beta-Sultams - A novel class of serine protease inhibitors by Beardsell, M, Hinchliffe, P, Wood, J, Wilmouth, R, Schofield, C, Page, M

Natural variants modify Klebsiella pneumoniae carbapenemase (KPC) acyl-enzyme conformational dynamics to extend antibiotic resistance. by Tooke, CL, Hinchliffe, P, Bonomo, RA, Schofield, CJ, Mulholland, AJ, Spencer, J

Cyclic boronates as versatile scaffolds for KPC-2 β-lactamase inhibition by Tooke, C, Hinchliffe, P, Krajnc, A, Mulholland, A, Brem, J, Schofield, C, Spencer, J

Tautomer-specific deacylation and Ω-loop flexibility explain the carbapenem-hydrolyzing broad-spectrum activity of the KPC-2 β-lactamase by Tooke, CL, Hinchliffe, P, Beer, M, Zinovjev, K, Colenso, CK, Schofield, CJ, Mulholland, AJ, Spencer, J

Structural and Biochemical Characterization of Rm3, a SubClass B3 Metallo-β-Lactamase Identified from a Functional Metagenomic Study. by Salimraj, R, Zhang, L, Hinchliffe, P, Wellington, E, Brem, J, Schofield, C, Gaze, W, Spencer, J

Sideromimic Modification of Lactivicin Dramatically Increases Potency against Extensively Drug-Resistant Stenotrophomonas maltophilia Clinical Isolates. by Calvopiña, K, Umland, K, Rydzik, A, Hinchliffe, P, Brem, J, Spencer, J, Schofield, C, Avison, M

Mechanistic insights into β-lactamase-catalysed carbapenem degradation through product characterisation by Lohans, C, Freeman, E, Van Groesen, E, Tooke, C, Hinchliffe, P, Spencer, J, Brem, J, Schofield, C

Interactions of hydrolyzed β-lactams with the L1 metallo-β-lactamase: Crystallography supports stereoselective binding of cephem/carbapenem products by Hinchliffe, P, Calvopiña, K, Rabe, P, Mojica, MF, Schofield, CJ, Dmitrienko, GI, Bonomo, RA, Vila, AJ, Spencer, J

Cyclobutanone mimics of intermediates in metallo-β-lactamase catalysis. by Abboud, M, Kosmopoulou, M, Krismanich, A, Johnson, J, Hinchliffe, P, Brem, J, Claridge, T, Spencer, J, Schofield, C, Dmitrienko, G

Structural/mechanistic insights into the efficacy of nonclassical β-lactamase inhibitors against extensively drug resistant Stenotrophomonas maltophilia clinical isolates by Calvopiña, K, Hinchliffe, P, Brem, J, Heesom, K, Johnson, S, Cain, R, Lohans, C, Fishwick, C, Schofield, C, Spencer, J, Avison, M

Profiling interactions of vaborbactam with metallo-β-lactamases by Langley, G, Cain, R, Tyrrell, J, Hinchliffe, P, Calvopiña, K, Tooke, C, Widlake, E, Dowson, C, Spencer, J, Walsh, T, Schofield, C, Brem, J

19F-NMR reveals the role of mobile loops in product and inhibitor binding by the São Paolo metallo-β-lactamase by Abboud, M, Hinchliffe, P, Brem, J, Macsics, R, Pfeffer, I, Makena, A, Umland, K, Rydzik, A, Li, G, Spencer, J, Claridge, T, Schofield, C

Crystal structures of VIM‐1 complexes explain active site heterogeneity in VIM‐class metallo‐β‐lactamases by Salimraj, R, Hinchliffe, P, Kosmopoulou, M, Tyrrell, J, Brem, J, Van Berkel, S, Verma, A, Owens, R, McDonough, M, Walsh, T, Schofield, C, Spencer, J

Faropenem reacts with serine and metallo-β-lactamases to give multiple products by Lucic, A, Hinchliffe, P, Malla, T, Tooke, C, Brem, J, Calvopina, K, Lohans, C, Rabe, P, McDonough, M, Armistead, T, Orville, A, Spencer, J, Schofield, C

Bicyclic boronate VNRX-5133 inhibits metallo- and serine-β-lactamases by Krajnc, A, Brem, J, Hinchliffe, P, Calvopiña, K, Panduwawala, TD, Lang, PA, Kamps, JJAG, Tyrrell, JM, Widlake, E, Saward, BG, Walsh, TR, Spencer, J, Schofield, CJ

Insights into the Mechanistic Basis of Plasmid-Mediated Colistin Resistance from Crystal Structures of the Catalytic Domain of MCR-1. by Hinchliffe, P, Yang, Q, Portal, E, Young, T, Li, H, Tooke, C, Carvalho, M, Paterson, N, Brem, J, Niumsup, P, Tansawai, U, Lei, L, Li, M, Shen, Z, Wang, Y, Schofield, C, Mulholland, A, Shen, J, Fey, N, Walsh, T, Spencer, J

An on-demand, drop-on-drop method for studying enzyme catalysis by serial crystallography by Butryn, A, Simon, PS, Aller, P, Hinchliffe, P, Massad, RN, Leen, G, Tooke, CL, Bogacz, I, Kim, I-S, Bhowmick, A, Brewster, AS, Devenish, NE, Brem, J, Kamps, JJAG, Lang, PA, Rabe, P, Axford, D, Beale, JH, Davy, B, Ebrahim, A, Orlans, J, Storm, SLS, Zhou, T, Owada, S, Tanaka, R, Tono, K, Evans, G, Owen, RL, Houle, FA, Sauter, NK, Schofield, CJ, Spencer, J, Yachandra, VK, Yano, J, Kern, JF, Orville, AM

Imitation of β-lactam binding enables broad-spectrum metallo-β-lactamase inhibitors by Brem, J, Panduwawala, T, Hansen, JU, Hewitt, J, Liepins, E, Donets, P, Espina, L, Farley, AJM, Shubin, K, Campillos, GG, Kiuru, P, Shishodia, S, Krahn, D, Leśniak, RK, Schmidt Adrian, J, Calvopiña, K, Turrientes, M-C, Kavanagh, ME, Lubriks, D, Hinchliffe, P, Langley, GW, Aboklaish, AF, Eneroth, A, Backlund, M, Baran, AG, Nielsen, EI, Speake, M, Kuka, J, Robinson, J, Grinberga, S, Robinson, L, McDonough, MA, Rydzik, AM, Leissing, TM, Jimenez-Castellanos, JC, Avison, MB, Da Silva Pinto, S, Pannifer, AD, Martjuga, M, Widlake, E, Priede, M, Hopkins Navratilova, I, Gniadkowski, M, Belfrage, AK, Brandt, P, Yli-Kauhaluoma, J, Bacque, E, Page, MGP, Björkling, F, Tyrrell, JM, Spencer, J, Lang, PA, Baranczewski, P, Cantón, R, McElroy, SP, Jones, PS, Baquero, F, Suna , E, Morrison, A, Walsh, TR, Schofield, CJ