1. Drenth, J. & Hol, W. G. J. (1967). A comparison of crystallographic data of the subtilopeptidases B and C. J. Mol. Biol. 28, 543-544.

1968

1971

1972

1975

6. Drenth, J., Hol, W. G. J. & Wierenga, R. K. (1975). Crystallization and preliminary X-ray investigation of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. J. Biol. Chem. 250, 5268-5269.

1978

8. Hol, W. G. J., van Duijnen, P. T. & Berendsen, H. J. C. (1978). The a-helix dipole and the properties of proteins. Nature 273, 443-446.

9. Matthews, D. A., Alden, R., Bolin, J., Filman, D., Freer, S., Hamlin, R., Hol, W. G. J., Kisliuk, R., Pastore, E., Plant, L., Xuong, N. & Kraut, J. (1978). Dihydrofolate reductase from Lactobacillus casei.  X-ray structure of the enzyme - methotrexate -NADPH complex. J. Biol. Chem. 253, 6946-6954.

10. Ploegman, J. H., Drent, G., Kalk, K. H. & Hol., W. G. J. (1978). Structure of bovine liver rhodanese.  I.  The structure determination at 2.5 Å resolution and a comparison of the conformation and sequence of its two domains. J. Mol. Biol. 123, 557-594.

1979

12. van Duijnen, P. T., Thole, B. T. & Hol, W. G. J. (1979). On the role of the active site helix in papain.  An ab initio molecular orbital study. Biophys. Chem. 9, 273-280.

13. Wierenga, R. K., de Jong, R. J., Kalk, K. H., Hol, W. G. J. & Drenth, J. (1979). Crystal structure of p-hydroxy benzoate hydroxylase. J. Mol. Biol. 131, 55-73.

14. Ferro, D. R. & Hol, W. G. J. (1979). Energy minimization of proteins.  An attempt to explicitly account for water-protein interactions. In Simulation of Enzyme Catalysis (van Duijnen, P. T. & Hol, W. G. J., eds.), pp. 141-183. CECAM, Paris.

15. Hol, W. G. J. (1979). The interaction of parallel and anti-parallel helices. In Simulation of Enzyme Catalysis (van Duijnen, P. T. & Hol, W. G. J., eds.), pp. 184-191. CECAM, Paris.

1981

17. Dijkstra, B. W., Kalk, K. H., Hol, W. G. J. & Drenth, J. (1981). Structure of bovine pancreatic phospholipase A2 at 1.7 Å resolution. J. Mol. Biol. 147, 97-123.

18. Hol, W. G. J., Halie, L. M. & Sander, C. (1981). The dipoles of the a-helix and the ß-sheet:  Their role in the folding of proteins. Nature 294, 532-536.

19. Brandenburg, N. P., Dempsey, S., Dijkstra, B. W., Lijk, L. J. & Hol, W. G. J. (1981). An interactive graphics system for comparing and model building of macromolecules. J. Appl. Cryst. 14, 274-279.

1982

21. Hol, W. G. J. (1982). In de eiwitkristallografie is een instrumentele revolutie op komst. Chemisch Magazine, 30-32.

22. van Schaick, E. J. M., Schutter, W. G., Gaykema, W. P. J., Schepman, A. M. H. & Hol, W. G. J. (1982). Structure of Panulirus interruptus hemocyanin at 5 Å resolution. J. Mol. Biol. 158, 457-483.

1983

24. Gaykema, W. P. J., van Schaick, E. J. M., Schutter, W. G. & Hol, W. G. J. (1983). Crystal structure of Panulirus interruptus hemocyanin. Life Chemistry Reports, Supplement Series Suppl. 1, 57-60.

25. Gaykema, W. P. J., van Schaick, E. J. M., Schutter, W. G. & Hol, W. G. J. (1983). The structure of Panulirus interruptus hemocyanin at 4.0 Å resolution and a preliminary description of the copper containing oxygen binding site. Chemica Scripta 21, 19-23.

26. Hol, W. G. J., Lijk, L. J. & Kalk, K. H. (1983). The high resolution three-dimensional structure of bovine liver rhodanese. Fundam. Appl. Toxicol. 3, 370-376.

27. Lijk, L. J., Kalk, K. H., Brandenburg, N. P. & Hol, W. G. J. (1983). The binding of metal cyanide complexes to rhodanese in the crystalline state. Biochemistry 22, 2952-2957.

28. Dijkstra, B. W., Renetseder, R., Kalk, K. H., Hol, W. G. J. & Drenth, J. (1983). Structure of porcine pancreatic phospholipase A2 at 2.6 Å resolution and comparison with bovine phospholipase A2. J. Mol. Biol. 168, 163-179.

29. Gaykema, W. P. J., Groendijk, H., Doorten, G., Vereijken, J. M. & Hol, W. G. J. (1983). Crystals containing a single subunit type of Panulirus interruptus hemocyanin. J. Mol. Biol. 168, 197-201.

30. Wierenga, R. K. & Hol, W. G. J. (1983). Predicted nucleotide-binding properties of p21 protein and its cancer-associated variant. Nature 302, 842-844.

1984

32. Hol, W. G. J. & De Maeyer, M. C. H. (1984). Electrostatic interactions between a-helix dipoles in crystals of an uncharged helical undecapeptide. Biopolymers 23, 809-817.

33. Gaykema, W. P. J., Hol, W. G. J., Vereijken, J. M., Soeter, N. M., Bak, H. J. & Beintema, J. J. (1984). 3.2 Å structure of the copper-containing, oxygen-carrying protein Panulirus interruptus hemocyanin. Nature 309, 23-29.

34. Lijk, L. J., Torfs, C. A., Kalk, K. H., De Maeyer, C. H. & Hol, W. G. J. (1984). Differences in the binding of sulfate, selenate and thiosulfate to bovine liver rhodanese, and a description of a binding site for ammonium and sodium ions. Eur. J. Biochem. 142, 399-408.

35. Wierenga, R. K., Hol, W. G. J., Misset, O. & Opperdoes, F. R. (1984). Preliminary crystallographic studies of triose phosphate isomerase from the blood parasite Trypanosoma brucei. J. Mol. Biol. 178, 487-490.

1985

37. Hol, W. G. J. (1985). The variable effective dielectric constant and uncertainties in the direction of the peptide dipole moment:  an investigation of dipole-dipole interactions in aa- and ßaß- units of proteins. J. Mol. Struct. (Theochem) 123, 27-43.

38. Wierenga, R. K., DeMaeyer, M. C. H. & Hol, W. G. J. (1985). The interaction of pyrophosphate moieties with a-helices in dinucleotide-binding proteins. Biochemistry 24, 1346-1357.

39. Witholt, B., van Gunsteren, W. F. & Hol, W. G. J. (1985). Protein engineering. Proc. Third European Cong. Biotechnology 4, 497-517.

40. Linzen, B., Soeter, N. M., Riggs, A. F., Schneider, H. J., Schartau, W., Moore, M. D., Yokota, E., Behrens, P. Q., Nakashima, H., Takagi, T., Nemoto, T., Vereijken, J. M., Bak, H. J., Beintema, J. J., Volbeda, A., Gaykema, W. P. J. & Hol, W. G. J. (1985). The structure of arthropod hemocyanins. Science 229, 519-524.

41. Hol, W. G. J. (1985). Effects of the a-helix dipole upon the functioning and structure of proteins and peptides. Adv. Biophys. 19, 133-165.

42. Pronk, S. E., Hofstra, H., Groendijk, H., Kingma, J., Swarte, M. B. A., Dorner, F., Drenth, J., Hol, W. G. J. & Witholt, B. (1985). Heat-labile enterotoxin of Escherichia coli:  characterization of different crystal forms. J. Biol. Chem. 260, 13580-13585.

43. Schierbeek, A. J., Renetseder, R., Dijkstra, B. W. & Hol, W. G. J. (1985). Investigations into the limitations of a rotation and a translation function. Proc. Daresbury Study Weekend on Molecular Replacement, Daresbury Laboratory, 16-21.

44. Hol, W. G. J., Volbeda, A. & Gaykema, W. P. J. (1985). Rotation functions, density averaging and phase extension:  Panulirus interruptus haemocyanin. Proc. Daresbury Study Weekend on Molecular Replacement, Daresbury Laboratory, 70-75.

45. Hol, W. G. J. (1985). Enzyme action, Oyez Publishers.

1986

47. Volbeda, A. & Hol, W. G. J. (1986). Structure of the copper-containing oxygen-transporting hemocyanins from arthropods. In Frontiers in Bioinorganic Chemistry (Xavier, A. V., ed.), pp. 584-593. VCG Verlagagsgesellschaft, Weinheim.

48. Volbeda, A. & Hol, W. G. J. (1986). Three-dimensional structure of haemocyanin from the spiny lobster, Panulirus interruptus, at 3.2 Å resolution. In Invertebrate Oxygen Carriers (Linzen, B., ed.), pp. 135-147. Springer Verlag, Berlin.

49. Vellieux, F. M. D., Frank, J., Swarte, M. B. A., Groendijk, H., Duine, J. A., Drenth, J. & Hol, W. G. J. (1986). Purification, crystallization and preliminary X-ray investigation of quino protein methylamine dehydrogenase from Thiobacillus versutus. Eur. J. Biochem. 154, 383-386.

50. Berendsen, H. J. C. & Hol, W. G. J. (1986). Long-range electrostatic forces. Europhysics News 17, 8-10.

51. Wierenga, R. K., Terpstra, P. & Hol, W. G. J. (1986). Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint. J. Mol. Biol. 187, 101-107.

52. Hol, W. G. J. (1986). Protein engineering:  toekomstige toepassingen. Biotechnologie in Nederland 3, 8-11.

53. Hol, W. G. J. (1986). Protein crystallography and computer graphics - toward rational drug design. Angewandte Chemie (Int. Ed.) 25, 767-778.

54. Hol, W. G. J. (1986). Proteinkristallographie und computer-graphik - auf dem weg zu einer planvollen arzneimittelentwicklung. Angewandte Chemie 98, 765-777.

1987

56. Hol, W. G. J. (1987). Structural basis for catalysis by rhodanese. In Biological Macromolecules and Assemblies (Jurnak, F. A. & McPherson, A., eds.), Vol. 3, pp. 483-522. Wiley, New York.

57. Wierenga, R. K., Swinkels, B., Michels, P. A. M., Osinga, K., Misset, O., Van Beeuman, J., Gibson, W., Postma, J. P. M., Borst, P., Opperdoes, F. R. & Hol, W. G. J. (1987). Common elements on the surface of glycolytic enzymes from Trypanosoma brucei may serve as topogenic signals for import into glycosomes. EMBO J. 6, 215-221.

58. Soeter, N. M., Jekel, P. A., Beintema, J. J., Volbeda, A. & Hol, W. G. J. (1987). Primary and tertiary structures of the first domain of Panulirus interruptus hemocyanin and comparison of arthropod hemocyanins. Eur. J. Biochem. 169, 323-332.

59. Hol, W. G. J. (1987). Protein crystallography, computer graphics and drug design. Pure and Applied Chemistry 59, 431-436.

60. Read, R. J., Wierenga, R. K., Groendijk, H., Lambeir, A., Opperdoes, F. R. & Hol, W. G. J. (1987). Preliminary crystallographic studies of glycosomal glyceraldehyde phosphate dehydrogenase from Trypanosoma brucei. J. Mol. Biol. 194, 573-575.

61. Wierenga, R. K., Kalk, K. H. & Hol, W. G. J. (1987). Structure determination of the glycosomal triosephosphate isomerase from Trypanosoma brucei brucei at 2.4 Å resolution. J. Mol. Biol. 198, 109-121.

62. Kelders, H. A., Kalk, K. H., Gros, P. & Hol, W. G. J. (1987). Automated protein crystallization and a new form of a subtilisin:eglin complex. Protein Engineering 1, 301-303.

63. Hol, W. G. J. (1987). Applying knowledge of protein structure and function. Trends in Biotechnology 5, 137-143.

64. Schreuder, H. A., van der Laan, J. M., Thunnissen, M. M. G. M., Kalk, K. H., Swarte, M. B. A., Hol, W. G. J. & Drenth, J. (1987). Crystallographic studies on the mechanism of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. In Flavins and Flavoproteins (McCormick, D. B. & Edmondson, D. E., eds.), pp. 527-538. Walter de Gruyter, Berlin.

65. van Berkel, W. J. H., Bakx, E. J., Müller, F., Weyer, W. J., Jekel, P. A., Beintema, J. J., Schreuder, H. A., van der Laan, J. M., Wierenga, R. K., Drenth, J. & Hol, W. G. J. (1987). Chemical modification of tyrosine-38 in p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens by 5'-P- fluorosulfonylbenzoyladenosine:  a probe for the elucidation of the NADPH binding site? In Flavins and Flavoproteins (McCormick, D. B. & Edmondson, D. E., eds.), pp. 549-552. Walter de Gruyter, Berlin, New York.

1988

67. Schreuder, H. A., Hol, W. G. J. & Drenth, J. (1988). Molecular modeling reveals the possible importance of a carbonyl oxygen binding pocket for the catalytic mechanism of p-hydroxybenzoate hydroxylase. J. Biol. Chem. 263, 3131-3136.

68. Volbeda, A. & Hol, W. G. J. (1988). Structure of arthropodan hemocyanin. In Proc. 4th Int. Symp. on Oxidative Reactions (Mason, H. S., ed.), pp. 291-307. Alan R. Liss, New York.

69. Gros, P., Groendijk, H., Drenth, J. & Hol, W. G. J. (1988). Experiments in membrane protein crystallization. J. Cryst. Growth 90, 193-200.

70. Kooystra, P. J. U., Kalk, K. H. & Hol, W. G. J. (1988). Soaking in Cs2SO4 reveals a cation-aromatic interaction in bovine liver rhodanese. Eur. J. Biochem. 177, 345-349.

1989

72. van der Klei, I. J., Lawson, C. L., Rozeboom, H. J., Dijkstra, B. W., Veenhuis, M., Harder, W. & Hol, W. G. J. (1989). Use of electron microscopy in the examination of lattice defects in crystals of alcohol oxidase. FEBS Lett. 244, 213-216.

73. Gros, P., Fujinaga, M., Dijkstra, B. W., Kalk, K. H. & Hol, W. G. J. (1989). Molecular dynamics refinement of the X-ray structure of thermitase complexed with eglin-c. In Computer Simulation of Biomolecular Systems (van Gunsteren, W. F. & Weiner, P. K., eds.), pp. 190-193. Escom, Leiden, The Netherlands.

74. Kelders, H. A., Kalk, K. H. & Hol, W. G. J. (1989). Crystallization of thermitase, a thermostable subtilisin, from sodium formate solution by means of an automated procedure. J. Mol. Biol. 205, 615-616.

75. Schierbeek, A. J., Swarte, M. B. A., Dijkstra, B. W., Vriend, G., Read, R. J., Hol, W. G. J., Drenth, J. & Betzel, C. (1989). X-ray structure of lipoamide dehydrogenase from Azotobacter vinelandii determined by a combination of molecular and isomorphous replacement techniques. J. Mol. Biol. 206, 365-379.

76. Volbeda, A. & Hol, W. G. J. (1989). Pseudo-twofold symmetry in the copper-binding domain of arthropodan hemocyanins:  possible implications for the evolution of oxygen transport proteins. J. Mol. Biol. 206, 531-546.

77. Volbeda, A., Feiters, M., Vincent, M., Bouwman, E. P. R., Dobson, R., Reedijk, J. & Hol, W. G. J. (1989). Spectroscopic investigations of Panulirus interruptus hemocyanin crystals. Eur. J. Biochem. 181, 669-673.

78. Vellieux, F. M. D., Groendijk, H., Huitema, F., Swarte, M. B. A., Drenth, J. & Hol, W. G. J. (1989). The use of solvent flattening procedures in the crystal structure determination of quino protein methylamine dehydrogenase. In Proceedings of the Daresbury Study Weekend on "Improving Protein Phases," (Bailey, S., Dodson, E. & Phillips, S., eds.), pp. 88-99. SERC Daresbury.

79. Vellieux, F. M. D., Huitema, F., Groendijk, H., Kalk, K. H., Frank, J., Jongejan, J. A., Duine, J. A., Drenth, J. & Hol, W. G. J. (1989). Structure of quinoprotein methylamine dehydrogenase at 2.25 Å resolution. EMBO J. 8, 2171-2178.

80. Schreuder, H. A., Prick, P., Wierenga, R. K., Vriend, G., Wilson, K., Hol, W. G. J. & Drenth, J. (1989). Crystal structure of p-hydroxybenzoate hydroxylase refined at 1.9 Å resolution. J. Mol. Biol. 208, 679-696.

81. Volbeda, A. & Hol, W. G. J. (1989). Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 Å resolution. J. Mol. Biol. 209, 249-279.

82. Vellieux, F. M. D. & Hol, W. G. J. (1989). A new model for the pro-PQQ cofactor of quinoprotein methylamine dehydrogenase. FEBS Lett. 255, 460-464.

83. van der Laan, J. M., Schreuder, H. A., Swarte, M. B. A., Wierenga, R. K., Kalk, K. H., Hol, W. G. J. & Drenth, J. (1989). The co-enzyme analogue adenosine-5-diphosphoribose displaces FAD in the active site of p-hydroxybenzoate hydroxylase.  An X-ray crystallographic investigation. Biochemistry 28, 7199-7205.

84. Gros, P., Fujinaga, M., Kalk, K. H., Dijkstra, B. W. & Hol, W. G. J. (1989). Crystallographic refinement by incorporation of molecular dynamics:  Thermostable serine protease thermitase complexed with eglin c. Acta Cryst. B45, 488-499.

85. Hol, W. G. J. (1989). Protein crystallography and drug design. Arzneim.-Forsch./Drug Res. 39, 1016-1018.

86. Gros, P., Fujinaga, M., Mattevi, A., Vellieux, F. M. D., van Gunsteren, W. F. & Hol, W. G. J. (1989). Protein structure refinement by molecular dynamics techniques. In Proc. Daresbury Study Weekend on Molecular Dynamics Refinement (Goodfellow, J., Henrick, K. & Hubbard, R., eds.), pp.1-15. SERC, Daresbury, UK.

87. Voorintholt, R., Kosters, M. T., Vegter, G., Vriend, G. & Hol, W. G. J. (1989). A very fast program to visualize protein surfaces, channels and cavities. J. Mol. Graph. 7, 243-245.

88. Gros, P., Betzel, C., Dauter, Z., Wilson, K. S. & Hol, W. G. J. (1989). Molecular dynamics refinement of a thermitase:eglin-c complex at 1.98 Å resolution and comparison of two crystal forms that differ in calcium content. J. Mol. Biol. 210, 347-367.

89. Hol, W. G. J. (1989). New developments in protein crystallography. In Advances in Protein Design (Blöcker, H., Collins, J., Schmid, R. D. & Schomburg, D., eds.), Vol. 12, pp. 27-34. GBF Monographs, VCH Verlagsgesellschaft, Weinheim.

90. Hol, W. G. J., Wierenga, R. K., Groendijk, H., Read, R. J., Thunnissen, A. M. W. H., Noble, M. E. M., Kalk, K. H., Vellieux, F. M. D., Opperdoes, F. R. & Michels, P. A. M. (1989). Protein crystallography, computer graphics and sleeping sickness. In Proc. Molecular Recognition:  Chemical and Biochemical Problems (Roberts, S. M., ed.), Vol. Special Publication, pp. 84-93. Royal Society Chemistry.

91. Opperdoes, F. R., Wierenga, R. K., Hol, W. G. J. & Michels, P. A. M. (1989). Rational design of trypanocidal drugs. In Immune Recognition and Evasion:  Molecular Aspects of Host-parasite Interaction (van der Ploeg, L. H. T., Cantor, C. R. & Vogel, J. J., eds.), pp. 295-304. Academic Press, New York.

92. Hol, W. G. J. (1989). Het ontwikkelen van nieuwe medicijnen. In Biochemie in Perspectief (van Dam-Mieras, R. C. E., ed.), pp. 43-84. Publ. Open Universiteit, Heerlen.

1990

94. Opperdoes, F. R., Wierenga, R. K., Noble, M. E. M., Hol, W. G. J., Wilson, M., Kuntz, D. A., Callens, M. & Perié, J. (1990). Unique properties of glycosomal enzymes. In Parasites:  Molecular Biology, Drug and Vaccine Design (Cerami, T. & Agabian, N., eds.), pp. 233-246. Wiley-Liss, New York.

95. Gros, P., van Gunsteren, W. F. & Hol, W. G. J. (1990). Inclusion of thermal motion in crystallographic structures by restrained molecular dynamics. Science 249, 1149-1152.

96. Hol, W. G. J. (1990). Katalytische Antilichamen. Natuur en Techniek 58, 784-793.

97. Hol, W. G. J., Volbeda, A. & Hazes, B. (1990). Structural studies of Panulirus interruptus hemocyanin. In Invertebrate Dioxygen Carriers (Préaux, G. & Lontie, R., eds.), pp. 185-188. Leuven University Press.

98. Vellieux, F. M. D., Kalk, K. H., Drenth, J. & Hol, W. G. J. (1990). Structure determination of quinoprotein methylamine dehydrogenase from Thiobacillus versutus. Acta Cryst. B46, 806-823.

99. Eschrich, K., van Berkel, W. J. H., Westphal, A. H., de Kok, A., Mettevi, A., Oblomova, G., Kalk, K. H. & Hol, W. G. J. (1990). Engineering of microheterogeneity-resistant p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. FEBS Lett. 277, 197-199.

100. Vellieux, F. M. D., Wierenga, R. K., Groendijk, H., Read, R. J., Noble, M. E. M., Verlinde, C. L. M. J. & Hol, W. G. J. (1990). Protein crystallography and the design of new drugs against sleeping sickness. In Proc. Workshop held at ILRAD, Nairobi, Kenya, 21-24 August 1989 (Peregrine, A. S., ed.), pp. 63-69. The International Laboratory for Research on Animal Diseases, Nairobi.

101. Mattevi, A., Schierbeek, A. J., Oblomova-Teplyakova, G. & Hol, W. G. J. (1990). The three-dimensional crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 Å resolution. In Flavoenzymes and Flavoproteins (Curti, A., Romchi, B. & Zanetti, C., eds.), pp. 549-556. W. de Gryter & Co., Berlin.

1991

103. Magnus, K. A., Lattman, E. A., Volbeda, A. & Hol, W. G. J. (1991). Hexamers of subunit II from Limulus hemocyanin (a 48-mer) have the same quaternary structure as whole Panuliris hemocyanin molecules. Proteins 9, 240-247.

104. Wierenga, R. K., Noble, M. E. M., Postma, J. P. M., Hol, W. G. J. & Opperdoes, F. R. (1991). The crystal structure of the 'open' and the 'closed' conformation of the flexible loop of trypanosomal triosephosphate isomerase. Proteins 10, 33-49.

105. Noble, M. E. M., Wierenga, R. K., Lambeir, A. M., Opperdoes, F. R., Thunnissen, A. M. W. H., Kalk, K. H., Groendijk, H. & Hol, W. G. J. (1991). The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes. Proteins 10, 50-69.

106. Sixma, T. K., Pronk, S. E., Kalk, K. H., Wartna, E. S., van Zanten, B. A. M., Witholt, B. & Hol, W. G. J. (1991). Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli. Nature 351, 371-377.

107. Verlinde, C. L. M. J., Noble, M. E. M., Kalk, K. H., Groendijk, H., Wierenga, R. K. & Hol, W. G. J. (1991). Anion binding to the active site of trypanosomal triosephosphate isomerase:  monohydrogen phosphate does not mimic sulphate. Eur. J. Biochem. 198, 53-57.

108. Mattevi, A., Schierbeek, A. J. & Hol, W. G. J. (1991). Three-dimensional structure of Azotobacter vinelandii lipoamide dehydrogenase refined at 2.2 Å resolution.  A comparison with glutathione reductase. J. Mol. Biol. 220, 975-994.

109. Noble, M. E. M., Verlinde, C. L. M. J., Groendijk, H., Kalk, K. H., Wierenga, R. K. & Hol, W. G. J. (1991). Crystallographic and molecular modelling studies on trypanosomal triosephosphate isomerase:  a critical assessment of predicted and observed structures of the complex with 2-phosphoglycerate. J. Med. Chem. 34, 2709-2718.

110. Wierenga, R. K., Noble, M. E. M., Vriend, G., Nauch, S. & Hol, W. G. J. (1991). The refined 1.83 Å structure of triosephosphate isomerase from Trypanosoma brucei in 2.4 M ammonium sulphate. J. Mol. Biol. 220, 995-1015.

111. Chen, L., Mathews, F. S., Davidson, V. L., Huizinga, E. G., Vellieux, F. M. D., Duine, J. A. & Hol, W. G. J. (1991). Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase. FEBBS Lett. 287, 163-166.

112. Schulze, E., Westphal, A. H., de Kok, A., Mattevi, A., Obmolova, G. & Hol, W. G. J. (1991). The catalytic domain of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii and E. coli.  Expression in E. coli, purification, properties and preliminary x-ray crystallography data. Eur. J. Biochem. 201, 561-568.

113. Hol, W. G. J. (1991). Kristallografisch onderzoek naar enzymen uit de slaapziekte parasiet als startpunt voor het ontwerp van nieuwe medicijnen. Natuurkundige Voordrachten, Nieuwe Reeks 69, 131-139.

114. Hol, W. G. J. (1991). Progress in protein research. Current Opinion in Structural Biology 1, 875-876.

115. Sixma, T. K., Pronk, S. E., Terwisscha van Scheltinga, A. C., Aguirre, A., Kalk, K. H., Vriend, G. & Hol, W. G. J. (1991). Native non-isomorphism in the structure determination of heat-labile enterotoxin (LT) from E. coli. In Proceedings Daresbury meeting on "Isomorphous Replacement and Anomalous Scattering" (Wolf, W., Evans, P. & Leslie, A. G. W., eds.), pp. 133-140.

116. Hol, W. G. J., Vellieux, F. M. D., Verlinde, C., Wierenga, R. K., Noble, M. E. M. & Read, R. J. (1991). Crystallographic investigations of glycolytic enzymes from Trypanosoma brucei:  potential starting points for the design of new drugs against African trypanosomiasis, or sleeping sickness. In Ramachandran Festschrift (Balaram, P. & Sasisekharan, S., eds.), pp. 215-244. Indian Academy of Sciences.

117. Schreuder, H. A., van der Laan, J. M., Hol, W. G. J. & Drenth, J. (1991). The structure of p-hydroxybenzoate hydroxylase. In Chemistry and Biochemistry of Flavoenzymes (Müller, F., ed.), Vol. 3, pp. 31-64. CRC Press, Boca Raton.

118. Gros, P., Teplyakov, A. V. & Hol, W. G. J. (1991). Effects of eglin-c binding to thermitase:  Three-dimensional structure comparison of native thermitase and thermitase eglin-c complexes. Proteins 12, 63-74.

1992

120. Sixma, T. K., Pronk, S. E., Kalk, K. H., van Zanten, B. A. M., Berghuis, A. M. & Hol, W. G. J. (1992). Lactose binding to heat-labile enterotoxin revealed by x-ray crystallography. Nature 355, 561-564.

121. Sixma, T. K., Terwisscha, A., Kalk, K. H., Zhou, K., Wartna, E. S. & Hol, W. G. J. (1992). X-Ray studies reveal lanthanide binding sites at the A/B5 interface of E. coli heat labile enterotoxin. FEBS Lett. 297, 179-182.

122. Hazes, B. & Hol, W. G. J. (1992). A comparison of antiparallel ß-barrels in immunoglobulins, superoxide dismutase and the third domain of arthropod hemocyanin suggests the importance of a short loop connecting two ß-strands. Proteins 12, 278-298.

123. Sixma, T. K., Pronk, S. E., Kalk, K. H., van Zanten, B. A. M., Witholt, B. & Hol, W. G. J. (1992). Three-dimensional structure of E. coli heat labile enterotoxin (LT):  Implications for the functions of LT and cholera toxin. In Bacterial Protein Toxins, Supplement 23 to Zentralblatt für Bakteriologie, Mikrobiologie und Hygiene (Witholt et al., ed.), pp. 182-188. Gustav Fischer, Stuttgart.

124. Verlinde, C. L. M. J., Rudenko, G. & Hol, W. G. J. (1992). In search of new lead compounds for trypanosomiasis drug design:  a protein structure-based linked fragment approach. J. Comp. Aided Mol. Design 46, 131-147.

125. Mattevi, A., Obmolova, G., Sokatch, J., Betzel, C. & Hol, W. G. J. (1992). The refined crystal structure of Pseudomonas putida lipoamide dehydrogenase complexed with NAD at 2.45 Å resolution. Proteins 13, 336-351.

126. Schreuder, H. A., van der Laan, J. M., Swarte, M. B. A., Kalk, K. H., Hol, W. G. J. & Drenth, J. (1992). Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3 Å resolution. Proteins 14, 178-190.

127. Chen, L., Mathews, F. S., Davidson, V., Huizinga, E. G., Vellieux, F. M. D. & Hol, W. G. J. (1992). Three-dimensional structure of methylamine dehydrogenase from Paracoccus denitrificans determined by molecular replacement at 2.8 Å resolution. Proteins 14, 288-299.

128. Mattevi, A., Obmolova, G., Schulze, G., Kalk, K. H., Westphal, A., de Kok, A. & Hol, W. G. J. (1992). Atomic structure of the cubic core of the pyruvate dehydrogenase multi-enzyme complex. Science 255, 1544-1550.

129. Mathews, F. S. & Hol, W. G. J. (1992). X-ray crystallographic studies of quinoproteins. In Principles and Applications of Quino Proteins (Davidson, V., ed.), pp. 245-273. Marcel Dekker, New York.

130. Chen, L., Durley, R., Poliks, B. J., Hamada, K., Chen, Z., Mathews, F. S., Davidson, V. L., Satow, Y., Huizinga, E. G., Vellieux, F. M. D. & Hol, W. G. J. (1992). Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin. Biochem. 31, 4959-4964.

131. Hol, W. G. J. (1992). Proteins, editorial overview. Current Opinion in Sturctural Biology 2, 843-844.

132. Huizinga, E. G., van Zanten, B. A. M., Duine, J. A., Jonge Jan, J. A., Huitema, F., Wilson, K. S. & Hol, W. G. J. (1992). The active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor. Biochemistry 31, 9789-9795.

133. Verlinde, C. L. M. J., Witmans, C. J., Pijning, T., Kalk, K. H., Hol, W. G. J., Callens, M. & Opperdoes, F. R. (1992). The structure of the complex between trypanosomal triosephosphate isomerase and N-hydroxy-4-phoshono-butanamide: Binding at the active site despite an "open" flexible loop conformation. Protein Science 1, 1578-1584.

134. Schreuder, H. A., de Boer, B., Sixma, T. K., Tepliakov, A. V., Aguirre, A. & Hol, W. G. J. (1992). Experiences with molecular replacement in the case of antithrombin III:  The combination of different starting models and exploration of the power of a "cross translation function". In "Molecular Replacement" - Proceedings CCP4 Study Weekend 31 Jan. - 1 Feb. 1992 (Dodson, E. J., Gover, S. & Wolf, W., eds.), pp. 106-115, Daresbury.

135. Streatfield, S. J., Sandkvist, S. M., Sixma, T. K., Bagdasarian, M., Hol, W. G. J. & Hirst, T. R. (1992). Intermolecular interactions between the A and B subunits of heat-labile enterotoxin from Escherichia coli promote holotoxin assembly and stability in vivo. Proc. Natl. Acad. Sci. USA 89, 12140-12144.

136. Sixma, T. K., Aguirre, A., Terwisscha van Scheltinga, A. C., Wartna, E. S., Kalk, K. H. & Hol, W. G. J. (1992). Heat-Labile enterotoxin crystal forms with variable A/B5 orientation - Analysis of conformational flexibility. FEBS Lett. 305, 81-85.

1993

138. Schreuder, H., de Boer, B., Pronk, S., Hol, W. G. J., Dijkema, R., Mulders, J. & Theunissen, H. (1993). Crystallization and preliminary X-ray analysis of human antithrombin III. J. Mol. Biol. 229, 249-250.

139. Vellieux, F. M. D., Hadju, J., Verlinde, C. L. M. J., Groendijk, H., Read, R. J., Greenough, T., Campbell, J. W., Kalk, K. H., Littlechild, J., Watson, H. C. & Hol, W. G. J. (1993). Structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei determined from Laue data. Proc. Natl. Acad. Sci. USA 90, 2355-2359.

140. Verlinde, C. L. M. J., Pijning, T., Kalk, K. H., van Calenbergh, S., Aershot, A. V., Herdewijn, P., Callens, M., Michels, P., Opperdoes, F. R., Wierenga, R. K. & Hol, W. G. J. (1993). Protein structure-based inhibitor design:  Towards new drugs for sleeping sickness. In Perspectives in Medicinal Chemistry (Testa, B., Kyburz, E., Fuhrer, W. & Giger, R., eds.), pp. 135-148. Verlag Helvetica Chimica Acta, Basel.

141. Hazes, B., Magnus, K. A., Bonaventura, C., Bonaventura, J., Dauter, Z., Kalk, K. H. & Hol, W. G. J. (1993). Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: clues for a mechanism, for allosteric regulation. Protein Science 2, 597-619.

142. Mattevi, A., Obmolova, G., Kalk, K. H., Westphal, A. H., de Kok, A. & Hol, W. G. J. (1993). Refined crystal structure of the catalytic domain of dihydrolipoyl transacetylase (E2p) from Azotobacter vinelandii at 2.6 Å resolution. J. Mol. Biol. 230, 1183-1199.

143. Mattevi, A., Obmolova, G., Kalk, K. H., van Berkel, W. J. H. & Hol, W. G. J. (1993). Three-dimensional structure of lipoamide dehydrogenase from Pseudomonas fluorescens at 2.8 Å resolution: analysis of redox and thermostability properties. J. Mol. Biol. 230, 1200-1215.

144. Sixma, T. K., Kalk, K. H., van Zanten, B. A. M., Dauter, Z., Kingma, J., Witholt, B. & Hol, W. G. J. (1993). Refined structure of Escherichia coli heat-labile enterotoxin, a close relative of cholera toxin. J. Mol. Biol. 230, 890-918.

145. Sixma, T. K., Stein, P. E., Hol, W. G. J. & Read, R. J. (1993). Comparison of the B-pentamers of heat-labile enterotoxin and verotoxin-I: Two structures with remarkable similarity and dissimilarity. Biochemistry 32, 191-198.

146. Mattevi, A., Obmolova, G., Kalk, K. H., Teplyakov, A. & Hol, W. G. J. (1993). Crystallographic analysis of substrate binding and catalysis in dihydrolipoyl transacetylase (E2p). Biochemistry 32, 3887-3901.

147. Schreuder, H., Arkema, A., de Boer, B., Kalk, K., Dijkema, R., Mulders, J., Theunissen, H. & Hol, W. G. J. (1993). Crystallization and preliminary crystallographic analysis of antistasin, a leech-derived inhibitor of blood coagulation factor Xa. J. Mol. Biol. 231, 1137-1138.

1994

149. Merritt, E. A., Sarfaty, S., van den Akker, F., L'hoir, C., Martial, J. A. & Hol, W. G. J. (1994). Crystal structure of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide. Protein Science 3, 166-175.

150. Mande, S. C., Mainfroid, V., Kalk, K. H., Goraj, K., Marital, J. A. & Hol, W. G. J. (1994). Crystal structure of recombinant human triosephosphate isomerase at 2.8 Å resolution. Protein Science 3, 810-821.

151. Verlinde, C. L. M. J. & Hol, W. G. J. (1994). Structure-based drug design: progress, results and challenges. Structure 2, 577-587.

152. Schreuder, H. A., de Boer, B., Dijkema, R., Mulders, J., Theunissen, H. J. M., Grootenhuis, P. D. J. & Hol, W. G. J. (1994). The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions. Nature Structural Biology 1, 48-54.

153. Van Calenbergh, S., van den Eeckhour, E., Herdewijn, P., de Bruyn, A., Verlinde, C., Hol, W., Callens, M., van Aerschot, A. & Rosenki, J. (1994). Synthesis and conformational analysis of 2'-Deoxy-2'-(3-methoxybenzamido)adenosine, a rational-designed inhibitor of trypanosomal glyceraldehyde phosphate dehydrogenase (GAPDH). Helvetica Chimica Acta 77, 631-644.

154. Magnus, K. A., Hazes, B., Ton-That, H., Bonaventura, C., Bonaventura, J. & Hol, W. G. J. (1994). Crystallographic analysis of oxygenated & deoxygenated states of arthropod hemocyanin shows unusual differences. Proteins 19, 302-309.

155. Merritt, E. A., Sixma, T. K., Kalk, K. H., van Zanten, B. A. M. & Hol, W. G. J. (1994). Galactose-binding site in Escherichia coli heat-labile enterotoxin (LT) and cholera toxin (CT). Mol. Microbiol. 13, 745-753.

156. de Kok, A., Berg, A., van Berkel, W., Fabisz-Kijowska, A., Westphal, A., van den Akker, F., Mattevi, A. & Hol, W. G. J. (1994). The pyruvate dehydrogenase complex from Azotobacter vinelandii. In Flavins and Flavoproteins 1993 (Yagi, K., ed.), pp. 535-544. Walter de Gruyter, Berlin, New York.

157. Schreuder, H. A., Mattevi, A., Obmolova, G., Kalk, K. H. & Hol, W. G. J. (1994). Crystal structures of wild-type p-hydroxybenzoate gydroxylase complexed with 4-aminobenzoate, 2, 4-dihydroxybenzoate and 2-hydroxy-4-aminobenzoate and of the Tyr222Ala mutant, complexed with 2-hydroxy-4-aminobenzoate.  Evidence for a proton channel and a new binding mode of the flavin ring. Biochemistry 33, 10161-10170.

158. Verlinde, C. L. M. J., Callens, M., Van Calenbergh, S., Van Aershot, A., Herdewijn, P., Hannaert, V., Michels, P. A. M., Opperdoes, F. R. & Hol, W. G. J. (1994). Selective inhibition of trypanosomal glyceraldehyde-3-phosphate dehydrogenase by protein structure-based design:  Towards new drugs for the treatment of sleeping sickness. J. Med. Chem. 37, 3605-3613.

159. Verlinde, C. L. M. J., Merritt, E. A., van den Akker, F., Kim, H., Feil, I. K., Delboni, L. F., Mande, S. C., Sarfaty, S. & Hol, W. G. J. (1994). Protein crystallography and infectious diseases. Protein Science 3, 1670-1686.

160. Pizza, M., Domenighini, M., Hol, W., Giannelli, V., Fontana, M. R., Giuliani, M. M., Magagnoli, C., Peppoioni, S., Manetti, R. & Rappuoli, R. (1994). Probing the structure-activity relationship of Escherichia coli LT-A by site directed mutagenesis. Mol. Microbiol. 14, 51-60.

161. Hol, W. G. J. (1994). Proteins - Editorial Overview:  On the diversity and essence of protein structure and function. Curr. Opin. in Struct. Biol. 4, 799-801.

162. Sandkvist, M., Overbye, L., Sixma, T. K., Hol, W. G. J. & Bagdasarian, M. (1994). Assembly of Escherichia coli heat-labile enterotoxin and its secretion from Vibrio cholerae. In Molecular Mechanisms of Bacterial Virulence (Kado, C. & Crossa, J., eds.), pp. 293-309. Kluwer Academic Publ., Dordrecht, The Netherlands.

163. Pizza, M., Rontana, M. R., Giuliani, M. M., Domenighini, M., Magagnoli, C., Giannelli, V., Nucci, D., Hol, W., Manetti, R. & Rappuoli, R. (1994). A genetically detoxified derivative of heat-labile Escherichia coli enterotoxin induces neutralizing antibodies against the A subunit. J. Exp. Med. 180, 2147-2153.

1995

165. Hol, W. G. J., Sixma, T. K. & Merritt, E. A. (1995). Structure and function of E. coli heat labile enterotoxin and cholera toxin B-pentamer. In Bacterial Toxins and Virulence Factors in Disease, Handbook of Natural Toxins (Moss, Vaughan, Itlewski & Tu, eds.), Vol. 8, pp. 185-223. Marcel Dekker, New York.

166. Merritt, E. A., Sarfaty, S., Pizza, M., Domenighini, M., Rappuoli, R. & Hol, W. G. J. (1995). Mutation of a buried residue causes loss of activity but no conformational change in the heat-labile enterotoxin of Escherichia coli. Nat. Struct. Biol. 2, 269-272.

167. Hendle, J., Mattevi, A., Westphal, A. H., Spee, J., de Kok, A., Teplyakov, A. & Hol, W. G. J. (1995). Crystallographic and enzymatic investigations on the role of Ser558, His610 and Asn614 in the catalytic mechanism of Azotobacter vinelandii dihydrolipoamide acetyltransferase (E2p). Biochemistry 34, 4287-4298.

168. Miller, H., Mande, S. S., Parsonage, D., Sarfaty, S. H., Hol, W. G. J. & Claiborne, A. (1995). An L40C mutation converts the cysteine-sulfenic acid redox center in enterococcal NADH peroxidase to a disulfide. Biochemistry 34, 5180-5190.

169. Merritt, E. A. & Hol, W. G. J. (1995). AB5 Toxins. Curr. Opin. in Struct. Biol. 5, 165-171.

170. Shoham, M., Scherf, T., Anglister, J., Levitt, M., Merritt, E. A. & Hol, W. G. J. (1995). Structural diversity in a conserved cholera toxin epitope involved in ganglioside binding. Protein Science 4, 841-848.

171. Mande, S. S., Parsonage, D., Claiborne, A. & Hol, W. G. J. (1995). Crystallographic analyses of NADH peroxidase Cys42Ala and Cys42Ser mutants:  Active site structures, mechanistic implications, and an unusual environment of Arg 303. Biochemistry 34, 6985-6992.

172. Merritt, E. A., Sarfaty, S., Chang, T. T., Palmer, L. M., Jobling, M. G., Holmes, R. K. & Hol, W. G. J. (1995). Surprising leads for a cholera toxin receptor-binding antagonist:  crystallographic studies of CTB mutants. Structure 3, 561-570.

173. van den Akker, F., Merritt, E. A., Pizza, M., Domenighini, M., Rappuoli, R. & Hol, W. G. J. (1995). The Arg7Lys mutant of heat-labile enterotoxin exhibits great flexibility of active site loop 47-56 of the A subunit. Biochemistry 34, 10996-11004.

174. van Calenbergh, S., Verlinde, C. L. M. J., Soenens, J., de Bruyn, A., Callens, M., Blaton, N. M., Peeters, O. M., Rozenski, J., Hol, W. G. J. & Herdewijn, P. (1995). Synthesis and structure-activity relationships of analogs of 2'-Deoxy-2'-(3-methoxybenzamido)adenosine, a selective inhibitor of trypanosomal glycosomal glyceraldehyde-3-phosphate dehydrogenase. J. Med. Chem. 38, 3838-3849.

175. Vellieux, F. M. D., Hadju, J. & Hol, W. G. J. (1995). Refined 3.2 Å structure of glycosomal holo glyceraldehyde phosphate dehydrogenase from Trypanosoma brucei brucei. Acta Cryst. D51, 575-589.

176. Rudenko, G., Bonten, E., d'Azzo, A. & Hol, W. G. J. (1995). Three-dimensional structure of the human 'Protective Protein': Structure of the precursor form suggests a complex activation mechanism. Structure 3, 1249-1259.

177. Kim, H., Feil, I. K., Verlinde, C. L. M. J., Petra, P. H. & Hol, W. G. J. (1995). Crystal structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase from Leishmania mexicana: Implication for structure-based drug design and a new position for the inorganic phosphate binding site. Biochemistry 34, 14975-14986.

178. Delboni, L. F., Mande, S. C., Rentier-Delrue, F., Mainfroid, V., Turley, S., Vellieux, F. M. D., Martial, J. A. & Hol, W. G. J. (1995). Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus.  An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions. Protein Science 4, 2594-2604.

1996

180. Mande, S. S., Sarfaty, S., Allen, M. D., Perham, R. N. & Hol, W. G. J. (1996). Protein-protein interactions in the pyruvate dehydrogenase multi-enzyme complex:  Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetyltransferase. Structure 4, 277-286.

181. Mainfroid, V., Mande, S. C., Hol, W. G. J., Martial, J. & Goraj, K. (1996). Stabilization of human triosephosphate isomerase by improvement of the stability of individual a-helices in dimeric as well as monomeric forms of the protein. Biochemistry 35, 4110-4117.

182. Mainfroid, V., Terpstra, P., Beauregard, M., Frère, J. M., Mande, S. C., Hol, W. G. J., Martial, J. A. & Goraj, K. (1996). Three hTIM mutants that provide new insights on why TIM is a dimer. J. Mol. Biol. 257, 441-456.

183. van den Akker, F., Steensma, E. & Hol, W. G. J. (1996). Tumor marker disaccharide D-Gal-b1,3-GalNAc complexed to heat-labile enterotoxin from Escherichia coli. Protein Science 5, 1184-1188.

184. van den Akker, F., Sarfaty, S., Twiddy, E. M., Connell, T. D., Holmes, R. K. & Hol, W. G. J. (1996). Crystal structure of a new heat-labile enterotoxin, LT-IIb. Structure 4, 665-678.

185. Feil, I. K., Reddy, R., de Haan, L., Merritt, E. A., van den Akker, F., Storm, D. R. & Hol, W. G. J. (1996). Protein engineering studies of A-chain loop 47-56 of Escherichia coli heat-labile enterotoxin point to a prominent role of this loop for cytotoxicity. Mol. Microbiol. 20, 823-832.

186. Yeh, J. I., Claiborne, A. & Hol, W. G. J. (1996). Structure of the native cystein-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8 Å resolution. Biochemistry 35, 9951-9957.

187. Hazes, B., Magnus, K. A., Kalk, K. H., Bonaventura, C. & Hol, W. G. J. (1996). Nitrate binding to Limulus polyphemus subunit type II hemocyanin and its functional implications. J. Mol. Biol. 262, 532-542.

188. Qiu, X., Pohl, E., Holmes, R. K. & Hol, W. G. J. (1996). High resolution structure of the diphtheria toxin repressor complexed with cobalt and manganese reveals an SH3-like third domain and suggests a possible role of phosphate as co-corepressor. Biochemistry 35, 12292-12302.

189. Rudenko, G., Bonten, E., d'Azzo, A. & Hol, W. G. J. (1996). Structure determination of human protective protein:  Two fold averaging reveals the three-dimensional structure of a domain which was entirely absent in the initial model. Acta Cryst. D52, 923-936.

190. Merritt, E. A., van den Akker, F. & Hol, W. G. J. (1996). E. coli heat labile enterotoxin and cholera toxin B-pentamer. In Protein Toxin Structure (Parker, M., ed.), pp. 147-172. R.G. Landes Co., Georgetown, TX.

191. de Haan, L., Verweij, W. R., Feil, I. K., Lijnema, T. H., Hol, W. G. J., Agsteribbe, E. & Wilschut, J. (1996). Mutants of the Escherichia coli heat-labile enterotoxin with reduced ADP-ribosylation activity or no activity retain the immunogenic properties of the native holotoxin. Infect. & Immun. 64, 5413-5416.

192. Hol, W. G. J. (1996). Editorial Overview:  Proteins, the sophisticated masters of the cell. Curr. Op. in Struct. Biol. 6, 777-780.

193. Teplyakov, A., Gros, P. & Hol, W. G. J. (1996). Crystallographic study of eglin-C binding to thermitase. In Subtilisin Enzymes: Practical Protein Engineering (Bott, R. & Betzel, C., eds.), pp. 5-9. Plenum Press, New York.

1997

195. Izard, T., Sarfaty, S., Westphal, A., de Kok, A. & Hol, W. G. J. (1997). Improvement of diffraction quality upon rehydration of dehydrated icosahedral Enterococcus faecalis pyruvate dehydrogenase core crystals. Protein Science 6, 913-915.

196. Pohl, E., Qiu, X., Must, L. M., Holmes, R. K. & Hol, W. G. J. (1997). Comparison of high-resolution structures of the diphtheria toxin repressor in complex with cobalt and zinc at the cation-anion binding site. Protein Science 6, 1114-1118.

197. Verlinde, C. L. M. J., Kim, H., Bernstein, B. E., Mande, S. C. & Hol, W. G. J. (1997). Antitrypanosomiasis drug development based on structures of glycolytic enzymes. In Structure-Based Drug Design (Veerapandian, P., ed.), pp. 365-394. Marcel Dekker, New York.

198. Merritt, E. A., Sarfaty, S., Jobling, M. G., Chang, T., Holmes, R. K., Hirst, T. R. & Hol, W. G. J. (1997). Structural studies of receptor binding by cholera toxin mutants. Protein Science 6, 1516-1528.

199. Claiborne, A., Crane III, E. J., Parsonage, D., Yeh, J. I., Hol, W. G. J. & Vervoort, J. (1997). NADH peroxidase from Enterococcus faecalis: Crystal structure. In Flavins and Flavoproteins (Stevenson, K. J., Massey, V. & Williams Jr., C. H., eds.), pp. 731-740. Univ. of Calgary Press, Alberta.

200. Yeh, J. I., Claiborne, A. & Hol, W. G. J. (1997). Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase. In Flavins and Flavoproteins (Stevenson, K. J., Massey, V. & Williams Jr., C. H., eds.), pp. 777-780. Univ. of Calgary Press, Alberta.

201. Lapatto, R., Krengel, U., Schreuder, H. A., Arkema, A., de Boer, B., Kalk, K. H., Hol, W. G. J., Grootenhuis, P. D. J., Mulders, J. W. M., Dijkema, R., Theunissen, H. J. M. & Dijkstra, B. W. (1997). X-ray structure of antistasin at 1.9 Å resolution and its modelled complex with blood coagulation factor Xa. EMBO J. 16, 5151-5161.

202. Merritt, E. A., Sarfaty, S., Feil, I. K. & Hol, W. G. J. (1997). Structural foundation for the design of receptor antagonists targeting E. coli heat-labile enterotoxin. Structure 5, 1485-1499.

203. Bernstein, B. E. & Hol, W. G. J. (1997). Probing the limits of the molecular replacement method:  The case of Trypanosoma brucei phosphoglycerate kinase. Acta Cryst. D53, 756-764.

204. van den Akker, F., Feil, I. K., Roach, C., Platas, A. A., Merritt, E. A. & Hol, W. G. J. (1997). Crystal structure of a heat-labile enterotoxin from Escherichia coli with increased thermostability introduced by an engineered disulfide bond in the A subunit. Protein Science 6, 2644-2649.

205. van den Akker, F., Pizza, M., Rappuoli, R. & Hol, W. G. J. (1997). Crystal structure of a non-toxic mutant of heat-labile enterotoxin which is a potent mucosal adjuvant. Protein Science 6, 2650-2654.

1998

207. Bernstein, B. E., Michels, P. A. M., Kim, H., Petra, P. H. & Hol, W. G. J. (1998). The importance of dynamic light scattering in obtaining multiple crystal forms of T. brucei PGK. Protein Science 7, 504-507.

208. Redinbo, M. R., Stewart, L., Kuhn, P., Champoux, J. J. & Hol, W. G. J. (1998). Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA. Science 279, 1504-1513.

209. Stewart, L., Redinbo, M. R., Qiu, X., Hol, W. G. J. & Champoux, J. J. (1998). A model for the mechanism of human topoisomerase I. Science 279, 1534-1541.

210. Verlinde, C. L. M. J., Kim, H., Bernstein, B. E., van den Akker, F., Minke, W. E., Hovey, B., Feil, I. K., Sarfaty, S., Roach, C., Merritt, E. A. & Hol, W. G. J. (1998). Protein crystallography, tropical diseases and drug design. In Rational Molecular Design in Drug Research, Alfred Benzon Symposium 42 (Liljefors, T., Jørgensen, F. S. & Krogsgaard-Larsen, P., eds.), pp. 295-305. Munksgaard, Copenhagen.

211. Chandra, N. R., Muirhead, H., Holbrook , J. J., Bernstein, B. E., Hol, W. G. J. & Sessions, R. b. (1998). A general method of domain closure is applied to phosphoglycerate kinase and the result compared with the crystal structure of a closed conformation of the enzyme. Proteins 30, 372-380.

212. de Haan, L., Feil, I. K., Verweij, W. R., Holtrop, M., Hol, W. G. J., Agsteribbe, E. & Wischut, J. (1998). Mutational analysis of the role of ADP-ribosylation activity and GM1-binding activity in the adjuvant properties of the Escherichia coli heat-labile enterotoxin towards intranasally administered keyhole limpet hemocyanin. Eur. J. Immunol. 28, 1243-1250.

213. Kim, H., Certa, U., Döbelli, H., Jakob, P. & Hol, W. G. J. (1998). Crystal structure of fructose-1,6-bisphosphate aldolase from the human malaria parasite Plasmodium falciparum. Biochemistry 37, 4388-4396.

214. Bernstein, B. E. & Hol, W. G. J. (1998). Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism. Biochemistry 37, 4429-4436.

215. Bernstein, B. E., Williams, D. M., Bressi, J. C., Kuhn, P., Gelb, M. H., Blackburn, G. M. & Hol, W. G. J. (1998). A bisubstrate analog induces unexpected conformational changes in phosphoglycerate kinase from Trypanosoma brucei. J. Mol. Biol. 279, 1137-1148.

216. Yeh, J. I. & Hol, W. G. J. (1998). A flash annealing technique to improve diffraction limits and lower mosaicity in crystals of glycerol kinase. Acta Cryst. D54, 479-480.

217. Hol, W. G. J., van den Akker, F., Minke, W. E., Hovey, B., Feil, I. K., Roach, C., Sarfaty, S., Verlinde, C. L. M. J. & Merritt, E. A. (1998). Towards the design of drugs and vaccines on the basis of the three-dimensional structure of the cholera toxin and E. coli heat-labile enterotoxin. In Proceeding of the Eighth European Workshop Conference on Bacterial Protein Toxins, June 29-July 4, 1997 as Supplement to "Zentral Blatt für Bakteriologie" (al., H. e., ed.), pp. 17-23. Gustave Fischer Verlag, Jena, Germany.

218. de Haan, L., Verweij, W. R., Feil, I. K., Holtrop, M., Hol, W. G. J., Agsteribbe, E. & Wilschut, J. (1998). Non-toxic variants of the Escherichia coli heat-labile enterotoxin as mucosal immunogens and adjuvants. S.T.P. Pharma Sciences 8, 75-80.

219. Kim, H. & Hol, W. G. J. (1998). Crystal structure of Leishmania mexicana glycosomal glyceraldehyde-3-phosphate dehydrogenase in a new crystal form confirms the putative physiological active site structure. J. Mol. Biol. 278, 5-11.

220. de Haan, L., Feil, I. K., Verweij, w. R., Holtrop, M., Hol, W. G. J., Agsteribbe, E. & Wilschut, J. (1998). Role of GM1-binding in the mucosal immunogenicity and adjuvanticity of the B subunit and holotoxin of the Escherichia coli heat-labile enterotoxin. Immunol. 94, 424-430.

221. Pohl, E., Holmes, R. K. & Hol, W. G. J. (1998). Motion of the DNA-binding domain with respect to the core of the diphtheria toxin repressor revealed in the crystal structures of apo- and holo-DtxR. J. Biol. Chem. 273, 22420-22427.

222. Merritt, E. A., Kuhn, P., Sarfaty, S., Erbe, J. L., Holmes, R. K. & Hol, W. G. J. (1998). The 1.25 Å resolution refinement of the cholera toxin B-pentamer:  evidence of peptide backbone strain at the receptor-binding site. J. Mol. Biol. 282, 1043-1059.

223. Aronov, A. M., Verlinde, C. L. M. J., Hol, W. G. J. & Gelb, M. H. (1998). Selective tight binding inhibitors of trypanosomal glyceraldehyde-3-phosphate dehydrogenase via structure-based drug design.
J. Med. Chem. 41, 4790-4799.

224. Feil, I. K., Platas, A. A., van den Akker, F., Reddy, R., Merritt, E. A., Storm, D. R. & Hol, W. G. J. (1998). Stepwise transplantation of an active site loop between heat-labile enterotoxins LT-II and LT-I and characterization of the obtained hybrid toxins. Protein Eng. 11, 1103-1109.

225. Hol, W. G. J. (1998). Proteins:  About individuals and assemblies.  Editorial overview. Curr. Opin. Struct. Biol. 8, 727-729.

1999

227. Hovey, B., Verlinde, C. L. M. J., Merritt, E. A. & Hol, W. G. J. (1999). Structure-based discovery of a pore-binding ligand:  Towards assembly inhibitors for cholera and related AB5 toxins. J. Mol. Biol. 285, 1169-1178.

228. van den Akker, F. & Hol, W. G. J. (1999). Model error assessment from difference density maps.  A novel method to assess the global and local correctness of macro-molecular crystal structures. Acta Cryst. D55, 206-218.

229. Redinbo, M. R., Champoux, J. J. & Hol, W. G. J. (1999). Structural insights into the function of type IB topoisomerases. Curr. Opin. Struct. Biol. 9, 29-36.

230. Izard, T., Ævarsson, A., Allen, M. D., Westphal, A. H., Perham, R. N., de Kok, A. & Hol, W. G. J. (1999). Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes. Proc. Natl. Acad. Sci. USA 96, 1240-1245.

231. Diller, D. J. & Hol, W. G. J. (1999). An accurate numerical model for calculating the equilibration rate of a hanging drop experiment. Acta Cryst. D55, 656-663.

232. Goranson-Siekierke, J., Pohl, E., Hol, W. G. J. & Holmes, R. K. (1999). Anion-coordinating residues at binding site 1 are essential for the biological activity of the diphtheria toxin repressor (DtxR). Infect. Immun. 67, 1806-1811.

233. Aronov, A. M., Suresh, S., Buckner, F. S., van Voorhis, W. C., Verlinde, C. L. M. J., Hol, W. G. J. & Gelb, M. H. (1999). Structure-based design of sub-micromolar, biologically active inhibitors of trypanosomatid glyceraldehyde-3-phosphate dehydrogenase. Proc. Natl. Acad. Sci. USA 96, 4273-4278.

234. Minke, W. E., Roach, C., Hol, W. G. J. & Verlinde, C. L. M. J. (1999). Structure-based exploration of the ganglioside GM1 binding sites of E. coli heat-labile enterotoxin and cholera toxin for the discovery of receptor antagonists. Biochemistry 38, 5684-5692.

235. Minke, W. E., Diller, D. J., Hol, W. G. J. & Verlinde, C. L. M. J. (1999). The role of waters in flexible docking strategies for carbohydrate derivatives:  heat-labile enterotoxin, a multivalent test case. J. Med. Chem. 42, 1778-1788.

236. Ævarsson, A., Seger, R., Turley, S., Sokatch, J. R. & Hol, W. G. J. (1999). Crystal structure of 2-oxoisovalerate dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes. Nat. Struct. Biol. 6, 785-792.

237. Diller, D. J., Pohl, E., Redinbo, M. R., Hovey, B. & Hol, W. G. J. (1999). A rapid method for positioning small flexible molecules, nucleic acids, and large protein fragments in experimental electron density maps. Proteins 36, 512-525.

238. Diller, D. J., Redinbo, M. R., Pohl, E. & Hol, W. G. J. (1999). A database method for automated map interpretation in protein crystallography. Proteins 36, 526-541.

239. Pohl, E., Holmes, R. K. & Hol, W. G. J. (1999). Crystal structure of a cobalt-activated diphtheria toxin repressor-DNA complex reveals a metal-binding SH3-like domain. J. Mol. Biol. 292, 653-667.

240. Redinbo, M. R., Stewart, L., Champoux, J. J. & Hol, W. G. J. (1999). Structural flexibility in human topoisomerase I revealed in multiple non-isomorphous crystal structures. J. Mol. Biol. 292, 685-696.

241. Kumar, A., Ævarsson, A. & Hol, W. G. J. (1999). Multi-protein assemblies with point group symmetry. In Perspectives in Structural Biology. A volume in honor of G.N. Ramachandran (Vijayan, M., Yathindra, N. & Kolaskar, A. S., eds.), pp. 449-466. Universities Press (India) Ltd., Hyderabad, India.

242. Minke, W. E., Hong, F., Verlinde, C. L. M. J., Hol, W. G. J. & Fan, E. (1999). Using a galactose library for exploration of a novel hydrophobic pocket in the receptor binding site of the E. coli heat-labile enterotoxin. J. Biol. Chem. 274, 33469-33473.

2000

244. Baca, A. M. & Hol, W. G. J. (2000). Overcoming codon bias:  A useful method for high-level overexpression of Plasmodium and AT-rich parasite genes in Escherichia coli. Intl. J. Parasitol. 30, 113-118.

245. Ævarsson, A., Chuang, J., Wynn, M., Turley, S., Chuang, D. & Hol, W. G. J. (2000). Crystal structure of human branched-chain a-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease. Structure 8, 277-291.

246. Fan, E., Zhang, Z., Minke, W. E., Hou, Z., Verlinde, C. L. M. J. & Hol, W. G. J. (2000). A 10⁵ gain in affinity for pentavalent ligands of E. coli heat-labile enterotoxin by modular structure-based design. J. Am. Chem. Soc. 122, 2663-2664.

247. Suresh, S., Drmota, T., Turley, S., Opperdoes, F. R., Michels, P. A. M. & Hol, W. G. J. (2000). A potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishmania mexicana. Structure Fold. Des. 8, 541-552.

248. van den Akker, F., Merritt, E. A. & Hol, W. G. J. (2000). Structure and function of cholera toxin and related enterotoxins. In Handbook of Experimental Pharmacology - Bacterial Protein Toxins (Aktories, K. & Just, I., eds.), Vol. 145, pp. 109-131. Springer-Verlag, Berlin.

249. Redinbo, M. R., Champoux, J. J. & Hol, W. G. J. (2000). Novel insights into catalytic mechanism from a crystal structure of human topoisomerase I in complex with DNA. Biochemistry 39, 6832-6840.

250. Minke, W. E., Pickens, J., Merritt, E. A., Fan, E., Verlinde, C. L. M. J. & Hol, W. G. J. (2000). Structure of m-carboxyphenyl-a-D-galactose complexed to heat-labile enterotoxin at 1.3 Å resolution:  surprising variations in ligand binding modes. Acta Cryst. D56, 795-804.

251. Chudzik, D. M., Michels, P. A., de Walque, S. & Hol, W. G. J. (2000). Structures of type 2 peroxisomal targeting signals in two trypanosomatid aldolases. J. Mol. Biol. 300, 697-707.

252. Baca, A. M., Sirawaraporn, R., Turley, S., Sirawaraporn, W. & Hol, W. G. J. (2000). Crystal structure of Mycobacterium tuberculosis 7,8-dihydropteroate synthase in complex with pterin monophosphate: New insight into the enzymatic mechanism and sulfa-drug action. J. Mol. Biol. 302, 1193-1212.

253.  Kim, Y., Yoon, K.-H., Khang, Y., Turley, S. & Hol, W. G. J. (2000). The 2.0 Å crystal structure of cephalosporin acylase. Stucture 8, 1059-1068.

254. Hol, W. G. J. (2000). Structural genomics for science and society. Nat. Struct. Biol. 7, 964-966.

255. Bressi, J. C., Choe, J., Hough, M. T., Buckner, F. S., Van Voorhis, W. C., Verlinde, C. L. M. J., Hol, W. G. J. & Gelb, M. H. (2000). Adenosine analogues as inhibitors of Trypanosoma brucei phosphoglycerate kinase: Elucidation of a novel binding mode for a 2-amino-N6-substituted adenosine derivative. J. Med. Chem. 43, 4135-4150.

256. Fan, E., Merritt, E. A., Verlinde, C. L. M. J. & Hol, W. G. J. (2000). AB5 toxins: structures and inhibitor design. Curr. Opin. Struct. Biol. 10, 680-686.

257. Fan, E., Merritt, E. A., Zhang, Z., Pickens, J., Roach, C., Ahn, M. & Hol, W. G. J. (2001). Exploration of the GM1 receptor binding site of heat-labile enterotoxin and cholera toxin by phenyl ring-containing galactose derivatives. Acta Cryst. D57, 201-212.

258. Feese, M. D., Ingason, B. P., Goranson-Siekierke, J., Holmes, R. K. & Hol, W. G. J. (2001). Crystal structure of the iron-dependent regulator (IdeR) from Mycobacterium tuberculosis at 2.0 Å resolution reveals the SH3-like fold and metal binding function of the third domain. J. Biol. Chem. 276, 5959-5966.

259. Verlinde, C. L. M. J., Hannaert, V., Blonski, C., Willson, M., Périé, J. J., Fothergill-Gilmore, L. A., Opperdoes, F. R., Gelb, M. H., Hol, W. G. J. & Michels, P. A. M. (2001). Glycolysis as a target for the design of new anti-trypanosome drugs. Drug Resistance Updates 4, 50-65.

260. Kumar, A., Roach, C., Hirsh, I. S., Turley, S., deWalque, S., Michels, P. A. M. & Hol, W. G. J. (2001). An unexpected extended conformation for the third TPR motif of the peroxin PEX5 from Trypanosoma brucei. J. Mol. Biol. 307, 271-282.

261. Pohl, E., Goranson-Siekierke, J., Choi, M. K., Roosild, T., Holmes, R. K. & Hol, W. G. J. (2001). Structures of three diphtheria toxin repressor (DtxR) variants with decreased repressor activity. Acta Cryst. D57, 619-627.

262. Ghosh, A. K., Hol, W. G. & Fan, E. (2001). Solid-phase synthesis of N-acyl-N'-alkyl/aryl disubstituted guanidines. J. Org. Chem. 66, 2161-2164.

263. Suresh, S., Bressi, J. C., Kennedy, K. J., Verlinde, C. L. M. J., Gelb, M. H. & Hol, W. G. J. (2001). Conformational changes in Leishmania mexicana glyceraldehyde-3-phosphate dehydrogenase induced by designed inhibitors. J. Mol. Biol. 309, 423-435.

264. Feese, M. D., Pohl, E., Holmes, R. K. & Hol, W. G. J. (2001). Iron-dependent regulators. In Handbook of Metalloproteins (Wieghardt, K., Huber, R., Poulos, T. & Messerschmidt, A., eds.), pp. 850-863. Wiley & Sons, Chichester.

265. Bressi, J. C., Verlinde, C. L. M. J., Aronov, A. M., Shaw, M. L., Shin, S. S., Nguyen, L. N., Suresh, S., Buckner, F. S., Van Voorhis, W. C., Kuntz, I. D., Hol, W. G. J. & Gelb, M. H. (2001). Adenosine analogues as selective inhibitors of glyceraldehyde-3-phosphate dehydrogenase of Trypanosomatidae via structure-based drug design. J. Med. Chem. 44, 2080-2093.

266. Aman, A. T., Fraser, S., Merritt, E. A., Rodigherio, C., Kenny, M., Ahn, M., Hol, W. G. J., Williams, N. A., Lencer, W. I. & Hirst, T. R. (2001). A mutant cholera toxin B subunit that binds GM1-ganglioside but lacks immunomodulatory or toxic activity. Proc. Natl. Acad. Sci. USA 98, 8536-8541.

267. Hol, W. G. J. & Verlinde, C. L. M. J. (2001). Macromolecular crystallography and medicine. In International Tables for Crystallography, Volume F.  Crystallography of Biological Macromolecules (Rossmann, M. & Arnold, E., eds.), pp. 10-43. Kluwer Academic Publishers, Dordrecht.

268. Kim, Y., Kim, S., Earnest, T. N. & Hol, W. G. J. (2001). Precursor structure of cephalosporin acylase: Insights into auto-proteolytic activation in a new N-terminal hydrolase family. J. Biol. Chem. 277, 2823-2829.

269. Kim, Y. & Hol, W. G. J. (2001). Structure of cephalosphorin acylase in complex with glutaryl-7-aminocephalosporanic acid and glutarate: insight into the basis of its substrate specificity. Chem. Biol. 8, 1253-1264.

2002

270. Pickens, J. C., Merritt, E. A., Ahn, M., Verlinde, C. L. M. J., Hol, W. G. J. & Fan, E. (2002). Anchor-based design of improved cholera toxin and E. coli heat-labile enterotoxin receptor binding antagonists that display multiple binding modes. Chem. Biol. 9, 215-224.

271. Davies, D. R., Interthal, H., Champoux, J. J. & Hol, W. G. J. (2002). The crystal structure of human tyrosyl-DNA phosphodiesterase, Tdp1. Structure 10, 237-248.

272. Kumar, A., Nguyen, K. T., Svrivathsan, S., Ornstein, B., Turley, S., Hirsh, I., Pei, D. & Hol, W. G. J. (2002). Crystals of peptide deformylase from Plasmodium falciparum reveal critical characteristics of the active site for drug design. Structure 10, 357-367.

273. Gelb, M. H. & Hol, W. G. J. (2002). Drugs against Tropical Protozoan Parasites : Target Selection, Structural Biology and Rational Medical Chemistry. Science 297, 343-344.

274. Merritt, E. A., Zhang, Z., Pickens, J. C., Ahn, M., Fan, E. & Hol, W. G. J. (2002). Characterization and crystal structure of a high-affinity pentavalent receptor-binding inhibitor for Cholera toxin and E. coli heat-labile enterotoxin. J. Am. Chem. Soc. 124, 8818-8824.
(Editor's Choice in Chemistry, Science 297, 3003 (2002))

275. Martinez, S. E., Glavas, N. A., Tang, X.-B., Turley, S., Hol, W. G. J. & Beavo, J. A. (2002). The two GAF domains in phosphodiesterase 2A have distinct roles in dimerization and in cGMP binding. Proc. Natl. Acad. Sci. USA, 99, 13260-13265

276. Zhang, Z., Merritt, E.A., Ahn, M., Roach, C., and Hol, W.G.J. (2002). Solution and Crystallographic Studies of Branched Multivalent Ligands that Inhibit the Receptor-Binding Process of Cholera Toxin. J. Am. Chem. Soc. 124, 12991-12998.

277. Davies, D.R., Interthal, H., Champoux, J.J., and Hol, W.G.J. (2002). Insights into Substrate Binding and Catalytic Mechanism of Human Tyrosyl DNA hosphodiesterase from Vanadate- and Tungstate- Inhibited Structures. J. Mol. Biol. 324, 917-932.

278. Choe, J., Suresh, S., Wisedchaisri, G., Kennedy, K.J., Gelb, M.H., and Hol, W.G.J. (2002). Anomalous Differences of Light Elements in Determining Precise Binding Modes of Ligand to Drug Target Proteins - the Case of Glycerol-3-phosphate Dehydrogenase from Leishmania mexicana. Chem & Biol 9, 1189-1197.

279. Verlinde, C.L.M.J., Bressi, J.C., Choe, J., Suresh, S., Buckner, F.S., Van Voorhis, W.C., Michels, P.A.M., Gelb, M.H., and Hol, W.G.J. (2002). Protein structure-based design of anti-protozoal drugs. J. Braz. Chem. Soc. 13, 843-848.

2003

280. Davies, D.R., Interthal, H., Champoux, J.J., and Hol, W.G.J. (2003). Crystal Structure of a Transition State Mimic for Tyrosyl-DNA Phosphodiesterase (Tdp1) Assembled from Vanadate,DNA, and a Topoisomerase I-derived Peptide. Chem & Biol. 10, 139-147 (Cover Figure).

281. Quigley, P. M., Korotkov, K., Baneyx, F. & Hol, W. G. J. (2003). The 1.6 Å Crystal Structure of the Novel Class Of Chaperones Represented by E.coli Hsp31 Reveals a Putative Catalytic Triad. PNAS 100, 3137-3142.

282. Choe, J., Guerra, D., Michels, P. A. M., Opperdoes, F. R. & Hol, W. G. J. (2003). Leishmania mexicana glycerol-3-phosphate dehydrogenase showed conformational changes upon binding a bisubstrate adduct.. J. Mol. Biol. 329, 335-349.

283. Moyersoen, J., Choe, J., Kumar, A., Voncken, G. J., Hol, W. G. J. & Michels, P. A. M. (2003). Characterization of Trypanosoma brucei PEX14 and its role in the import of glycosomal matrix proteins. Eur. J. Biochem. 270, 2059-2067 (Cover Figure).

284. Tinker, J. K., Erbe, J. L., Hol, W. G. J. & Holmes, R. K. (2003). Cholera Holotoxin Assembly Requires a Hydrophobic Domain at the A-B5 Interface: Mutational Analysis and Development of an in vitro Assembly System. Infect. Immun. 71, 4093-4101

285. Hu, X., Nguyen, K.T., Verlinde, C.L.M.J., Hol, W.G.J., and Pei, D. (2003). Structure-Based Design of a Macrocyclic Inhibitor for Peptide Deformylase. J. Med. Chem 46, 3771-3774.

286. Choe, J., Moyersoen, J., Roach, C., Carter, T., Fan, E., Michels, P. A. M. & Hol, W. G. J. (2003). Analysis of the sequence motifs responsible for the interaction of peroxins 14 and 5 involved in glycosome biogenesis in Trypanosoma brucei. Biochemistry 42, 10915-10922

287. Robien, M. A., Krumm, B. E., Sandkvist, M. & Hol, W. G. J. (2003). Crystal structure of the extracellular protein secretion NTPase EpsE of Vibrio cholerae. J Mol Biol 333, 657-674.

288. Martinez, S. E., Tang, X., Hol, W. G. J. & Beavo, J. A. (2003). Cyclic Nucleotide-binding Phosphodiesterase and Cyclase GAF Domains. In Handbook of Cell Signaling (Bradshaw, R., ed.), Vol. 2, pp. 525-529. Academic Press.

289. Buscaglia, C. A., Coppens, I., Hol, W. G. J. & Nussenzweig, V. (2003). Sites of Interaction between Aldolase and Thrombospondin-related Anonymous Protein in Plasmodium. Mol. Biol. Cell 14, 4947-4957.

2004

290. Deng, J., Davies, D. R., Wisedchaisri, G., Wu, M., Hol, W. G. J. & Mehlin, C. (2004). An Improved Protocol for Rapid Freezing of Protein Samples for Long-Term Storage. Acta Crystallogr. D 60, 203-204.

291. Interthal, H., Quigley, P. M., Hol, W. G. J. & Champoux, J. J. (2004). The role of Lysine 532 in the catalytic mechanism of human topoisomerase I. J. Biol. Chem. 279, 2984-2992.

292. Quigley, P. M., Korotkov, K., Baneyx, F. & Hol, W. G. J. (2004). A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function. Protein Sci. 13, 269-277.

293. Mitchell, D. D., Pickens, J. C., Korotkov, K., Fan, E. & Hol, W. G. J. (2004). 3,5-Substituted Phenyl Galactosides as Leads in Designing Effective Cholera Toxin Antagonists: Synthesis and Crystallographic Studies. Bioorganic & Med Chem 12, 907-920.

294. Yeh, J. I., Charrier, V., Paulo, J., Hou, L., Darbon, E., Claiborne, A., Hol, W. G. J. & Deutscher, J. (2004). Structures of Enterococcal Glycerol Kinase in the Absence and Presence of Glycerol: Correlation of conformation to substrate binding and a mechanism of activation by phosphorylation. Biochemistry 43, 362-373.

295. Davies, D. R., Interthal, H., Champoux, J. J. & Hol, W. G. J. (2004). Explorations of Peptide and Oligonucleotide Binding Sites of Tyrosyl-DNA Phosphodiesterase (Tdp1) Using Vanadate Complexes. J Med. Chem. 47, 829-837.

296. Robien, M. A., Nguyen, K. T., Kumar, A., Hirsh, I., Turley, S., Pei, D. & Hol, W. G. J. (2004). Crystal Engineering of Plasmodium falciparum peptide deformylase. Protein Sci. 13, 1155-1163.

297. O'Neal, C. J., Amaya, E. I., Jobling, M. G., Holmes, R. K. & Hol, W. G. J. (2004). Crystal structures of an intrinsically active cholera toxin mutant yield insight into the toxin activation mechanism. Biochemistry 43, 3772-3782.

298.Roberts, D. M., Liao, R. P., Wisedchaisri, G., Hol, W. G. J. & Sherman, D. R. (2004). Two sensor kinases contribute to the hypoxic response of Mycobacterium tuberculosis. J Biol. Chem. 279, 23082-23087.

299. Abendroth, J., Rice, A. E., McLuskey, K., Bagdasarian, M. & Hol, W. G. J. (2004). The crystal structure of the periplasmic domain of the type II secretion system protein EpsM from Vibrio cholerae: the simplest version of the ferredoxin fold. J. Mol. Biol. 338, 585-596.

300. Zhang, Z., Pickens, J. C., Hol, W. G. J. & Fan, E. Solution and solid-phase syntheses of guanidine-bridged, water-soluble linkers for multivalent ligand design. Org. Lett. 6, 1377-1380.

301. Sastry, M. S. R., Quigley, P. M., Hol, W. G. J. & Baneyx, F. (2004). Chaperone Hsp31 linker region is a thermal gate modulating high affinity substrate binding. PNAS 101, 8587-8592.

302. Wisedchaisri, G., Holmes, R. K. & Hol, W. G. J. (2004). Crystal Structure of an IdeR-DNA Complex Reveals a Conformational Change in Activated IdeR for Base-specific Interactions. JMB 342, 1155-1169.

303. Pickens, J. C., Mitchell, D. D., Tan, X.-J., Zhang, Z., Verlinde, C. L. M. J., Hol, W. G. J. & Fan, E. (2004) Rational Design of Bivalent Ligands Targeting the B Subunits of Cholera Toxin and Heat-Labile Enterotoxin from E. coli. Chem & Biol.11, 1205-1215.

304. Fan, E., O'Neal, C. J., Mitchell, D. D., Robien, M. A., Zhang, Z., et al. (2004). Structural Biology and Structure-based Inhibitor Design of Cholera Toxin and Heat-labile Enterotoxin. IJMM 294, 217-223

305. Deng, J., Schnaufer, A., Salavati, R., Stuart, K. & Hol, W. G. J. (2004). High Resolution Crystal Structure of an Editosome Enzyme from Trypanosoma brucei: RNA Editing ligase I. J Mol Biol 343, 601-613

306. Abendroth, J., Bagdasarian, M., Sandkvist, M. & Hol, W. G. J. (2004). The structure of the cytoplasmic domain of EpsL, an inner membrane component of the type II secretion system of Vibrio cholerae: a member of the actin-like ATPase superfamily. J Mol Biol 344, 619-633.

307. Moyersoen, J., Choe, J., Fan, E., Hol, W. G. J. & Michels, P. A. M. (2004). Biogenesis of peroxisomes and glycosomes: trypanosomatid glycosome assembly is a promising new drug target. FEMS Microbiol. Rev 28, 603-643.

308. Davies, D.R. & Hol, W.G.J. 2004 The Power of Vanadate In Crystallographic Investigations of Phosphoryl Transfer Enzymes. FEBS Lett. 577, 315-321.

309. Chou, C. J., Wisedchaisri, G., Holmes, R. K., Hol, W. G. J. & Beeson, C. (2004). Functional Studies of the Mycobacterium tuberculosis Iron-Dependent Regulator. J Biol. Chem. 279, 53554 - 53561.

310. Strynadka, N. C. & Hol, W. G. J. (2004). Proteins The dazzling complexity and flexibility of proteins. Curr. Opin. Struct. Biol 14, 687-689

311. Alexandrov, A., Vignali, M., LaCount, D., Quartley, E., deVries, C., De Rosa, D., Babulski, J., Mitchell, S., Schoenfeld, L., Fields, S., Hol, W., Dumont, M., Phizicky, E. & Grayhack, E. (2004). A facile method for high-throughput co-expression of protein pairs. Mol. Cell. Proteomics 3, 934-938.

2005

312. Liu, J., Zhang, Z., Tan, X.-J., Hol, W. G. J., Verlinde, C. L. M. J. & Fan, E. (2005). Protein Heterodimerization through Ligand-Bridged Multivalent Pre-organization: Enhancing Ligand Binding toward Both Protein Targets. JACS 127, 2044-2045.

313. Abendroth, J., Murphy, P., Sandkvist, M., Bagdasarian, M. & Hol, W. G. J. (2005). The X-ray structure of the Type II Secretion System Complex Formed by the N-Terminal Domain of EpsE and the Cytoplasmic Domain of EpsL of Vibrio cholerae. J. Mol. Biol. 348, 845-855.

314. O'Neal, C. J., Jobling, M. G., Holmes, R. K. & Hol, W. G. J. (2005). Structural basis for the activation of cholera toxin by human ARF6-GTP. Science 309, 1093-1096.

315. Schnick, C., Robien, M. A., Brzozoski, A. M., Dodson, E. J., Murshodov, G. N., Anderson, L., Luft, J., Mehlin, C., Hol, W. G. J., Brannigan, J. A. & Wilkinson, A. J. (2005). Crystal structures of the Plasmodium falciparum Purine Nucleoside Phosphorylase complexed with sulphate and its natural substrate inosine. Acta Crystallogr. D 61, 1245-1254

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