Structural probing of a pathogenic tRNA dimer

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

Compilation of tRNA sequences and sequences of tRNA genes

Sprinzl, M. (2004) · Nucleic Acids Research · doi:10.1093/nar/gki012 · Cited by 1,916 · 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

Compilation of tRNA sequences and sequences of tRNA genes

Sprinzl, M. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.1.148 · Cited by 750 · see citing works

A subtype of diabetes mellitus associated with a mutation of mitochondrial DNA.

Kadowaki, T., Kadowaki, H., Mori, Y., Tobe, K., Sakuta, R., Suzuki, Y., Tanabe, Y., Sakura, H., Awata, T., Goto, Y.-I., et al. (1994) · New England Journal of Medicine · doi:10.1056/nejm199404073301403 · Cited by 551 · see citing works

Mitochondrial function in normal and diabetic β-cells

Maechler, P., & Wollheim, C. B. (2001) · Nature · doi:10.1038/414807a · Cited by 519 · 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

Identification of the primary site of the human immunodeficiency virus type 1 RNA dimerization in vitro

Skripkin, E., Paillart, J. C., Marquet, R., Ehresmann, B., & Ehresmann, C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.11.4945 · Cited by 401 · see citing works

Search for characteristic structural features of mammalian mitochondrial tRNAs

Helm, M., Brulé, H., FRIEDE, D., et al. (2000) · RNA · doi:10.1017/s1355838200001047 · Cited by 284 · 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

Ordered Interstrand and Intrastrand DNA Transfer During Reverse Transcription

Panganiban, A. T., & Fiore, D. (1988) · Science · doi:10.1126/science.2457948 · Cited by 221 · see citing works

Mutational analysis of the bipartite dimer linkage structure of human immunodeficiency virus type 1 genomic RNA

Paillart, J. C., Marquet, R., Skripkin, E., Ehresmann, B., & Ehresmann, C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47011-1 · Cited by 201 · see citing works

Crystal structures of coaxially stacked kissing complexes of the HIV-1 RNA dimerization initiation site.

Ennifar, E., Walter, P., Ehresmann, B., Ehresmann, C., & Dumas, P. (2001) · Nature Structural Biology · doi:10.1038/nsb727 · Cited by 199 · see citing works

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

Chomyn, A., Enriquez, J. A., Micol, V., Fernandez-Silva, P., & Attardi, G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m908734199 · Cited by 197 · see citing works

Dimerization of human immunodeficiency virus (type 1) RNA: stimulation by cations and possible mechanism

Marquet, R., Baudin, F., Gabus, C., Darlix, J., Mougel, M., Ehresmann, C., & Ehresmann, B. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.9.2349 · Cited by 180 · see citing works

Kissing-Loop Model of HIV-1 Genome Dimerization: HIV-1 RNAs Can Assume Alternative Dimeric Forms, and All Sequences Upstream or Downstream of Hairpin 248−271 Are Dispensable for Dimer Formation

Laughrea, M., & Jetté, L. (1996) · Biochemistry · doi:10.1021/bi951838f · Cited by 175 · see citing works

Lead-catalyzed cleavage of yeast tRNAPhe mutants

Behlen, L. S., Sampson, J. R., DiRenzo, A. B., & Uhlenbeck, O. C. (1990) · Biochemistry · doi:10.1021/bi00462a013 · Cited by 155 · see citing works

A Kissing Complex Together with a Stable Dimer Is Involved in the HIV-1Lai RNA Dimerization Process in Vitro

Muriaux, D. M., Fossé, P., & Paoletti, J. (1996) · Biochemistry · doi:10.1021/bi952822s · Cited by 152 · see citing works

Stabilization of RNA Structure by Mg Ions

Laing, L. G., Gluick, T. C., & Draper, D. E. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1256 · Cited by 151 · 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

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

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

Decreased aminoacylation of mutant tRNAs in MELAS but not in MERRF patients

Börner, G. V. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.4.467 · Cited by 92 · 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

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

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 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

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

Impairment of tRNA processing by point mutations in mitochondrial tRNA^Leu(UUR) associated with mitochondrial diseases

Rossmanith, W., & Karwan, R. M. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00928-4 · Cited by 73 · see citing works

Enormously Fast RNA Hydrolysis by Lanthanide(III) Ions under Physiological Conditions: Eminent Candidates for Novel Tools of Biotechnology

Matsumura, K., & Komiyama, M. (1997) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a021765 · 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 Short Autocomplementary Sequence Plays an Essential Role in Avian Sarcoma−Leukosis Virus RNA Dimerization

Fossé, P., Motté, N., Roumier, A., Gabus, C., Muriaux, D. M., Darlix, J., & Paoletti, J. (1996) · Biochemistry · doi:10.1021/bi9613786 · Cited by 57 · see citing works

The np 3243 MELAS mutation: damned if you aminoacylate, damned if you don't

Jacobs, H. T. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.4.463 · Cited by 45 · see citing works

Use of terbium as a probe of tRNA tertiary structure and folding

Hargittai, M. R. S., & Musier‐Forsyth, K. (2000) · RNA · doi:10.1017/s135583820000128x · Cited by 42 · see citing works

Magnesium-dependent alternative foldings of active and inactive Escherichia coli tRNAGIU revealed by chemical probing

Madore, É., Florentz, C., Giegé, R., & Lapointe, J. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.17.3583 · Cited by 39 · see citing works

Dimers of alanine transfer RNA with acceptor activity.

Loehr, J. S., & Keller, E. B. (1968) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.61.3.1115 · Cited by 38 · see citing works

Serine Specific Transfer Ribonucleic Acids. 16. Aggregation of Serine Specific Transfer Ribonucleic Acids

Zachau, H. G. (1968) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1968.tb00406.x · Cited by 36 · see citing works

Mitochondrial tRNALeu isoforms in lung carcinoma cybrid cells containing the np 3243 mtDNA mutation

Meziane, A. E. (1998) · Human Molecular Genetics · doi:10.1093/hmg/7.13.2141 · Cited by 36 · see citing works

Properties of a dimer of tRNATyr (Escherichia coli)

Yang, S. K., Soell, D., & Crothers, D. M. (1972) · Biochemistry · doi:10.1021/bi00762a016 · 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

GEL FILTRATION PROPERTIES OF CCD-PREPARED E. COLI B sRNA

Schleich, T., & Goldstein, J. (1964) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.52.3.744 · Cited by 31 · see citing works

The pathogenic U3271C human mitochondrial tRNALeu(UUR) mutation disrupts a fragile anticodon stem

Wittenhagen, L. M. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg131 · Cited by 26 · see citing works

Increased mitochondrial processing intermediates associated with three tRNALeu(UUR) gene mutations

Koga, A., Koga, Y., Akita, Y., Fukiyama, R., Ueki, I., Yatsuga, S., & Matsuishi, T. (2003) · Neuromuscular Disorders · doi:10.1016/s0960-8966(02)00267-5 · Cited by 24 · see citing works

Dimer formation by tRNAs.

Kholod, N. (1999) · PubMed · Cited by 15 · see citing works

Specific aggregation of yeast glycine tRNA

HAMPEL, A. E., Cherayil, J. D., & Bock, R. M. (1971) · Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis · doi:10.1016/0005-2787(71)90053-0 · Cited by 14 · see citing works

tRNA processing in human mitochondrial disorders

Masucci, J. P., & Schon, E. A. (1996) · Molecular Biology Reports · doi:10.1007/bf00988727 · Cited by 10 · see citing works

Interdomain Communication between Weak Structural Elements within a Disease-Related Human tRNA

Roy, M. D., Wittenhagen, L. M., Vozzella, B. E., et al. (2003) · Biochemistry · doi:10.1021/bi035711z · Cited by 8 · 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

Ab initio study on the dimer structures of trimethylaluminum and dimethylaluminumhydride

Hiraoka, Y. S., & Mashita, M. (1994) · Journal of Crystal Growth · doi:10.1016/0022-0248(94)91094-4 · Cited by 28 · see citing works

Anticodon conformation and accessibility in wild-type and suppressor tryptophan. tRNA from E.coli.

Buckingham, R. H. (1976) · Nucleic Acids Research · doi:10.1093/nar/3.4.965 · Cited by 22 · see citing works

Comparison of calculated structural parameters and infrared spectra with experimental data for dimeric dibenzyl carbamic acid

Jamróz, M. H., Dobrowolski, J. C., Rode, J. E., et al. (2002) · Journal of Molecular Structure THEOCHEM · doi:10.1016/s0166-1280(02)00465-7 · Cited by 14 · see citing works

Infrared spectroscopic evidence for the initial step of dissociation of the stable benzoic acid cyclic dimer with microsolvation by a single water molecule

Katada, M., & Fujii, A. (2017) · Chemical Physics Letters · doi:10.1016/j.cplett.2017.07.028 · Cited by 8 · see citing works

고분자 재료의 형광 크랙센서

조성열, 김지은, 김중곤, et al. (2008) · Polymer(Korea) · Cited by 4 · see citing works