β-Lactamase inhibitors: a survey of the patent literature 2000 – 2004

Bibliography

• GEORGOPAPADAKOU NH: Penicillin-binding proteins and bacterial resistance to β-lactams. Antimicrob. Agents Chemother. (1993) 37(10):2045-2053.
   PubMed Web of Science ®Google Scholar
• LIVERMORE DM: Interplay of impermeability and chromosomal β-lactamase in imipenem-resistant Pseudomonas aeruginosa. Antimicrob. Agents Chemother. (1992) 36(9):2046-2048.
   PubMed Web of Science ®Google Scholar
• SRIKUMAR R, TSANG E, POOLE K: Contribution of the MexAB-OprM multidrug efflux system to the β-lactam resistance of penicillin-binding protein and β-lactamase-derepressed mutants of Pseudomonas aeruginosa. J. Antimicrob. Chemother. (1999) 44(4):537-540.
   PubMed Web of Science ®Google Scholar
• SAMAHA-KFOURY JN, ARAJ GF: Recent developments in β-lactamases and extended spectrum β-lactamases. Br. Med. J. (2003) 327:1209-1213.
   PubMed Web of Science ®Google Scholar
• LIVERMORE D: Of Pseudomonas, porins, pumps and carbapenems. J. Antimicrob. Chemother. (2001) 47:247-250.
   PubMed Web of Science ®Google Scholar
• SUTHERLAND R: β-Lactam/β-lactamase inhibitor combinations: development, antibacterial activity and clinical applications. Infect. (1995) 23(4):191-200.
   PubMed Web of Science ®Google Scholar
• MARTINEZ-MARTINEZ L, HERNANDEZ-ALLES S, ALBERTI S, JACOBY GA: In vivo selection of porin-deficient mutants of Klebsiella pneumoniae with increased resistance to cefoxitin and expended-spectrum cephalosporins. Antimicrob. Agents Chemother. (1996) 40:342-348.
   PubMed Web of Science ®Google Scholar
• GEORGOPAPADAKOU NH, SYKES RB: Enzymes interacting with β-lactam antibiotics. In: Handbook of Experimental Pharmacology. Volume 67-II. Antibiotics containing the β-lactam structure. Demain AL, Solomon NA (Eds), Springer-Verlag, Berlin Heidelberg, Germany (1983):1-77.
   Google Scholar
• COULTON S, FRANCOIS I: β-Lactamases: targets for drug design. In: Progress in Medicinal Chemistry. Volume 31. Ellis GP, Luscombe DK (Eds), Elsevier Science, London (1994):297-349.
   Google Scholar
• PAGE MGP: β-Lactamase inhibitors. Drug Resist. Updat. (2000) 3:109-125.
   PubMed Web of Science ®Google Scholar
• ABRAHAM EP, CHAIN E: An enzyme from bacteria able to destroy penicillin. Nature (1940) 146(3713):837.
   Google Scholar
• AMBLER RP: The structure of β-lactamases. Philos. Trans. R. Soc. Lond. Ser. B (1980) 289:321-331.
   PubMed Web of Science ®Google Scholar
• MEDERIOS AA: Evolution and dissemination of β-lactamases accelerated by generation of β-lactam antibiotics. Clin. Infect. Dis. (1997) 24(Suppl.1):S19-S45.
   PubMed Web of Science ®Google Scholar
• LIVERMORE DM, HAWKEY PM: CTX-M: changing the face of ESBLs in the UK. J. Antimicrob. Chemother. (2005) 56:451-454.
   PubMed Web of Science ®Google Scholar
• WALSH TR, TOLEMAN MA, POIREL L, NORDMANN P: Metallo-β-lactamase: The quiet before the storm? Clin. Microbiol. Rev. (2005) 18(2):306-325.
   Google Scholar
• DUBOIS V, POIREL L, ARPIN C et al.: SHV-49, a novel inhibitor-resistant β-lactamase in a clinical isolate of Klebsiella pneumoniae. Antimicrob. Agents Chemother. (2004) 48(11):4466-4469.
   PubMed Web of Science ®Google Scholar
• SUN T, BETHEL CR, BONOMO RA, KNOX JR: Inhibitor-resistant class A β-lactamases: consequences of Ser130-to-Gly mutation seen in apo and tazobactam structures of the SHV-1 variant. Biochem. (2004) 43(44):14111-14117.
   PubMedGoogle Scholar
• SULTON D, PAGAN-RODERIGUEZ D, ZHOU X et al.: Clavulanic acid inactivation of SHV-1 and the inhibitor-resistant Ser130Gly SHV-1 β-lactamase: Insight into the mechanism of inhibition. J. Biol. Chem. (2005) 280(42):35528-35536.
   PubMedGoogle Scholar
• MAITI SN, PHILLIPS OA, MICETICH RG, LIVERMORE DM: β-Lactamase inhibitors: agents to overcome bacterial resistance. Curr. Med. Chem. (1998) 5:441-456.
   PubMed Web of Science ®Google Scholar
• LEE N, YUEN K-Y, KUMANA CR: Clinical role of β-lactam/β-lactamase inhibitor combinations. Drugs (2003) 63(14):1511-1524.
   PubMed Web of Science ®Google Scholar
• BROWN AG, BUTTERWORTH D, COLE M et al.: Naturally occurring β-lactamase inhibitors with antibacterial activity. J. Antibiot. (1976) 29(6):668-669.
   PubMed Web of Science ®Google Scholar
• GEORGOPAPADAKOU NH: β-Lactamase inhibitors: evolving compounds for evolving resistance targets. Expert. Opin. Investig. Drugs (2004) 13(10):1307-1318.
   PubMed Web of Science ®Google Scholar
• SCHITO GC, GEORGOPOULOS A, PRIETO J: Antibacterial activity of oral antibiotics against community-acquired respiratory pathogens from three European countries. J. Antimicrob. Chemother. (2002) 50(Suppl.):7-11.
   PubMedGoogle Scholar
• LIRAS P, RODRÍGUEZ-GARCÍA A: Clavulanic acid, a β-lactamase inhibitor: biosynthesis and molecular genetics. Appl. Microbiol. Biotechnol. (2000) 54:467-475.
   PubMedGoogle Scholar
• TAHLAN K, PARK HU, WONG A, BEATTY PH, JENSEN SE: Two sets of paralogous genes encoded the enzymes involved in the early stages of clavulanic acid and clavam metabolite biosynthesis in Streptomyces clavuligerus. Antimicrob. Agents Chemother. (2004) 48(3):930-939.
   PubMedGoogle Scholar
• ROUBOS JA, KRABBEN P, DE LAAT WTAM, BABUŠKA R, HEIJNEN JJ: Clavulanic acid degradation in Streptomyces clavuligerus fed-batch cultivations. Biotechnol. Prog. (2002) 18(3):451-457.
   PubMedGoogle Scholar
• LEE SD, PARK SW, OH KK, HONG SI, KIM SW: Improvement for the production of clavulanic acid by mutant Streptomyces clavuligerus. Lett. Applied Microbiol. (2002) 34:370-375.
   PubMed Web of Science ®Google Scholar
• BADINO AC: Influence of dissolved oxygen and shear conditions on clavulanic acid production by Streptomyces clavuligerus. Bioprocess Biosyst. Eng. (2005) 27(2):99-104.
   PubMedGoogle Scholar
• RICHTER HG, ANGEHRN P, HUBSCHWERLEN C et al.: Design, synthesis and evaluation of 2β-alkenyl penam sulfone acids as inhibitors of β-lactamases. J. Med. Chem. (1996) 39:3712-3722.
   PubMed Web of Science ®Google Scholar
• BASKER MJ, OSBORNE NF: 6-(Substituted methylene)penems, potent broad-spectrum inhibitors of bacterial β-lactamase. I. Racemic 6-ethylidenepenems. J. Antibiot. (1990) 43(1):70-75.
   PubMedGoogle Scholar
• BENNETT, BROOM NJ, COLEMAN K et al.: 6-(Substituted methylene)penems, potent broad spectrum inhibitors of bacterial β-lactamase. IV. Kidney stability, serum binding and additional biological evaluation of racemic derivatives. J. Antibiot. (1991) 44(3):338-343.
   PubMedGoogle Scholar
• PHILLIPS OA, CZAJKOWSKI DP, SPEVAK P et al.: SYN-1012: a new β-lactamase inhibitor of penem skeleton. J. Antibiot. (1997) 50(4):350-356.
   PubMedGoogle Scholar
• BROOM NJ, FARMER TF, OSBORNE NF, TYLER JW: Studies on the mechanism of action of (5R)-(Z)-6-(1-methyl-1,2,3-triazol-4-ylmethylene) penem-3-carboxylic acid (BRL 42715), a potent inhibitor of bacterial β-lactamase. J. Chem. Soc. Chem. Commun. (1992):1663-1664.
   Google Scholar
• TABEI K, FENG X, VENKATESAN AM et al.: Mechanism of inactivation of β-lactamases by novel 6-methylidene penems elucidated using electrospray ionization mass spectrometry. J. Med. Chem. (2004) 47(14):3674-3688.
   PubMedGoogle Scholar
• BONFIGLIO G, RUSSO G, NICOLETTI G: Recent developments in carbapenems. Expert Opin. Investig. Drugs (2002) 11(4):529-544.
   PubMed Web of Science ®Google Scholar
• NORDMANN P, POIREL L: Emerging carbapenemases in Gram-positive aerobes. Clin. Microbiol. Infect. (2002) 8(6):321-331.
   PubMed Web of Science ®Google Scholar
• GREENLEE ML, LAUB JB, BALKOVEC JM et al.: Synthesis and SAR of thioester and thiol inhibitors of IMP-1 metallo-β-lactamase. Bioorg. Med. Chem. Lett. (1999) 9(17):2549-2554.
   PubMed Web of Science ®Google Scholar
• PAYNE DJ, BATESON JH, GASSON BC et al.: Inhibition of metallo-β-lactamases by a series of mercaptoacetic acid thiol ester derivatives. Antimicrob. Agents Chemother. (1997) 41(1):135-140.
   PubMed Web of Science ®Google Scholar
• SIEMANN S, CLARKE AJ, VISWANATHA T, DMITRIENKO GI: Thiols as classical and slow-binding inhibitors of IMP-1 and other binuclear metallo-β-lactamases Biochemistry (2003) 42(6):1673-1683.
   Google Scholar
• WALTER MW, HERNANDEZ VM, ADLINGTON RM et al.: Hydroxamate inhibitors of Aeromonas hydrophilia AE036 metallo-β-lactamases. Bioorg. Chem. (1999) 27(1):35-40.
   Web of Science ®Google Scholar
• TONEY JH, HAMMOND GG, FITZGERALD PM et al.: Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-β-lactamase. J. Biol. Chem. (2001) 276:31913-31918.
   PubMed Web of Science ®Google Scholar
• MOLOUGHNEY JG, THOMAS JD, TONEY JH: Novel IMP-1 metallo-β-lactamase inhibitors can reverse meropenem resistance in Escherichia coli expressing IMP-1. FEMS Microbiol. Lett. (2005) 243:65-71.
   PubMedGoogle Scholar
• MOLLARD C, MOALI C, PAPAMICAEL C et al.: Thiomandelic acid, a broad-spectrum inhibitor of zinc β-lactamases. J. Biol. Chem. (2001) 276(48):45015-45023.
   PubMed Web of Science ®Google Scholar
• DAMBLON C, JENSEN M, ABABOU A et al.: The inhibitor thiomandelic acid binds to both metal ions in metallo-β-lactamase and induces positive cooperativity in metal binding. J. Biol. Chem. (2003) 278(31):29240-29251.
   PubMedGoogle Scholar
• TSANG WY, DHANDA A, SCHOFIELD CJ, FRÈRE J-M, GALLENI M, PAGE MI: The inhibition of metallo-β-lactamase by thioxo-cephalosporin derivatives. Bioorg. Med. Chem. Lett. (2004) 14(7):1737-1739.
   PubMedGoogle Scholar
• BADARAU A, LLINÁS A, LAWS AP, DAMBLON C, PAGE MI: Inhibitors of metallo-β-lactamase generated from β-lactam antibiotics. Biochem. (2005) 44(24):8578-8589.
   PubMedGoogle Scholar
• SANDANAYAKA VP, FEIGELSON GB, PRASHAD AS, YANG Y, PETERSEN PJ: Allyl and propargyl substituted penam sulfones as versatile intermediates toward the syntheses of new β-lactamase inhibitors. Bioorg. Med. Chem. Lett. (2001) 11(8):997-1000.
   PubMedGoogle Scholar
• NAGANO R, ADACHI Y, IMAMURA H, YAMADA K, HASHIZUME T, MORISHIMA H: Carbapenem derivatives as potential inhibitors of various β-lactamases, including class B metallo-β-lactamases. Antimicrob. Agents Chemother. (1999) 43(10):2497-2503.
   PubMedGoogle Scholar
• NAGANO R, ADACHI Y, HASHIZUME T, MORISHIMA H: In vitro antibacterial activity and mechanism of action of J-111225, a novel 1β-methylcarbapenem, against transferable IMP-1 metallo-β-lactamase producers. Antimicrob. Chemother. (2000) 45(3):271-276.
   Google Scholar
• CRICHLOW GV, NUKAGA M, DOPPALAPUDI VR, BUYNAK JD, KNOX JR: Inhibition of class C β-lactamases: structure of a reaction intermediate with a cephem sulfone. Biochem. (2001) 40:6233-6239.
   PubMedGoogle Scholar
• JELSCH C, MOUREY L, MASSON JM, SAMAMA JP: Crystal structure of Escherichia coli TEM-1 β-lactamase at 1.8 Å resolution. Proteins (1993) 16(4):364-83.
   PubMed Web of Science ®Google Scholar
• BUSH K, MOBASHERY S: How β-lactamases have driven pharmaceutical drug discovery. From mechanistic knowledge to clinical circumvention. Adv. Exp. Med. Biol. (1998) 456:71-98.
   PubMedGoogle Scholar
• CASELLI E, POWERS RA, BLASCZCAK LC, WU CY, PRATI F, SHOICHET BK: Energetic, structural, and antimicrobial analyses of β-lactam side chain recognition by β-lactamases. Chem. Biol. (2001) 8(1):17-31.
   PubMedGoogle Scholar
• POWERS RA, SHOICHET BK: Structure-based approach for binding site identification on AmpC β-lactamase. J. Med. Chem. (2002) 45:3222-3234.
   PubMed Web of Science ®Google Scholar
• YANG Y, JANOTA K, TAEI K et al.: Mechanism of inhibition of the class A β-lactamases PC1 and TEM-1 by tazobactam. Observation of reaction products by electrospray ionization mass spectrometry. J. Biol. Chem. (2000) 275(35):26674-26682.
   PubMedGoogle Scholar