Drawz SM, Bonomo RA. 2010. Three decades of β-lactamase inhibitors. Clin Microbiol Rev 23:160-201. http://dx.doi.org/10.1128/CMR.00037-09.
Parker AC, Smith CJ. 1993. Genetic and biochemical analysis of a novel Ambler class A β-lactamase responsible for cefoxitin resistance in Bacteroides species. Antimicrob Agents Chemother 37:1028-1036. http://dx.doi.org/10.1128/AAC.37.5.1028.
Monnaie D, Frere JM. 1993. Interaction of clavulanate with class C β-lactamases. FEBS Lett 334:269-271. http://dx.doi.org/10.1016/0014-5793(93)80692-N.
Papp-Wallace KM, Bethel CR, Distler AM, Kasuboski C, Taracila M, Bonomo RA. 2010. Inhibitor resistance in the KPC-2 β-lactamase, a preeminent property of this class A β-lactamase. Antimicrob Agents Chemother 54:890-897. http://dx.doi.org/10.1128/AAC.00693-09.
Bush K. 2015. A resurgence of β-lactamase inhibitor combinations effective against multidrug-resistant Gram-negative pathogens. Int J Antimicrob Agents 46:483-493. http://dx.doi.org/10.1016/j.ijantimicag.2015.08.011.
Bonnefoy A, Dupuis-Hamelin C, Steier V, Delachaume C, Seys C, Stachyra T, Fairley M, Guitton M, Lampilas M. 2004. In vitro activity of AVE1330A, an innovative broad-spectrum non-β-lactam β-lactamase inhibitor. J Antimicrob Chemother 54:410-417. http://dx.doi.org/10.1093/jac/dkh358.
Coleman K. 2011. Diazabicyclooctanes (DBOs): a potent new class of non-β-lactam β-lactamase inhibitors. Curr Opin Microbiol 14:550-555. http://dx.doi.org/10.1016/j.mib.2011.07.026.
Stachyra T, Pechereau MC, Bruneau JM, Claudon M, Frere JM, Miossec C, Coleman K, Black MT. 2010. Mechanistic studies of the inactivation of TEM-1 and P99 by NXL104, a novel non-β-lactam β-lactamase inhibitor. Antimicrob Agents Chemother 54:5132-5138. http://dx.doi.org/10.1128/AAC.00568-10.
Ehmann DE, Jahic H, Ross PL, Gu RF, Hu J, Kern G, Walkup GK, Fisher SL. 2012. Avibactam is a covalent, reversible, non-β-lactam β-lactamase inhibitor. Proc Natl Acad Sci U S A 109:11663-11668. http://dx.doi.org/10.1073/pnas.1205073109.
Wilmouth RC, Kassamally S, Westwood NJ, Sheppard RJ, Claridge TD, Aplin RT, Wright PA, Pritchard GJ, Schofield CJ. 1999. Mechanistic insights into the inhibition of serine proteases by monocyclic lactams. Biochemistry 38:7989-7998. http://dx.doi.org/10.1021/bi990098y.
Ehmann DE, Jahic H, Ross PL, Gu RF, Hu J, Durand-Reville TF, Lahiri S, Thresher J, Livchak S, Gao N, Palmer T, Walkup GK, Fisher SL. 2013. Kinetics of avibactam inhibition against class A, C, and D β-lactamases. J Biol Chem 288:27960-27971. http://dx.doi.org/10.1074/jbc.M113.485979.
Livermore DM, Mushtaq S, Warner M, Zhang J, Maharjan S, Doumith M, Woodford N. 2011. Activities of NXL104 combinations with ceftazidime and aztreonam against carbapenemase-producing Enterobacteriaceae. Antimicrob Agents Chemother 55:390-394. http://dx.doi.org/10.1128/AAC.00756-10.
Mushtaq S, Warner M, Williams G, Critchley I, Livermore DM. 2010. Activity of chequerboard combinations of ceftaroline and NXL104 versus β-lactamase-producing Enterobacteriaceae. J Antimicrob Chemother 65:1428-1432. http://dx.doi.org/10.1093/jac/dkq161.
Castanheira M, Sader HS, Farrell DJ, Mendes RE, Jones RN. 2012. Activity of ceftaroline-avibactam tested against Gram-negative organism populations, including strains expressing one or more β-lactamases and methicillin-resistant Staphylococcus aureus carrying various staphylococcal cassette chromosome mec types. Antimicrob Agents Chemother 56:4779-4785. http://dx.doi.org/10.1128/AAC.00817-12.
Biedenbach DJ, Kazmierczak K, Bouchillon SK, Sahm DF, Bradford PA. 2015. In vitro activity of aztreonam-avibactam against a global collection of Gram-negative pathogens from 2012 and 2013. Antimicrob Agents Chemother 59:4239-4248. http://dx.doi.org/10.1128/AAC.00206-15.
van Duin D, Bonomo RA. 2016. Ceftazidime/avibactam and ceftolozane/tazobactam: "second generation" β-lactam/β-lactamase combinations. Clin Infect Dis 63:234-241. http://dx.doi.org/10.1093/cid/ciw243.
Liscio JL, Mahoney MV, Hirsch EB. 2015. Ceftolozane/tazobactam and ceftazidime/avibactam: two novel β-lactam/β-lactamase inhibitor combination agents for the treatment of resistant Gram-negative bacterial infections. Int J Antimicrob Agents 46:266-271. http://dx.doi.org/10.1016/j.ijantimicag.2015.05.003.
Crandon JL, Nicolau DP. 2013. Human simulated studies of aztreonam and aztreonam-avibactam to evaluate activity against challenging gram-negative organisms, including metallo-β-lactamase producers. Antimicrob Agents Chemother 57:3299-3306. http://dx.doi.org/10.1128/AAC.01989-12.
Felici A, Amicosante G, Oratore A, Strom R, Ledent P, Joris B, Fanuel L, Frere JM. 1993. An overview of the kinetic parameters of class B β-lactamases. Biochem J 291(Pt 1):151-155. http://dx.doi.org/10.1042/bj2910151.
Fast W, Sutton LD. 2013. Metallo-β-lactamase: inhibitors and reporter substrates. Biochim Biophys Acta 1834:1648-1659. http://dx.doi.org/10.1016/j.bbapap.2013.04.024.
Cornaglia G, Giamarellou H, Rossolini GM. 2011. Metallo-β-lactamases: a last frontier for β-lactams? Lancet Infect Dis 11:381-393. http://dx.doi.org/10.1016/S1473-3099(11)70056-1.
Meini MR, Llarrull LI, Vila AJ. 2015. Overcoming differences: the catalytic mechanism of metallo-β-lactamases. FEBS Lett 589:3419-3432. http://dx.doi.org/10.1016/j.febslet.2015.08.015.
van Berkel SS, Brem J, Rydzik AM, Salimraj R, Cain R, Verma A, Owens RJ, Fishwick CW, Spencer J, Schofield CJ. 2013. Assay platform for clinically relevant metallo-β-lactamases. J Med Chem 56:6945-6953. http://dx.doi.org/10.1021/jm400769b.
Bebrone C, Anne C, De Vriendt K, Devreese B, Rossolini GM, Van Beeumen J, Frere JM, Galleni M. 2005. Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-β-lactamase by site-directed mutagenesis. J Biol Chem 280:28195-28202. http://dx.doi.org/10.1074/jbc.M414052200.
Lassaux P, Traore DA, Loisel E, Favier A, Docquier JD, Sohier JS, Laurent C, Bebrone C, Frere JM, Ferrer JL, Galleni M. 2011. Biochemical and structural characterization of the subclass B1 metallo-β-lactamase VIM-4. Antimicrob Agents Chemother 55:1248-1255. http://dx.doi.org/10.1128/AAC.01486-09.
Laraki N, Franceschini N, Rossolini GM, Santucci P, Meunier C, de Pauw E, Amicosante G, Frere JM, Galleni M. 1999. Biochemical characterization of the Pseudomonas aeruginosa 101/1477 metallo-β-lactamase IMP-1 produced by Escherichia coli. Antimicrob Agents Chemother 43:902-906.
Mercuri PS, Garcia-Saez I, De Vriendt K, Thamm I, Devreese B, Van Beeumen J, Dideberg O, Rossolini GM, Frere JM, Galleni M. 2004. Probing the specificity of the subclass B3 FEZ-1 metallo-β-lactamase by site-directed mutagenesis. J Biol Chem 279:33630-33638. http://dx.doi.org/10.1074/jbc.M403671200.
Rydzik AM, Brem J, van Berkel SS, Pfeffer I, Makena A, Claridge TD, Schofield CJ. 2014. Monitoring conformational changes in the NDM-1 metallo-β-lactamase by 19F NMR spectroscopy. Angew Chem Int Ed Engl 53:3129-3133. http://dx.doi.org/10.1002/anie.201310866.
Brem J, Struwe WB, Rydzik AM, Tarhonskaya H, Pfeffer I, Flashman E, van Berkel SS, Spencer J, Claridge TD, McDonough MA, Benesch JL, Schofield CJ. 2015. Studying the active-site loop movement of the Sao Paolo metallo-β-lactamase-1. Chem Sci 6:956-963. http://dx.doi.org/10.1039/C4SC01752H.
Adams RW, Holroyd CM, Aguilar JA, Nilsson M, Morris GA. 2013. "Perfecting" WATERGATE: clean proton NMR spectra from aqueous solution. Chem Commun (Camb) 49:358-360. http://dx.doi.org/10.1039/C2CC37579F.
Xu G, Evans JS. 1996. The application of "excitation sculpting" in the construction of selective one-dimensional homonuclear coherence-transfer experiments. J Magn Reson B 111:183-185. http://dx.doi.org/10.1006/jmrb.1996.0079.
Dalvit C, Pevarello P, Tato M, Veronesi M, Vulpetti A, Sundstrom M. 2000. Identification of compounds with binding affinity to proteins via magnetization transfer from bulk water. J Biomol NMR 18:65-68. http://dx.doi.org/10.1023/A:1008354229396.
Galleni M, Lamotte-Brasseur J, Rossolini GM, Spencer J, Dideberg O, Frere JM, Metallo-β-lactamases Working Group. 2001. Standard numbering scheme for class B β-lactamases. Antimicrob Agents Chemother 45:660-663. http://dx.doi.org/10.1128/AAC.45.3.660-663.2001.
Carfi A, Pares S, Duee E, Galleni M, Duez C, Frere JM, Dideberg O. 1995. The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J 14:4914-4921.
Murphy TA, Simm AM, Toleman MA, Jones RN, Walsh TR. 2003. Biochemical characterization of the acquired metallo-β-lactamase SPM-1 from Pseudomonas aeruginosa. Antimicrob Agents Chemother 47:582-587. http://dx.doi.org/10.1128/AAC.47.2.582-587.2003.
Murphy TA, Catto LE, Halford SE, Hadfield AT, Minor W, Walsh TR, Spencer J. 2006. Crystal structure of Pseudomonas aeruginosa SPM-1 provides insights into variable zinc affinity of metallo-β-lactamases. J Mol Biol 357:890-903. http://dx.doi.org/10.1016/j.jmb.2006.01.003.
Hernandez Valladares M, Felici A, Weber G, Adolph HW, Zeppezauer M, Rossolini GM, Amicosante G, Frere JM, Galleni M. 1997. Zn(II) dependence of the Aeromonas hydrophila AE036 metallo-β-lactamase activity and stability. Biochemistry 36:11534-11541. http://dx.doi.org/10.1021/bi971056h.
Bebrone C. 2007. Metallo-β-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily. Biochem Pharmacol 74:1686-1701. http://dx.doi.org/10.1016/j.bcp.2007.05.021.
Docquier JD, Lamotte-Brasseur J, Galleni M, Amicosante G, Frere JM, Rossolini GM. 2003. On functional and structural heterogeneity of VIM-type metallo-β-lactamases. J Antimicrob Chemother 51:257-266. http://dx.doi.org/10.1093/jac/dkg067.
Thomas PW, Zheng M, Wu S, Guo H, Liu D, Xu D, Fast W. 2011. Characterization of purified New Delhi metallo-β-lactamase-1. Biochemistry 50:10102-10113. http://dx.doi.org/10.1021/bi201449r.
Mercuri PS, Bouillenne F, Boschi L, Lamotte-Brasseur J, Amicosante G, Devreese B, van Beeumen J, Frere JM, Rossolini GM, Galleni M. 2001. Biochemical characterization of the FEZ-1 metallo-β-lactamase of Legionella gormanii ATCC 33297T produced in Escherichia coli. Antimicrob Agents Chemother 45:1254-1262. http://dx.doi.org/10.1128/AAC.45.4.1254-1262.2001.
Choi H, Paton RS, Park H, Schofield CJ. 2016. Investigations on recyclisation and hydrolysis in avibactam mediated serine β-lactamase inhibition. Org Biomol Chem 14:4116-4128. http://dx.doi.org/10.1039/C6OB00353B.