Sweeney, R. P., Danby, P. M., Geissner, A., Karimi, R., Brask, J. & Withers, S. G. “Development of an active site titration reagent for alpha-amylases”. Chemical Science 12, 683-687,(2021). doi:10.1039/d0sc05380e
Li, J., Solhi, L., Goddard-Borger, E. D., Mathieu, Y., Wakarchuk, W. W., Withers, S. G. & Brumer, H. “Four cellulose-active lytic polysaccharide monooxygenases from Cellulomonas species”. Biotechnology for Biofuels 14,(2021). doi:10.1186/s13068-020-01860-3
Wolfsgruber, A., Thonhofer, M., Weber, P., Nasseri, S. A., Fischer, R., Schalli, M., Stutz, A. E., Withers, S. G. & Wrodnigg, T. M. “N-Alkylated Iminosugar Based Ligands: Synthesis and Inhibition of Human Lysosomal beta-Glucocerebrosidase”. Molecules 25,(2020). doi:10.3390/molecules25204618
Weber, P., Thonhofer, M., Averill, S., Davies, G. J., Santana, A. G., Muller, P., Nasseri, S. A., Offen, W. A., Pabst, B. M., Paschke, E., Schalli, M., Torvisco, A., Tschernutter, M., Tysoe, C., Windischhofer, W., Withers, S. G., Wolfsgruber, A., Wrodnigg, T. M. & Stutz, A. E. “Mechanistic Insights into the Chaperoning of Human Lysosomal-Galactosidase Activity: Highly Functionalized Aminocyclopentanes andC-5a-Substituted Derivatives of 4-epi-Isofagomine”. Molecules 25,(2020). doi:10.3390/molecules25174025
Rahfeld, P. & Withers, S. G. “Toward universal donor blood: Enzymatic conversion of A and B to O type”. J. Biol. Chem. 295, 325-334,(2020). doi:10.1074/jbc.REV119.008164
Nieto-Dominguez, M., de Toro, B. F., de Eugenio, L. I., Santana, A. G., Bejarano-Munoz, L., Armstrong, Z., Mendez-Liter, J. A., Asensio, J. L., Prieto, A., Withers, S. G., Canada, F. J. & Martinez, M. J. “Thioglycoligase derived from fungal GH3 beta-xylosidase is a multi-glycoligase with broad acceptor tolerance”. Nature Communications 11,(2020). doi:10.1038/s41467-020-18667-3
Harmsen, R. A. G., Aam, B. B., Madhuprakash, J., Hamre, A. G., Goddard-Borger, E. D., Withers, S. G., Eijsink, V. G. H. & Sorlie, M. “Chemoenzymatic Synthesis of Chito-oligosaccharides with Alternating N-D-Acetylglucosamine and D-Glucosamine”. Biochemistry 59, 4581-4590,(2020). doi:10.1021/acs.biochem.0c00839
da Fonseca, M. J. M., Armstrong, Z., Withers, S. G. & Briers, Y. “High-Throughput Generation of Product Profiles for Arabinoxylan-Active Enzymes from Metagenomes”. Appl. Environ. Microbiol. 86,(2020). doi:10.1128/aem.01505-20
Zoidl, M., Wolfsgruber, A., Schalli, M., Nasseri, S. A., Weber, P., Stutz, A. E., Withers, S. G. & Wrodnigg, T. M. “Synthesis of modified 1,5-imino-d-xylitols as ligands for lysosomal -glucocerebrosidase”. Monatshefte Fur Chemie 150, 831-842,(2019). doi:10.1007/s00706-019-02427-1
Tysoe, C. R., Caner, S., Calvert, M. B., Win-Mason, A., Brayer, G. D. & Withers, S. G. “Synthesis of montbretin A analogues yields potent competitive inhibitors of human pancreatic alpha-amylase”. Chemical Science 10, 11073-11077,(2019). doi:10.1039/c9sc02610j
Tegl, G., Hanson, J., Chen, H. M., Kwan, D. H., Santana, A. G. & Withers, S. G. “Facile Formation of -thioGlcNAc Linkages to Thiol-Containing Sugars, Peptides, and Proteins using a Mutant GH20 Hexosaminidase”. Angewandte Chemie-International Edition 58, 1632-1637,(2019). doi:10.1002/anie.201809928
Tan, Y. M., Zhang, Y., Han, Y. B., Liu, H., Chen, H. F., Ma, F. Q., Withers, S. G., Feng, Y. & Yang, G. Y. “Directed evolution of an alpha 1,3-fucosyltransferase using a single-cell ultrahigh-throughput screening method”. Science Advances 5,(2019). doi:10.1126/sciadv.aaw8451
Strazzulli, A., Perugino, G., Mazzone, M., Rossi, M., Withers, S. G. & Moracci, M. “X Probing the role of an invariant active site His in family GH1 beta-glycosidases”. J. Enzyme Inhib. Med. Chem. 34, 973-980,(2019). doi:10.1080/14756366.2019.1608198
Schalli, M., Weber, P., Nasseri, S. A., Gomez, A. T., Muller, P., Stutz, A. E., Withers, S. G., Wolfsgruber, A. & Wrodnigg, T. M. “Biologically active branched-chain aminocyclopentane tetraols from d-galactose”. Monatshefte Fur Chemie 150, 861-870,(2019). doi:10.1007/s00706-019-02428-0
Rahfeld, P., Wardman, J. F., Mehr, K., Huff, D., Morgan-Lang, C., Chen, H. M., Hallam, S. J. & Withers, S. G. “Prospecting for microbial ?-N-acetylgalactosaminidases yields a new class of GH31 O-glycanase”. J. Biol. Chem. 294, 16400-16415,(2019). doi:10.1074/jbc.RA119.010628
Rahfeld, P., Sim, L., Moon, H., Constantinescu, I., Morgan-Lang, C., Hallam, S. J., Kizhakkedathu, J. N. & Withers, S. G. “An enzymatic pathway in the human gut microbiome that converts A to universal O type blood”. Nature Microbiology 4, 1475-1485,(2019). doi:10.1038/s41564-019-0469-7
McKimm-Breschkin, J. L., Barrett, S., McKenzie-Kludas, C., McAuley, J., Streltsov, V. A. & Withers, S. G. “Passaging of an influenza A(H1N1)pdm09 virus in a difluoro sialic acid inhibitor selects for a novel, but unfit I106M neuraminidase mutant”. Antiviral Research 169,(2019). doi:10.1016/j.antiviral.2019.104542
Macdonald, S. S., Armstrong, Z., Morgan-Lang, C., Osowiecka, M., Robinson, K., Hallam, S. J. & Withers, S. G. “Development and Application of a High-Throughput Functional Metagenomic Screen for Glycoside Phosphorylases”. Cell Chemical Biology 26, 1001-+,(2019). doi:10.1016/j.chembiol.2019.03.017
Janesch, B., Baumann, L., Mark, A., Thompson, N., Rahmani, S., Sim, L., Withers, S. G. & Wakarchuk, W. W. “Directed evolution of bacterial polysialyltransferases”. Glycobiology 29, 588-598,(2019). doi:10.1093/glycob/cwz021
Armstrong, Z., Liu, F., Kheirandish, S., Chen, H. M., Mewis, K., Duo, T. M., Morgan-Lang, C., Hallam, S. J. & Withers, S. G. “High-Throughput Recovery and Characterization of Metagenome-Derived Glycoside Hydrolase-Containing Clones as a Resource for Biocatalyst Development”. Msystems 4,(2019). doi:10.1128/mSystems.00082-19
Armstrong, Z., Liu, F., Chen, H. M., Hallam, S. J. & Withers, S. G. “Systematic Screening of Synthetic Gene-Encoded Enzymes for Synthesis of Modified Glycosides”. Acs Catalysis 9, 3219-3227,(2019). doi:10.1021/acscatal.8b05179
Chen, H and Withers, S.G. “Synthesis of azido-deoxy and amino-deoxy glycosides and glycosyl fluorides for screening of glycosidase libraries and assembly of substituted glycosides” (2018) Carbohydr. Res. 467, 33-34.
Nasseri, S. A., Betschart, L., Opaleva, D., Rahfeld, P. and Withers, S.G. “A mechanism based approach to screening metagenomic libraries for unconventional glycosidases” (2018) Angew. Chemie 57, 11359-11364.
Gao, Z., Thompson, A., Paulson, J and Withers, S.G. “Proximity Ligation-Based Fluorogenic Imaging Agents for Neuraminidases” (2018) Angew. Chemie 57, 13538-13541.
Tysoe, C.R. and Withers, S.G. “Structural dissection of helianthamide reveals the basis of its potent inhibition of human pancreatic -amylase”. (2018) Biochemistry 57, 5384-5387.
Perrella, N.N., Withers, S.G., and Lopes, A.R.“Identity and role of the non-Conserved Acid/Base Catalytic residue in the GH29 fucosidase from the spider Nephilingis cruentata” (2018) Glycobiology, 28, 925-932.
Du, Ting; Buenbrazo, Nakita; Kell, Laura; Rahmani, Sadia; Sim, Lyann; Withers, Stephen; DeFrees, Shawn; Wakarchuk, Warren “A bacterial expression platform for production of therapeutic proteins containing human-like O-linked glycans.” (2019) Cell Chemical Biology, In Press, Accepted Sept 2018.
Vickers, C., Liu, F., Abe, K., Salama-Alber, O., Jenkins, M., Springate, C.M.K., Burke, J.E., Withers, S.G. and Boraston, A.B. “Endo-fucoidan hydrolases from glycoside hydrolase family 107 display structural and mechanistic similarities to -L-fucosidases from glycoside hydrolase family 29” (2018) J. Biol. Chem. 293, 18296-18308
Brockerman, J.A., Okon, M., Withers, S.G. and McIntosh, L.P. “The pKa values of the catalytic residues in the retaining glycoside hydrolase T26H mutant of T4 lysozyme” (2019) Protein Science In Press, accepted Dec. 2018
Gao, Z., Ovchinnikova, O.G., Huang, B., Liu, F., Williams, D.E., Andersen, R.J. Lowary, T.L., Whitfield, C. and Withers, S.G. “A High-Throughput “FP-Tag” Assay for the Identification of Glycosyltransferase Inhibitors” (2019) J Am Chem Soc In Press, provisionally accepted Jan 2019.
Saxena, H., Hsu, B., de Asis, M., Zierke, M, Sim, L., Withers, S.G. and Wakarchuk, W., “Characterization of a Thermostable Endoglucanase from Cellulomonas fimi ATCC484” (2018) Biochemistry and Cell Biology 96, 68-76.
Macdonald, S.S., Patel, A., Larmour, V.L.C., Morgan-Lang, C., Hallam, S.J., Mark, B.L., and Withers, S.G. “Structural and mechanistic analysis of a Beta-glucoside phosphorylase identified by screening a metagenomic library” (2018) J Biol Chem 293, 3451-3467.
Smirnova, I., Kasho, V., Jiang, X., Chen, H.-M., Withers, S.G. and Kaback, R.H. “Oversized galactosides as a probe for conformational dynamics in LacY” (2018) PNAS 115, 4146-4151.
Hettle, A. G., Vickers, A. C., Robb, C.S., Liu, F., Withers S.G., Hehemann, J-H., and Boraston A.B. “The molecular basis of polysaccharide sulfatase activity and a nomenclature of catalytic subsites in this class of enzyme” (2018) Structure 26, 747-758.
Weber, P., Nasseri, S.A., Pabst, B.M., Gomez, A.T., Müller, P., Paschke, E. Tschernutter, M., Windischhofer, W., Withers, S.G., Wrodnigg, T.M., and Stütz, A.E. “Potent GH20 N-Acetyl--D-hexosaminidase inhibitors: N-Substituted 4-acetamido-5-amino- 1-hydroxymethyl-cyclopentanediols” (2018) Molecules 23, 708.
Blaukopf, M., Worrall, L., Kosma, P., Strynadka, N.C.J. and Withers, S.G. “Insights into heptosyltransferase I catalysis and inhibition through the structure of its ternary complex” (2018) Structure In Press
Armstrong, Z., Mewis, K., Liu, F., Scofield, M., Durno, W., Chen, H., Mehr, K., Hanson, N., Konwar, K., Withers, S.G., and Hallam, S.J. “Metagenomics reveals functional synergy and novel polysaccharide utilization loci in the Castor canadensis fecal microbiome” (2018) ISME J In Press
Kötzler, M.P., Robinson, K., Chen, H-M., Okon, M., McIntosh, L.P. and Withers, S.G. “Modulating the nucleophile of a glycoside hydrolase through site-specific incorporation of fluoroglutamic acids (2018) J. Am. Chem. Soc. In Press
Irmisch, S., Jo, S., Roach, C., Jancsik, S., Yuen, M., Madilao, L., O’Neil-Johnson, M., Williams, R., Withers, S.G. and Bohlmann, J. “Discovery of UDP-Glycosyltransferases and BAHD-Acyltransferases in the Biosynthesis of the Anti-Diabetic Plant Metabolite Montbretin A ” (2018) The Plant Cell, In Press
Mageroy, M.H., Jancsik, S., Yuen, M.M.S, Fischer, M., Withers, S.G., Paetz, C., Schneider, B., MacKay, J., and Bohlmann, J. “Conifer defense against insects: A white spruce family-1 UGT involved in acetophenone metabolism” (2017) Plant Physiol. 175, 641-651.
Wakarchuk, W., Saxena, H., Hsu, B., de Asis, M., Zierke, M, Sim, L. and Withers, S.G. “Characterization of a Thermostable Endoglucanase from Cellulomonas fimi ATCC484” (2017) Biochemistry and Cell Biology In Press.
Centko, R.M., Ratnaweera, P.B., Tysoe, C.R., Withers, S.G., Dilip De Silva, E. and Andersen,R.J. “Alpha-glucosidase and alpha-amylase inhibiting thiodiketopiperazines from the endophytic fungus Setosphaeria rostrata isolated from the medicinal plant Costus speciosus in Sri Lanka” (2017) Phytochemistry Letters, In Press.
Duo, T., Robinson, K., Greig, I., Chen, H., Patrick, B.O. and Withers, S.G. “Remarkable reactivity differences between glucosides with identical leaving groups” (2017) J Am. Chem. Soc 8, 139, 15994-15999.
Armstrong, Z., Rahfeld, P. and Withers, S.G. “Discovery of New Glycosidases from Metagenomic Libraries” (2017) Methods Enzymol. 597, 3-23.
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. 442, 31-40.
Gao, Z., Niikura, M, and Withers, S. G. “Ultrasensitive fluorogenic neuraminidase titration reagents” (2017) Angew. Chemie, 129(22), 6208-6212.
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 May 1;27(5):425-437. doi: 10.1093/glycob/cwx013.
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