메뉴 건너뛰기




Volumn 324, Issue 4, 2002, Pages 807-822

Solution structure and ligand recognition of the WW domain pair of the yeast splicing factor Prp40

Author keywords

CTD repeat; NMR structure; Proline rich; Prp40; WW domain

Indexed keywords

AMINO ACID; BINDING PROTEIN; LIGAND; MESSENGER RNA PRECURSOR; PEPTIDE; PROLINE; PROTEIN SUBUNIT; RNA POLYMERASE II; SMALL NUCLEAR RIBONUCLEOPROTEIN;

EID: 0036928101     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01145-2     Document Type: Article
Times cited : (72)

References (57)
  • 2
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson, T. (1995). Protein modules and signalling networks. Nature, 373, 573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 3
    • 0035783061 scopus 로고    scopus 로고
    • Protein repeats: Structures, functions, and evolution
    • Andrade, M. A., Perez-Iratxeta, C. & Ponting, C. P. (2001). Protein repeats: Structures, functions, and evolution. J. Struct. Biol. 134, 117-131.
    • (2001) J. Struct. Biol. , vol.134 , pp. 117-131
    • Andrade, M.A.1    Perez-Iratxeta, C.2    Ponting, C.P.3
  • 4
    • 0029050883 scopus 로고
    • Nuclear magnetic dipole interactions in field-oriented proteins: Information for structure determination in solution
    • Tolman, J. R., Flanagan, J. M., Kennedy, M. A. & Prestegard, J. H. (1995). Nuclear magnetic dipole interactions in field-oriented proteins: Information for structure determination in solution. Proc. Natl Acad. Sci. 92, 9279.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 9279
    • Tolman, J.R.1    Flanagan, J.M.2    Kennedy, M.A.3    Prestegard, J.H.4
  • 5
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid cryalline medium
    • Tjandra, N. & Bax, A. (1997). Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid cryalline medium. Science, 278, 1111-1114.
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 7
    • 0030963093 scopus 로고    scopus 로고
    • Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy
    • Tjandra, N., Garrett, D. S., Gronenborn, A. M., Bax, A. & Clore, G. M. (1997). Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Nature Struct. Biol. 4, 443-449.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 443-449
    • Tjandra, N.1    Garrett, D.S.2    Gronenborn, A.M.3    Bax, A.4    Clore, G.M.5
  • 8
    • 0027988814 scopus 로고
    • The WW domain: A signalling site in dystrophin?
    • Bork, P. & Sudol, M. (1994). The WW domain: A signalling site in dystrophin? Trends Biochem. Sci. 19, 531-533.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 531-533
    • Bork, P.1    Sudol, M.2
  • 9
    • 0033168375 scopus 로고    scopus 로고
    • The FF domain: A novel motif that often accompanies WW domains
    • Bedford, M. T. & Leder, P. (1999). The FF domain: A novel motif that often accompanies WW domains. Trends Biochem. Sci. 24, 264-265.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 264-265
    • Bedford, M.T.1    Leder, P.2
  • 10
    • 0030911051 scopus 로고    scopus 로고
    • Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals
    • Abovich, N. & Rosbach, M. (1997). Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals. Cell, 89, 403-412.
    • (1997) Cell , vol.89 , pp. 403-412
    • Abovich, N.1    Rosbach, M.2
  • 11
    • 0033634673 scopus 로고    scopus 로고
    • Functional recognition of the 5′ splice site by the U4/U6·U5 tri-snRNP defines a novel ATP-dependent step in early spliceosome assembly
    • Maroney, P. A., Romfo, C. M. & Nilsen, T. W. (2000). Functional recognition of the 5′ splice site by the U4/U6·U5 tri-snRNP defines a novel ATP-dependent step in early spliceosome assembly. Mol. Cell, 6, 317-328.
    • (2000) Mol. Cell , vol.6 , pp. 317-328
    • Maroney, P.A.1    Romfo, C.M.2    Nilsen, T.W.3
  • 12
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motif in signalling proteins with their cognate domains
    • Kay, B. M., Williamson, M. P. & Sudol, M. (2000). The importance of being proline: The interaction of proline-rich motif in signalling proteins with their cognate domains. FASEB J. 14, 231-241.
    • (2000) FASEB J. , vol.14 , pp. 231-241
    • Kay, B.M.1    Williamson, M.P.2    Sudol, M.3
  • 13
    • 0037154967 scopus 로고    scopus 로고
    • Integrating mRNA processing with transcription
    • Proudfoot, N. J., Furger, A. & Dye, M. J. (2002). Integrating mRNA processing with transcription. Cell, 108, 501-512.
    • (2002) Cell , vol.108 , pp. 501-512
    • Proudfoot, N.J.1    Furger, A.2    Dye, M.J.3
  • 14
    • 0037041395 scopus 로고    scopus 로고
    • An extensive network of coupling among gene expression machines
    • Maniatis, T. & Reed, R. (2002). An extensive network of coupling among gene expression machines. Nature, 416, 499-506.
    • (2002) Nature , vol.416 , pp. 499-506
    • Maniatis, T.1    Reed, R.2
  • 15
    • 0034617224 scopus 로고    scopus 로고
    • Rsp5 WW domains interact directly with the carboxyl-terminal domain of RNA polymerase II
    • Chang, A., Cheang, S., Espanel, X. & Sudol, M. (2000). Rsp5 WW domains interact directly with the carboxyl-terminal domain of RNA polymerase II. J. Biol. Chem. 275, 20562-20571.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20562-20571
    • Chang, A.1    Cheang, S.2    Espanel, X.3    Sudol, M.4
  • 16
    • 0034704145 scopus 로고    scopus 로고
    • The splicing factor, Prp40, binds the phosphorylated carboxyl-terminal domain of RNA polymerase II
    • Morris, D. P. & Greenleaf, A. L. (2000). The splicing factor, Prp40, binds the phosphorylated carboxyl-terminal domain of RNA polymerase II. J. Biol. Chem. 275, 39935-39943.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39935-39943
    • Morris, D.P.1    Greenleaf, A.L.2
  • 17
    • 0037138411 scopus 로고    scopus 로고
    • WW and SH3 domains, two different scaffolds to recognize proline-rich ligands
    • Macias, M. J., Wiesner, S. & Sudol, M. (2002). WW and SH3 domains, two different scaffolds to recognize proline-rich ligands. FEBS Letters, 513, 30-37.
    • (2002) FEBS Letters , vol.513 , pp. 30-37
    • Macias, M.J.1    Wiesner, S.2    Sudol, M.3
  • 18
    • 0029775570 scopus 로고    scopus 로고
    • Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide
    • Macias, M. J., Hyvonen, M., Baraldi, E., Schultz, J., Sudol, M., Saraste, M. & Oschkinat, H. (1996). Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide. Nature, 382, 646-649.
    • (1996) Nature , vol.382 , pp. 646-649
    • Macias, M.J.1    Hyvonen, M.2    Baraldi, E.3    Schultz, J.4    Sudol, M.5    Saraste, M.6    Oschkinat, H.7
  • 19
    • 0343081091 scopus 로고    scopus 로고
    • Stucture of a WW domain containing fragment of dystrophin in complex with β-dystroglycan
    • Huang, X., Poy, F., Zhang, R., Joachimiak, A., Sudol, M. & Eck, M. (2000). Stucture of a WW domain containing fragment of dystrophin in complex with β-dystroglycan. Nature Struct. Biol. 7, 634-638.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 634-638
    • Huang, X.1    Poy, F.2    Zhang, R.3    Joachimiak, A.4    Sudol, M.5    Eck, M.6
  • 20
    • 0035027506 scopus 로고    scopus 로고
    • Solution structure of a Nedd4 WW domain-ENaC peptide complex
    • Kanelis, V., Rotin, D. & Forman-Kay, J. D. (2001). Solution structure of a Nedd4 WW domain-ENaC peptide complex. Nature Struct. Biol. 8, 407-412.
    • (2001) Nature Struct. Biol. , vol.8 , pp. 407-412
    • Kanelis, V.1    Rotin, D.2    Forman-Kay, J.D.3
  • 21
    • 0035861991 scopus 로고    scopus 로고
    • Solution structures of the YAP65 WW domain and the variant L30K in complex with the peptides GTP-PPPYTVG, N-(n-octyl)-GPPPY and PLPPY and the application of peptide libraries reveal a minimal binding epitope
    • Pires, J. R., Taha-Nejad, F., Toepert, F., Ast, T., Hoffmuller, U., Schneider-Mergener, J. et al. (2001). Solution structures of the YAP65 WW domain and the variant L30K in complex with the peptides GTP-PPPYTVG, N-(n-octyl)-GPPPY and PLPPY and the application of peptide libraries reveal a minimal binding epitope. J. Mol. Biol. 314, 1147-1156.
    • (2001) J. Mol. Biol. , vol.314 , pp. 1147-1156
    • Pires, J.R.1    Taha-Nejad, F.2    Toepert, F.3    Ast, T.4    Hoffmuller, U.5    Schneider-Mergener, J.6
  • 22
    • 18344376699 scopus 로고    scopus 로고
    • Normalization of nomenclature for peptide motifs as ligands of modular protein domains
    • Aasland, R., Abrams, C., Ampe, C., Ball, L., Bedford, M. T., Cesareni, G. et al. (2002). Normalization of nomenclature for peptide motifs as ligands of modular protein domains. FEBS Letters, 513, 141-144.
    • (2002) FEBS Letters , vol.513 , pp. 141-144
    • Aasland, R.1    Abrams, C.2    Ampe, C.3    Ball, L.4    Bedford, M.T.5    Cesareni, G.6
  • 23
    • 0030910308 scopus 로고    scopus 로고
    • FBP WW domains and the Abl SH3 domain bind to a specific class of proline-rich ligands
    • Bedford, M. T., Chan, D. C. & Leder, P. (1997). FBP WW domains and the Abl SH3 domain bind to a specific class of proline-rich ligands. EMBO J. 16, 2376-2383.
    • (1997) EMBO J. , vol.16 , pp. 2376-2383
    • Bedford, M.T.1    Chan, D.C.2    Leder, P.3
  • 24
    • 0029981652 scopus 로고    scopus 로고
    • For-min binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains
    • Chan, D. C., Bedford, M. T. & Leder, P. (1996). For-min binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains. EMBO J. 15, 1045-1054.
    • (1996) EMBO J. , vol.15 , pp. 1045-1054
    • Chan, D.C.1    Bedford, M.T.2    Leder, P.3
  • 25
    • 0033885803 scopus 로고    scopus 로고
    • Structural basis for phosphoserine-proline recognition by group IV WW domains
    • Verdecia, M. A., Bowman, M. E., Lu, K. P., Hunter, T. & Noel, J. P. (2000). Structural basis for phosphoserine-proline recognition by group IV WW domains. Nature Struct. Biol. 7, 639-643.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 639-643
    • Verdecia, M.A.1    Bowman, M.E.2    Lu, K.P.3    Hunter, T.4    Noel, J.P.5
  • 26
    • 0040017910 scopus 로고    scopus 로고
    • Function of WW domains as phosphserine- or phosphothreonine-binding modules
    • Lu, P. J., Zhou, X. Z., Shen, M. S. & Lu, K. P. (1999). Function of WW domains as phosphserine- or phosphothreonine-binding modules. Science, 283, 1325-1328.
    • (1999) Science , vol.283 , pp. 1325-1328
    • Lu, P.J.1    Zhou, X.Z.2    Shen, M.S.3    Lu, K.P.4
  • 28
    • 0034061258 scopus 로고    scopus 로고
    • Towards an understanding of beta-sheet structures: Design of a prototype WW domain
    • Macias, M. J., Gervais, V., Civera, C. & Oschkinat, H. (2000). Towards an understanding of beta-sheet structures: Design of a prototype WW domain. Nature Struct. Biol. 7, 375-379.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 375-379
    • Macias, M.J.1    Gervais, V.2    Civera, C.3    Oschkinat, H.4
  • 29
    • 0007902080 scopus 로고    scopus 로고
    • NMR studies of tandem WW domains of Nedd4 in complex with a PY motif-containing region of the epithelial sodium channel
    • Kanelis, V., Farrow, N. A., Kay, L. E., Rotin, D. & Forman-Kay, J. D. (1998). NMR studies of tandem WW domains of Nedd4 in complex with a PY motif-containing region of the epithelial sodium channel. Biochem. Cell Biol. 76, 341-350.
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 341-350
    • Kanelis, V.1    Farrow, N.A.2    Kay, L.E.3    Rotin, D.4    Forman-Kay, J.D.5
  • 30
    • 0034048847 scopus 로고    scopus 로고
    • Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data
    • Dosset, P., Hus, J. C., Blackledge, M. & Marion, D. (2000). Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data. J. Biomol. NMR, 16, 23-28.
    • (2000) J. Biomol. NMR , vol.16 , pp. 23-28
    • Dosset, P.1    Hus, J.C.2    Blackledge, M.3    Marion, D.4
  • 31
    • 0033145058 scopus 로고    scopus 로고
    • Order matrix analysis of residual dipolar couplings using singular value decomposition
    • Losonczi, J. A., Andrec, M., Fischer, M. W. F. & Prestegard, J. H. (1999). Order matrix analysis of residual dipolar couplings using singular value decomposition. J. Magn. Reson. 138, 334-342.
    • (1999) J. Magn. Reson. , vol.138 , pp. 334-342
    • Losonczi, J.A.1    Andrec, M.2    Fischer, M.W.F.3    Prestegard, J.H.4
  • 32
    • 0034884233 scopus 로고    scopus 로고
    • A novel interactive tool for rigid-body modeling of multi-domain macromolecules using residual dipolar couplings
    • Dosset, P., Hus, J. C., Marion, D. & Blackledge, M. (2001). A novel interactive tool for rigid-body modeling of multi-domain macromolecules using residual dipolar couplings. J. Biomol. NMR, 20, 223-231.
    • (2001) J. Biomol. NMR , vol.20 , pp. 223-231
    • Dosset, P.1    Hus, J.C.2    Marion, D.3    Blackledge, M.4
  • 34
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R. & Thornton, J. M. (1996). AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR, 8, 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 35
    • 0037138362 scopus 로고    scopus 로고
    • EVH1 domains: Structure, function and interactions
    • Ball, L. J., Jarchau, T., Oschkinat, H. & Walter, U. (2002). EVH1 domains: Structure, function and interactions. FEBS Letters, 513, 45-52.
    • (2002) FEBS Letters , vol.513 , pp. 45-52
    • Ball, L.J.1    Jarchau, T.2    Oschkinat, H.3    Walter, U.4
  • 36
    • 0025079058 scopus 로고
    • Tails of RNA polymerase II
    • Corden, J. L. (1990). Tails of RNA polymerase II. Trends Biochem. Sci. 15, 383-387.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 383-387
    • Corden, J.L.1
  • 37
    • 0029760928 scopus 로고    scopus 로고
    • Reversible phosphorylation of the C-terminal domain of RNA polymerase II
    • Dahmus, M. E. (1996). Reversible phosphorylation of the C-terminal domain of RNA polymerase II. J. Biol. Chem. 271, 19009-19012.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19009-19012
    • Dahmus, M.E.1
  • 38
    • 0030869754 scopus 로고    scopus 로고
    • Interaction of WW domains with hematopoetic transcription factor p45/NF-E2 and RNA polymerase II
    • Gavva, N. R., Gavva, R., Ermekova, K., Sudol, M. & Shen, C. J. (1997). Interaction of WW domains with hematopoetic transcription factor p45/NF-E2 and RNA polymerase II. J. Biol. Chem. 272, 24105-24108.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24105-24108
    • Gavva, N.R.1    Gavva, R.2    Ermekova, K.3    Sudol, M.4    Shen, C.J.5
  • 39
    • 0035670548 scopus 로고    scopus 로고
    • Genetic interactions between the ESS1 prolyl-isomerase and the RSP5 ubiquitin ligase reveal opposing effects on RNA polymerase II function
    • Wu, X., Chang, A., Sudol, M. & Hanes, S. D. (2001). Genetic interactions between the ESS1 prolyl-isomerase and the RSP5 ubiquitin ligase reveal opposing effects on RNA polymerase II function. Curr. Genet. 40, 234-242.
    • (2001) Curr. Genet. , vol.40 , pp. 234-242
    • Wu, X.1    Chang, A.2    Sudol, M.3    Hanes, S.D.4
  • 40
    • 0033615705 scopus 로고    scopus 로고
    • Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3′-end formation
    • Morris, D. P., Phatnani, H. P. & Greenleaf, A. L. (1999). Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3′-end formation. J. Biol. Chem. 274, 31583-31587.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31583-31587
    • Morris, D.P.1    Phatnani, H.P.2    Greenleaf, A.L.3
  • 41
    • 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. (1999). Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog. NMR Spectrosc. 34, 93-158.
    • (1999) Prog. NMR Spectrosc. , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 42
    • 0028545648 scopus 로고
    • Measurement of HN-Hα J-couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods
    • Kubinowa, H., Grzesiek, S., Delaglio, F. & Bax, A. (1994). Measurement of HN-Hα J-couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods. J. Biomol. NMR, 4, 871-878.
    • (1994) J. Biomol. NMR , vol.4 , pp. 871-878
    • Kubinowa, H.1    Grzesiek, S.2    Delaglio, F.3    Bax, A.4
  • 43
    • 0031111521 scopus 로고    scopus 로고
    • NCγ couplings in isotopically enriched proteins
    • NCγ couplings in isotopically enriched proteins. J. Biomol. NMR, 9, 323-328.
    • (1997) J. Biomol. NMR , vol.9 , pp. 323-328
    • Hu, J.1    Bax, A.2
  • 44
    • 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. & Sorensen, O. W. (1999). Pulse sequences for measurement of one-bond (15)N-(1)H coupling constants in the protein backbone. J. Magn. Reson. 140, 259-263.
    • (1999) J. Magn. Reson. , vol.140 , pp. 259-263
    • Lerche, M.H.1    Meissner, A.2    Poulsen, F.M.3    Sorensen, O.W.4
  • 45
    • 0032113480 scopus 로고    scopus 로고
    • A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information
    • Clore, G. M. & Gronenborn, A. M. (1998). A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information. J. Magn. Reson. 133, 216-221.
    • (1998) J. Magn. Reson. , vol.133 , pp. 216-221
    • Clore, G.M.1    Gronenborn, A.M.2
  • 47
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J. & Bax, A. (1995). NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR, 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 48
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels, C., Xia, T.-H., Billeter, M., Güntert, P. & Wüthrich, K. (1995). The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR, 5, 1-10.
    • (1995) J. Biomol. NMR , vol.5 , pp. 1-10
    • Bartels, C.1    Xia, T.-H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 49
    • 34249765651 scopus 로고
    • NMRView: A computer-program for the visualization and analysis of NMR data
    • Johnson, B. A. & Blevins, R. A. (1994). NMRView: A computer-program for the visualization and analysis of NMR data. J. Biomol. NMR, 4, 603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 51
    • 0031110495 scopus 로고    scopus 로고
    • Floating stereospecific assignment revisited: Application to an 18 kDa protein and comparison with J-coupling data
    • Folmer, R. H., Hilbers, C. W., Konings, R. N. & Nilges, M. (1997). Floating stereospecific assignment revisited: Application to an 18 kDa protein and comparison with J-coupling data. J. Biomol. NMR, 9, 245-258.
    • (1997) J. Biomol. NMR , vol.9 , pp. 245-258
    • Folmer, R.H.1    Hilbers, C.W.2    Konings, R.N.3    Nilges, M.4
  • 52
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for protein chemical shifts and sequence homology
    • Cornilescu, G., Delaglio, F. & Bax, A. (1999). Protein backbone angle restraints from searching a database for protein chemical shifts and sequence homology. J. Biomol. NMR, 13, 289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 53
    • 0347988396 scopus 로고    scopus 로고
    • Ambiguous NOEs and automated NOE assignment
    • Nilges, M. & O'Donoghue, S. I. (1998). Ambiguous NOEs and automated NOE assignment. Prog. NMR Spectrosc. 32, 107-139.
    • (1998) Prog. NMR Spectrosc. , vol.32 , pp. 107-139
    • Nilges, M.1    O'Donoghue, S.I.2
  • 55
    • 0031574072 scopus 로고    scopus 로고
    • The CLU-STAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F. & Higgins, D. G. (1997). The CLU-STAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucl. Acids Res. 25, 4876-4882.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 56
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis macromolecular structures
    • Koradi, R., Billeter, M. & Wüthrich, K. (1996). MOLMOL: A program for display and analysis macromolecular structures. J. Mol. Graphics, 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 57
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of portein-ligand interactions
    • Wallace, A. C., Laskowski, R. A. & Thornton, J. M. (1995). LIGPLOT: A program to generate schematic diagrams of portein-ligand interactions. Protein Eng. 8, 127-134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.