1. Lee, D., Oh, E.-S., Woods, A., Couchman, J.R., Lee, W., Solution structure of a syndecan-4 cytoplasmic domain and its interaction with phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 1998, 273, 13022-13029.
  2. Lee, J.-H., Lim, S.-K., Huh, S.-H., Lee, D., Lee, W., Solution structures of the melanocyte stimulating hormones by two-dimensional NMR Spectroscopy and dynamical simulated annealing calculations. Eur. J. Biochem. 1998, 257, 31-40.
  3. Lee, D., Lee, W., An influence of the exchange rate on NOE intensities of a ligand: application to 37 kDa Trp-holo-repressor/operator DNA complex. J. Kor. Magn. Reson. Soc. 1998, 2, 33-40.
  4. Cho, H.-S., Ha, N.-C., Choi, G., Kim, H.-J., Lee, D., Oh, K.S., Kim, K.S., Lee, W., Choi, K.W., Oh, B.-H., Crystal structure of Δ5-3-ketosteroid isomerase from Pseudomonas testosteroni in complex with equilenin settles the correct hydrogen bonding scheme for transition state stabilization. J. Biol. Chem. 1999, 274, 32863-32868.
  5. Shin, J., Lee, W., Lee, D., Koo, B.-K., Lim, Y., Woods, A., Couchman, J.R., Oh, E.-S., Solution structure of the dimeric cytoplasmic domain of syndecan-4. Biochemistry 2001, 40, 8471-8478.
  6. Lee, D., Damberger, F.F., Peng, G., Horst, R., Güntert, P., Nikonova, L., Leal, W.S., Wüthrich, K., NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH. FEBS Lett. 2002, 531, 314-318.
  7. Bromek, K., Lee, D., Hauhart, R., Krych-Goldberg, M., Atkinson, J.P., Barlow, P.N., Pervushin, K., Polychromatic selective population inversion for TROSY experiments with large proteins.  J. Am. Chem. Soc. 2005, 127, 405-411.
  8. Lee, D., Vögeli, B., Pervushin K., Detection of C’,Cα correlations in proteins using a new time- and sensitivity-optimal experiment. J. Biomol. NMR 2005, 31, 273-278.
  9. Lee, D., Pervushin, K., Bischof, D., Braun, M., Thöny-Meyer, L., Unusual heme-histidine bond in the active site of a chaperone. J. Am. Chem. Soc. 2005, 127, 3716-3717.
  10. Lee, D., Hilty, C., Wider, G., Wüthrich, K., Effective rotational correlation times of proteins from NMR relaxation interference. J. Magn. Reson. 2006, 178, 72-76.
  11. Lee, D., Walsh, J.D., Mikhailenko, I., Yu, P., Migliorini, M., Wu, Y., Krueger, S., Curtis, J.E., Harris, B., Lockett, S., Blacklow, S.C., Strickland, D.K., Wang, Y.-X., RAP uses a histidine switch to regulate its interaction with LRP in the ER and Golgi. Mol. Cell 2006, 22, 423-430.
  12. Walsh, J.D., Lee, D., Migliorini, M., Yu, P., Strickland, D.K., Wang, Y.-X., NMR assignment of domain 2 of receptor-associated protein. J. Biomol. NMR 2006, 36, S5, 54.
  13. Lee, D., Walsh, J.D., Migliorini, M., Yu, P., Strickland, D.K., Wang, Y.-X., NMR assignments of domain 3 of receptor-associated protein (RAP). J. Biomol. NMR 2006, 36, S5, 56.
  14. Reiter, N.J, Lee, D., Wang, Y.-X., Tonelli, M., Bahrami, A., Cornilescu, C.C., Butcher, S.E., Resonance assignments for the two N-terminal RNA recognition motifs (RRM) of the S. cerevisiae Pre-mRNA Processing Protein Prp24. J. Biomol. NMR 2006, 36, S5, 58.
  15. Lee, D., Walsh, J.D., Yu, P., Markus, M.A., Choli-Papadopoulou, T., Schwieters, C.D., Krueger, S., Draper, D.E., Wang, Y.-X., The structure of free L11 and functional dynamic of L11 in free, L11-rRNA(58nt) binary and L11-rRNA(58nt)-thiostrepton ternary complexes. J. Mol. Biol. 2007, 367, 1007-1022.
  16. Bae, E., Reiter, N.J, Bingman, C.A., Kwan, S., Lee, D., Philips, G.N. Jr., Butcher, S.E., Brow, D.A., Structure and interactions of the first three RNA recognition motifs of splicing factor Prp24. J. Mol. Biol. 2007, 367, 1447-1458.
  17. Lee, D., Walsh, J.D., Migliorini, M., Yu, P., Cai, T., Schwieters, C.D., Krueger, S., Strickland, D.K., Wang, Y.-X., The structure of receptor-associated protein (RAP). Protein Sci. 2007, 16, 1628-1640.
  18. Lee, D., Walter, K.F.A., Brückner, A.-K., Hilty, C., Becker, S., Griesinger, C., Bilayer in small bicelles revealed by lipid-protein interactions using NMR spectroscopy. J. Am. Chem. Soc. 2008, 130, 13822-13823.
  19. Schmidt, H., Himmel, S., Walter, K.F.A., Klaukien, V., Funk, M., Lee, D., Transverse relaxation-optimized HCN experiment for tautomeric states of histidine sidechains. J. Kor. Magn. Reson. Soc. 2008, 12, 89-95.
  20. Lee, D., Vijayan, V., Montaville, P., Becker, S., Griesinger, C., Sensitivity enhancement of methyl-TROSY by longitudinal 1H relaxation optimization. J. Kor. Magn. Reson. Soc. 2009, 13, 15-26.
  21. Rodriguez-Castaneda, F., Maestre-Martinez, M., Coudevylle, N., Dimova, K., Junge, H., Lipstein, N., Lee, D., Becker, S., Brose, N., Jahn, O., Carlomagno, T., Griesinger, C., Modular architecture of the Munc13-1/calmodulin complex enables short-term plasticity. EMBO J. 2010, 29, 680-691.
  22. Dervillez, X., Klaukien, V., Dürr, R., Koch, J., Kreutz, A., Haarmann, T., Stoll, M., Lee, D., Carlomagno, T., Schnierle, B., Königs, C., Griesinger, C., Dietrich, U., Peptide ligands targeting CD4-induced epitopes on native HIV-1 gp120 mimic CCR5 domains and inhibit HIV-1 entry. J. Virol. 2010, 84, 10131-10138.
  23. Himmel, S., Wolff, S., Becker, S., Lee, D., Griesinger, C., Detection and identification of protein-phosphorylation sites in histidines through HNP correlation patterns. Angew. Chem. Int. Ed. 2010, 49, 8971-8974.
  24. Michel, E., Damberger, F.F., Ishida, Y., Fiorito, F., Lee, D., Leal, W.S., Wüthrich, K., Dynamic conformational equilibria in the physiological function of the Bombyx mori pheromone-binding protein. J. Mol. Biol. 2011, 408, 922-931.
  25. Fenwick, R.B., Esteban-Martin, S., Richter, B., Lee, D., Walter, K.F.A, Milovanovic, D., Becker, S., Lakomek, N.-A., Griesinger, C., Salvatella, X., Weak long-range correlated motions in a surface patch of ubiquitin involved in molecular recognition. J. Am. Chem. Soc. 2011, 133, 10336-10339.   
  26. Ban, D., Funk, M. Gulich, R., Egger, D., Sabo, T.M., Walter, K.F.A., Fenwick, R.B., Giller, K., Pichierri, F., de Groot, B.L., Lange, O.F., Grubmüller, H., Salvatella, X., Wolf, M., Loidl, A., Kree, R., Becker, S., Lakomek, N.-A., Lee, D., Lunkenheimer, P., Griesinger, C., Kinetics of conformational sampling in ubiquitin. Angew. Chem. Int. Ed. 2011, 50, 11437-11440.   
  27. Sabo, T.M., Bakhtiari, D., Walter, K.F.A., McFeeters, R.L., Giller, K., Becker, S., Griesinger, C., Lee, D., Thermal coefficients of the methyl groups within ubiquitin. Protein Sci. 2012, 21, 562-570. 
  28. Lee, Y., Zeng, H., Mazur, A., Wegstroth, M., Carlomagno, T., Reese, M., Lee, D., Becker, S., Griesinger C., Hilty, C., Hyperpolarized binding Pocket NOE for determination of competitive ligand binding. Angew. Chem. Int. Ed. 2012,  51, 5179-5182.
  29. Meirovitch, E., Lee, D., Walter, K.F.A., Griesinger, C., Standard tensorial analysis of local ordering in proteins from residual dipolar couplings. J. Phys. Chem. B. 2012,  116, 6106-6117.
  30. Ban, D., Gossert, A.D., Giller, K., Becker, S., Griesinger, C., Lee, D., Exceeding the limit of dynamics studies on biomolecules using high spin-lock field strengths with a cryogenically cooled probehead. J. Magn. Reson. 2012, 221, 1-4.
  31. Himmel, S., Zschiedrich, C., Becker, S., Hsiao, H.-H., Wolff, S., Diethmaier, C., Urlaub, H., Lee, D., Griesinger, C., Stülke, J., Determinants of interaction specificity of the Bacillus subtilis GlcT antitermination protein: Functionality and phosphorylation specificity depend on the arrangement of the regulatory domains. J. Biol. Chem. 2012, 287, 27731-27742.
  32. Mazur, A., Hammesfahr, B., Griesinger, C., Lee, D., Kollmar, M., ShereKhan - Calculating exchange parameters in relaxation dispersion data from CPMG experiments. Bioinformatics 2013, 29, 1819-1820.
  33. Ban, D., Mazur, A., Carneiro, M.G., Sabo, T.M., Giller, K., Koharudin, L.M.I., Becker, S., Gronenborn, A.M., Griesinger, C., Lee, D., Enhanced accuracy of kinetic information from CT-CPMG experiments by transverse rotating-frame spectroscopy. J. Biomol. NMR 2013, 57, 73-82.
  34. Ban, D., Sabo, T.M., Griesinger, C., Lee, D., Measuring dynamic and kinetic information in the previously inaccessible supra-tc window of nanoseconds to microseconds by solution NMR spectroscopy. Molecules 2013, 18, 11904-11937. 
  35. Sabo, T.M., Smith, C.A., Ban, D., Mazur, A., Lee, D., Griesinger, C.: ORIUM: Optimized RDC-based iterative and unified model-free analysis. J. Biomol. NMR  2014, 58, 287-301.

  36. Bibow, S., Carneiro, M.G., Sabo, T.M., Schwiegk, C., Becker, S., Riek, R., Lee, D.: Measuring membrane protein bond orientations in nanodics via residual dipolar couplings. Protein Sci. 2014, 23, 851-856.

  37. Edwards, L.J., Savostyanov, D.V., Welderufael, Z.T., Lee, D., Kuprov, I.: Quantum mechanical NMR simulation algorithm for protein-size spin systems. J. Magn. Reson. 2014, 243, 107-113.

  38. Michielssens, S., Peters, J.H., Ban, D., Pratihar, S., Seeliger, D., Sharma, M., Giller, K., Sabo, T.M., Becker, S., Lee, D., Griesinger, C., de Groot, B.L.: A designed conformational shift to control protein binding specificity. Angew. Chem. Int. Ed. 2014, 53, 10367-10371.

  39. Smith, C.A., Ban, D., Pratihar, S., Giller, K., Schwiegk, C., de Groot, B.L., Becker, S., Griesinger, C., Lee, D.: Population shuffling of protein conformations. Angew. Chem. Int. Ed. 2015, 54, 207-210.

  40. Kim, D.H., Lee, C., Cho, Y.J., Lee, S.H., Cha, E.J., Lim, J.E., Sabo, T.M., Griesinger, C., Lee, D., Han, K.H.: A pre-structured helix in the intrinsically disordered 4EBP1. Mol. Biosyst. 2015, 11, 366-369.

  41. Carneiro, M.G., Koharudin, L.M.I., Griesinger, C., Gronenborn, A.M., Lee, D.: 1H, 13C and 15N resonance assignment of the anti-HIV lectin from Oscillatoria agardhiiBiomol. NMR Assign2015, 9, 317-319.

  42. Carneiro, M.G., Koharudin, L.M.I., Ban, D., Sabo, T.M., Trigo-Mourino P., Mazur, A., Griesinger, C., Gronenborn, A.M., Lee, D.*: Sampling of glycan-bound conformers by the anti-HIV lectin Oscillatoria agardhii agglutinin in the absence of sugar. Angew. Chem. Int. Ed. 2015, 54, 6462-6465.

  43. Pilger, J., Mazur, A., Monecke, P., Schreuder, H., Elshorst, B., Bartoschek, S., Langer, T., Schiffer, A., Krimm, I., Wegstroth, M., Lee, D., Hessler, G., Wendt, K.U., Becker, S., Griesinger, C.: A Combination of spin diffusion methods for the determination of protein-ligand complex structural ensembles. Angew. Chem. Int. Ed.  2015, 54, 6511-6515.

  44. Sabo, T.M., Trent, J.O., Lee, D.: Population shuffling between ground and high energy excited states. Protein Sci. 2015, 24, 1714-1719.

  45. Carneiro, M.G., Reddy, J.G., Griesinger, C., Lee, D.: Speeding-up exchange-mediated saturation transfer experiments by Fourier transform. J. Biomol. NMR  2015, 63, 237-244.

  46. Smith, C.A., Ban, D., Pratihar, S., Giller, K., Paulat, M., Becker, S., Griesinger, C., Lee, D., de Groot, B.L.: Allosteric switch regulates protein-protein binding through collective motion. Proc. Nat. Acad. Sci.  2016, 113, 3269-3274.

  47. Chakrabarti, K.S., Ban, D., Partihar, S., Reddy, J.G., Becker, S., Griesinger, C., Lee, D.: High-power 1H composite pulse decoupling provides artifact free exchange-mediated saturation transfer (EST) experiments. J. Magn. Reson. 2016, 269, 65-69.

  48. Partihar, S., Sabo, T.M., Ban, D., Fenwick, R.B., Becker, S., Salvatella, X., Griesinger, C., Lee, D.: Kinetics of the antibody recognition site in the third IgG-binding domain of protein G. Angew. Chem. Int. Ed. 2016 In press.