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Volumn 49, Issue 1, 2014, Pages 69-89

Functional implications of ribosomal RNA methylation in response to environmental stress

Author keywords

Adaptation; Cold shock; Extremophile; Heat shock; Methyltransferase; Oxidative stress; Prokaryote; Transcriptome

Indexed keywords

BACTERIAL RNA; GUIDE RNA; RIBONUCLEOPROTEIN; RIBOSOME RECYCLING FACTOR; RIBOSOME RNA; RNA 16S; RNA 23S; RNA METHYLTRANSFERASE; SMALL NUCLEOLAR RIBONUCLEOPROTEIN; SMALL SUBUNIT RIBOSOMAL RNA; TRANSCRIPTOME; TRANSFER RNA; UNTRANSLATED RNA;

EID: 84893100455     PISSN: 10409238     EISSN: 15497798     Source Type: Journal    
DOI: 10.3109/10409238.2013.859229     Document Type: Review
Times cited : (28)

References (215)
  • 1
    • 84860741715 scopus 로고    scopus 로고
    • Mutations in NSUN2 cause autosomal-recessive intellectual disability
    • Abbasi-Moheb L, Mertel S, Gonsior M, et al. (2012). Mutations in NSUN2 cause autosomal-recessive intellectual disability. Am J Hum Gen 90:847-55.
    • (2012) Am J Hum Gen , vol.90 , pp. 847-855
    • Abbasi-Moheb, L.1    Mertel, S.2    Gonsior, M.3
  • 2
    • 0037088598 scopus 로고    scopus 로고
    • Characterization of the 23 S ribosomal RNA m5U1939 methyltransferase from Escherichia coli
    • Agarwalla S, Kealey JT, Santi DV, Stroud RM. (2002). Characterization of the 23 S ribosomal RNA m5U1939 methyltransferase from Escherichia coli. J Biol Chem 277:8835-40.
    • (2002) J Biol Chem , vol.277 , pp. 8835-8840
    • Agarwalla, S.1    Kealey, J.T.2    Santi, D.V.3    Stroud, R.M.4
  • 3
    • 0015541340 scopus 로고
    • The effect of growth temperatures on the in vivo ribose methylation of Bacillus stearothermophilus transfer RNA
    • Agris P, Koh H, Söll D. (1973). The effect of growth temperatures on the in vivo ribose methylation of Bacillus stearothermophilus transfer RNA. Arch Biochem Biophys 154:277-82.
    • (1973) Arch Biochem Biophys , vol.154 , pp. 277-282
    • Agris, P.1    Koh, H.2    Söll, D.3
  • 4
    • 29544450711 scopus 로고    scopus 로고
    • Rapid tRNA decay can result from lack of nonessential modifications
    • Alexandrov A, Chernyakov I, Gu W, et al. (2006). Rapid tRNA decay can result from lack of nonessential modifications. Mol Cell 21: 87-96.
    • (2006) Mol Cell , vol.21 , pp. 87-96
    • Alexandrov, A.1    Chernyakov, I.2    Gu, W.3
  • 5
    • 33646806139 scopus 로고    scopus 로고
    • YebU is a m5C methyltransferase specific for 16 S rRNA nucleotide 1407
    • Andersen NM, Douthwaite S. (2006). YebU is a m5C methyltransferase specific for 16 S rRNA nucleotide 1407. J Mol Biol 359:777-86.
    • (2006) J Mol Biol , vol.359 , pp. 777-786
    • Andersen, N.M.1    Douthwaite, S.2
  • 6
    • 2442686628 scopus 로고    scopus 로고
    • A novel partial modification at C2501 in Escherichia coli 23S ribosomal RNA
    • Andersen TE, Porse BT, Kirpekar F. (2004). A novel partial modification at C2501 in Escherichia coli 23S ribosomal RNA. RNA (New York, NY) 10:907-13.
    • (2004) RNA (New York, NY) , vol.10 , pp. 907-913
    • Andersen, T.E.1    Porse, B.T.2    Kirpekar, F.3
  • 7
    • 78649637486 scopus 로고    scopus 로고
    • S-Adenosylmethioninedependent radical-based modification of biological macromolecules
    • Atta M, Mulliez E, Arragain S, et al. (2010). S- Adenosylmethioninedependent radical-based modification of biological macromolecules. Curr Opin Struct Biol 20:684-92.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 684-692
    • Atta, M.1    Mulliez, E.2    Arragain, S.3
  • 8
    • 50549192559 scopus 로고
    • Modification of the aminoacid code after bromination of transfer {RNA}
    • Bakès J, Befort N, Weil JH, Ebel JP. (1965). Modification of the aminoacid code after bromination of transfer {RNA}. Biochem Biophys Res Commun 19:84-8.
    • (1965) Biochem Biophys Res Commun , vol.19 , pp. 84-88
    • Bakès, J.1    Befort, N.2    Weil, J.H.3    Ebel, J.P.4
  • 9
    • 0028088197 scopus 로고
    • The single pseudouridine residue in Escherichia coli 16S RNA is located at position 516
    • Bakin A, Kowalak JA, McCloskey JA, Ofengand J. (1994). The single pseudouridine residue in Escherichia coli 16S RNA is located at position 516. Nucl Acids Res 22:3681-4.
    • (1994) Nucl Acids Res , vol.22 , pp. 3681-3684
    • Bakin, A.1    Kowalak, J.A.2    McCloskey, J.A.3    Ofengand, J.4
  • 10
    • 0027438034 scopus 로고
    • Four newly located pseudouridylate residues in Escherichia coli 23S ribosomal RNA are all at the peptidyltransferase center: Analysis by the application of a new sequencing technique
    • Bakin A, Ofengand J. (1993). Four newly located pseudouridylate residues in Escherichia coli 23S ribosomal RNA are all at the peptidyltransferase center: analysis by the application of a new sequencing technique. Biochemistry 32:9754-62.
    • (1993) Biochemistry , vol.32 , pp. 9754-9762
    • Bakin, A.1    Ofengand, J.2
  • 11
    • 84874271270 scopus 로고    scopus 로고
    • NCBI GEO: Archive for functional genomics data sets - Update
    • Barrett T, Wilhite SE, Ledoux P, et al. (2013). NCBI GEO: archive for functional genomics data sets - update. Nucl Acids Res 41:D991-5.
    • (2013) Nucl Acids Res , vol.41
    • Barrett, T.1    Wilhite, S.E.2    Ledoux, P.3
  • 12
    • 84855258750 scopus 로고    scopus 로고
    • YhiQ is RsmJ, the methyltransferase responsible for methylation of G1516 in 16S rRNA of e
    • Basturea GN, Dague DR, Deutscher MP, Rudd KE. (2012). YhiQ is RsmJ, the methyltransferase responsible for methylation of G1516 in 16S rRNA of E. coli. J Mol Biol 415:16-21.
    • (2012) Coli. J Mol Biol , vol.415 , pp. 16-21
    • Basturea, G.N.1    Dague, D.R.2    Deutscher, M.P.3    Rudd, K.E.4
  • 13
    • 35549012369 scopus 로고    scopus 로고
    • Substrate specificity and properties of the Escherichia coli 16S rRNA methyltransferase, RsmE
    • Basturea GN, Deutscher MP, Dague DR, Rudd KE. (2007). Substrate specificity and properties of the Escherichia coli 16S rRNA methyltransferase, RsmE. RNA (New York, NY) 13:1969-76.
    • (2007) RNA (New York, NY) , vol.13 , pp. 1969-1976
    • Basturea, G.N.1    Deutscher, M.P.2    Dague, D.R.3    Rudd, K.E.4
  • 14
    • 33344476204 scopus 로고    scopus 로고
    • Identification and characterization of RsmE, the founding member of a new RNA base methyltransferase family
    • Basturea GN, Rudd KE, Deutscher MP. (2006). Identification and characterization of RsmE, the founding member of a new RNA base methyltransferase family. RNA (New York, NY) 12:426-34.
    • (2006) RNA (New York, NY) , vol.12 , pp. 426-434
    • Basturea, G.N.1    Rudd, K.E.2    Deutscher, M.P.3
  • 15
    • 83255187900 scopus 로고    scopus 로고
    • Requirement of rRNA methylation for 80S ribosome assembly on a cohort of cellular Internal Ribosome Entry Sites
    • Basu A, Das P, Chaudhuri S, et al. (2011). Requirement of rRNA methylation for 80S ribosome assembly on a cohort of cellular Internal Ribosome Entry Sites. Mol Cell Biol 31:4482-99.
    • (2011) Mol Cell Biol , vol.31 , pp. 4482-4499
    • Basu, A.1    Das, P.2    Chaudhuri, S.3
  • 16
    • 6044222469 scopus 로고    scopus 로고
    • The A2453-C2499 wobble base pair in Escherichia coli 23S ribosomal RNA is responsible for pH sensitivity of the peptidyltransferase active site conformation
    • Bayfield MA, Thompson J, Dahlberg AE. (2004). The A2453-C2499 wobble base pair in Escherichia coli 23S ribosomal RNA is responsible for pH sensitivity of the peptidyltransferase active site conformation. Nucl Acids Res 32:5512-18.
    • (2004) Nucl Acids Res , vol.32 , pp. 5512-5518
    • Bayfield, M.A.1    Thompson, J.2    Dahlberg, A.E.3
  • 17
    • 84866603533 scopus 로고    scopus 로고
    • The Escherichia coli RlmN methyltransferase is a dual-specificity enzyme that modifies both rRNA and tRNA and controls translational accuracy
    • Benítez-Páez A, Villarroya M, Armengod M-E. (2012). The Escherichia coli RlmN methyltransferase is a dual-specificity enzyme that modifies both rRNA and tRNA and controls translational accuracy. RNA (New York, NY) 18: 1783-95.
    • (2012) RNA (New York, NY) , vol.18 , pp. 1783-1795
    • Benítez-Páez, A.1    Villarroya, M.2    Armengod, M.-E.3
  • 18
    • 34247589630 scopus 로고    scopus 로고
    • The ribosomal peptidyl transferase
    • Beringer M, Rodnina MV. (2007). The ribosomal peptidyl transferase. Mol Cell 26:311-21.
    • (2007) Mol Cell , vol.26 , pp. 311-321
    • Beringer, M.1    Rodnina, M.V.2
  • 19
    • 0035863196 scopus 로고    scopus 로고
    • A primordial tRNA modification required for the evolution of life?
    • Björk G, Jacobsson K, Nilsson K. (2001). A primordial tRNA modification required for the evolution of life? EMBO J 20:231-9.
    • (2001) EMBO J , vol.20 , pp. 231-239
    • Björk, G.1    Jacobsson, K.2    Nilsson, K.3
  • 20
    • 0016780419 scopus 로고
    • Physiological and biochemical studies on the function of 5-methyluridine in the transfer ribonucleic acid of Escherichia coli
    • Björk GR, Neidhardt FC. (1975). Physiological and biochemical studies on the function of 5-methyluridine in the transfer ribonucleic acid of Escherichia coli. J Bacteriol 124:99-111.
    • (1975) J Bacteriol , vol.124 , pp. 99-111
    • Björk, G.R.1    Neidhardt, F.C.2
  • 21
    • 84858968097 scopus 로고    scopus 로고
    • Structural insights into methyltransferase KsgA function in 30S ribosomal subunit biogenesis
    • Boehringer D, O'Farrell HC, Rife JP, Ban N. (2012). Structural insights into methyltransferase KsgA function in 30S ribosomal subunit biogenesis. J Biol Chem 287:10453-9.
    • (2012) J Biol Chem , vol.287 , pp. 10453-10459
    • Boehringer, D.1    O'farrell, H.C.2    Rife, J.P.3    Ban, N.4
  • 22
    • 15444361014 scopus 로고
    • The methylation of nucleic acids
    • Borek E, Srinivasan P. (1966). The methylation of nucleic acids. Annu Rev Biochem 35:275-98.
    • (1966) Annu Rev Biochem , vol.35 , pp. 275-298
    • Borek, E.1    Srinivasan, P.2
  • 23
    • 0035449350 scopus 로고    scopus 로고
    • Translational misreading: A tRNA modification counteracts a +2 ribosomal frameshift
    • Brégeon D, Colot V, Radman M, Taddei F. (2001). Translational misreading: a tRNA modification counteracts a +2 ribosomal frameshift. Genes Dev 15:2295-306.
    • (2001) Genes Dev , vol.15 , pp. 2295-2306
    • Brégeon, D.1    Colot, V.2    Radman, M.3    Taddei, F.4
  • 24
    • 70349675501 scopus 로고    scopus 로고
    • Parallel isotope-based quantification of modified tRNA nucleosides
    • Brückl T, Globisch D, Wagner M, et al. (2009). Parallel isotope-based quantification of modified tRNA nucleosides. Angew Chem (Int Ed. Eng) 48:7932-4.
    • (2009) Angew Chem (Int Ed. Eng) , vol.48 , pp. 7932-7934
    • Brückl, T.1    Globisch, D.2    Wagner, M.3
  • 25
    • 0027492777 scopus 로고
    • 5S rRNA modification in the hyperthermophilic archaea Sulfolobus solfataricus and Pyrodictium occultum
    • Bruenger E, Kowalak JA, Kuchino Y, et al. (1993). 5S rRNA modification in the hyperthermophilic archaea Sulfolobus solfataricus and Pyrodictium occultum. FASEB J 7:196-200.
    • (1993) FASEB J , vol.7 , pp. 196-200
    • Bruenger, E.1    Kowalak, J.A.2    Kuchino, Y.3
  • 26
    • 33947100861 scopus 로고    scopus 로고
    • The genome of Hyperthermus butylicus: A sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 C
    • Brügger K, Chen L, Stark M, et al. (2007). The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 C. Archaea (Vancouver, BC) 2: 127-35.
    • (2007) Archaea (Vancouver, BC) , vol.2 , pp. 127-135
    • Brügger, K.1    Chen, L.2    Stark, M.3
  • 27
    • 0033637117 scopus 로고    scopus 로고
    • RNA methylation under heat shock control
    • Bügl H, Fauman EB, Staker BL, et al. (2000). RNA methylation under heat shock control. Mol Cell 6:349-60.
    • (2000) Mol Cell , vol.6 , pp. 349-360
    • Bügl, H.1    Fauman, E.B.2    Staker, B.L.3
  • 28
    • 13444283630 scopus 로고    scopus 로고
    • Interaction network containing conserved and essential protein complexes in Escherichia coli
    • Butland G, Peregrin-Alvarez JM, Li J, et al. (2005). Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433:531-7.
    • (2005) Nature , vol.433 , pp. 531-537
    • Butland, G.1    Peregrin-Alvarez, J.M.2    Li, J.3
  • 29
    • 0034596029 scopus 로고    scopus 로고
    • The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23 S ribosomal RNA methyltransferase
    • Caldas T, Binet E, Bouloc P, et al. (2000). The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23 S ribosomal RNA methyltransferase. J Biol Chem 275:16414-19.
    • (2000) J Biol Chem , vol.275 , pp. 16414-16419
    • Caldas, T.1    Binet, E.2    Bouloc, P.3
  • 30
    • 0035163770 scopus 로고    scopus 로고
    • Identification and site of action of the remaining four putative pseudouridine synthases in Escherichia coli
    • Campo M Del, Kaya Y, Ofengand J. (2001). Identification and site of action of the remaining four putative pseudouridine synthases in Escherichia coli. RNA (New York, NY) 7:1603-15.
    • (2001) RNA (New York, NY) , vol.7 , pp. 1603-1615
    • Del Campo, M.1    Kaya, Y.2    Ofengand, J.3
  • 31
    • 12844276454 scopus 로고    scopus 로고
    • Number, position, and significance of the pseudouridines in the large subunit ribosomal RNA of Haloarcula marismortui and Deinococcus radiodurans
    • Campo M Del, Recinos C. (2005). Number, position, and significance of the pseudouridines in the large subunit ribosomal RNA of Haloarcula marismortui and Deinococcus radiodurans. RNA (New York, NY) 11: 210-19.
    • (2005) RNA (New York, NY) , vol.11 , pp. 210-219
    • Del Campo, M.1    Recinos, C.2
  • 32
    • 78651335915 scopus 로고    scopus 로고
    • The RNA modification database, RNAMDB: 2011 update
    • Cantara WA, Crain PF, Rozenski J, et al. (2011). The RNA modification database, RNAMDB: 2011 update. Nucl Acids Res 39: D195-201.
    • (2011) Nucl Acids Res , vol.39
    • Cantara, W.A.1    Crain, P.F.2    Rozenski, J.3
  • 34
    • 35648960799 scopus 로고    scopus 로고
    • Expanding the nucleotide repertoire of the ribosome with post-transcriptional modifications
    • Chow CS, Lamichhane TN, Mahto SK. (2007). Expanding the nucleotide repertoire of the ribosome with post-transcriptional modifications. ACS Chem Biol 2:610-19.
    • (2007) ACS Chem Biol , vol.2 , pp. 610-619
    • Chow, C.S.1    Lamichhane, T.N.2    Mahto, S.K.3
  • 35
    • 80053925220 scopus 로고    scopus 로고
    • Network-based functional modeling of genomics, transcriptomics and metabolism in bacteria
    • Cloots L, Marchal K. (2011). Network-based functional modeling of genomics, transcriptomics and metabolism in bacteria. Curr Opin Microbiol 14:599-607.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 599-607
    • Cloots, L.1    Marchal, K.2
  • 36
    • 22244449849 scopus 로고    scopus 로고
    • Two different mechanisms for tRNA ribose methylation in Archaea: A short survey
    • Clouet-d'Orval B, Gaspin C, Mougin A. (2005). Two different mechanisms for tRNA ribose methylation in Archaea: a short survey. Biochimie 87:889-95.
    • (2005) Biochimie , vol.87 , pp. 889-895
    • Clouet-D'orval, B.1    Gaspin, C.2    Mougin, A.3
  • 37
    • 55349106559 scopus 로고    scopus 로고
    • Mechanistic insight into the ribosome biogenesis functions of the ancient protein KsgA
    • Connolly K, Rife JP, Culver G. (2008). Mechanistic insight into the ribosome biogenesis functions of the ancient protein KsgA. Mol Microbiol 70:1062-75.
    • (2008) Mol Microbiol , vol.70 , pp. 1062-1075
    • Connolly, K.1    Rife, J.P.2    Culver, G.3
  • 38
    • 0032540887 scopus 로고    scopus 로고
    • The rluC gene of Escherichia coli codes for a pseudouridine synthase that is solely responsible for synthesis of pseudouridine at positions 955, 2504, and 2580 in 23 S ribosomal RNA
    • Conrad J, Sun D, Englund N, Ofengand J. (1998). The rluC gene of Escherichia coli codes for a pseudouridine synthase that is solely responsible for synthesis of pseudouridine at positions 955, 2504, and 2580 in 23 S ribosomal RNA. J Biol Chem 273:18562-6.
    • (1998) J Biol Chem , vol.273 , pp. 18562-18566
    • Conrad, J.1    Sun, D.2    Englund, N.3    Ofengand, J.4
  • 39
    • 33646555833 scopus 로고    scopus 로고
    • Protein translocation through a tunnel induces changes in folding kinetics: A lattice model study
    • Contreras Martínez LM, Martínez-Veracoechea FJ, Pohkarel P, et al. (2006). Protein translocation through a tunnel induces changes in folding kinetics: a lattice model study. Biotechnol Bioeng 94: 105-17.
    • (2006) Biotechnol Bioeng , vol.94 , pp. 105-117
    • Contreras Martínez, L.M.1    Martínez-Veracoechea, F.J.2    Pohkarel, P.3
  • 40
    • 34547946010 scopus 로고    scopus 로고
    • Intracellular ribosome display via SecM translation arrest as a selection for antibodies with enhanced cytosolic stability
    • Contreras-Martínez LM, DeLisa MP. (2007). Intracellular ribosome display via SecM translation arrest as a selection for antibodies with enhanced cytosolic stability. J Mol Biol 372:513-24.
    • (2007) J Mol Biol , vol.372 , pp. 513-524
    • Contreras-Martínez, L.M.1    Delisa, M.P.2
  • 43
    • 58149191269 scopus 로고    scopus 로고
    • MODOMICS: A database of RNA modification pathways. 2008 update
    • Czerwoniec A, Dunin-Horkawicz S, Purta E, et al. (2009). MODOMICS: a database of RNA modification pathways. 2008 update. Nucl Acids Res 37:D118-21.
    • (2009) Nucl Acids Res , vol.37
    • Czerwoniec, A.1    Dunin-Horkawicz, S.2    Purta, E.3
  • 44
    • 0018462013 scopus 로고
    • Role of ribothymidine in the thermal stability of transfer RNA as monitored by proton magnetic resonance
    • Davanloo P, Sprinzl M, Watanabe K, et al. (1979). Role of ribothymidine in the thermal stability of transfer RNA as monitored by proton magnetic resonance. Nucl Acids Res 6:1571-81.
    • (1979) Nucl Acids Res , vol.6 , pp. 1571-1581
    • Davanloo, P.1    Sprinzl, M.2    Watanabe, K.3
  • 45
    • 0031803072 scopus 로고    scopus 로고
    • Post-transcriptional gene regulatory mechanisms in eukaryotes: An overview
    • Day D, Tuite MF. (1998). Post-transcriptional gene regulatory mechanisms in eukaryotes: an overview. J Endocrinol 157:361-71.
    • (1998) J Endocrinol , vol.157 , pp. 361-371
    • Day, D.1    Tuite, M.F.2
  • 46
    • 0036629250 scopus 로고    scopus 로고
    • RRNA modifications and ribosome function
    • Decatur W, Fournier M. (2002). rRNA modifications and ribosome function. Trends Biochem Sci 27:344-51.
    • (2002) Trends Biochem Sci , vol.27 , pp. 344-351
    • Decatur, W.1    Fournier, M.2
  • 47
    • 33646128243 scopus 로고    scopus 로고
    • The adenosine dimethyltransferase KsgA recognizes a specific conformational state of the 30S ribosomal subunit
    • Desai PM, Rife JP. (2006). The adenosine dimethyltransferase KsgA recognizes a specific conformational state of the 30S ribosomal subunit. Arch Biochem Biophys 449:57-63.
    • (2006) Arch Biochem Biophys , vol.449 , pp. 57-63
    • Desai, P.M.1    Rife, J.P.2
  • 48
    • 84872032385 scopus 로고    scopus 로고
    • Transcriptome-wide mapping of N(6)-methyladenosine by m(6)A-seq based on immunocapturing and massively parallel sequencing
    • Dominissini D, Moshitch-Moshkovitz S, Salmon-Divon M, et al. (2013). Transcriptome-wide mapping of N(6)-methyladenosine by m(6)A-seq based on immunocapturing and massively parallel sequencing. Nature Protocols 8:176-89.
    • (2013) Nature Protocols , vol.8 , pp. 176-189
    • Dominissini, D.1    Moshitch-Moshkovitz, S.2    Salmon-Divon, M.3
  • 49
    • 84860779086 scopus 로고    scopus 로고
    • Topology of the human and mouse m6A RNA methylomes revealed by m6A-seq
    • Dominissini D, Moshitch-Moshkovitz S, Schwartz S, et al. (2012). Topology of the human and mouse m6A RNA methylomes revealed by m6A-seq. Nature 485:201-6.
    • (2012) Nature , vol.485 , pp. 201-206
    • Dominissini, D.1    Moshitch-Moshkovitz, S.2    Schwartz, S.3
  • 51
    • 84879642219 scopus 로고    scopus 로고
    • Transcriptomewide mapping of 5-methylcytidine RNA modifications in bacteria, archaea, and yeast reveals m5C within archaeal mRNAs
    • Edelheit S, Schwartz S, Mumbach MR, et al. (2013). Transcriptomewide mapping of 5-methylcytidine RNA modifications in bacteria, archaea, and yeast reveals m5C within archaeal mRNAs. PLoS Genet 9:e1003602.
    • (2013) PLoS Genet , vol.9
    • Edelheit, S.1    Schwartz, S.2    Mumbach, M.R.3
  • 52
    • 0036081355 scopus 로고    scopus 로고
    • Gene expression omnibus: NCBI gene expression and hybridization array data repository
    • Edgar R, Domrachev M, Lash AE. (2002). Gene expression omnibus: NCBI gene expression and hybridization array data repository. Nucl Acids Res 30:207-10.
    • (2002) Nucl Acids Res , vol.30 , pp. 207-210
    • Edgar, R.1    Domrachev, M.2    Lash, A.E.3
  • 53
    • 84870152928 scopus 로고    scopus 로고
    • Biosynthesis and function of posttranscriptional modifications of transfer RNAs
    • El Yacoubi B, Bailly M, de Crécy-Lagard V. (2012). Biosynthesis and function of posttranscriptional modifications of transfer RNAs. Annu Rev Genet 46:69-95.
    • (2012) Annu Rev Genet , vol.46 , pp. 69-95
    • El Yacoubi, B.1    Bailly, M.2    De Crécy-Lagard, V.3
  • 54
    • 78149292161 scopus 로고    scopus 로고
    • Specificity and kinetics of 23S rRNA modification enzymes RlmH and RluD
    • Ero R, Leppik M, Liiv A, Remme J. (2010). Specificity and kinetics of 23S rRNA modification enzymes RlmH and RluD. RNA (NY) 16: 2075-84.
    • (2010) RNA (NY) , vol.16 , pp. 2075-2084
    • Ero, R.1    Leppik, M.2    Liiv, A.3    Remme, J.4
  • 55
    • 52949137027 scopus 로고    scopus 로고
    • Identification of pseudouridine methyltransferase in Escherichia coli
    • Ero R, Peil L, Liiv A, Remme J. (2008). Identification of pseudouridine methyltransferase in Escherichia coli. RNA (NY) 14:2223-33.
    • (2008) RNA (NY) , vol.14 , pp. 2223-2233
    • Ero, R.1    Peil, L.2    Liiv, A.3    Remme, J.4
  • 56
    • 84877750692 scopus 로고    scopus 로고
    • FTO-mediated formation of N6- hydroxymethyladenosine and N6-formyladenosine in mammalian RNA
    • Fu Y, Jia G, Pang X, et al. (2013). FTO-mediated formation of N6- hydroxymethyladenosine and N6-formyladenosine in mammalian RNA. Nature Commun 4:1798.
    • (2013) Nature Commun , vol.4 , pp. 1798
    • Fu, Y.1    Jia, G.2    Pang, X.3
  • 57
    • 0034615782 scopus 로고    scopus 로고
    • Archaeal homologs of eukaryotic methylation guide small nucleolar RNAs: Lessons from the Pyrococcus genomes
    • Gaspin C, Cavaillé J, Erauso G, Bachellerie JP. (2000). Archaeal homologs of eukaryotic methylation guide small nucleolar RNAs: lessons from the Pyrococcus genomes. J Mol Biol 297:895-906.
    • (2000) J Mol Biol , vol.297 , pp. 895-906
    • Gaspin, C.1    Cavaillé, J.2    Erauso, G.3    Bachellerie, J.P.4
  • 58
    • 84875514519 scopus 로고    scopus 로고
    • {RNA} Pseudouridylation: New insights into an old modification
    • Ge J, Yu Y-T. (2013). {RNA} pseudouridylation: new insights into an old modification. Trends Biochem Sci 38:210-18.
    • (2013) Trends Biochem Sci , vol.38 , pp. 210-218
    • Ge, J.1    Yu, Y.-T.2
  • 59
    • 0014674092 scopus 로고
    • Role of modifications in tyrosine transfer RNA: A modified base affecting ribosome binding
    • Gefter ML, Russell RL. (1969). Role of modifications in tyrosine transfer RNA: a modified base affecting ribosome binding. J Mol Biol 39:145-57.
    • (1969) J Mol Biol , vol.39 , pp. 145-157
    • Gefter, M.L.1    Russell, R.L.2
  • 60
    • 58249104513 scopus 로고    scopus 로고
    • Identification of 8-methyladenosine as the modification catalyzed by the radical SAM methyltransferase Cfr that confers antibiotic resistance in bacteria
    • Giessing AMB, Jensen SS, Rasmussen A, et al. (2009). Identification of 8-methyladenosine as the modification catalyzed by the radical SAM methyltransferase Cfr that confers antibiotic resistance in bacteria. RNA (NY) 15:327-36.
    • (2009) RNA (NY) , vol.15 , pp. 327-336
    • Giessing, A.M.B.1    Jensen, S.S.2    Rasmussen, A.3
  • 61
    • 84862160503 scopus 로고    scopus 로고
    • Mass spectrometry in the biology of {RNA} and its modifications
    • Giessing AMB, Kirpekar F. (2012). Mass spectrometry in the biology of {RNA} and its modifications. J Proteom 75:3434-49.
    • (2012) J Proteom , vol.75 , pp. 3434-3449
    • Giessing, A.M.B.1    Kirpekar, F.2
  • 62
    • 84865133343 scopus 로고    scopus 로고
    • The last rRNA methyltransferase of E. Coli revealed: The yhiR gene encodes adenine- N 6 methyltransferase specific for modification of A2030 of 23S ribosomal RNA
    • Golovina AY, Dzama MM, Osterman I, et al. (2012). The last rRNA methyltransferase of E. coli revealed: the yhiR gene encodes adenine- N6 methyltransferase specific for modification of A2030 of 23S ribosomal RNA. RNA (NY) 18:1725-34.
    • (2012) RNA (NY) , vol.18 , pp. 1725-1734
    • Golovina, A.Y.1    Dzama, M.M.2    Osterman, I.3
  • 63
    • 0028938473 scopus 로고
    • Nucleotide modification and base conversion of RNA: Summary and outlook
    • Grosjean H, Björk G, Maden BEH. (1995a). Nucleotide modification and base conversion of RNA: summary and outlook. Biochimie 77: 3-6.
    • (1995) Biochimie , vol.77 , pp. 3-6
    • Grosjean, H.1    Björk, G.2    Maden, B.E.H.3
  • 64
    • 71849108697 scopus 로고    scopus 로고
    • Deciphering synonymous codons in the three domains of life: Co-evolution with specific tRNA modification enzymes
    • Grosjean H, de Crécy-Lagard V, Marck C. (2010). Deciphering synonymous codons in the three domains of life: co-evolution with specific tRNA modification enzymes. FEBS Lett 584:252-64.
    • (2010) FEBS Lett , vol.584 , pp. 252-264
    • Grosjean, H.1    De Crécy-Lagard, V.2    Marck, C.3
  • 65
    • 56349150890 scopus 로고    scopus 로고
    • RNomics and modomics in the halophilic archaea Haloferax volcanii: Identification of RNA modification genes
    • Grosjean H, Gaspin C, Marck C, et al. (2008). RNomics and modomics in the halophilic archaea Haloferax volcanii: identification of RNA modification genes. BMC Genom 9:470.
    • (2008) BMC Genom , vol.9 , pp. 470
    • Grosjean, H.1    Gaspin, C.2    Marck, C.3
  • 66
    • 0028943560 scopus 로고
    • Posttranscriptionally modified nucleosides in transfer RNA: Their locations and frequencies
    • Grosjean H, Sprinzl M, Steinberg S. (1995b). Posttranscriptionally modified nucleosides in transfer RNA: their locations and frequencies. Biochimie 77:139-41.
    • (1995) Biochimie , vol.77 , pp. 139-141
    • Grosjean, H.1    Sprinzl, M.2    Steinberg, S.3
  • 67
    • 0000960472 scopus 로고
    • On the physical basis for ambiguity in genetic coding interactions
    • Grosjean HJ, Henau S De, Crothers DM. (1978). On the physical basis for ambiguity in genetic coding interactions. Proc Natl Acad Sci USA 75:610-14.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 610-614
    • Grosjean, H.J.1    De Henau, S.2    Crothers, D.M.3
  • 68
    • 0001445292 scopus 로고    scopus 로고
    • Identification of the 16S rRNA m5C967 Methyltransferase from Escherichia coli
    • Gu XR, Gustafsson C, Ku J, et al. (1999). Identification of the 16S rRNA m5C967 Methyltransferase from Escherichia coli. Biochemistry 38: 4053-7.
    • (1999) Biochemistry , vol.38 , pp. 4053-4057
    • Gu, X.R.1    Gustafsson, C.2    Ku, J.3
  • 69
    • 80051732583 scopus 로고    scopus 로고
    • Bacterial transcriptomics: What is beyond the RNA horiz-ome?
    • Gü ell M, Yus E, Lluch-Senar M, Serrano L. (2011). Bacterial transcriptomics: what is beyond the RNA horiz-ome? Nat Rev Microbiol 9:658-69.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 658-669
    • Gü Ell, M.1    Yus, E.2    Lluch-Senar, M.3    Serrano, L.4
  • 70
    • 84864777887 scopus 로고    scopus 로고
    • Mechanisms of SecMmediated stalling in the ribosome
    • Gumbart J, Schreiner E, Wilson DN, et al. (2012). Mechanisms of SecMmediated stalling in the ribosome. Biophys J 103:331-41.
    • (2012) Biophys J , vol.103 , pp. 331-341
    • Gumbart, J.1    Schreiner, E.2    Wilson, D.N.3
  • 71
    • 0019162933 scopus 로고
    • Unusual modification patterns in the transfer ribonucleic acids of archaebacteria
    • Gupta R, Woese CR. (1980). Unusual modification patterns in the transfer ribonucleic acids of archaebacteria. Curr Microbiol 4:245-9.
    • (1980) Curr Microbiol , vol.4 , pp. 245-249
    • Gupta, R.1    Woese, C.R.2
  • 72
    • 0031912037 scopus 로고    scopus 로고
    • Identification of the rrmA gene encoding the 23S rRNA m1G745 methyltransferase in Escherichia coli and characterization of an m1G745-deficient mutant
    • Gustafsson C, Persson B. (1998). Identification of the rrmA gene encoding the 23S rRNA m1G745 methyltransferase in Escherichia coli and characterization of an m1G745-deficient mutant. J Bacteriol 180:359-65.
    • (1998) J Bacteriol , vol.180 , pp. 359-365
    • Gustafsson, C.1    Persson, B.2
  • 73
    • 0029832294 scopus 로고    scopus 로고
    • Identification of new RNA modifying enzymes by iterative genome search using known modifying enzymes as probes
    • Gustafsson C, Reid R, Greene PJ, Santi DV. (1996). Identification of new RNA modifying enzymes by iterative genome search using known modifying enzymes as probes. Nucl Acids Res 24:3756-62.
    • (1996) Nucl Acids Res , vol.24 , pp. 3756-3762
    • Gustafsson, C.1    Reid, R.2    Greene, P.J.3    Santi, D.V.4
  • 74
    • 33645943707 scopus 로고    scopus 로고
    • Influence of phylogeny on posttranscriptional modification of rRNA in thermophilic prokaryotes: The complete modification map of 16S rRNA of Thermus thermophilus
    • Guymon R, Pomerantz SC, Crain PF, McCloskey J. (2006). Influence of phylogeny on posttranscriptional modification of rRNA in thermophilic prokaryotes: the complete modification map of 16S rRNA of Thermus thermophilus. Biochemistry 45:4888-99.
    • (2006) Biochemistry , vol.45 , pp. 4888-4899
    • Guymon, R.1    Pomerantz, S.C.2    Crain, P.F.3    McCloskey, J.4
  • 75
    • 0036828880 scopus 로고    scopus 로고
    • Active site in RrmJ, a heat shock-induced methyltransferase
    • Hager J, Staker BL, Bugl H, Jakob U. (2002). Active site in RrmJ, a heat shock-induced methyltransferase. J Biol Chem 277:41978-86.
    • (2002) J Biol Chem , vol.277 , pp. 41978-41986
    • Hager, J.1    Staker, B.L.2    Bugl, H.3    Jakob, U.4
  • 76
    • 0035958741 scopus 로고    scopus 로고
    • Recognition of nucleotide {G745} in 23 S ribosomal {RNA} by the RrmA methyltransferase
    • Hansen LH, Kirpekar F, Douthwaite S. (2001). Recognition of nucleotide {G745} in 23 S ribosomal {RNA} by the RrmA methyltransferase. J Mol Biol 310:1001-10.
    • (2001) J Mol Biol , vol.310 , pp. 1001-1010
    • Hansen, L.H.1    Kirpekar, F.2    Douthwaite, S.3
  • 77
    • 0036214016 scopus 로고    scopus 로고
    • Posttranscriptional modifications in the A-loop of 23S rRNAs from selected archaea and eubacteria
    • Hansen M, Kirpekar F, Ritterbusch W, Vester B. (2002). Posttranscriptional modifications in the A-loop of 23S rRNAs from selected archaea and eubacteria. RNA (NY) 8:202-13.
    • (2002) RNA (NY) , vol.8 , pp. 202-213
    • Hansen, M.1    Kirpekar, F.2    Ritterbusch, W.3    Vester, B.4
  • 79
    • 78649267733 scopus 로고    scopus 로고
    • Grand challenge commentary: RNA epigenetics?
    • He C. (2010). Grand challenge commentary: RNA epigenetics? Nature Chem Biol 6:863-5.
    • (2010) Nature Chem Biol , vol.6 , pp. 863-865
    • He, C.1
  • 80
    • 32644447756 scopus 로고    scopus 로고
    • Post-transcriptional nucleotide modification and alternative folding of RNA
    • Helm M. (2006). Post-transcriptional nucleotide modification and alternative folding of RNA. Nucl Acids Res 34:721-33.
    • (2006) Nucl Acids Res , vol.34 , pp. 721-733
    • Helm, M.1
  • 81
    • 0015121549 scopus 로고
    • Change in methylation of 16S ribosomal RNA associated with mutation to kasugamycin resistance in Escherichia coli
    • Helser T, Davies J, Dahlberg J. (1971). Change in methylation of 16S ribosomal RNA associated with mutation to kasugamycin resistance in Escherichia coli. Nature 233:12-14.
    • (1971) Nature , vol.233 , pp. 12-14
    • Helser, T.1    Davies, J.2    Dahlberg, J.3
  • 82
    • 0015494418 scopus 로고
    • Mechanism of kasugamycin resistance in Escherichia coli
    • Helser TL, Davies JE, Dahlberg JE. (1972). Mechanism of kasugamycin resistance in Escherichia coli. Nature 235:6-9.
    • (1972) Nature , vol.235 , pp. 6-9
    • Helser, T.L.1    Davies, J.E.2    Dahlberg, J.E.3
  • 83
    • 0001195354 scopus 로고
    • Structure of a ribonucleic acid
    • Holley RW, Apgar J, Everett GA, et al. (1965). Structure of a ribonucleic acid. Science 147:1462-5.
    • (1965) Science , vol.147 , pp. 1462-1465
    • Holley, R.W.1    Apgar, J.2    Everett, G.A.3
  • 84
    • 0022273096 scopus 로고
    • Two tRNA1Ile species from an extreme thermophile, Thermus thermophilus HB8: Effect of 2-thiolation of ribothymidine on the thermostability of tRNA
    • Horie N, Hara-Yokoyama M, Yokoyama S, et al. (1985). Two tRNA1Ile species from an extreme thermophile, Thermus thermophilus HB8: effect of 2-thiolation of ribothymidine on the thermostability of tRNA. Biochemistry 24:5711-15.
    • (1985) Biochemistry , vol.24 , pp. 5711-5715
    • Horie, N.1    Hara-Yokoyama, M.2    Yokoyama, S.3
  • 85
    • 0015018530 scopus 로고
    • Mass spectral analysis of modified ribonucleosides obtained by degradation of 14 alkali-stable dinucleotides isolated from yeast ribonucleic acid
    • Howlett HA, Johnson MW, Trim AR, et al. (1971). Mass spectral analysis of modified ribonucleosides obtained by degradation of 14 alkali-stable dinucleotides isolated from yeast ribonucleic acid. Anal Biochem 39:429-40.
    • (1971) Anal Biochem , vol.39 , pp. 429-440
    • Howlett, H.A.1    Johnson, M.W.2    Trim, A.R.3
  • 86
    • 84876156249 scopus 로고    scopus 로고
    • Molecular functions of small regulatory noncoding RNA
    • Huang Y, Zhang JL, Yu XL, et al. (2013). Molecular functions of small regulatory noncoding RNA. Biochemistry (Moscow) 78:221-30.
    • (2013) Biochemistry (Moscow) , vol.78 , pp. 221-230
    • Huang, Y.1    Zhang, J.L.2    Yu, X.L.3
  • 87
    • 84880791572 scopus 로고    scopus 로고
    • NSun2-mediated cytosine-5 methylation of vault noncoding RNA determines its processing into regulatory small RNAs
    • Hussain S, Sajini A, Blanco S, et al. (2013). NSun2-mediated cytosine-5 methylation of vault noncoding RNA determines its processing into regulatory small RNAs. Cell Rep 4:255-61.
    • (2013) Cell Rep , vol.4 , pp. 255-261
    • Hussain, S.1    Sajini, A.2    Blanco, S.3
  • 88
    • 36749000444 scopus 로고    scopus 로고
    • Dissection of 16S rRNA methyltransferase (KsgA) function in Escherichia coli
    • Inoue K, Basu S, Inouye M. (2007). Dissection of 16S rRNA methyltransferase (KsgA) function in Escherichia coli. J Bacteriol 189:8510-18.
    • (2007) J Bacteriol , vol.189 , pp. 8510-8518
    • Inoue, K.1    Basu, S.2    Inouye, M.3
  • 89
    • 0015883489 scopus 로고
    • Partial purification of ribosomal RNA (m1G)-and rRNA (m2G) methylases from Escherichia coli and demonstration of some proteins affecting their apparent activity
    • Isaksson LA. (1973). Partial purification of ribosomal RNA (m1G)-and rRNA (m2G) methylases from Escherichia coli and demonstration of some proteins affecting their apparent activity. Biochim Biophys Acta 312:122-33.
    • (1973) Biochim Biophys Acta , vol.312 , pp. 122-133
    • Isaksson, L.A.1
  • 90
    • 58749114577 scopus 로고    scopus 로고
    • Path of nascent polypeptide in exit tunnel revealed by molecular dynamics simulation of ribosome
    • Ishida H, Hayward S. (2008). Path of nascent polypeptide in exit tunnel revealed by molecular dynamics simulation of ribosome. Biophys J 95:5962-73.
    • (2008) Biophys J , vol.95 , pp. 5962-5973
    • Ishida, H.1    Hayward, S.2
  • 91
    • 44949173836 scopus 로고    scopus 로고
    • Structure, dynamics, and function of {RNA} modification enzymes
    • Ishitani R, Yokoyama S, Nureki O. (2008). Structure, dynamics, and function of {RNA} modification enzymes. Curr Opin Struct Biol 18: 330-9.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 330-339
    • Ishitani, R.1    Yokoyama, S.2    Nureki, O.3
  • 92
    • 0028314657 scopus 로고
    • Ribosome recycling factor (ribosome releasing factor) is essential for bacterial growth
    • Janosi L, Shimizu I, Kaji A. (1994). Ribosome recycling factor (ribosome releasing factor) is essential for bacterial growth. Proc Natl Acad Sci USA 91:4249-53.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4249-4253
    • Janosi, L.1    Shimizu, I.2    Kaji, A.3
  • 93
    • 84862803181 scopus 로고    scopus 로고
    • Regulation of small RNA stability: Methylation and beyond
    • Ji L, Chen X. (2012). Regulation of small RNA stability: methylation and beyond. Cell Res 22:624-36.
    • (2012) Cell Res , vol.22 , pp. 624-636
    • Ji, L.1    Chen, X.2
  • 94
    • 84872847340 scopus 로고    scopus 로고
    • Reversible {RNA} adenosine methylation in biological regulation
    • Jia G, Fu Y, He C. (2013). Reversible {RNA} adenosine methylation in biological regulation. Trends Genet 29:108-15.
    • (2013) Trends Genet , vol.29 , pp. 108-115
    • Jia, G.1    Fu, Y.2    He, C.3
  • 95
    • 0000211141 scopus 로고
    • The discovery of 5-methyl-cytosine in tuberculinic acid, the nucleic acid of the tubercle bacillus
    • Johnson TB, Coghill RD. (1925). The discovery of 5-methyl-cytosine in tuberculinic acid, the nucleic acid of the tubercle bacillus. J Am Chem Soc 47:2838-44.
    • (1925) J Am Chem Soc , vol.47 , pp. 2838-2844
    • Johnson, T.B.1    Coghill, R.D.2
  • 96
    • 77952279419 scopus 로고    scopus 로고
    • Metabolomic and transcriptomic stress response of Escherichia coli
    • doi:10.1038/msb.2010.18
    • Jozefczuk S, Klie S, Catchpole G, et al. (2010). Metabolomic and transcriptomic stress response of Escherichia coli. Mol Syst Biol 6:364. doi:10.1038/msb.2010.18.
    • (2010) Mol Syst Biol , vol.6 , pp. 364
    • Jozefczuk, S.1    Klie, S.2    Catchpole, G.3
  • 97
    • 0016594168 scopus 로고
    • Proton nuclear magnetic resonance of modified bases of valine transfer ribonucleic acid (Escherichia coli). Direct monitor of sequential thermal unfolding
    • Kastrup RV, Schmidt PG. (1975). Proton nuclear magnetic resonance of modified bases of valine transfer ribonucleic acid (Escherichia coli). Direct monitor of sequential thermal unfolding. Biochemistry 14: 3612-18.
    • (1975) Biochemistry , vol.14 , pp. 3612-3618
    • Kastrup, R.V.1    Schmidt, P.G.2
  • 98
    • 0026604504 scopus 로고
    • Conformation rigidity of N4-acetyl-20-O-methylcytidine found in tRNA of extremely thermophilic archaebacteria (Archaea)
    • Kawai G, Hashizume T, Yasuda M, et al. (1992). Conformation rigidity of N4-acetyl-20-O-methylcytidine found in tRNA of extremely thermophilic archaebacteria (Archaea). Nucl Nucl 11:759-71.
    • (1992) Nucl Nucl , vol.11 , pp. 759-771
    • Kawai, G.1    Hashizume, T.2    Yasuda, M.3
  • 99
    • 23744453392 scopus 로고    scopus 로고
    • A new mechanism for chloramphenicol, florfenicol and clindamycin resistance: Methylation of 23S ribosomal RNA at A2503
    • Kehrenberg C, Schwarz S, Jacobsen L, et al. (2005). A new mechanism for chloramphenicol, florfenicol and clindamycin resistance: methylation of 23S ribosomal RNA at A2503. Mol Microbiol 57:1064-73.
    • (2005) Mol Microbiol , vol.57 , pp. 1064-1073
    • Kehrenberg, C.1    Schwarz, S.2    Jacobsen, L.3
  • 100
    • 77953682110 scopus 로고    scopus 로고
    • Detection of RNA modifications
    • Kellner S, Burhenne J, Helm M. (2010). Detection of RNA modifications. RNA Biol 7:237-47.
    • (2010) RNA Biol , vol.7 , pp. 237-247
    • Kellner, S.1    Burhenne, J.2    Helm, M.3
  • 102
    • 84861385355 scopus 로고    scopus 로고
    • Base methylations in the double-stranded RNA by a fused methyltransferase bearing unwinding activity
    • Kimura S, Ikeuchi Y, Kitahara K, et al. (2012). Base methylations in the double-stranded RNA by a fused methyltransferase bearing unwinding activity. Nucl Acids Res 40:4071-85.
    • (2012) Nucl Acids Res , vol.40 , pp. 4071-4085
    • Kimura, S.1    Ikeuchi, Y.2    Kitahara, K.3
  • 103
    • 77950361036 scopus 로고    scopus 로고
    • Fine-tuning of the ribosomal decoding center by conserved methyl-modifications in the Escherichia coli 16S rRNA
    • Kimura S, Suzuki T. (2010). Fine-tuning of the ribosomal decoding center by conserved methyl-modifications in the Escherichia coli 16S rRNA. Nucl Acids Res 38:1341-52.
    • (2010) Nucl Acids Res , vol.38 , pp. 1341-1352
    • Kimura, S.1    Suzuki, T.2
  • 104
    • 0033950924 scopus 로고    scopus 로고
    • Mapping posttranscriptional modifications in 5S ribosomal RNA by MALDI mass spectrometry
    • Kirpekar F, Douthwaite S, Roepstorff P. (2000). Mapping posttranscriptional modifications in 5S ribosomal RNA by MALDI mass spectrometry. RNA (NY) 6:296-306.
    • (2000) RNA (NY) , vol.6 , pp. 296-306
    • Kirpekar, F.1    Douthwaite, S.2    Roepstorff, P.3
  • 105
    • 0035898634 scopus 로고    scopus 로고
    • Small nucleolar RNA-guided post-transcriptional modification of cellular RNAs
    • Kiss T. (2001). Small nucleolar RNA-guided post-transcriptional modification of cellular RNAs. EMBO J 20:3617-22.
    • (2001) EMBO J , vol.20 , pp. 3617-3622
    • Kiss, T.1
  • 106
    • 0016764579 scopus 로고
    • Minimal post-transcriptional modification of yeast mitochondrial ribosomal RNA
    • Klootwijk J, Klein I, Grivell L. (1975). Minimal post-transcriptional modification of yeast mitochondrial ribosomal RNA. J Mol Biol 97: 337-50.
    • (1975) J Mol Biol , vol.97 , pp. 337-350
    • Klootwijk, J.1    Klein, I.2    Grivell, L.3
  • 108
    • 64049105717 scopus 로고    scopus 로고
    • Tertiary interactions within the ribosomal exit tunnel
    • Kosolapov A, Deutsch C. (2009). Tertiary interactions within the ribosomal exit tunnel. Nat Struct Mol Biol 16:405-11.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 405-411
    • Kosolapov, A.1    Deutsch, C.2
  • 109
    • 0034637542 scopus 로고    scopus 로고
    • Identities and phylogenetic comparisons of posttranscriptional modifications in 16 S ribosomal RNA from Haloferax volcanii
    • Kowalak J, Bruenger E, Crain PF, McCloskey J. (2000). Identities and phylogenetic comparisons of posttranscriptional modifications in 16 S ribosomal RNA from Haloferax volcanii. J Biol Chem 275: 24484-9.
    • (2000) J Biol Chem , vol.275 , pp. 24484-24489
    • Kowalak, J.1    Bruenger, E.2    Crain, P.F.3    McCloskey, J.4
  • 110
    • 0028272470 scopus 로고
    • The role of posttranscriptional modification in stabilization of transfer RNA from hyperthermophiles
    • Kowalak J, Dalluge JJ, McCloskey J, Stetter KO. (1994). The role of posttranscriptional modification in stabilization of transfer RNA from hyperthermophiles. Biochemistry 33:7869-76.
    • (1994) Biochemistry , vol.33 , pp. 7869-7876
    • Kowalak, J.1    Dalluge, J.J.2    McCloskey, J.3    Stetter, K.O.4
  • 111
    • 0016610083 scopus 로고
    • Presence of the methylester of 5-carboxymethyl uridine in the wobble position of the anticodon of tRNAArgIII from brewer's yeast
    • Kuntzel B, Weissenbach J, Wolff RE, et al. (1975). Presence of the methylester of 5-carboxymethyl uridine in the wobble position of the anticodon of tRNAArgIII from brewer's yeast. Biochimie 57: 61-70.
    • (1975) Biochimie , vol.57 , pp. 61-70
    • Kuntzel, B.1    Weissenbach, J.2    Wolff, R.E.3
  • 112
    • 62549159996 scopus 로고    scopus 로고
    • 20-O-methylation stabilizes Piwiassociated small RNAs and ensures DNA elimination in Tetrahymena
    • Kurth HM, Mochizuki K. (2009). 20-O-methylation stabilizes Piwiassociated small RNAs and ensures DNA elimination in Tetrahymena. RNA (NY) 15:675-85.
    • (2009) RNA (NY) , vol.15 , pp. 675-685
    • Kurth, H.M.1    Mochizuki, K.2
  • 113
    • 0028086499 scopus 로고
    • The DIM1 gene responsible for the conserved m62Am62A dimethylation in the 30- terminal loop of 18 S rRNA is essential in yeast
    • Lafontaine D, Delcour J, Glasser A-L, et al. (1994). The DIM1 gene responsible for the conserved m62Am62A dimethylation in the 30- terminal loop of 18 S rRNA is essential in yeast. J Mol Biol 241: 492-7.
    • (1994) J Mol Biol , vol.241 , pp. 492-497
    • Lafontaine, D.1    Delcour, J.2    Glasser, A.-L.3
  • 114
    • 0028866774 scopus 로고
    • The 18S rRNA dimethylase Dim1p is required for pre-ribosomal RNA processing in yeast
    • Lafontaine D, Vandenhaute J, Tollervey D. (1995). The 18S rRNA dimethylase Dim1p is required for pre-ribosomal RNA processing in yeast. Genes Dev 9:2470-81.
    • (1995) Genes Dev , vol.9 , pp. 2470-2481
    • Lafontaine, D.1    Vandenhaute, J.2    Tollervey, D.3
  • 115
    • 0015043629 scopus 로고
    • Altered methylation of ribosomal RNA in an erythromycin-resistant strain of Staphylococcus aureus
    • Lai CJ, Weisblum B. (1971). Altered methylation of ribosomal RNA in an erythromycin-resistant strain of Staphylococcus aureus. Proc Natl Acad Sci USA 68:856-60.
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 856-860
    • Lai, C.J.1    Weisblum, B.2
  • 116
    • 78651135051 scopus 로고
    • Further studies on the alkylation of nucleic acids and their constituent nucleotides
    • Lawley PD, Brookes P. (1963). Further studies on the alkylation of nucleic acids and their constituent nucleotides. Biochem J 89: 127-38.
    • (1963) Biochem J , vol.89 , pp. 127-138
    • Lawley, P.D.1    Brookes, P.2
  • 117
    • 34247097013 scopus 로고    scopus 로고
    • Methyltransferase that modifies guanine 966 of the 16 S rRNA: Functional identification and tertiary structure
    • Lesnyak DV, Osipiuk J, Skarina T, et al. (2007). Methyltransferase that modifies guanine 966 of the 16 S rRNA: functional identification and tertiary structure. J Biol Chem 282:5880-7.
    • (2007) J Biol Chem , vol.282 , pp. 5880-5887
    • Lesnyak, D.V.1    Osipiuk, J.2    Skarina, T.3
  • 118
    • 33750290824 scopus 로고    scopus 로고
    • Identification of Escherichia coli m2G methyltransferases: I. The ycbY gene encodes a methyltransferase specific for G2445 of the 23 S rRNA
    • Lesnyak DV, Sergiev PV, Bogdanov AA, Dontsova OA. (2006). Identification of Escherichia coli m2G methyltransferases: I. The ycbY gene encodes a methyltransferase specific for G2445 of the 23 S rRNA. J Mol Biol 364:20-5.
    • (2006) J Mol Biol , vol.364 , pp. 20-25
    • Lesnyak, D.V.1    Sergiev, P.V.2    Bogdanov, A.A.3    Dontsova, O.A.4
  • 119
    • 37349128219 scopus 로고    scopus 로고
    • RRNA modifications in an intersubunit bridge of the ribosome strongly affect both ribosome biogenesis and activity
    • Liang X, Liu Q, Fournier MJ. (2007). rRNA modifications in an intersubunit bridge of the ribosome strongly affect both ribosome biogenesis and activity. Mol Cell 28:965-77.
    • (2007) Mol Cell , vol.28 , pp. 965-977
    • Liang, X.1    Liu, Q.2    Fournier, M.J.3
  • 120
  • 121
    • 23044469032 scopus 로고    scopus 로고
    • Reassignment of sense codons in vivo
    • Link AJ, Tirrell DA. (2005). Reassignment of sense codons in vivo. Methods 36:291-8.
    • (2005) Methods , vol.36 , pp. 291-298
    • Link, A.J.1    Tirrell, D.A.2
  • 122
    • 60649086618 scopus 로고    scopus 로고
    • Single 23S rRNA mutations at the ribosomal peptidyl transferase centre confer resistance to valnemulin and other antibiotics in Mycobacterium smegmatis by perturbation of the drug binding pocket
    • Long KS, Poehlsgaard J, Hansen LH, et al. (2009). Single 23S rRNA mutations at the ribosomal peptidyl transferase centre confer resistance to valnemulin and other antibiotics in Mycobacterium smegmatis by perturbation of the drug binding pocket. Mol Microbiol 71: 1218-27.
    • (2009) Mol Microbiol , vol.71 , pp. 1218-1227
    • Long, K.S.1    Poehlsgaard, J.2    Hansen, L.H.3
  • 123
    • 0014537519 scopus 로고
    • Inhibition of viral multiplication with chemically modified ribonucleic acids. II. Inhibition of the multiplication of an arbovirus (Sindbis virus) on chick embryo fibroblasts
    • Louisot P, Colobert L, Beck G, Ebel JP. (1969). Inhibition of viral multiplication with chemically modified ribonucleic acids. II. Inhibition of the multiplication of an arbovirus (Sindbis virus) on chick embryo fibroblasts. Ann Inst Pasteur 117:98-114.
    • (1969) Ann Inst Pasteur , vol.117 , pp. 98-114
    • Louisot, P.1    Colobert, L.2    Beck, G.3    Ebel, J.P.4
  • 124
    • 0035162971 scopus 로고    scopus 로고
    • The rlmB gene is essential for formation of Gm2251 in 23S rRNA but not for ribosome maturation in Escherichia coli
    • Lövgren J, Wikström P. (2001). The rlmB gene is essential for formation of Gm2251 in 23S rRNA but not for ribosome maturation in Escherichia coli. J Bacteriol 183:6957-60.
    • (2001) J Bacteriol , vol.183 , pp. 6957-6960
    • Lövgren, J.1    Wikström, P.2
  • 125
    • 28544449949 scopus 로고    scopus 로고
    • Folding zones inside the ribosomal exit tunnel
    • Lu J, Deutsch C. (2005). Folding zones inside the ribosomal exit tunnel. Nat Struct Mol Biol 12:1123-9.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 1123-1129
    • Lu, J.1    Deutsch, C.2
  • 126
    • 0031705811 scopus 로고    scopus 로고
    • The gene for 16S rRNA methyltransferase (ksgA) functions as a multicopy suppressor for a cold-sensitive mutant of era, an essential RAS-like GTP-binding protein in Escherichia
    • Lu Q, Inouye M. (1998). The gene for 16S rRNA methyltransferase (ksgA) functions as a multicopy suppressor for a cold-sensitive mutant of era, an essential RAS-like GTP-binding protein in Escherichia. J Bacteriol 180:5243-6.
    • (1998) J Bacteriol , vol.180 , pp. 5243-5246
    • Lu, Q.1    Inouye, M.2
  • 127
    • 84875692043 scopus 로고    scopus 로고
    • MODOMICS: A database of RNA modification pathways - 2013 update
    • Machnicka MA, Milanowska K, Oglou OO, et al. (2013). MODOMICS: a database of RNA modification pathways - 2013 update. Nucl Acids Res 41:D262-7.
    • (2013) Nucl Acids Res , vol.41
    • Machnicka, M.A.1    Milanowska, K.2    Oglou, O.O.3
  • 128
    • 0345306616 scopus 로고    scopus 로고
    • Identifying the methyltransferases for m5U747 and m5U1939 in 23S rRNA using MALDI mass spectrometry
    • Madsen CT. (2003). Identifying the methyltransferases for m5U747 and m5U1939 in 23S rRNA using MALDI mass spectrometry. Nucl Acids Res 31:4738-46.
    • (2003) Nucl Acids Res , vol.31 , pp. 4738-4746
    • Madsen, C.T.1
  • 129
    • 55349135212 scopus 로고    scopus 로고
    • Ribosome biogenesis; The KsgA protein throws a methyl-mediated switch in ribosome assembly
    • Mangat CS, Brown ED. (2008). Ribosome biogenesis; the KsgA protein throws a methyl-mediated switch in ribosome assembly. Mol Microbiol 70:1051-3.
    • (2008) Mol Microbiol , vol.70 , pp. 1051-1053
    • Mangat, C.S.1    Brown, E.D.2
  • 130
    • 30944437007 scopus 로고    scopus 로고
    • Nascent peptide in the "birth canal" of the ribosome
    • Mankin AS. (2006). Nascent peptide in the "birth canal" of the ribosome. Trends Biochem Sci 31:11-13.
    • (2006) Trends Biochem Sci , vol.31 , pp. 11-13
    • Mankin, A.S.1
  • 131
    • 0031832046 scopus 로고    scopus 로고
    • The RNA modification database - 1998
    • McCloskey JA, Crain PF. (1998). The RNA modification database - 1998. Nucl Acids Res 26:196-7.
    • (1998) Nucl Acids Res , vol.26 , pp. 196-197
    • McCloskey, J.A.1    Crain, P.F.2
  • 132
    • 13444266430 scopus 로고    scopus 로고
    • The small subunit rRNA modification database
    • McCloskey JA, Rozenski J. (2005). The small subunit rRNA modification database. Nucl Acids Res 33:D135-8.
    • (2005) Nucl Acids Res , vol.33
    • McCloskey, J.A.1    Rozenski, J.2
  • 133
    • 33746821849 scopus 로고    scopus 로고
    • Modifications in Thermus thermophilus 23 S ribosomal RNA are centered in regions of RNA-RNA contact
    • Mengel-Jørgensen J, Jensen SS, Rasmussen A, et al. (2006). Modifications in Thermus thermophilus 23 S ribosomal RNA are centered in regions of RNA-RNA contact. J Biol Chem 281: 22108-17.
    • (2006) J Biol Chem , vol.281 , pp. 22108-22117
    • Mengel-Jørgensen, J.1    Jensen, S.S.2    Rasmussen, A.3
  • 134
    • 84862649489 scopus 로고    scopus 로고
    • Comprehensive analysis of mRNA methylation reveals enrichment in 30 UTRs and near stop codons
    • Meyer KD, Saletore Y, Zumbo P, et al. (2012). Comprehensive analysis of mRNA methylation reveals enrichment in 30 UTRs and near stop codons. Cell 149:1635-46.
    • (2012) Cell , vol.149 , pp. 1635-1646
    • Meyer, K.D.1    Saletore, Y.2    Zumbo, P.3
  • 135
    • 70350452791 scopus 로고    scopus 로고
    • Proteome changes in human bronchoalveolar cells following styrene exposure indicate involvement of oxidative stress in the molecular-response mechanism
    • Mörbt N, Mögel I, Kalkhof S, et al. (2009). Proteome changes in human bronchoalveolar cells following styrene exposure indicate involvement of oxidative stress in the molecular-response mechanism. Proteomics 9:4920-33.
    • (2009) Proteomics , vol.9 , pp. 4920-4933
    • Mörbt, N.1    Mögel, I.2    Kalkhof, S.3
  • 137
    • 77950476036 scopus 로고    scopus 로고
    • 5-Methylcytosine in RNA: Detection, enzymatic formation and biological functions
    • Motorin Y, Lyko F, Helm M. (2010). 5-Methylcytosine in RNA: detection, enzymatic formation and biological functions. Nucl Acids Res 38:1415-30.
    • (2010) Nucl Acids Res , vol.38 , pp. 1415-1430
    • Motorin, Y.1    Lyko, F.2    Helm, M.3
  • 138
    • 0023734317 scopus 로고
    • Codon and aminoacid specificities of a transfer RNA are both converted by a single post-transcriptional modification
    • Muramatsu T, Nishikawa K, Nemoto F, et al. (1988). Codon and aminoacid specificities of a transfer RNA are both converted by a single post-transcriptional modification. Nature 336:179-81.
    • (1988) Nature , vol.336 , pp. 179-181
    • Muramatsu, T.1    Nishikawa, K.2    Nemoto, F.3
  • 139
    • 1842506046 scopus 로고    scopus 로고
    • Control of SecA and SecM translation by protein secretion
    • Nakatogawa H, Murakami A, Ito K. (2004). Control of SecA and SecM translation by protein secretion. Curr Opin Microbiol 7: 145-50.
    • (2004) Curr Opin Microbiol , vol.7 , pp. 145-150
    • Nakatogawa, H.1    Murakami, A.2    Ito, K.3
  • 140
    • 0017171104 scopus 로고
    • The methylation of tRNA
    • Nau F. (1976). The methylation of tRNA. Biochimie 58:629-45.
    • (1976) Biochimie , vol.58 , pp. 629-645
    • Nau, F.1
  • 141
    • 78650475398 scopus 로고    scopus 로고
    • Phenotypic landscape of a bacterial cell
    • Nichols RJ, Sen S, Choo YJ, et al. (2011). Phenotypic landscape of a bacterial cell. Cell 144:143-56.
    • (2011) Cell , vol.144 , pp. 143-156
    • Nichols, R.J.1    Sen, S.2    Choo, Y.J.3
  • 142
    • 34547751877 scopus 로고    scopus 로고
    • Identification of the RsmG methyltransferase target as 16S rRNA nucleotide G527 and characterization of Bacillus subtilis rsmG mutants
    • Nishimura K, Johansen SK, Inaoka T, et al. (2007). Identification of the RsmG methyltransferase target as 16S rRNA nucleotide G527 and characterization of Bacillus subtilis rsmG mutants. J Bacteriol 189: 6068-73.
    • (2007) J Bacteriol , vol.189 , pp. 6068-6073
    • Nishimura, K.1    Johansen, S.K.2    Inaoka, T.3
  • 143
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • Nissen P, Hansen J, Ban N, et al. (2000). The structural basis of ribosome activity in peptide bond synthesis. Science 289:920-30.
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3
  • 144
    • 84875377560 scopus 로고    scopus 로고
    • N6-methyl-adenosine (m6A) in RNA: An old modification with a novel epigenetic function
    • Niu Y, Zhao X, Wu Y-S, et al. (2013). N6-methyl-adenosine (m6A) in RNA: an old modification with a novel epigenetic function. Genom Proteom Bioinf 11:8-17.
    • (2013) Genom Proteom Bioinf , vol.11 , pp. 8-17
    • Niu, Y.1    Zhao, X.2    Wu, Y.-S.3
  • 145
    • 0032455220 scopus 로고    scopus 로고
    • Posttranscriptional modifications in 16S and 23S rRNAs of the archaeal hyperthermophile Sulfolobus solfataricus
    • Noon K, Bruenger E, McCloskey J. (1998). Posttranscriptional modifications in 16S and 23S rRNAs of the archaeal hyperthermophile Sulfolobus solfataricus. J Bacteriol 180:2883-8.
    • (1998) J Bacteriol , vol.180 , pp. 2883-2888
    • Noon, K.1    Bruenger, E.2    McCloskey, J.3
  • 146
    • 0028296185 scopus 로고
    • Mining treasures from "junk DNA"
    • Nowak R. (1994). Mining treasures from "junk DNA". Science 263: 608-10.
    • (1994) Science , vol.263 , pp. 608-610
    • Nowak, R.1
  • 147
    • 33646179813 scopus 로고    scopus 로고
    • Recognition of a complex substrate by the KsgA/Dim1 family of enzymes has been conserved throughout evolution
    • O'Farrell HC, Pulicherla N, Desai PM, Rife JP. (2006). Recognition of a complex substrate by the KsgA/Dim1 family of enzymes has been conserved throughout evolution. RNA (NY) 12:725-33.
    • (2006) RNA (NY) , vol.12 , pp. 725-733
    • O'farrell, H.C.1    Pulicherla, N.2    Desai, P.M.3    Rife, J.P.4
  • 148
    • 33846678393 scopus 로고    scopus 로고
    • Loss of a conserved 7- methylguanosine modification in 16S rRNA confers low-level streptomycin resistance in bacteria
    • Okamoto S, Tamaru A, Nakajima C, et al. (2007). Loss of a conserved 7- methylguanosine modification in 16S rRNA confers low-level streptomycin resistance in bacteria. Mol Microbiol 63:1096-106.
    • (2007) Mol Microbiol , vol.63 , pp. 1096-1106
    • Okamoto, S.1    Tamaru, A.2    Nakajima, C.3
  • 149
    • 79952442443 scopus 로고    scopus 로고
    • Methylated 23S rRNA nucleotide m2G1835 of Escherichia coli ribosome facilitates subunit association
    • Osterman I, Sergiev PV, Tsvetkov PO, et al. (2011). Methylated 23S rRNA nucleotide m2G1835 of Escherichia coli ribosome facilitates subunit association. Biochimie 93:725-9.
    • (2011) Biochimie , vol.93 , pp. 725-729
    • Osterman, I.1    Sergiev, P.V.2    Tsvetkov, P.O.3
  • 150
    • 84875530060 scopus 로고    scopus 로고
    • N6-methyl-adenosine modification in messenger and long non-coding {RNA}
    • Pan T. (2013). N6-methyl-adenosine modification in messenger and long non-coding {RNA}. Trends Biochem Sci 38:204-9.
    • (2013) Trends Biochem Sci , vol.38 , pp. 204-209
    • Pan, T.1
  • 151
    • 0027245490 scopus 로고
    • Modification of tRNA as a regulatory device
    • Persson B. (1993). Modification of tRNA as a regulatory device. Mol Microbiol 8:1011-16.
    • (1993) Mol Microbiol , vol.8 , pp. 1011-1016
    • Persson, B.1
  • 152
    • 79959287938 scopus 로고    scopus 로고
    • Biosynthesis and function of tRNA modifications in Archaea
    • Phillips G, Crécy-Lagard V de. (2011). Biosynthesis and function of tRNA modifications in Archaea. Curr Opin Microbiol 14:335-41.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 335-341
    • Phillips, G.1    De Crécy-Lagard, V.2
  • 153
    • 38549164687 scopus 로고    scopus 로고
    • The 3D rRNA modification maps database: With interactive tools for ribosome analysis
    • Piekna-Przybylska D, Decatur W, Fournier MJ. (2008). The 3D rRNA modification maps database: with interactive tools for ribosome analysis. Nucl Acids Res 36:D178-83.
    • (2008) Nucl Acids Res , vol.36
    • Piekna-Przybylska, D.1    Decatur, W.2    Fournier, M.J.3
  • 154
    • 0035942753 scopus 로고    scopus 로고
    • Ribosomal peptidyl transferase can withstand mutations at the putative catalytic nucleotide
    • Polacek N, Gaynor M, Yassin A, Mankin AS. (2001). Ribosomal peptidyl transferase can withstand mutations at the putative catalytic nucleotide. Nature 411:498-501.
    • (2001) Nature , vol.411 , pp. 498-501
    • Polacek, N.1    Gaynor, M.2    Yassin, A.3    Mankin, A.S.4
  • 155
    • 68349113708 scopus 로고    scopus 로고
    • Structural and functional divergence within the Dim1/KsgA family of rRNA methyltransferases
    • Pulicherla N, Pogorzala L, Xu Z, et al. (2009). Structural and functional divergence within the Dim1/KsgA family of rRNA methyltransferases. J Mol Biol 391:884-93.
    • (2009) J Mol Biol , vol.391 , pp. 884-893
    • Pulicherla, N.1    Pogorzala, L.2    Xu, Z.3
  • 156
    • 52949120327 scopus 로고    scopus 로고
    • YbeA is the m3Psi methyltransferase RlmH that targets nucleotide 1915 in 23S rRNA
    • Purta E, Kaminska KH, Kasprzak JM, et al. (2008a). YbeA is the m3Psi methyltransferase RlmH that targets nucleotide 1915 in 23S rRNA. RNA (NY) 14:2234-44.
    • (2008) RNA (NY) , vol.14 , pp. 2234-2244
    • Purta, E.1    Kaminska, K.H.2    Kasprzak, J.M.3
  • 157
    • 52949109757 scopus 로고    scopus 로고
    • YccW is the m5C methyltransferase specific for 23S rRNA nucleotide 1962
    • Purta E, O'Connor M, Bujnicki JM, Douthwaite S. (2008b). YccW is the m5C methyltransferase specific for 23S rRNA nucleotide 1962. J Mol Biol 383:641-51.
    • (2008) J Mol Biol , vol.383 , pp. 641-651
    • Purta, E.1    O'connor, M.2    Bujnicki, J.M.3    Douthwaite, S.4
  • 158
    • 65949090299 scopus 로고    scopus 로고
    • YgdE is the 20-O-ribose methyltransferase RlmM specific for nucleotide C2498 in bacterial 23S rRNA
    • Purta E, O'Connor M, Bujnicki JM, Douthwaite S. (2009). YgdE is the 20-O-ribose methyltransferase RlmM specific for nucleotide C2498 in bacterial 23S rRNA. Mol Microbiol 72:1147-58.
    • (2009) Mol Microbiol , vol.72 , pp. 1147-1158
    • Purta, E.1    O'connor, M.2    Bujnicki, J.M.3    Douthwaite, S.4
  • 159
    • 33750990817 scopus 로고    scopus 로고
    • Early days of tRNA research: Discovery, function, purification and sequence analysis
    • RajBhandary UL, Kohrer C. (2006). Early days of tRNA research: discovery, function, purification and sequence analysis. J Biosci 31: 439-52.
    • (2006) J Biosci , vol.31 , pp. 439-452
    • Rajbhandary, U.L.1    Kohrer, C.2
  • 160
    • 67349284731 scopus 로고    scopus 로고
    • Interplay between the heat shock response and translation in Escherichia coli
    • RasoulyA, Ron EZ. (2009). Interplay between the heat shock response and translation in Escherichia coli. Res Microbiol 160:288-96.
    • (2009) Res Microbiol , vol.160 , pp. 288-296
    • Rasouly, A.1    Ron, E.Z.2
  • 162
    • 84881113615 scopus 로고    scopus 로고
    • The ribosome as a versatile catalyst: Reactions at the peptidyl transferase center
    • Rodnina MV. (2013). The ribosome as a versatile catalyst: reactions at the peptidyl transferase center. Curr Opin Struct Biol 23:595-602.
    • (2013) Curr Opin Struct Biol , vol.23 , pp. 595-602
    • Rodnina, M.V.1
  • 163
    • 0038508659 scopus 로고    scopus 로고
    • Peptide bond formation on the ribosome: Structure and mechanism
    • Rodnina MV, Wintermeyer W. (2003). Peptide bond formation on the ribosome: structure and mechanism. Curr Opin Struct Biol 13:334-40.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 334-340
    • Rodnina, M.V.1    Wintermeyer, W.2
  • 164
    • 0014694355 scopus 로고
    • An iron-dependent modification of several transfer {RNA} species in Escherichia coli
    • Rosenberg AH, Gefter ML. (1969). An iron-dependent modification of several transfer {RNA} species in Escherichia coli. J Mol Biol 46: 581-4.
    • (1969) J Mol Biol , vol.46 , pp. 581-584
    • Rosenberg, A.H.1    Gefter, M.L.2
  • 166
    • 34347378274 scopus 로고    scopus 로고
    • Pimet, the Drosophila homolog of HEN1, mediates 20-O-methylation of Piwi-interacting RNAs at their 30 ends
    • Saito K, Sakaguchi Y, Suzuki T, et al. (2007). Pimet, the Drosophila homolog of HEN1, mediates 20-O-methylation of Piwi-interacting RNAs at their 30 ends. Genes Dev 21:1603-8.
    • (2007) Genes Dev , vol.21 , pp. 1603-1608
    • Saito, K.1    Sakaguchi, Y.2    Suzuki, T.3
  • 167
    • 0014214150 scopus 로고
    • Alteration of codon recognition of Escherichia coli transfer {RNA} by modification with cyanogen bromide
    • Saneyoshi M, Nishimura S. (1967). Alteration of codon recognition of Escherichia coli transfer {RNA} by modification with cyanogen bromide. Biochim Biophy Acta (BBA) - Nucl Acids Protein Synth 145: 208-10.
    • (1967) Biochim Biophy Acta (BBA) - Nucl Acids Protein Synth , vol.145 , pp. 208-210
    • Saneyoshi, M.1    Nishimura, S.2
  • 168
    • 59649120058 scopus 로고    scopus 로고
    • RNA cytosine methylation analysis by bisulfite sequencing
    • doi: 10.1093/nar/gkn954
    • Schaefer M, Pollex T, Hanna K, Lyko F. (2009). RNA cytosine methylation analysis by bisulfite sequencing. Nucl Acids Res 37:e12. doi: 10.1093/nar/gkn954.
    • (2009) Nucl Acids Res , vol.37
    • Schaefer, M.1    Pollex, T.2    Hanna, K.3    Lyko, F.4
  • 169
    • 80053321198 scopus 로고    scopus 로고
    • Complete modification maps for the cytosolic small and large subunit rRNAs of Euglena gracilis: Functional and evolutionary implications of contrasting patterns between the two rRNA components
    • Schnare MN, Gray MW. (2011). Complete modification maps for the cytosolic small and large subunit rRNAs of Euglena gracilis: functional and evolutionary implications of contrasting patterns between the two rRNA components. J Mol Biol 413:66-83.
    • (2011) J Mol Biol , vol.413 , pp. 66-83
    • Schnare, M.N.1    Gray, M.W.2
  • 170
    • 27644491082 scopus 로고    scopus 로고
    • Structures of the bacterial ribosome at 3.5A ° resolution
    • Schuwirth BS, Borovinskaya MA, Hau CW, et al. (2005). Structures of the bacterial ribosome at 3.5A ° resolution. Science 310:827-34.
    • (2005) Science , vol.310 , pp. 827-834
    • Schuwirth, B.S.1    Borovinskaya, M.A.2    Hau, C.W.3
  • 172
    • 33749354360 scopus 로고    scopus 로고
    • Structure of the 70S ribosome complexed with mRNA and tRNA
    • Selmer M, Dunham CM, Murphy FV, et al. (2006). Structure of the 70S ribosome complexed with mRNA and tRNA. Science 313:1935-42.
    • (2006) Science , vol.313 , pp. 1935-1942
    • Selmer, M.1    Dunham, C.M.2    Murphy, F.V.3
  • 173
    • 33750378312 scopus 로고    scopus 로고
    • Identification of Escherichia coli m2G methyltransferases: II. The ygjO gene encodes a methyltransferase specific for G1835 of the 23 S rRNA
    • Sergiev PV, Lesnyak DV, Bogdanov A, Dontsova O. (2006). Identification of Escherichia coli m2G methyltransferases: II. The ygjO gene encodes a methyltransferase specific for G1835 of the 23 S rRNA. J Mol Biol 364:26-31.
    • (2006) J Mol Biol , vol.364 , pp. 26-31
    • Sergiev, P.V.1    Lesnyak, D.V.2    Bogdanov, A.3    Dontsova, O.4
  • 174
    • 36348929415 scopus 로고    scopus 로고
    • The ybiN gene of Escherichia coli encodes adenine-N6 methyltransferase specific for modification of A1618 of 23 S ribosomal RNA, a methylated residue located close to the ribosomal exit tunnel
    • Sergiev PV, Serebryakova MV, Bogdanov A, Dontsova O. (2008). The ybiN gene of Escherichia coli encodes adenine-N6 methyltransferase specific for modification of A1618 of 23 S ribosomal RNA, a methylated residue located close to the ribosomal exit tunnel. J Mol Biol 375:291-300.
    • (2008) J Mol Biol , vol.375 , pp. 291-300
    • Sergiev, P.V.1    Serebryakova, M.V.2    Bogdanov, A.3    Dontsova, O.4
  • 175
    • 65349111880 scopus 로고    scopus 로고
    • Impact of rRNA methylations on ribosome recycling and fidelity of initiation in Escherichia coli
    • Seshadri A, Dubey B, Weber MHW, Varshney U. (2009). Impact of rRNA methylations on ribosome recycling and fidelity of initiation in Escherichia coli. Mol Microbiol 72:795-808.
    • (2009) Mol Microbiol , vol.72 , pp. 795-808
    • Seshadri, A.1    Dubey, B.2    Weber, M.H.W.3    Varshney, U.4
  • 176
    • 0141953259 scopus 로고    scopus 로고
    • Structure of the mammalian mitochondrial ribosome reveals an expanded functional role for its component proteins
    • Sharma MR, Koc EC, Datta PP, et al. (2003). Structure of the mammalian mitochondrial ribosome reveals an expanded functional role for its component proteins. Cell 115:97-108.
    • (2003) Cell , vol.115 , pp. 97-108
    • Sharma, M.R.1    Koc, E.C.2    Datta, P.P.3
  • 178
    • 77957291981 scopus 로고    scopus 로고
    • Subribosomal particle analysis reveals the stages of bacterial ribosome assembly at which rRNA nucleotides are modified
    • Siibak T, Remme J. (2010). Subribosomal particle analysis reveals the stages of bacterial ribosome assembly at which rRNA nucleotides are modified. RNA (New York, NY) 16:2023-32.
    • (2010) RNA (New York, NY) , vol.16 , pp. 2023-2032
    • Siibak, T.1    Remme, J.2
  • 179
    • 0028932720 scopus 로고
    • Implications of a functional large ribosomal RNA with only three modified nucleotides
    • Sirum-Connolly K, Peltier JM, Crain PF, et al. (1995). Implications of a functional large ribosomal RNA with only three modified nucleotides. Biochimie 77:30-9.
    • (1995) Biochimie , vol.77 , pp. 30-39
    • Sirum-Connolly, K.1    Peltier, J.M.2    Crain, P.F.3
  • 180
    • 0026455198 scopus 로고
    • Methylation sites in Escherichia coli ribosomal RNA: Localization and identification of four new sites of methylation in 23S rRNA
    • Smith JE, Cooperman BS, Mitchell P. (1992). Methylation sites in Escherichia coli ribosomal RNA: localization and identification of four new sites of methylation in 23S rRNA. Biochemistry 31:10825-34.
    • (1992) Biochemistry , vol.31 , pp. 10825-10834
    • Smith, J.E.1    Cooperman, B.S.2    Mitchell, P.3
  • 181
    • 84876907152 scopus 로고    scopus 로고
    • Genome-wide profiling of 5-formylcytosine reveals its roles in epigenetic priming
    • Song C-X, Szulwach KE., Dai Q, et al. (2013). Genome-wide profiling of 5-formylcytosine reveals its roles in epigenetic priming. Cell 153: 678-91.
    • (2013) Cell , vol.153 , pp. 678-691
    • Song, C.-X.1    Szulwach, K.E.2    Dai, Q.3
  • 182
    • 84869392308 scopus 로고    scopus 로고
    • Mapping new nucleotide variants genome and transcriptome
    • Song C-X, Yi C, He C. (2012). Mapping new nucleotide variants genome and transcriptome. Nat Biotech 30:1107-16.
    • (2012) Nat Biotech , vol.30 , pp. 1107-1116
    • Song, C.-X.1    Yi, C.2    He, C.3
  • 183
    • 84855612043 scopus 로고    scopus 로고
    • Functional genomic and advanced genetic studies reveal novel insights into the metabolism, regulation, and biology of Haloferax volcanii
    • 14 pp
    • Soppa J. (2011). Functional genomic and advanced genetic studies reveal novel insights into the metabolism, regulation, and biology of Haloferax volcanii. Archaea 2011:602408. 14 pp.
    • (2011) Archaea , vol.2011 , pp. 602408
    • Soppa, J.1
  • 184
    • 0015575958 scopus 로고
    • Two genetic loci for resistance to kasugamycin in Escherichia coli
    • Sparling P, Ikeya Y, Elliot D. (1973). Two genetic loci for resistance to kasugamycin in Escherichia coli. J Bacteriol 113:704-10.
    • (1973) J Bacteriol , vol.113 , pp. 704-710
    • Sparling, P.1    Ikeya, Y.2    Elliot, D.3
  • 185
    • 84860751168 scopus 로고    scopus 로고
    • Widespread occurrence of 5-methylcytosine in human coding and non-coding RNA
    • Squires JE, Patel HR, Nousch M, et al. (2012). Widespread occurrence of 5-methylcytosine in human coding and non-coding RNA. Nucl Acids Res 40:5023-33.
    • (2012) Nucl Acids Res , vol.40 , pp. 5023-5033
    • Squires, J.E.1    Patel, H.R.2    Nousch, M.3
  • 186
    • 39749110083 scopus 로고    scopus 로고
    • Small non-coding RNAs in animal development
    • Stefani G, Slack FJ. (2008). Small non-coding RNAs in animal development. Nat Rev Mol Cell Biol 9:219-30.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 219-230
    • Stefani, G.1    Slack, F.J.2
  • 187
    • 84936744064 scopus 로고    scopus 로고
    • Analysis of CLIP and iCLIP methods for nucleotide-resolution studies of protein-RNA interactions
    • doi:10.1186/gb-2012-13-8-r67
    • Sugimoto Y, König J, Hussain S, et al. (2012). Analysis of CLIP and iCLIP methods for nucleotide-resolution studies of protein-RNA interactions. Genome Biol 13:R67. doi:10.1186/gb-2012-13-8-r67.
    • (2012) Genome Biol , vol.13
    • Sugimoto, Y.1    König, J.2    Hussain, S.3
  • 188
    • 80755169463 scopus 로고    scopus 로고
    • Human mitochondrial tRNAs: Biogenesis, function, structural aspects, and diseases
    • Suzuki T, Nagao A, Suzuki T. (2011). Human mitochondrial tRNAs: biogenesis, function, structural aspects, and diseases. Annu Rev Genet 45:299-329.
    • (2011) Annu Rev Genet , vol.45 , pp. 299-329
    • Suzuki, T.1    Nagao, A.2    Suzuki, T.3
  • 189
    • 83255176666 scopus 로고    scopus 로고
    • Transforming biochemical engineering with cell-free biology
    • Swartz JR. (2012). Transforming biochemical engineering with cell-free biology. AIChE J 58:5-13.
    • (2012) AIChE J , vol.58 , pp. 5-13
    • Swartz, J.R.1
  • 191
    • 84858730787 scopus 로고    scopus 로고
    • Ribosome evolution: Emergence of peptide synthesis machinery
    • Tamura K. (2011). Ribosome evolution: Emergence of peptide synthesis machinery. J Biosci 36:921-8.
    • (2011) J Biosci , vol.36 , pp. 921-928
    • Tamura, K.1
  • 192
    • 0016321036 scopus 로고
    • Methylation of 16S RNA during ribosome assembly in vitro
    • Thammana P. (1974). Methylation of 16S RNA during ribosome assembly in vitro. Nature 251:682-6.
    • (1974) Nature , vol.251 , pp. 682-686
    • Thammana, P.1
  • 193
    • 38049060422 scopus 로고    scopus 로고
    • The methyltransferase YfgB/RlmN is responsible for modification of adenosine 2503 in 23S rRNA
    • Toh S-M, Xiong L, Bae T, Mankin AS. (2008). The methyltransferase YfgB/RlmN is responsible for modification of adenosine 2503 in 23S rRNA. RNA (New York, NY) 14:98-106.
    • (2008) RNA (New York, NY) , vol.14 , pp. 98-106
    • Toh, S.-M.1    Xiong, L.2    Bae, T.3    Mankin, A.S.4
  • 194
    • 0033050006 scopus 로고    scopus 로고
    • Purification, cloning, and characterization of the 16S RNA m5C967 methyltransferase from Escherichia coli
    • Tscherne JS, Nurse K, Popienick P, et al. (1999a). Purification, cloning, and characterization of the 16S RNA m5C967 methyltransferase from Escherichia coli. Biochemistry 38:1884-92.
    • (1999) Biochemistry , vol.38 , pp. 1884-1892
    • Tscherne, J.S.1    Nurse, K.2    Popienick, P.3
  • 195
    • 0033534617 scopus 로고    scopus 로고
    • Purification, cloning, and characterization of the 16S RNA m2G1207 methyltransferase from Escherichia coli
    • Tscherne JS, Nurse K, Popienick P, Ofengand J. (1999b). Purification, cloning, and characterization of the 16S RNA m2G1207 methyltransferase from Escherichia coli. J Biol Chem 274:924-9.
    • (1999) J Biol Chem , vol.274 , pp. 924-929
    • Tscherne, J.S.1    Nurse, K.2    Popienick, P.3    Ofengand, J.4
  • 196
    • 9244225692 scopus 로고    scopus 로고
    • Guide RNAs with 50 caps and novel box C/D snoRNA-like domains for modification of snRNAs in metazoa
    • Tycowski K, Aab A, Steitz J. (2004). Guide RNAs with 50 caps and novel box C/D snoRNA-like domains for modification of snRNAs in metazoa. Curr Biol 14:1985-95.
    • (2004) Curr Biol , vol.14 , pp. 1985-1995
    • Tycowski, K.1    Aab, A.2    Steitz, J.3
  • 197
    • 0032214692 scopus 로고    scopus 로고
    • Modification of U6 spliceosomal RNA is guided by other small RNAs
    • Tycowski KT, You ZH, Graham PJ, Steitz J. (1998). Modification of U6 spliceosomal RNA is guided by other small RNAs. Mol Cell 2: 629-38.
    • (1998) Mol Cell , vol.2 , pp. 629-638
    • Tycowski, K.T.1    You, Z.H.2    Graham, P.J.3    Steitz, J.4
  • 198
    • 0020606884 scopus 로고
    • Kasugamycin resistant mutants of Bacillus stearothermophilus lacking the enzyme for the methylation of two adjacent adenosines in 16S ribosomal RNA
    • Van Buul CP, Damm JB, Van Knippenberg PH. (1983). Kasugamycin resistant mutants of Bacillus stearothermophilus lacking the enzyme for the methylation of two adjacent adenosines in 16S ribosomal RNA. Mol Gen Genet: MGG 189:475-8.
    • (1983) Mol Gen Genet: MGG , vol.189 , pp. 475-478
    • Van Buul, C.P.1    Damm, J.B.2    Van Knippenberg, P.H.3
  • 199
    • 0021760747 scopus 로고
    • Partial methylation of two adjacent adenosines in ribosomes from Euglena gracilis chloroplasts suggests evolutionary loss of an intermediate stage in the methyl-transfer reaction
    • Van Buul C, Hamersma M, Visser W, Van Knippenberg PH. (1984). Partial methylation of two adjacent adenosines in ribosomes from Euglena gracilis chloroplasts suggests evolutionary loss of an intermediate stage in the methyl-transfer reaction. Nucl Acids Res 12:9205-8.
    • (1984) Nucl Acids Res , vol.12 , pp. 9205-9208
    • Van Buul, C.1    Hamersma, M.2    Visser, W.3    Van Knippenberg, P.H.4
  • 200
    • 70949102952 scopus 로고    scopus 로고
    • Next generation sequencing of microbial transcriptomes: Challenges and opportunities
    • Van Vliet AHM. (2010). Next generation sequencing of microbial transcriptomes: challenges and opportunities. FEMS Microbiol Lett 302:1-7.
    • (2010) FEMS Microbiol Lett , vol.302 , pp. 1-7
    • Van Vliet, A.H.M.1
  • 201
    • 0014214135 scopus 로고
    • Inhibition of leucyl-RNA synthetase by periodateoxidized transfer {RNA} modified by hydroxylamine
    • Vries GM De. (1967). Inhibition of leucyl-RNA synthetase by periodateoxidized transfer {RNA} modified by hydroxylamine. Biochim Biophys Acta (BBA) - Nucl Acids Protein Synth 145:169-71.
    • (1967) Biochim Biophys Acta (BBA) - Nucl Acids Protein Synth , vol.145 , pp. 169-171
    • De Vries, G.M.1
  • 202
    • 84862156291 scopus 로고    scopus 로고
    • Structure of the bifunctional methyltransferase YcbY (RlmKL) that adds the m7G2069 and m2G2445 modifications in Escherichia coli 23S rRNA
    • Wang K-T, Desmolaize B, Nan J, et al. (2012). Structure of the bifunctional methyltransferase YcbY (RlmKL) that adds the m7G2069 and m2G2445 modifications in Escherichia coli 23S rRNA. Nucl Acids Res 40:5138-48.
    • (2012) Nucl Acids Res , vol.40 , pp. 5138-5148
    • Wang, K.-T.1    Desmolaize, B.2    Nan, J.3
  • 203
    • 0016219098 scopus 로고
    • Replacement of ribothymidine by 5-methyl-2-thiouridine in sequence GT C in tRNA of an extreme thermophile
    • Watanabe K, Oshima T, Saneyoshi M, Nishimupa S. (1974). Replacement of ribothymidine by 5-methyl-2-thiouridine in sequence GT C in tRNA of an extreme thermophile. FEBS Lett 43:59-63.
    • (1974) FEBS Lett , vol.43 , pp. 59-63
    • Watanabe, K.1    Oshima, T.2    Saneyoshi, M.3    Nishimupa, S.4
  • 204
    • 0242300069 scopus 로고    scopus 로고
    • The genome of Nanoarchaeum equitans: Insights into early archaeal evolution and derived parasitism
    • Waters E, Hohn MJ, Ahel I, et al. (2003). The genome of Nanoarchaeum equitans: insights into early archaeal evolution and derived parasitism. Proc Natl Acad Sci USA 100:12984-8.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12984-12988
    • Waters, E.1    Hohn, M.J.2    Ahel, I.3
  • 205
    • 50549204962 scopus 로고
    • Effects of chemical modifications on the biological properties of s-RNA
    • Weil J-H, Befort N, Rether B, Ebel J-P. (1964). Effects of chemical modifications on the biological properties of s-RNA. Biochem Biophys Res Commun 15:447-52.
    • (1964) Biochem Biophys Res Commun , vol.15 , pp. 447-452
    • Weil, J.-H.1    Befort, N.2    Rether, B.3    Ebel, J.-P.4
  • 206
    • 0035370526 scopus 로고    scopus 로고
    • Spliceosomal UsnRNP biogenesis, structure and function
    • Will CL, Lührmann R. (2001). Spliceosomal UsnRNP biogenesis, structure and function. Curr Opin Cell Biol 13:290-301.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 290-301
    • Will, C.L.1    Lührmann, R.2
  • 207
    • 0035808304 scopus 로고    scopus 로고
    • Localization of the protein {L2} in the 50 S subunit and the 70 S E. Coli ribosome
    • Willumeit R, Forthmann S, Beckmann J, et al. (2001). Localization of the protein {L2} in the 50 S subunit and the 70 S E. coli ribosome. J Mol Biol 305:167-77.
    • (2001) J Mol Biol , vol.305 , pp. 167-177
    • Willumeit, R.1    Forthmann, S.2    Beckmann, J.3
  • 208
    • 43249093216 scopus 로고    scopus 로고
    • A conserved rRNA methyltransferase regulates ribosome biogenesis
    • Xu Z, O'Farrell HC, Rife JP, Culver GM. (2008). A conserved rRNA methyltransferase regulates ribosome biogenesis. Nat Struct Mol Biol 15:534-6.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 534-536
    • Xu, Z.1    O'farrell, H.C.2    Rife, J.P.3    Culver, G.M.4
  • 209
    • 79952748781 scopus 로고    scopus 로고
    • RNA methylation by radical SAM enzymes RlmN and Cfr proceeds via methylene transfer and hydride shift
    • Yan F, Fujimori DG. (2011). RNA methylation by radical SAM enzymes RlmN and Cfr proceeds via methylene transfer and hydride shift. Proc Natl Acad Sci USA 108:3930-4.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 3930-3934
    • Yan, F.1    Fujimori, D.G.2
  • 210
    • 77949777140 scopus 로고    scopus 로고
    • RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA
    • Yan F, LaMarre JM, Röhrich R, et al. (2010). RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA. J Am Chem Soc 132:3953-64.
    • (2010) J Am Chem Soc , vol.132 , pp. 3953-3964
    • Yan, F.1    Lamarre, J.M.2    Röhrich, R.3
  • 211
    • 0035801225 scopus 로고    scopus 로고
    • Wobble modification defect in tRNA disturbs codon-anticodon interaction in a mitochondrial disease
    • Yasukawa T, Suzuki T, Ishii N, et al. (2001). Wobble modification defect in tRNA disturbs codon-anticodon interaction in a mitochondrial disease. EMBO J 20:4794-802.
    • (2001) EMBO J , vol.20 , pp. 4794-4802
    • Yasukawa, T.1    Suzuki, T.2    Ishii, N.3
  • 212
    • 0000238430 scopus 로고
    • Molecular mechanism of codon recognition by tRNA species with modified uridine in the first position of the anticodon
    • Yokoyama S,Watanabe T, Murao K, et al. (1985). Molecular mechanism of codon recognition by tRNA species with modified uridine in the first position of the anticodon. Proc Natl Acad Sci USA 82:4905-9.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4905-4909
    • Yokoyama, S.1    Watanabe, T.2    Murao, K.3
  • 213
    • 13644256193 scopus 로고    scopus 로고
    • Methylation as a crucial step in plant microRNA biogenesis
    • Yu B, Yang Z, Li J, et al. (2005). Methylation as a crucial step in plant microRNA biogenesis. Science (New York, NY) 307:932-5.
    • (2005) Science (New York, NY) , vol.307 , pp. 932-935
    • Yu, B.1    Yang, Z.2    Li, J.3
  • 214
    • 76449115656 scopus 로고    scopus 로고
    • Integrating multiple "omics" analysis for microbial biology: Application and methodologies
    • Zhang W, Li F, Nie L. (2010). Integrating multiple "omics" analysis for microbial biology: application and methodologies. Microbiology (Reading, Engl) 156:287-301.
    • (2010) Microbiology (Reading, Engl) , vol.156 , pp. 287-301
    • Zhang, W.1    Li, F.2    Nie, L.3
  • 215
    • 84872274463 scopus 로고    scopus 로고
    • ALKBH5 is a mammalian RNA demethylase that impacts RNA metabolism and mouse fertility
    • Zheng G, Dahl JA, Niu Y, et al. (2013). ALKBH5 is a mammalian RNA demethylase that impacts RNA metabolism and mouse fertility. Mol cell 49:18-29.
    • (2013) Mol Cell , vol.49 , pp. 18-29
    • Zheng, G.1    Dahl, J.A.2    Niu, Y.3


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