interdisciplinary reviews. RNA 2 38453211
2026 tsRNA-10547 generated by m1A modification-mediated tRNA shearing promotes colorectal cancer metastasis via suppressing CHRNA9. Archives of biochemistry and biophysics 0 42142645
2025 Comprehensive Analysis of RNA Modifications Related Genes in the Diagnosis and Subtype Classification of Dilated Cardiomyopathy. Journal of inflammation research 0 40395552
2025 RNase P generated tRFSer-GCT promotes fat storage in adipocytes via Adrb2 signaling. The Journal of biological chemistry 0 41101502
2025 Association of genetic variants in m1A modification core genes and neuroblastoma risk. BMC cancer 0 41107791
2025 Substrate and enzyme determinants for recognition by human mitochondrial RNase P. Nucleic acids research 0 41261864

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