SEARCH

SEARCH BY CITATION

REFERENCES

  • 1
    Hill AA, Hunter CP, Tsung BT, Tucker-Kellog G, Brown EL. Genomic analysis of gene expression in C. elegans. Science 2000; 290: 809812.
  • 2
    Jansson M, Li Y-C, Jendeberg L, Anderson S, Montelione GT, Nilsson B. High level production of uniformly 15N- and 13C-enriched fusion proteins in Escherichia coli containing (15NH4)2SO4 and 13C6-glucose as sole nitrogen and carbon sources. J Biomol NMR 1996; 7: 131141.
  • 3
    Zhang O, Kay LE, Olivier JP, Forman-Kay JD. Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J Biomol NMR 1994; 4: 845858.
  • 4
    Vuister GW, Bax A. Quantitative J correlation: a new approach for measuring homonuclear three-bond J(HNHα) coupling constants in 15N-enriched proteins. J Am Chem Soc 1993; 115: 77727777.
  • 5
    Muhandiram DR, Kay LE. Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity. J Magn Reson B 1994; 103: 203216.
  • 6
    Kay LE. Pulsed-field gradient-enhanced three-dimensional NMR experiment for correlating 13Cα/β, 13C′, and 1Hα chemical shift in uniformly 13C-labeled proteins dissolved in H2O. J Am Chem Soc 1993; 115: 20552057.
  • 7
    Montelione GT, Lyons BA, Emerson SD, Tashiro M. An efficient triple resonance experiment using carbon-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically enriched proteins. J Am Chem Soc 1992; 114: 1097410975.
  • 8
    Lyons BA, Montelione GT. An HCCNH triple-resonance experiment using carbon-13 isotropic mixing for correlating backbone amide and side-chain aliphatic resonances in isotopically enriched proteins. J Magn Reson B 1993; 101: 206209.
  • 9
    Grzesiek S, Anglister J, Bax A. Correlation of backbone amide and aliphatic side-chain resonances in 13C/15N-enriched proteins by isotropic mixing of 13C magnetization. J Magn Reson B 1993; 101: 114119.
  • 10
    Logan TM, Olejniczak ET, Xu RX, Fesik SW. A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments. J Biomol NMR 1993; 3: 225231.
  • 11
    Pascal SM, Muhandiram DR, Yamazaki T, Forman-Kay JD, Kay LE. Simultaneous acquisition of 15N- and 13C-edited NOE spectra of proteins dissolved in H2O. J Magn Res B 1994; 103: 197201.
  • 12
    Vuister GW, Clore GM, Gronenborn AM, Powers R, Garrett DS, Tschudin R, Bax A. Increased resolution and improved spectral quality in 4-dimensional 13C/13C-separated HMQC-NOESY-HMQC spectra using pulsed field gradients. J Magn Reson B 1993; 101: 210213.
  • 13
    Neri D, Szyperski T, Otting G, Senn H, Wütrich K. 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 13C labeling. Biochemistry 1989; 28: 75107516.
  • 14
    Brünger AT. X-PLOR Version 3.1. A system for X-ray crystallography and NMR. New Haven, CT: Yale University Press; 1992.
  • 15
    Holm L, Sander C. Touring protein fold space with Dali/FSSP. Nucleic Acids Res 1998; 26: 316319.
  • 16
    Ecker DJ, Butt TR, Marsh J, Sternberg EJ, Margolis N, Monia BP, Jonnalagadda S, Khan MI, Weber PL, Mueller L, Crooke ST. Gene synthesis, expression, structures, and functional activities of site-specific mutants of ubiquitin. J Biol Chem 1987; 262: 1421314221.
  • 17
    Sloper-Mould KE, Jemc JC, Pickart CM, Hicke L. Distinct functional surface regions on ubiquitin. J Biol Chem 2001; 276: 3048330489.
  • 18
    Lake MW, Wuebbens MM, Rajagopalan KV, Schindelin H. Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Nature 2001; 414: 325329.
  • 19
    Hochstrasser M. All in the ubiquitin family. Science 2000; 289: 563564.
  • 20
    Laskowski RA, Rullmann JAC, MacArthur MW, Kaptein R, Thornton JM. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 1996; 8: 477486.
  • 21
    Kraulis PJ. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 1991; 24: 946950.