SHIRLEY_UPDATE_PUBLICATIONS

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27) R. J. Dennis, E.J. Taylor, M. S. Maculey, K. A. Stubbs, J.P. Turkenburg, S.J. Hart, G. Black,
D. J. Vocadlo*, G.J. Davies*. Structure and mechanism of a bacterial -glucosaminidase having
O-GlcNAcase activity. Nat. Struct. Mol. Biol. 2006, In the Press.
26) N. Cetinbas, M. S. Macauley, K. A. Stubbs, R. Drapala, D. J. Vocadlo* Identification of
Asp(174) and Asp(175) as the Key Catalytic Residues of Human O-GlcNAcase by Functional
Analysis of Site-Directed Mutants. Biochemistry 2006, 45, 3835-3844
25) K. A. Stubbs, N. Zhang, and D. J. Vocadlo*, A Divergent Synthesis of 2-Acyl Derivatives of
PUGNAc Yields Selective Inhibitors of O-GlcNAcase. Org. Biomol. Chem., 2005, 4, 839-845.
24) K. A. Stubbs, M. A. Macauley, and Vocadlo, D. J. *, A Simple and Concise Synthesis of Aryl
2-acetamido-2-deoxy-1-thio--D-glucopyranosides. Carbohydr. Res., 2006, Feb 9, On-Line.
23) Molecular basis for G protein control of ATP sulfurylase in bacteria. G. J. Mougous, D. H.
Lee, S. C. Hubbard, M. W. Schelle, D. J. Vocadlo, J. M. Berger*, and C. R. Bertozzi*. Mol. Cell.,
2006, 21, 109-122.
22) Human O-GlcNAcase catalyses hydrolysis of thioglycosides without acid catalysis. M. S.
Macauley, K.A. Stubbs, D. J. Vocadlo*. J. Am. Chem. Soc., 2005, 14, 17202-17203.
21) M. S. Macauley, G. E. Whitworth, A. Debowski, D. Chin, and D. J. Vocadlo*. Human OGlcNAcase uses substrate-assisted catalysis: kinetic analysis and development of highly
selective, cell permeable, mechanism-inspired inhibitors. J. Biol. Chem., 2005, 280, 2531325322.
20) D. J. Vocadlo and S. G. Withers*. Detailed comparative analysis of the catalytic mechanisms
of -N-acetylglucosaminidases from families 3 and 20 of glycoside hydrolases. Biochemistry,
2005, 44, 12809-12818.
19) D. J. Vocadlo and S. G. Withers*. The chemical synthesis of dissacharide probes of the hen
egg white mechanism. Carbohydr. Res. 2005, 340, 379-88.
18) D. J. Vocadlo* and C. R. Bertozzi*. A strategy for functional proteomic analysis of
glycosidase activity from cell lysates, Angew. Chem. Int. Ed., 2004, 43, 5338-5342.
17) J. K. Yang, H.-J. Yoon, H. J. Ahn, B. I. Lee, J.-D. Pedelacq, E. C. Liong, J. Berendzen, M.
Laivenieks, C. Vieille, G. J. Zeikus, D. J. Vocadlo, S. G. Withers, and S. W. Suh.* Crystal
structure of -D-xylosidase from Thermoanaerobacterium saccharolyticum, a glycoside hydrolase
of family 39. J. Mol. Biol. 2004, 335, 155-165.
16) D. J. Vocadlo, H. Hang, E.-J. Kim, J. Hanover, C. R. Bertozzi*. A chemical approach for
identification of O-GlcNAc modified proteins. Proc. Nat. Acad. Sci., USA, 2003, 100, 9116-9121.
15) S. J. Williams, B. L. Mark, D. J. Vocadlo, M.N.G. James, and S. G. Withers*. Aspartate 313
in the Streptomyces plicatus -hexosaminidase plays a critical role in substrate assisted catalysis
by orienting the 2-acetamido group and stabilizing the transition state. J. Biol. Chem., 2002, 277,
40055-40065.
14) D. J. Vocadlo, J. Wicki, K. Rupitz, S. G. Withers*. A case for reverse protonation:
identification of the acid/base catalyst residue in Thermoanaerobacterium saccharolyticum xylosidase and detailed kinetic analysis of a site-directed mutant. Biochemistry 2002, 41, 92369246.
13) D. J. Vocadlo, J. Wicki, K. Rupitz, S. G. Withers*. Mechanism of Thermoanaerobacterium
saccharolyticum -xylosidase: kinetic studies. Biochemistry 2002, 41, 9727-9735.
12) B. L. Mark, D. J. Vocadlo, S. Knapp, S. G. Withers, M. N. G. James*. Biochemical and
structural assessment of the 1-N-azasugar GalNAc-isofagomine as a potent family 20 -Nacetylhexosaminidase inhibitor. J. Biol. Chem. 2001, 276, 42131-42137.
11) D. J. Vocadlo, G. J. Davies, R. Laine, S. G. Withers*. Catalysis by hen egg white lysozyme
proceeds via a covalent intermediate. Nature. 2001, 412, 835-3838.
10) B. L. Mark, D. J. Vocadlo, S. Knapp, B. Triggs-Raine, S. G. Withers, M. N. G. James*.
Crystallographic evidence for substrate-assisted catalysis in a bacterial -hexosaminidase. J.
Biol. Chem. 2001, 276, 10330-10337.
9) Y. Hou, D. J. Vocadlo, S. G. Withers, D. Mahuran*. Characterization of the Glu and Asp
residues in the active site of human -hexosaminidase B. Biochemistry. 2001, 40, 2201-2209.
5) Y. Hou, D. Vocadlo, S. Withers, and D. Mahuran*. Role of Arg211 in the Active Site of Human
-Hexosaminidase B. Biochemistry. 2000, 39, 6219-6227.
4) D. J. Vocadlo, C. Mayer, He, S. M., Withers, S. G*. Mechanism of action and identification of
Asp242 as the catalytic nucleophile of Vibrio furnisii N-acetyl--D-glucosaminidase using 2acetamido-2-deoxy-5-fluoro--L-idopyranosyl fluoride. Biochemistry 2000, 39, 117-126.
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