Publications: 2011-current

Jongkees, S. A. K., Caner, S., Tysoe, C. R., Brayer, G. D., Withers, S. G. and Suga, H. “Rapid discovery of potent and selective glycosidase-inhibiting de novo peptides” (2017) Cell Chemical Biology. In Press.

Gao, Z., Niikura, M, and Withers, S. G. “Ultrasensitive fluorogenic neuraminidase titration reagents” (2017) Angew. Chemie, In Press, accepted Jan 24 2017.
Schalli, M. Wolfsgruber, A., Santana, A. G., Tysoe, C. R., Fischer, R., Thonhofer, M., Withers, S. G. and Stuetz, A. “C-5a-Substituted Validamine Type Glycosidase Inhibitors” (2017) Carbohydr. Res. 440, 1-9.

Strazzulli, A., Cobucci-Ponzano, B, Carillo, S., Bedini, E., Corsaro, M. M., Pocsfalvi, G., Withers, S. G., Rossi, M and Moracci, M. “Introducing transgalactosylation activity into a GH42 b-galactosidase” (2017) Glycobiology In Press.

Santana, A. G., Tysoe, C. R., Hu, G., Kronstad, J., Goddard-Borger, E., and Withers, S. G. “Fungal glycolipid hydrolase inhibitors and their effect on Cryptococcus neoformans” (2017) ChemBioChem 18, 284-290.10.1002/cbic.201600538

Ma, F.; Fischer, M.; Han, Y.; Withers, S.G.; Feng, Y.; Yang, G. Substrate Engineering Enabling Fluorescence Droplet Entrapment For IVC-FACS Based Ultrahigh-Throughput Screening. ANALYTICAL CHEMISTRY 2016, 88(17), 8587-8595. Doi:10.1021/acs.analchem.6b01712

 

Danby, P.M.; Withers, S.G. Advances in Enzymatic Glycoside Synthesis. ACS CHEMICAL BIOLOGY 2016, 11, 1784-1794. Doi:10.1021/acschembio.6b00340

 

Zoidl, M.; Gonzalez Santana, A.; Torvisco, A.; Tysoe, C.T.; Siriwardena, A.; Withers, S. G.; Wrodnigg, T. M . The Staudinger/aza-Wittig Reaction As Key Step For The Concise Synthesis of 1-C-Alkyl-Iminoalditol Glycomimetics. CARBOHYDRATE RESEARCH 2016, 429, 62-70. Doi:10.1016/j.carres.2016.04.006

 

Santana, A.G.; Vadlamani, G.; Mark, B. L.; Withers, S. G. N-Acetyl Glycals Are Tight-Binding And Environmentally Insensitive Inhibitors Of Hexosaminidases. CHEMICAL COMMUNICATIONS, 2016, 52, 7943-7946. Doi:http://10.1039/C6CC02520J

 

Caner, S.; Zhang, X.; Jiang, J.; Chen, H.; Nguyen, N. T.; Overkleeft, O.; Brayer, G.D.; Withers, S. G. Glucosyl Epi-cyclophellitol Allows Mechanism-Based Inactivation And Structural Analysis of Human Pancreatic Alpha-Amylase. FEBS LETTERS 2016, 590, 1143-1151. Doi:10.1002/1873-3468.12143

 

Tysoe, C.T.; Williams, L.K.; Keyzers, R.; Nguyen, N.; Tarling, C.; Wicki, J.; Goddard-Borger, E.D.; Aguda, A.; Perry, S.; Foster, L.J.; Andersen, R.J.; Brayer, G.D.; Withers, S. G. Potent Human Alpha-Amylase Inhibition By The Beta-Defensin-Like Protein Helianthamide. ACS CENTRAL SCIENCE, 2016, 2, 154-161. Doi:10.1021/acscentsci.5b00399

 

Thonhofer, M.; Weber, P.; Gonzalez Santana, A.; Fischer, R.; Pabst, B. M.; Paschke, E.; Schalli, M.; Stütz, A. E.; Tschernutter, M.; Windischhofer, W.; Withers, S. G. Synthesis Of C-5a-Chain Extended Derivatives Of 4-Epi-Isofagomine: Notable Beta-Galactosidase Inhibitors And Activity Promotors Of GM1-Gangliosidosis-Related Human Lysosomal Beta-Galactosidase Mutant R201C. CARBOHYDRATE RESEARCH 2016, 429, 71-80. Doi:10.1016/j.carres.2016.03.020

 

Kwan, D. H.; Jin, Y.; Jiang, J.; Chen, H.; Kötzler, M. P.; Overkleeft, H.S.; Davies, G. J.; Withers, S. G. Chemoenzymatic Synthesis Of 6-Phosphocyclophellitol As A Novel Probe Of 6-Phospho Beta-Glucosidases. FEBS LETTERS 2016, 590, 461-468. Doi:10.1002/1873-3468.12059

 

Chen, H.; Armstrong, Z.; Hallam, S.J.; Withers, S. G. Synthesis And Evaluation Of A Series Of 6-Chloro-4-Methylumbelliferyl Glycosides As Fluorogenic Reagents For Screening Metagenomic Libraries For Glycosidase Activity. CARBOHYDRATE RESEARCH 2016, 421, 33-39. Doi:10.1016/j.carres.2015.12.010

 

McNamara, J. T.; Morgan, J. L.; W Fischer, M.; Rich, J.; Chen, H.; Withers, S. G.; Zimmer, J. Observing Cellulose Biosynthesis And Membrane Translocation In Crystallo. NATURE 2016, 529, 329-334. Doi:10.1038/nature16966

 

Yuen, V. G.; Coleman, J.; Withers, S. G.; Andersen, R. J.; Brayer, G. D.; Mustafa, S.; McNeill, J. H. Glucose Lowering Effect Of Montbretin A In Zucker Diabetic Fatty Rats. MOLECULAR AND CELLULAR BIOCHEMISTRY 2016, 411, 473-381. Doi:10.1007/s11010-015-2599-4

 

Kötzler, M. P.; Withers, S. G. Proteolytic Cleavage Driven By Glycosylation. JOURNAL OF BIOLOGICAL CHEMISTRY 2016, 291, 429-434. Doi:10.1074/jbc.C115.698696

 

Mehr, K.; Withers, S. G. Mechanisms Of The Sialidase And Trans-Sialidase Activities of Bacterial Sialyltransferases From Glycosyltransferase Family 80 (GT80). GLYCOBIOLOGY 2016, 26, 353-359. Doi:10.1093/glycob/cwv105

 

Thonhofer, M.; Santana, A. G.; Fischer, R.; Gomez, A. T.; Saf, R.; Schalli, M.; Stütz, A.E.; Withers, S. G. 5-Fluoro Derivatives Of 4-Epi-Isofagomine As D-Galactosidase Inhibitors And Potential Pharmacological Chaperones For GM1-Gangliosidosis As Well As Fabry’s Disease. CARBOHYDRATE RESEARCH 2016, 420, 6-12. Doi:10.1016/j.carres.2015.10.009

 

Morgan, J. L.; McNamara, J. T.; Fischer, M.; Rich, J.; Chen, H. M.; Withers, S. G.; Zimmer, J. Observing Cellulose Biosynthesis And Membrane Translocation In Crystallo. NATURE 2016, 531, 329–334. Doi:

 

Yu, C.-C.; Withers, S. G. (2015) Adv. Synth. Catal. 357 (8), 1633-1654 “Recent Developments in Enzymatic Synthesis of Modified Sialic Acid Derivatives”. Doi

 

Kwan, D. H.; Ernst, S.; Kötzler, M. P.; Withers, S. G. (2015) Glycobiology 25 (8), 806-811 “Chemoenzymatic Synthesis of a Type 2 Blood Group A Tetrasaccharide and Development of High-throughput Assays Enables a Platform for Screening Blood Group Antigen-cleaving Enzymes”. Doi

 

Arns, S.; Tan, J.; Sun, S.; Galey, A.; Zisman, N.; Ross, F.; Udechukwu, J.; Dercho, S.; Gusti, V.; Paquette, J.; Webb, M.; Bourque, E.; Withers, S. G.; Liggins, R. (2015) Bioorg. Med. Chem. Lett. 25 (12), 2505-2509 “Assessing the oral bioavailability of difluorosialic acid prodrugs, potent viral neuraminidase inhibitors, using a snapshot PK screening assay”. Doi

 

Volkers, G.; Worrall, L. J.; Kwan, D. H.; Yu, C.-C.; Baumann, L.; Lameignere, E.; Wasney, G. A.; Scott, N. E.; Wakarchuk, W.; Foster, L. J.; Withers, S. G.; Strynadka, N. C. J. (2015) Nat. Struct. Mol. Biol. 22 (8), 627-635 “Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation”. Doi

 

Bohlmann, J., Gesell, A., Blaukopf, M., Madilao, L., Yuen, M. M., Withers, S. G., Mattsson, J. and Russell, J. H. (2015) Plant Physiol., in press “The gymnosperm cytochrome P450 CYP750B1 catalyzes stereospecific monoterpene hydroxylation of (+)-sabinene in thujone biosynthesis in Thuja plicata”. Doi

 

Yang, G. Y., Li, C., Fischer, M., Cairo, C. W., Feng, Y. and Withers, S. G. (2015) Angew. Chemie, in press “A FRET probe for cell-based imaging of ganglioside-processing enzyme activity and high-throughput screening”. Pubmed

 

Han, Y. B., Wu, L., Rich, J. R., Huang, F. T., Withers, S. G., Feng, Y. and Yang, G. Y. (2015) Appl. Microbiol. Biotechnol., in press “Comprehensive characterization of sphingolipid ceramide N-deacylase for the synthesis and fatty acid remodeling of glycosphingolipids”. Pubmed

 

Sobhanifar, S., Worrall, L. J., Gruninger, R. J., Wasney, G. A., Blaukopf, M., Baumann, L., Lameignere, E., Solomonson, M., Brown, E. D., Withers, S. G. and Strynadka, N. C. (2015) Proc. Natl. Acad. Sci. USA 112, E576-85 “Structure and mechanism of Staphylococcus aureus TarM, the wall teichoic acid alpha-glycosyltransferase”. Pubmed

 

Weck, S., Robinson, K., Smith, M. R. and Withers, S. G. (2015) Chem. Commun. 51, 2933-5 “Understanding viral neuraminidase inhibition by substituted difluorosialic acids”. Pubmed

 

Macdonald, S. S., Blaukopf, M. and Withers, S. G. (2015) J. Biol. Chem. 290, 4887-95 “N-acetylglucosaminidases from CAZy family GH3 are really glycoside phosphorylases, thereby explaining their use of histidine as an acid/base catalyst in place of glutamic acid”. Pubmed

 

Williams, L. K.; Zhang, X.; Caner, S.; Tysoe, C.; Nguyen, N. T.; Wicki, J.; Williams, D. E.; Coleman, J.; McNeill, J. H.; Yuen, V.; Andersen, R. J.; Withers, S. G.; Brayer, G. D. (2015) Nat. Chem. Biol. 11 (9), 691-696 “The amylase inhibitor montbretin A reveals a new glycosidase inhibition motif”. Doi

 

Kwan, D. H.; Constantinescu, I.; Chapanian, R.; Higgins, M. A.; Kötzler, M. P.; Samain, E.; Boraston, A. B.; Kizhakkedathu, J. N.; Withers, S. G. (2015) J. Am. Chem. Soc. 137 (17), 5695-5705 “Toward Efficient Enzymes for the Generation of Universal Blood through Structure-Guided Directed Evolution”. Doi

 

Chapanian, R., Kwan, D. H., Constantinescu, I., Shaikh, F. A., Rossi, N. A., Withers, S. G. and Kizhakkedathu, J. N. (2014) Nat. Commun. 5, 4683 “Enhancement of biological reactions on cell surfaces via macromolecular crowding”. Pubmed

 

Kwan, D. H. and Withers, S. G. (2014) Proc. Natl. Acad. Sci. USA 111, 10904-5 “Periplasmic de-acylase helps bacteria don their biofilm coat”. Pubmed

 

Duo, T., Goddard-Borger, E. D. and Withers, S. G. (2014) Chem. Commun. 50, 9379-82 “Fluoro-glycosyl acridinones are ultra-sensitive active site titrating agents for retaining beta-glycosidases”. Pubmed

 

Zoidl, M., Müller, B., Torvisco, A., Tysoe, C., Benazza, M., Siriwardena, A., Withers, S. G. and Wrodnigg, T. M. (2014) Bioorg. Med. Chem. Lett. 24, 2777-80 “Concise synthesis of C-1-cyano-iminosugars via a new Staudinger/aza Wittg/Strecker multicomponent reaction strategy”. Pubmed

 

Syson, K., Stevenson, C. E., Rashi, A. M., Saalbach, G., Tang, M., Tuukkanen, A., Svergun, D. I., Withers, S. G., Lawson, D. M. and Bornemann S. (2014) Biochemistry 53, 2494-504 “Structural insight into how streptomyces coelicolor maltosyl transferase GIgE binds α-maltose 1-phospate and forms a maltosyl-enzyme intermediate”. Pubmed

 

Rempel, B.P. and Withers S. G. (2014) Org. Biolmol. Chem. 12, 2592-5 “Phosphodiesters serve as potentially tunable aglycones for fluoro sugar inactivators of retaining β-glycosidases”. Pubmed

 

Buchini, S., Gallat, F. X., Greig, I. R., Kim, J. H., Wakatsuki, S., Chavas, L. M. and Withers S. G. (2014) Angew. Chemie 53, 3382-6 “Tuning mechanisms-based inactivators of neuraminidases: mechanistic and structural insights” Pubmed

 

Jongkees, S. A., Yoo, H. and Withers, S. G. (2014) J. Biol. Chem. 289, 11385-95 “Mechanistic investigations of unsaturated glucuronyl hydrolase from Clostridium perfringens”. Pubmed

 

Tysoe, C. and Withers, S. G. (2014) Curr. Top Med. Chem. 14, 865-74 “Fluorinated mechanism-based inhibitors: common themes and recent developments”. Pubmed

 

Knott, B. C., Haddad Momeni, M., Crowley, M. F., Mackenzie, L. F., Götz, A. W., Sandgren, M., Withers, S. G., Ståhlberg, J. and Beckham, G. T.. (2014) J. Am. Chem. Soc. 136, 321-9 “The mechanism of cellulose hydrolysis by a two-step, retaining cellobiohydrolase elucidated by structural and transition path sampling studies”. Pubmed

 

Jongkees, S. A., Yoo, H. and Withers, S. G. (2014) Chembiochem. 15, 124-34 “Mechanistic insights from substrate preference in unsaturated glucuronyl hydrolase”. Pubmed

 

Yu, C. C., Hill, T., Kwan, D. H., Chen, H. M., Lin, C. C., Wakarchuk, W. and Withers, S. G. (2014) Anal. Biochem. 444, 67-74 “A plate-based high-throughput activity assay for polysialyltransferase from Neisseria meningitidis”. Pubmed

 

Yu, C. C., Huang, L. D., Kwan, D. H., Wakarchuk, W. W., Withers, S. G. and Lin, C.C. (2013) Chem. Commun. 49, 10166-8 “A glyco-gold nanoparticle based assay for a-2,8-polysialyltransferase from Neisseria meningitidis”. Pubmed

 

Bie, H., Yin, J., He, X., Kermode, A. R., Goddard-Borger, E. D., Withers, S. G. and James, M. N. (2013) Nat Chem Biol. 9, 739-45 “Insights into mucopolysaccharidosis I from the structure and action of alpha-L-iduronidase”. Pubmed

 

Jongkees, S. A. and Withers, S.G. (2013) Acc. Chem. Res. 47, 226-35 “Unusual enzymatic glycoside cleavage mechanisms”. Pubmed

 

Mewis, K., Armstrong, Z., Song, Y. C., Baldwin, S. A., Withers, S. G. and Hallam, S. J. (2013) J. Biotechnol. 167, 462-71 “Biomining active cellulases from a mining bioremediation system”. Pubmed

 

Shaikh, F. A., Lammerts van Bueren, A., Davies, G. J. and Withers, S. G. (2013) Biochemistry 52, 5857-64 “Identifying the catalytic acid/base in GH29 alpha-L-fucosidase subfamilies”. Pubmed

 

Armstrong, Z. and Withers, S. G. (2013) Biopolymers 99, 666-74 “Synthesis of glycans and glycopolymers through engineered enzymes”. Pubmed

 

Caner, S., Nguyen, N., Aguda, A., Zhang, R., Pan, Y. T., Withers, S. G. and Brayer, G. D. (2013) Glycobiology 23, 1075-83 “The structure of the Mycobacterium smegmatis trehalose synthase reveals an unusual active site configuration and acarbose-binding mode”. Pubmed

 

Ratananikom, K., Choengpanya, K., Tongtubtim, N., Charoenrat, T., Withers, S. G. and Kongsaeree, P. T. (2013) Carbohydr. Res. 373, 35-41 “Mutational analysis in the glycone binding pocket of Dalbergia cochinchinensis GH1 β- glucosidase to improve catalytic efficiency”. Pubmed

 

Ludwiczek, M. L., D’Angelo, I., Yalloway, G. N., Brockerman, J. A., Okon, M., Nielsen, J. E., Strynadka, N. C., Withers, S. G. and McIntosh, L. P. (2013) Biochemistry 52, 3138-56 “Strategies for modulating the pH-dependent activity of a family 11 glycoside hydrolase”. Pubmed

 

Kim, J. H., Resende, R., Wennekes, T., Chen, H. M., Bance, N., Buchini, S., Watts, A. G., Pilling, P., Streltsov, V. A., Petric, M., Liggins, R., Barrett, S., McKimm-Breschkin, J. L., Niikura, M. and Withers, S. G. (2013) Science 340, 71-5 “Mechanism-based covalent neuraminidase inhibitors with broad-spectrum influenza antiviral activity”. Pubmed

 

Thompson, J., Pikis, A., Rich, J., Hall, B. G. and Withers, S. G. (2013) FEBS Lett., 587, 799-803 “a-Galacturonidase(s): a new class of Family 4 glycoside hydrolases with strict specificity and a unique CHEV active site motif”. Pubmed

 

Rakic, B., Rao, F. V., Freimann, K., Wakarchuk, W., Strynadka, N. C. and Withers, S.G. (2013) Glycobiology, 23, 536-45 “Structure-based mutagenic analysis of mechanism and substrate specificity in mammalian glycosyltransferases: porcine ST3Gal-I”. Pubmed

 

Stocker, B. L., Jongkees, S. A., Win-Mason, A. L., Dangerfield, E. M., Withers, S. G. and Timmer, M. S. (2013) Carbohydr. Res. 367, 29-32 “The ‘mirror-image’ postulate as a guide to the selection and evaluation of pyrrolidines as a-l-fucosidase inhibitors”. Pubmed

 

Chan, P. H., Cheung, A. H., Okon, M., Chen, H. M., Withers, S. G. and McIntosh, L. P. (2013) Biochemistry 52, 320-32 “Investigating the structural dynamics of a-1,4-galactosyltransferase C from Neisseria meningitidis by nuclear magnetic resonance spectroscopy”. Pubmed

 

Shim, J.-H. and Withers, S. G. (2013) Food Science Biotechnology 22, 269-73 “Improvement of the expression level of beta-glucosidase from Agrobacterium sp. inEscherichia coli by rare codon optimization”.

 

Vocadlo, D. J. and Withers, S. G. (2012) Curr. Opin. Chem. Biol. 16, 461-4 “How to make a difference: mechanisms of protein and nucleic acid modifying enzymes”. Pubmed

 

Yip, V. L. and Withers S. G. (2012) Biochemistry 51, 8464-74 “Identification of Tyr241 as a key catalytic base in the Family 4 glycoside hydrolase BglT from Thermotoga maritime”. Pubmed

 

Williams, L. K., Li, C., Withers, S. G. and Brayer, G. D. (2012) J. Med Chem. 55, 10177-86 “Order and disorder: the differential structural impacts of myricetin and ethyl caffeate on human amylase, an anti-diabetic target”. Pubmed

 

Chan, P. H. W., Weissbach, S., Okon, M., Withers, S. G. and McIntosh, L. P. (2012) Biochemistry 51, 8278-92 “NMR spectral assignments of α-1,4-galactosyltransferase LgtC from Neisseria meningitidis: substrate binding and multiple conformational states”. Pubmed

 

Shim, J-H., Chen, H., Rich, J. R., Goddard-Borger, E. D. and Withers, S. G. (2012) PEDS 25, 465-72 “Directed evolution of a β-glucosidase from Agrobacterium sp. enhances its glycosynthase catalytic activity toward C3-OH modified donor sugar”. Pubmed

 

Rich, J. R. and Withers, S. G. (2012) Angew. Chemie 51, 8640-3 “A chemoenzymatic total synthesis of the neurogenic starfish ganglioside LLG-3 using an engineered and evolved synthase”. Pubmed

 

Reitinger, S., Petriv, O. I., Mehr, K., Hansen, C. L. and Withers, S. G. (2012) J. Virol. Methods 185, 171-4 “Purification and quantitation of bacteriophage M13 using desalting spin columns and digital PCR”. Pubmed

 

Withers, S. G. and Davies, G. J. (2012) Nature Chem. Biol. 8, 952-3 “The case of the missing base”. Pubmed

 

Michikawa, M., Ichinose, H., Momma, M., Biely, P., Jongkees, S., Yoshida, M., Kotake, T., Tsumuraya, Y., Withers, S., Fujimoto, Z. and Kaneko, S. (2012) J. Biol. Chem. 287, 14069-77 “Structural and biochemical characterization of glycoside hydrolase family 79 β-glucuronidase from Acidobacterium capsulatum”. Pubmed

 

Goddard-Borger, E. D., Tropak, M. B., Yonekawa, S., Tysoe, C. R., Mahuran, D. J. and Withers, S. G. (2012) J. Med. Chem. 55, 2737-45 “Rapid assembly of a library of lipophilic iminosugars via the thiol-ene reaction yields promising pharmacological chaperones for the treatment of Gaucher Disease”. Pubmed

 

Goddard-Borger, E. D., Sakaguchi, K., Reitinger, S., Watanabe, N., Ito, M. and Withers, S. G. (2012) J. Am. Chem. Soc. 134, 3895-902 “Mechanistic insights into the 1,3-xylanases: useful enzymes for manipulation of algal biomass”. Pubmed

 

Pengthaisong, S., Chen, C. F., Withers, S. G., Kuaprasert, B. and Ketudat Cairns, J. R. (2012) Carbohydr. Res. 352, 51-9 “Rice BGlu1 wild type and glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition”. Pubmed

 

Pengthaisong, S., Withers, S. G., Kuaprasert, B., Svasti, J. and and Cairns, J. R. (2012) Prot. Sci. 21, 362-72 “Structural investigation of the basis for cellooligosaccharide synthesis by rice BGlu1 glycosynthases”. Pubmed

 

Win-Mason, A. L., Jongkees, S. A. K., Withers, S. G., Tyler, P. C., Timmer, M. S. M. and Stocker, B. L. (2011) J. Org Chem. 76, 9611-21 “Stereoselective total synthesis of aminoiminohexitols via carbamate annulation”. Pubmed

 

Jongkees, S. A. K. and Withers, S. G. (2011) J Am Chem Soc. 133, 19334-7 “Glycoside cleavage by a new mechanism in unsaturated glucuronyl hydrolases”. Pubmed

 

Fröhlich, R. F. G., Fantur, K., Furneaux, R. H., Paschke, E., Stütz, A. E., Wicki, J., Withers, S. G. and Wrodnigg, T. M. (2011) Bioorg. Med. Chem. Letts. 21, 6872-5 “A fluorescent probe for GM1 gangliosidosis related β-galactosidase: N-(Dansylamino)hexylaminocarbonylpentyl-1,5-dideoxy-1,5-imino-D-galactitol”. Pubmed

 

Rich, J. R., Cunningham, A.-M., Gilbert, M. and Withers, S. G. (2011) Chem. Commun. 47, 10806-8 “Glycosphingolipid synthesis employing a combination of recombinant glycosyltransferases and an endoglycoceramidase glycosynthase”. Pubmed

 

Zhang, R., Pan, Y-T, He, S., Lam, M., Brayer, G. D., Elbein, A. D. and Withers, S. G. (2011) J. Biol. Chem. 286, 35601-9 “Mechanistic analysis of trehalose synthase from Mycobacterium smegmatis”. Pubmed

 

Lee, S., Greig, I. R., Vocadlo, D., McCarter, J. D., Patrick, B. O. and Withers, S. G. (2011) J. Am. Chem. Soc. 133, 15826-9 “Structural, mechanistic and computational analysis of the effects of anomeric fluorines on anomeric fluoride departure in 5-fluoroxylosyl fluorides”. Pubmed

 

Rempel, B. P., Tropak, M. B., Mahuran, D. J. and Withers, S. G. (2011) Angew. Chemie 50, 10381-3 “Tailoring the specificity and reactivity of a mechanism-based inactivator of glucocerebrosidase for potential therapeutic applications”. Pubmed

 

Fröhlich, R. F. G., Furneaux, R. H., Mahuran, D. J., Saf, R., Stütz, A. E., Tropak, M. B., Wicki, J., Withers, S. G. and Wrodnigg, T. M. (2011) Carbohydr. Res. 346, 1592-8 “1-Deoxy-D-galactonojirimycins with dansyl capped N-substituents as ß-galactosidase inhibitors and potential probes for GMI gangliosidosis affected cell lines”. Pubmed

 

Kwan, D. H. and Withers, S. G. (2011) J. Carb. Chem. 30, 181-205 “Towards efficient enzymatic glycan synthesis: Directed evolution and enzyme engineering”.Pdf

 

Hill, T, Tropak, M. B., Mahuran, D. and Withers, S. G. (2011) ChemBioChem 12, 2151-4 “Synthesis, kinetic evaluation and cell based analysis of C-alkylated isofagomines as chaperones of ß-glucocerebrosidase”. Pubmed

 

Lee, H. J., Lairson, L. L., Rich, J. R., Lameignere, E., Wakarchuk, W. W., Withers, S. G. and Strynadka, N. C. J. (2011) J. Biol. Chem. 286, 35922–32 “Structural and kinetic analysis of substrate binding to the sialyltransferase Cst-II from Campylobacter jejuni”. Pubmed

 

Lin, L. Y-C., Rakic, B., Chiu, C. P. C., Lameignere, E., Wakarchuk, W. W., Withers, S. G. and. Strynadka, N.C.J. (2011) J. Biol. Chem. 286, 37237–48 “Structure and mechanism of the lipooligosaccharide sialyltransferase from Neisseria meningitidis”. Pubmed

 

Goddard-Borger, E. D., Fiege, B., Kwan, E. M. and Withers, S. G. (2011) Chembiochem 12, 1703-11 “Glycosynthase-mediated assembly of xylanase substrates and inhibitors”. Pubmed

 

Kwan, D. H., Chen, H., Ratananikom, K., Hancock, S. M., Watanabe, Y., Kongsaeree, P. T., Samuels, A. L. and Withers, S. G. (2011) Angew. Chemie 50, 300-3 “Self-immobilizing fluorogenic imaging agents of enzyme activity”. Pubmed

 

Torpenholt, S., Le Nours, J., Christensen, U., Jahn, M., Withers, S., Østergaard, P. R., Borchert, T. V., Poulsen, J.-C. and Lo-Leggio, L. (2011) Carbohydr. Res. 346, 2028–33 “Activity of three ß-1,4-galactanases on small chromogenic substrates”. Pubmed