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Volumn 36, Issue SUPPL. 1, 2008, Pages

BioMagResBank

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE; CARBON 13; HYDROGEN; LIGAND; NUCLEIC ACID; PEPTIDE DERIVATIVE; PROTEIN DERIVATIVE;

EID: 38549138986     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkm957     Document Type: Article
Times cited : (1414)

References (39)
  • 3
    • 0033578363 scopus 로고    scopus 로고
    • The 3D NOESY-[H-1,N-15,H-1]-ZQ-TROSY NMR experiment with diagonal peak suppression
    • Pervushin, K.V., Wider, G., Riek, R. and Wüthrich, K. (1999) The 3D NOESY-[H-1,N-15,H-1]-ZQ-TROSY NMR experiment with diagonal peak suppression. Proc. Natl Acad. Sci. USA, 96, 9607-9612:
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 9607-9612
    • Pervushin, K.V.1    Wider, G.2    Riek, R.3    Wüthrich, K.4
  • 4
    • 0024572653 scopus 로고
    • Creation of a nuclear magnetic resonance data repository and literature database
    • Ulrich, E.L., Markley, J.L. and Kyogoku, Y. (1989) Creation of a nuclear magnetic resonance data repository and literature database. Prot. Seq. Data Anal., 2, 23-37.
    • (1989) Prot. Seq. Data Anal , vol.2 , pp. 23-37
    • Ulrich, E.L.1    Markley, J.L.2    Kyogoku, Y.3
  • 5
    • 0026223896 scopus 로고
    • A relational database for sequence-specific protein NMR data
    • Seavey, B.R., Farr, E.A., Westler, W.M. and Markley, J.L. (1991) A relational database for sequence-specific protein NMR data. J. Biomol. NMR, 1, 217-236.
    • (1991) J. Biomol. NMR , vol.1 , pp. 217-236
    • Seavey, B.R.1    Farr, E.A.2    Westler, W.M.3    Markley, J.L.4
  • 8
    • 24344440618 scopus 로고    scopus 로고
    • Probabilistic identification of spin systems and their assignments including coil-helix inference as output (PISTACHIO)
    • Eghbalnia, H.R., Bahrami, A., Wang, L., Assadi, A. and Markley, J.L. (2005) Probabilistic identification of spin systems and their assignments including coil-helix inference as output (PISTACHIO). J. Biomol. NMR, 32, 219-233.
    • (2005) J. Biomol. NMR , vol.32 , pp. 219-233
    • Eghbalnia, H.R.1    Bahrami, A.2    Wang, L.3    Assadi, A.4    Markley, J.L.5
  • 9
    • 0034923123 scopus 로고    scopus 로고
    • Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data
    • Moseley, H.N., Monleon, D. and Montelione, G.T. (2001) Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data. Meth. Enzymol., 339 91-108.
    • (2001) Meth. Enzymol , vol.339 , pp. 91-108
    • Moseley, H.N.1    Monleon, D.2    Montelione, G.T.3
  • 10
    • 0000714031 scopus 로고    scopus 로고
    • Automated sequence-specific NMR assignment of homologous proteins using the program GARANT
    • Bartels, C., Billeter, M., Güntert, P. and Wüthrich, K. (1996) Automated sequence-specific NMR assignment of homologous proteins using the program GARANT. J. Biomol. NMR, 7, 207-213.
    • (1996) J. Biomol. NMR , vol.7 , pp. 207-213
    • Bartels, C.1    Billeter, M.2    Güntert, P.3    Wüthrich, K.4
  • 11
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann, T., Güntert, P. and Wüthrich, K. (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol., 319, 209-227.
    • (2002) J. Mol. Biol , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 12
    • 33749524593 scopus 로고    scopus 로고
    • Automated protein structure determination from NMR spectra
    • Lopez-Mendez, B. and Güntert, P. (2006) Automated protein structure determination from NMR spectra. J. Am. Chem. Soc., 128, 13112-13122.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 13112-13122
    • Lopez-Mendez, B.1    Güntert, P.2
  • 13
  • 14
    • 0031851289 scopus 로고    scopus 로고
    • New technique in structural NMR - anisotropic interactions
    • Prestegard, J.H. (1998) New technique in structural NMR - anisotropic interactions. Nat. Struct. Biol., 5, 517-522.
    • (1998) Nat. Struct. Biol , vol.5 , pp. 517-522
    • Prestegard, J.H.1
  • 16
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • Tjandra, N. and Bax, A. (1997). Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science, 278, 1111-1114.
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 18
    • 1442306656 scopus 로고    scopus 로고
    • Assignment validation, software suite for the evaluation and presentation of protein resonance assignment data
    • Moseley, H.N., Sahota, G. and Montelione, G.T. (2004) Assignment validation, software suite for the evaluation and presentation of protein resonance assignment data. J. Biomol. NMR, 28, 341-355.
    • (2004) J. Biomol. NMR , vol.28 , pp. 341-355
    • Moseley, H.N.1    Sahota, G.2    Montelione, G.T.3
  • 19
    • 23144462958 scopus 로고    scopus 로고
    • Linear analysis of carbon-13 chemical shift differences and its application to the detection and correction of errors in referencing and spin system identifications
    • Wang, L., Eghbalnia, H.R., Bahrami, A. and Markley, J.L. (2005) Linear analysis of carbon-13 chemical shift differences and its application to the detection and correction of errors in referencing and spin system identifications. J. Biomol NMR, 32, 13-22.
    • (2005) J. Biomol NMR , vol.32 , pp. 13-22
    • Wang, L.1    Eghbalnia, H.R.2    Bahrami, A.3    Markley, J.L.4
  • 20
    • 0001078409 scopus 로고
    • The STAR File: A new format for electronic data transfer and archiving
    • Hall, S.R. (1991) The STAR File: A new format for electronic data transfer and archiving. J. Chem. Inf. Comput. Sci., 31, 326-333.
    • (1991) J. Chem. Inf. Comput. Sci , vol.31 , pp. 326-333
    • Hall, S.R.1
  • 21
  • 22
    • 0006747152 scopus 로고
    • STAR dictionary definition language: Initial specification
    • Hall, S.R. and Cook, A.P.F. (1995) STAR dictionary definition language: initial specification. J. Chem. Inf. Comput. Sci., 35, 819-825.
    • (1995) J. Chem. Inf. Comput. Sci , vol.35 , pp. 819-825
    • Hall, S.R.1    Cook, A.P.F.2
  • 24
    • 0034020917 scopus 로고    scopus 로고
    • STAR/mmCIF: An extensive ontology for macromolecular structure and beyond
    • Westbrook, J.D. and Bourne, P.E. (2000) STAR/mmCIF: An extensive ontology for macromolecular structure and beyond. Bioinformatics, 16, 159-168.
    • (2000) Bioinformatics , vol.16 , pp. 159-168
    • Westbrook, J.D.1    Bourne, P.E.2
  • 27
    • 0026410969 scopus 로고
    • Relationship between Nuclear Magnetic Resonance chemical shift and protein secondary structure
    • Wishart, D.S., Sykes, B.D. and Richards, F.M. (1991) Relationship between Nuclear Magnetic Resonance chemical shift and protein secondary structure. J. Mol. Biol., 222, 311-333.
    • (1991) J. Mol. Biol , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 28
    • 0028393784 scopus 로고
    • The 13C chemical-shift index: A simple method for the identification of protein secondary structure using 13C chemical shift data
    • Wishart, D.S. and Sykes, B.D. (1994) The 13C chemical-shift index: A simple method for the identification of protein secondary structure using 13C chemical shift data. J. Biomol. NMR, 4, 171-180.
    • (1994) J. Biomol. NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 29
    • 23144441604 scopus 로고    scopus 로고
    • BioMagResBank databases DOCR and FRED containing converted and filtered sets of experimental NMR restraints and coordinates from over 500 protein PDB structures
    • Doreleijers, J.F., Nederveen, A., Vranken, W., Lin, J., Bonvin, A.M.J.J., Kaptein, R., Markley, J.L. and Ulrich, E.L. (2003) BioMagResBank databases DOCR and FRED containing converted and filtered sets of experimental NMR restraints and coordinates from over 500 protein PDB structures. J. Biomol. NMR, 32, 1-12.
    • (2003) J. Biomol. NMR , vol.32 , pp. 1-12
    • Doreleijers, J.F.1    Nederveen, A.2    Vranken, W.3    Lin, J.4    Bonvin, A.M.J.J.5    Kaptein, R.6    Markley, J.L.7    Ulrich, E.L.8
  • 30
    • 0037986814 scopus 로고    scopus 로고
    • BioMagResBank database with sets of experimental NMR constraints corresponding to the structures of over 1400 biomolecules deposited in the Protein Data Bank
    • Doreleijers, J.F., Mading, S., Maziuk, D., Sojourner, K., Yin, L., Zhu, J., Markley, J.L. and Ulrich, E.L. (2003) BioMagResBank database with sets of experimental NMR constraints corresponding to the structures of over 1400 biomolecules deposited in the Protein Data Bank. J. Biomol. NMR, 26, 139-146.
    • (2003) J. Biomol. NMR , vol.26 , pp. 139-146
    • Doreleijers, J.F.1    Mading, S.2    Maziuk, D.3    Sojourner, K.4    Yin, L.5    Zhu, J.6    Markley, J.L.7    Ulrich, E.L.8
  • 32
    • 33645795710 scopus 로고    scopus 로고
    • Comparison of different torsion angle approaches for NMR structure determination
    • Bardiaux, B., Malliavin, T.E., Nilges, M. and Mazur, A.K. (2006) Comparison of different torsion angle approaches for NMR structure determination. J. Biomol. NMR, 34, 153-166.
    • (2006) J. Biomol. NMR , vol.34 , pp. 153-166
    • Bardiaux, B.1    Malliavin, T.E.2    Nilges, M.3    Mazur, A.K.4
  • 34
    • 33646041930 scopus 로고    scopus 로고
    • TASSER-based refinement of NMR structures
    • Lee, S.Y., Zhang, Y. and Skolnick, J. (2006) TASSER-based refinement of NMR structures. Proteins, 63, 451-456.
    • (2006) Proteins , vol.63 , pp. 451-456
    • Lee, S.Y.1    Zhang, Y.2    Skolnick, J.3
  • 35
    • 34748821686 scopus 로고    scopus 로고
    • Programmed ribosomal frameshifting in SIV is induced by a highly structured RNA stem-loop
    • Marcheschi, R.J., Staple, D.W. and Butcher, S.E. (2007) Programmed ribosomal frameshifting in SIV is induced by a highly structured RNA stem-loop. J. Mol. Biol., 26, 652-663.
    • (2007) J. Mol. Biol , vol.26 , pp. 652-663
    • Marcheschi, R.J.1    Staple, D.W.2    Butcher, S.E.3
  • 36
    • 14344256801 scopus 로고    scopus 로고
    • Cell-free protein production and labeling protocol for NMR-based structural proteomics
    • Vinarov, D.A., Lytle, B.L., Peterson, F.C., Tyler, E., Volkman, B.F. and Markley, J.L. (2004) Cell-free protein production and labeling protocol for NMR-based structural proteomics. Nat. Methods, 1, 149-153.
    • (2004) Nat. Methods , vol.1 , pp. 149-153
    • Vinarov, D.A.1    Lytle, B.L.2    Peterson, F.C.3    Tyler, E.4    Volkman, B.F.5    Markley, J.L.6
  • 37
    • 8744267531 scopus 로고    scopus 로고
    • Lytle, B.L., Peterson, F.C., Qui, S.H., Luo, M., Zhao, Q., Markley, J.L. and Volkman, B.F, (2004) Solution structure of a ubiquitin-like domain of tubulin-folding cofactor B. J. Biol. Chem., 279, 46787-46793.
    • Lytle, B.L., Peterson, F.C., Qui, S.H., Luo, M., Zhao, Q., Markley, J.L. and Volkman, B.F, (2004) Solution structure of a ubiquitin-like domain of tubulin-folding cofactor B. J. Biol. Chem., 279, 46787-46793.


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