메뉴 건너뛰기




Volumn 426, Issue 1, 2014, Pages 43-50

Crystal structure of human poly(A) polymerase gamma reveals a conserved catalytic core for canonical poly(A) polymerases

Author keywords

3 end processing; mRNA processing; neo PAP; poly(A) polymerase gamma; polyadenylation

Indexed keywords

CALCIUM ION; CORDYCEPIN; CORDYCEPIN TRIPHOSPHATE; CYCLIN DEPENDENT KINASE; DEOXYADENOSINE TRIPHOSPHATE; DNA POLYMERASE; MESSENGER RNA; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; POLYNUCLEOTIDE ADENYLYLTRANSFERASE ALPHA; POLYNUCLEOTIDE ADENYLYLTRANSFERASE BETA; POLYNUCLEOTIDE ADENYLYLTRANSFERASE GAMMA; UNCLASSIFIED DRUG; VALINE; DIVALENT CATION; POLY(A) POLYMERASE GAMMA;

EID: 84890860107     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.09.025     Document Type: Article
Times cited : (20)

References (61)
  • 1
    • 42449084129 scopus 로고    scopus 로고
    • Protein factors in pre-mRNA 3′-end processing
    • C.R. Mandel, Y. Bai, and L. Tong Protein factors in pre-mRNA 3′-end processing Cell Mol Life Sci 65 2008 1099 1122
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1099-1122
    • Mandel, C.R.1    Bai, Y.2    Tong, L.3
  • 2
    • 84857743195 scopus 로고    scopus 로고
    • Structural biology of poly(A) site definition
    • Q. Yang, and S. Doublié Structural biology of poly(A) site definition Wiley Interdiscip Rev RNA 2 2011 732 747
    • (2011) Wiley Interdiscip Rev RNA , vol.2 , pp. 732-747
    • Yang, Q.1    Doublié, S.2
  • 3
    • 0037164730 scopus 로고    scopus 로고
    • Polyadenylation: A tail of two complexes
    • N. Proudfoot, and J. O'Sullivan Polyadenylation: a tail of two complexes Curr Biol 12 2002 R855 R857
    • (2002) Curr Biol , vol.12
    • Proudfoot, N.1    O'Sullivan, J.2
  • 4
    • 0033059981 scopus 로고    scopus 로고
    • Formation of mRNA 3′ ends in eukaryotes: Mechanism, regulation, and interrelationships with other steps in mRNA synthesis
    • J. Zhao, L. Hyman, and C. Moore Formation of mRNA 3′ ends in eukaryotes: mechanism, regulation, and interrelationships with other steps in mRNA synthesis Microbiol Mol Biol Rev 63 1999 405 445
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 405-445
    • Zhao, J.1    Hyman, L.2    Moore, C.3
  • 6
    • 60149110358 scopus 로고    scopus 로고
    • Pre-mRNA processing reaches back to transcription and ahead to translation
    • M.J. Moore, and N.J. Proudfoot Pre-mRNA processing reaches back to transcription and ahead to translation Cell 136 2009 688 700
    • (2009) Cell , vol.136 , pp. 688-700
    • Moore, M.J.1    Proudfoot, N.J.2
  • 7
    • 84879408529 scopus 로고    scopus 로고
    • Alternative cleavage and polyadenylation: Extent, regulation and function
    • R. Elkon, A.P. Ugalde, and R. Agami Alternative cleavage and polyadenylation: extent, regulation and function Nat Rev Genet 14 2013 496 506
    • (2013) Nat Rev Genet , vol.14 , pp. 496-506
    • Elkon, R.1    Ugalde, A.P.2    Agami, R.3
  • 8
    • 77953284100 scopus 로고    scopus 로고
    • Molecular mechanisms of eukaryotic pre-mRNA 3′ end processing regulation
    • S. Millevoi, and S. Vagner Molecular mechanisms of eukaryotic pre-mRNA 3′ end processing regulation Nucleic Acids Res 38 2010 2757 2774
    • (2010) Nucleic Acids Res , vol.38 , pp. 2757-2774
    • Millevoi, S.1    Vagner, S.2
  • 9
    • 79952459288 scopus 로고    scopus 로고
    • Crystal structure of a human cleavage factor CFI(m)25/CFI(m)68/RNA complex provides an insight into poly(A) site recognition and RNA looping
    • Q. Yang, M. Coseno, G.M. Gilmartin, and S. Doublié Crystal structure of a human cleavage factor CFI(m)25/CFI(m)68/RNA complex provides an insight into poly(A) site recognition and RNA looping Structure 19 2011 368 377
    • (2011) Structure , vol.19 , pp. 368-377
    • Yang, Q.1    Coseno, M.2    Gilmartin, G.M.3    Doublié, S.4
  • 10
    • 77953454014 scopus 로고    scopus 로고
    • Structural basis of UGUA recognition by the Nudix protein CFIm25 and implications for a regulatory role in mRNA 3′ processing
    • Q. Yang, G.M. Gilmartin, and S. Doublié Structural basis of UGUA recognition by the Nudix protein CFIm25 and implications for a regulatory role in mRNA 3′ processing Proc Natl Acad Sci USA 107 2010 10062 10067
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 10062-10067
    • Yang, Q.1    Gilmartin, G.M.2    Doublié, S.3
  • 11
    • 84859266588 scopus 로고    scopus 로고
    • The structure of human cleavage factor I(m) hints at functions beyond UGUA-specific RNA binding: A role in alternative polyadenylation and a potential link to 5′ capping and splicing
    • Q. Yang, G.M. Gilmartin, and S. Doublié The structure of human cleavage factor I(m) hints at functions beyond UGUA-specific RNA binding: a role in alternative polyadenylation and a potential link to 5′ capping and splicing RNA Biol 8 2011 748 753
    • (2011) RNA Biol , vol.8 , pp. 748-753
    • Yang, Q.1    Gilmartin, G.M.2    Doublié, S.3
  • 12
    • 84878151459 scopus 로고    scopus 로고
    • Alternative cleavage and polyadenylation: The long and short of it
    • B. Tian, and J.L. Manley Alternative cleavage and polyadenylation: the long and short of it Trends Biochem Sci 38 2013 312 320
    • (2013) Trends Biochem Sci , vol.38 , pp. 312-320
    • Tian, B.1    Manley, J.L.2
  • 13
    • 84855257053 scopus 로고    scopus 로고
    • Fungal Virulence and development is regulated by alternative pre-mRNA 3′ end processing in Magnaporthe oryzae
    • M. Franceschetti, E. Bueno, R.A. Wilson, S.L. Tucker, C. Gomez-Mena, and G. Calder et al. Fungal Virulence and development is regulated by alternative pre-mRNA 3′ end processing in Magnaporthe oryzae PLoS Pathog 7 2011 e1002441
    • (2011) PLoS Pathog , vol.7 , pp. 1002441
    • Franceschetti, M.1    Bueno, E.2    Wilson, R.A.3    Tucker, S.L.4    Gomez-Mena, C.5    Calder, G.6
  • 14
    • 0008146244 scopus 로고    scopus 로고
    • 3′-End processing of pre-mRNA in eukaryotes
    • E. Wahle, and U. Rüegsegger 3′-End processing of pre-mRNA in eukaryotes FEMS Microbiol Rev 23 1999 277 295
    • (1999) FEMS Microbiol Rev , vol.23 , pp. 277-295
    • Wahle, E.1    Rüegsegger, U.2
  • 15
    • 69249151288 scopus 로고    scopus 로고
    • Poly(A) tail length is controlled by the nuclear poly(A)-binding protein regulating the interaction between poly(A) polymerase and the cleavage and polyadenylation specificity factor
    • U. Kuhn, M. Gundel, A. Knoth, Y. Kerwitz, S. Rudel, and E. Wahle Poly(A) tail length is controlled by the nuclear poly(A)-binding protein regulating the interaction between poly(A) polymerase and the cleavage and polyadenylation specificity factor J Biol Chem 284 2009 22803 22814
    • (2009) J Biol Chem , vol.284 , pp. 22803-22814
    • Kuhn, U.1    Gundel, M.2    Knoth, A.3    Kerwitz, Y.4    Rudel, S.5    Wahle, E.6
  • 16
    • 7444272009 scopus 로고    scopus 로고
    • Messenger RNA turnover in eukaryotes: Pathways and enzymes
    • S. Meyer, C. Temme, and E. Wahle Messenger RNA turnover in eukaryotes: pathways and enzymes Crit Rev Biochem Mol Biol 39 2004 197 216
    • (2004) Crit Rev Biochem Mol Biol , vol.39 , pp. 197-216
    • Meyer, S.1    Temme, C.2    Wahle, E.3
  • 17
    • 2442482777 scopus 로고    scopus 로고
    • Structure and function of poly(A) binding proteins
    • U. Kuhn, and E. Wahle Structure and function of poly(A) binding proteins Biochim Biophys Acta 1678 2004 67 84
    • (2004) Biochim Biophys Acta , vol.1678 , pp. 67-84
    • Kuhn, U.1    Wahle, E.2
  • 18
    • 0025787944 scopus 로고
    • Cloning and expression of the essential gene for poly(A) polymerase from S. Cerevisiae
    • J. Lingner, J. Kellermann, and W. Keller Cloning and expression of the essential gene for poly(A) polymerase from S. cerevisiae Nature 354 1991 496 498
    • (1991) Nature , vol.354 , pp. 496-498
    • Lingner, J.1    Kellermann, J.2    Keller, W.3
  • 19
    • 0025871846 scopus 로고
    • Primary structure and expression of bovine poly(A) polymerase
    • T. Raabe, F.J. Bollum, and J.L. Manley Primary structure and expression of bovine poly(A) polymerase Nature 353 1991 229 234
    • (1991) Nature , vol.353 , pp. 229-234
    • Raabe, T.1    Bollum, F.J.2    Manley, J.L.3
  • 20
    • 0025987814 scopus 로고
    • Isolation and expression of cDNA clones encoding mammalian poly(A) polymerase
    • E. Wahle, G. Martin, E. Schiltz, and W. Keller Isolation and expression of cDNA clones encoding mammalian poly(A) polymerase EMBO J 10 1991 4251 4257
    • (1991) EMBO J , vol.10 , pp. 4251-4257
    • Wahle, E.1    Martin, G.2    Schiltz, E.3    Keller, W.4
  • 21
    • 46049095239 scopus 로고    scopus 로고
    • Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein
    • G. Meinke, C. Ezeokonkwo, P. Balbo, W. Stafford, C. Moore, and A. Bohm Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein Biochemistry 47 2008 6859 6869
    • (2008) Biochemistry , vol.47 , pp. 6859-6869
    • Meinke, G.1    Ezeokonkwo, C.2    Balbo, P.3    Stafford, W.4    Moore, C.5    Bohm, A.6
  • 22
    • 84879531881 scopus 로고    scopus 로고
    • The 25 kDa subunit of cleavage factor im is a RNA-binding protein that interacts with the poly(A) polymerase in Entamoeba histolytica
    • M. Pezet-Valdez, J. Fernandez-Retana, J.D. Ospina-Villa, M.E. Ramirez-Moreno, E. Orozco, and S. Charcas-Lopez et al. The 25 kDa subunit of cleavage factor Im is a RNA-binding protein that interacts with the poly(A) polymerase in Entamoeba histolytica PLoS One 8 2013 e67977
    • (2013) PLoS One , vol.8 , pp. 67977
    • Pezet-Valdez, M.1    Fernandez-Retana, J.2    Ospina-Villa, J.D.3    Ramirez-Moreno, M.E.4    Orozco, E.5    Charcas-Lopez, S.6
  • 23
    • 41549109256 scopus 로고    scopus 로고
    • Determinants of substrate specificity in RNA-dependent nucleotidyl transferases
    • G. Martin, S. Doublié, and W. Keller Determinants of substrate specificity in RNA-dependent nucleotidyl transferases Biochim Biophys Acta 1779 2008 206 216
    • (2008) Biochim Biophys Acta , vol.1779 , pp. 206-216
    • Martin, G.1    Doublié, S.2    Keller, W.3
  • 24
    • 3843067711 scopus 로고    scopus 로고
    • Biochemical and structural insights into substrate binding and catalytic mechanism of mammalian poly(A) polymerase
    • G. Martin, A. Moglich, W. Keller, and S. Doublié Biochemical and structural insights into substrate binding and catalytic mechanism of mammalian poly(A) polymerase J Mol Biol 341 2004 911 925
    • (2004) J Mol Biol , vol.341 , pp. 911-925
    • Martin, G.1    Moglich, A.2    Keller, W.3    Doublié, S.4
  • 25
    • 0034664049 scopus 로고    scopus 로고
    • Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP
    • G. Martin, W. Keller, and S. Doublié Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP EMBO J 19 2000 4193 4203
    • (2000) EMBO J , vol.19 , pp. 4193-4203
    • Martin, G.1    Keller, W.2    Doublié, S.3
  • 26
    • 0034714329 scopus 로고    scopus 로고
    • Structure of yeast poly(A) polymerase alone and in complex with 3′-dATP
    • J. Bard, A.M. Zhelkovsky, S. Helmling, T.N. Earnest, C.L. Moore, and A. Bohm Structure of yeast poly(A) polymerase alone and in complex with 3′-dATP Science 289 2000 1346 1349
    • (2000) Science , vol.289 , pp. 1346-1349
    • Bard, J.1    Zhelkovsky, A.M.2    Helmling, S.3    Earnest, T.N.4    Moore, C.L.5    Bohm, A.6
  • 27
    • 84880676352 scopus 로고    scopus 로고
    • Isolated pseudo-RNA-recognition motifs of SR proteins can regulate splicing using a noncanonical mode of RNA recognition
    • A. Clery, R. Sinha, O. Anczukow, A. Corrionero, A. Moursy, and G.M. Daubner et al. Isolated pseudo-RNA-recognition motifs of SR proteins can regulate splicing using a noncanonical mode of RNA recognition Proc Natl Acad Sci USA 110 2013 E2802 E2811
    • (2013) Proc Natl Acad Sci USA , vol.110
    • Clery, A.1    Sinha, R.2    Anczukow, O.3    Corrionero, A.4    Moursy, A.5    Daubner, G.M.6
  • 28
    • 34548382114 scopus 로고    scopus 로고
    • Mechanism of poly(A) polymerase: Structure of the enzyme-MgATP-RNA ternary complex and kinetic analysis
    • P.B. Balbo, and A. Bohm Mechanism of poly(A) polymerase: structure of the enzyme-MgATP-RNA ternary complex and kinetic analysis Structure 15 2007 1117 1131
    • (2007) Structure , vol.15 , pp. 1117-1131
    • Balbo, P.B.1    Bohm, A.2
  • 29
    • 0034731317 scopus 로고    scopus 로고
    • An intronless gene encoding a poly(A) polymerase is specifically expressed in testis
    • Y.J. Lee, Y. Lee, and J.H. Chung An intronless gene encoding a poly(A) polymerase is specifically expressed in testis FEBS Lett 487 2000 287 292
    • (2000) FEBS Lett , vol.487 , pp. 287-292
    • Lee, Y.J.1    Lee, Y.2    Chung, J.H.3
  • 30
    • 0029857320 scopus 로고    scopus 로고
    • Cell-cycle related regulation of poly(A) polymerase by phosphorylation
    • D.F. Colgan, K.G. Murthy, C. Prives, and J.L. Manley Cell-cycle related regulation of poly(A) polymerase by phosphorylation Nature 384 1996 282 285
    • (1996) Nature , vol.384 , pp. 282-285
    • Colgan, D.F.1    Murthy, K.G.2    Prives, C.3    Manley, J.L.4
  • 31
    • 0035865250 scopus 로고    scopus 로고
    • Expressing the human genome
    • R. Tupler, G. Perini, and M.R. Green Expressing the human genome Nature 409 2001 832 833
    • (2001) Nature , vol.409 , pp. 832-833
    • Tupler, R.1    Perini, G.2    Green, M.R.3
  • 32
    • 0034935020 scopus 로고    scopus 로고
    • Identification and functional characterization of neo-poly(A) polymerase, an RNA processing enzyme overexpressed in human tumors
    • S.L. Topalian, S. Kaneko, M.I. Gonzales, G.L. Bond, Y. Ward, and J.L. Manley Identification and functional characterization of neo-poly(A) polymerase, an RNA processing enzyme overexpressed in human tumors Mol Cell Biol 21 2001 5614 5623
    • (2001) Mol Cell Biol , vol.21 , pp. 5614-5623
    • Topalian, S.L.1    Kaneko, S.2    Gonzales, M.I.3    Bond, G.L.4    Ward, Y.5    Manley, J.L.6
  • 33
    • 0035877792 scopus 로고    scopus 로고
    • Purification, characterization, and cloning of the cDNA of human signal recognition particle RNA 3′-adenylating enzyme
    • K. Perumal, K. Sinha, D. Henning, and R. Reddy Purification, characterization, and cloning of the cDNA of human signal recognition particle RNA 3′-adenylating enzyme J Biol Chem 276 2001 21791 21796
    • (2001) J Biol Chem , vol.276 , pp. 21791-21796
    • Perumal, K.1    Sinha, K.2    Henning, D.3    Reddy, R.4
  • 34
    • 0035823480 scopus 로고    scopus 로고
    • A novel nuclear human poly(A) polymerase (PAP), PAP gamma
    • C.B. Kyriakopoulou, H. Nordvarg, and A. Virtanen A novel nuclear human poly(A) polymerase (PAP), PAP gamma J Biol Chem 276 2001 33504 33511
    • (2001) J Biol Chem , vol.276 , pp. 33504-33511
    • Kyriakopoulou, C.B.1    Nordvarg, H.2    Virtanen, A.3
  • 35
    • 0037011168 scopus 로고    scopus 로고
    • Control of poly(A) polymerase level is essential to cytoplasmic polyadenylation and early development in Drosophila
    • F. Juge, S. Zaessinger, C. Temme, E. Wahle, and M. Simonelig Control of poly(A) polymerase level is essential to cytoplasmic polyadenylation and early development in Drosophila EMBO J 21 2002 6603 6613
    • (2002) EMBO J , vol.21 , pp. 6603-6613
    • Juge, F.1    Zaessinger, S.2    Temme, C.3    Wahle, E.4    Simonelig, M.5
  • 36
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • C. Notredame, D.G. Higgins, and J. Heringa T-Coffee: a novel method for fast and accurate multiple sequence alignment J Mol Biol 302 2000 205 217
    • (2000) J Mol Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 37
    • 84859900820 scopus 로고    scopus 로고
    • Novel interactions at the essential N-terminus of poly(A) polymerase that could regulate poly(A) addition in Saccharomyces cerevisiae
    • C. Ezeokonkwo, M.A. Ghazy, A. Zhelkovsky, P.C. Yeh, and C. Moore Novel interactions at the essential N-terminus of poly(A) polymerase that could regulate poly(A) addition in Saccharomyces cerevisiae FEBS Lett 586 2012 1173 1178
    • (2012) FEBS Lett , vol.586 , pp. 1173-1178
    • Ezeokonkwo, C.1    Ghazy, M.A.2    Zhelkovsky, A.3    Yeh, P.C.4    Moore, C.5
  • 38
    • 79960102692 scopus 로고    scopus 로고
    • Integration of the genetic map and genome assembly of fugu facilitates insights into distinct features of genome evolution in teleosts and mammals
    • W. Kai, K. Kikuchi, S. Tohari, A.K. Chew, A. Tay, and A. Fujiwara et al. Integration of the genetic map and genome assembly of fugu facilitates insights into distinct features of genome evolution in teleosts and mammals Genome Biol Evol 3 2011 424 442
    • (2011) Genome Biol Evol , vol.3 , pp. 424-442
    • Kai, W.1    Kikuchi, K.2    Tohari, S.3    Chew, A.K.4    Tay, A.5    Fujiwara, A.6
  • 39
    • 33846781442 scopus 로고    scopus 로고
    • X-ray crystallographic and steady state fluorescence characterization of the protein dynamics of yeast polyadenylate polymerase
    • P.B. Balbo, J. Toth, and A. Bohm X-ray crystallographic and steady state fluorescence characterization of the protein dynamics of yeast polyadenylate polymerase J Mol Biol 366 2007 1401 1415
    • (2007) J Mol Biol , vol.366 , pp. 1401-1415
    • Balbo, P.B.1    Toth, J.2    Bohm, A.3
  • 40
    • 20744437001 scopus 로고    scopus 로고
    • RONN: The bio-basis function neural network technique applied to the detection of natively disordered regions in proteins
    • Z.R. Yang, R. Thomson, P. McNeil, and R.M. Esnouf RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins Bioinformatics 21 2005 3369 3376
    • (2005) Bioinformatics , vol.21 , pp. 3369-3376
    • Yang, Z.R.1    Thomson, R.2    McNeil, P.3    Esnouf, R.M.4
  • 42
    • 0033581011 scopus 로고    scopus 로고
    • DNA polymerases: Structural diversity and common mechanisms
    • T.A. Steitz DNA polymerases: structural diversity and common mechanisms J Biol Chem 274 1999 17395 17398
    • (1999) J Biol Chem , vol.274 , pp. 17395-17398
    • Steitz, T.A.1
  • 43
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • [Suppl.]
    • H. Ashkenazy, E. Erez, E. Martz, T. Pupko, and N. Ben-Tal ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids Nucleic Acids Res 38 2010 W529 W533 [Suppl.]
    • (2010) Nucleic Acids Res , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 45
    • 39449085013 scopus 로고    scopus 로고
    • ERK is a novel regulatory kinase for poly(A) polymerase
    • S.H. Lee, H.S. Choi, H. Kim, and Y. Lee ERK is a novel regulatory kinase for poly(A) polymerase Nucleic Acids Res 36 2008 803 813
    • (2008) Nucleic Acids Res , vol.36 , pp. 803-813
    • Lee, S.H.1    Choi, H.S.2    Kim, H.3    Lee, Y.4
  • 46
    • 33947514003 scopus 로고    scopus 로고
    • Multiple histone deacetylases and the CREB-binding protein regulate pre-mRNA 3′-end processing
    • T. Shimazu, S. Horinouchi, and M. Yoshida Multiple histone deacetylases and the CREB-binding protein regulate pre-mRNA 3′-end processing J Biol Chem 282 2007 4470 4478
    • (2007) J Biol Chem , vol.282 , pp. 4470-4478
    • Shimazu, T.1    Horinouchi, S.2    Yoshida, M.3
  • 47
    • 19644361850 scopus 로고    scopus 로고
    • Kinetic studies of yeast polyA polymerase indicate an induced fit mechanism for nucleotide specificity
    • P.B. Balbo, G. Meinke, and A. Bohm Kinetic studies of yeast polyA polymerase indicate an induced fit mechanism for nucleotide specificity Biochemistry 44 2005 7777 7786
    • (2005) Biochemistry , vol.44 , pp. 7777-7786
    • Balbo, P.B.1    Meinke, G.2    Bohm, A.3
  • 49
    • 0032425080 scopus 로고    scopus 로고
    • The mechanism of action of T7 DNA polymerase
    • S. Doublié, and T. Ellenberger The mechanism of action of T7 DNA polymerase Curr Opin Struct Biol 8 1998 704 712
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 704-712
    • Doublié, S.1    Ellenberger, T.2
  • 53
    • 0030464460 scopus 로고    scopus 로고
    • SEAVIEW and PHYLO-WIN: Two graphic tools for sequence alignment and molecular phylogeny
    • N. Galtier, M. Gouy, and C. Gautier SEAVIEW and PHYLO-WIN: two graphic tools for sequence alignment and molecular phylogeny Comput Appl Biosci 12 1996 543 548
    • (1996) Comput Appl Biosci , vol.12 , pp. 543-548
    • Galtier, N.1    Gouy, M.2    Gautier, C.3
  • 54
    • 0034849408 scopus 로고    scopus 로고
    • MRBAYES: Bayesian inference of phylogenetic trees
    • J.P. Huelsenbeck, and F. Ronquist MRBAYES: Bayesian inference of phylogenetic trees Bioinformatics 17 2001 754 755
    • (2001) Bioinformatics , vol.17 , pp. 754-755
    • Huelsenbeck, J.P.1    Ronquist, F.2
  • 56
    • 0029962371 scopus 로고    scopus 로고
    • Mutational analysis of mammalian poly(A) polymerase identifies a region for primer binding and catalytic domain, homologous to the family X polymerases, and to other nucleotidyltransferases
    • G. Martin, and W. Keller Mutational analysis of mammalian poly(A) polymerase identifies a region for primer binding and catalytic domain, homologous to the family X polymerases, and to other nucleotidyltransferases EMBO J 15 1996 2593 2603
    • (1996) EMBO J , vol.15 , pp. 2593-2603
    • Martin, G.1    Keller, W.2
  • 57
    • 79951468769 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray diffraction of a disulfide cross-linked complex between bovine poly(A) polymerase and a chemically modified 15-mer oligo(A) RNA
    • Q. Yang, F. Faucher, M. Coseno, J. Heckman, and S. Doublié Purification, crystallization and preliminary X-ray diffraction of a disulfide cross-linked complex between bovine poly(A) polymerase and a chemically modified 15-mer oligo(A) RNA Acta Crystallogr Sect F Struct Biol Cryst Commun 67 2011 241 244
    • (2011) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.67 , pp. 241-244
    • Yang, Q.1    Faucher, F.2    Coseno, M.3    Heckman, J.4    Doublié, S.5
  • 58
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Academic Press New York
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Macromolecular Crystallography, Part A 276 1997 Academic Press New York 307 326
    • (1997) Macromolecular Crystallography, Part A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 59
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • A. Vagin, and A. Teplyakov MOLREP: an automated program for molecular replacement J Appl Crystallogr 30 1997 1022 1025
    • (1997) J Appl Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.