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Publications

Goto:
1986-1990
1991-1995
1996-2000
2000-2005
2006-2010
Theses

1986-1990

1. Kemmink, J., Vuister, G. W., Boelens, R., Dijkstra, K. & Kaptein, R. "Nuclear Spin Coherence Transfer in Photochemical Reactions" (1986) J. Am. Chem. Soc. 108, 5631-5633.

2. Vuister, G. W. & Boelens, R. "Three-Dimensional J-Resolved NMR Spectroscopy" (1987) J. Magn. Reson. 73, 328-333.

3. Endo, T., Oya, M., Kaptein, R., Vuister, G. W., Kihara, H., Mohri, N., Tanaka,S & Ohno, M. "Proton NMR Resonance Assignments and Surface Accessibility of the Tryptophan Residues of a Dimeric Phospholipase A2 from Trimeresurus flavoviridis" (1988) FEBS Lett. 230, 57-60.

4. Mayo, K. H., Schussheim, A., Vuister, G. W., Boelens, R., Kaptein, R., Engelhard, M. & Hess, B. "Mobility and Solvent Exposure of Aromatic Residues in Bacteriorhodopsin Investigated by 1H-NMR and Photo-CIDNP-NMR Spectroscopy" (1988) FEBS Letters 235, 163-168.

5. Vuister, G. W., Boelens, R. & Kaptein, R. "Nonselective Three-Dimensional NMR Spectroscopy. The 3D NOE-HOHAHA Experiment" (1989) J. Magn. Reson. 80, 176-185.

6. Vuister, G. W., de Waard, P., Boelens, R., Vliegenthart, J. F. G. & Kaptein, R. "The Use of 3D NMR in Structural Studies of Oligosaccharides" (1989) J. Am. Chem. Soc. 111,772-774.

7. Boelens, R., Vuister, G. W., Koning, T. M. G. & Kaptein, R. "The Observation of Spin-Diffusion in Biomolecules by 3D NOE-NOE Spectroscopy" (1989) J. Am. Chem. Soc. 111, 8525-8526.

8. Boelens, R., Vuister, G. W., Padilla, A., Kleywegt, G. J., de Waard, P., Koning, T. M. G. & Kaptein, R. "Three-Dimensional NMR Spectroscopy of Biomolecules" (1989) Procedings of the Sixth Conversation in the Dicipline Biomolecular Stereodynamics, State University of New York at Albany, June 06-10, 1989, 63-81.

9. Rullmann, J. A. C., Boelens, R., Lamerichs, R. M. J. N., Vuister, G. W. & Kaptein, R. “NMR Studies of Proteins and Protein-DNA interactions” (1989) in Modeling of Molecular Structures and Properties, Proceedings of the 44th International Meeting of Physical Chemistry, Ed. J. L. Rivail, Elsevier, Amsterdam, 661-678.

10. Vuister, G. W., Boelens, R., Padilla, A., Kleywegt, G. J. & Kaptein, R. "Assignment Strategies in Hononuclear Three-Dimensional 1H NMR Spectra of Proteins" (1990) Biochemistry 29, 1829-1839.

11. Padilla, A., Vuister, G. W., Boelens, R., Kleywegt, G. J., Cavé, A., Parello, J. & Kaptein, R. "Homonuclear Three-Dimensional 1H NMR Spectroscopy of Pike Parvalbumin. Comparison of Short and Medium Range NOEs from 2D and 3D Spectra" (1990) J. Am. Chem. Soc. 112, 5024-5030.

12. Breg, J. N., Boelens, R., Vuister, G. W. & Kaptein, R. “3D NOE-NOE Spectroscopy of Proteins. Observation of Sequential 3D NOE Cross Peaks in Arc Repressor” (1990) J. Magn. Reson. 87, 646-651.

13. de Waard, P., Boelens, R., Vuister, G.W., & Vliegenthart, J.F.G. “Structural Studies by 1H/13C Two-Dimensional and Three-Dimensional HMQC-NOE at Natural Abundance on Complex Carbohydrates” (1990) J. Am. Chem. Soc. 112, 3232-3234.

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1991-1995

14. Vuister, G. W. “Homonuclear Three-Dimensional NMR Spectroscopy of Biomolecules”, (1991), Ph.D. Thesis, Utrecht, The Netherlands.

15. Vuister, G. W., Boelens, R., Kaptein, R., Hurd, R. E., John, B. & Van Zijl, P. C. M “Gradient-Enhanced HMQC and HSQC spectroscopy. Applications to 15N labeled Mnt repressor in 1H2O”, (1991) J. Am. Chem. Soc. 113, 9688-9690.

16. Vuister, G. W., Boelens, R., Padilla, A. & Kaptein, R. “Statistical Analysis of Double NOE Transfer Pathways in Proteins as Measured in 3D NOE-NOE Spectroscopy”, (1991) J. Biomol. NMR 1, 421-438.

17. Moonen, C. T. W., Van Gelderen, P., Vuister, G. W. & Van Zijl, P. C. M. “Gradient-Enhanced Exchange Spectroscopy (GEXSY)”, (1992) J. Magn. Reson. 97, 419-425.

18. de Waard, P., Leeflang, B. R., Vliegenthart, J. F. G., Boelens, R., Vuister, G. W. & Kaptein, R. “Application of 2D and 3D Experiments to the Conformational Study on a Diantennery Oligosaccharide” (1992) J. Biomol. NMR 2, 211-226.

19. Vuister, G. W., Boelens, R., Kaptein, R., Burgering, M. & Van Zijl, P. C. M. “Gradient-Enhanced 3D NOESY-HMQC Spectroscopy”, (1992) J. Biomol. NMR 2, 301-305.

20. Vuister, G. W. & Bax, A. “Resolution Enhancement and Spectral Editing of Uniformly 13C Enriched Proteins by Homonuclear Broadband 13C Decoupling.” (1992) J. Magn. Reson. 98, 428-435.

21. Vuister, G. W. & Bax, A. “Measurement of Two-Bond JCOHa Coupling Constants in Proteins Uniformly Enriched in 13C” (1992) J. Biomol. NMR 2, 401-405.

22. Vuister, G. W., Ruiz-Cabello, J. & van Zijl, P. C. M. “Gradient-Enhanced Muliple-Quantum Filter (ge-MQF). A Simple way for Obtaining Single-Scan Phase-Sensitive HMQC Spectra” (1992) J. Magn. Reson. 100, 215-220.

23. Vuister, G. W., Delaglio, F. & Bax, A. “An Emperical Correlation Between 1J­CaHa and Protein Backbone Conformation” (1992) J. Am. Chem. Soc. 114, 9674-9675.

24. Ruiz-Cabello, J., Vuister, G. W., Moonen, C. T. W., Van Gelderen, P. & Van Zijl, P. C. M. “Gradient-Enhanced Heteronuclear Correlation Spectroscopy. Theory and Experimental Aspects.” (1992), J. Magn. Reson. 100, 282-302.

25. Vuister, G. W., Delaglio, F. & Bax, A. “The Use of 1J­CaHa Coupling Constants as a Probe for Protein Backbone Conformation” (1993) J. Biomol. NMR 3, 67-80.

26. Vuister, G. W., Clore, G. M., Gronenborn, A. M., Powers, R., Garrett, D. S., Tschudin, R. & Bax, A. “Increased Resolution and Improved Spectral Quality in Four-Dimensional 13C/13C Separated HMQC-NOESY-HMQC Spectra Using Pulsed Field Gradients” (1993) J. Magn. Reson. B 101, 210-213.

27. Vuister, G. W., Yamazaki, T., Torchia, D. A. & Bax, A. “Measurement of Two- and Three-Bond 13C-1H J Couplings to the C­d Carbons of Leucine Residues in Staphylococcal Nuclease” (1993) J. Biomol. NMR 3, 297-306.

28. Vuister, G. W., Wang, A. C. & Bax, A. (1993) “Measurement of Three-Bond Nitrogen-Carbon Couplings in Proteins Uniformly Enriched in 15N and 13C” J. Am. Chem. Soc. 115, 5334-5335.

29. Vuister, G. W. & Bax, A. (1993) “Quantitative J Correlation: A New Approach for Measuring Homonuclear Three-Bond J(HNHa) Coupling Constants in 15N-Enriched Proteins”, J. Am. Chem. Soc. 115, 7772-7777.

30. Grzesiek, S., Vuister, G. W. & Bax, A. (1993) “A Simple and Sensitive Experiment for Measurement of JCC Couplings Between Backbone Carbonyl and Methyl Protons in Isotopically Enriched Proteins”, J. Biomolec. NMR 3, 487-493.

31. Bax, A., Vuister, G. W., Grzesiek, S., Delaglio, F., Wang, A. C., Tschudin, R. & Zhu, G. (1994) “Measurement of Homo- and Heteronuclear J Couplings from Quantitative J Correlation”, in James, T.L. & Oppenheimer, N.J. (eds) Methods in Enzymology 239, 79-105.

32. Kleywegt, G.J., Vuister, G.W., Padilla, A., Knegtel, R. M. A., Boelens, R. & Kaptein, R. (1993) “Computer-Assisted Assignment of Homonuclear 3D NMR Spectra of Proteins. Application to Pike Parvalbumin III” J. Magn. Reson. B 102, 166-176.

33. Vuister, G. W. & Bax, A. (1993) “Measurement of Two- and Three-bond Proton to Methyl Carbon J Couplings in Proteins Uniformly Enriched in 13C” J. Magn. Reson. B 102, 228-231.

34. Vuister, G. W. & Bax, A. (1994) “Measurement of Four-bond HN-Ha J Couplings in Staphyloccal Nuclease” J. Biomol. NMR 4, 193-200.

35. Vuister, G.W., Kim, S.J., Wu, C. & Bax, A (1994) “NMR Evidence for Similarities Between the DNA-Binding Regions of Drosophila melanogaster Heat Shock Factor and Helix-Turn-Helix and HNF-3/fork head Families of Transcription Factors” Biochemistry 33, 10-16.

36. Garrett, D.S., Kuszewski, J., Hancock, T., Lodi, P.J., Vuister, G.W., Gronenborn, A.M. & Clore, G.M. (1994) “The Impact of Direct Refinement Against Three-bond HN-CaH Coupling constants on Protein Structure Determination by NMR” J. Magn. Reson. B 104, 99-103.

37. Bax, A., Delaglio F., Grzesiek, S. & Vuister, G.W. (1994) “Resonance Assignment of Methionine Methyl Groups and c3 Angular Information from Long Range Proton-Carbon and Carbon-Carbon J Correlation in a Calmodulin-Peptide Complex” J. Biomolec. NMR 4, 787-797.

38. Vuister, G.W., Kim, S-.J., Wu, M. & Bax, A. (1994) “2D and 3D NMR Study of Phenylalanine Residues in Proteins by Reverse Isotopic Labeling”, J. Am. Chem. Soc. 116, 9206-9210.

39. Vuister, G.W., Kim, S-.J., Orosz, A., Marquardt, J., Wu, C. & Bax, A. (1994) “Solution Structure of the DNA-Binding Domain of Drosophila Heat Shock Transcription Factor”, Nature Struct. Biol. 1, 605-614.

40. Wang, A.C., Lodi, P.J, Qin, J., Vuister, G.W., Gronenborn, A.M. & Clore, G.M. (1994) “An Efficient Triple Resonance Experiment for Proton-Directed Sequential Backbone Assignment of Medium-Sized Proteins”, J. Magn. Reson. B 105, 196-198.

41. 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.

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1996-2000

42. Vuister, G.W., Knegtel, R.M.A. & Gincel, E. (1996) “DNA-binding by Heat-Shock Transcription Factors”, Biological Structure and Dynamics, Proceedings of the Ninth Conversation, State University of New York, Albany, NY,1995, Sarma, R.H. & Sarma, M.H. (Eds.) Adenine Press 1996, pp 91-107.

43. Tessari, M., Vis, H., Boelens, R., Kaptein, R. & Vuister, G.W. (1997) “Quantitative measurement of relaxation interference effects between 1HN CSA and 1H-15N dipolar interaction: correlation with secondary structure”, J. Am. Chem. Soc. 119, 8985-8990. (PDF)

44. Tessari, M., Mulder, F., Boelens, R., & Vuister, G.W. (1997) “Determination of Amide Proton CSA in 15N-Labeled Proteins using 1H CSA/15N-1H Dipolar and 15N CSA/15N-1H Dipolar Cross-Correlation Rates”, J. Magn. Reson. 127, 128-133. (PDF)

45. Whitehead, B., Tessari, M., Düx, P., Boelens, R., Kaptein, R., & Vuister, G.W. (1997) “An 15N-filtered 2D 1H-TOCSY experiment for assignment of aromatic ring resonances and selective identification of tyrosine ring resonances in proteins: description and application to Photoactive Yellow Protein”, J. Biomol. NMR 9, 313-316. (PDF)

46. Tessari, M., Gentile, L., Taylor, S.J., Shalloway, D., Nicholson, L. & Vuister, G.W. (1997) “Heteronuclear NMR studies of the combined SH3-SH2 domains of pp60 c-Src. The effects of phosphopeptide binding”, Biochemistry 36, 14561-14571. (PDF)

47. Düx, P., Whitehead, B., Boelens, R., Kaptein, R., & Vuister, G.W. (1997) “Measurement of 15N-1H Coupling Constants in Uniformily 15N Labeled Proteins. Application to the Photoactive Yellow Protein”, J. Biomol. NMR 10, 301-306. (PDF)

48. Rubinstenn, G., Vuister, G.W., Mulder, F.A.A., Düx, P.E., Boelens, R., Hellingwerf, K.J. & Kaptein, R. (1998) The long-lived intermediate of the Photoactive Yellow Protein photocycle is disordered in solution”, Nature Struct. Biol. 5, 568-570. (PDF)

49. Düx, P.E., Rubinstenn, G., Vuister, G.W., Boelens, R., Mulder, F.A.A., Hård, K., Hoff, W.D., Kroon, A.R., Crielaard, W., Hellingwerf, K.J. & Kaptein, R. (1998) “Solution structure and backbone dynamics of the photoactive yellow protein”, Biochemistry 37, 12689-12699. (PDF)

50. Reinking, J.L., Gentile, L.N., Tessari, T., Vuister, G.W. & Nicholson, L.K. (1998) “Mechanisms of Regulation in the Regulatory Apparatus of pp60c-Src” J. Biomol. Struct. & Dynamics 16, 53-62.

51. Kloks, C.P.A.M., Hoffmann, A., Ominchinski, J.G., Vuister, G.W., Hilbers, C.W., & Grzesiek, S. (1998) “Resonance Assignment and Secondary Structure of the Cold Shock Domain of the Human YB-1 Protein”, J. Biomol. NMR 12, 463-464. (PDF).

52. Whitehead, B., Tessari, M., Versteeg, H.H., van Delft, S., van Bergen en Henegouwen, P.M.P., & Vuister, G.W. (1998) “Sequence-specific 1H, 13C and 15N assignment of the EH1 domain of mouse Eps15”, J. Biomol. NMR 12, 465-466. (PDF)

53. Pineda-Lucena, A., Vuister, G.W., Hilbers, C.W. (1999) “Sequence-specific 1H, 13C and 15N assignment of the single-stranded DNA-binding protein of the bacteriophage f29” J. Biomol. NMR 13, 303-304. (PDF)

54. Vuister, G.W., Tessari, M., Karimi-Nejad, Y., & Whitehead, B. (1999) “Pulse Sequences for Measuring Coupling Constants” in “Modern Techniques in Protein NMR 16”, Berliner, L.J & Krishna, N.R (Eds.), Plenum Publishing Corporation, New York, 195-257.

55. Rubinstenn, G., Vuister, G.W., Zwanenburg, N., Hellingwerf, K.J., Boelens, R., & Kaptein, R. (1999) “NMR experiments to study photo-intermediates: Application to the Photoactive Yellow Protein”, J. Magn. Reson. 137, 443-447. (PDF)

56. Carotenuto, A., Tessari, M., Whitehead, B., Aelen, J.M.A., van Bergen en Henegouwen, P.M.P., & Vuister, G.W. (1999) “Sequence-specific 1H, 13C and 15N assignment and secondary structure of the apo EH2 domain of mouse Eps15”, J. Biomol. NMR 14, 97-98. (PDF)

57. Whitehead, B., Tessari, M., Carotenuto, A., Bergen en Henegouwen, P.M.P. van, & Vuister, G.W. (1999) “The EH1 domain of Eps15 is structurally classified as a member of the S100 subclass of EF-hand-containing proteins, Biochemistry 38, 11271-11277. (PDF)

58. Tessari, T. & Vuister, G.W. (2000) “A novel experiment for the quantitative measurement of CSA(1HN)/CSA(15N) cross-correlated relaxation in 15N-labeled proteins”, J. Biomol. NMR 16, 171-174. (PDF)

59. Spronk, C.A.E.M., Tessari, M., Kaan, A.M., Jansen, J.F.A., Vermeulen, M., Stunnenberg, H.G & Vuister, G.W. (2000) "The Mad1-Sin3B interaction involves a novel helical fold", Nature Struct. Biol. 7, 1100-1104. (PDF)

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2001-2005

60. Spronk, C.A.E.M., Jansen, J.F.A., Tessari, M., Kaan, A.M., Aelen, J.M.A., Lasonder, E., M., Stunnenberg, H.G & Vuister, G.W (2001) "Sequence-specific assignment of the PAH2 domain of Sin3B free- and bound to Mad1", J. Biomol. NMR 19, 377-378. (PDF)

61. Kloks, P.A.M., Spronk, C.A.E.M., Tessari, M., Vuister, G.W., Grzesiek, S. & Hilbers C.W. (2002) "Solution Structure and Backbone Dynamics of the Cold-Shock Domain of Human YB-1", J. Mol.Biol.316, 317-326. (PDF)

62. Walma, T., Spronk, C.A.E.M., Tessari, M., Aelen, J.M.A., Schepens, J., Hendriks, W. & Vuister, G.W. (2002) “Structure, Dynamics and Binding Characteristics of the Second PDZ Domain of PTP-BL”, J. Mol. Biol 316., 1101-1110. (PDF)

63. Spronk, C.A.E.M., Linge, J.P. & Hilbers C.W. & Vuister, G.W. (2002), “Improving the quality of protein structures derived by NMR spectroscopy”, J. Biomol. NMR 22, 281-289. (PDF)

64. Ingen, H. van, Vuister, G.W. & Tessari, M. (2002), “A two-dimensional artifact from asynchronous decoupling”, J. Magn. Reson 156, 258-261. (PDF)

65. Ingen, H. van,. Tessari, M. & Vuister, G.W (2002) “A 3D double-sensitivity enhanced X-filtered TOCSY-TOCSY experiment”, J. Biomol. NMR 24, 155-160. (PDF)

66. Spronk, C.A.E.M., Nabuurs, S.B., Bonvin, A.M.J.J., Krieger, E., Vuister, G.W. & Vriend, G. (2003), “The precision of NMR structure ensembles revisited”, J. Biomol. NMR 25,225-234. (PDF)

67. Hilge, M, Siegal, G., Vuister, G.W., Guntert, P., Gloor, S.M. & Abrahams, J.P. (2003) “ATP-induced conformational changes of the nucleotide binding domain of Na,K-ATPase”, Nature Struct. Biol. 10, 468-474. (PDF)

68. Nabuurs, S.B., Spronk, C.A.E.M, Krieger, E., Maassen, H., Vriend, G. & Vuister, G.W. (2003) “Quantitative evaluation of experimental NMR restraints”, J. Am. Chem. Soc.125,12026-12034. (PDF)

69. Wingens, M., Walma, T., van Ingen, H., Stortelers, C., van Leeuwen, J.E.M., van Zoelen, E.J.J. & Vuister, G.W. (2003) “Structural analysis of an EGF/TGFa chimera with unique ERBb binding specificity”, J. Biol. Chem. 278, 39114-39123. (PDF)

70. Walma, T., Aelen, J.M.A., Nabuurs, S., van den Berk, L., Oostendorp, M., Hendriks, W. & Vuister, G.W. (2004) “A closed binding pocket modifies the binding properties of an alternatively spliced form of the second PDZ domain of PTP-BL”, Structure 12, 11-20. (PDF).

71. Ingen, H. van, Lasonder, E., Jansen, J.F.A., Kaan, A., Spronk, C.A.E.M., Stunnenberg, H.G & Vuister, G.W (2004) “Extension of the binding motif of the Sin3 Interacting Domain of the Mad-family proteins”, Biochemistry 43, 46-53.

72. Nabuurs, S.B., Nederveen, A.J., Vranken, W., Doreleijers, J.F., Bonvin, A.M.J.J., Vuister, G.W., Vriend, G. & Spronk, C.A.E.M. (2004) "DRESS, a Database of REfined Solution nmr Structures", Proteins, Struct., Func., Genet. 45, 483-486.

73. Harrold A. van den Burg,, H.A., Spronk, C.A.E.M., Boeren, S., Kennedy, M.A., Visser, J.P.C., Vuister, G.W., de Wit, P.J.G.M., & Vervoort, J. (2004) "Binding of the AVR4 elicitor of Cladosporium fulvum to chitotriose units is facilitated by positive allosteric protein-protein interactions", J. Biol. Chem. 279, 16786-16796.

74. Nabuurs, S.B., Spronk, C.A.E.M., Vriend, G. & Vuister, G.W. (2004) “Concepts and tools for validation of NMR data and structures”, Concepts in Magn. Reson. 22A, 90-105.

75. Kloks, C.P.A.M., Tessari, M., Vuister, G.W., & Hilbers, C.W. (2004) “Backbone dynamics and equilibrium between the native state and a partially unfolded state”, Biochemistry 43, 10237-10246.

76. van den Berg, L.C.J., van Ham, M.A., te Lindert, M.M., Walma, T., Aelen, J.M.A., Vuister, G.W. & Hendriks, W.J.A.J. (2004) “The Interaction of PTP-BL PDZ domains with RIL: An enigmatic role for the RIL LIM domain, Mol. Biol. Reports 31, 203-215.

77. Spronk, C.A.E.M., Nabuurs, S.B., Vriend, G. & Vuister, G.W. (2004) “Validation of High-Resolution NMR-Structures”, Prog. NMR Spectr. 45, 315-337.

78. Gianni, S., Travaglini-Allocatelli, C., Calosci, N., Aelen, J.M.A., Vuister, G.W., & Brunori, M. (2005) “Kinetic folding mechanism of PDZ2 from PTP-BL”, Protein. Eng. Des. Sel. 18, 389-395.

79. Duquesne, A., de Ruijter, M., Brouwer, J., Drijfhout, J.W., Nabuurs, S.N., Spronk, C.A.E.M., Vuister, G.W., Ubbink, M. & Canters, G.W. (2005) “Solution structure of the second PDZ domain of the neuronal adaptor protein X11α and its interaction with the C-terminal peptide of the human Copper Chaperone for Superoxide dismutase”, J. Biomol. NMR 32, 209-218.

80. Nabuurs, S, Krieger, E., Spronk, C.A.E.M., Nederveen, A.J, Vriend, G., & Vuister, G.W. (2005) “Definition of a new information-based per-residue quality parameter”, J. Biomol. NMR 33, 123-134.

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2006-2010

81. Nabuurs, S, Spronk, C.A.E.M., Vuister, G.W. & Vriend, G. (2006) “Traditional Biomolecular Structure Determination by NMR Spectroscopy Allows for Major Errors”, PLoS Comput. Biol. 2, e9.

82. Van Ingen, H., Baltussen, M.A.H, Aelen, J. & Vuister, G.W. (2006) “Role of Structural and Dynamical Plasticity in Sin3: The Free PAH2 Domain is a Folded Module in mSin3B”, J. Mol. Biol. 358, 485-497.

83. Van Ingen, H., Vuister, G.W., Wijmenga, S.S., Tessari, M. (2006) “CEESY: characterizing the conformation of unobservable protein states”, J. Am. Chem. Soc. 128, 3856-3857.

84. Hilge, M., Aelen, J.M.A., Vuister, G.W. (2006) “Ca2+-regulation in the Na+/Ca2+ exchanger involves two Markedly Different Ca2+ Sensors”, Mol. Cell 22, 15-25.

85. Gianni, S., Walma, T., Arcovito, A., Calosci, N., Bellelli, A., Engstöm, Å., Travaglini-Allocatelli, C., Brunori, M., Jemth, P. & Vuister, G.W. (2006) “Demonstration of Long-Range Interactions in a PDZ Domain by NMR, Kinetics, and Protein Enginering”, Structure 14, 1801-1809.

86. Gianni, S., Geirerhaas, C.D., Calosci, N., Jemth, P., Vuister, G.W., Travaglini-Allocatelli, C., Vendruscolo, M. & Brunori, M. (2007) “A PDZ domain recapitulates a unifying mechanism for protein folding”, Proc. Natl. Acad. Sci. U.S.A. 104, 128-133.

87. Hilge, M., Aelen, J.M.A., Perrakis, A. & Vuister, G.W. (2007) “Structural basis for Ca2+ regulation in the Na+/Ca2+ exchanger.” Annals N.Y. Acad. Sci., in press.

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Theses

1. Dux, P. Thesis “NMR Spectroscopic Studies on the Photoactive Yellow Protein”, PhD. November 1997.

2. Walma, T., Thesis “The second PDZ domain of PTP-BL. The architecture of intracellular glue”, PhD. November 2004.

3. Van den Berk, L., Thesis “Binding characteristics of PTP-BL PDZ domains”, PhD. December 2005.

4. Nabuurs, S., Thesis “On the quality of NMR structures” PhD. (Cum Laude) February 2006.

5. Van Ingen, H., Thesis “The second PAH domain of Sin3. Structural Biology and NMR Methodology”, PhD. September 2006.

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Last revised: February 15th 2007