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References for Wim Hol Research Summary Part II

1. Spangler, B. D. (1992). Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin. Microbiol. Rev. 56, 622-647.
2. Oppenheimer, N. J. (1978). Structural determination and stereospecificity of the choleragen-catalyzed reaction of NAD+ with guanidines. J. Biol. Chem. 253, 4907-4910.
3. 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.
4. 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 accepted
5. 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.
6. 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.
7. 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.
8. 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.
9. 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.
10. van den Akker, F., Steensma, E. & Hol, W. G. J. (1996). Tumor marker disaccharide D-Gal-ß1,3-GalNAc complexed to heat-labile enterotoxin from Escherichia coli. 5, 1. Protein Science 5, 184-1188.
11. Merritt, E. A., Sarfaty, S., Feil, I. K. & Hol, W. G. J. (1997). Structural foundation for the design of receptor antagonists targeting Escherichia coli heat-labile enterotoxin. Structure 5, 1485-1499.
12. 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.
13. Merritt, E. A., Kuhn, P., Sarfaty, S., Erbe, J. L., Holmes, R. K. & Hol, W. G. J. (1998). 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.
14. 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.
15. van den Akker, F., Merritt, E. A. & Hol, W. G. J. (1999). Structure and function of cholera toxin and related enterotoxins. In Handbook of Experimental Pharmacology (Aktories, K., ed.), Vol. 145. Springer-Verlag, Berlin.
16. Minke, W. E., Pickens, J., Merritt, E. A., Fan, E., Verlinde, C. L. M. J. & Hol, W. G. J. (2000). Structure of m-carboxyphenyl-D-galactose complexed to heat-labile enterotoxin at 1.3 Å resolution: surprising variations in ligand binding modes. Acta Cryst. D56, 795-804.
17. 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.
18. 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.
19. 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.
20. 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 Submitted
21. Fan, E., Zhang, Z., Minke, W. E., Hou, Z., Verlinde, C. L. M. J. & Hol, W. G. J. (2000). High affinity pentavalent ligands of Escherichia coli heat-labile enterotoxin by modular structure-based design. J. Am. Chem. Soc. 122, 2663-2664. Highlighted in Chemical & Engineering News (March 27, 2000) vol. 78, p. 22.
22. 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)).
23. Zhang, Z., Merritt, E. A., Ahn, M., Roach, C., Hou, Z., Verlinde, C. L. M. J., Hol, W. G. J. & Fan, E. (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.
24. Zhang, Z., Pickens, J. C., Hol, W. G. J. & Fan, E. (2004). Solution and solid-phase syntheses of guanidine-bridged, water-soluble linkers for multivalent ligand design. Org. Lett. Submitted
25. Michels, P., Hannaert, V. & Bringaud, F. (2000). Metabolic aspects of glycosomes in trypanosomatidae - new data and views. Parasitol Today 16, 482-489.
26. Brocard, C. B., Jedeszko, C., Song, H. C., Terlecky, S. R. & Walton, P. A. (2003). Protein structure and import into the peroxisomal matrix. Traffic 4, 74-82.
27. Eckert, J. H. & Erdmann, R. (2003). Peroxisome biogenesis. Rev. Physiol. Biochem. Pharmacol. 147, 75-121.
28. Sparkes, I. & Baker, A. (2002). Peroxisome biogenesis and protein import in plants, animals and yeasts: enigma and variations? Mol Membr Biol 19, 171-185.
29. Moyersoen, J., Choe, J., Fan, E., Hol, W. G. J. & Michels, P. A. M. (2004). Glycosome biogenesis in trypanosomes; a promising drug target. FEMS Microbiol Reviews in preparation
30. Suresh, S., 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.
31. Choe, J., Suresh, S., Wisedchaisri, G., Kennedy, K. J., Gelb, M. H. & 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.
32. 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.
33. Purdue, P. & Lazarow, P. (2001). Peroxisome biogenesis. Annu Rev Cell Dev Biol. 17, 701-752.
34. 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.
35. 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).
36. 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.
37. Gupta, M., Fujimori, A. & Pommier, Y. (1995). Eukaryotic DNA topoisomerases I.. Biochim. Biophys. Acta 1262, 1-14.
38. Wang, J. C. (1996). DNA Topoisomerases. Annu. Rev. Biochem. 65, 635-692.
39. 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.
40. Champoux, J. J. (1998). Domains of human topoisomerase I and associated functions. . Prog. Nucleic Acid Res. Mol. Biol. 60, 111-132.
41. Bodley, A. L. & Shapiro, T. A. (1995). Molecular and cytotoxic effects of camptothecin, a topoisomerase I inhibitor, on trypanosomes and Leishmania. Proc Natl Acad Sci U S A 92, 3726-30.
42. Bodley, A. L., Cumming, J. N. & Shapiro, T. A. (1998). Effects of camptothecin, a topoisomerase I inhibitor, on Plasmodium falciparum. Biochem Pharmacol 55, 709-11.
43. Jonckers, T. H., van Miert, S., Cimanga, K., Bailly, C., Colson, P., De Pauw-Gillet, M. C., van den Heuvel, H., Claeys, M., Lemiere, F., Esmans, E. L., Rozenski, J., Quirijnen, L., Maes, L., Dommisse, R., Lemiere, G. L., Vlietinck, A. & Pieters, L. (2002). Synthesis, cytotoxicity, and antiplasmodial and antitrypanosomal activity of new neocryptolepine derivatives. J Med Chem 45, 3497-508.
44. 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.
45. 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.
46. 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.
47. 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.
48. Yang, S. W., Burgin, A. B., Jr., Huizenga, B. N., Robertson, C. A., Yao, K. C. & Nash, H. A. (1996). A eukaryotic enzyme that can disjoin dead-end covalent complexes between DNA and type I topoisomerases. Proc Natl Acad Sci U S A 93, 11534-9.
49. Pouliot, J. J., Yao, K. C., Robertson, C. A. & Nash, H. A. (1999). Yeast gene for a Tyr-DNA phosphodiesterase that repairs topoisomerase I complexes. Science 286, 552-5.
50. Interthal, H., Pouliot, J. J. & Champoux, J. J. (2001). The tyrosyl-DNA phosphodiesterase Tdp1 is a member of the phospholipase D superfamily. Proc. Natl. Acad. Sci. USA 98, 12009-12014.
51. 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.
52. Davies, D. R., Interthal, H., Champoux, J. J. & 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.
53. Davies, D. R., Interthal, H., Champoux, J. J. & 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).
54. 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.
55. Frieden, T., Sterling, T., Munsiff, S., Watt, C. & C., D. (2003). Tuberculosis. Lancet 362, 887-899.
56. Dye, C., Scheele, S., Dolin, P., Pathania, V. & Raviglione, M. (1999). Consensus statement. Global burden of tuberculosis: estimated incidence, prevalence, and mortality by country. WHO Global Surveillance and Monitoring Project. JAMA 282, 677-686.
57. Enarson, D. A. & Murray, J. F. (1996). In Tuberculosis (Rom, W. N., and Garay, S.,, ed.), pp. 55-75. Little, Brown and Co., Boston.
58. Rodriguez, G. M., Voskuil, M. I., Gold, B., Schoolnik, G. K. & Smith, I. (2002). IdeR, an Essential Gene in Mycobacterium tuberculosis: Role of IdeR in Iron-Dependent Gene Expression, Iron Metabolism, and Oxidative Stress Response. Infect. Immun. 70, 3371-3381.
59. 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.
60. Wisedchaisri, G., Holmes, R. K. & Hol, W. G. J. (2004). The crystal structure of mycobacterium tuberculosis IdeR in complex with mbtA/mbtB operator DNA. in preparation
61. 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.
62. Park, H., Guinn, K., Harrell, M., Liao, R., Voskuil, M., Tompa, M., Schoolnik, G. & Sherman, D. (2003). Rv3133c/dosR is a transcription factor that mediates the hypoxic response of Mycobacterium tuberculosis. Mol Microbiol. 48, 833-843.
63. Roberts, D. M., Liao, R. P., Wisedchaisri, G., Hol, W. G. J. & Sherman, D. R. (2004). Characterization of a novel sensor kinase DosS2 and the DosR-DosS two-component signaling mechanism involved in the response of Mycobacterium tuberculosis to hypoxic conditions. J. Biol. Chem. submitted
64. Myllykallio, H., Lipowski, G., Leduc, D., Filee, J., Forterre, P. & Liebl, U. (2002). An Alternative Flavin-Dependent Mechanism for Thymidylate Synthesis. Science 297, 105-107.
65. Sibley, C. (2003). Personal communication.
66. Bracchi-Ricard V, N. K., Zhou Y, Rajagopalan PT, Chakrabarti D, Pei D. (2001). Characterization of an eukaryotic peptide deformylase from Plasmodium falciparum. Arch Biochem Biophys. 396
67. Wiesner, J., Sanderbrand, S., Altincicek, B., Beck, E. & Jomaa, H. (2001). Seeking new targets for antiparasitic agents. Trends Parasitol 17, 7-8.
68. 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.
69. 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. in press
70. Hu, X., Nguyen, K. T., Verlinde, C. L. M. J., Hol, W. G. J. & Pei, D. (2003). Structure-Based Design of a Macrocyclic Inhibitor for Peptide Deformylase. J. Med. Chem 46, 3771-3774.
71. Ingason, B. P., Robien, M. A., Turley, S., Krumm, B. E., Verlinde, C. L. M. J., Pei, D. & Hol, W. G. J. (2004). Cyclic inhibitors bound to P. falciparum peptide deformylase. in preparation
72. Kappe, S., Kaiser, K. & Matuschewski, K. (2003). The Plasmodium sporozoite journey: a rite of passage. Trends Parasitol. . 19, 135-143.
73. 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.
74. 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.
75. Sandkvist, M. & Bagdasarian, M. (1996). Secretion of recombinant proteins by gram-negative bacteria. Curr Opin Biotechnol, 7, 505-511.
76. Russel, M. (1998). Macromolecular assembly and secretion across the bacterial cell envelope: type II protein secretion systems. J Mol Biol 279, 485-499.
77. Sandkvist, M. (2001). Biology of type II secretion. Mol Microbiol 40,, 271-283.
78. Sandkvist, M. (2001). Type II secretion and pathogenesis. Infect Immun 69, 3523-3535.
79. 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.
80. Abendroth, J., Rice, A. E., McLuskey, K., Bagdasarian, M. & Hol, W. G. J. (2003). 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. In press
81. Schneider, A. (2001). Unique aspects of mitochondrial biogenesis in trypanosomatids. International Journal for Parasitology 31, 1403-1415.
82. Pollard, V. W., Harris, M. E. & Hajduk, S. L. (1992). Native mRNA editing complexes from Trypanosoma brucei mitochondria. EMBO 11, 4429-4438.
83. Stuart, K., Allen, T. E., Heidmann, S. & Seiwert, S. D. (1997). RNA editing in kinetoplastid protozoa. Microbiol Mol Biol Rev 61, 105-120.
84. Huang, C., Cruz-Reyes, J., Zhelonkina, A., O'Hearn, S., Wirtz, E. & Sollner-Webb, B. (2001). Roles for ligases in the RNA editing complex of Trypanosoma brucei: band IV is needed for U-deletion and RNA repair. EMBO J 20, 4694-4703.
85. Stuart, K., Panigrahi, A. K., Schnaufer, A., Drozdz, M., Clayton, C. & Salavati, R. (2002). Composition of the editing complex of Trypanosoma brucei. Philos Trans R Soc Lond B Biol Sci 357
86. Simpson, L., Sbicego, S. & Aphasizhev, R. (2003). Uridine insertion/deletion RNA editing in trypanosome mitochondria: a complex business. RNA 9, 265-276.
87. Schnaufer, A., Aswini K. Panigrahi, A. K., Brian Panicucci, B., Robert P. Igo, R. P. J., Salavati, R. & Stuart, K. (2001). An RNA Ligase Essential for RNA Editing and Survival of the Bloodstream Form of Trypanosoma brucei. Science 291, 2159-2162.
88. Deng, J., Schnaufer, A., Stuart, K. & Hol, W. G. J. (2004). Crystal structure of T. brucei RNA ligase Rel1 catalytic domain in complex with ATP at 1.2Å resolution. in preparation
89. Kim, D.-W., Kang, S.-M. & Yoon, K.-H. (1999). Isolation of novel Pseudomonas diminuta KAC-1 strain producing glutaryl 7-Aminocephalosporanic acid acylase. J. Microbiol. 37, 200-205.
90. Kim, Y., Yoon, K.-H., Khang, Y., Turley, S. & Hol, W. G. J. (2000). The 2.0 Å crystal structure of cephalosporin acylase. Structure Fold. Des. 8, 1059-1068.
91. 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.
92. Kim, Y. & Hol, W. G. J. (2001). Structure of cephalosporin acylase in complex with glutaryl-7-aminocephalosporanic acid and glutarate: insight into the basis of its substrate specificity. Chem. Biol. 8, 1253-1264.
93. 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. PNAS 99, 13260-13265.
94. 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.
95. Richmond, C., Glasner, J., Mau, R., Jin, H. & Blattner, F. (1999). Genome-wide expression profiling in Escherichia coli K-12. Nucleic Acids Res. 27, 3821-3835.
96. Malki, A., Kern, R., Abdallah, J. & Richarme, G. (2003). Characterization of the Escherichia coli YedU protein as a molecular chaperone. Biochem Biophys Res Commun. 301, 430-436.
97. Honbou, K., Suzuki, N., Horiuchi, M., Niki, T., Taira, T., Ariga , H. & Inagaki, F. (2003). The crystal structure of DJ-1, a protein related to male fertility and Parkinson's disease. J Biol Chem. 278, 31380-31384.
98. Huai, Q., Sun, Y., Wang, H., Chin, L., Li, L., Robinson, H. & Ke, H. (2003). Crystal structure of DJ-1/RS and implication on familial Parkinson's disease. FEBS Lett. 549, 171-175.
99. Lee, S.-J., Kim, S., Kim, I.-K., Ko, J., Jeong, C.-S., Kim, G.-H., Park, C., Kang, S.-O., Suh, P.-G., Lee, H.-S. & Cha, S.-S. (2003). Crystal Structures of Human DJ-1 and Escherichia coli Hsp31, Which Share an Evolutionarily Conserved Domain. J. Biol. Chem. 278, 44552-44559.
100. Tao, X. & Tong, L. (2003). Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease. J Biol Chem. 278, 31372-31379.
101. Wilson, M. A., Collins, J. L., Hod, Y., Ringe, D. & Petsko, G. A. (2003). The 1.1-A resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease. PNAS 100, 9256-9261.
102. 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.
103. 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.
104. 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 submitted

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