Aligning the Symmetry of the Type III Secretion System Needle Complex. Worrall L, Hu J, Strynadka NCJ. (2020) J Chem Inf Model.

A Slippery Scaffold: Synthesis and Recycling of the Bacterial Cell Wall Carrier Lipid. Workman SD, Strynadka NCJ. (2020) J Mol Biol.

Crystallographic analysis of Staphylococcus aureus LcpA, the primary wall teichoic acid ligase. Li FKK, Rosell FI, Gale RT, Simorre JP, Brown ED, Strynadka NCJ. (2020) J Biol Chem. 295: 2629-2639.

Towards capture of dynamic assembly and action of the T3SS at near atomic resolution. Hu J, Worrall LJ, Strynadka NCJ. (2020) Curr Opin Struct Biol. 61: 71-78.

On the road to structure-based development of anti-virulence therapeutics targeting the type III secretion system injectisome. Lyons BJE, Strynadka NCJ. (2019) Medchemcomm. 10: 1273-1289.

T3S injectisome needle complex structures in four distinct states reveal the basis of membrane coupling and assembly. Hu J, Worrall LJ, Vuckovic M, Hong C, Deng W, Atkinson CE, Brett Finlay B, Yu Z, Strynadka NCJ. (2019) Nat Microbiol. 4: 2010-2019.

Structural Insights into Bacteriophage GIL01 gp7 Inhibition of Host LexA Repressor. Caveney NA, Pavlin A, Caballero G, Bahun M, Hodnik V, de Castro L, Fornelos N, Butala M, Strynadka NCJ. (2019) Structure. 27: 1094-1102.

Structural insight into YcbB-mediated beta-lactam resistance in Escherichia coli. Caveney NA, Caballero G, Voedts H, Niciforovic A, Worrall LJ, Vuckovic M, Fonvielle M, Hugonnet JE, Arthur M, Strynadka NCJ. (2019) Nat Commun. 10: 1849.

A Hybrid Secretion System Facilitates Bacterial Sporulation: A Structural Perspective. Zeytuni N, Strynadka NCJ. (2019) Microbiol Spectr. 7

Structural and kinetic analyses of penicillin-binding protein 4 (PBP4)-mediated antibiotic resistance in Staphylococcus aureus. Alexander JAN, Chatterjee SS, Hamilton SM, Eltis LD, Chambers HF, Strynadka NCJ. (2018) J Biol Chem. 293: 19854-19865.

Cryo-EM analysis of the T3S injectisome reveals the structure of the needle and open secretin. Hu J, Worrall LJ, Hong C, Vuckovic M, Atkinson CE, Caveney N, Yu Z, Strynadka NCJ. (2018) Nat Commun. 9: 3840.

Heptosyltransferase I Catalysis and Inhibition through the Structure of Its Ternary Complex. Blaukopf M, Worrall L, Kosma P, Strynadka NCJ, Withers SG. (2018) Structure 26: 1399-1407.

Structural Basis for Binding of Fluorescent CMP-Neu5Ac Mimetics to Enzymes of the Human ST8Sia Family. Volkers G, Lizak C, Niesser J, Rosell FI, Preidl J, Gnanapragassam VS, Horstkorte R, Rademann J, Strynadka NCJ. (2018) ACS Biol. 13: 2320-2328.

Enzyme structures of the bacterial peptidoglycan and wall teichoic acid biogenesis pathways. Caveney NA, Li FK, Strynadka NCJ. (2018) Curr Opin Struct Biol. 53: 45-58.

IpdAB, a virulence factor in Mycobacterium tuberculosis, is a cholesterol ring-cleaving hydrolase. Crowe AM, Workman SD, Watanabe N, Worrall LJ, Strynadka NCJ, Eltis LD. (2018) Proc Natl Acad Sci U S A. 115: E3378-E3387.

Secretins revealed: structural insights into the giant gated outer membrane portals of bacteria. Majewski DD, Worrall LJ, Strynadka NCJ. (2018) Curr Opin Struct Biol. 51: 61-72.

Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling. Workman SD, Worrall LJ, Strynadka NCJ. (2018) Nat Commun. 20: 1159.

PBP4 activity and its overexpression are necessary for PBP4-mediated high-level β-lactam resistance. Basuino L, Jousselin A, Alexander JAN, Strynadka NCJ, Pinho MG, Chambers HF, Chatterjee SS. (2018) J Antimicrob Chemother. 73: 1177-1180.

Structural characterization of SpoIIIAB sporulation-essential protein in Bacillus subtilis. Zeytuni N, Flanagan KA, Worrall LJ, Massoni SC, Camp AH, Strynadka NCJ. (2018) J Struct Biol. 202: 105-112.

B. subtilis LytR-CpsA-Psr Enzymes Transfer Wall Teichoic Acids from Authentic Lipid-Linked Substrates to Mature Peptidoglycan In Vitro. Gale RT, Li FKK, Sun T, Strynadka NCJ, Brown ED. (2017) Cell Chem Biol. 24: 1537-1546.

Near-atomic resolution cryoelectron microscopy structure of the 30-fold homooligomeric SpoIIIAG channel essential to spore formation in Bacillus subtilis. Zeytuni N, Hong C, Flanagan KA, Worrall LJ, Theiltges KA, Vuckovic M, Huang RK, Massoni SC, Camp AH, Yu Z, Strynadka NC. (2017) Proc Natl Acad Sci U S A. 114: E7073-E7081.

X-ray crystallographic structure of a bacterial polysialyltransferase provides insight into the biosynthesis of capsular polysialic acid. Lizak C, Worrall LJ, Baumann L, Pfleiderer MM, Volkers G, Sun T, Sim L, Wakarchuk W, Withers SG, Strynadka NC. (2017) Sci Rep. 7: 5842.

Assembly, structure, function and regulation of type III secretion systems. Deng W, Marshall NC, Rowland JL, McCoy JM, Worrall LJ, Santos AS, Strynadka NCJ, Finlay BB. (2017) Nat Rev Microbiol. 15: 323-337.

High-Level Resistance of Staphylococcus aureus to β-Lactam Antibiotics Mediated by Penicillin-Binding Protein 4 (PBP4). Hamilton SM, Alexander JAN, Choo EJ, Basuino L, da Costa TM, Severin A, Chung M, Aedo S, Strynadka NCJ, Tomasz A, Chatterjee SS, Chambers HF. (2017) Antimicrob Agents Chemother. 61: e02727-16.

Structural Insights into Inhibition of Escherichia coli Penicillin-binding Protein 1B. King DT, Wasney GA, Nosella M, Fong A, Strynadka NC. (2017) J Biol Chem. 292: 979-993.

Near-atomic-resolution cryo-EM analysis of the Salmonella T3S injectisome basal body. Worrall LJ, Hong C, Vuckovic M, Deng W, Bergeron JRC, Majewski DD, Huang RK, Spreter T, Finlay BB, Yu Z, Strynadka NC. (2016) Nature. 540: 597-601.

Structure and Mechanism of Staphylococcus aureus TarS, the Wall Teichoic Acid β-glycosyltransferase Involved in Methicillin Resistance. Sobhanifar S, Worrall LJ, King DT, Wasney GA, Baumann L, Gale RT, Nosella M, Brown ED, Withers SG, Strynadka NC. (2016) PLoS Pathog. 12: e1006067.

Identification of Two Phosphate Starvation-induced Wall Teichoic Acid Hydrolases Provides First Insights into the Degradative Pathway of a Key Bacterial Cell Wall Component. Myers CL, Li FK, Koo BM, El-Halfawy OM, French S, Gross CA, Strynadka NC, Brown ED. (2016) J Biol Chem. 291: 26066-26082.

One ring to rule them all: Current trends in combating bacterial resistance to the β-lactams. King DT, Sobhanifar S, Strynadka NC. (2016) Protein Sci. 25: 787-803.

Structural and Kinetic Characterization of Diazabicyclooctanes as Dual Inhibitors of Both Serine-β-Lactamases and Penicillin-Binding Proteins. King AM, King DT, French S, Brouillette E, Asli A, Alexander JA, Vuckovic M, Maiti SN, Parr TR Jr, Brown ED, Malouin F, Strynadka NC, Wright GD. (2016) ACS Chem Biol. 11: 864-8.

The Structure of a Type 3 Secretion System (T3SS) Ruler Protein Suggests a Molecular Mechanism for Needle Length Sensing. Bergeron JR, Fernández L, Wasney GA, Vuckovic M, Reffuveille F, Hancock RE, Strynadka NC. (2016) J Biol Chem. 291: 1676-91.

Structural analysis of SepL, an enteropathogenic Escherichia coli type III secretion-system gatekeeper protein. Burkinshaw BJ, Souza SA, Strynadka NC. (2015) Acta Crystallogr F Struct Biol Commun. 71: 1300-8.

Antagonism screen for inhibitors of bacterial cell wall biogenesis uncovers an inhibitor of undecaprenyl diphosphate synthase. Farha MA, Czarny TL, Myers CL, Worrall LJ, French S, Conrady DG, Wang Y, Oldfield E, Strynadka NC, Brown ED. (2015) Proc Natl Acad Sci U S A. 112: 11048-53.

Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation. Volkers G, Worrall LJ, Kwan DH, Yu CC, Baumann L, Lameignere E, Wasney GA, Scott NE, Wakarchuk W, Foster LJ, Withers SG, Strynadka NC. (2015) Nat Struct Mol Biol. 22: 627-35.

Structure and mechanism of Staphylococcus aureus TarM, the wall teichoic acid α-glycosyltransferase. Sobhanifar S, Worrall LJ, Gruninger RJ, Wasney GA, Blaukopf M, Baumann L, Lameignere E, Solomonson M, Brown ED, Withers SG, Strynadka NC. (2015) Proc Natl Acad Sci U S A. 112: E576-85.

The modular structure of the inner-membrane ring component PrgK facilitates assembly of the type III secretion system basal body. Bergeron JRC, Worrall LJ, De S, Sgourakis NG, Cheung AH, Lameignere E, Okon M, Wasney GA, Baker D, McIntosh LP, Strynadka NC. (2015) Structure. 23: 161-172.

The Salmonella type III secretion system virulence effector forms a new hexameric chaperone assembly for export of effector/chaperone complexes. Tsai CL, Burkinshaw BJ, Strynadka NC, Tainer JA. (2015) J Bacteriol. 197: 672-5.

Substrate specificities and conformational flexibility of 3-ketosteroid 9α-hydroxylases. Penfield JS, Worrall LJ, Strynadka NC, Eltis LD. (2014) J Biol Chem. 289: 25523-36.

Aspergillomarasmine A overcomes metallo-β-lactamase antibiotic resistance. King AM, Reid-Yu SA, Wang W, King DT, De Pascale G, Strynadka NC, Walsh TR, Coombes BK, Wright GD. (2014) Nature. 510: 503-6.

Structural insights into the lipoprotein outer membrane regulator of penicillin-binding protein 1B. King DT, Lameignere E, Strynadka NC. (2014) J Biol Chem. 289: 19245-53.

Assembly and structure of the T3SS. Burkinshaw BJ, Strynadka NC. (2014) Biochim Biophys Acta. 1843: 1649-63.

Polyphosphate suppresses complement via the terminal pathway. Wat JM, Foley JH, Krisinger MJ, Ocariza LM, Lei V, Wasney GA, Lameignere E, Strynadka NC, Smith SA, Morrissey JH, Conway EM. (2013) Blood. 123: 768-76.

Fortifying the wall: synthesis, regulation and degradation of bacterial peptidoglycan. Sobhanifar S, King DT, Strynadka NC. (2013) Curr Opin Struct Biol. 23: 695-703.

Targeting metallo-β-lactamase enzymes in antibiotic resistance. King DT, Strynadka NC. (2013) Future Med Chem. 5: 1243-63.

A Refined Model of the Prototypical Salmonella SPI-1 T3SS Basal Body Reveals the Molecular Basis for Its Assembly. Bergeron JR, Worrall LJ, Sgourakis NG, Dimaio F, Pfuetzner RA, Felise HB, Vuckovic M, Yu AC, Miller SI, Baker D, Strynadka NC. (2013) PLoS Pathog. 9: e1003307.

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

Optimization and structure-activity relationships of a series of potent inhibitors of methicillin-resistant Staphylococcus aureus (MRSA) pyruvate kinase as novel antimicrobial agents Kumar, N. S., E. A. Amandoron, A. Cherkasov, B. B. Finlay, H. Gong, L. Jackson, S. Kaur, T. Lian, A. Moreau, C. Labriere, N. E. Reiner, R. H. See, N. C. Strynadka, L. Thorson, E. W. Wong, L. Worrall, R. Zoraghi and R. N. Young. (2012) Bioorg. Med. Chem. 20: 7069-7082.

Structural insights into the anti-methicillin-resistant Staphylococcus aureus (MRSA) activity of ceftobiprole Lovering, A. L., M. C. Gretes, S. S. Safadi, F. Danel, L. de Castro, M. G. Page and N. C. Strynadka. (2012) J. Biol. Chem. 287: 32096-32102.

The zinc regulated antivirulence pathway of Salmonella is a multiprotein immunoglobulin adhesion system Prehna, G., Y. Li, N. Stoynov, M. Okon, M. Vuckovic, L. P. McIntosh, L. J. Foster, B. B. Finlay and N. C. Strynadka. (2012) J. Biol. Chem. 287: 32324-32337.

New Delhi metallo-beta-lactamase: structural insights into beta-lactam recognition and inhibition King, D. T., L. J. Worrall, R. Gruninger and N. C. Strynadka. (2012) J. Am. Chem. Soc. 134: 11362-11365.

Structural perspective of peptidoglycan biosynthesis and assembly Lovering, A. L., S. S. Safadi and N. C. Strynadka. (2012) Annu. Rev. Biochem. 81: 451-478.

A protein export pathway involving Escherichia coli porins Prehna, G., G. Zhang, X. Gong, M. Duszyk, M. Okon, L. P. McIntosh, J. H. Weiner and N. C. Strynadka. (2012) Structure 20: 1154-1166.

Characterization of alpha2,3- and alpha2,6-sialyltransferases from Helicobacter acinonychis Schur, M. J., E. Lameignere, N. C. Strynadka and W. W. Wakarchuk. (2012) Glycobiology 22: 997-1006.

Structural insight into the bacterial mucinase StcE essential to adhesion and immune evasion during enterohemorrhagic E. coli infection Yu, A. C., L. J. Worrall and N. C. Strynadka. (2012) Structure 20: 707-717.

Sec24 interaction is essential for localization and virulence-associated function of the bacterial effector protein NleA Thanabalasuriar, A., J. Bergeron, A. Gillingham, M. Mimee, J. L. Thomassin, N. Strynadka, J. Kim and S. Gruenheid. (2012) Cell. Microbiol. 14: 1206-1218.

Structure of Salmonella effector protein SopB N-terminal domain in complex with host Rho GTPase Cdc42 Burkinshaw, B. J., G. Prehna, L. J. Worrall and N. C. Strynadka. (2012) J. Biol. Chem. 287: 13348-13355.

Cheminformatics-driven discovery of selective, nanomolar inhibitors for staphylococcal pyruvate kinase Axerio-Cilies, P., R. H. See, R. Zoraghi, L. Worral, T. Lian, N. Stoynov, J. Jiang, S. Kaur, L. Jackson, H. Gong, R. Swayze, E. Amandoron, N. S. Kumar, A. Moreau, M. Hsing, N. Strynadka, W. R. McMaster, B. B. Finlay, L. J. Foster, R. N. Young, N. E. Reiner and A. Cherkasov. (2012) ACS Chem. Biol. 7: 350-359.

Methicillin-resistant Staphylococcus aureus (MRSA) pyruvate kinase as a target for bis-indole alkaloids with antibacterial activities Zoraghi, R., L. Worrall, R. H. See, W. Strangman, W. L. Popplewell, H. Gong, T. Samaai, R. D. Swayze, S. Kaur, M. Vuckovic, B. B. Finlay, R. C. Brunham, W. R. McMaster, M. T. Davies-Coleman, N. C. Strynadka, R. J. Andersen and N. E. Reiner. (2011) J. Biol. Chem. 286: 44716-44725.

Activity of 3-ketosteroid 9alpha-hydroxylase (KshAB) indicates cholesterol side chain and ring degradation occur simultaneously in Mycobacterium tuberculosis Capyk, J. K., I. Casabon, R. Gruninger, N. C. Strynadka, and L. D. Eltis. (2011) J. Biol. Chem. 286: 40717-40724.

Structure and mechanism of the lipooligosaccharide sialyltransferase from Neisseria meningitidis Lin, L. Y., B. Rakic, C. P. Chiu, E. Lameignere, W. W. Wakarchuk, S. G. Withers and N. C. Strynadka. (2011) J. Biol. Chem. 286: 37237-37248.

Structural and kinetic analysis of substrate binding to the sialyltransferase Cst-II from Campylobacter jejuni Lee, H. J., L. L. Lairson, J. R. Rich, E. Lameignere, W. W. Wakarchuk, S. G. Withers and N. C. Strynadka. (2011) J. Biol. Chem. 286: 35922-35932.

Crystal structure of New Delhi metallo-beta-lactamase reveals molecular basis for antibiotic resistance King, D. and N. Strynadka. (2011) Protein Sci. 20: 1484-1491.

Identification of pyruvate kinase in methicillin-resistant Staphylococcus aureus as a novel antimicrobial drug target Zoraghi, R., R. H. See, P. Axerio-Cilies, N. S. Kumar, H. Gong, A. Moreau, M. Hsing, S. Kaur, R. D. Swayze, L. Worrall, E. Amandoron, T. Lian, L. Jackson, J. Jiang, L. Thorson, C. Labriere, L. Foster, R. C. Brunham, W. R. McMaster, B. B. Finlay, N. C. Strynadka, A. Cherkasov, R. N. Young and N. E. Reiner. (2011) Antimicrob. Agents Chemother. 55: 2042-2053.

Structural overview of the bacterial injectisome Worrall, L. J., E. Lameignere and N. Strynadka. (2011) Curr Opin Microbiol. 14: 3-8.

Structure of a SLC26 anion transporter STAS domain in complex with acyl carrier protein: implications for E. coli YchM in fatty acid metabolism Babu, M., J. F. Greenblatt, A. Emili, N. C. Strynadka, R. A. Reithmeier and T. F. Moraes. (2010) Structure 18: 1450-1462.

Interactions of the transmembrane polymeric rings of the Salmonella enterica serovar Typhimurium type III secretion system Sanowar, S., P. Singh, R. A. Pfuetzner, I. Andre, H. Zheng, T. Spreter, N. C. Strynadka, T. Gonen, D. Baker, D. R. Goodlett and S. I. Miller. (2010) MBio 1.

A flavin-dependent monooxygenase from Mycobacterium tuberculosis involved in cholesterol catabolism Dresen, C., L. Y. Lin, I. D'Angelo, E. I. Tocheva, N. Strynadka, and L. D. Eltis. (2010) J. Biol. Chem. 285: 22264-22275.

Structure of the bacterial teichoic acid polymerase TagF provides insights into membrane association and catalysis Lovering, A. L., L. Y. Lin, E. W. Sewell, T. Spreter, E. D. Brown and N. C. Strynadka. (2010) Nat. Struct. Mol. Biol. 17: 582-589.

Crystal structure of the C-terminal domain of the Salmonella type III secretion system export apparatus protein InvA Worrall, L. J., M. Vuckovic and N. C. Strynadka. (2010) Protein Sci. 19: 1091-1096.

Circular permutation of Bacillus circulans xylanase: a kinetic and structural study Reitinger, S., Y. Yu, J. Wicki, M. Ludwiczek, I. D'Angelo, S. Baturin, M. Okon, N. C. Strynadka, S. Lutz, S. G. Withers and L. P. McIntosh. (2010) Biochemistry 49: 2464-2474.

Cyclobutanone analogues of beta-lactams revisited: insights into conformational requirements for inhibition of serine- and metallo-beta-lactamases Johnson, J. W., M. Gretes, V. J. Goodfellow, L. Marrone, M. L. Heynen, N. C. Strynadka and G. I. Dmitrienko. (2010) J. Am. Chem. Soc. 132: 2558-2560.

Protein crystallography reveals a role for the FS0 cluster of Escherichia coli nitrate reductase A (NarGHI) in enzyme maturation Rothery, R. A., M. G. Bertero, T. Spreter, N. Bouromand, N. C. Strynadka and J. H. Weiner. (2010) J. Biol. Chem. 285: 8801-8807.

NMR spectroscopic characterization of the sialyltransferase CstII from Campylobacter jejuni: histidine 188 is the general base Chan, P. H., L. L. Lairson, H. J. Lee, W. W. Wakarchuk, N. C. Strynadka, S. G. Withers and L. P. McIntosh. (2009) Biochemistry 48: 11220-11230.

Structural insight into mammalian sialyltransferases Rao, F. V., J. R. Rich, B. Rakic, S. Buddai, M. F. Schwartz, K. Johnson, C. Bowe, W. W. Wakarchuk, S. Defrees, S. G. Withers and N. C. Strynadka. (2009) Nat. Struct. Mol. Biol. 16: 1186-1188.

Inhibition of Neisseria meningitidis sialic acid synthase by a tetrahedral intermediate analogue Liu, F., H. J. Lee, N. C. Strynadka and M. E. Tanner. (2009) Biochemistry 48: 9194-9201.

Insights into the bacterial transferrin receptor: the structure of transferrin-binding protein B from Actinobacillus pleuropneumoniae Moraes, T. F., R. H. Yu, N. C. Strynadka and A. B. Schryvers. (2009) Mol. Cell 35: 523-533.

Designer enzymes for glycosphingolipid synthesis by directed evolution Hancock, S. M., J. R. Rich, M. E. Caines, N. C. Strynadka and S. G. Withers. (2009) Nat. Chem. Biol. 5: 508-514.

Structural and kinetic characterizations of the polysialic acid O-acetyltransferase OatWY from Neisseria meningitidis Lee, H. J., B. Rakic, M. Gilbert, W. W. Wakarchuk, S. G. Withers and N. C. Strynadka. (2009) J. Biol. Chem. 284: 24501-24511.

A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system Spreter, T., C. K. Yip, S. Sanowar, I. Andre, T. G. Kimbrough, M. Vuckovic, R. A. Pfuetzner, W. Deng, A. C. Yu, B. B. Finlay, D. Baker, S. I. Miller and N. C. Strynadka. (2009) Nat. Struct. Mol. Biol. 16: 468-476.

Insights into positive and negative requirements for protein-protein interactions by crystallographic analysis of the beta-lactamase inhibitory proteins BLIP, BLIP-I, and BLP Gretes, M., D. C. Lim, L. de Castro, S. E. Jensen, S. G. Kang, K. J. Lee and N. C. Strynadka. (2009) J. Mol. Biol. 389: 289-305.

Studies of a ring-cleaving dioxygenase illuminate the role of cholesterol metabolism in the pathogenesis of Mycobacterium tuberculosis Yam, K. C., I. D'Angelo, R. Kalscheuer, H. Zhu, J. X. Wang, V. Snieckus, L. H. Ly, P. J. Converse, W. R. Jacobs, Jr., N. C. Strynadka and L. D. Eltis. (2009) PLoS Pathog. 5: e1000344.

Characterization of 3-ketosteroid 9{alpha}-hydroxylase, a Rieske oxygenase in the cholesterol degradation pathway of Mycobacterium tuberculosis Capyk, J. K., I. D'Angelo, N. C. Strynadka and L. D. Eltis. (2009) J. Biol. Chem. 284: 9937-9946.

Structural characterization of the type-III pilot-secretin complex from Shigella flexneri Okon, M., T. F. Moraes, P. I. Lario, A. L. Creagh, C. A. Haynes, N. C. Strynadka and L. P. McIntosh. (2008) Structure 16: 1544-1554.

Putting glycobiology on a structural footing. van Aalten, D. M. and N. C. Strynadka (2008) Curr. Opin. Struct. Biol. 18: 525-526.

The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR Wilke, M. S., M. Heller, A. L. Creagh, C. A. Haynes, L. P. McIntosh, K. Poole and N. C. Strynadka. (2008) Proc. Natl. Acad. Sci. U.S.A. 105: 14832-14837.

The structural basis for T-antigen hydrolysis by Streptococcus pneumoniae: a target for structure-based vaccine design Caines, M. E., H. Zhu, M. Vuckovic, L. M. Willis, S. G. Withers, W. W. Wakarchuk and N. C. Strynadka. (2008) J. Biol. Chem. 283: 31279-31283.

Identification of dynamic structural motifs involved in peptidoglycan glycosyltransfer Lovering, A. L., L. De Castro and N. C. Strynadka. (2008) J. Mol. Biol. 383: 167-177.

Structural details of the glycosyltransferase step of peptidoglycan assembly Lovering, A. L., M. Gretes and N. C. Strynadka. (2008) Curr. Opin. Struct. Biol. 18: 534-543.

Structural analysis of the essential self-cleaving type III secretion proteins EscU and SpaS Zarivach, R., W. Deng, M. Vuckovic, H. B. Felise, H. V. Nguyen, S. I. Miller, B. B. Finlay and N. C. Strynadka. (2008) Nature 453: 124-127.

In vitro selection and characterization of ceftobiprole-resistant methicillin-resistant Staphylococcus aureus Banerjee, R., M. Gretes, L. Basuino, N. Strynadka and H. F. Chambers. (2008) Antimicrob. Agents Chemother. 52: 2089-2096.

Piecing together the type III injectisome of bacterial pathogens Moraes, T. F., T. Spreter and N. C. Strynadka. (2008) Curr. Opin. Struct. Biol. 18: 258-266.

The bacterial virulence factor NleA inhibits cellular protein secretion by disrupting mammalian COPII function Kim, J., A. Thanabalasuriar, T. Chaworth-Musters, J. C. Fromme, E. A. Frey, P. I. Lario, P. Metalnikov, K. Rizg, N. A. Thomas, S. F. Lee, E. L. Hartland, P. R. Hardwidge, T. Pawson, N. C. Strynadka, B. B. Finlay, R. Schekman and S. Gruenheid. (2007) Cell Host Microbe 2: 160-171.

High-resolution structure of the major periplasmic domain from the cell shape-determining filament MreC Lovering, A. L. and N. C. Strynadka. (2007) J. Mol. Biol. 372: 1034-1044.

Protein modulator of multidrug efflux gene expression in Pseudomonas aeruginosa Daigle, D. M., L. Cao, S. Fraud, M. S. Wilke, A. Pacey, R. Klinoski, N. C. Strynadka, C. R. Dean and K. Poole. (2007) J. Bacteriol. 189: 5441-5451.

Structural analysis of the alpha-2,3-sialyltransferase Cst-I from Campylobacter jejuni in apo and substrate-analogue bound forms Chiu, C. P., L. L. Lairson, M. Gilbert, W. W. Wakarchuk, S. G. Withers and N. C. Strynadka. (2007) Biochemistry 46: 7196-7204.

The structural basis of glycosidase inhibition by five-membered iminocyclitols: the clan a glycoside hydrolase endoglycoceramidase as a model system Caines, M. E., S. M. Hancock, C. A. Tarling, T. M. Wrodnigg, R. V. Stick, A. E. Stutz, A. Vasella, S. G. Withers and N. C. Strynadka. (2007) Angew Chem. Int. Ed. Engl. 46: 4474-4476.

Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis Lovering, A. L., L. H. de Castro, D. Lim and N. C. Strynadka. (2007) Science 315: 1402-1405.

Structural and mechanistic analyses of endo-glycoceramidase II, a membrane-associated family 5 glycosidase in the Apo and GM3 ganglioside-bound forms Caines, M. E., M. D. Vaughan, C. A. Tarling, S. M. Hancock, R. A. Warren, S. G. Withers and N. C. Strynadka. (2007) J. Biol. Chem. 282: 14300-14308.

Structural analysis of a prototypical ATPase from the type III secretion system Zarivach, R., M. Vuckovic, W. Deng, B. B. Finlay and N. C. Strynadka. (2007) Nat. Struct. Mol. Biol. 14: 131-137.

An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane Moraes, T. F., M. Bains, R. E. Hancock and N. C. Strynadka. (2007) Nat. Struct. Mol. Biol. 14: 85-87.

Binding hot spots in the TEM1-BLIP interface in light of its modular architecture Reichmann, D., M. Cohen, R. Abramovich, O. Dym, D. Lim, N. C. Strynadka and G. Schreiber. (2007) J. Mol. Biol. 365: 663-679.

Structure-based mutagenesis of SigE verifies the importance of hydrophobic and electrostatic residues in type III chaperone function Knodler, L. A., M. Bertero, C. Yip, N. C. Strynadka and O. Steele-Mortimer. (2006) Mol. Microbiol. 62: 928-940.

High-throughput screening methodology for the directed evolution of glycosyltransferases Aharoni, A., K. Thieme, C. P. Chiu, S. Buchini, L. L. Lairson, H. Chen, N. C. Strynadka, W. W. Wakarchuk and S. G. Withers. (2006) Nat. Methods 3: 609-614.

Structural polymorphism in bacterial EspA filaments revealed by cryo-EM and an improved approach to helical reconstruction Wang, Y. A., X. Yu, C. Yip, N. C. Strynadka and E. H. Egelman. (2006) Structure 14: 1189-1196.

Structural analysis of an “open” form of PBP1B from Streptococcus pneumoniae Lovering, A. L., L. De Castro, D. Lim and N. C. Strynadka. (2006) Protein Sci. 15: 1701-1709.

New structural insights into the bacterial type III secretion system Yip, C. K. and N. C. Strynadka. (2006) Trends Biochem. Sci. 31: 223-230.

Expanding the thioglycoligase strategy to the synthesis of alpha-linked thioglycosides allows structural investigation of the parent enzyme/substrate complex Kim, Y. W., A. L. Lovering, H. Chen, T. Kantner, L. P. McIntosh, N. C. Strynadka and S. G. Withers. (2006) J Am. Chem. Soc. 128: 2202-2203.

CesT is a multi-effector chaperone and recruitment factor required for the efficient type III secretion of both LEE- and non-LEE-encoded effectors of enteropathogenic Escherichia coli Thomas, N. A., W. Deng, J. L. Puente, E. A. Frey, C. K. Yip, N. C. Strynadka and B. B. Finlay. (2005) Mol. Microbiol. 57: 1762-1779.

Beta-lactam antibiotic resistance: a current structural perspective Wilke, M. S., A. L. Lovering and N. C. Strynadka. (2005) Curr. Opin. Microbiol. 8: 525-533.

Structural characterization of the molecular platform for type III secretion system assembly Yip, C. K., T. G. Kimbrough, H. B. Felise, M. Vuckovic, N. A. Thomas, R. A. Pfuetzner, E. A. Frey, B. B. Finlay, S. I. Miller and N. C. Strynadka . (2005) Nature 435: 702-707.

Backbone chemical shift assignments of the LexA catalytic domain in its active conformation Okon, M., R. A. Pfuetzner, M. Vuckovic, J. W. Little, N. C. Strynadka and L. P. McIntosh. (2005) J. Biomol. NMR 31: 371-372.

Investigation of the environment surrounding iron-sulfur cluster 4 of Escherichia coli dimethylsulfoxide reductase Cheng, V. W., R. A. Rothery, M. G. Bertero, N. C. Strynadka and J. H. Weiner. (2005) Biochemistry 44: 8068-8077.

Structure and biochemical analysis of a secretin pilot protein Lario, P. I., R. A. Pfuetzner, E. A. Frey, L. Creagh, C. Haynes, A. T. Maurelli and N. C. Strynadka. (2005) EMBO J. 24: 1111-1121

Structural characterization of a type III secretion system filament protein in complex with its chaperone Yip, C. K., B. B. Finlay and N. C. Strynadka. (2005) Nat. Struct. Mol. Biol. 12: 75-81.

Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A Bertero, M. G., R. A. Rothery, N. Boroumand, M. Palak, F. Blasco, N. Ginet, J. H. Weiner and N. C. Strynadka. (2005) J. Biol. Chem. 280: 14836-14843.

Structural and mechanistic analysis of sialic acid synthase NeuB from Neisseria meningitidis in complex with Mn2+, phosphoenolpyruvate, and N-acetylmannosaminitol Gunawan, J., D. Simard, M. Gilbert, A. L. Lovering, W. W. Wakarchuk, M. E. Tanner and N. C. Strynadka. (2005) J. Biol. Chem. 280: 3555-3563.

Mechanistic and structural analysis of a family 31 alpha-glycosidase and its glycosyl-enzyme intermediate Lovering, A. L., S. S. Lee, Y. W. Kim, S. G. Withers and N. C. Strynadka. (2005) J. Biol. Chem. 280: 2105-2115.

Structural and biochemical identification of a novel bacterial oxidoreductase Loschi, L., S. J. Brokx, T. L. Hills, G. Zhang, M. G. Bertero, A. L. Lovering, J. H. Weiner and N. C. Strynadka. (2004) J. Biol. Chem. 279: 50391-50400.

Crystal structures of the Apo and penicillin-acylated forms of the BlaR1 beta-lactam sensor of Staphylococcus aureus Wilke, M. S., T. L. Hills, H. Z. Zhang, H. F. Chambers and N. C. Strynadka. (2004) J. Biol. Chem. 279: 47278-47287.

Structural characterization of the RNase E S1 domain and identification of its oligonucleotide-binding and dimerization interfaces Schubert, M., R. E. Edge, P. Lario, M. A. Cook, N. C. Strynadka, G. A. Mackie and L. P. McIntosh. (2004) J. Mol. Biol. 341: 37-54.

The catalytic subunit of Escherichia coli nitrate reductase A contains a novel [4Fe-4S] cluster with a high-spin ground state Rothery, R. A., M. G. Bertero, R. Cammack, M. Palak, F. Blasco, N. C. Strynadka and J. H. Weiner. (2004) Biochemistry 43: 5324-5333.

Intermediate trapping on a mutant retaining alpha-galactosyltransferase identifies an unexpected aspartate residue Lairson, L. L., C. P. Chiu, H. D. Ly, S. He, W. W. Wakarchuk, N. C. Strynadka and S. G. Withers. (2004) J. Biol. Chem. 279: 28339-28344.

Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analog Chiu, C. P., A. G. Watts, L. L. Lairson, M. Gilbert, D. Lim, W. W. Wakarchuk, S. G. Withers and N. C. Strynadka. (2004) Nat. Struct. Mol. Biol. 11: 163-170.

Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A Bertero, M. G., R. A. Rothery, M. Palak, C. Hou, D. Lim, F. Blasco, J. H. Weiner and N. C. Strynadka. (2003) Nat. Struct. Biol. 10: 681-687.

Engineering the primary substrate specificity of Streptomyces griseus trypsin Page, M. J., S. L. Wong, J. Hewitt, N. C. Strynadka and R. T. MacGillivray. (2003) Biochemistry 42: 9060-9066.

One step closer to a sweet conclusion Withers, S. G., W. W. Wakarchuk and N. C. Strynadka. (2002) Chem. Biol. 9: 1270-1273.

Signal peptidases Paetzel, M., A. Karla, N. C. Strynadka and R. E. Dalbey. (2002) Chem. Rev. 102: 4549-4580.

Structural basis for the beta lactam resistance of PBP2a from methicillin-resistant Staphylococcus aureus Lim, D and N. C. Strynadka. (2002) Nat. Struct. Biol. 9: 870-876.

Crystal structure of the MexR repressor of the mexRAB-oprM multidrug efflux operon of Pseudomonas aeruginosa Lim, D., K. Poole and N. C. Strynadka. (2002) J. Biol. Chem. 277: 29253-29259.

Crystal structure of a bacterial signal peptidase apoenzyme: implications for signal peptide binding and the Ser-Lys dyad mechanism Paetzel, M., R. E. Dalbey and N. C. Strynadka. (2002) J. Biol. Chem. 277: 9512-9519.

Catalysis and binding in L-ribulose-5-phosphate 4-epimerase: a comparison with L-fuculose-1-phosphate aldolase Samuel, J., Y. Luo, P. M. Morgan, N. C. Strynadka and M. E. Tanner. (2001) Biochemistry 40: 14772-14780.

The structure of L-ribulose-5-phosphate 4-epimerase: an aldolase-like platform for epimerization Luo, Y., J. Samuel, S. C. Mosimann, J. E. Lee, M. E. Tanner and N. C. Strynadka . (2001) Biochemistry 40: 14763-14771.

Structural and biochemical characterization of the type III secretion chaperones CesT and SigE Luo, Y., M. G. Bertero, E. A. Frey, R. A. Pfuetzner, M. R. Wenk, L. Creagh, S. L. Marcus, D. Lim, F. Sicheri, C. Kay, C. Haynes, B. B. Finlay and N. C. Strynadka. (2001) Nat. Struct. Biol. 8: 1031-1036.

Crystal structure and kinetic analysis of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase Lim, D., H. U. Park, L. De Castro, S. G. Kang, H. S. Lee, S. Jensen, K. J. Lee and N. C. Strynadka. (2001) Nat. Struct. Biol. 8: 848-852.

Crystal structure of LexA: a conformational switch for regulation of self-cleavage. Luo, Y., R. A. Pfuetzner, S. Mosimann, M. Paetzel, E. A. Frey, M. Cherney, B. Kim, J. W. Little and N. C. Strynadka. (2001) Cell 106: 585-594.

Structure and characterization of AgfB from Salmonella enteritidis thin aggregative fimbriae White, A. P., S. K. Collinson, P. A. Banser, D. L. Gibson, M. Paetzel, N. C. Strynadka and W. W. Kay. (2001) J. Mol. Biol. 311: 735-749.

Effect of divalent metal cations on the dimerization of OXA-10 and -14 class D beta-lactamases from Pseudomonas aeruginosa Danel, F., M. Paetzel, N. C. Strynadka and M. G. Page. (2001) Biochemistry 40: 9412-9420.

Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs Persson, K., H. D. Ly, M. Dieckelmann, W. W. Wakarchuk, S. G. Withers and N. C. Strynadka . (2001) Nat. Struct. Biol. 8: 166-175

Insights into the molecular basis for the carbenicillinase activity of PSE-4 beta-lactamase from crystallographic and kinetic studies. Lim, D., F. Sanschagrin, L. Passmore, L. De Castro, R. C. Levesque and N. C. Strynadka. (2001) Biochemistry 40: 395-402

Structure of a sialic acid-activating synthetase, CMP-acylneuraminate synthetase in the presence and absence of CDP Mosimann, S. C., M. Gilbert, D. Dombroswki, R. To, W. Wakarchuk and N. C. Strynadka. (2001) J. Biol. Chem. 276: 8190-8196.

The structure of UDP-N-acetylglucosamine 2-epimerase reveals homology to phosphoglycosyl transferases Campbell, R. E., S. C. Mosimann, M. E. Tanner and N. C. Strynadka. (2000) Biochemistry 39: 14993-15001.

Crystal structure of the class D beta-lactamase OXA-10 Paetzel, M., F. Danel, L. de Castro, S. C. Mosimann, M. G. Page and N. C. Strynadka. (2000) Nat. Struct. Biol. 7: 918-925.

The structure and mechanism of bacterial type I signal peptidases. A novel antibiotic target Paetzel, M., R. E. Dalbey and N. C. Strynadka. (2000) Pharmacol. Ther. 87: 27-49.

Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex Luo, Y., E. A. Frey, R. A. Pfuetzner, A. L. Creagh, D. G. Knoechel, C. A. Haynes, B. B. Finlay and N. C. Strynadka. (2000) Nature 405: 1073-1077.

Enteropathogenic E. coli translocated intimin receptor, Tir, interacts directly with alpha-actinin Goosney, D. L., R. DeVinney, R. A. Pfuetzner, E. A. Frey, N. C. Strynadka and B. B. Finlay. (2000) Curr. Biol. 10: 735-738.

Mutational evidence of transition state stabilization by serine 88 in Escherichia coli type I signal peptidase Carlos, J. L., P. A. Klenotic, M. Paetzel, N. C. Strynadka and R. E. Dalbey. (2000) Biochemistry 39: 7276-7283.

The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation Campbell, R. E., S. C. Mosimann, I. van De Rijn, M. E. Tanner and N. C. Strynadka. (2000) Biochemistry 39: 7012-7023.

Structure-based design guides the improved efficacy of deacylation transition state analogue inhibitors of TEM-1 beta-Lactamase(,) Ness, S., R. Martin, A. M. Kindler, M. Paetzel, M. Gold, S. E. Jensen, J. B. Jones and N. C. Strynadka. (2000) Biochemistry 39: 5312-5321.

The role of the conserved box E residues in the active site of the Escherichia coli type I signal peptidase Klenotic, P. A., J. L. Carlos, J. C. Samuelson, T. A. Schuenemann, W. R. Tschantz, M. Paetzel, N. C. Strynadka and R. E. Dalbey. (2000) J. Biol. Chem. 275: 6490-6498.

Common protein architecture and binding sites in proteases utilizing a Ser/Lys dyad mechanism Paetzel, M. and N. C. Strynadka. (1999) Protein Sci. 8: 2533-2536.

Enteropathogenic Escherichia coli translocated intimin receptor, Tir, requires a specific chaperone for stable secretion Abe, A., M. de Grado, R. A. Pfuetzner, C. Sanchez-Sanmartin, R. Devinney, J. L. Puente, N. C. Strynadka and B. B. Finlay. (1999) Mol Microbiol. 33: 1162-1175.

Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor Paetzel, M., R. E. Dalbey and N. C. Strynadka. (1998) Nature 396: 186-190.