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Volumn 394, Issue , 2005, Pages 525-545

Structure determination of protein/RNA complexes by NMR

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEOLIN; PROTEIN; RNA;

EID: 16244394790     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(05)94022-6     Document Type: Article
Times cited : (37)

References (82)
  • 1
    • 1842577742 scopus 로고    scopus 로고
    • Structural analysis of cooperative RNA binding by the la motif and central RRM domain of human la protein
    • Alfano C., Sanfelice D., Babon J., Kelly G., Jacks A., Curry S., Conte M.R. Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein. Nat. Struct. Mol. Biol. 11:2004;323-329
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 323-329
    • Alfano, C.1    Sanfelice, D.2    Babon, J.3    Kelly, G.4    Jacks, A.5    Curry, S.6    Conte, M.R.7
  • 2
    • 0030755124 scopus 로고    scopus 로고
    • Structural basis of the RNA-binding specificity of human U1A protein
    • Allain F.H.T., Howe P.W.A., Neuhaus D., Varani G. Structural basis of the RNA-binding specificity of human U1A protein. Embo J. 16:1997;5764-5774
    • (1997) Embo J. , vol.16 , pp. 5764-5774
    • Allain, F.H.T.1    Howe, P.W.A.2    Neuhaus, D.3    Varani, G.4
  • 3
    • 0034672094 scopus 로고    scopus 로고
    • Molecular basis of sequence-specific recognition of pre-ribosomal RNA by nucleolin
    • Allain F. H.-T., Bouvet P., Dieckmann T., Feigon J. Molecular basis of sequence-specific recognition of pre-ribosomal RNA by nucleolin. Embo J. 19:2000a;6870-6881
    • (2000) Embo J. , vol.19 , pp. 6870-6881
    • Allain, F.H.-T.1    Bouvet, P.2    Dieckmann, T.3    Feigon, J.4
  • 4
    • 0034692906 scopus 로고    scopus 로고
    • Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR study of the interaction with its RNA target
    • Allain F. H.-T., Gilbert D.E., Bouvet P., Feigon J. Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR study of the interaction with its RNA target. J. Mol. Biol. 303:2000b;227-241
    • (2000) J. Mol. Biol. , vol.303 , pp. 227-241
    • Allain, F.H.-T.1    Gilbert, D.E.2    Bouvet, P.3    Feigon, J.4
  • 5
    • 0034911866 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods to study structure and dynamics of RNA-protein complexes
    • Allen M., Varani L., Varani G. Nuclear magnetic resonance methods to study structure and dynamics of RNA-protein complexes. Methods Enzymol. 339:2001;357-376
    • (2001) Methods Enzymol. , vol.339 , pp. 357-376
    • Allen, M.1    Varani, L.2    Varani, G.3
  • 6
    • 0035800599 scopus 로고    scopus 로고
    • Structure-based analysis of protein-RNA interactions using the program ENTANGLE
    • Allers J., Shamoo Y. Structure-based analysis of protein-RNA interactions using the program ENTANGLE. J. Mol. Biol. 311:2001;75-86
    • (2001) J. Mol. Biol. , vol.311 , pp. 75-86
    • Allers, J.1    Shamoo, Y.2
  • 10
    • 0032999204 scopus 로고    scopus 로고
    • Refinement of the structure of protein-RNA complexes by residual dipolar coupling analysis
    • Bayer P., Varani L., Varani G. Refinement of the structure of protein-RNA complexes by residual dipolar coupling analysis. J. Biomol. NMR. 14:1999;149-155
    • (1999) J. Biomol. NMR , vol.14 , pp. 149-155
    • Bayer, P.1    Varani, L.2    Varani, G.3
  • 11
    • 0344196970 scopus 로고    scopus 로고
    • Fingering nucleic acids: The RNA did it
    • Berg J.M. Fingering nucleic acids: The RNA did it. Nat. Struct. Biol. 10:2003;986-987
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 986-987
    • Berg, J.M.1
  • 12
    • 0027753933 scopus 로고
    • Analysis of the RNA-recognition motif and RS and RGG domains: Conservation in metazoan pre-mRNA splicing factors
    • Birney E., Kumar S., Krainer A.R. Analysis of the RNA-recognition motif and RS and RGG domains: Conservation in metazoan pre-mRNA splicing factors. Nucleic Acids Res. 21:1993;5803-5816
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5803-5816
    • Birney, E.1    Kumar, S.2    Krainer, A.R.3
  • 13
    • 0000112965 scopus 로고    scopus 로고
    • Isotope-filtered NMR methods for the study of biomolecular structure and interactions
    • Breeze A.L. Isotope-filtered NMR methods for the study of biomolecular structure and interactions. Prog. Nucl. Magn. Reson. Spectrosc. 36:2000;323-372
    • (2000) Prog. Nucl. Magn. Reson. Spectrosc. , vol.36 , pp. 323-372
    • Breeze, A.L.1
  • 15
    • 0026338995 scopus 로고
    • Use of polyethyleneimine in purification of DNA-binding proteins
    • Burgess R.R. Use of polyethyleneimine in purification of DNA-binding proteins. Methods Enzymol. 208:1991;3-10
    • (1991) Methods Enzymol. , vol.208 , pp. 3-10
    • Burgess, R.R.1
  • 17
    • 0034724279 scopus 로고    scopus 로고
    • Recognition of a conserved class of RNA tetraloops by Saccharomyces cerevisiae RNase III
    • Chanfreau C., Buckle M., Jacquier A. Recognition of a conserved class of RNA tetraloops by Saccharomyces cerevisiae RNase III. Proc. Natl. Acad. Sci. USA. 97:2000;3142-3147
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3142-3147
    • Chanfreau, C.1    Buckle, M.2    Jacquier, A.3
  • 18
    • 0034254909 scopus 로고    scopus 로고
    • Accurate and rapid docking of protein-protein complexes on the basis of intermolecular nuclear overhauser enhancement data and dipolar couplings by rigid body minimization
    • Clore G.M. Accurate and rapid docking of protein-protein complexes on the basis of intermolecular nuclear overhauser enhancement data and dipolar couplings by rigid body minimization. Proc. Natl. Acad. Sci. USA. 97:2000;9021-9025
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9021-9025
    • Clore, G.M.1
  • 19
    • 0032012610 scopus 로고    scopus 로고
    • Direct structure refinement against residual dipolar couplings in the presence of rhombicity of unknown magnitude
    • Clore G.M., Gronenborn A.M., Tjandra N. Direct structure refinement against residual dipolar couplings in the presence of rhombicity of unknown magnitude. J. Magn. Reson. 131:1998;159-162
    • (1998) J. Magn. Reson. , vol.131 , pp. 159-162
    • Clore, G.M.1    Gronenborn, A.M.2    Tjandra, N.3
  • 20
    • 0031599782 scopus 로고    scopus 로고
    • 3D C(CC)H TOCSY experiment for assigning protons and carbons in uniformly 13C- and selectively 2H-labeled RNA
    • Dayie K.T., Tolbert T.J., Williamson J.R. 3D C(CC)H TOCSY experiment for assigning protons and carbons in uniformly 13C- and selectively 2H-labeled RNA. J. Magn. Reson. 130:1998;97-101
    • (1998) J. Magn. Reson. , vol.130 , pp. 97-101
    • Dayie, K.T.1    Tolbert, T.J.2    Williamson, J.R.3
  • 21
    • 0037169646 scopus 로고    scopus 로고
    • NMR dipolar couplings for the structure determination of biopolymers in solution
    • de Alba E., Tjandra N. NMR dipolar couplings for the structure determination of biopolymers in solution. Prog. Nucl. Magn. Reson. Spectrosc. 40:2002;175-197
    • (2002) Prog. Nucl. Magn. Reson. Spectrosc. , vol.40 , pp. 175-197
    • De Alba, E.1    Tjandra, N.2
  • 22
    • 2242469712 scopus 로고    scopus 로고
    • Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element
    • De Guzman R.N., Wu Z.R., Stalling C.C., Pappalardo L., Borer P.N., Summers M.F. Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element. Science. 279:1998;384-388
    • (1998) Science , vol.279 , pp. 384-388
    • De Guzman, R.N.1    Wu, Z.R.2    Stalling, C.C.3    Pappalardo, L.4    Borer, P.N.5    Summers, M.F.6
  • 23
    • 0031114540 scopus 로고    scopus 로고
    • Assignment methodology for larger RNA oligonucleotides: Application to an ATP-binding RNA aptamer
    • Dieckmann T., Feigon J. Assignment methodology for larger RNA oligonucleotides: Application to an ATP-binding RNA aptamer. J. Biomol. NMR. 9:1997;259-272
    • (1997) J. Biomol. NMR , vol.9 , pp. 259-272
    • Dieckmann, T.1    Feigon, J.2
  • 24
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • Dominguez C., Boelens R., Bonvin A.M.J.J. HADDOCK: A protein-protein docking approach based on biochemical or biophysical information. J. Am. Chem. Soc. 125:2003;1731-1737
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.J.J.3
  • 25
    • 1442286437 scopus 로고    scopus 로고
    • NMR structure of the 101-nucleotide core encapsidation signal of the Moloney murine leukemia virus
    • D'Souza V., Dey A., Habib D., Summers M.F. NMR structure of the 101-nucleotide core encapsidation signal of the Moloney murine leukemia virus. J. Mol. Biol. 337:2004;427-442
    • (2004) J. Mol. Biol. , vol.337 , pp. 427-442
    • D'Souza, V.1    Dey, A.2    Habib, D.3    Summers, M.F.4
  • 26
    • 0034801402 scopus 로고    scopus 로고
    • Measurement of (13)C(alpha)-(13)C(beta) dipolar couplings in (15)N,(13)C,(2)H-labeled proteins: Application to domain orientation in maltose binding protein
    • Evenas J., Mittermaier A., Yang D., Kay L.E. Measurement of (13)C(alpha)-(13)C(beta) dipolar couplings in (15)N,(13)C,(2)H-labeled proteins: Application to domain orientation in maltose binding protein. J. Am. Chem. Soc. 123:2001;2858-2864
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2858-2864
    • Evenas, J.1    Mittermaier, A.2    Yang, D.3    Kay, L.E.4
  • 27
    • 0034912670 scopus 로고    scopus 로고
    • Solution nuclear magnetic resonance probing of cation binding sites on nucleic acids
    • Feigon J., Butcher S.E., Finger L.D., Hud N.V. Solution nuclear magnetic resonance probing of cation binding sites on nucleic acids. Methods Enzymol. 338:2001;400-420
    • (2001) Methods Enzymol. , vol.338 , pp. 400-420
    • Feigon, J.1    Butcher, S.E.2    Finger, L.D.3    Hud, N.V.4
  • 28
    • 0345099648 scopus 로고    scopus 로고
    • Solution structures of stem-loop RNAs that bind to the two N-terminal RNA-binding domains of nucleolin
    • Finger L.D., Trantirek L., Johansson C., Feigon J. Solution structures of stem-loop RNAs that bind to the two N-terminal RNA-binding domains of nucleolin. Nucleic Acids Res. 31:2003;6461-6472
    • (2003) Nucleic Acids Res. , vol.31 , pp. 6461-6472
    • Finger, L.D.1    Trantirek, L.2    Johansson, C.3    Feigon, J.4
  • 29
    • 0032113850 scopus 로고    scopus 로고
    • Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA
    • Foster M.P., Wuttke D.S., Clemens K.R., Jahnke W., Radhakrishnan I., Tennant L., Reymond M., Chung J., Wright P.E. Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA. J. Biomol. NMR. 12:1998;51-71
    • (1998) J. Biomol. NMR , vol.12 , pp. 51-71
    • Foster, M.P.1    Wuttke, D.S.2    Clemens, K.R.3    Jahnke, W.4    Radhakrishnan, I.5    Tennant, L.6    Reymond, M.7    Chung, J.8    Wright, P.E.9
  • 31
    • 0031595590 scopus 로고    scopus 로고
    • The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins
    • Gardner K.H., Kay L.E. The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins. Annu. Rev. Biophys. Biomol. Struct. 27:1998;357-406
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 357-406
    • Gardner, K.H.1    Kay, L.E.2
  • 32
    • 0030570466 scopus 로고    scopus 로고
    • Nucleolin is a sequence-specific RNA-binding protein: Characterization of targets on pre-ribosomal RNA
    • Ghisolfi-Nieto L., Joseph G., Puvion-Dutilleul F., Amalric F., Bouvet P. Nucleolin is a sequence-specific RNA-binding protein: Characterization of targets on pre-ribosomal RNA. J. Mol. Biol. 260:1996;34-53
    • (1996) J. Mol. Biol. , vol.260 , pp. 34-53
    • Ghisolfi-Nieto, L.1    Joseph, G.2    Puvion-Dutilleul, F.3    Amalric, F.4    Bouvet, P.5
  • 33
    • 0031714689 scopus 로고    scopus 로고
    • Structure calculation of biological macromolecules from NMR Q
    • Guntert P. Structure calculation of biological macromolecules from NMR Q. Rev. Biophys. 31:1998;145-237
    • (1998) Rev. Biophys. , vol.31 , pp. 145-237
    • Guntert, P.1
  • 34
  • 35
    • 0036606483 scopus 로고    scopus 로고
    • Principles of docking: An overview of search algorithms and a guide to scoring functions
    • Halperin I., Ma B.Y., Wolfson H., Nussinov R. Principles of docking: An overview of search algorithms and a guide to scoring functions. Proteins. 47:2002;409-443
    • (2002) Proteins , vol.47 , pp. 409-443
    • Halperin, I.1    Ma, B.Y.2    Wolfson, H.3    Nussinov, R.4
  • 37
    • 0036500804 scopus 로고    scopus 로고
    • The structure of the Dead ringer-DNA complex reveals how AT-rich interaction domains (ARIDs) recognize DNA
    • Iwahara J., Iwahara M., Daughdrill G.W., Ford J., Clubb R.T. The structure of the Dead ringer-DNA complex reveals how AT-rich interaction domains (ARIDs) recognize DNA. Embo J. 21:2002;1197-1209
    • (2002) Embo J. , vol.21 , pp. 1197-1209
    • Iwahara, J.1    Iwahara, M.2    Daughdrill, G.W.3    Ford, J.4    Clubb, R.T.5
  • 38
    • 1642348680 scopus 로고    scopus 로고
    • Solution structure of the complex formed by the two N-terminal RNA-binding domains of nucleolin and a pre-rRNA target
    • Johansson C., Finger L.D., Trantirek L., Mueller T.D., Kim S., Laird-Offringa I.A., Feigon J. Solution structure of the complex formed by the two N-terminal RNA-binding domains of nucleolin and a pre-rRNA target. J. Mol. Biol. 337:2004;799-816
    • (2004) J. Mol. Biol. , vol.337 , pp. 799-816
    • Johansson, C.1    Finger, L.D.2    Trantirek, L.3    Mueller, T.D.4    Kim, S.5    Laird-Offringa, I.A.6    Feigon, J.7
  • 39
    • 0028804911 scopus 로고
    • Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli
    • Kane J.F. Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli. Curr. Opin. Biotechnol. 6:1995;494-500
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 494-500
    • Kane, J.F.1
  • 40
    • 0034146355 scopus 로고    scopus 로고
    • Evaluation of cross-correlation effects and measurement of one-bond couplings in proteins with short transverse relaxation times
    • Kontaxis G., Clore G.M., Bax A. Evaluation of cross-correlation effects and measurement of one-bond couplings in proteins with short transverse relaxation times. J. Magn. Reson. 143:2000;184-196
    • (2000) J. Magn. Reson. , vol.143 , pp. 184-196
    • Kontaxis, G.1    Clore, G.M.2    Bax, A.3
  • 41
    • 0034767343 scopus 로고    scopus 로고
    • Determining binding sites in protein-nucleic acid complexes by cross-saturation
    • Lane A.N., Kelly G., Ramos A., Frenkiel T.A. Determining binding sites in protein-nucleic acid complexes by cross-saturation. J. Biomol. NMR. 21:2001;127-139
    • (2001) J. Biomol. NMR , vol.21 , pp. 127-139
    • Lane, A.N.1    Kelly, G.2    Ramos, A.3    Frenkiel, T.A.4
  • 43
    • 0033185668 scopus 로고    scopus 로고
    • Pulse sequences for measurement of one-bond (15)N-(1)H coupling constants in the protein backbone
    • Lerche M.H., Meissner A., Poulsen F.M., Sørensen O.W. Pulse sequences for measurement of one-bond (15)N-(1)H coupling constants in the protein backbone. J. Magn. Reson. 140:1999;259-263
    • (1999) J. Magn. Reson. , vol.140 , pp. 259-263
    • Lerche, M.H.1    Meissner, A.2    Poulsen, F.M.3    Sørensen, O.W.4
  • 44
    • 0035838382 scopus 로고    scopus 로고
    • Current topics in RNA-protein recognition: Control of specificity and biological function through induced fit and conformational capture
    • Leulliot N., Varani G. Current topics in RNA-protein recognition: Control of specificity and biological function through induced fit and conformational capture. Biochemistry. 40:2001;7947-7956
    • (2001) Biochemistry , vol.40 , pp. 7947-7956
    • Leulliot, N.1    Varani, G.2
  • 46
    • 0035095521 scopus 로고    scopus 로고
    • Large-scale purification of a stable form of recombinant tobacco etch virus protease
    • Lucast L.J., Batey R.T., Doudna J.A. Large-scale purification of a stable form of recombinant tobacco etch virus protease. Biotechniques. 30:2001;544-554
    • (2001) Biotechniques , vol.30 , pp. 544-554
    • Lucast, L.J.1    Batey, R.T.2    Doudna, J.A.3
  • 47
    • 0042674372 scopus 로고    scopus 로고
    • JE-TROSY: Combined J- and TROSY-spectroscopy for the measurement of one-bond couplings in macromolecules
    • Luy B., Marino J.P. JE-TROSY: Combined J- and TROSY-spectroscopy for the measurement of one-bond couplings in macromolecules. J. Magn. Reson. 163:2003;92-98
    • (2003) J. Magn. Reson. , vol.163 , pp. 92-98
    • Luy, B.1    Marino, J.P.2
  • 48
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides S.C. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 60:1996;512-538
    • (1996) Microbiol. Rev. , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 49
    • 0032710024 scopus 로고    scopus 로고
    • A novel loop-loop recognition motif in the yeast ribosomal protein L30 autoregulatory RNA complex
    • Mao H., White S.A., Williamson J.R. A novel loop-loop recognition motif in the yeast ribosomal protein L30 autoregulatory RNA complex. Nat. Struct. Biol. 6:1999;1139-1147
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1139-1147
    • Mao, H.1    White, S.A.2    Williamson, J.R.3
  • 50
    • 0032795253 scopus 로고    scopus 로고
    • J-coupling restraints for structural refinements of RNA
    • Marino J.P., Schwalbe H., Griesinger C. J-coupling restraints for structural refinements of RNA. Acc. Chem. Res. 32:1999;614-623
    • (1999) Acc. Chem. Res. , vol.32 , pp. 614-623
    • Marino, J.P.1    Schwalbe, H.2    Griesinger, C.3
  • 51
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labeling of recombinant proteins
    • Marley J., Lu M., Bracken C. A method for efficient isotopic labeling of recombinant proteins. J. Biomol. NMR. 20:2001;71-75
    • (2001) J. Biomol. NMR , vol.20 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3
  • 52
    • 0024819449 scopus 로고
    • Synthesis of small RNAs using T7 RNA polymerase
    • Milligan J.F., Uhlenbeck O.C. Synthesis of small RNAs using T7 RNA polymerase. Methods Enzymol. 180:1989;51-62
    • (1989) Methods Enzymol. , vol.180 , pp. 51-62
    • Milligan, J.F.1    Uhlenbeck, O.C.2
  • 54
    • 0024836418 scopus 로고
    • Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance
    • Muchmore D.C., McIntosh L.P., Russell C.B., Anderson D.E., Dahlquist F.W. Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance. Methods Enzymol. 177:1989;44-73
    • (1989) Methods Enzymol. , vol.177 , pp. 44-73
    • Muchmore, D.C.1    McIntosh, L.P.2    Russell, C.B.3    Anderson, D.E.4    Dahlquist, F.W.5
  • 55
    • 0028205651 scopus 로고
    • A general purification procedure for chemically synthesized oligoribonucleotides
    • Murray J.B., Collier A.K., Arnold J.R.P. A general purification procedure for chemically synthesized oligoribonucleotides. Anal. Biochem. 218:1994;177-184
    • (1994) Anal. Biochem. , vol.218 , pp. 177-184
    • Murray, J.B.1    Collier, A.K.2    Arnold, J.R.P.3
  • 57
  • 58
    • 0029283884 scopus 로고
    • Chemical shifts and three-dimensional protein structures
    • Oldfield E. Chemical shifts and three-dimensional protein structures. J. Biomol. NMR. 5:1995;217-225
    • (1995) J. Biomol. NMR , vol.5 , pp. 217-225
    • Oldfield, E.1
  • 60
    • 0033637980 scopus 로고    scopus 로고
    • Impact of transverse relaxation optimized spectroscopy (TROSY) on NMR as a technique in structural biology
    • Pervushin K. Impact of transverse relaxation optimized spectroscopy (TROSY) on NMR as a technique in structural biology. Q. Rev. Biophys. 33:2000;161-197
    • (2000) Q. Rev. Biophys. , vol.33 , pp. 161-197
    • Pervushin, K.1
  • 61
    • 1242340502 scopus 로고    scopus 로고
    • New applications of 2D filtered/edited NOESY for assignment and structure elucidation of RNA and RNA-protein complexes
    • Peterson R.D., Theimer C.A., Wu H.H., Feigon J. New applications of 2D filtered/edited NOESY for assignment and structure elucidation of RNA and RNA-protein complexes. J. Biomol. NMR. 28:2004;59-67
    • (2004) J. Biomol. NMR , vol.28 , pp. 59-67
    • Peterson, R.D.1    Theimer, C.A.2    Wu, H.H.3    Feigon, J.4
  • 62
    • 0002669787 scopus 로고
    • TEV protease, recombinant: A site-specific protease for efficient cleavage of affinity tags from expressed proteins
    • Polayes D.A., Goldstein A., Hughes A.J., Johnston S.A., Dougherty W.G. TEV protease, recombinant: A site-specific protease for efficient cleavage of affinity tags from expressed proteins. Focus. 16:1994;2-5
    • (1994) Focus , vol.16 , pp. 2-5
    • Polayes, D.A.1    Goldstein, A.2    Hughes, A.J.3    Johnston, S.A.4    Dougherty, W.G.5
  • 63
    • 0034480326 scopus 로고    scopus 로고
    • NMR structures of biomolecules using field oriented media and residual dipolar couplings
    • Prestegard J.H., Al-Hashimi H.M., Tolman T.R. NMR structures of biomolecules using field oriented media and residual dipolar couplings. Q. Rev. Biophys. 33:2000;371-424
    • (2000) Q. Rev. Biophys. , vol.33 , pp. 371-424
    • Prestegard, J.H.1    Al-Hashimi, H.M.2    Tolman, T.R.3
  • 65
    • 0034703760 scopus 로고    scopus 로고
    • Mapping the interfaces of protein-nucleic acid complexes using cross-saturation
    • Ramos A., Kelly G., Hollingworth D., Pastore A., Frenkiel T. Mapping the interfaces of protein-nucleic acid complexes using cross-saturation. J. Am. Chem. Soc. 122:2000b;11311-11314
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 11311-11314
    • Ramos, A.1    Kelly, G.2    Hollingworth, D.3    Pastore, A.4    Frenkiel, T.5
  • 66
    • 0035977647 scopus 로고    scopus 로고
    • [(13)C,(13)C]- and [(13)C,(1)H]-TROSY in a triple resonance experiment for ribose-base and intrabase correlations in nucleic acids
    • Riek R., Pervushin K., Fernandez C., Kainosho M., Wuthrich K. [(13)C,(13)C]- and [(13)C,(1)H]-TROSY in a triple resonance experiment for ribose-base and intrabase correlations in nucleic acids. J. Am. Chem. Soc. 123:2001;658-664
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 658-664
    • Riek, R.1    Pervushin, K.2    Fernandez, C.3    Kainosho, M.4    Wuthrich, K.5
  • 67
    • 0037551646 scopus 로고    scopus 로고
    • Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments
    • Ruckert M., Otting G. Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments. J. Am. Chem. Soc. 122:2000;7793-7797
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 7793-7797
    • Ruckert, M.1    Otting, G.2
  • 68
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler M., Schleucher J., Griesinger C. Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog. Nucl. Magn. Reson. Spectrosc. 34:1999;93-158
    • (1999) Prog. Nucl. Magn. Reson. Spectrosc. , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 69
    • 0037711199 scopus 로고    scopus 로고
    • The dsRNA binding protein family: Critical roles, diverse cellular functions
    • Saunders L.R., Barber G.N. The dsRNA binding protein family: Critical roles, diverse cellular functions. Faseb J. 17:2003;961-983
    • (2003) Faseb J. , vol.17 , pp. 961-983
    • Saunders, L.R.1    Barber, G.N.2
  • 70
    • 0034840624 scopus 로고    scopus 로고
    • RNA oligonucleotide synthesis via 5′-silyl-2′-orthoester chemistry
    • Scaringe S.A. RNA oligonucleotide synthesis via 5′-silyl-2′- orthoester chemistry. Methods. 23:2001;206-217
    • (2001) Methods , vol.23 , pp. 206-217
    • Scaringe, S.A.1
  • 71
    • 0032855035 scopus 로고    scopus 로고
    • High-performance liquid chromatography purification of homogenous-length RNA produced by trans cleavage with a hammerhead ribozyme
    • Shields T.P., Mollova E., Marie L.S., Hansen M.R., Pardi A. High-performance liquid chromatography purification of homogenous-length RNA produced by trans cleavage with a hammerhead ribozyme. Rna. 5:1999;1259-1267
    • (1999) Rna , vol.5 , pp. 1259-1267
    • Shields, T.P.1    Mollova, E.2    Marie, L.S.3    Hansen, M.R.4    Pardi, A.5
  • 72
    • 0034913608 scopus 로고    scopus 로고
    • A TROSY relayed HCCH-COSY experiment for correlating adenine H2/H8 resonances in uniformly 13C-labeled RNA molecules
    • Simon B., Zanier K., Sattler M. A TROSY relayed HCCH-COSY experiment for correlating adenine H2/H8 resonances in uniformly 13C-labeled RNA molecules. J. Mol. Biol. 20:2001;173-176
    • (2001) J. Mol. Biol. , vol.20 , pp. 173-176
    • Simon, B.1    Zanier, K.2    Sattler, M.3
  • 73
    • 0344641932 scopus 로고    scopus 로고
    • The NMR structure of the 5S rRNA E-domain-protein L25 complex shows preformed and induced recognition
    • Stoldt M., Wohnert J., Ohlenschlager O., Gorlach M., Brown L.R. The NMR structure of the 5S rRNA E-domain-protein L25 complex shows preformed and induced recognition. Embo J. 18:1999;6508-6521
    • (1999) Embo J. , vol.18 , pp. 6508-6521
    • Stoldt, M.1    Wohnert, J.2    Ohlenschlager, O.3    Gorlach, M.4    Brown, L.R.5
  • 74
    • 0027379754 scopus 로고
    • SP6 RNA polymerase efficiently synthesizes RNA from short double-stranded DNA templates
    • Stump W.T., Hall K.B. SP6 RNA polymerase efficiently synthesizes RNA from short double-stranded DNA templates. Nucl. Acids Res. 21:1993;5480-5484
    • (1993) Nucl. Acids Res. , vol.21 , pp. 5480-5484
    • Stump, W.T.1    Hall, K.B.2
  • 75
    • 0031576691 scopus 로고    scopus 로고
    • Preparation of specifically deuterated and C-13-labeled RNA for NMR studies using enzymatic synthesis
    • Tolbert T.J., Williamson J.R. Preparation of specifically deuterated and C-13-labeled RNA for NMR studies using enzymatic synthesis. J. Am. Chem. Soc. 119:1997;12100-12108
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 12100-12108
    • Tolbert, T.J.1    Williamson, J.R.2
  • 76
    • 0034070741 scopus 로고    scopus 로고
    • The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein
    • Varani L., Gunderson S.I., Mattaj I.W., Kay L.E., Neuhaus D., Varani G. The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein. Nat. Struct. Biol. 7:2000;329-335
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 329-335
    • Varani, L.1    Gunderson, S.I.2    Mattaj, I.W.3    Kay, L.E.4    Neuhaus, D.5    Varani, G.6
  • 78
    • 0033784534 scopus 로고    scopus 로고
    • Induced fit in RNA-protein recognition
    • Williamson J.R. Induced fit in RNA-protein recognition. Nat. Struct. Biol. 7:2000;834-837
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 834-837
    • Williamson, J.R.1
  • 79
    • 3042704491 scopus 로고    scopus 로고
    • Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III
    • Wu H., Henras A., Chanfreau G., Feigon J. Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III. Proc. Natl. Acad. Sci. USA. 101:2004;8307-8312
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8307-8312
    • Wu, H.1    Henras, A.2    Chanfreau, G.3    Feigon, J.4
  • 82
    • 0037090685 scopus 로고    scopus 로고
    • Solution structure of the LicT-RNA antitermination complex: CAT clamping RAT
    • Yang Y.S., Declerck N., Manival X., Aymerich S., Kochoyan M. Solution structure of the LicT-RNA antitermination complex: CAT clamping RAT. Embo J. 21:2002;1987-1997
    • (2002) Embo J. , vol.21 , pp. 1987-1997
    • Yang, Y.S.1    Declerck, N.2    Manival, X.3    Aymerich, S.4    Kochoyan, M.5


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