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Volumn 12, Issue 2, 2013, Pages 302-311

Proteomic analysis reveals diverse classes of arginine methylproteins in mitochondria of trypanosomes

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; ARGININE METHYLPROTEIN; PROTEOME; UNCLASSIFIED DRUG;

EID: 84874025753     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M112.022533     Document Type: Article
Times cited : (59)

References (54)
  • 1
    • 58149295717 scopus 로고    scopus 로고
    • Protein arginine methylation in mammals: Who, what, and why
    • Bedford, M. T., and Clarke, S. G. (2009) Protein arginine methylation in mammals: who, what, and why. Mol. Cell 33, 1-13
    • (2009) Mol. Cell , vol.33 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 3
    • 51549095388 scopus 로고    scopus 로고
    • Substrate profiling of PRMT1 reveals amino acid sequences that extend beyond the "RGG," paradigm
    • Wooderchak, W. L., Zang, T., Zhou, Z. S., Acuña, M., Tahara, S. M., and Hevel, J. M. (2008) Substrate profiling of PRMT1 reveals amino acid sequences that extend beyond the "RGG" paradigm. Biochemistry 47, 9456-9466
    • (2008) Biochemistry , vol.47 , pp. 9456-9466
    • Wooderchak, W.L.1    Zang, T.2    Zhou, Z.S.3    Acuña, M.4    Tahara, S.M.5    Hevel, J.M.6
  • 4
    • 3342936604 scopus 로고    scopus 로고
    • PRMT3 is a ribosomal protein meth- yltransferase that affects the cellular levels of ribosomal subunits
    • Bachand, F., and Silver, P. A. (2004) PRMT3 is a ribosomal protein meth- yltransferase that affects the cellular levels of ribosomal subunits. EMBO J. 23, 2641-2650
    • (2004) EMBO J. , vol.23 , pp. 2641-2650
    • Bachand, F.1    Silver, P.A.2
  • 5
    • 34247612060 scopus 로고    scopus 로고
    • The arginine methyltransferase rmt2 is enriched in the nucleus and copurifies with the nuclear porins nup49, nup57 and nup100
    • Olsson, I., Berrez, J. M., Leipus, A., Ostlund, C., and Mutvei, A. (2007) The arginine methyltransferase Rmt2 is enriched in the nucleus and copurifies with the nuclear porins Nup49, Nup57 and Nup100. Exp. Cell Res. 313, 1778-1789
    • (2007) Exp. Cell Res. , vol.313 , pp. 1778-1789
    • Olsson, I.1    Berrez, J.M.2    Leipus, A.3    Ostlund, C.4    Mutvei, A.5
  • 6
    • 34147145820 scopus 로고    scopus 로고
    • Regulation of the nuclear poly(A)-binding protein by arginine methylation in fission yeast
    • Perreault, A., Lemieux, C., and Bachand, F. (2007) Regulation of the nuclear poly(A)-binding protein by arginine methylation in fission yeast. J. Biol. Chem. 282, 7552-7562
    • (2007) J. Biol. Chem. , vol.282 , pp. 7552-7562
    • Perreault, A.1    Lemieux, C.2    Bachand, F.3
  • 7
    • 48849107682 scopus 로고    scopus 로고
    • Identifying and quantifying sites of protein methylation by heavy methyl SILAC
    • Chapter 14, Unit 14.19
    • Ong, S.-E., and Mann, M. (2006) Identifying and quantifying sites of protein methylation by heavy methyl SILAC. Curr. Protoc. Protein Sci. Chapter 14, Unit 14.19
    • (2006) Curr. Protoc. Protein Sci.
    • Ong, S.-E.1    Mann, M.2
  • 10
    • 35349012982 scopus 로고    scopus 로고
    • Post-transcriptional regulation of gene expression in trypanosomes and leishmanias
    • Clayton, C., and Shapira, M. (2007) Post-transcriptional regulation of gene expression in trypanosomes and leishmanias. Mol. Biochem. Parasit. 156, 93-101
    • (2007) Mol. Biochem. Parasit. , vol.156 , pp. 93-101
    • Clayton, C.1    Shapira, M.2
  • 11
    • 28044460265 scopus 로고    scopus 로고
    • Unexplained complexity of the mitochondrial genome and transcriptome in kinetoplastid flagellates
    • Lukes, J., Hashimi, H., and Ziková, A. (2005) Unexplained complexity of the mitochondrial genome and transcriptome in kinetoplastid flagellates. Curr. Genet. 48, 277-299
    • (2005) Curr. Genet. , vol.48 , pp. 277-299
    • Lukes, J.1    Hashimi, H.2    Ziková, A.3
  • 13
    • 79961043508 scopus 로고    scopus 로고
    • Protein arginine methylation in parasitic protozoa
    • Fisk, J. C., and Read, L. K. (2011) Protein arginine methylation in parasitic protozoa. Eukaryot Cell 10, 1013-1022
    • (2011) Eukaryot Cell , vol.10 , pp. 1013-1022
    • Fisk, J.C.1    Read, L.K.2
  • 14
    • 77953801717 scopus 로고    scopus 로고
    • TbPRMT6 is a type I protein arginine methyltransferase that contributes to cytokinesis in trypanosoma brucei
    • Fisk, J. C., Zurita-Lopez, C., Sayegh, J., Tomasello, D. L., Clarke, S. G., and Read, L. K. (2010) TbPRMT6 Is a Type I Protein Arginine Methyltransferase That Contributes to Cytokinesis in Trypanosoma brucei. Eukaryot Cell 9, 866-877
    • (2010) Eukaryot Cell , vol.9 , pp. 866-877
    • Fisk, J.C.1    Zurita-Lopez, C.2    Sayegh, J.3    Tomasello, D.L.4    Clarke, S.G.5    Read, L.K.6
  • 15
    • 66449092553 scopus 로고    scopus 로고
    • A type III protein arginine methyltransferase from the protozoan parasite trypanosoma brucei
    • Fisk, J. C., Sayegh, J., Zurita-Lopez, C., Menon, S., Presnyak, V., Clarke, S. G., and Read, L. K. (2009) A type III protein arginine methyltransferase from the protozoan parasite Trypanosoma brucei. J. Biol. Chem. 284, 11590-11600
    • (2009) J. Biol. Chem. , vol.284 , pp. 11590-11600
    • Fisk, J.C.1    Sayegh, J.2    Zurita-Lopez, C.3    Menon, S.4    Presnyak, V.5    Clarke, S.G.6    Read, L.K.7
  • 16
    • 34748853038 scopus 로고    scopus 로고
    • Evolution- arily divergent type II protein arginine methyltransferase in trypanosoma brucei
    • Pasternack, D. A., Sayegh, J., Clarke, S., and Read, L. K. (2007) Evolution- arily divergent type II protein arginine methyltransferase in Trypanosoma brucei. Eukaryot Cell 6, 1665-1681
    • (2007) Eukaryot Cell , vol.6 , pp. 1665-1681
    • Pasternack, D.A.1    Sayegh, J.2    Clarke, S.3    Read, L.K.4
  • 17
    • 27644531658 scopus 로고    scopus 로고
    • In vitro and in vivo analysis of the major type I protein arginine methyltransferase from trypanosoma brucei
    • Pelletier, M., Pasternack, D. A., and Read, L. K. (2005) In vitro and in vivo analysis of the major type I protein arginine methyltransferase from Trypanosoma brucei. Mol. Biochem. Parasitol. 144, 206-217
    • (2005) Mol. Biochem. Parasitol. , vol.144 , pp. 206-217
    • Pelletier, M.1    Pasternack, D.A.2    Read, L.K.3
  • 18
    • 34147094091 scopus 로고    scopus 로고
    • Differential effects of arginine meth- ylation on RBP16 mRNA binding, guide RNA(gRNA) binding, and gRNAcontaining ribonucleoprotein complex (gRNP) formation
    • Goulah, C. C., and Read, L. K. (2007) Differential effects of arginine meth- ylation on RBP16 mRNA binding, guide RNA(gRNA) binding, and gRNAcontaining ribonucleoprotein complex (gRNP) formation. J. Biol. Chem. 282, 7181-7190
    • (2007) J. Biol. Chem. , vol.282 , pp. 7181-7190
    • Goulah, C.C.1    Read, L.K.2
  • 19
    • 53149112760 scopus 로고    scopus 로고
    • TbRGG2, an essential RNA editing accessory factor in two trypanosoma brucei life cycle stages
    • Fisk, J. C, Ammerman, M. L, Presnyak, V., and Read, L. K. (2008) TbRGG2, an essential RNA editing accessory factor in two Trypanosoma brucei life cycle stages. J. Biol. Chem. 283, 23016-23025
    • (2008) J. Biol. Chem. , vol.283 , pp. 23016-23025
    • Fisk, J.C.1    Ammerman, M.L.2    Presnyak, V.3    Read, L.K.4
  • 20
    • 79953184730 scopus 로고    scopus 로고
    • A novel member of the RNase D exoribonuclease family functions in mitochondrial guide RNA metabolism in trypanosoma brucei
    • Zimmer, S. L, McEvoy, S. M., Li, J., Qu, J., and Read, L. K. (2011) A novel member of the RNase D exoribonuclease family functions in mitochondrial guide RNA metabolism in Trypanosoma brucei. J. Biol. Chem. 286, 10329-10340
    • (2011) J. Biol. Chem. , vol.286 , pp. 10329-10340
    • Zimmer, S.L.1    McEvoy, S.M.2    Li, J.3    Qu, J.4    Read, L.K.5
  • 21
    • 0025351935 scopus 로고
    • Addition of uridines to edited RNAs in trypanosome mitochondria occurs independently of transcription
    • Harris, M. E., Moore, D. R., and Hajduk, S. L. (1990) Addition of uridines to edited RNAs in trypanosome mitochondria occurs independently of transcription. J. Biol. Chem. 265, 11368-11376
    • (1990) J. Biol. Chem. , vol.265 , pp. 11368-11376
    • Harris, M.E.1    Moore, D.R.2    Hajduk, S.L.3
  • 22
    • 67049119810 scopus 로고    scopus 로고
    • A straightforward and highly efficient precipitation/on-pellet digestion procedure coupled with a long gradient nano-LC separation and orbitrap mass spectrometry for label-free expression profiling of the swine heart mitochondrial proteome
    • Duan, X., Young, R., Straubinger, R. M., Page, B., Cao, J., Wang, H., Yu, H., Canty, J. M., and Qu, J. (2009) A straightforward and highly efficient precipitation/on-pellet digestion procedure coupled with a long gradient nano-LC separation and orbitrap mass spectrometry for label-free expression profiling of the swine heart mitochondrial proteome. J. Proteome Res. 8, 2838-2850
    • (2009) J. Proteome Res. , vol.8 , pp. 2838-2850
    • Duan, X.1    Young, R.2    Straubinger, R.M.3    Page, B.4    Cao, J.5    Wang, H.6    Yu, H.7    Canty, J.M.8    Qu, J.9
  • 23
    • 33746581154 scopus 로고    scopus 로고
    • Arginine methylation regulates mitochondrial gene expression in trypanosoma brucei through multiple effector proteins
    • Goulah, C. C, Pelletier, M., and Read, L. K. (2006) Arginine methylation regulates mitochondrial gene expression in Trypanosoma brucei through multiple effector proteins. RNA 12, 1545-1555
    • (2006) RNA , vol.12 , pp. 1545-1555
    • Goulah, C.C.1    Pelletier, M.2    Read, L.K.3
  • 25
    • 84861142055 scopus 로고    scopus 로고
    • High- throughput method development for sensitive, accurate, and reproducible quantification of therapeutic monoclonal antibodies in tissues using orthogonal array optimization and nano liquid chromatography/selected reaction monitoring mass spectrometry
    • Duan, X., Abuqayyas, L, Dai, L, Balthasar, J. P., and Qu, J. (2012) High- throughput method development for sensitive, accurate, and reproducible quantification of therapeutic monoclonal antibodies in tissues using orthogonal array optimization and nano liquid chromatography/selected reaction monitoring mass spectrometry. Anal. Chem. 84, 4373-4382
    • (2012) Anal. Chem. , vol.84 , pp. 4373-4382
    • Duan, X.1    Abuqayyas, L.2    Dai, L.3    Balthasar, J.P.4    Qu, J.5
  • 26
    • 60649099160 scopus 로고    scopus 로고
    • Accurate localization and relative quantification of arginine methylation using nanoflow liquid chromatography coupled to electron transfer dissociation and orbitrap mass spectrometry
    • Wang, H., Straubinger, R. M., Aletta, J. M., Cao, J., Duan, X., Yu, H., and Qu, J. (2009) Accurate localization and relative quantification of arginine methylation using nanoflow liquid chromatography coupled to electron transfer dissociation and orbitrap mass spectrometry. J. Am. Soc. Mass Spectr. 20, 507-519
    • (2009) J. Am. Soc. Mass Spectr. , vol.20 , pp. 507-519
    • Wang, H.1    Straubinger, R.M.2    Aletta, J.M.3    Cao, J.4    Duan, X.5    Yu, H.6    Qu, J.7
  • 27
    • 65549106401 scopus 로고    scopus 로고
    • Methyl group migration during the fragmentation of singly charged ions of trimethyllysine-containing peptides: Precaution of using MS/MS of singly charged ions for interrogating peptide methylation
    • Xiong, L, Ping, L, Yuan, B., and Wang, Y. (2009) Methyl group migration during the fragmentation of singly charged ions of trimethyllysine-containing peptides: precaution of using MS/MS of singly charged ions for interrogating peptide methylation. J. Am. Soc. Mass Spectrom. 20, 1172-1181
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 1172-1181
    • Xiong, L.1    Ping, L.2    Yuan, B.3    Wang, Y.4
  • 28
    • 18744375196 scopus 로고    scopus 로고
    • Identifying and quantifying in vivo methylation sites by heavy methyl SILAC
    • Ong, S. E., Mittler, G., and Mann, M. (2004) Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. Nat. Methods 1, 119-126
    • (2004) Nat. Methods , vol.1 , pp. 119-126
    • Ong, S.E.1    Mittler, G.2    Mann, M.3
  • 31
    • 67249130258 scopus 로고    scopus 로고
    • The F(0)F(1)-ATP synthase complex contains novel subunits and is essential for procyclic trypanosoma brucei
    • Zikova, A., Schnaufer, A., Dalley, R. A., Panigrahi, A. K., and Stuart, K. D. (2009) The F(0)F(1)-ATP synthase complex contains novel subunits and is essential for procyclic Trypanosoma brucei. PLoS Pathog. 5, e1000436
    • (2009) PLoS Pathog. , vol.5
    • Zikova, A.1    Schnaufer, A.2    Dalley, R.A.3    Panigrahi, A.K.4    Stuart, K.D.5
  • 32
  • 33
    • 18144381509 scopus 로고    scopus 로고
    • Mitochondrial initiation factor 2 of trypanosoma brucei binds imported formylated elongatortype tRNA(Met)
    • Charrière, F., Tan, T. H. P., and Schneider, A. (2005) Mitochondrial initiation factor 2 of Trypanosoma brucei binds imported formylated elongatortype tRNA(Met). J. Biol. Chem. 280, 15659-15665
    • (2005) J. Biol. Chem. , vol.280 , pp. 15659-15665
    • Charrière, F.1    Tan, T.H.P.2    Schneider, A.3
  • 34
    • 44649128170 scopus 로고    scopus 로고
    • 3′ adenylation determines mRNA abundance and monitors completion of RNA editing in T. Brucei mitochondria
    • Etheridge, R. D., Aphasizheva, I., Gershon, P. D., and Aphasizhev, R. (2008) 3′ adenylation determines mRNA abundance and monitors completion of RNA editing in T. brucei mitochondria. EMBO J. 27, 1596-1608
    • (2008) EMBO J. , vol.27 , pp. 1596-1608
    • Etheridge, R.D.1    Aphasizheva, I.2    Gershon, P.D.3    Aphasizhev, R.4
  • 35
    • 42449091992 scopus 로고    scopus 로고
    • TbRGG1, an essential protein involved in kinetoplastid RNA metabolism that is associated with a novel multiprotein complex
    • Hashimi, H., Zikova, A., Panigrahi, A. K., Stuart, K. D., and Lukes, J. (2008) TbRGG1, an essential protein involved in kinetoplastid RNA metabolism that is associated with a novel multiprotein complex. RNA 14, 970-980
    • (2008) RNA , vol.14 , pp. 970-980
    • Hashimi, H.1    Zikova, A.2    Panigrahi, A.K.3    Stuart, K.D.4    Lukes, J.5
  • 36
    • 28044439400 scopus 로고    scopus 로고
    • An essential RNase III insertion editing endonuclease in trypanosoma brucei
    • Carnes, J., Trotter, J. R., Ernst, N. L., Steinberg, A., and Stuart, K. (2005) An essential RNase III insertion editing endonuclease in Trypanosoma brucei. Proc. Natl. Acad. Sci. 102, 16614-16619
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , pp. 16614-16619
    • Carnes, J.1    Trotter, J.R.2    Ernst, N.L.3    Steinberg, A.4    Stuart, K.5
  • 37
    • 33646870148 scopus 로고    scopus 로고
    • Compositionally and functionally distinct editosomes in trypanosoma brucei
    • Panigrahi, A. K., Ernst, N. L., Domingo, G. J., Fleck, M., Salavati, R., and Stuart, K. D. (2006) Compositionally and functionally distinct editosomes in Trypanosoma brucei. RNA 12, 1038-1049
    • (2006) RNA , vol.12 , pp. 1038-1049
    • Panigrahi, A.K.1    Ernst, N.L.2    Domingo, G.J.3    Fleck, M.4    Salavati, R.5    Stuart, K.D.6
  • 38
    • 0024272032 scopus 로고
    • Localization of a type II DNA topoisomerase to two sites at the periphery of the kinetoplast DNA of crithidia fasciculata
    • Melendy, T., Sheline, C., and Ray, D. S. (1988) Localization of a type II DNA topoisomerase to two sites at the periphery of the kinetoplast DNA of Crithidia fasciculata. Cell 55, 1083-1088
    • (1988) Cell , vol.55 , pp. 1083-1088
    • Melendy, T.1    Sheline, C.2    Ray, D.S.3
  • 39
    • 79952292701 scopus 로고    scopus 로고
    • A second mitochondrial DNA primase is essential for cell growth and kinetoplast minicircle DNA replication in trypanosoma brucei
    • Hines, J. C., and Ray, D. S. (2011) A second mitochondrial DNA primase is essential for cell growth and kinetoplast minicircle DNA replication in Trypanosoma brucei. Eukaryot Cell 10, 445-454
    • (2011) Eukaryot Cell , vol.10 , pp. 445-454
    • Hines, J.C.1    Ray, D.S.2
  • 40
    • 77749330824 scopus 로고    scopus 로고
    • A mitochondrial DNA primase is essential for cell growth and kinetoplast DNA replication in trypanosoma brucei
    • Hines, J. C., and Ray, D. S. (2010) A mitochondrial DNA primase is essential for cell growth and kinetoplast DNA replication in Trypanosoma brucei. Mol. Cell. Biol. 30, 1319-1328
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 1319-1328
    • Hines, J.C.1    Ray, D.S.2
  • 41
    • 0036342502 scopus 로고    scopus 로고
    • Multiple mito- chondrial DNA polymerases in trypanosoma brucei
    • Klingbeil, M. M., Motyka, S. A., and Englund, P. T. (2002) Multiple mito- chondrial DNA polymerases in Trypanosoma brucei. Mol. Cell 10, 175-186
    • (2002) Mol. Cell , vol.10 , pp. 175-186
    • Klingbeil, M.M.1    Motyka, S.A.2    Englund, P.T.3
  • 42
    • 6344222803 scopus 로고    scopus 로고
    • Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes
    • Pal, S., Vishwanath, S. N., Erdjument-Bromage, H., Tempst, P., and Sif, S. (2004) Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes. Mol. Cell. Biol. 24, 9630-9645
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9630-9645
    • Pal, S.1    Vishwanath, S.N.2    Erdjument-Bromage, H.3    Tempst, P.4    Sif, S.5
  • 44
    • 33646743169 scopus 로고    scopus 로고
    • Regulation of the EBNA1 epstein-barr virus protein by serine phosphorylation and arginine methylation
    • Shire, K., Kapoor, P., Jiang, K., Hing, M. N., Sivachandran, N., Nguyen, T., and Frappier, L. (2006) Regulation of the EBNA1 Epstein-Barr virus protein by serine phosphorylation and arginine methylation. J. Virol. 80, 5261-5272
    • (2006) J. Virol. , vol.80 , pp. 5261-5272
    • Shire, K.1    Kapoor, P.2    Jiang, K.3    Hing, M.N.4    Sivachandran, N.5    Nguyen, T.6    Frappier, L.7
  • 45
    • 0036205436 scopus 로고    scopus 로고
    • PABP1 identified as an arginine methyl- transferase substrate using high-density protein arrays
    • Lee, J., and Bedford, M. T. (2002) PABP1 identified as an arginine methyl- transferase substrate using high-density protein arrays. EMBO R 3, 268-273
    • (2002) EMBO R , vol.3 , pp. 268-273
    • Lee, J.1    Bedford, M.T.2
  • 46
    • 79959241965 scopus 로고    scopus 로고
    • Combinatorial peptide ligand library treatment followed by a dual-enzyme, dual-activation approach on a nanoflow liquid chromatography/orbitrap/electron transfer dissociation system for comprehensive analysis of swine plasma proteome
    • Tu, C., Li, J., Young, R., Page, B. J., Engler, F., Halfon, M. S., Canty, J. M., Jr., and Qu, J. (2011) Combinatorial peptide ligand library treatment followed by a dual-enzyme, dual-activation approach on a nanoflow liquid chromatography/orbitrap/electron transfer dissociation system for comprehensive analysis of swine plasma proteome. Anal. Chem. 83, 4802-4813
    • (2011) Anal. Chem , vol.83 , pp. 4802-4813
    • Tu, C.1    Li, J.2    Young, R.3    Page, B.J.4    Engler, F.5    Halfon, M.S.6    Canty Jr., J.M.7    Qu, J.8
  • 47
    • 30944438032 scopus 로고    scopus 로고
    • ATP synthase is responsible for maintaining mitochondrial membrane potential in bloodstream form trypanosoma brucei
    • Brown, S. V., Hosking, P., Li, J., and Williams, N. (2006) ATP synthase is responsible for maintaining mitochondrial membrane potential in bloodstream form Trypanosoma brucei. Euk. Cell 5, 45-53
    • (2006) Euk. Cell , vol.5 , pp. 45-53
    • Brown, S.V.1    Hosking, P.2    Li, J.3    Williams, N.4
  • 48
    • 33644872283 scopus 로고    scopus 로고
    • The F1-ATP synthase complex in bloodstream stage trypanosomes has an unusual and essential function
    • Mar 8
    • Schnaufer, A., Clark-Walker, G. D., Steinberg, A. G., and Stuart, K. (2005) The F1-ATP synthase complex in bloodstream stage trypanosomes has an unusual and essential function.[erratum appears in EMBO J. 2006 Mar 8; 25(5):1175-6].
    • (2005) Erratum Appears in EMBO J. , vol.25 , Issue.5 , pp. 1175-1176
    • Schnaufer, A.1    Clark-Walker, G.D.2    Steinberg, A.G.3    Stuart, K.4
  • 49
    • 84874071358 scopus 로고    scopus 로고
    • EMBO J. 24, 4029-4040
    • EMBO J. , vol.24 , pp. 4029-4040
  • 50
    • 77951217870 scopus 로고    scopus 로고
    • Methyl- ation of ribosomal protein S10 by protein-arginine methyltransferase 5 regulates ribosome biogenesis
    • Ren, J., Wang, Y., Liang, Y., Zhang, Y., Bao, S., and Xu, Z. (2010) Methyl- ation of ribosomal protein S10 by protein-arginine methyltransferase 5 regulates ribosome biogenesis. J. Biol. Chem. 285, 12695-12705
    • (2010) J. Biol. Chem. , vol.285 , pp. 12695-12705
    • Ren, J.1    Wang, Y.2    Liang, Y.3    Zhang, Y.4    Bao, S.5    Xu, Z.6
  • 51
    • 84857734775 scopus 로고    scopus 로고
    • Uridine insertion/deletion editing in trypanosomes: A playground for RNA-guided information transfer
    • Aphasizhev, R., and Aphasizheva, I. (2011) Uridine insertion/deletion editing in trypanosomes: a playground for RNA-guided information transfer. Wiley Interdiscip. Rev. RNA 2, 669-685
    • (2011) Wiley Interdiscip. Rev. RNA , vol.2 , pp. 669-685
    • Aphasizhev, R.1    Aphasizheva, I.2
  • 52
    • 37549054714 scopus 로고    scopus 로고
    • RNA editing in trypanosoma brucei requires three different editosomes
    • Carnes, J., Trotter, J. R., Peltan, A., Fleck, M., and Stuart, K. (2008) RNA editing in Trypanosoma brucei requires three different editosomes. Mol. Cell. Biol. 28, 122-130
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 122-130
    • Carnes, J.1    Trotter, J.R.2    Peltan, A.3    Fleck, M.4    Stuart, K.5


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