Mitochondrial protein synthesis: Figuring the fundamentals, complexities and complications, of mammalian mitochondrial translation

Sequence and organization of the human mitochondrial genome

Anderson, S., Bankier, A. T., Barrell, B. G., de Bruijn, M. H. L., Coulson, A. R., Drouin, J., Eperon, I. C., Nierlich, D. P., Roe, B. A., Sanger, F., et al. (1981) · Nature · doi:10.1038/290457a0 · Cited by 9,640 · see citing works

The Structural Basis of Ribosome Activity in Peptide Bond Synthesis

Nissen, P., Hansen, J., Ban, N., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.920 · Cited by 2,269 · see citing works

High Resolution Structure of the Large Ribosomal Subunit from a Mesophilic Eubacterium

Harms, J. M., Schluenzen, F., Zarivach, R., Bashan, A., Gat, S., Agmon, I., Bartels, H., Franceschi, F. J., & Yonath, A. (2001) · Cell · doi:10.1016/s0092-8674(01)00546-3 · Cited by 899 · see citing works

A Genetically Encoded Tag for Correlated Light and Electron Microscopy of Intact Cells, Tissues, and Organisms

Shu, X., Lev‐Ram, V., Deerinck, T. J., Qi, Y. B., Ramko, E. B., Davidson, M. W., Jin, Y., Ellisman, M. H., & Tsien, R. Y. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1001041 · Cited by 834 · see citing works

Structure of the Yeast Mitochondrial Large Ribosomal Subunit

Amunts, A., Brown, A., Bai, X., Llacer, J. L., Hussain, T., Emsley, P., Long, F., Murshudov, G. N., Scheres, S. H. W., & Ramakrishnan, V. (2014) · Science · doi:10.1126/science.1249410 · Cited by 580 · see citing works

Super-resolution microscopy reveals that mammalian mitochondrial nucleoids have a uniform size and frequently contain a single copy of mtDNA

Kukat, C., Wurm, C., Spåhr, H., Falkenberg, M., Larsson, N., & Jakobs, S. (2011) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1109263108 · Cited by 551 · see citing works

Assembly of Bacterial Ribosomes

Shajani, Z., Sykes, M. T., & Williamson, J. R. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062608-160432 · Cited by 505 · see citing works

Copurification of E. coli RNAase E and PNPase: Evidence for a specific association between two enzymes important in RNA processing and degradation

Carpousis, A. J., Houwe, G. V., Ehretsmann, C. P., & Krisch, H. M. (1994) · Cell · doi:10.1016/0092-8674(94)90363-8 · Cited by 433 · see citing works

Polynucleotide phosphorylase and ribonuclease II are required for cell viability and mRNA turnover in Escherichia coli K-12.

Donovan, W. P., & Kushner, S. R. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.1.120 · Cited by 432 · see citing works

The Layered Structure of Human Mitochondrial DNA Nucleoids

Bogenhagen, D. F., Rousseau, D. L., & Burke, S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708444200 · Cited by 426 · see citing works

The mitochondrial genome of yeast

Borst, P., & Grivell, L. A. (1978) · Cell · doi:10.1016/0092-8674(78)90257-x · Cited by 387 · see citing works

Structure of the mammalian mitochondrial ribosome reveals an expanded functional role for its component proteins.

Sharma, M. R., Koc, E., Datta, P., Booth, T. M., Spremulli, L., & Agrawal, R. (2003) · Cell · doi:10.1016/s0092-8674(03)00762-1 · Cited by 373 · see citing works

PNPASE Regulates RNA Import into Mitochondria

Wang, G., Chen, H.-W., Oktay, Y., Zhang, J., Allen, E. L., Smith, G. M., Fan, K. C., Hong, J. S., French, S. W., McCaffery, J. M., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.035 · Cited by 366 · cited 2× · see citing works

Structurally Distinct, Stage-Specific Ribosomes Occur in Plasmodium

Gunderson, J. H., Sogin, M. L., Woollett, G. R., Hollingdale, M. R., de la Cruz, V. F., Waters, A. P., & McCutchan, T. F. (1987) · Science · doi:10.1126/science.3672135 · Cited by 325 · see citing works

Methylation of 12S rRNA Is Necessary for In Vivo Stability of the Small Subunit of the Mammalian Mitochondrial Ribosome

Metodiev, M. D., Lesko, N., Park, C. B., Cámara, Y., Shi, Y., Wibom, R., Hultenby, K. R., Gustafsson, C. M., & Larsson, N. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.03.001 · Cited by 310 · see citing works

Mitochondrial DNA nucleoid structure

Bogenhagen, D. F. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2011.11.005 · Cited by 290 · see citing works

The ribosome filter hypothesis

Mauro, V. P., & Edelman, G. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192442499 · Cited by 260 · see citing works

The Large Subunit of the Mammalian Mitochondrial Ribosome

Koc, E. C., Burkhart, W., Blackburn, K., Moyer, M. B., Schlatzer, D., Moseley, M. A., & Spremulli, L. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106510200 · Cited by 252 · see citing works

The Small Subunit of the Mammalian Mitochondrial Ribosome

Koc, E. C., Burkhart, W., Blackburn, K., Moseley, M. A., & Spremulli, L. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100727200 · Cited by 246 · see citing works

The Mitochondrial RNA-Binding Protein GRSF1 Localizes to RNA Granules and Is Required for Posttranscriptional Mitochondrial Gene Expression

Antonická, H., Sasarman, F., Nishimura, T., Paupe, V., & Shoubridge, E. A. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.02.006 · Cited by 240 · see citing works

GRSF1 Regulates RNA Processing in Mitochondrial RNA Granules

Jourdain, A. A., Koppen, M., Wydro, M. M., Rodley, C. D. M., Lightowlers, R. N., Chrzanowska‐Lightowlers, Z. M., & Martinou, J. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.02.005 · Cited by 238 · see citing works

Architecture of the large subunit of the mammalian mitochondrial ribosome

Greber, B. J., Boehringer, D., Leitner, A., Bieri, P., Voigts-Hoffmann, F., Erzberger, J. P., Leibundgut, M., Aebersold, R. H., & Ban, N. (2013) · Nature · doi:10.1038/nature12890 · Cited by 225 · see citing works

Mitochondrial nucleoid interacting proteins support mitochondrial protein synthesis

He, J.-Y., Cooper, H. M., Reyes, A., Re, M. D., Sembongi, H., Litwin, T., Gao, J., Neuman, K., Fearnley, I., Spinazzola, A., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks266 · Cited by 220 · see citing works

Protein synthesis in mitochondria. Requirements for the incorporation of radioactive amino acids into mitochondrial protein

ROODYN, D., Reis, P., & WORK, T. (1961) · Biochemical Journal · doi:10.1042/bj0800009 · Cited by 217 · see citing works

Incorporation of Labeled Amino Acids into the Protein of Muscle and Liver Mitochondria

McLean, J., Cohn, G. L., Brandt, I. K., & Simpson, M. V. (1958) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64722-2 · Cited by 213 · see citing works

Mitochondrial and Cytoplasmic Polysomes from Neurospora crassa

Küntzel, H., & Noll, H. (1967) · Nature · doi:10.1038/2151340a0 · Cited by 204 · see citing works

A Human Mitochondrial Transcription Factor Is Related to RNA Adenine Methyltransferases and Binds S-Adenosylmethionine

McCulloch, V., Seidel-Rogol, B. L., & Shadel, G. S. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.4.1116-1125.2002 · Cited by 200 · see citing works

A functional peptidyl‐tRNA hydrolase, ICT1, has been recruited into the human mitochondrial ribosome

Richter‐Dennerlein, R., Rorbach, J., Pajak, A., Smith, P., Wessels, H. J. C. T., Huynen, M. A., Smeitink, J. A. M., Lightowlers, R. N., & Chrzanowska‐Lightowlers, Z. M. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.14 · Cited by 193 · see citing works

Oxygen Consumption Can Regulate the Growth of Tumors, a New Perspective on the Warburg Effect

Chen, Y., Cairns, R. A., Papandreou, I., Koong, A. C., & Denko, N. C. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007033 · Cited by 187 · see citing works

Mitochondrial tRNA Import and Its Consequences for Mitochondrial Translation

Schneider, A. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060109-092838 · Cited by 186 · see citing works

Eukaryotic 5S rRNA biogenesis

Ciganda, M., & Williams, N. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.74 · Cited by 181 · see citing works

Mutations in MTFMT Underlie a Human Disorder of Formylation Causing Impaired Mitochondrial Translation

Tucker, E. J., Hershman, S. G., Köhrer, C., Belcher-Timme, C. A., Patel, J., Goldberger, O., Christodoulou, J., Silberstein, J. M., McKenzie, M., Ryan, M. T., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.07.010 · Cited by 176 · see citing works

Hungry Codons Promote Frameshifting in Human Mitochondrial Ribosomes

Temperley, R., Richter‐Dennerlein, R., Dennerlein, S., Lightowlers, R. N., & Chrzanowska‐Lightowlers, Z. M. (2010) · Science · doi:10.1126/science.1180674 · Cited by 174 · see citing works

Translation initiation with 70S ribosomes: an alternative pathway for leaderless mRNAs

Moll, I. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh663 · Cited by 174 · see citing works

NAD+-dependent Deacetylase SIRT3 Regulates Mitochondrial Protein Synthesis by Deacetylation of the Ribosomal Protein MRPL10

Yang, Y., Çimen, H., Han, M.-J., Shi, T., Deng, J., Koç, H., Palacios, O. M., Montier, L., Bai, Y., Tong, Q., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.053421 · Cited by 164 · see citing works

Polynucleotide Phosphorylase Functions as Both an Exonuclease and a Poly(A) Polymerase in Spinach Chloroplasts

Yehudai-Resheff, S., Hirsh, M., & Schuster, G. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.16.5408-5416.2001 · Cited by 161 · see citing works

Mutations in C12orf65 in Patients with Encephalomyopathy and a Mitochondrial Translation Defect

Antonická, H., Østergaard, E., Sasarman, F., Weraarpachai, W., Wibrand, F., Pedersen, A. M. B., Rodenburg, R. J., van der Knaap, M. S., Smeitink, J. A. M., Chrzanowska‐Lightowlers, Z. M., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.06.004 · Cited by 159 · see citing works

Gene expressions and copy numbers associated with metastatic phenotypes of uterine cervical cancer

Lyng, H., Brøvig, R. S., Svendsrud, D. H., Holm, R., Kaalhus, O., Knutstad, K., Oksefjell, H., Sundfør, K., Kristensen, G. B., & Stokke, T. (2006) · BMC Genomics · doi:10.1186/1471-2164-7-268 · Cited by 158 · see citing works

Modeling a Minimal Ribosome Based on Comparative Sequence Analysis

Mears, J. A., Cannone, J. J., Stagg, S. M., Gutell, R. R., Agrawal, R. K., & Harvey, S. C. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00568-5 · Cited by 153 · see citing works

Human Mitochondrial Transcription Factor B1 Interacts with the C-Terminal Activation Region of h-mtTFA and Stimulates Transcription Independently of Its RNA Methyltransferase Activity

McCulloch, V., & Shadel, G. S. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.16.5816-5824.2003 · Cited by 142 · see citing works

Cloning of a new gene encoding an antigen recognized by melanoma-specific HLA-A24-restricted tumor-infiltrating lymphocytes.

Robbins, P. F., El‐Gamil, M., Li, Y. F., Topalian, S. L., Rivoltini, L., Sakaguchi, K., Appella, E., Kawakami, Y., & Rosenberg, S. A. (1995) · The Journal of Immunology · doi:10.4049/jimmunol.154.11.5944 · Cited by 140 · see citing works

Properties of Human Mitochondrial Ribosomes

O'Brien, T. W. (2003) · IUBMB Life · doi:10.1080/15216540310001626610 · Cited by 138 · see citing works

Proteomic Analysis of the Mammalian Mitochondrial Ribosome

Suzuki, T., Terasaki, M., Takemoto‐Hori, C., Hanada, T., Ueda, T., Wada, A., & Watanabe, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103236200 · Cited by 138 · see citing works

Evolution of a protein-rich mitochondrial ribosome: implications for human genetic disease

O’Brien, T. W. (2002) · Gene · doi:10.1016/s0378-1119(01)00808-3 · Cited by 135 · see citing works

Import of tRNAs and aminoacyl-tRNA synthetases into mitochondria

Duchêne, A.-M., Pujol, C., & Maréchal-Drouard, L. (2009) · Current Genetics · doi:10.1007/s00294-008-0223-9 · Cited by 133 · see citing works

mtRF1a Is a Human Mitochondrial Translation Release Factor Decoding the Major Termination Codons UAA and UAG

Soleimanpour‐Lichaei, H. R., Kühl, I., Gaisne, M., Passos, J. F., Wydro, M. M., Rorbach, J., Temperley, R., Bonnefoy, N., Tate, W. P., Lightowlers, R. N., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.031 · Cited by 132 · see citing works

Evidence for the Presence of 5S rRNA in Mammalian Mitochondria

Magalhães, P. J., Andreu, A. L., & Schon, E. A. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.9.2375 · Cited by 131 · see citing works

Identification of Mammalian Mitochondrial Translational Initiation Factor 3 and Examination of Its Role in Initiation Complex Formation with Natural mRNAs

Koc, E. C., & Spremulli, L. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202498200 · Cited by 128 · see citing works

Human ERAL1 is a mitochondrial RNA chaperone involved in the assembly of the 28S small mitochondrial ribosomal subunit

Dennerlein, S., Rozanska, A. L., Wydro, M. M., Chrzanowska‐Lightowlers, Z. M., & Lightowlers, R. N. (2010) · Biochemical Journal · doi:10.1042/bj20100757 · Cited by 128 · see citing works

Protein composition of the bovine mitochondrial ribosome.

Matthews, D. E., Hessler, R. A., Denslow, N. D., Edwards, J. S., & O’Brien, T. W. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34199-1 · Cited by 128 · see citing works

The post-transcriptional life of mammalian mitochondrial RNA

Rorbach, J., & Minczuk, M. (2012) · Biochemical Journal · doi:10.1042/bj20112208 · Cited by 118 · see citing works

Biological significance of 5S rRNA import into human mitochondria: role of ribosomal protein MRP-L18.Preprint

Smirnov, A., Entelis, N., Martin, R., & Tarassov, I. (2011) · Genes & Development · doi:10.1101/gad.624711 · Cited by 117 · see citing works

Evidence for the Translation Initiation of Leaderless mRNAs by the Intact 70 S Ribosome without Its Dissociation into Subunits in Eubacteria

Udagawa, T., Shimizu, Y., & Ueda, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308784200 · Cited by 116 · see citing works

Isolation of DAP3, a Novel Mediator of Interferon-γ-induced Cell Death

Kissil, J. L., Deiss, L. P., Bayewitch, M. L., Raveh, T., Khaspekov, G. L., & Kimchi, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.46.27932 · Cited by 116 · see citing works

Initial Steps in RNA Processing and Ribosome Assembly Occur at Mitochondrial DNA Nucleoids

Bogenhagen, D. F., Martin, D. W., & Koller, A. A. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.013 · Cited by 115 · see citing works

Mutation in PNPT1, which encodes a polyribonucleotide nucleotidyltransferase, impairs RNA import into mitochondria and causes respiratory-chain deficiency.

Vedrenne, V., Gowher, A., de Lonlay, P., Nitschké, P., Serre, V., Boddaert, N., Altuzarra, C., Mager-Heckel, A., Chretien, F., Entelis, N., et al. (2012) · American Journal of Human Genetics · doi:10.1016/j.ajhg.2012.09.001 · Cited by 114 · see citing works

5 S rRNA and tRNA Import into Human Mitochondria

Entelis, N., Kolesnikova, O., Dogan, S., Martin, R. P., & Tarassov, I. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103906200 · Cited by 113 · see citing works

MTERF3 Regulates Mitochondrial Ribosome Biogenesis in Invertebrates and Mammals

Wredenberg, A., Lagouge, M., Bratić, A. M., Metodiev, M. D., Spåhr, H., Mourier, A., Freyer, C., Ruzzenente, B., Tain, L. S., Grönke, S., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003178 · Cited by 113 · see citing works

EF-G2mt Is an Exclusive Recycling Factor in Mammalian Mitochondrial Protein Synthesis

Tsuboi, M., Morita, H., Nozaki, Y., Akama, K., Ueda, T., Ito, K., Nierhaus, K. H., & Takeuchi, N. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.06.028 · Cited by 112 · see citing works

The human mitochondrial ribosome recycling factor is essential for cell viability

Rorbach, J., Richter‐Dennerlein, R., Wessels, H. J. C. T., Wydro, M. M., Pękalski, M. Ł., Farhoud, M. H., Kühl, I., Gaisne, M., Bonnefoy, N., Smeitink, J. A. M., et al. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn576 · Cited by 112 · see citing works

Structural Compensation for the Deficit of rRNA with Proteins in the Mammalian Mitochondrial Ribosome

Suzuki, T., Terasaki, M., Takemoto‐Hori, C., Hanada, T., Ueda, T., Wada, A., & Watanabe, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100432200 · Cited by 112 · see citing works

A Single Mammalian Mitochondrial Translation Initiation Factor Functionally Replaces Two Bacterial Factors

Gaur, R., Grasso, D., Datta, P. P., Krishna, P. D. V., Das, G., Spencer, A. C., Agrawal, R. K., Spremulli, L. L., & Varshney, U. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.11.021 · Cited by 111 · see citing works

Studies of mouse mitochondrial DNA in escherichia coli: Structure and function of the eucaryotic-procaryotic chimeric plasmids

Chang, A. C. Y., Lansman, R. A., Clayton, D. A., & Cohen, S. N. (1975) · Cell · doi:10.1016/0092-8674(75)90014-8 · Cited by 110 · 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

Interaction of Mammalian Mitochondrial Ribosomes with the Inner Membrane

Liu, M., & Spremulli, L. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002173200 · Cited by 107 · see citing works

Isolation of yeast mitochondrial ribosomes highly active in protein synthesis

Grivell, L. A., Reijnders, L., & Borst, P. (1971) · Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis · doi:10.1016/0005-2787(71)90811-2 · Cited by 105 · see citing works

Studies on the Biosynthesis of Mitochondrial Protein Components*

Beattie, D. S., BASFORD, R. E., & Koritz, S. B. (1966) · Biochemistry · doi:10.1021/bi00867a018 · Cited by 102 · see citing works

Absence of a 5S RNA Component in the Mitochondrial Ribosomes of Neurospora crassa

Lizardi, P. M., & Luck, D. (1971) · Nature New Biology · doi:10.1038/newbio229140a0 · Cited by 99 · see citing works

Incorporation of amino acids into the protein of isolated mitochondria. A search for optimum conditions and a relationship to oxidative phosphorylation

TRUMAN, D., & Körner, A. (1962) · Biochemical Journal · doi:10.1042/bj0830588 · Cited by 99 · see citing works

Mitochondrial Enzyme Rhodanese Is Essential for 5 S Ribosomal RNA Import into Human Mitochondria*

Smirnov, A., Comte, C., Mager-Heckel, A., Addis, V., Krasheninnikov, I., Martin, R., Entelis, N., & Tarassov, I. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.151183 · Cited by 98 · see citing works

Correlative Light- and Electron Microscopy with chemical tags

Perković, M., Kunz, M., Endesfelder, U., Bunse, S., Wigge, C., Zhou, Y., Hodirnau, V.-V., Scheffer, M. P., Seybert, A., Malkusch, S., et al. (2014) · Journal of Structural Biology · doi:10.1016/j.jsb.2014.03.018 · Cited by 94 · see citing works

A Structural Model for the Large Subunit of the Mammalian Mitochondrial Ribosome

Mears, J. A., Sharma, M. R., Gutell, R. R., McCook, A. S., Richardson, P. E., Caulfield, T. R., Agrawal, R. K., & Harvey, S. C. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.01.094 · Cited by 92 · see citing works

Human C4orf14 interacts with the mitochondrial nucleoid and is involved in the biogenesis of the small mitochondrial ribosomal subunit

He, J., Cooper, H. M., Reyes, A., Re, M. D., Kazak, L., Wood, S. R., Mao, C. C., Fearnley, I. M., Walker, J. E., & Holt, I. J. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks257 · Cited by 89 · see citing works

Mitochondrial Ribosomal RNA (rRNA) Methyltransferase Family Members Are Positioned to Modify Nascent rRNA in Foci near the Mitochondrial DNA Nucleoid

Lee, K.-W., Okot-Kotber, C. I., LaComb, J. F., & Bogenhagen, D. F. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.515692 · Cited by 88 · see citing works

A homozygous mutation of C12orf65 causes spastic paraplegia with optic atrophy and neuropathy (SPG55)

Shimazaki, H., Takiyama, Y., Ishiura, H., Sakai, C., Matsushima, Y., Hatakeyama, H., Honda, J., Sakoe, K., Naoi, T., Namekawa, M., et al. (2012) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2012-101212 · Cited by 88 · see citing works

A Surfeit of Factors: Why is Ribosome Assembly So Much More Complicated in Eukaryotes than Bacteria?

Hage, A. E., & Tollervey, D. W. (2004) · RNA Biology · doi:10.4161/rna.1.1.932 · Cited by 85 · see citing works

Mammalian Mitochondrial Ribosomal Proteins (4)

O’Brien, T. W., Liu, J., Sylvester, J. E., Mougey, E. B., Fischel‐Ghodsian, N., Thiede, B., Wittmann‐Liebold, B., & Graack, H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909762199 · Cited by 84 · see citing works

Comparative studies on mitochondrial and cytoplasmic ribosomes of Tetrahymena pyriformis

Chi, J. C. H., & Suyama, Y. (1970) · Journal of Molecular Biology · doi:10.1016/0022-2836(70)90082-3 · Cited by 84 · see citing works

Intragenomic 16S rDNA Divergence in Haloarcula marismortui Is an Adaptation to Different Temperatures

López‐López, A., Benlloch, S., Bonfá, M., Rodríguez‐Valera, F., & Mira, Á. (2007) · Journal of Molecular Evolution · doi:10.1007/s00239-007-9047-3 · Cited by 83 · see citing works

Evidence for an Active Role of IF3mt in the Initiation of Translation in Mammalian Mitochondria

Christian, B. E., & Spremulli, L. L. (2009) · Biochemistry · doi:10.1021/bi8023493 · Cited by 76 · see citing works

A Proteomics Approach to the Identification of Mammalian Mitochondrial Small Subunit Ribosomal Proteins

Koc, E. C., Burkhart, W., Blackburn, K., Moseley, M. A., Koç, H., & Spremulli, L. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003596200 · Cited by 74 · see citing works

Identification and cloning of human mitochondrial translational release factor 1 and the ribosome recycling factor

Zhang, Y., & Spremulli, L. L. (1998) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(98)00223-1 · Cited by 73 · see citing works

C7orf30 is necessary for biogenesis of the large subunit of the mitochondrial ribosome

Rorbach, J., Gammage, P. A., & Minczuk, M. A. (2012) · Nucleic Acids Research · doi:10.1093/nar/gkr1282 · Cited by 73 · see citing works

Cryo-EM structure of the small subunit of the mammalian mitochondrial ribosome

Kaushal, P. S., Sharma, M. R., Booth, T. M., Haque, E., Tung, C., Sanbonmatsu, K. Y., Spremulli, L. L., & Agrawal, R. K. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1401657111 · Cited by 73 · see citing works

Preferential Selection of the 5′-Terminal Start Codon on Leaderless mRNAs by Mammalian Mitochondrial Ribosomes

Christian, B. E., & Spremulli, L. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.149054 · Cited by 71 · see citing works

Mammalian Mitochondrial Ribosomal Proteins

Goldschmidt‐Reisin, S., Kitakawa, M., Herfurth, E., Wittmann‐Liebold, B., Grohmann, L., & Graack, H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.52.34828 · Cited by 68 · see citing works

Regulation of mammalian mitochondrial translation by post-translational modifications

Koc, E. C., & Koç, H. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.03.003 · Cited by 66 · see citing works

Ribosomes bind leaderless mRNA in Escherichia coli through recognition of their 5′-terminal AUG

Brock, J. E., Pourshahian, S., Giliberti, J., Limbach, P. A., & Janssen, G. R. (2008) · RNA · doi:10.1261/rna.1089208 · Cited by 64 · see citing works

Silencing of the Nuclear RPS10 Gene Encoding Mitochondrial Ribosomal Protein Alters Translation in Arabidopsis Mitochondria

Kwasniak, M., Majewski, P., Skibior, R., Adamowicz-Skrzypkowska, A., Czarna, M., Śliwińska, E., & Jańska, H. (2013) · The Plant Cell · doi:10.1105/tpc.113.111294 · Cited by 63 · see citing works

Lack of secondary structure characterizes the 5′ ends of mammalian mitochondrial mRNAs

Jones, C. N., Wilkinson, K. A., Hung, K. T., Weeks, K. M., & Spremulli, L. L. (2008) · RNA · doi:10.1261/rna.909208 · Cited by 61 · see citing works

Protein synthesis in mitochondria

Pel, H. J., & Grivell, L. A. (1994) · Molecular Biology Reports · doi:10.1007/bf00986960 · Cited by 60 · see citing works

Expression of differentiation-related genes in colorectal cancer: possible implications for prognosis.

van Belzen, N., Dinjens, W. N. M., Eussen, B. H. J., & Bosman, F. T. (1998) · PubMed · doi:10.14670/hh-13.1233 · Cited by 60 · see citing works

The Mitochondrial Ribosome of Xenopus laevis

Swanson, R. F., & Dawid, I. B. (1970) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.66.1.117 · Cited by 58 · see citing works

Specialization from synthesis: How ribosome diversity can customize protein function

Filipovska, A., & Rackham, O. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.02.032 · Cited by 57 · see citing works

The apoptosis mediator mDAP-3 is a novel member of a conserved family of mitochondrial proteins

Berger, T., Brigl, M., Herrmann, J. M., Vielhauer, V., Luckow, B., Schlöndorff, D., & Kretzler, M. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.20.3603 · Cited by 51 · see citing works

Human G-proteins, ObgH1 and Mtg1, associate with the large mitochondrial ribosome subunit and are involved in translation and assembly of respiratory complexes

Kotani, T., Akabane, S., Takeyasu, K., Ueda, T., & Takeuchi, N. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt079 · Cited by 50 · see citing works

Termination of Protein Synthesis in Mammalian Mitochondria

Chrzanowska‐Lightowlers, Z. M., Pajak, A., & Lightowlers, R. N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.290585 · Cited by 49 · see citing works

Novel C12orf65 mutations in patients with axonal neuropathy and optic atrophy

Tucci, A., Liu, Y., Preza, E., Pitceathly, R. D. S., Chalasani, A., Plagnol, V., Land, J. M., Trabzuni, D., Ryten, M., UKBEC, O. B. O., et al. (2013) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2013-306387 · Cited by 49 · see citing works

Identification of four proteins from the small subunit of the mammalian mitochondrial ribosome using a proteomics approach

Koc, E. C., Burkhart, W., Blackburn, K., Koç, H., Moseley, M. A., & Spremulli, L. L. (2001) · Protein Science · doi:10.1110/ps.35301 · Cited by 48 · see citing works

Interaction of bovine mitochondrial ribosomes with messenger RNA

Liao, H. X., & Spremulli, L. L. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83265-3 · Cited by 46 · see citing works

Delineation of C12orf65-related phenotypes: a genotype–phenotype relationship

Spiegel, R., Mandel, H., Saada, A., Lerer, I., Burger, A., Shaag, A., Shalev, S. A., Jabaly-Habib, H., Goldsher, D., Gomori, J. M., et al. (2014) · European Journal of Human Genetics · doi:10.1038/ejhg.2013.284 · Cited by 44 · see citing works

Physical characterization of ribosomes from purified mitochondria of yeast

Stegeman, W. J., Cooper, C. S., & Avers, C. J. (1970) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(70)90759-x · Cited by 44 · see citing works

Bovine mitochondrial ribosomes possess a high affinity binding site for guanine nucleotides

Denslow, N. D., Anders, J. C., & O’Brien, T. W. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)92860-7 · Cited by 43 · see citing works

HMRF1L is a human mitochondrial translation release factor involved in the decoding of the termination codons UAA and UAG

Nozaki, Y., Matsunaga, N., Ishizawa, T., Ueda, T., & Takeuchi, N. (2008) · Genes to Cells · doi:10.1111/j.1365-2443.2008.01181.x · Cited by 42 · see citing works

Expression, Purification, and Mechanistic Studies of Bovine Mitochondrial Translational Initiation Factor 2

Ma, J., & Spremulli, L. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.10.5805 · Cited by 42 · see citing works

Correlative microscopy in biology—Instrumentation and methods

(1989) · Journal of Steroid Biochemistry · doi:10.1016/0022-4731(89)90316-6 · Cited by 40 · see citing works

Current Views of the Structure of the Mammalian Mitochondrial Ribosome

Koc, E. C., Haque, M. E., & Spremulli, L. L. (2010) · Israel Journal of Chemistry · doi:10.1002/ijch.201000002 · Cited by 40 · see citing works

Identification of Mammalian Mitochondrial Ribosomal Proteins (MRPs) by N-Terminal Sequencing of Purified Bovine MRPs and Comparison to Data Bank Sequences: The Large Subribosomal Particle,

Graack, H., Bryant, M. L., & O’Brien, T. W. (1999) · Biochemistry · doi:10.1021/bi991543s · Cited by 39 · see citing works

Approaches toward super-resolution fluorescence imaging of mitochondrial proteins using PALM

Brown, T. A., Fetter, R. D., Tkachuk, A. N., & Clayton, D. A. (2010) · Methods · doi:10.1016/j.ymeth.2010.01.001 · Cited by 39 · see citing works

Transcription-independent role for human mitochondrial RNA polymerase in mitochondrial ribosome biogenesis

Surovtseva, Y. V., & Shadel, G. S. (2013) · Nucleic Acids Research · doi:10.1093/nar/gks1447 · Cited by 39 · see citing works

Evolution of proteins in mammalian cytoplasmic and mitochondrial ribosomes

Pietromonaco, S. F., Hessler, R. A., & O’Brien, T. W. (1986) · Journal of Molecular Evolution · doi:10.1007/bf02099958 · Cited by 38 · see citing works

Proteins of mammalian mitochondrial ribosomes

Pietromonaco, S. F., Denslow, N. D., & O’Brien, T. W. (1991) · Biochimie · doi:10.1016/0300-9084(91)90062-6 · Cited by 37 · see citing works

Transcription in yeast mitochondria: Isolation and physical mapping of messenger RNAs for subunits of cytochrome c oxidase and ATPase

Moorman, A. F. M., van Ommen, G. B., & Grivell, L. A. (1978) · Molecular and General Genetics MGG · doi:10.1007/bf00275114 · Cited by 34 · see citing works

Solution structure and siRNA‐mediated knockdown analysis of the mitochondrial disease‐related protein C12orf65

Kogure, H., Hikawa, Y., Hagihara, M., Tochio, N., Koshiba, S., Inoue, Y., Güntert, P., Kigawa, T., Yokoyama, S., & Nameki, N. (2012) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24152 · Cited by 33 · see citing works

Importance of the osmolarity of the incubation medium on amino acid incorporation into protein by isolated rat liver mitochondria

Haldar, D., & Freeman, K. B. (1969) · Biochemical Journal · doi:10.1042/bj1110653 · Cited by 31 · see citing works

Mitochondrial transformation: time for concerted action

Lightowlers, R. N. (2011) · EMBO Reports · doi:10.1038/embor.2011.93 · Cited by 29 · see citing works

Optic Atrophy and a Leigh-Like Syndrome Due to Mutations in the C12orf65 Gene

Heidary, G., Calderwood, L., Cox, G. F., Robson, C. D., Teot, L. A., Mullon, J., & Anselm, I. A. (2013) · Journal of Neuro-Ophthalmology · doi:10.1097/wno.0000000000000076 · Cited by 29 · see citing works

In vitro suppression of UGA codons in a mitochondrial mRNA

de Ronde, A., van Loon, A. P. G. M., Grivell, L. A., & Kohli, J. (1980) · Nature · doi:10.1038/287361a0 · Cited by 28 · see citing works

Amino acid incorporation into the protein of mitochondria and mitochondrial fragments from beef heart

Kroon, A. M. (1963) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(63)91245-9 · Cited by 27 · see citing works

Contacts between mammalian mitochondrial translational initiation factor 3 and ribosomal proteins in the small subunit

Haque, M. E., Koç, H., Çimen, H., Koc, E. C., & Spremulli, L. L. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.09.013 · Cited by 24 · see citing works

Effects of length and mRNA secondary structure on the interaction of bovine mitochondrial ribosomes with messenger RNA.

Liao, H. X., & Spremulli, L. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38463-7 · Cited by 24 · see citing works

Structural basis for S -adenosylmethionine binding and methyltransferase activity by mitochondrial transcription factor B1

Guja, K. E., Venkataraman, K., Yakubovskaya, E., Shi, H., Mejía, E., Hambardjieva, E., Karzai, A. W., & García–Díaz, M. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt547 · Cited by 24 · see citing works

Identification of mitochondrial gene products by DNA-directed protein synthesis in vitro

Moorman, A. F. M., Grivell, L. A., Lamie, F., & Smits, H. L. (1978) · Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis · doi:10.1016/0005-2787(78)90192-2 · Cited by 24 · see citing works

A starter kit for point-localization super-resolution imaging

Manley, S., Gunzenhäuser, J., & Olivier, N. (2011) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2011.10.009 · Cited by 23 · see citing works

Phenotypic investigations of the depletion of EngA inEscherichia coliare consistent with a role in ribosome biogenesis

Bharat, A., & Brown, E. D. (2014) · FEMS Microbiology Letters · doi:10.1111/1574-6968.12403 · Cited by 22 · see citing works

Heart-specific splice-variant of a human mitochondrial ribosomal protein (mRNA processing; tissue specific splicing)

Spirina, O., Bykhovskaya, Y., Kajava, A. V., O’Brien, T. W., Nierlich, D. P., Mougey, E. B., Sylvester, J. E., Graack, H., Wittmann‐Liebold, B., & Fischel‐Ghodsian, N. (2000) · Gene · doi:10.1016/s0378-1119(00)00504-7 · Cited by 21 · see citing works

Mutations in the mitochondrial gene C12ORF65 lead to syndromic autosomal recessive intellectual disability and show genotype phenotype correlation

Buchert, R., Uebe, S., Radwan, F., Tawamie, H., Issa, S., Shimazaki, H., Henneke, M., Ekici, A. B., Reis, A., & Jamra, R. A. (2013) · European Journal of Medical Genetics · doi:10.1016/j.ejmg.2013.09.010 · Cited by 21 · see citing works

Overexpression and Purification of Mammalian Mitochondrial Translational Initiation Factor 2 and Initiation Factor 3

Grasso, D., Christian, B. E., Spencer, A. C., & Spremulli, L. L. (2007) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)30004-9 · Cited by 19 · see citing works

Mitoribosomal regulation of OXPHOS biogenesis in plants

Jańska, H., & Kwasniak, M. (2014) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00079 · Cited by 19 · see citing works

A Conserved N-Terminal Sequence Targets Human DAP3 to Mitochondria

Morgan, C., Jacques, C., Savagner, F., Tourmen, Y., Mirebeau‐Prunier, D., Malthièry, Y., & Reynier, P. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.4119 · Cited by 18 · see citing works

In-vitro translation of mitochondrial mRNAs by yeast mitochondrial ribosomes is hampered by the lack of start-codon recognition

Dekker, P., Papadopoulou, B., & Grivell, L. A. (1993) · Current Genetics · doi:10.1007/bf00336745 · Cited by 17 · see citing works

Cloning, expression, and mapping of PDCD9, the human homolog of Gallus gallus pro-apoptotic protein p52

Carim‐Todd, L., Sumoy, L., Nadal, M., Estivill, X., & Escarceller, M. (1999) · Cytogenetic and Genome Research · doi:10.1159/000015397 · Cited by 17 · see citing works

Mitochondrial transfection for studying organellar DNA repair, genome maintenance and aging

Mileshina, D., Ibrahim, N., Boesch, P., Lightowlers, R. N., Dietrich, A., & Weber‐Lotfi, F. (2011) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2011.05.002 · Cited by 16 · see citing works

A critical study of amino acid incorporation into protein by isolated liver mitochondria from adult rats

Sandell, S., Löw, H., & von der Decken, A. (1967) · Biochemical Journal · doi:10.1042/bj1040575 · Cited by 12 · see citing works

Mitochondrial Genome Engineering: The Revolution May Not Be CRISPR-Ized

Gammage, P., Moraes, C. T., & Minczuk, M. (2017) · Trends in Genetics · doi:10.1016/j.tig.2017.11.001 · Cited by 310 · see citing works

Structure of the large ribosomal subunit from human mitochondria

Brown, A., Amunts, A., Bai, X., Sugimoto, Y., Edwards, P. C., Murshudov, G. N., Scheres, S. H. W., & Ramakrishnan, V. (2014) · Science · doi:10.1126/science.1258026 · Cited by 324 · see citing works

MicroRNA and mRNA cargo of extracellular vesicles from porcine adipose tissue-derived mesenchymal stem cells

Eirin, A., Riester, S. M., Zhu, X. Y., Tang, H. R., Evans, J. M., O’Brien, D. R., van Wijnen, A. J., & Lerman, L. O. (2014) · Gene · doi:10.1016/j.gene.2014.08.041 · Cited by 293 · see citing works

The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass

Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · see citing works

Control of mitochondrial biogenesis and function by the ubiquitin–proteasome system

Brągoszewski, P., Turek, M., & Chacińska, A. (2017) · Open Biology · doi:10.1098/rsob.170007 · Cited by 186 · see citing works

Yeast as a system for modeling mitochondrial disease mechanisms and discovering therapies

Lasserre, J.-P., Dautant, A., Aiyar, R. S., Kucharczyk, R., Glatigny, A., Tribouillard‐Tanvier, D., Rytka, J., Blondel, M., Skoczeń, N., Reynier, P., et al. (2015) · Disease Models & Mechanisms · doi:10.1242/dmm.020438 · Cited by 158 · see citing works

The process of mammalian mitochondrial protein synthesis

Mai, N., Chrzanowska‐Lightowlers, Z. M., & Lightowlers, R. N. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2456-0 · Cited by 140 · see citing works

Small is big in Arabidopsis mitochondrial ribosome

Waltz, F., Nguyen, T.-T., Arrivé, M., Bochler, A., Chicher, J., Hammann, P., Kühn, L., Quadrado, M., Mireau, H., Hashem, Y., et al. (2019) · Nature Plants · doi:10.1038/s41477-018-0339-y · Cited by 112 · see citing works

Roles of mitochondria in neuronal development

Son, G., & Han, J. (2018) · BMB Reports · doi:10.5483/bmbrep.2018.51.11.226 · Cited by 117 · see citing works

Mutations of Human NARS2, Encoding the Mitochondrial Asparaginyl-tRNA Synthetase, Cause Nonsyndromic Deafness and Leigh Syndrome

Simon, M. T., Richard, É. M., Wang, X., Shahzad, M., Huang, V. H., Qaiser, T. A., Potluri, P., Mahl, S. E., Dávila, A., Nazli, S., et al. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005097 · Cited by 117 · see citing works

Human mitochondrial COX1 assembly into cytochrome <i>c</i> oxidase at a glance

Dennerlein, S., & Rehling, P. (2015) · Journal of Cell Science · doi:10.1242/jcs.161729 · Cited by 79 · see citing works

Mammalian mitochondrial ribosomal small subunit (MRPS) genes: A putative role in human disease

Gopisetty, G., & Rajkumar, T. (2016) · Gene · doi:10.1016/j.gene.2016.05.008 · Cited by 72 · see citing works

The translational landscape of Arabidopsis mitochondria

Planchard, N., Bertin, P., Quadrado, M., Dargel-Graffin, C., Hatin, I., Namy, O., & Mireau, H. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky489 · Cited by 58 · see citing works

A variant inMRPS14(uS14m) causes perinatal hypertrophic cardiomyopathy with neonatal lactic acidosis, growth retardation, dysmorphic features and neurological involvement

Jackson, C. B., Huemer, M., Bolognini, R., Martin, F., Szinnai, G., Donner, B. C., Richter, U., Battersby, B. J., Nuoffer, J., Suomalainen, A., et al. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy374 · Cited by 45 · see citing works

The human RNA-binding protein RBFA promotes the maturation of the mitochondrial ribosome

Rozanska, A. L., Richter‐Dennerlein, R., Rorbach, J., Gao, F., Lewis, R. J., Chrzanowska‐Lightowlers, Z. M., & Lightowlers, R. N. (2017) · Biochemical Journal · doi:10.1042/bcj20170256 · Cited by 44 · see citing works

Structure of Human Mitochondrial Translation Initiation Factor 3 Bound to the Small Ribosomal Subunit

Koripella, R. K., Sharma, M. R., Haque, M. E., Risteff, P., Spremulli, L. L., & Agrawal, R. K. (2019) · iScience · doi:10.1016/j.isci.2018.12.030 · Cited by 44 · see citing works

Plant mitochondrial protein import: the ins and outs

Ghifari, A. S., Gill-Hille, M., & Murcha, M. W. (2018) · Biochemical Journal · doi:10.1042/bcj20170521 · Cited by 41 · see citing works

Translational control in aging and neurodegeneration

Skariah, G., & Todd, P. K. (2020) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1628 · Cited by 40 · see citing works

Structural insights into unique features of the human mitochondrial ribosome recycling

Koripella, R. K., Sharma, M. R., Risteff, P., Keshavan, P., & Agrawal, R. K. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1815675116 · Cited by 39 · see citing works

Identification of G8969>A in mitochondrial ATP6 gene that severely compromises ATP synthase function in a patient with IgA nephropathy

Wen, S., Niedźwiecka, K., Zhao, W., Xu, S., Liang, S., Zhu, X., Xie, H., Tribouillard‐Tanvier, D., Giraud, M., Zeng, C., et al. (2016) · Scientific Reports · doi:10.1038/srep36313 · Cited by 33 · see citing works

MrpL35, a mitospecific component of mitoribosomes, plays a key role in cytochrome c oxidase assembly

Box, J. M., Kaur, J., & Stuart, R. A. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-04-0239 · Cited by 33 · see citing works

Age-And Gender-Related Pattern of Methylation in the MT-RNR1 Gene

D’Aquila, P., Giordano, M., Montesanto, A., Rango, F. D., Passarino, G., & Bellizzi, D. (2015) · Epigenomics · doi:10.2217/epi.15.30 · Cited by 31 · see citing works

Drosophila protease ClpXP specifically degrades DmLRPPRC1 controlling mitochondrial mRNA and translation

Matsushima, Y., Hirofuji, Y., Aihara, M., Song, Y., Uchiumi, T., Kaguni, L. S., & Kang, D. (2017) · Scientific Reports · doi:10.1038/s41598-017-08088-6 · Cited by 28 · see citing works

Human mitochondrial ribosomes can switch structural tRNAs – but when and why?

Chrzanowska‐Lightowlers, Z. M., Rorbach, J., & Minczuk, M. A. (2017) · RNA Biology · doi:10.1080/15476286.2017.1356551 · Cited by 27 · see citing works

Structural insights into unique features of the human mitochondrial ribosome recycling

Sharma, M. R., Koripella, R. K., & Agrawal, R. K. (2019) · Worldwide Protein Data Bank · doi:10.2210/pdb6nu3/pdb · Cited by 27 · see citing works

Mitochondrial translation defects and human disease

Webb, B. D., Díaz, G. A., & Prasun, P. (2020) · Journal of Translational Genetics and Genomics · doi:10.20517/jtgg.2020.11 · Cited by 26 · see citing works

New Strains of Akkermansia muciniphila and Faecalibacterium prausnitzii are Effective for Improving the Muscle Strength of Mice with Immobilization-Induced Muscular Atrophy

Byeon, H. R., Jang, S.-Y., Lee, Y., Kim, D., Hong, M.-G., Lee, D., Shin, J., & Seo, J. (2022) · Journal of Medicinal Food · doi:10.1089/jmf.2021.k.0148 · Cited by 28 · see citing works

Mitochondrial ribosomal small subunit proteins (MRPS) MRPS6 and MRPS23 show dysregulation in breast cancer affecting tumorigenic cellular processes

Oviya, R. P., Gopisetty, G., Shirley, S., Velusamy, S., Jayavelu, S., & Rajkumar, T. (2021) · Gene · doi:10.1016/j.gene.2021.145697 · Cited by 24 · see citing works

Integration of Eukaryotic Energy Metabolism: The Intramitochondrial and Cytosolic Energy States ([ATP]f/[ADP]f[Pi])

Wilson, D. F., & Matschinsky, F. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105550 · Cited by 24 · see citing works

Exposure to arginine analog canavanine induces aberrant mitochondrial translation products, mitoribosome stalling, and instability of the mitochondrial proteome

Konovalova, S. A., Hilander, T., Loayza‐Puch, F., Rooijers, K., Agami, R., & Tyynismaa, H. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.06.018 · Cited by 24 · see citing works

The intriguing realm of protein biogenesis: Facing the green co-translational protein maturation networks

Breiman, A., Fieulaine, S., Meinnel, T., & Giglione, C. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2015.11.002 · Cited by 23 · see citing works

Pan-Cancer Analysis of Mitochondria Chaperone-Client Co-Expression Reveals Chaperone Functional Partitioning

Galai, G., Ben-David, H., Levin, L., Orth, M. F., Grünewald, T. G. P., Pilosof, S., Bershtein, S., & Rotblat, B. (2020) · Cancers · doi:10.3390/cancers12040825 · Cited by 19 · see citing works

The 55S mammalian mitochondrial ribosome and its tRNA-exit region

Kaushal, P. S., Sharma, M. R., & Agrawal, R. K. (2015) · Biochimie · doi:10.1016/j.biochi.2015.03.013 · Cited by 19 · see citing works

Translation initiation in mammalian mitochondria- a prokaryotic perspective

Ayyub, S. A., & Varshney, U. (2019) · RNA Biology · doi:10.1080/15476286.2019.1690099 · Cited by 18 · see citing works

Biochemical Characterization of Pathogenic Mutations in Human Mitochondrial Methionyl-tRNA Formyltransferase

Sinha, A., Köhrer, C., Weber, M. H. W., Masuda, I., Mootha, V. K., Hou, Y., & RajBhandary, U. L. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.610626 · Cited by 15 · see citing works

A Primer Genetic Toolkit for Exploring Mitochondrial Biology and Disease Using Zebrafish

Sabharwal, A., Campbell, J. M., Schwab, T. L., WareJoncas, Z., Wishman, M. D., Ata, H., Liu, W., Ichino, N., Hunter, D. E., Bergren, J. D., et al. (2022) · Genes · doi:10.3390/genes13081317 · Cited by 15 · see citing works

Fidelity of translation in the presence of mammalian mitochondrial initiation factor 3

Ayyub, S. A., Aswathy, S. L., Dobriyal, D., Aluri, S., Spremulli, L. L., & Varshney, U. (2017) · Mitochondrion · doi:10.1016/j.mito.2017.08.006 · Cited by 13 · see citing works

Messenger RNA delivery to mitoribosomes – hints from a bacterial toxin

Bruni, F., Proctor‐Kent, Y., Lightowlers, R. N., & Chrzanowska‐Lightowlers, Z. M. (2020) · FEBS Journal · doi:10.1111/febs.15342 · Cited by 13 · see citing works

Transcriptomic response of Drosophila melanogaster pupae developed in hypergravity

Hateley, S. L., Hosamani, R., Bhardwaj, S. R., Pachter, L. S., & Bhattacharya, S. (2016) · Genomics · doi:10.1016/j.ygeno.2016.09.002 · Cited by 13 · see citing works

Schizosaccharomyces pombe Mti2 and Mti3 act in conjunction during mitochondrial translation initiation

Luo, Y., Su, R., Wang, Y., Xie, W., Liu, Z., & Huang, Y. K. (2019) · FEBS Journal · doi:10.1111/febs.15021 · Cited by 13 · see citing works

The Mitochondrial Ribosome: A World of Opportunities for Mitochondrial Dysfunction Toward Parkinson's Disease

Gonçalves, A. M. R., Pereira-Santos, A. R., Esteves, A. R., Cardoso, S. M., & Empadinhas, N. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7997 · Cited by 13 · see citing works

Co-expression Network Analysis Reveals Key Genes Related to Ankylosing spondylitis Arthritis Disease: Computational and Experimental Validation.

Najafzadeh, L., Mahmoudi, M., Ebadi, M., & Shasaltaneh, M. D. (2021) · PubMed Central · doi:10.30498/ijb.2021.2630 · Cited by 12 · see citing works

Capture of Somatic mtDNA Point Mutations with Severe Effects on Oxidative Phosphorylation in Synaptosome Cybrid Clones from Human Brain

McKenzie, M., Chiotis, M., Hroudová, J., Sanchez, M. I. G. L., Lim, S. C., Cook, M. J., McKelvie, P. A., Cotton, R. G. H., Murphy, M., John, J. C. S., et al. (2014) · Human Mutation · doi:10.1002/humu.22694 · Cited by 12 · see citing works

Post-transcriptional diversity in riboproteins and RNAs in aging and cancer

da Cruz, J. B., & Lemos, B. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.08.012 · Cited by 10 · see citing works

Mitochondrial DNA sequencing reveals association of variants and haplogroup M33a2′3 with High altitude pulmonary edema susceptibility in Indian male lowlanders

Sharma, S., Singh, S., Gupta, R. K., Ganju, L., Singh, S. B., Kumar, B., & Singh, Y. (2019) · Scientific Reports · doi:10.1038/s41598-019-47500-1 · Cited by 11 · see citing works

Failure to Guard: Mitochondrial Protein Quality Control in Cancer

Friedlander, J. E., Shen, N., Zeng, A., Korm, S., & Feng, H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158306 · Cited by 11 · see citing works

High Mitochondrial Protein Expression as a Potential Predictor of Relapse Risk in Acute Myeloid Leukemia Patients with the Monocytic FAB Subtypes M4 and M5

Selheim, F., Aasebø, E., Bruserud, Ø., & Hernandez-Valladares, M. (2023) · Cancers · doi:10.3390/cancers16010008 · Cited by 9 · see citing works

Mammalian mitochondrial translation — revealing consequences of divergent evolution

Al-Faresi, R. A. Z., Lightowlers, R. N., & Chrzanowska‐Lightowlers, Z. M. (2019) · Biochemical Society Transactions · doi:10.1042/bst20190265 · Cited by 9 · see citing works

Pervasive Mitochondrial tRNA Gene Loss in Clade B of Haplosclerid Sponges (Porifera, Demospongiae)

Lavrov, D. V., Turner, T. L., & Vicente, J. (2025) · Genome Biology and Evolution · doi:10.1093/gbe/evaf020 · Cited by 8 · see citing works

The Analysis of Yeast Mitochondrial Translation

Carlström, A., Rzepka, M., & Ott, M. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0834-0_17 · Cited by 8 · see citing works

A Genome-Wide Functional Screen Identifies Enhancer and Protective Genes for Amyloid Beta-Peptide Toxicity

Picón-Pagès, P., Bosch-Morató, M., Subirana, L., Rubio-Moscardó, F., Guivernau, B., Fanlo-Ucar, H., Zeylan, M. E., Senyuz, S., Herrera-Fernández, V., Vicente, R., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021278 · Cited by 6 · see citing works

Methionine Improves Boar Sperm Quality by Promoting Mitochondrial Translation during Liquid Storage

Tan, M., Zhao, Y., Li, R., Li, C., Cai, J., & He, B. (2024) · Animals · doi:10.3390/ani14152227 · Cited by 5 · see citing works

Mitochondrial translation impairment-triggered neuroinflammation mediates fluoride-induced cognitive deficits

Liu, W., Wang, C., Tang, H., Tian, Z., Li, D., Chen, G., & Wang, A. (2025) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2025.119187 · Cited by 4 · see citing works

Biological Mechanisms of Aflatoxin B1-Induced Bile Metabolism Abnormalities in Ducklings

Chu, Y., Yu, A., Wang, H., Rajput, S. A., Yu, Q., & Qi, D. (2024) · Animals · doi:10.3390/ani14202996 · Cited by 4 · see citing works

Insights into the Biomarker Potential of Humanin and Mots-c Expression and Telomere Length in Alzheimer’s Disease

Rodríguez‐Esparragón, F., Cazorla-Rivero, S., Torrealba, E., Cánovas-Molina, Á., Hernández, A. N. G., Martín-Alfaro, R., Afonso-Medina, M. P., de Saavedra-Álvarez, M. T. M., Pérez-Santana, C. G., Bartolomé, C., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262210866 · Cited by 3 · see citing works

MRPL47 deficiency drives mitochondrial dysfunction via ROS-p38-p21 signaling in non-small cell lung cancer

Bhandari, N., Yengkhom, G., Acharya, D., Bhat, V., Chatterjee, A., Yalshetti, S., Arandkar, S., Chaube, B., & Shukla, S. K. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.111058 · Cited by 3 · see citing works

The Insertion Domain of Mti2 Facilitates the Association of Mitochondrial Initiation Factors with Mitoribosomes in Schizosaccharomyces pombe

Luo, Y., Bähler, J., & Huang, Y. (2025) · Biomolecules · doi:10.3390/biom15050695 · Cited by 2 · see citing works

The Protein Biosynthetic Machinery of Mitochondria

Spremulli, L. L. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.10066-5 · Cited by 2 · see citing works

Pleiotropic regulation of mitochondrial translational factors in governing proliferation, apoptosis and metastasis during cancer progression

Agarwal, N., Sharma, U., Shree, A., Kumar, R. R., Gorain, J. K., Vishwas, V., Jahan, F., Singh, A., Palanichamy, J. K., Pushpam, D., et al. (2026) · World Journal of Clinical Oncology · doi:10.5306/wjco.v17.i1.113600 · Cited by 1 · see citing works

Mitochondrial ribosomes in apicomplexan and trypanosomatid parasites: Dissimilar drivers of complexity and convergent features

Gahura, O., & Chauhan, P. S. (2026) · PLoS Pathogens · doi:10.1371/journal.ppat.1013920 · Cited by 1 · see citing works

GARUDA: the first complete mitochondrial genome of the endangered Javan hawk-eagle (Nisaetus bartelsi) and its phylogenetic relationships within Accipitridae

Priyono, D., Prakarsa, T. B., Eprilurahman, R., Arisuryanti, T., Ula, A. L., Abdul-Latiff, M. A. B., & Rahayuningsih, M. (2026) · Scientific Reports · doi:10.1038/s41598-026-57251-5

Importance of conserved hydrophobic pocket region in yeast mitoribosomal mL44 protein for mitotranslation and transcript preference

Box, J. M., Higgins, M. E., & Stuart, R. A. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107519 · Cited by 1 · see citing works

Assessment of mitochondrial DNA mutations in Chinese family with essential hypertension

Sun, G., He, F., Yao, H.-M., Han, Z., Lu, W.-J., Chen, X.-J., Wang, Z.-B., & Qiu, C. (2014) · Mitochondrial DNA Part A · doi:10.3109/19401736.2014.961148

Mitochondrial Ribosomal Protein S17 Silencing Inhibits Proliferation and Invasiveness of Lung Cancer Cells

Lee, W. R., & Ha, K. S. (2025) · Journal of Cancer Prevention · doi:10.15430/jcp.24.023

Mitochondrial Translation Inhibition Triggers an Rst2-Controlled Transcriptional Reprogramming of Carbon Metabolism in Stationary-Phase Cells of Fission Yeast

Luo, Y., Hassan, S., Raut, S., & Bähler, J. (2025) · Biomolecules · doi:10.3390/biom15101354

Mitochondrial mutations

Mahdi, A. G. M., & Mahdi, B. M. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-24836-8.00007-9

Études structurales de la trans-traduction, cible privilégiée pour le développement de nouveaux antibiotiques

Guyomar, C. (2018) · doi:10.70675/fbc75c6ez3a43z4ec9zab44z8e4d0b359aaa

Characterization of the mitochondrial translation apparatus of Arabidopsis thaliana

Waltz, F. (2018) · doi:10.70675/a2a2f5d9z45c7z4e67za4f5z548291e132d1

Structural characterization of the rescue mechanism of proteins synthesis in bacteria

D’Urso, G. (2022) · doi:10.70675/41c69952z9b9fz4022za074z400d52d844c8

Syndrome de Barth et recherche de voies thérapeutiques

Almyre, C. (2024) · theses.fr (ABES) · doi:10.70675/6de95820z84d7z467ez9477zb31adc2ae471

Peroxiredoxin 6 Silencing Remodels Lipid Metabolism and Redox Pathways to Promote Ferroptosis-Mediated Radiosensitization in Nonsmall Cell Lung Cancer

Pal, D., Patwardhan, R. S., & Sandur, S. K. (2026) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6c00317

Amino acid incorporation into the protein of mitochondria and mitochondrial fragments from beef heart

Kroon, A. M. (1963) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(63)91245-9 · Cited by 27 · see citing works

Organization and regulation of mitochondrial protein synthesis

Ott, M., Amunts, A., & Brown, A. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014334 · Cited by 282 · see citing works

Insights into Structural Basis of Mammalian Mitochondrial Translation

Sharma, M. R., Kaushal, P. S., Gupta, M. S., Banavali, N. K., & Agrawal, R. K. (2013) · Springer eBooks · doi:10.1007/978-3-642-39426-3_1 · Cited by 10 · see citing works

Translation in Mitochondrial Ribosomes

Chrzanowska‐Lightowlers, Z. M., & Lightowlers, R. N. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3171-3_4 · Cited by 1 · see citing works

High-resolution structures of mitochondrial ribosomes and their functional implications

Bieri, P., Greber, B. J., & Ban, N. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2017.12.009 · Cited by 59 · see citing works