메뉴 건너뛰기




Volumn 20, Issue 1, 2014, Pages 88-102

The C-terminal extension of Lsm4 interacts directly with the 3′ end of the histone mRNP and is required for efficient histone mRNA degradation

Author keywords

ERI1; Histone mRNA; Lsm proteins; MRNA degradation; SLBP

Indexed keywords

HISTONE; MESSENGER RNA; POLYADENYLATED RNA;

EID: 84890612895     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.042531.113     Document Type: Article
Times cited : (25)

References (53)
  • 3
    • 0035171131 scopus 로고    scopus 로고
    • Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B and the Sm-like protein LSm4, and their interaction with the SMN protein
    • Brahms H, Meheus L, de Brabandere V, Fischer U, Luhrmann R. 2001. Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B and the Sm-like protein LSm4, and their interaction with the SMN protein. RNA 7: 1531-1542.
    • (2001) RNA , vol.7 , pp. 1531-1542
    • Brahms, H.1    Meheus, L.2    De Brabandere, V.3    Fischer, U.4    Luhrmann, R.5
  • 4
    • 38549117402 scopus 로고    scopus 로고
    • SLIP1, a factor required for activation of histone mRNA translation by the stem-loop binding protein
    • Cakmakci NG, Lerner RS, Wagner EJ, Zheng L-X, Marzluff WF. 2008. SLIP1, a factor required for activation of histone mRNA translation by the stem-loop binding protein. Mol Cell Biol 28: 1182-1194.
    • (2008) Mol Cell Biol , vol.28 , pp. 1182-1194
    • Cakmakci, N.G.1    Lerner, R.S.2    Wagner, E.J.3    Zheng, L.-X.4    Marzluff, W.F.5
  • 5
    • 84875479075 scopus 로고    scopus 로고
    • Rapid degradation of replication-dependent histone mRNAs largely occurs on mRNAs bound by nuclear cap-binding proteins 80 and 20
    • Choe J, Kim KM, Park S, Lee YK, Song OK, Kim MK, Lee BG, Song HK, Kim YK. 2013. Rapid degradation of replication-dependent histone mRNAs largely occurs on mRNAs bound by nuclear cap-binding proteins 80 and 20. Nucleic Acids Res 41: 1307-1318.
    • (2013) Nucleic Acids Res , vol.41 , pp. 1307-1318
    • Choe, J.1    Kim, K.M.2    Park, S.3    Lee, Y.K.4    Song, O.K.5    Kim, M.K.6    Lee, B.G.7    Song, H.K.8    Kim, Y.K.9
  • 6
    • 52949141485 scopus 로고    scopus 로고
    • Lsm1 mutations impairing the ability of the Lsm1p-7p-Pat1p complex to preferentially bind to oligoadenylated RNA affect mRNA decay in vivo
    • Chowdhury A, Tharun S. 2008. lsm1 mutations impairing the ability of the Lsm1p-7p-Pat1p complex to preferentially bind to oligoadenylated RNA affect mRNA decay in vivo. RNA 14: 2149-2158.
    • (2008) RNA , vol.14 , pp. 2149-2158
    • Chowdhury, A.1    Tharun, S.2
  • 7
    • 34250804009 scopus 로고    scopus 로고
    • The decapping activator Lsm1p-7p-Pat1p complex has the intrinsic ability to distinguish between oligoadenylated and polyadenylated RNAs
    • Chowdhury A, Mukhopadhyay J, Tharun S. 2007. The decapping activator Lsm1p-7p-Pat1p complex has the intrinsic ability to distinguish between oligoadenylated and polyadenylated RNAs. RNA 13: 998-1016.
    • (2007) RNA , vol.13 , pp. 998-1016
    • Chowdhury, A.1    Mukhopadhyay, J.2    Tharun, S.3
  • 8
    • 2442566370 scopus 로고    scopus 로고
    • Cytoplasmic foci are sites of mRNA decay in human cells
    • Cougot N, Babajko S, Seraphin B. 2004. Cytoplasmic foci are sites of mRNA decay in human cells. J Cell Biol 165: 31-40.
    • (2004) J Cell Biol , vol.165 , pp. 31-40
    • Cougot, N.1    Babajko, S.2    Seraphin, B.3
  • 9
    • 35948951960 scopus 로고    scopus 로고
    • Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae
    • Decker CJ, Teixeira D, Parker R. 2007. Edc3p and a glutamine/asparagine- rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae. J Cell Biol 179: 437-449.
    • (2007) J Cell Biol , vol.179 , pp. 437-449
    • Decker, C.J.1    Teixeira, D.2    Parker, R.3
  • 10
    • 0141888419 scopus 로고    scopus 로고
    • A 3 exonuclease that specifically interacts with the 3 end of histone mRNA
    • Dominski Z, Yang X, Kaygun H, Marzluff WF. 2003. A 3 exonuclease that specifically interacts with the 3 end of histone mRNA. Mol Cell 12: 295-305.
    • (2003) Mol Cell , vol.12 , pp. 295-305
    • Dominski, Z.1    Yang, X.2    Kaygun, H.3    Marzluff, W.F.4
  • 12
    • 11144335418 scopus 로고    scopus 로고
    • Nuclear export of metazoan replication-dependent histone mRNAs is dependent onRNA length and is mediated by TAP
    • Erkmann JA, Sanchez R, Treichel N, Marzluff WF, Kutay U. 2005a. Nuclear export of metazoan replication-dependent histone mRNAs is dependent onRNA length and is mediated by TAP. RNA11: 45-58.
    • (2005) RNA11 , pp. 45-58
    • Erkmann, J.A.1    Sanchez, R.2    Treichel, N.3    Marzluff, W.F.4    Kutay, U.5
  • 13
    • 19644372547 scopus 로고    scopus 로고
    • Nuclear import of the stem-loop binding protein and localization during the cell cycle
    • Erkmann JA, Wagner EJ, Dong J, Zhang YP, Kutay U, Marzluff WF. 2005b. Nuclear import of the stem-loop binding protein and localization during the cell cycle. Mol Biol Cell 16: 2960-2971.
    • (2005) Mol Biol Cell , vol.16 , pp. 2960-2971
    • Erkmann, J.A.1    Wagner, E.J.2    Dong, J.3    Zhang, Y.P.4    Kutay, U.5    Marzluff, W.F.6
  • 14
    • 29144481702 scopus 로고    scopus 로고
    • Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping
    • Fenger-Gron M, Fillman C, Norrild B, Lykke-Andersen J. 2005. Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping. Mol Cell 20: 905-915.
    • (2005) Mol Cell , vol.20 , pp. 905-915
    • Fenger-Gron, M.1    Fillman, C.2    Norrild, B.3    Lykke-Andersen, J.4
  • 15
    • 78649949096 scopus 로고    scopus 로고
    • Upf1 ATPase-dependent mRNP disassembly is required for completion of nonsense-mediated mRNA decay
    • Franks TM, Singh G, Lykke-Andersen J. 2010. Upf1 ATPase-dependent mRNP disassembly is required for completion of nonsense-mediated mRNA decay. Cell 143: 938-950.
    • (2010) Cell , vol.143 , pp. 938-950
    • Franks, T.M.1    Singh, G.2    Lykke-Andersen, J.3
  • 16
    • 77950260836 scopus 로고    scopus 로고
    • Lsm1-7 complexes bind to specific sites in viral RNA genomes and regulate their translation and replication
    • Galao RP, Chari A, Alves-Rodrigues I, Lobao D, Mas A, Kambach C, Fischer U, Diez J. 2010. Lsm1-7 complexes bind to specific sites in viral RNA genomes and regulate their translation and replication. RNA 16: 817-827.
    • (2010) RNA , vol.16 , pp. 817-827
    • Galao, R.P.1    Chari, A.2    Alves-Rodrigues, I.3    Lobao, D.4    Mas, A.5    Kambach, C.6    Fischer, U.7    Diez, J.8
  • 17
    • 2942595765 scopus 로고    scopus 로고
    • Nonsense-mediated messenger RNA decay is initiated by endonucleolytic cleavage in Drosophila
    • Gatfield D, Izaurralde E. 2004. Nonsense-mediated messenger RNA decay is initiated by endonucleolytic cleavage in Drosophila. Nature 429: 575-578.
    • (2004) Nature , vol.429 , pp. 575-578
    • Gatfield, D.1    Izaurralde, E.2
  • 18
    • 0023666085 scopus 로고
    • Translation is required for regulation of histone mRNA degradation
    • Graves RA, Pandey NB, Chodchoy N, Marzluff WF. 1987. Translation is required for regulation of histone mRNA degradation. Cell 48: 615-626.
    • (1987) Cell , vol.48 , pp. 615-626
    • Graves, R.A.1    Pandey, N.B.2    Chodchoy, N.3    Marzluff, W.F.4
  • 19
    • 0020600551 scopus 로고
    • Regulation of human histone gene expression: Kinetics of accumulation and changes in the rate of synthesis and in the half-lives of individual histone mRNAs during the HeLa cell cycle
    • Heintz N, Sive HL, Roeder RG. 1983. Regulation of human histone gene expression: Kinetics of accumulation and changes in the rate of synthesis and in the half-lives of individual histone mRNAs during the HeLa cell cycle. Mol Cell Biol 3: 539-550.
    • (1983) Mol Cell Biol , vol.3 , pp. 539-550
    • Heintz, N.1    Sive, H.L.2    Roeder, R.G.3
  • 21
    • 57049126216 scopus 로고    scopus 로고
    • SMG6 is the catalytic endonuclease that cleaves mRNAs containing nonsense codons in metazoan
    • Huntzinger E, Kashima I, Fauser M, Sauliere J, Izaurralde E. 2008. SMG6 is the catalytic endonuclease that cleaves mRNAs containing nonsense codons in metazoan. RNA 14: 2609-2617.
    • (2008) RNA , vol.14 , pp. 2609-2617
    • Huntzinger, E.1    Kashima, I.2    Fauser, M.3    Sauliere, J.4    Izaurralde, E.5
  • 22
    • 33845957402 scopus 로고    scopus 로고
    • Untemplated oligoadenylation promotes degradation of RISC-cleaved transcripts
    • Ibrahim F, Rohr J, Jeong WJ, Hesson J, Cerutti H. 2006. Untemplated oligoadenylation promotes degradation of RISC-cleaved transcripts. Science 314: 1893.
    • (2006) Science , vol.314 , pp. 1893
    • Ibrahim, F.1    Rohr, J.2    Jeong, W.J.3    Hesson, J.4    Cerutti, H.5
  • 23
    • 26944503146 scopus 로고    scopus 로고
    • Regulated degradation of replicationdependent histone mRNAs requires both ATR and Upf1
    • Kaygun H, Marzluff WF. 2005a. Regulated degradation of replicationdependent histone mRNAs requires both ATR and Upf1. Nat Struct Mol Biol 12: 794-800.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 794-800
    • Kaygun, H.1    Marzluff, W.F.2
  • 24
    • 23344452109 scopus 로고    scopus 로고
    • Translation termination is involved in histone mRNA degradation when DNA replication is inhibited
    • Kaygun H, Marzluff WF. 2005b. Translation termination is involved in histone mRNA degradation when DNA replication is inhibited. Mol Cell Biol 25: 6879-6888.
    • (2005) Mol Cell Biol , vol.25 , pp. 6879-6888
    • Kaygun, H.1    Marzluff, W.F.2
  • 25
    • 69749116302 scopus 로고    scopus 로고
    • A new MIF4G domain-containing protein, CTIF, directs nuclear cap-binding protein CBP80/20-dependent translation
    • Kim KM, Cho H, Choi K, Kim J, Kim BW, Ko YG, Jang SK, Kim YK. 2009. A new MIF4G domain-containing protein, CTIF, directs nuclear cap-binding protein CBP80/20-dependent translation. Genes Dev 23: 2033-2045.
    • (2009) Genes Dev , vol.23 , pp. 2033-2045
    • Kim, K.M.1    Cho, H.2    Choi, K.3    Kim, J.4    Kim, B.W.5    Ko, Y.G.6    Jang, S.K.7    Kim, Y.K.8
  • 26
    • 33845407784 scopus 로고    scopus 로고
    • Reconstitution, activities, and structure of the eukaryotic RNA exosome
    • Liu Q, Greimann JC, Lima CD. 2006. Reconstitution, activities, and structure of the eukaryotic RNA exosome. Cell 127: 1223-1237.
    • (2006) Cell , vol.127 , pp. 1223-1237
    • Liu, Q.1    Greimann, J.C.2    Lima, C.D.3
  • 27
    • 84874742223 scopus 로고    scopus 로고
    • Crystal structure of an RNA-bound 11-subunit eukaryotic exosome complex
    • Makino DL, Baumgartner M, Conti E. 2013. Crystal structure of an RNA-bound 11-subunit eukaryotic exosome complex. Nature 495: 70-75.
    • (2013) Nature , vol.495 , pp. 70-75
    • Makino, D.L.1    Baumgartner, M.2    Conti, E.3
  • 28
    • 54149091257 scopus 로고    scopus 로고
    • Metabolism and regulation of canonical histone mRNAs: Life without a poly(A) tail
    • Marzluff WF, Wagner EJ, Duronio RJ. 2008. Metabolism and regulation of canonical histone mRNAs: Life without a poly(A) tail. Nat Rev Genet 9: 843-854.
    • (2008) Nat Rev Genet , vol.9 , pp. 843-854
    • Marzluff, W.F.1    Wagner, E.J.2    Duronio, R.J.3
  • 29
    • 0033517098 scopus 로고    scopus 로고
    • Characterization of Sm-like proteins in yeast and their association with U6 snRNA
    • Mayes AE, Verdone L, Legrain P, Beggs JD. 1999. Characterization of Sm-like proteins in yeast and their association with U6 snRNA. EMBO J 18: 4321-4331.
    • (1999) EMBO J , vol.18 , pp. 4321-4331
    • Mayes, A.E.1    Verdone, L.2    Legrain, P.3    Beggs, J.D.4
  • 30
    • 0023651444 scopus 로고
    • Oligoribonucleotide synthesis using T7 RNA polymerase and synthetic DNA templates
    • Milligan JF, Groebe DR, Witherell GW, Uhlenbeck OC. 1987. Oligoribonucleotide synthesis using T7 RNA polymerase and synthetic DNA templates. Nucleic Acids Res 15: 8783-8794.
    • (1987) Nucleic Acids Res , vol.15 , pp. 8783-8794
    • Milligan, J.F.1    Groebe, D.R.2    Witherell, G.W.3    Uhlenbeck, O.C.4
  • 31
    • 38149023239 scopus 로고    scopus 로고
    • Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5 to 3 and 3 to 5
    • Mullen TE, Marzluff WF. 2008. Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5 to 3 and 3 to 5. Genes Dev 22: 50-65.
    • (2008) Genes Dev , vol.22 , pp. 50-65
    • Mullen, T.E.1    Marzluff, W.F.2
  • 32
    • 34147223557 scopus 로고    scopus 로고
    • A+U-rich instability elements differentially activate 5-3 and 3-5 mRNA decay
    • Murray EL, Schoenberg DR. 2007. A+U-rich instability elements differentially activate 5-3 and 3-5 mRNA decay. Mol Cell Biol 27: 2791-2799.
    • (2007) Mol Cell Biol , vol.27 , pp. 2791-2799
    • Murray, E.L.1    Schoenberg, D.R.2
  • 33
    • 15444368560 scopus 로고    scopus 로고
    • Decay of mRNAs targeted by RISC requires XRN1, the Ski complex, and the exosome
    • Orban TI, Izaurralde E. 2005. Decay of mRNAs targeted by RISC requires XRN1, the Ski complex, and the exosome. RNA 11: 459-469.
    • (2005) RNA , vol.11 , pp. 459-469
    • Orban, T.I.1    Izaurralde, E.2
  • 34
    • 77956642517 scopus 로고    scopus 로고
    • Human Pat1b connects deadenylation with mRNA decapping and controls the assembly of processing bodies
    • Ozgur S, Chekulaeva M, Stoecklin G. 2010. Human Pat1b connects deadenylation with mRNA decapping and controls the assembly of processing bodies. Mol Cell Biol 30: 4308-4323.
    • (2010) Mol Cell Biol , vol.30 , pp. 4308-4323
    • Ozgur, S.1    Chekulaeva, M.2    Stoecklin, G.3
  • 35
    • 0023462745 scopus 로고
    • The stem-loop structure at the 3 end of histone mRNA is necessary and sufficient for regulation of histone mRNA stability
    • Pandey NB, Marzluff WF. 1987. The stem-loop structure at the 3 end of histone mRNA is necessary and sufficient for regulation of histone mRNA stability. Mol Cell Biol 7: 4557-4559.
    • (1987) Mol Cell Biol , vol.7 , pp. 4557-4559
    • Pandey, N.B.1    Marzluff, W.F.2
  • 36
    • 0025941413 scopus 로고
    • Different complexes are formed on the 3 end of histone mRNA in nuclear and polysomal extracts
    • Pandey NB, Sun J-H, Marzluff WF. 1991. Different complexes are formed on the 3 end of histone mRNA in nuclear and polysomal extracts. Nucleic Acids Res 19: 5653-5659.
    • (1991) Nucleic Acids Res , vol.19 , pp. 5653-5659
    • Pandey, N.B.1    Sun, J.-H.2    Marzluff, W.F.3
  • 37
    • 0035022015 scopus 로고    scopus 로고
    • Multiple functional interactions between components of the Lsm2-Lsm8 complex, U6 snRNA, and the yeast La protein
    • Pannone BK, Kim SD, Noe DA, Wolin SL. 2001. Multiple functional interactions between components of the Lsm2-Lsm8 complex, U6 snRNA, and the yeast La protein. Genetics 158: 187-196.
    • (2001) Genetics , vol.158 , pp. 187-196
    • Pannone, B.K.1    Kim, S.D.2    Noe, D.A.3    Wolin, S.L.4
  • 38
    • 33847417585 scopus 로고    scopus 로고
    • P bodies and the control of mRNA translation and degradation
    • Parker R, Sheth U. 2007. P bodies and the control of mRNA translation and degradation. Mol Cell 25: 635-646.
    • (2007) Mol Cell , vol.25 , pp. 635-646
    • Parker, R.1    Sheth, U.2
  • 39
    • 0742288008 scopus 로고    scopus 로고
    • The enzymes and control of eukaryotic mRNA turnover
    • Parker R, Song H. 2004. The enzymes and control of eukaryotic mRNA turnover. Nat Struct Mol Biol 11: 121-127.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 121-127
    • Parker, R.1    Song, H.2
  • 40
    • 0036786956 scopus 로고    scopus 로고
    • The stem-loop binding protein is required for efficient translation of histone mRNA in vivo and in vitro
    • Sanchez R, Marzluff WF. 2002. The stem-loop binding protein is required for efficient translation of histone mRNA in vivo and in vitro. Mol Cell Biol 22: 7093-7104.
    • (2002) Mol Cell Biol , vol.22 , pp. 7093-7104
    • Sanchez, R.1    Marzluff, W.F.2
  • 41
    • 0028321764 scopus 로고
    • The site of 3 end formation of histone messenger RNA is a fixed distance from the downstream element recognized by the U7 snRNP
    • Scharl EC, Steitz JA. 1994. The site of 3 end formation of histone messenger RNA is a fixed distance from the downstream element recognized by the U7 snRNP. EMBO J 13: 2432-2440.
    • (1994) EMBO J , vol.13 , pp. 2432-2440
    • Scharl, E.C.1    Steitz, J.A.2
  • 43
    • 19644400971 scopus 로고    scopus 로고
    • Uridine addition after microRNA-directed cleavage
    • Shen B, Goodman HM. 2004. Uridine addition after microRNA-directed cleavage. Science 306: 997.
    • (2004) Science , vol.306 , pp. 997
    • Shen, B.1    Goodman, H.M.2
  • 44
    • 3042870747 scopus 로고
    • Histone mRNA concentrations are regulated at the level of transcription and mRNA degradation
    • Sittman DB, Graves RA, Marzluff WF. 1983. Histone mRNA concentrations are regulated at the level of transcription and mRNA degradation. Proc Natl Acad Sci 80: 1849-1853.
    • (1983) Proc Natl Acad Sci , vol.80 , pp. 1849-1853
    • Sittman, D.B.1    Graves, R.A.2    Marzluff, W.F.3
  • 45
    • 36248947229 scopus 로고    scopus 로고
    • 3 Terminal oligo U-tract-mediated stimulation of decapping
    • Song MG, Kiledjian M. 2007. 3 Terminal oligo U-tract-mediated stimulation of decapping. RNA 13: 2356-2365.
    • (2007) RNA , vol.13 , pp. 2356-2365
    • Song, M.G.1    Kiledjian, M.2
  • 47
    • 60849102145 scopus 로고    scopus 로고
    • Knockdown of SLBPresults in nuclear retention of histonemRNA
    • Sullivan KD, Mullen TE, Marzluff WF, Wagner EJ. 2009. Knockdown of SLBPresults in nuclear retention of histonemRNA.RNA15: 459-472.
    • (2009) RNA , vol.15 , pp. 459-472
    • Sullivan, K.D.1    Mullen, T.E.2    Marzluff, W.F.3    Wagner, E.J.4
  • 48
    • 84872474666 scopus 로고    scopus 로고
    • Structure of histone mRNA stem-loop, human stem-loop binding protein, and 3hExo ternary complex
    • Tan D, Marzluff WF, Dominski Z, Tong L. 2013. Structure of histone mRNA stem-loop, human stem-loop binding protein, and 3hExo ternary complex. Science 339: 318-321.
    • (2013) Science , vol.339 , pp. 318-321
    • Tan, D.1    Marzluff, W.F.2    Dominski, Z.3    Tong, L.4
  • 49
    • 84884849501 scopus 로고    scopus 로고
    • Structural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteins
    • von Moeller H, Lerner R, Ricciardi A, Basquin C, Marzluff WF, Conti E. 2013. Structural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteins. Nucleic Acids Res 14: 7960-7971.
    • (2013) Nucleic Acids Res , vol.14 , pp. 7960-7971
    • Von Moeller, H.1    Lerner, R.2    Ricciardi, A.3    Basquin, C.4    Marzluff, W.F.5    Conti, E.6
  • 50
    • 0032931845 scopus 로고    scopus 로고
    • Two Xenopus proteins that bind the 3 end of histone mRNA: Implications for translational control of histone synthesis during oogenesis
    • Wang Z-F, Ingledue TC, Dominski Z, Sanchez R, Marzluff WF. 1999. Two Xenopus proteins that bind the 3 end of histone mRNA: Implications for translational control of histone synthesis during oogenesis. Mol Cell Biol 19: 835-845.
    • (1999) Mol Cell Biol , vol.19 , pp. 835-845
    • Wang, Z.-F.1    Ingledue, T.C.2    Dominski, Z.3    Sanchez, R.4    Marzluff, W.F.5
  • 51
    • 0028953185 scopus 로고
    • The sequence of the stem and flanking sequences at the 3 end of histone mRNA are critical determinants for the binding of the stem-loop binding protein
    • Williams AS, Marzluff WF. 1995. The sequence of the stem and flanking sequences at the 3 end of histone mRNA are critical determinants for the binding of the stem-loop binding protein. Nucleic Acids Res 23: 654-662.
    • (1995) Nucleic Acids Res , vol.23 , pp. 654-662
    • Williams, A.S.1    Marzluff, W.F.2
  • 52
    • 33750044572 scopus 로고    scopus 로고
    • Characterization of 3hExo, a 3 exonuclease specifically interacting with the 3 end of histone mRNA
    • Yang XC, Purdy M, Marzluff WF, Dominski Z. 2006. Characterization of 3hExo, a 3 exonuclease specifically interacting with the 3 end of histone mRNA. J Biol Chem 281: 30447-30454.
    • (2006) J Biol Chem , vol.281 , pp. 30447-30454
    • Yang, X.C.1    Purdy, M.2    Marzluff, W.F.3    Dominski, Z.4
  • 53
    • 57749186710 scopus 로고    scopus 로고
    • Reconstitution of recombinant human LSm complexes for biochemical, biophysical, and cell biological studies
    • Zaric BL, Kambach C. 2008. Reconstitution of recombinant human LSm complexes for biochemical, biophysical, and cell biological studies. Methods Enzymol 448: 57-74.
    • (2008) Methods Enzymol , vol.448 , pp. 57-74
    • Zaric, B.L.1    Kambach, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.