메뉴 건너뛰기




Volumn 22, Issue 15, 2003, Pages 3919-3929

Group II intron splicing factors derived by diversification of an ancient RNA-binding domain

Author keywords

Chloroplast; CRM domain; Group II intron; UPF 0044

Indexed keywords

PROTEIN; PROTEIN CAF1; PROTEIN CAF2; PROTEIN CRS2; RIBONUCLEOPROTEIN; RNA; UNCLASSIFIED DRUG;

EID: 0042525906     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg372     Document Type: Article
Times cited : (131)

References (51)
  • 1
    • 0024639674 scopus 로고
    • Tissue-dependent plastid RNA splicing in maize
    • Barkan, A. (1989) Tissue-dependent plastid RNA splicing in maize. Plant Cell, 1, 437-445.
    • (1989) Plant Cell , vol.1 , pp. 437-445
    • Barkan, A.1
  • 2
    • 0026353505 scopus 로고
    • Inactivation of maize transposon Mu suppresses a mutant phenotype by activating an outward-reading promoter near the end of Mu1
    • Barkan, A. and Martienssen, R.A. (1991) Inactivation of maize transposon Mu suppresses a mutant phenotype by activating an outward-reading promoter near the end of Mu1. Proc. Natl Acad. Sci. USA, 88, 3502-3506.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3502-3506
    • Barkan, A.1    Martienssen, R.A.2
  • 3
    • 0037039310 scopus 로고    scopus 로고
    • Recruitment of intron-encoded and co-opted proteins in splicing of the bI3 group I intron RNA
    • Bassi, G.S., de Oliviera, D.M., White, M.F. and Weeks, K.M. (2002) Recruitment of intron-encoded and co-opted proteins in splicing of the bI3 group I intron RNA. Proc. Natl Acad. Sci. USA, 99, 128-133.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 128-133
    • Bassi, G.S.1    De Oliviera, D.M.2    White, M.F.3    Weeks, K.M.4
  • 4
    • 0035368207 scopus 로고    scopus 로고
    • The ins and outs of group II introns
    • Bonen, L. and Vogel, J. (2001) The ins and outs of group II introns. Trends Genet., 17, 322-331.
    • (2001) Trends Genet. , vol.17 , pp. 322-331
    • Bonen, L.1    Vogel, J.2
  • 5
    • 0034013204 scopus 로고    scopus 로고
    • Defective splicing of the first nad4 intron is associated with lack of several complex I subunits in the Nicotinia sylvestris NMS1 nuclear mutant
    • Brangeon, J. et al. (2000) Defective splicing of the first nad4 intron is associated with lack of several complex I subunits in the Nicotinia sylvestris NMS1 nuclear mutant. Plant J., 21, 269-280.
    • (2000) Plant J. , vol.21 , pp. 269-280
    • Brangeon, J.1
  • 6
    • 0022552726 scopus 로고
    • The generality of self-splicing RNA: Relationship to nuclear mRNA splicing
    • Cech, T.R. (1986) The generality of self-splicing RNA: relationship to nuclear mRNA splicing. Cell, 44, 207-210.
    • (1986) Cell , vol.44 , pp. 207-210
    • Cech, T.R.1
  • 7
    • 0033169013 scopus 로고    scopus 로고
    • Assaying RNA chaperone activity in vivo using a novel RNA folding trap
    • Clodi, E., Semrad, K. and Schroeder, R. (1999) Assaying RNA chaperone activity in vivo using a novel RNA folding trap. EMBO J., 18, 3776-3782.
    • (1999) EMBO J. , vol.18 , pp. 3776-3782
    • Clodi, E.1    Semrad, K.2    Schroeder, R.3
  • 8
    • 0028276865 scopus 로고
    • Eschericia coli proteins, including ribosomal protein S12, facilitate in vitro splicing of phage T4 introns by acting as RNA chaperones
    • Coetzee, T., Herschlag, D. and Belfort, M. (1994) Eschericia coli proteins, including ribosomal protein S12, facilitate in vitro splicing of phage T4 introns by acting as RNA chaperones. Genes Dev., 8, 1575-1588.
    • (1994) Genes Dev. , vol.8 , pp. 1575-1588
    • Coetzee, T.1    Herschlag, D.2    Belfort, M.3
  • 9
    • 0033792637 scopus 로고    scopus 로고
    • The question remains: Is the spliceosome a ribozyme
    • Collins, C.A. and Guthrie, C. (2000) The question remains: is the spliceosome a ribozyme. Nat. Struct. Biol., 7, 850-854.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 850-854
    • Collins, C.A.1    Guthrie, C.2
  • 10
    • 0036493198 scopus 로고    scopus 로고
    • Compilation and analysis of group II intron insertions in bacterial genomes: Evidence for retroelement behavior
    • Dai, L. and Zimmerly, S. (2002) Compilation and analysis of group II intron insertions in bacterial genomes: evidence for retroelement behavior. Nucleic Acids Res., 30, 1091-1102.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1091-1102
    • Dai, L.1    Zimmerly, S.2
  • 11
    • 0037278926 scopus 로고    scopus 로고
    • ORF-less and reverse-transcriptase-encoding group II introns in achaebacteria, with a pattern of homing into related group II intron ORFs
    • Dai, L. and Zimmerly, S. (2003) ORF-less and reverse-transcriptase-encoding group II introns in achaebacteria, with a pattern of homing into related group II intron ORFs. RNA, 9, 14-19.
    • (2003) RNA , vol.9 , pp. 14-19
    • Dai, L.1    Zimmerly, S.2
  • 12
    • 0033552870 scopus 로고    scopus 로고
    • Mobile introns: Retrohoming by complete reverse splicing
    • Eickbush, T.H. (1999) Mobile introns: retrohoming by complete reverse splicing. Curr. Biol., 9, R11-R14.
    • (1999) Curr. Biol. , vol.9
    • Eickbush, T.H.1
  • 13
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson, O., Nielsen, H., Brunak, S. and von Heijne, G. (2000) Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J. Mol. Biol., 300, 1005-1016.
    • (2000) J. Mol. Biol. , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 14
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S. and Song, O. (1989) A novel genetic system to detect protein-protein interactions. Nature, 340, 245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 16
    • 0034810056 scopus 로고    scopus 로고
    • Metal ion coordination by the AGC triad in domain 5 contributes to group II intron catalysis
    • Gordon, P.M. and Piccirilli, J. (2001) Metal ion coordination by the AGC triad in domain 5 contributes to group II intron catalysis. Nat. Struct. Biol., 8, 893-898.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 893-898
    • Gordon, P.M.1    Piccirilli, J.2
  • 17
    • 0033965261 scopus 로고    scopus 로고
    • Metal ion catalysis during the exon-ligation step of nuclear pre-mRNA splicing: Extending the parallels between the spliceosome and group II introns
    • Gordon, P.M., Sontheimer, E.J. and Piccirilli, J.A. (2000) Metal ion catalysis during the exon-ligation step of nuclear pre-mRNA splicing: extending the parallels between the spliceosome and group II introns. RNA, 6, 199-205.
    • (2000) RNA , vol.6 , pp. 199-205
    • Gordon, P.M.1    Sontheimer, E.J.2    Piccirilli, J.A.3
  • 18
    • 0026656909 scopus 로고
    • A tyrosyl-tRNA synthetase binds specifically to the group I intron catalytic core
    • Guo, Q. and Lambowitz, A.M. (1992) A tyrosyl-tRNA synthetase binds specifically to the group I intron catalytic core. Genes Dev., 6, 1357-1372.
    • (1992) Genes Dev. , vol.6 , pp. 1357-1372
    • Guo, Q.1    Lambowitz, A.M.2
  • 19
    • 0029163563 scopus 로고
    • RNA chaperones and the RNA folding problem
    • Herschlag, D. (1995) RNA chaperones and the RNA folding problem. J. Biol. Chem., 270, 20871-20874.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20871-20874
    • Herschlag, D.1
  • 20
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Higgins, D., Thompson, J., Gibson, T., Thompson, J.D., Higgins, D.G. and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Higgins, D.1    Thompson, J.2    Gibson, T.3    Thompson, J.D.4    Higgins, D.G.5    Gibson, T.J.6
  • 21
    • 0033536621 scopus 로고    scopus 로고
    • The maturase encoded by a group I intron from Aspergillus nidulans stabilizes RNA tertiary structure and promotes rapid splicing
    • Ho, Y. and Waring, R. (1999) The maturase encoded by a group I intron from Aspergillus nidulans stabilizes RNA tertiary structure and promotes rapid splicing. J. Mol. Biol., 292, 987-1001.
    • (1999) J. Mol. Biol. , vol.292 , pp. 987-1001
    • Ho, Y.1    Waring, R.2
  • 22
    • 0035865141 scopus 로고    scopus 로고
    • Recruitment of a peptidyl-tRNA hydrolase as a facilitator of group II intron splicing in chloroplasts
    • Jenkins, B.D. and Barkan, A. (2001) Recruitment of a peptidyl-tRNA hydrolase as a facilitator of group II intron splicing in chloroplasts. EMBO J., 20, 872-879.
    • (2001) EMBO J. , vol.20 , pp. 872-879
    • Jenkins, B.D.1    Barkan, A.2
  • 23
    • 0031106356 scopus 로고    scopus 로고
    • Nuclear mutations that block group II RNA splicing in maize chloroplasts reveal several intron classes with distinct requirements for splicing factors
    • Jenkins, B.D., Kulhanek, D.J. and Barkan, A. (1997) Nuclear mutations that block group II RNA splicing in maize chloroplasts reveal several intron classes with distinct requirements for splicing factors. Plant Cell, 9, 283-296.
    • (1997) Plant Cell , vol.9 , pp. 283-296
    • Jenkins, B.D.1    Kulhanek, D.J.2    Barkan, A.3
  • 24
    • 0002671710 scopus 로고    scopus 로고
    • Group I and group II ribozymes as RNPs: Clues to the past and guides to the future
    • Gesteland, R.F., Cech, T.R. and Atkins, J.F. (eds). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Lambowitz, A.M., Caprara, M.G., Zimmerly, S. and Perlman, P.S. (1999) Group I and group II ribozymes as RNPs: clues to the past and guides to the future. In Gesteland, R.F., Cech, T.R. and Atkins, J.F. (eds), The RNA World. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 451-485.
    • (1999) The RNA World , pp. 451-485
    • Lambowitz, A.M.1    Caprara, M.G.2    Zimmerly, S.3    Perlman, P.S.4
  • 25
    • 9844256088 scopus 로고    scopus 로고
    • A bacterial group II intron encoding reverse transcriptase, maturase and DNA endonuclease activities: Biochemical demonstration of maturase activity and insertion of new genetic information within the intron
    • Matsuura, M. et al. (1997) A bacterial group II intron encoding reverse transcriptase, maturase and DNA endonuclease activities: biochemical demonstration of maturase activity and insertion of new genetic information within the intron. Genes Dev., 11, 2910-2924.
    • (1997) Genes Dev. , vol.11 , pp. 2910-2924
    • Matsuura, M.1
  • 26
    • 0017115214 scopus 로고
    • Peptidyl-transfer RNA dissociates during protein synthesis from ribosomes of Eschericia coli
    • Menninger, J. (1976) Peptidyl-transfer RNA dissociates during protein synthesis from ribosomes of Eschericia coli. J. Biol. Chem., 251, 3392-3398.
    • (1976) J. Biol. Chem. , vol.251 , pp. 3392-3398
    • Menninger, J.1
  • 27
    • 0029066770 scopus 로고
    • Structure and actvities of group II introns
    • Michel, F. and Ferat, J.-L. (1995) Structure and actvities of group II introns. Annu. Rev. Biochem., 64, 435-461.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 435-461
    • Michel, F.1    Ferat, J.-L.2
  • 28
    • 0024428420 scopus 로고
    • Comparative and functional anatomy of group II catalytic introns - A review
    • Michel, F., Umesono, K. and Ozeki, H. (1989) Comparative and functional anatomy of group II catalytic introns - a review. Gene, 82, 5-30.
    • (1989) Gene , vol.82 , pp. 5-30
    • Michel, F.1    Umesono, K.2    Ozeki, H.3
  • 29
    • 0037077127 scopus 로고    scopus 로고
    • A DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing
    • Mohr, S., Stryker, J.M. and Lambowitz, A.M. (2002) A DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing. Cell, 109, 769-779.
    • (2002) Cell , vol.109 , pp. 769-779
    • Mohr, S.1    Stryker, J.M.2    Lambowitz, A.M.3
  • 30
    • 0002340095 scopus 로고    scopus 로고
    • RNA-RNA interactions in nuclear pre-mRNA splicing
    • Simons, R.W. and Grunberg-Manago, M. (eds). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Nilsen, T.W. (1998) RNA-RNA interactions in nuclear pre-mRNA splicing. In Simons, R.W. and Grunberg-Manago, M. (eds), RNA Structure and Function. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 279-307.
    • (1998) RNA Structure and Function , pp. 279-307
    • Nilsen, T.W.1
  • 31
    • 1842832249 scopus 로고    scopus 로고
    • Crystal structure of E.coli YhbY: A representative of a novel class of RNA binding proteins
    • Ostheimer, G.J., Barkan, A. and Matthews, B.W. (2002) Crystal structure of E.coli YhbY: a representative of a novel class of RNA binding proteins. Structure, 10, 1593-1601.
    • (2002) Structure , vol.10 , pp. 1593-1601
    • Ostheimer, G.J.1    Barkan, A.2    Matthews, B.W.3
  • 32
    • 0033571587 scopus 로고    scopus 로고
    • A factor related to pseudouridine synthases is required for chloroplast group II intron trans-splicing in Chlamydomonas reinhardtii
    • Perron, K., Goldschmidt-Clermont, M. and Rochaix, J.-D. (1999) A factor related to pseudouridine synthases is required for chloroplast group II intron trans-splicing in Chlamydomonas reinhardtii. EMBO J., 18, 6481-6490.
    • (1999) EMBO J. , vol.18 , pp. 6481-6490
    • Perron, K.1    Goldschmidt-Clermont, M.2    Rochaix, J.-D.3
  • 33
    • 0032103821 scopus 로고    scopus 로고
    • The architectural organization and mechanistic functions of group II intron structural elements
    • Qin, P.Z. and Pyle, A.M. (1998) The architectural organization and mechanistic functions of group II intron structural elements. Curr. Opin. Struct. Biol., 8, 301-308.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 301-308
    • Qin, P.Z.1    Pyle, A.M.2
  • 34
    • 0035794689 scopus 로고    scopus 로고
    • Identification of an RNA-protein complex involved in chloroplast group II intron trans-splicing in Chlamydomonas reinhardtii
    • Rivier, C., Goldschmidt-Clermont, M. and Rochaix, J.-D. (2001) Identification of an RNA-protein complex involved in chloroplast group II intron trans-splicing in Chlamydomonas reinhardtii. EMBO J., 20, 1765-1773.
    • (2001) EMBO J. , vol.20 , pp. 1765-1773
    • Rivier, C.1    Goldschmidt-Clermont, M.2    Rochaix, J.-D.3
  • 35
    • 0030738859 scopus 로고    scopus 로고
    • Crystal structure at 1.2 Å resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase
    • Schmitt, E., Mechulam, Y., Fromant, M., Plateau, P. and Blanquet, S. (1997) Crystal structure at 1.2 Å resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase. EMBO J., 16, 4760-4769.
    • (1997) EMBO J. , vol.16 , pp. 4760-4769
    • Schmitt, E.1    Mechulam, Y.2    Fromant, M.3    Plateau, P.4    Blanquet, S.5
  • 36
    • 0024961642 scopus 로고
    • Mitochondrial splicing requires a protein from a novel helicase family
    • Seraphin, B., Simon, M., Boulet, A. and Faye, G. (1989) Mitochondrial splicing requires a protein from a novel helicase family. Nature, 337, 84-87.
    • (1989) Nature , vol.337 , pp. 84-87
    • Seraphin, B.1    Simon, M.2    Boulet, A.3    Faye, G.4
  • 37
    • 0026261876 scopus 로고
    • Five easy pieces
    • Sharp, P.A. (1991) 'Five easy pieces'. Science, 254, 663.
    • (1991) Science , vol.254 , pp. 663
    • Sharp, P.A.1
  • 38
    • 0036233276 scopus 로고    scopus 로고
    • A novel mechanism for protein-assisted group I intron splicing
    • Solem, A., Chatterjee, P. and Caprara, M. (2002) A novel mechanism for protein-assisted group I intron splicing. RNA, 8, 412-425.
    • (2002) RNA , vol.8 , pp. 412-425
    • Solem, A.1    Chatterjee, P.2    Caprara, M.3
  • 39
    • 0030833215 scopus 로고    scopus 로고
    • Metal ion catalysis during splicing of premessenger RNA
    • Sontheimer, E.J., Sun, S. and Piccirilli, J. (1997) Metal ion catalysis during splicing of premessenger RNA. Nature, 388, 801-805.
    • (1997) Nature , vol.388 , pp. 801-805
    • Sontheimer, E.J.1    Sun, S.2    Piccirilli, J.3
  • 40
    • 0036304522 scopus 로고    scopus 로고
    • Productive folding to the native state by a group II intron ribozyme
    • Swisher, J.F., Su, L.J., Brenowitz, M., Anderson, V.E. and Pyle, A.M. (2002) Productive folding to the native state by a group II intron ribozyme. J. Mol. Biol., 315, 297-310.
    • (2002) J. Mol. Biol. , vol.315 , pp. 297-310
    • Swisher, J.F.1    Su, L.J.2    Brenowitz, M.3    Anderson, V.E.4    Pyle, A.M.5
  • 41
    • 0034844560 scopus 로고    scopus 로고
    • CRS1 is a novel group II intron splicing factor that was derived from a domain of ancient origin
    • Till, B., Schmitz-Linneweber, C., Williams-Carrier, R. and Barkan, A. (2001) CRS1 is a novel group II intron splicing factor that was derived from a domain of ancient origin. RNA, 7, 1227-1238.
    • (2001) RNA , vol.7 , pp. 1227-1238
    • Till, B.1    Schmitz-Linneweber, C.2    Williams-Carrier, R.3    Barkan, A.4
  • 42
    • 0034910710 scopus 로고    scopus 로고
    • Coevolution of group II intron RNA structures with their intron-encoded reverse transcriptases
    • Toor, N., Hausner, G. and Zimmerly, S. (2001) Coevolution of group II intron RNA structures with their intron-encoded reverse transcriptases. RNA, 7, 1142-1152.
    • (2001) RNA , vol.7 , pp. 1142-1152
    • Toor, N.1    Hausner, G.2    Zimmerly, S.3
  • 43
    • 0037343641 scopus 로고    scopus 로고
    • Bacteria and Archaea group II introns: Additional mobile genetic elements in the envronment
    • Toro, N. (2003) Bacteria and Archaea group II introns: additional mobile genetic elements in the envronment. Environ. Microbiol., 5, 143-151.
    • (2003) Environ. Microbiol. , vol.5 , pp. 143-151
    • Toro, N.1
  • 44
    • 0035909314 scopus 로고    scopus 로고
    • Splicing-related catalysis by protein-free snRNAs
    • Valadkhan, S. and Manley, J.L. (2001) Splicing-related catalysis by protein-free snRNAs. Nature, 413, 701-707.
    • (2001) Nature , vol.413 , pp. 701-707
    • Valadkhan, S.1    Manley, J.L.2
  • 45
    • 0037133955 scopus 로고    scopus 로고
    • 2+-dependent chemistry at the catalytic core?
    • 2+-dependent chemistry at the catalytic core? Cell, 109, 149-152.
    • (2002) Cell , vol.109 , pp. 149-152
    • Villa, T.1    Pleiss, J.A.2    Guthrie, C.3
  • 46
    • 0345062264 scopus 로고    scopus 로고
    • Comparative analysis of splicing of the complete set of chloroplast group II introns in three higher plants mutants
    • Vogel, J., Borner, T. and Hess, W. (1999) Comparative analysis of splicing of the complete set of chloroplast group II introns in three higher plants mutants. Nucleic Acids Rev., 27, 3866-3874.
    • (1999) Nucleic Acids Rev. , vol.27 , pp. 3866-3874
    • Vogel, J.1    Borner, T.2    Hess, W.3
  • 47
    • 0036712305 scopus 로고    scopus 로고
    • RNA chaperone StpA loosens interaction of the tertiary structure in the td group I intron in vivo
    • Waldsich, C., Grossberger, R. and Schroeder, R. (2002) RNA chaperone StpA loosens interaction of the tertiary structure in the td group I intron in vivo. Genes Dev., 16, 2300-2312.
    • (2002) Genes Dev. , vol.16 , pp. 2300-2312
    • Waldsich, C.1    Grossberger, R.2    Schroeder, R.3
  • 48
    • 0034604543 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the yeast resolving enzyme CceI reveals catalytic residues and relationship with the intron-splicing factor Mrs1
    • Wardleworth, B.J., Kvaratskhelia, M. and White, M.F. (2000) Site-directed mutagenesis of the yeast resolving enzyme CceI reveals catalytic residues and relationship with the intron-splicing factor Mrs1. J. Biol. Chem., 275, 23725-23728.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23725-23728
    • Wardleworth, B.J.1    Kvaratskhelia, M.2    White, M.F.3
  • 49
    • 0030916948 scopus 로고    scopus 로고
    • Protein-facilitated RNA folding
    • Weeks, K.M. (1997) Protein-facilitated RNA folding. Curr. Opin. Struct. Biol., 7, 336-342.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 336-342
    • Weeks, K.M.1
  • 50
    • 0029050588 scopus 로고
    • Efficient protein-facilitated splicing of the yeast mitochondrial bI5 intron
    • Weeks, K.M. and Cech, T.R. (1995) Efficient protein-facilitated splicing of the yeast mitochondrial bI5 intron. Biochemistry, 34, 7728-7738.
    • (1995) Biochemistry , vol.34 , pp. 7728-7738
    • Weeks, K.M.1    Cech, T.R.2
  • 51
    • 0037110588 scopus 로고    scopus 로고
    • Structure of HI1333 (YhbY), a putative RNA-binding protein from Haemophilus influenzae
    • Willis, M.A., Krajewski, W., Chalamasetty, V.R., Retty, P., A., H. and Herzberg, O. (2002) Structure of HI1333 (YhbY), a putative RNA-binding protein from Haemophilus influenzae. Proteins, 49, 423-426.
    • (2002) Proteins , vol.49 , pp. 423-426
    • Willis, M.A.1    Krajewski, W.2    Chalamasetty, V.R.3    Retty, P.A.H.4    Herzberg, O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.