메뉴 건너뛰기




Volumn 88, Issue 2, 1997, Pages 235-242

The solution structure of the S1 RNA binding domain: A member of an ancient nucleic acid-binding fold

Author keywords

[No Author keywords available]

Indexed keywords

RNA BINDING PROTEIN;

EID: 0031471204     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81844-9     Document Type: Article
Times cited : (360)

References (66)
  • 1
    • 0025796712 scopus 로고
    • The SWISS-PROT sequence data bank
    • Bairoch, A., and Boeckmann, B. (1991). The SWISS-PROT sequence data bank. Nucleic. Acids Res. 19, 2247-2250.
    • (1991) Nucleic. Acids Res. , vol.19 , pp. 2247-2250
    • Bairoch, A.1    Boeckmann, B.2
  • 2
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G.J. (1993). ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 3
    • 12044252858 scopus 로고
    • Methodological advances in protein NMR
    • Bax, A., and Grzesiek, S. (1993). Methodological advances in protein NMR. Accounts Chem. Res. 26, 131-138.
    • (1993) Accounts Chem. Res. , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek, S.2
  • 4
    • 0025815146 scopus 로고
    • Vaccinia virus encoded elF-2a homolog abrogates the antiviral effect of interferon
    • Beattie, E., Tartaglia, J., and Paolettit, E. (1991). Vaccinia virus encoded elF-2a homolog abrogates the antiviral effect of interferon. Virol. 183, 419-422.
    • (1991) Virol. , vol.183 , pp. 419-422
    • Beattie, E.1    Tartaglia, J.2    Paolettit, E.3
  • 5
    • 0028050261 scopus 로고
    • OWL - a non-redundant, composite protein sequence database
    • Bleasby, A.J., Akrigg, D., and Attwood, T.K. (1994). OWL - a non-redundant, composite protein sequence database. Nucleic Acids Res. 22, 3574-3577.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3574-3577
    • Bleasby, A.J.1    Akrigg, D.2    Attwood, T.K.3
  • 6
    • 0026062066 scopus 로고
    • Ribosome-messenger recognition - MRNA target sites for ribosomal protein S1
    • Boni, I.V., Isaeva, D.M., Musychenko, M.L., and Tzareva, N.V. (1991). Ribosome-messenger recognition - mRNA target sites for ribosomal protein S1. Nucleic Acids Res. 19, 155-162.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 155-162
    • Boni, I.V.1    Isaeva, D.M.2    Musychenko, M.L.3    Tzareva, N.V.4
  • 7
    • 0029890667 scopus 로고    scopus 로고
    • Evidence that Spt6p controls chromatin structure by a direct interaction with histones
    • Bortvin, A., and Winston, F. (1996). Evidence that Spt6p controls chromatin structure by a direct interaction with histones. Science 272, 1473-1476.
    • (1996) Science , vol.272 , pp. 1473-1476
    • Bortvin, A.1    Winston, F.2
  • 8
    • 0003769049 scopus 로고
    • New Haven, Connecticut: Department of Molecular Biophysics and Biochemistry, Yale University
    • Brunger, A.T. (1993). X-PLOR Manual, Version 3.1 (New Haven, Connecticut: Department of Molecular Biophysics and Biochemistry, Yale University).
    • (1993) X-PLOR Manual, Version 3.1
    • Brunger, A.T.1
  • 9
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNA-binding proteins
    • Burd, C.G., and Dreyfuss, G. (1994). Conserved structures and diversity of functions of RNA-binding proteins. Science 265, 615-621.
    • (1994) Science , vol.265 , pp. 615-621
    • Burd, C.G.1    Dreyfuss, G.2
  • 10
    • 0029041105 scopus 로고
    • NMR solution structure of a double-stranded RNA binding domain from Drosophila Staufen protein reveals homology to the N terminal domain of ribosomal protein S5
    • Bycroft, M., Grunert, S., Murzin, A.G., Proctor, M., and St. Johnston, D. (1995). NMR solution structure of a double-stranded RNA binding domain from Drosophila Staufen protein reveals homology to the N terminal domain of ribosomal protein S5. EMBO J. 14, 3563-3571.
    • (1995) EMBO J. , vol.14 , pp. 3563-3571
    • Bycroft, M.1    Grunert, S.2    Murzin, A.G.3    Proctor, M.4    St. Johnston, D.5
  • 11
    • 0028269435 scopus 로고
    • Copurification of Escherichia coli RNAse E and PNPase - Evidence for a specific association between 2 enzymes important in RNA processing and degradation
    • Carpousis, A.J., Vanhouwe, G., Ehretsmann, C., and Krisch, H.M. (1994). Copurification of Escherichia coli RNAse E and PNPase - evidence for a specific association between 2 enzymes important in RNA processing and degradation. Cell 76, 889-900.
    • (1994) Cell , vol.76 , pp. 889-900
    • Carpousis, A.J.1    Vanhouwe, G.2    Ehretsmann, C.3    Krisch, H.M.4
  • 12
    • 0027411514 scopus 로고
    • Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase
    • Cavarelli, J., Rees, B., Ruff, M., Thierry, J.C., and Moras, D. (1993). Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature 362, 181-184.
    • (1993) Nature , vol.362 , pp. 181-184
    • Cavarelli, J.1    Rees, B.2    Ruff, M.3    Thierry, J.C.4    Moras, D.5
  • 13
    • 0028433524 scopus 로고
    • Regulation of eukaryotic protein synthesis by protein kinases that phosphorylate initiation factor elF-2 Mol
    • Clemens, M.J. (1994). Regulation of eukaryotic protein synthesis by protein kinases that phosphorylate initiation factor elF-2 Mol. Biol. Rep. 19, 201-210.
    • (1994) Biol. Rep. , vol.19 , pp. 201-210
    • Clemens, M.J.1
  • 14
    • 0028923019 scopus 로고
    • Surprises at the 3′-end of prokaryotic RNA
    • Cohen, S.N. (1995). Surprises at the 3′-end of prokaryotic RNA. Cell 80, 829-832.
    • (1995) Cell , vol.80 , pp. 829-832
    • Cohen, S.N.1
  • 15
    • 0026088747 scopus 로고
    • Requirement of the RNA helicase like protein PRP22 for release of messenger RNA from spliceosomes
    • Company, M., Arenas, J., and Abelson, J. (1991). Requirement of the RNA helicase like protein PRP22 for release of messenger RNA from spliceosomes. Nature 349, 487-493.
    • (1991) Nature , vol.349 , pp. 487-493
    • Company, M.1    Arenas, J.2    Abelson, J.3
  • 16
    • 0027380985 scopus 로고
    • RNAse E activity is conferred by a single polypeptide: Overexpression, purification, and properties of the ams/rne/hmp1 gene product
    • Cormack, R.S., Genereaux, J.L., and Mackie, G.A. (1993). RNAse E activity is conferred by a single polypeptide: overexpression, purification, and properties of the ams/rne/hmp1 gene product. Proc. Natl. Acad. Sci. USA 90, 9006-9010.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9006-9010
    • Cormack, R.S.1    Genereaux, J.L.2    Mackie, G.A.3
  • 18
    • 0028901673 scopus 로고
    • Cloning of a cDNA encoding a human DNA-binding protein similar to ribosomal protein S1
    • Eklund, E.A., Lee, S.W., and Skalnik, D.G. (1995). Cloning of a cDNA encoding a human DNA-binding protein similar to ribosomal protein S1. Gene 155, 231-235.
    • (1995) Gene , vol.155 , pp. 231-235
    • Eklund, E.A.1    Lee, S.W.2    Skalnik, D.G.3
  • 19
    • 0029744175 scopus 로고    scopus 로고
    • A new gene locus of Bordetella pertussis defines a novel family of prokaryotic transcriptional accessory proteins
    • Fuchs, T.M., Deppisch, H., Scarlato, V., and Gross, R. (1996). A new gene locus of Bordetella pertussis defines a novel family of prokaryotic transcriptional accessory proteins. J. Bact. 178, 4445-4452.
    • (1996) J. Bact. , vol.178 , pp. 4445-4452
    • Fuchs, T.M.1    Deppisch, H.2    Scarlato, V.3    Gross, R.4
  • 20
    • 0027258576 scopus 로고
    • The KH domain occurs in a diverse set of RNA-binding proteins that include the antiterminator NusA and is probably involved in binding to nucleic acid
    • Gibson, T.J., Thompson, J.D., and Heringa, J. (1993).The KH domain occurs in a diverse set of RNA-binding proteins that include the antiterminator NusA and is probably involved in binding to nucleic acid. FEBS Lett. 324, 361-366.
    • (1993) FEBS Lett. , vol.324 , pp. 361-366
    • Gibson, T.J.1    Thompson, J.D.2    Heringa, J.3
  • 21
    • 0026730491 scopus 로고
    • Translational initiation factor IF1 and factor eIF2a share an RNA binding motif with prokaryotic ribosomal protein S1 and polynucleotide phosphorylase
    • Gribskov, M. (1992). Translational initiation factor IF1 and factor eIF2a share an RNA binding motif with prokaryotic ribosomal protein S1 and polynucleotide phosphorylase. Gene 119, 107-111.
    • (1992) Gene , vol.119 , pp. 107-111
    • Gribskov, M.1
  • 22
    • 0028874810 scopus 로고
    • Fold recognition and ab-initio structure predictions using hidden markov-models and beta-strand pair potentials
    • Hubbard, T.J., and Park, J. (1995). Fold recognition and ab-initio structure predictions using hidden markov-models and beta-strand pair potentials. Proteins 23, 398-402.
    • (1995) Proteins , vol.23 , pp. 398-402
    • Hubbard, T.J.1    Park, J.2
  • 23
    • 0030056206 scopus 로고    scopus 로고
    • Evidence for physical and functional association between EMB-5 and LIN-12 in Caenorhabditis elegans
    • Hubbard, E.J.A., Dong, Q., and Greenwald, I. (1996). Evidence for physical and functional association between EMB-5 and LIN-12 in Caenorhabditis elegans. Science 273, 112-115.
    • (1996) Science , vol.273 , pp. 112-115
    • Hubbard, E.J.A.1    Dong, Q.2    Greenwald, I.3
  • 24
    • 0025975458 scopus 로고
    • Genetic interaction between the β subunit of RNA polymerase and the arginine-rich domain of Escherichia coli NusA protein
    • Ito, K., Egawa, K. and Nakamura, Y. (1991). Genetic interaction between the β subunit of RNA polymerase and the arginine-rich domain of Escherichia coli NusA protein. J. Bact. 173, 1492-1501.
    • (1991) J. Bact. , vol.173 , pp. 1492-1501
    • Ito, K.1    Egawa, K.2    Nakamura, Y.3
  • 25
    • 0029915450 scopus 로고    scopus 로고
    • Solution structure of prokaryotic ribosomal protein S17 by high-resolution NMR spectroscopy
    • Jaishree, T.N., Ramakrishnan, V., and White, S.W. (1996). Solution structure of prokaryotic ribosomal protein S17 by high-resolution NMR spectroscopy. Biochemistry 35, 2845-2853.
    • (1996) Biochemistry , vol.35 , pp. 2845-2853
    • Jaishree, T.N.1    Ramakrishnan, V.2    White, S.W.3
  • 27
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 28
    • 0029058994 scopus 로고
    • Structure of the dsRNA binding domain of Escherichia coli RNAse-III
    • Kharrat, A., Macias, M.J., Gibson, T.J., Nilges, M., and Pastore A. (1995). Structure of the dsRNA binding domain of Escherichia coli RNAse-III. EMBO J. 14, 3572-3584.
    • (1995) EMBO J. , vol.14 , pp. 3572-3584
    • Kharrat, A.1    Macias, M.J.2    Gibson, T.J.3    Nilges, M.4    Pastore, A.5
  • 29
    • 0028559548 scopus 로고
    • Toxic shock syndrome toxin-1 complexed with a class II major histocompatibility molecule HLA-DR1
    • Kim, J., Urban, R.G., Strominger, J.L., and Wiley, D.C. (1994). Toxic shock syndrome toxin-1 complexed with a class II major histocompatibility molecule HLA-DR1. Science 266, 1870-1874.
    • (1994) Science , vol.266 , pp. 1870-1874
    • Kim, J.1    Urban, R.G.2    Strominger, J.L.3    Wiley, D.C.4
  • 30
    • 0026244229 scopus 로고
    • Molscript - a program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). Molscript - a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 31
    • 0028362547 scopus 로고
    • A subunit of an archaeal DNA-dependent RNA polymerase contains the S1 motif
    • Langer, D., Lottspeich. F., and Zillig, W. (1994). A subunit of an archaeal DNA-dependent RNA polymerase contains the S1 motif. Nucleic Acids Res. 22, 694.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 694
    • Langer, D.1    Lottspeich, F.2    Zillig, W.3
  • 32
    • 0028932769 scopus 로고
    • NusA contacts nascent RNA in Escherichia coli transcription complexes
    • Liu, K., and Hanna, M.M. (1995). NusA contacts nascent RNA in Escherichia coli transcription complexes. J. Mol. Biol. 247, 547-558.
    • (1995) J. Mol. Biol. , vol.247 , pp. 547-558
    • Liu, K.1    Hanna, M.M.2
  • 33
    • 0027315727 scopus 로고
    • RNA recognition - a family matter
    • Mattaj, I.W. (1993). RNA recognition - a family matter. Cell 73, 837-840.
    • (1993) Cell , vol.73 , pp. 837-840
    • Mattaj, I.W.1
  • 34
    • 0029094248 scopus 로고
    • Recruiting proteins to the RNA world
    • Mattaj, I.W., and Nagai, K. (1995). Recruiting proteins to the RNA world. Nat. Struct. Biol. 2, 518-522.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 518-522
    • Mattaj, I.W.1    Nagai, K.2
  • 36
    • 0027479161 scopus 로고
    • OB (oligonucleotide oligosaccharide binding) fold - Common structural and functional solution for nonhomologous sequences
    • Murzin, A.G. (1993). OB (oligonucleotide oligosaccharide binding) fold - common structural and functional solution for nonhomologous sequences. EMBO J. 12, 861-867.
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 37
    • 0028961335 scopus 로고
    • SCOP - a Structural Classification of Proteins database for the investigation of sequences and structures
    • Murzin, A.G., Brenner, S.E., Hubbard, T., and Chothia, C. (1995). SCOP - a Structural Classification of Proteins database for the investigation of sequences and structures. J. Mol. Biol. 247, 536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 38
    • 0029988528 scopus 로고    scopus 로고
    • 3-Dimensional structure and stability of the KH domain - Molecular insights into the fragile-X syndrome
    • Musco, G., Stier, G., Joseph, C., Morelli, M.A.C., Nilges, M., Gibson, T.J., and Pastore, A. (1996). 3-Dimensional structure and stability of the KH domain - molecular insights into the fragile-X syndrome. Cell 85, 237-245.
    • (1996) Cell , vol.85 , pp. 237-245
    • Musco, G.1    Stier, G.2    Joseph, C.3    Morelli, M.A.C.4    Nilges, M.5    Gibson, T.J.6    Pastore, A.7
  • 39
    • 0025221731 scopus 로고
    • Crystal-structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein-A
    • Nagai, K., Oubridge, C., Jessen, T.H., Li, J., and Evans, P.R. (1990). Crystal-structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein-A. Nature 348, 515-520.
    • (1990) Nature , vol.348 , pp. 515-520
    • Nagai, K.1    Oubridge, C.2    Jessen, T.H.3    Li, J.4    Evans, P.R.5
  • 40
    • 0028990057 scopus 로고
    • The RNP domain - A sequence-specific RNA-binding domain involved in processing and transport of RNA
    • Nagai, K., Oubridge, C., Ito, N., Avis, J., and Evans, P. (1995). The RNP domain - a sequence-specific RNA-binding domain involved in processing and transport of RNA.Trends Biochem. Sci. 20, 235-240.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 235-240
    • Nagai, K.1    Oubridge, C.2    Ito, N.3    Avis, J.4    Evans, P.5
  • 41
    • 0024435833 scopus 로고
    • Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA binding domain of the 434-repressor by biosynthetically directed fractional C-13 labeling
    • Neri, D., Szyperski, T., Otting, G., Senn, H., and Wuthrich, K. (1989). Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA binding domain of the 434-repressor by biosynthetically directed fractional C-13 labeling. Biochem. 28, 7510-7516.
    • (1989) Biochem. , vol.28 , pp. 7510-7516
    • Neri, D.1    Szyperski, T.2    Otting, G.3    Senn, H.4    Wuthrich, K.5
  • 43
    • 0027955358 scopus 로고
    • Cytoplasmic axial filaments in Escherichia coli cells: Possible function in the mechanism of chromosome segregation and cell division
    • Okada, Y., Wachi, M., Hirata, A., Suzuki, K., Nagai, K., and Matsuhashi, M. (1994). Cytoplasmic axial filaments in Escherichia coli cells: possible function in the mechanism of chromosome segregation and cell division. J. Bact. 776, 917-922.
    • (1994) J. Bact. , vol.776 , pp. 917-922
    • Okada, Y.1    Wachi, M.2    Hirata, A.3    Suzuki, K.4    Nagai, K.5    Matsuhashi, M.6
  • 44
    • 0029643954 scopus 로고
    • The crystal structure of the lysyl-tRNA synthetase (LysU)from Escherichia coli
    • Onesti, S., Miller, A.D., and Brick, P. (1995). The crystal structure of the lysyl-tRNA synthetase (LysU)from Escherichia coli. Structure 3, 163-176.
    • (1995) Structure , vol.3 , pp. 163-176
    • Onesti, S.1    Miller, A.D.2    Brick, P.3
  • 45
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 Angstrom resolution of the RNA-binding domain of the U1a spliceosomal protein complexed with an RNA hairpin
    • Oubridge, C., Ito, H., Evans, P.R., Teo, C.H., and Nagai, K. (1994). Crystal structure at 1.92 Angstrom resolution of the RNA-binding domain of the U1a spliceosomal protein complexed with an RNA hairpin. Nature 372, 432-438.
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, H.2    Evans, P.R.3    Teo, C.H.4    Nagai, K.5
  • 46
    • 0027945686 scopus 로고
    • A protein complex mediating messenger RNA degradation in Escherichia coli
    • Py, B., Causton, H., Mudd, E.A., and Higgins, C.F. (1994). A protein complex mediating messenger RNA degradation in Escherichia coli. Mol. Micro. 14, 717-729.
    • (1994) Mol. Micro. , vol.14 , pp. 717-729
    • Py, B.1    Causton, H.2    Mudd, E.A.3    Higgins, C.F.4
  • 48
    • 0023088853 scopus 로고
    • Nucleotide sequence of the PNP gene of Escherichia coli encoding polynucleotide phosphorylase; homology of the primary structure of the protein with the RNA binding domain of ribosomal protein S1
    • Regnier, P., GrunbergManago, M., and Portier, C. (1987). Nucleotide sequence of the PNP gene of Escherichia coli encoding polynucleotide phosphorylase; homology of the primary structure of the protein with the RNA binding domain of ribosomal protein S1. J. Biol. Chem. 262, 63-68.
    • (1987) J. Biol. Chem. , vol.262 , pp. 63-68
    • Regnier, P.1    GrunbergManago, M.2    Portier, C.3
  • 49
    • 0028923775 scopus 로고
    • High-affinity RNA ligands to Escherichia coli ribosomes and ribosomal protein S1 - Comparison of natural and unnatural binding sites
    • Ringquist, S., Jones, T., Snyder, E.E., Gibson, T., Boni, I., and Gold, L. (1995). High-affinity RNA ligands to Escherichia coli ribosomes and ribosomal protein S1 - comparison of natural and unnatural binding sites. Biochemistry 34, 3640-3648.
    • (1995) Biochemistry , vol.34 , pp. 3640-3648
    • Ringquist, S.1    Jones, T.2    Snyder, E.E.3    Gibson, T.4    Boni, I.5    Gold, L.6
  • 50
    • 0028158628 scopus 로고
    • PHD - an automatic mail server for protein secondary structure prediction
    • Rost, B., Sander, C., and Schneider, R. (1994). PHD - an automatic mail server for protein secondary structure prediction. Comp. Applic. Biosci. 10, 53-60.
    • (1994) Comp. Applic. Biosci. , vol.10 , pp. 53-60
    • Rost, B.1    Sander, C.2    Schneider, R.3
  • 51
    • 0028104155 scopus 로고
    • The bacteriophage T4 regB ribonuclease - Stimulation of the purified enzyme by ribosomal protein S1
    • Ruckman, J., Ringquist, S., Brody, E., and Gold, L. (1994).The bacteriophage T4 regB ribonuclease - stimulation of the purified enzyme by ribosomal protein S1. J. Biol. Chem. 269, 26655-26662.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26655-26662
    • Ruckman, J.1    Ringquist, S.2    Brody, E.3    Gold, L.4
  • 52
    • 0026030641 scopus 로고
    • Database of homology-derived protein structures and the structural meaning of sequence alignment
    • Sander, C., and Schneider, R. (1991). Database of homology-derived protein structures and the structural meaning of sequence alignment. Proteins 9, 56-68.
    • (1991) Proteins , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 53
    • 0027296211 scopus 로고
    • Universal nucleic acid-binding domain revealed by crystal structure of the B. Subtilis major cold-shock protein
    • Schindelin, H., Marahiel, M.A., and Heinemann, U. (1993). Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein. Nature 364, 164-168.
    • (1993) Nature , vol.364 , pp. 164-168
    • Schindelin, H.1    Marahiel, M.A.2    Heinemann, U.3
  • 54
    • 0029052511 scopus 로고
    • Crystal structure of a replication fork single-stranded DNA binding protein (T4gp32) complexed to DNA
    • Shamoo, Y., Friedman, A.M., Parsons, M.R., Konigsberg, W.H., and Steitz, T.A. (1995). Crystal structure of a replication fork single-stranded DNA binding protein (T4gp32) complexed to DNA. Nature 376, 362-366.
    • (1995) Nature , vol.376 , pp. 362-366
    • Shamoo, Y.1    Friedman, A.M.2    Parsons, M.R.3    Konigsberg, W.H.4    Steitz, T.A.5
  • 55
    • 0027273728 scopus 로고
    • The premessenger RNA-binding K-protein contains a novel evolutionarily conserved motif
    • Siomi, H., Matunis, M.J., Michael, W.M., and Dreyfuss, G. (1993). The premessenger RNA-binding K-protein contains a novel evolutionarily conserved motif. Nucleic Acids Res. 21, 1193-1198.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1193-1198
    • Siomi, H.1    Matunis, M.J.2    Michael, W.M.3    Dreyfuss, G.4
  • 58
    • 0002584387 scopus 로고
    • A convenient and accurate method for the measurement of the values of spin-spin coupling constants
    • Stonehouse, J., and Keeler, J. (1995). A convenient and accurate method for the measurement of the values of spin-spin coupling constants. J. Mag. Res. (A) 112, 43-57.
    • (1995) J. Mag. Res. (A) , vol.112 , pp. 43-57
    • Stonehouse, J.1    Keeler, J.2
  • 59
    • 0020671323 scopus 로고
    • Structure and functions of ribosomal protein S1
    • Subramanian, A.R. (1983) Structure and functions of ribosomal protein S1. Prog. Nucleic Acid Res. Mol. Biol. 28, 101-142.
    • (1983) Prog. Nucleic Acid Res. Mol. Biol. , vol.28 , pp. 101-142
    • Subramanian, A.R.1
  • 60
    • 0029938467 scopus 로고    scopus 로고
    • Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7
    • Subramanya, H.S., Doherty, A.J., Ashford, S.R., and Wigley, D.B. (1996). Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7. Cell 85, 607-615.
    • (1996) Cell , vol.85 , pp. 607-615
    • Subramanya, H.S.1    Doherty, A.J.2    Ashford, S.R.3    Wigley, D.B.4
  • 62
    • 0026688006 scopus 로고
    • VacB, a novel chromosomal gene required for expression of virulence genes on the large plasmid of Shigella flexneri
    • Tobe, T., Sasakawa, C., Okada, N., Honma, Y., and Yoshikawa, M. (1992). VacB, a novel chromosomal gene required for expression of virulence genes on the large plasmid of Shigella flexneri. J. Bact. 174, 6359-6367.
    • (1992) J. Bact. , vol.174 , pp. 6359-6367
    • Tobe, T.1    Sasakawa, C.2    Okada, N.3    Honma, Y.4    Yoshikawa, M.5
  • 63
    • 0027394312 scopus 로고
    • Ribosomal protein S1 and NusA protein complexed to recombination protein β of phage λ
    • Venkatesh, T.V., and Radding, C.M. (1993). Ribosomal protein S1 and NusA protein complexed to recombination protein β of phage λ. J. Bact. 175, 1844-1846.
    • (1993) J. Bact. , vol.175 , pp. 1844-1846
    • Venkatesh, T.V.1    Radding, C.M.2
  • 64
    • 0027973352 scopus 로고
    • Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein family
    • Williamson, R.A., Martorell, G., Carr, M.D., Murphy, G.A. Docherty, J., Freedman, R.B., and Feeney, J. (1994). Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein family. Biochemistry 33, 11745-11759.
    • (1994) Biochemistry , vol.33 , pp. 11745-11759
    • Williamson, R.A.1    Martorell, G.2    Carr, M.D.3    Murphy, G.A.4    Docherty, J.5    Freedman, R.B.6    Feeney, J.7
  • 65
    • 0028409179 scopus 로고
    • Structural and functional-properties of the evolutionarily ancient Y box family of nucleic acid binding-proteins
    • Wolffe, A.P. (1994). Structural and functional-properties of the evolutionarily ancient Y box family of nucleic acid binding-proteins. Bioessays 16, 245-251.
    • (1994) Bioessays , vol.16 , pp. 245-251
    • Wolffe, A.P.1
  • 66
    • 0027531685 scopus 로고
    • DNA sequencing and expression of the gene rnb encoding Escherichia coli ribonuclease II
    • Zilhao, R., Camelo, L., and Arraiano, C.M. (1993). DNA sequencing and expression of the gene rnb encoding Escherichia coli ribonuclease II. Mol. Micro. 8, 43-51.
    • (1993) Mol. Micro. , vol.8 , pp. 43-51
    • Zilhao, R.1    Camelo, L.2    Arraiano, C.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.