The mitochondrial myopathy, encephalopathy, lactic acidosis, and stroke-like episode syndrome-associated human mitochondrial tRNALeu(UUR) mutation causes aminoacylation deficiency and concomitant reduced association of mRNA with ribosomes

[57] Sequencing end-labeled DNA with base-specific chemical cleavages

Maxam, A. M., & Gilbert, W. (1980) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(80)65059-9 · Cited by 14,678 · see citing works

A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity

(1984) · Analytical Biochemistry · doi:10.1016/0003-2697(84)90381-6 · Cited by 4,950 · see citing works

A mutation in the tRNALeu(UUR) gene associated with the MELAS subgroup of mitochondrial encephalomyopathies

Goto, Y.-I., Nonaka, I., & Horai, S. (1990) · Nature · doi:10.1038/348651a0 · Cited by 2,070 · see citing works

Human Cells Lacking mtDNA: Repopulation with Exogenous Mitochondria by Complementation

King, M. P., & Attardi, G. M. (1989) · Science · doi:10.1126/science.2814477 · Cited by 1,659 · see citing works

Myoclonic epilepsy and ragged-red fiber disease (MERRF) is associated with a mitochondrial DNA tRNALys mutation

Shoffner, J. M., Lott, M. T., Lezza, A. M. S., Seibel, P., Ballinger, S. W., & Wallace, D. C. (1990) · Cell · doi:10.1016/0092-8674(90)90059-n · Cited by 1,468 · see citing works

Human cells lacking mtDNA: repopulation with exogenous mitochondria by complementation

(1990) · Trends in Genetics · doi:10.1016/0168-9525(90)90040-d · Cited by 1,386 · see citing works

Mutation in mitochondrial tRNALeu(UUR) gene in a large pedigree with maternally transmitted type II diabetes mellitus and deafness

van den Ouweland, J. M. W., Lemkes, H. H. P. J., Ruitenbeek, W., Sandkuijl, L. A., de Vijlder, M. F., Struyvenberg, P. A. A., van de Kamp, J. J. P., & Maassen, J. A. (1992) · Nature Genetics · doi:10.1038/ng0892-368 · Cited by 1,127 · see citing works

MELAS mutation in mtDNA binding site for transcription termination factor causes defects in protein synthesis and in respiration but no change in levels of upstream and downstream mature transcripts.

Chomyn, A., Martinuzzi, A., Yoneda, M., Daga, A., Hurko, O., Johns, D. R., Lai, S. T., Nonaka, I., Angelini, C. I., & Attardi, G. M. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.10.4221 · Cited by 491 · see citing works

Defects in mitochondrial protein synthesis and respiratory chain activity segregate with the tRNA(Leu(UUR)) mutation associated with mitochondrial myopathy, encephalopathy, lactic acidosis, and strokelike episodes

King, M. P., Koga, Y., Davidson, M., & Schon, E. A. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.2.480 · Cited by 458 · see citing works

Mitochondrial DNA Mutations and Pathogenesis

Schon, E. A., Bonilla, E., & DiMauro, S. (1997) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1022685929755 · Cited by 421 · see citing works

An operational RNA code for amino acids and possible relationship to genetic code.

SCHIMMEL, P. R., Giegé, R., Moras, D., & Yokoyama, S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.19.8763 · Cited by 418 · see citing works

Direct analysis of aminoacylation levels of tRNAs in vivo. Application to studying recognition of Escherichia coli initiator tRNA mutants by glutaminyl-tRNA synthetase.

Varshney, U., Lee, C. P., & RajBhandary, U. L. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54288-5 · Cited by 404 · see citing works

Termination of transcription in human mitochondria: Identification and purification of a DNA binding protein factor that promotes termination

Kruse, B., Narasimhan, N., & Attardi, G. M. (1989) · Cell · doi:10.1016/0092-8674(89)90853-2 · Cited by 311 · see citing works

In Vitro Genetic Transfer of Protein Synthesis and Respiration Defects to Mitochondrial DNA-Less Cells with Myopathy-Patient Mitochondria

Chomyn, A., Meola, G., Bresolin, N., Lai, S. T., Scarlato, G., & Attardi, G. M. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.4.2236 · Cited by 301 · see citing works

Marked replicative advantage of human mtDNA carrying a point mutation that causes the MELAS encephalomyopathy.

Yoneda, M., Chomyn, A., Martinuzzi, A., Hurko, O., & Attardi, G. M. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.23.11164 · Cited by 291 · see citing works

MtDNA mutation in MERRF syndrome causes defective aminoacylation of tRNALys and premature translation termination

Enriquez, J. A., Chomyn, A., & Attardi, G. (1995) · Nature Genetics · doi:10.1038/ng0595-47 · Cited by 285 · see citing works

Modification Defect at Anticodon Wobble Nucleotide of Mitochondrial tRNAsLeu(UUR) with Pathogenic Mutations of Mitochondrial Myopathy, Encephalopathy, Lactic Acidosis, and Stroke-like Episodes

Yasukawa, T., Suzuki, T., Suzuki, T., Ueda, T., Ohta, S., & Watanabe, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.6.4251 · Cited by 268 · see citing works

A novel mitochondrial point mutation in a maternal pedigree with sensorineural deafness

Reid, F. M., Vernham, G. A., & Jacobs, H. T. (1994) · Human Mutation · doi:10.1002/humu.1380030311 · Cited by 266 · see citing works

Phosphorylation of eukaryotic initiation factor 2 during physiological stresses which affect protein synthesis.

Scorsone, K. A., Panniers, R., Rowlands, A., & Henshaw, E. C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47829-5 · Cited by 254 · see citing works

tRNA IDENTITY

Normanly, J., & Abelson, J. N. (1989) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.58.070189.005121 · Cited by 242 · see citing works

Impairment of mitochondrial transcription termination by a point mutation associated with the MELAS subgroup of mitochondrial encephalomyopathies

Hess, J. F., Parisi, M. A., Bennett, J. L., & Clayton, D. A. (1991) · Nature · doi:10.1038/351236a0 · Cited by 234 · see citing works

A protein complex mediating mRNA degradation in Escherichia coli

Py, B., Causton, H. C., Mudd, E. A., & Higgins, C. F. (1994) · Molecular Microbiology · doi:10.1111/j.1365-2958.1994.tb01309.x · Cited by 225 · see citing works

Relaxation of a transfer RNA specificity by removal of modified nucleotides

Perret, V., Garcia-Brugger, A., Grosjean, H., Ebel, J., Florentz, C., & Giegé, R. (1990) · Nature · doi:10.1038/344787a0 · Cited by 214 · see citing works

[18] In vivo labeling and analysis of human mitochondrial translation products

Chomyn, A. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)64020-8 · Cited by 207 · see citing works

The mtDNA‐encoded ND6 subunit of mitochondrial NADH dehydrogenase is essential for the assembly of the membrane arm and the respiratory function of the enzyme

Bai, Y., & Attardi, G. M. (1998) · The EMBO Journal · doi:10.1093/emboj/17.16.4848 · Cited by 188 · see citing works

The Deafness-Associated Mitochondrial DNA Mutation at Position 7445, Which Affects tRNASer(UCN) Precursor Processing, Has Long-Range Effects on NADH Dehydrogenase Subunit ND6 Gene Expression

Guan, M., Enrı́quez, J. A., Fischel‐Ghodsian, N., Puranam, R. S., Lin, C. P., Maw, M. A., & Attardi, G. M. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.10.5868 · Cited by 187 · see citing works

The Transfer RNA Identity Problem: a Search for Rules

Saks, M. E., Sampson, J. R., & Abelson, J. N. (1994) · Science · doi:10.1126/science.7506844 · Cited by 174 · see citing works

Chloroplast mRNA 3′‐end processing by a high molecular weight protein complex is regulated by nuclear encoded RNA binding proteins.

Hayes, R., Kudla, J., Schuster, G., Gabay, L., Maliga, P., & Gruissem, W. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00451.x · Cited by 171 · see citing works

Effects of deprival of glucose or individual amino acids on polyribosome distribution and rate of protein synthesis in cultured mammalian cells

van Venrooij, W. J. W., Henshaw, E. C., & Hirsch, C. A. (1972) · Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis · doi:10.1016/0005-2787(72)90480-7 · Cited by 132 · see citing works

Control of Initiation of Protein Synthesis in Human Cells

Vaughan, M. H., & Hansen, B. S. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43365-6 · Cited by 130 · see citing works

Mitochondrial mutation associated with nonsyndromic deafness

Fischel‐Ghodsian, N., Prezant, T. R., Fournier, P., Stewart, I. A., & Maw, M. A. (1995) · American Journal of Otolaryngology · doi:10.1016/0196-0709(95)90078-0 · Cited by 128 · see citing works

The DExH Box Protein Suv3p Is a Component of a Yeast Mitochondrial 3′-to-5′ Exoribonuclease That Suppresses Group I Intron Toxicity

Margossian, S. P., Li, H., Zassenhaus, H. P., & Butow, R. A. (1996) · Cell · doi:10.1016/s0092-8674(00)80975-7 · Cited by 119 · see citing works

Tight Control of Respiration by NADH Dehydrogenase ND5 Subunit Gene Expression in Mouse Mitochondria

Bai, Y., Shakeley, R. M., & Attardi, G. M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.3.805-815.2000 · Cited by 115 · see citing works

The General Occurrence of 55 S Ribosomes in Mammalian Liver Mitochondria

O’Brien, T. W. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62239-2 · Cited by 108 · see citing works

Complex I deficiency is Associated with 3243G:C Mitochondrial DNA in Osteosarcoma Cell Cybrids

Dunbar, D. R., Moonie, P., Zeviani, M., & Holt, I. J. (1996) · Human Molecular Genetics · doi:10.1093/hmg/5.1.123 · Cited by 107 · see citing works

Post-transcriptional regulation of the steady-state levels of mitochondrial tRNAs in HeLa cells

King, M. P., & Attardi, G. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82194-9 · Cited by 104 · see citing works

An unusual RNA tertiary interaction has a role for the specific aminoacylation of a transfer RNA.

Hou, Y., Westhof, É., & Giegé, R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.14.6776 · Cited by 102 · see citing works

A tRNA suppressor mutation in human mitochondria

Meziane, A. E., Lehtinen, S. K., Hance, N., Nijtmans, L. G. J., Dunbar, D. R., Holt, I. J., & Jacobs, H. T. (1998) · Nature Genetics · doi:10.1038/ng0498-350 · Cited by 101 · see citing works

Efficient Selection and Characterization of Mutants of a Human Cell Line Which are Defective in Mitochondrial DNA-Encoded Subunits of Respiratory NADH Dehydrogenase

Hofhaus, G., & Attardi, G. M. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.2.964 · Cited by 101 · see citing works

Search for differences in post-transcriptional modification patterns of mitochondrial DNA-encoded wild-type and mutant human tRNALys and tRNALeu(UUR)

Helm, M., Florentz, C., Chomyn, A., & Attardi, G. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.3.756 · Cited by 99 · see citing works

Pathophysiology of the MELAS 3243 Transition Mutation

Flierl, A., Reichmann, H., & Seibel, P. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.43.27189 · Cited by 90 · see citing works

Deficiency of subunits of complex I and mitochondrial encephalomyopathy

Ichiki, T., Tanaka, M., Nishikimi, M., Suzuki, H., Ozawa, T., Kobayashi, M., & Wada, Y. (1988) · Annals of Neurology · doi:10.1002/ana.410230312 · Cited by 90 · see citing works

The Diabetes-associated 3243 Mutation in the Mitochondrial tRNALeu(UUR) Gene Causes Severe Mitochondrial Dysfunction without a Strong Decrease in Protein Synthesis Rate

Janssen, G. M. C., Maassen, J. A., & van den Ouweland, J. M. W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.42.29744 · Cited by 86 · see citing works

The structures and functions of transfer RNA

Goddard, J. P. (1978) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(78)90021-4 · Cited by 82 · see citing works

The mitochondrial tRNALeu(UUR) mutation in MELAS: a model for pathogenesis

Schon, E. A., Koga, Y., Davidson, M. M., Moraes, C. T., & King, M. P. (1992) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(92)90226-r · Cited by 74 · see citing works

[17] Analysis of aminoacylation of human mitochondrial tRNAs

Enrı́quez, J. A., & Attardi, G. M. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)64019-1 · Cited by 73 · see citing works

‘Lipidic particles’ are intermembrane attachment sites

Hui, S. W., & Stewart, T. P. (1981) · Nature · doi:10.1038/290427a0 · Cited by 73 · see citing works

Two cases of NADH-coenzyme Q reductase deficiency: Relationship to MELAS syndrome

Kobayashi, M., Morishita, H., Sugiyama, N., Yokochi, K., Nakano, M., Wada, Y., Hotta, Y., Terauchi, A., & Nonaka, I. (1987) · The Journal of Pediatrics · doi:10.1016/s0022-3476(87)80158-0 · Cited by 72 · see citing works

Expression of the mitochondrial genome in HeLa cells

Ojala, D., & Attardi, G. M. (1972) · Journal of Molecular Biology · doi:10.1016/0022-2836(72)90282-3 · Cited by 63 · see citing works

Cloning and Sequence Analysis of the Human Mitochondrial Translational Initiation Factor 2 cDNA

Ma, L., & Spremulli, L. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.4.1859 · Cited by 50 · see citing works

Influence of tRNA tertiary structure and stability on aminoacylation by yeast aspartyl-tRNA synthetase

Puglisi, J. D., Pütz, J., Florentz, C., & Giegé, R. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.1.41 · Cited by 47 · see citing works

Production of Microcell Hybrids

Killary, A. M., & Lott, S. T. (1996) · Methods · doi:10.1006/meth.1996.0002 · Cited by 46 · see citing works

Fine mapping of mitochondrial RNAs derived from the mtDNA region containing a point mutation associated with MELAS

Koga, Y., Davidson, M. M., Schon, E. A., & King, M. P. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.3.657 · Cited by 44 · see citing works

Deficiency of subunits in heart mitochondrial NADH-ubiquinone oxidoreductase of a patient with mitochondrial encephalomyopathy and cardiomyopathy

Tanaka, M., Nishikimi, M., Suzuki, H., Ozawa, T., Nishizawa, M., Tanaka, K., & Miyatake, T. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(86)91061-2 · Cited by 41 · see citing works

Functional Analysis of in Vivo and in Organello Footprinting of HeLa Cell Mitochondrial DNA in Relationship to ATP and Ethidium Bromide Effects on Transcription

Micol, V., Fernández‐Silva, P., & Attardi, G. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.30.18896 · Cited by 38 · see citing works

Mitochondrial leucine tRNA mutation in neurological diseases

Johns, D., & Hurko, O. (1991) · The Lancet · doi:10.1016/0140-6736(91)90272-q · Cited by 29 · see citing works

Regulation of polypeptide chain initiation and activity of initiation factor eIF-2 in Chinese-hamster-ovary cell mutants containing temperature-sensitive aminoacyl-tRNA synthetases

Austin, S. A., Pollard, J. W., Jagus, R., & Clemens, M. J. (1986) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1986.tb09635.x · Cited by 25 · see citing works

Effect of rate-limiting elongation on bacteriophage MS2 RNA-directed protein synthesis in extracts of Escherichia coli

Goldman, E. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90252-2 · Cited by 25 · see citing works

Yeast tRNAMet recognition by methionyl-tRNA synthetase requires determinants from the primary, secondary and tertiary structure: a review

Senger, B., & Fasiolo, F. (1996) · Biochimie · doi:10.1016/s0300-9084(96)80006-x · Cited by 9 · see citing works

[1]In vivo footprinting of human mitochondrial DNA in cultured cell systems

Micol, V., Fernández‐Silva, P., & Peattardi, G. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)64003-8 · Cited by 3 · see citing works

Mitochondrial threshold effects

Rossignol, R., Faustin, B., Rocher, C., Malgat, M., Mazat, J., & Letellier, T. (2003) · Biochemical Journal · doi:10.1042/bj20021594 · Cited by 802 · see citing works

The genetics and pathology of oxidative phosphorylation

Smeitink, J. A. M., van den Heuvel, L., & DiMauro, S. (2001) · Nature Reviews Genetics · doi:10.1038/35072063 · Cited by 718 · see citing works

Mitochondrial DNA mutations and human disease

Tuppen, H. A. L., Blakely, E. L., Turnbull, D. M., & Taylor, R. W. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.09.005 · Cited by 676 · see citing works

MELAS syndrome: Clinical manifestations, pathogenesis, and treatment options

El‐Hattab, A. W., Adesina, A. M., Jones, J. Y., & Scaglia, F. (2015) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2015.06.004 · Cited by 612 · see citing works

Human Mitochondrial tRNAs: Biogenesis, Function, Structural Aspects, and Diseases

Suzuki, T., Nagao, A., & Suzuki, T. (2011) · Annual Review of Genetics · doi:10.1146/annurev-genet-110410-132531 · Cited by 554 · see citing works

Emerging roles of tRNA in adaptive translation, signalling dynamics and disease

Kirchner, S., & Ignatova, Z. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3861 · Cited by 524 · see citing works

Mitochondrial Diabetes

Maassen, J. A., ‘t Hart, L. M., van Essen, E., Heine, R. J., Nijpels, G., Jahangir Tafrechi, R. S., Raap, A. K., Janssen, G. M. C., & Lemkes, H. H. P. J. (2004) · Diabetes · doi:10.2337/diabetes.53.2007.s103 · Cited by 439 · see citing works

Codon-specific translational defect caused by a wobble modification deficiency in mutant tRNA from a human mitochondrial disease

Kirino, Y., Yasukawa, T., Ohta, S., Akira, S., Ishihara, K., Watanabe, K., & Suzuki, T. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405173101 · Cited by 288 · see citing works

Human mitochondrial tRNAs in health and disease

Florentz, C., Sohm, B., Tóth, P., P�tz, J., & Sissler, M. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-2343-1 · Cited by 249 · see citing works

Mitochondrial diseases: from molecular mechanisms to therapeutic advances

Wen, H., Deng, H., Li, B., Chen, J., Zhu, J., Zhang, X., Yoshida, S., & Zhou, Y. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02044-3 · Cited by 248 · see citing works

Mitochondrial Disease—Its Impact, Etiology, and Pathology

McFarland, R., Taylor, R. W., & Turnbull, D. M. (2007) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(06)77005-3 · Cited by 192 · see citing works

Specific correlation between the wobble modification deficiency in mutant tRNAs and the clinical features of a human mitochondrial disease

Kirino, Y., Goto, Y., Campos, Y., Arenas, J., & Suzuki, T. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500563102 · Cited by 168 · see citing works

The MTERF family proteins: Mitochondrial transcription regulators and beyond

Roberti, M., Polosa, P. L., Bruni, F., Manzari, C., Deceglie, S., Gadaleta, M. N., & Cantatore, P. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.01.013 · Cited by 166 · see citing works

Mitochondrial tRNA 3' end metabolism and human disease

Levinger, L. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh884 · Cited by 152 · see citing works

The A3243G tRNALeu(UUR) MELAS mutation causes amino acid misincorporation and a combined respiratory chain assembly defect partially suppressed by overexpression of EFTu and EFG2

Sasarman, F., Antonická, H., & Shoubridge, E. A. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn265 · Cited by 148 · see citing works

Molecular neuropathology of MELAS: level of heteroplasmy in individual neurones and evidence of extensive vascular involvement

Betts, J., Jaros, E., Perry, R. H., Schaefer, A. M., Taylor, R. W., Abdel‐All, Z., Lightowlers, R. N., & Turnbull, D. M. (2006) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2006.00731.x · Cited by 142 · see citing works

Human Mitochondrial Leucyl-tRNA Synthetase Corrects Mitochondrial Dysfunctions Due to the tRNA Leu(UUR) A3243G Mutation, Associated with Mitochondrial Encephalomyopathy, Lactic Acidosis, and Stroke-Like Symptoms and Diabetes

Li, R., & Guan, M. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01614-09 · Cited by 131 · see citing works

Mitochondrial DNA mutations in patients with postlingual, nonsyndromic hearing impairment

Jacobs, H. T., Hutchin, T. P., Käppi, T., Gillies, G., Minkkinen, K., Walker, J., Thompson, K., Rovio, A. T., Carella, M., Melchionda, S., et al. (2004) · European Journal of Human Genetics · doi:10.1038/sj.ejhg.5201250 · Cited by 128 · see citing works

Biochemical characterization of the mitochondrial tRNASer(UCN) T7511C mutation associated with nonsyndromic deafness

Li, X. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh226 · Cited by 126 · see citing works

Mitochondrial DNA: Impacting Central and Peripheral Nervous Systems

Carelli, V., & Chan, D. C. (2014) · Neuron · doi:10.1016/j.neuron.2014.11.022 · Cited by 127 · see citing works

Genetic, pathogenetic, and phenotypic implications of the mitochondrial A3243G tRNALeu(UUR) mutation

Finsterer, J. (2007) · Acta Neurologica Scandinavica · doi:10.1111/j.1600-0404.2007.00836.x · Cited by 125 · see citing works

A deafness-associated tRNAHismutation alters the mitochondrial function, ROS production and membrane potential

Gong, S., Peng, Y., Jiang, P., Wang, M., Fan, M., Wang, X., Zhou, H., Li, H., Yan, Q., Huang, T., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku466 · Cited by 117 · see citing works

A functionally dominant mitochondrial DNA mutation

Sacconi, S., Salviati, L., Nishigaki, Y., Walker, W. F., Hernandez-Rosa, E., Trevisson, E., Delplace, S., Desnuelle, C., Shanske, S., Hirano, M., et al. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn073 · Cited by 113 · see citing works

Pathogenesis of Stroke-Like Episodes in MELAS: Analysis of Neurovascular Cellular Mechanisms

Iizuka, T., & Sakai, F. (2005) · Current Neurovascular Research · doi:10.2174/1567202052773544 · Cited by 112 · see citing works

Human mitochondrial diseases caused by lack of taurine modification in mitochondrial tRNAs

Suzuki, T., Nagao, A., & Suzuki, T. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.65 · Cited by 112 · see citing works

The exome sequencing identified the mutation in YARS2 encoding the mitochondrial tyrosyl-tRNA synthetase as a nuclear modifier for the phenotypic manifestation of Leber's hereditary optic neuropathy-associated mitochondrial DNA mutation

Jiang, P., Jin, X., Peng, Y., Wang, M., Liu, H., Liu, X., Zhang, Z., Ji, Y., Zhang, J., Liang, M., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv498 · Cited by 106 · see citing works

Impact of disease-related mitochondrial mutations on tRNA structure and function

Wittenhagen, L. M. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.09.006 · Cited by 102 · see citing works

A compendium of human mitochondrial gene expression machinery with links to disease

Shutt, T. E., & Shadel, G. S. (2010) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20571 · Cited by 101 · see citing works

Estrogen and Mitochondria: A New Paradigm for Vascular Protection?

DUCKLES, S. P. (2006) · Molecular Interventions · doi:10.1124/mi.6.1.6 · Cited by 95 · see citing works

Simultaneous A8344G heteroplasmy and mitochondrial DNA copy number quantification in Myoclonus Epilepsy and Ragged-Red Fibers (MERRF) syndrome by a multiplex Molecular Beacon based real-time fluorescence PCR

Szuhai, K. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.3.e13 · Cited by 93 · see citing works

Correction of the consequences of mitochondrial 3243A>G mutation in the MT-TL1 gene causing the MELAS syndrome by tRNA import into mitochondria

Karicheva, O., Kolesnikova, O., Schirtz, T., Vysokikh, M., Mager-Heckel, A., Lombès, A., Boucheham, A., Krasheninnikov, I., Martin, R., Entelis, N., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr546 · Cited by 86 · see citing works

Mitochondrial Gene Mutations in the tRNALeu(UUR) Region and Diabetes: Prevalence and Clinical Phenotypes in Japan

Ohkubo, K., Yamano, A., Nagashima, M., Mori, Y., Anzai, K., Akehi, Y., Nomiyama, R., Asano, T., Urae, A., & Ono, J. (2001) · Clinical Chemistry · doi:10.1093/clinchem/47.9.1641 · Cited by 92 · see citing works

Towards Understanding Human Mitochondrial Leucine Aminoacylation Identity

Sohm, B., Frugier, M., Brulé, H., Olszak, K., Przykorska, A., & Florentz, C. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00373-5 · Cited by 92 · see citing works

Disorders of mitochondrial protein synthesis

Jacobs, H. T. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg285 · Cited by 91 · see citing works

Dimerization of a pathogenic human mitochondrial tRNA

Wittenhagen, L. M., & Kelley, S. O. (2002) · Nature Structural Biology · doi:10.1038/nsb820 · Cited by 90 · see citing works

A history of mitochondrial diseases

DiMauro, S. (2010) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-010-9082-x · Cited by 88 · see citing works

Mitochondrial Retinal Dystrophy Associated with the m.3243A>G Mutation

de Laat, P., Smeitink, J. A. M., Janssen, M. C. H., KEUNEN, J. E. E., & Boon, C. J. F. (2013) · Ophthalmology · doi:10.1016/j.ophtha.2013.05.013 · Cited by 87 · see citing works

Impaired nitric oxide production in children with MELAS syndrome and the effect of arginine and citrulline supplementation

El‐Hattab, A. W., Emrick, L., Hsu, J. W.-C., Chanprasert, S., Almannai, M., Craigen, W. J., Jahoor, F., & Scaglia, F. (2016) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2016.01.010 · Cited by 83 · see citing works

MTERF2 is a nucleoid component in mammalian mitochondria

Pellegrini, M., Asin-Cayuela, J., Erdjument‐Bromage, H., Tempst, P., Larsson, N., & Gustafsson, C. M. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.01.018 · Cited by 82 · see citing works

A Deafness- and Diabetes-associated tRNA Mutation Causes Deficient Pseudouridinylation at Position 55 in tRNAGlu and Mitochondrial Dysfunction

Wang, M., Liu, H., Zheng, J., Chen, B., Zhou, M., Fan, W., Wang, H., Liang, X., Zhou, X.-L., Eriani, G., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.739482 · Cited by 79 · see citing works

The Pathogenic A3243G Mutation in Human Mitochondrial tRNALeu(UUR) Decreases the Efficiency of Aminoacylation

Park, H. J., Davidson, E., & King, M. P. (2002) · Biochemistry · doi:10.1021/bi026882r · Cited by 79 · see citing works

Oxidative Insults and Mitochondrial DNA Mutation Promote Enhanced Autophagy and Mitophagy Compromising Cell Viability in Pluripotent Cell Model of Mitochondrial Disease

Lin, D., Huang, Y.-W., Ho, C., Hung, P., Hsu, M., Wang, T.-J., Wu, T., Lee, T., Huang, Z.-D., Chang, P.-C., et al. (2019) · Cells · doi:10.3390/cells8010065 · Cited by 74 · see citing works

Nuclear-encoded factors involved in post-transcriptional processing and modification of mitochondrial tRNAs in human disease

Powell, C. A., Nicholls, T. J., & Minczuk, M. (2015) · Frontiers in Genetics · doi:10.3389/fgene.2015.00079 · Cited by 84 · see citing works

Molecular pathology of MELAS and l-arginine effects

Koga, Y., Povalko, N., Nishioka, J., Katayama, K., Yatsuga, S., & Matsuishi, T. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.09.005 · Cited by 71 · see citing works

The Role of Mitochondrial DNA Mutations in Hearing Loss

Ding, Y., Leng, J., Fan, F., Xia, B., & Xu, P. (2013) · Biochemical Genetics · doi:10.1007/s10528-013-9589-6 · Cited by 71 · see citing works

Role of taurine in the pathologies of MELAS and MERRF

Schaffer, S. W., Jong, C. J., Ito, T., & Azuma, J. (2012) · Amino Acids · doi:10.1007/s00726-012-1414-8 · Cited by 69 · see citing works

Mitochondrial tRNA mutations associated with deafness

Zheng, J., Ji, Y., & Guan, M. (2012) · Mitochondrion · doi:10.1016/j.mito.2012.04.001 · Cited by 66 · see citing works

A Pathogenesis-associated Mutation in Human Mitochondrial tRNALeu(UUR) Leads to Reduced 3′-End Processing and CCA Addition

Levinger, L., Oestreich, I., Florentz, C., & Mörl, M. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.008 · Cited by 65 · see citing works

Mitochondrial diabetes: Pathophysiology, clinical presentation, and genetic analysis

Maassen, J. A. (2002) · American Journal of Medical Genetics · doi:10.1002/ajmg.10346 · Cited by 65 · see citing works

A Member of the Arabidopsis Mitochondrial Transcription Termination Factor Family Is Required for Maturation of Chloroplast Transfer RNAIle(GAU)

Romani, I., Manavski, N., Morosetti, A., Tadini, L., Maier, S., Kühn, K., Ruwe, H., Schmitz‐Linneweber, C., Wanner, G., Leister, D., et al. (2015) · PLANT PHYSIOLOGY · doi:10.1104/pp.15.00964 · Cited by 63 · see citing works

Mitochondria in migraine pathophysiology – does epigenetics play a role?

Fila, M., Pawłowska, E., & Błasiak, J. (2019) · Archives of Medical Science · doi:10.5114/aoms.2019.86061 · Cited by 62 · see citing works

Coronary heart disease is associated with a mutation in mitochondrial tRNA

Jia, Z., Wang, X., Qin, Y., Xue, L., Jiang, P., Meng, Y., Shi, S., Wang, Y., Mo, J. Q., & Guan, M. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt256 · Cited by 61 · see citing works

Evolution Meets Disease: Penetrance and Functional Epistasis of Mitochondrial tRNA Mutations

Moreno‐Loshuertos, R., Ferrín, G., Acín‐Pérez, R., Gallardo, M. E., Viscomi, C. F., Martos, A. P., Zeviani, M., Fernández‐Silva, P., & Enrı́quez, J. A. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1001379 · Cited by 60 · see citing works

Mitochondrial transcription: Lessons from mouse models

Peralta, S., Wang, X., & Moraes, C. T. (2011) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2011.11.001 · Cited by 60 · see citing works

A novel mitochondrial tRNALeu(UUR) mutation in a patient with features of MERRF and Kearns–Sayre syndrome

Nishigaki, Y., Tadesse, S., Bonilla, E., Shungu, D. C., Hersh, S. P., Keats, B. J. B., Berlín, C. I., Goldberg, M. F., Vockley, J. E., DiMauro, S., et al. (2003) · Neuromuscular Disorders · doi:10.1016/s0960-8966(02)00283-3 · Cited by 60 · see citing works

Impaired mitochondrial Ca2+ homeostasis in respiratory chain-deficient cells but efficient compensation of energetic disadvantage by enhanced anaerobic glycolysis due to low ATP steady state levels

VONKLEISTRETZOW, J., Hornig‐Do, H., Schauen, M., Eckertz, S., DINH, T., STASSEN, F., Lottmann, N., Bust, M., Galunska, B. T., & Wielckens, K. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.04.015 · Cited by 59 · see citing works

Mitochondrial diseases in adults

Morgia, C. L., Maresca, A., Caporali, L., Valentino, M. L., & Carelli, V. (2020) · Journal of Internal Medicine · doi:10.1111/joim.13064 · Cited by 58 · see citing works

Overexpressed mitochondrial leucyl-tRNA synthetase suppresses the A3243G mutation in the mitochondrial tRNA^Leu(UUR) gene

Park, H., Davidson, E., & King, M. P. (2008) · RNA · doi:10.1261/rna.1208808 · Cited by 58 · see citing works

Disease‐related versus polymorphic mutations in human mitochondrial tRNAs

Florentz, C., & Sissler, M. (2001) · EMBO Reports · doi:10.1093/embo-reports/kve111 · Cited by 58 · see citing works

Arginine and Citrulline for the Treatment of MELAS Syndrome

El‐Hattab, A. W., Almannai, M., & Scaglia, F. (2017) · Journal of Inborn Errors of Metabolism and Screening · doi:10.1177/2326409817697399 · Cited by 58 · see citing works

ADHD symptoms in neurometabolic diseases: Underlying mechanisms and clinical implications

Homaei, S. C., Halleland, H. B., Kleppe, R., Betari, N., Reif, A., & Haavik, J. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2021.11.012 · Cited by 56 · see citing works

Mitochondrial DNA Haplogroups Do Not Play a Role in the Variable Phenotypic Presentation of the A3243G Mutation

Torroni, A., Campos, Y., Rengo, C., Sellitto, D., Achilli, A., Magri, C., Semino, O., García‐Redondo, A., Jara, P., Arenas, J., et al. (2003) · The American Journal of Human Genetics · doi:10.1086/373936 · Cited by 57 · see citing works

Aminoacylation properties of pathology-related human mitochondrial tRNALysvariants

Sissler, M., Helm, M., Frugier, M., Giegé, R., & Florentz, C. (2004) · RNA · doi:10.1261/rna.5267604 · Cited by 56 · see citing works

Comparative proteomics as a new tool for exploring human mitochondrial tRNA disorders

Rabilloud, T., Strub, J.-M., Carte, N., Luche, S., Van Dorsselaer, A., Lunardi, J., Giegé, R., & Florentz, C. (2002) · Biochemistry · doi:10.1021/bi0114776 · Cited by 55 · see citing works

Critical role of AMP-activated protein kinase in the balance between mitophagy and mitochondrial biogenesis in MELAS disease

Garrido‐Maraver, J., Paz, M. V., Cordero, M. D., Lorite, J. B., Oropesa-Ávila, M., de la Mata, M., Pavón, A. D., de Lavera, I., Alcocer‐Gómez, E., Galán, F., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.08.027 · Cited by 55 · see citing works

The 7472insC Mitochondrial DNA Mutation Impairs the Synthesis and Extent of Aminoacylation of tRNASer(UCN) but Not Its Structure or Rate of Turnover

Toompuu, M., Yasukawa, T., Suzuki, T., Hakkinen, T., Spelbrink, J. N., Watanabe, K., & Jacobs, H. T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200338200 · Cited by 52 · see citing works

Metabolically induced heteroplasmy shifting and l-arginine treatment reduce the energetic defect in a neuronal-like model of MELAS

Desquiret‐Dumas, V., Guéguen, N., Barth, M., Chevrollier, A., Hancock, S. A., Wallace, D. C., Amati‐Bonneau, P., Henrion, D., Bonneau, D., Reynier, P., et al. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.01.010 · Cited by 51 · see citing works

MELAS: clinical phenotype and morphological brain abnormalities

Sparaco, M., Simonati, A., Cavallaro, T., Bartolomei, L., Grauso, M., Piscioli, F., Morelli, L., & Rizzuto, N. (2003) · Acta Neuropathologica · doi:10.1007/s00401-003-0716-z · Cited by 49 · see citing works

In Vivo and In Organello Analyses of Mitochondrial Translation

Fernández‐Silva, P., Acín‐Pérez, R., Fernández‐Vizarra, E., Martos, A. P., & Enrı́quez, J. A. (2007) · Methods in cell biology · doi:10.1016/s0091-679x(06)80028-2 · Cited by 48 · see citing works

Sequence analysis of the complete mitochondrial DNA in 10 commonly used inbred rat strains

Schlick, N., Jensen‐Seaman, M. I., Orlebeke, K., Kwitek, A. E., Jacob, H. J., & Lazar, J. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00234.2006 · Cited by 46 · see citing works

Resolving complexity in mitochondrial disease: Towards precision medicine

Boggan, R. M., Lim, A. Z., Taylor, R. W., McFarland, R., & Pickett, S. J. (2019) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2019.09.003 · Cited by 45 · see citing works

Maternally transmitted late-onset non-syndromic deafness is associated with the novel heteroplasmic T12201C mutation in the mitochondrial tRNAHis gene

Yan, X., Wang, X., Wang, Z., Sun, S., Chen, G., He, Y., Mo, J. Q., Li, R., Jiang, P., Lin, Q., et al. (2011) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2011-100219 · Cited by 45 · see citing works

A deafness-associated tRNA mutation caused pleiotropic effects on the m1G37 modification, processing, stability and aminoacylation of tRNAIle and mitochondrial translation

Meng, F., Zhou, M., Xiao, Y., Mao, X., Zheng, J., Lin, J., Lin, T., Ye, Z., Cang, X., Fu, Y., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1225 · Cited by 44 · see citing works

Reversible infantile respiratory chain deficiency: A clinical and molecular study

Mimaki, M., Hatakeyama, H., Komaki, H., Yokoyama, M., Arai, H., Kirino, Y., Suzuki, T., Nishino, I., Nonaka, I., & Goto, Y. (2010) · Annals of Neurology · doi:10.1002/ana.22111 · Cited by 44 · see citing works

Contribution of the tRNAIle 4317A→G mutation to the phenotypic manifestation of the deafness-associated mitochondrial 12S rRNA 1555A→G mutation

Meng, F., He, Z., Tang, X., Zheng, J., Jin, X., Zhu, Y., Ren, X., Zhou, M., Wang, M., Gong, S., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000530 · Cited by 43 · see citing works

Mitochondrial tRNA mutations associated with deafness

Jing, Z., Ji, Y., & Guan, M. (2012) · Journal of Otology · doi:10.1016/s1672-2930(12)50009-7 · Cited by 43 · see citing works

A deafness-associated tRNAAspmutation alters the m1G37 modification, aminoacylation and stability of tRNAAspand mitochondrial function

Wang, M., Peng, Y., Zheng, J., Zheng, B., Jin, X., Liu, H., Wang, Y., Tang, X., Huang, T., Jiang, P., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw726 · Cited by 42 · see citing works

Contrasting phenotypes in three patients with novel mutations in mitochondrial tRNA genes

Anitori, R. P., Manning, K., Quan, F., Weleber, R. G., Buist, N. R. M., Shoubridge, E. A., & Kennaway, N. G. (2004) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2004.10.003 · Cited by 41 · see citing works

Contribution of nuclear and mitochondrial gene mutations in mitochondrial encephalopathy, lactic acidosis, and stroke-like episodes (MELAS) syndrome

Chakrabarty, S., Govindaraj, P., Sankaran, B. P., Nagappa, M., Kabekkodu, S. P., Jayaram, P., Mallya, S. P., Deepha, S., Ponmalar, J. N. J., Arivinda, H. R., et al. (2021) · Journal of Neurology · doi:10.1007/s00415-020-10390-9 · Cited by 40 · see citing works

Gene expression profiling of skeletal muscle in exercise-trained and sedentary rats with inborn high and low VO2max

Bye, A., Høydal, M. A., Catalucci, D., Langaas, M., Kemi, O. J., Beisvåg, V., Koch, L. G., Britton, S. L., Ellingsen, Ø., & Wisløff, U. (2008) · Physiological Genomics · doi:10.1152/physiolgenomics.90282.2008 · Cited by 38 · see citing works

Homoplasmic MELAS A3243G mtDNA mutation in a colon cancer sample

Lorenc, A., Bryk, J., Golik, P., Kupryjańczyk, J., Ostrowski, J., Pronicki, M., Semczuk, A., Szołkowska, M., & Bartnik, E. (2003) · Mitochondrion · doi:10.1016/s1567-7249(03)00106-5 · Cited by 36 · see citing works

Clinical syndromes associated with mtDNA mutations: where we stand after 30 years

Carelli, V., & Morgia, C. L. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170097 · Cited by 34 · see citing works

Historical perspective on mitochondrial medicine

DiMauro, S., & Garone, C. (2010) · Developmental Disabilities Research Reviews · doi:10.1002/ddrr.102 · Cited by 34 · see citing works

New evidence of a mitochondrial genetic background paradox: Impact of the J haplogroup on the A3243G mutation

Pierron, D., Rocher, C., Amati-Bonneau, P., Reynier, P., Martin‐Négrier, M., Allouche, S., Batandier, C., de Camaret, B. M., Godinot, C., Rötig, A., et al. (2008) · BMC Medical Genetics · doi:10.1186/1471-2350-9-41 · Cited by 34 · see citing works

Structural probing of a pathogenic tRNA dimer

ROY, M. D., WITTENHAGEN, L. M., & KELLEY, S. O. (2005) · RNA · doi:10.1261/rna.7143305 · Cited by 31 · see citing works

Mutation in the mitochondrial tRNAVal causes mitochondrial encephalopathy, lactic acidosis and stroke-like episodes

Glatz, C. E., D׳Aco, K., Smith, S. A., & Sondheimer, N. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.04.003 · Cited by 33 · see citing works

Human mitochondrial tRNA quality control in health and disease

Belostotsky, R., Frishberg, Y., & Entelis, N. (2012) · RNA Biology · doi:10.4161/rna.9.1.18009 · Cited by 33 · see citing works

Molecular Investigations on tRNAs Involved in Human Mitochondrial Disorders

Florentz, C. (2002) · Bioscience Reports · doi:10.1023/a:1016065107165 · Cited by 32 · see citing works

A hypertension-associated mitochondrial DNA mutation alters the tertiary interaction and function of tRNALeu(UUR)

Zhou, M., Wang, M., Xue, L., Lin, Z., He, Q., Shi, W., Chen, Y., Jin, X., Li, H., Jiang, P., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.787028 · Cited by 31 · see citing works

Maternally inherited diabetes is associated with a homoplasmic T10003C mutation in the mitochondrial tRNAGly gene

Liu, H., Li, R., Li, W., Wang, M., Ji, J., Zheng, J., Mao, Z., Mo, J. Q., Jiang, P., Lü, J., et al. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.01.004 · Cited by 32 · see citing works

Muscle 3243A→G mutation load and capacity of the mitochondrial energy‐generating system

Janssen, A. J. M., Schuelke, M., Smeitink, J. A. M., Trijbels, F. J. M., Sengers, R. C. A., Lucke, B., Wintjes, L. T., Morava, É., van Engelen, B. G. M., Smits, B. W., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21328 · Cited by 32 · see citing works

Proteomic consequences of a human mitochondrial tRNA mutation beyond the frame of mitochondrial translation

Tryoen-Tóth, P., Richert, S., Sohm, B., Mine, M., Marsac, C., Van Dorsselaer, A., Leize, E., & Florentz, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301530200 · Cited by 31 · see citing works

A new mechanism for mtDNA pathogenesis: impairment of post-transcriptional maturation leads to severe depletion of mitochondrial tRNASer(UCN) caused by T7512C and G7497A point mutations

Mollers, M. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki876 · Cited by 31 · see citing works

Inflexibility of AMPK-mediated metabolic reprogramming in mitochondrial disease

Lin, D., Kao, S., Ho, C. S., Wei, Y., Hung, P., Hsu, M., Wu, T., Wang, T.-J., Jian, Y.-R., Lee, T., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.20617 · Cited by 31 · see citing works

Mitochondrial tRNA mutations in 887 Chinese subjects with hearing loss

Zheng, J., Bai, X., Xiao, Y., Ji, Y., Meng, F., Aishanjiang, M., Gao, Y., Wang, H., Fu, Y., & Guan, M. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.03.005 · Cited by 31 · see citing works

Restoration of mitochondrial function through activation of hypomodified tRNAs with pathogenic mutations associated with mitochondrial diseases

Tomoda, E., Nagao, A., Shirai, Y. M., Asano, K., Suzuki, T., Battersby, B. J., & Suzuki, T. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad139 · Cited by 31 · see citing works

Mitochondrial Diseases ‐ An Expanding Spectrum of Disorders and Affected Genes

von Kleist-Retzow, J., Schauseil-Zipf, U., Michalk, D. V., & Kunz, W. S. (2003) · Experimental Physiology · doi:10.1113/eph8802509 · Cited by 31 · see citing works

Molecular dysfunction associated with the human mitochondrial 3302A>G mutation in the MTTL1 (mt-tRNALeu(UUR)) gene

Maniura‐Weber, K., Helm, M., Engemann, K., Eckertz, S., Möllers, M., Schauen, M., Hayrapetyan, A., von Kleist-Retzow, J., Lightowlers, R. N., Bindoff, L. A., et al. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl727 · Cited by 30 · see citing works

Defective Expression of the Mitochondrial-tRNA Modifying Enzyme GTPBP3 Triggers AMPK-Mediated Adaptive Responses Involving Complex I Assembly Factors, Uncoupling Protein 2, and the Mitochondrial Pyruvate Carrier

Martínez-Zamora, A., Meseguer, S., Esteve, J. M., Villarroya, M., Aguado, C., Enrı́quez, J. A., Knecht, E., & Armengod, M. ‐. (2015) · PLoS ONE · doi:10.1371/journal.pone.0144273 · Cited by 30 · see citing works

The potential risks of abnormal transmission of mtDNA through assisted reproductive technologies

John, J. C. S., Lloyd, R. E. I., & Shourbagy, S. H. E. (2004) · Reproductive BioMedicine Online · doi:10.1016/s1472-6483(10)60496-8 · Cited by 30 · see citing works

Search for Difference in Aminoacylation of Mitochondrial DNA‐encoded Wild‐type and Mutant Human tRNALeu?(UUR)

Wang, Z.-C., Xue‐min, W., You‐Xin, J., Jiao, B., Xu, F., Mingyong, M., & Ke‐Jun, Z. (2003) · IUBMB Life · doi:10.1080/1521654031000110190 · Cited by 1 · see citing works

Reduction of mitochondrial tRNALeu(UUR) aminoacylation by some MELAS‐associated mutations

Hao, R., Yao, Y., Zheng, Y., Xu, M., & Wang, E. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.11.004 · Cited by 26 · see citing works

The A3243G tRNALeu(UUR) MELAS mutation causes amino acid misincorporation and a combined respiratory chain assembly defect partially suppressed by overexpression of EFTu and EFG2

Sasarman, F., Antonická, H., & Shoubridge, E. A. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn265 · Cited by 148 · see citing works

Defects in mitochondrial protein synthesis and respiratory chain activity segregate with the tRNA(Leu(UUR)) mutation associated with mitochondrial myopathy, encephalopathy, lactic acidosis, and strokelike episodes

King, M. P., Koga, Y., Davidson, M., & Schon, E. A. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.2.480 · Cited by 458 · see citing works

The mitochondrial tRNALeu(UUR) mutation in MELAS: a model for pathogenesis

Schon, E. A., Koga, Y., Davidson, M. M., Moraes, C. T., & King, M. P. (1992) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(92)90226-r · Cited by 74 · see citing works