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Volumn 17, Issue 11, 2012, Pages 12478-12505

Development of new drugs for an old target - The penicillin binding proteins

Author keywords

lactam resistance; Inhibitors; Non lactam; Penicillin binding protein; Substrate analogs; Transition state analogs

Indexed keywords

ANTIINFECTIVE AGENT; BETA LACTAMASE; ENZYME INHIBITOR; PENICILLIN BINDING PROTEIN; PENICILLIN DERIVATIVE;

EID: 84870218839     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules171112478     Document Type: Review
Times cited : (86)

References (106)
  • 2
    • 62449089680 scopus 로고    scopus 로고
    • Microbial drug discovery: 80 years of progress
    • Demain, A.L.; Sanchez, S. Microbial drug discovery: 80 Years of progress. J. Antibiot. 2009, 62, 5-16.
    • (2009) J. Antibiot. , vol.62 , pp. 5-16
    • Demain, A.L.1    Sanchez, S.2
  • 3
    • 84902052420 scopus 로고
    • Resistance of staphylococcus aureus to the action of penicillin
    • Rammelkamp, C.H.; Maxon, T. Resistance of Staphylococcus aureus to the Action of Penicillin. Proc. Soc. Exp. Biol. Med. 1942, 51, 386-389.
    • (1942) Proc. Soc. Exp. Biol. Med. , vol.51 , pp. 386-389
    • Rammelkamp, C.H.1    Maxon, T.2
  • 4
    • 78149466664 scopus 로고    scopus 로고
    • Beta-lactam and glycopeptide antibiotics: First and last line of defense?
    • Jovetic, S.; Zhu, Y.; Marcone, G.L.; Marinelli, F.; Tramper, J. beta-Lactam and glycopeptide antibiotics: First and last line of defense? Trends Biotechnol. 2010, 28, 596-604.
    • (2010) Trends Biotechnol. , vol.28 , pp. 596-604
    • Jovetic, S.1    Zhu, Y.2    Marcone, G.L.3    Marinelli, F.4    Tramper, J.5
  • 5
    • 0030681046 scopus 로고    scopus 로고
    • Methicillin resistance in staphylococci: Molecular and biochemical basis and clinical implications
    • Chambers, H.F. Methicillin resistance in staphylococci: Molecular and biochemical basis and clinical implications. Clin. Microbiol. Rev. 1997, 10, 781-791.
    • (1997) Clin. Microbiol. Rev. , vol.10 , pp. 781-791
    • Chambers, H.F.1
  • 6
    • 74249108028 scopus 로고    scopus 로고
    • Three decades of beta-lactamase inhibitors
    • Drawz, S.M.; Bonomo, R.A. Three decades of beta-lactamase inhibitors. Clin. Microbiol. Rev. 2010, 23, 160-201.
    • (2010) Clin. Microbiol. Rev. , vol.23 , pp. 160-201
    • Drawz, S.M.1    Bonomo, R.A.2
  • 7
    • 65549165914 scopus 로고    scopus 로고
    • What antimicrobial resistance has taught us about horizontal gene transfer
    • Barlow, M. What antimicrobial resistance has taught us about horizontal gene transfer. Methods Mol. Biol. 2009, 532, 397-411.
    • (2009) Methods Mol. Biol. , vol.532 , pp. 397-411
    • Barlow, M.1
  • 8
    • 1942437430 scopus 로고    scopus 로고
    • A PBP2x from a clinical isolate of streptococcus pneumoniae exhibits an alternative mechanism for reduction of susceptibility to beta-lactam antibiotics
    • Pernot, L.; Chesnel, L.; Le Gouellec, A.; Croize, J.; Vernet, T.; Dideberg, O.; Dessen, A. A PBP2x from a clinical isolate of Streptococcus pneumoniae exhibits an alternative mechanism for reduction of susceptibility to beta-lactam antibiotics. J. Biol. Chem. 2004, 279, 16463-16470.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16463-16470
    • Pernot, L.1    Chesnel, L.2    Le Gouellec, A.3    Croize, J.4    Vernet, T.5    Dideberg, O.6    Dessen, A.7
  • 9
    • 0025374274 scopus 로고
    • Insertion of an extra amino acid is the main cause of the low affinity of penicillin-binding protein 2 in penicillin-resistant strains of neisseria gonorrhoeae
    • Brannigan, J.A.; Tirodimos, I.A.; Zhang, Q.Y.; Dowson, C.G.; Spratt, B.G. Insertion of an extra amino acid is the main cause of the low affinity of penicillin-binding protein 2 in penicillin-resistant strains of Neisseria gonorrhoeae. Mol. Microbiol. 1990, 4, 913-919.
    • (1990) Mol. Microbiol. , vol.4 , pp. 913-919
    • Brannigan, J.A.1    Tirodimos, I.A.2    Zhang, Q.Y.3    Dowson, C.G.4    Spratt, B.G.5
  • 10
    • 0035984795 scopus 로고    scopus 로고
    • Diversity of beta-lactam resistance-conferring amino acid substitutions in penicillin-binding protein 3 of haemophilus influenzae
    • Dabernat, H.; Delmas, C.; Seguy, M.; Pelissier, R.; Faucon, G.; Bennamani, S.; Pasquier, C. Diversity of beta-lactam resistance-conferring amino acid substitutions in penicillin-binding protein 3 of Haemophilus influenzae. Antimicrob. Agents Ch. 2002, 46, 2208-2218.
    • (2002) Antimicrob. Agents Ch. , vol.46 , pp. 2208-2218
    • Dabernat, H.1    Delmas, C.2    Seguy, M.3    Pelissier, R.4    Faucon, G.5    Bennamani, S.6    Pasquier, C.7
  • 11
    • 0033031086 scopus 로고    scopus 로고
    • Beta-lactam-resistant streptococcus pneumoniae: Epidemiology and evolutionary mechanism
    • Hakenbeck, R. beta-lactam-resistant Streptococcus pneumoniae: Epidemiology and evolutionary mechanism. Chemotherapy 1999, 45, 83-94.
    • (1999) Chemotherapy , vol.45 , pp. 83-94
    • Hakenbeck, R.1
  • 12
    • 22144437663 scopus 로고    scopus 로고
    • Bacterial resistance to antibiotics: Modified target sites
    • Lambert, P.A. Bacterial resistance to antibiotics: Modified target sites. Adv. Drug Deliv. Rev. 2005, 57, 1471-1485.
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , pp. 1471-1485
    • Lambert, P.A.1
  • 13
    • 62549121211 scopus 로고    scopus 로고
    • Molecular mechanisms disrupting porin expression in ertapenem-resistant klebsiella and enterobacter spp. clinical isolates from the UK
    • Doumith, M.; Ellington, M.J.; Livermore, D.M.; Woodford, N. Molecular mechanisms disrupting porin expression in ertapenem-resistant Klebsiella and Enterobacter spp. clinical isolates from the UK. J. Antimicrob. Chemother. 2009, 63, 659-667.
    • (2009) J. Antimicrob. Chemother. , vol.63 , pp. 659-667
    • Doumith, M.1    Ellington, M.J.2    Livermore, D.M.3    Woodford, N.4
  • 14
    • 0035093095 scopus 로고    scopus 로고
    • Of pseudomonas, porins, pumps and carbapenems
    • Livermore, D.M. Of Pseudomonas, Porins, Pumps and carbapenems. J. Antimicrob. Chemother. 2001, 47, 247-250.
    • (2001) J. Antimicrob. Chemother. , vol.47 , pp. 247-250
    • Livermore, D.M.1
  • 15
    • 69949174478 scopus 로고    scopus 로고
    • Has the era of untreatable infections arrived?
    • Livermore, D.M. Has the era of untreatable infections arrived? J. Antimicrob. Chemother. 2009, 64 (Suppl. 1), i29-i36.
    • (2009) J. Antimicrob. Chemother. , vol.64 , Issue.SUPPL. 1
    • Livermore, D.M.1
  • 16
    • 70349739265 scopus 로고    scopus 로고
    • The clinical consequences of antimicrobial resistance
    • Rice, L.B. The clinical consequences of antimicrobial resistance. Curr. Opin. Microbiol. 2009, 12, 476-481.
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 476-481
    • Rice, L.B.1
  • 17
    • 84862993049 scopus 로고    scopus 로고
    • Sustainable farming: Get pigs off antibiotics
    • Aarestrup, F. Sustainable farming: Get pigs off antibiotics. Nature 2012, 486, 465-466.
    • (2012) Nature , vol.486 , pp. 465-466
    • Aarestrup, F.1
  • 18
    • 77950255824 scopus 로고    scopus 로고
    • The 10 x '20 initiative: Pursuing a global commitment to develop 10 new antibacterial drugs by 2020
    • Infectious Diseases Society of America
    • Infectious Diseases Society of America. The 10 x '20 Initiative: Pursuing a global commitment to develop 10 new antibacterial drugs by 2020. Clin. Infect. Dis. 2010, 50, 1081-1083.
    • (2010) Clin. Infect. Dis. , vol.50 , pp. 1081-1083
  • 20
    • 44949121648 scopus 로고    scopus 로고
    • Predictable and unpredictable evolution of antibiotic resistance
    • Courvalin, P. Predictable and unpredictable evolution of antibiotic resistance. J. Intern. Med. 2008, 264, 4-16.
    • (2008) J. Intern. Med. , vol.264 , pp. 4-16
    • Courvalin, P.1
  • 21
    • 77951060664 scopus 로고    scopus 로고
    • Current challenges in antimicrobial chemotherapy: Focus on beta-lactamase inhibition
    • Bebrone, C.; Lassaux, P.; Vercheval, L.; Sohier, J.S.; Jehaes, A.; Sauvage, E.; Galleni, M. Current challenges in antimicrobial chemotherapy: Focus on beta-lactamase inhibition. Drugs 2010, 70, 651-679.
    • (2010) Drugs , vol.70 , pp. 651-679
    • Bebrone, C.1    Lassaux, P.2    Vercheval, L.3    Sohier, J.S.4    Jehaes, A.5    Sauvage, E.6    Galleni, M.7
  • 22
    • 84870194932 scopus 로고    scopus 로고
    • Beta-lactamase inhibitors: Non-beta-lactams
    • Frére, J.-M., Ed.; Nova Science Publisher, Inc: Hauppauge, NY, USA
    • Pratt, R.F. Beta-lactamase inhibitors: Non-beta-lactams. In Beta-lactamases; Frére, J.-M., Ed.; Nova Science Publisher, Inc: Hauppauge, NY, USA, 2012; pp. 259-292.
    • (2012) Beta-lactamases , pp. 259-292
    • Pratt, R.F.1
  • 23
    • 81155162497 scopus 로고    scopus 로고
    • Diazabicyclooctanes (DBOs): A potent new class of non-beta-lactam beta-lactamase inhibitors
    • Coleman, K. Diazabicyclooctanes (DBOs): A potent new class of non-beta-lactam beta-lactamase inhibitors. Curr. Opin. Microbiol. 2011, 14, 550-555.
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 550-555
    • Coleman, K.1
  • 24
    • 67749143907 scopus 로고    scopus 로고
    • In vitro activity of NXL104 in combination with beta-lactams against klebsiella pneumoniae isolates producing KPC carbapenemases
    • Endimiani, A.; Choudhary, Y.; Bonomo, R.A. In vitro activity of NXL104 in combination with beta-lactams against Klebsiella pneumoniae isolates producing KPC carbapenemases. Antimicrob. Agents Ch. 2009, 53, 3599-3601.
    • (2009) Antimicrob. Agents Ch. , vol.53 , pp. 3599-3601
    • Endimiani, A.1    Choudhary, Y.2    Bonomo, R.A.3
  • 25
    • 67650718178 scopus 로고    scopus 로고
    • In vitro activity of the {beta}-lactamase inhibitor NXL104 against KPC-2 carbapenemase and enterobacteriaceae expressing KPC carbapenemases
    • Stachyra, T.; Levasseur, P.; Pechereau, M.C.; Girard, A.M.; Claudon, M.; Miossec, C.; Black, M.T. In vitro activity of the {beta}-lactamase inhibitor NXL104 against KPC-2 carbapenemase and Enterobacteriaceae expressing KPC carbapenemases. J. Antimicrob. Chemother. 2009, 64, 326-329.
    • (2009) J. Antimicrob. Chemother. , vol.64 , pp. 326-329
    • Stachyra, T.1    Levasseur, P.2    Pechereau, M.C.3    Girard, A.M.4    Claudon, M.5    Miossec, C.6    Black, M.T.7
  • 27
    • 80053095983 scopus 로고    scopus 로고
    • Resistance drives antibacterial drug development
    • Theuretzbacher, U. Resistance drives antibacterial drug development. Curr. Opin. Pharmacol. 2011, 11, 433-438.
    • (2011) Curr. Opin. Pharmacol. , vol.11 , pp. 433-438
    • Theuretzbacher, U.1
  • 28
    • 73849149415 scopus 로고    scopus 로고
    • Hydrolysis and inhibition profiles of beta-lactamases from molecular classes A to D with doripenem, imipenem, and meropenem
    • Queenan, A.M.; Shang, W.; Flamm, R.; Bush, K. Hydrolysis and inhibition profiles of beta-lactamases from molecular classes A to D with doripenem, imipenem, and meropenem. Antimicrob. Agents Ch. 2010, 54, 565-569.
    • (2010) Antimicrob. Agents Ch. , vol.54 , pp. 565-569
    • Queenan, A.M.1    Shang, W.2    Flamm, R.3    Bush, K.4
  • 29
    • 66249125680 scopus 로고    scopus 로고
    • Ceftobiprole: First cephalosporin with activity against methicillin-resistant staphylococcus aureus
    • Vidaillac, C.; Rybak, M.J. Ceftobiprole: First cephalosporin with activity against methicillin-resistant Staphylococcus aureus. Pharmacotherapy 2009, 29, 511-525.
    • (2009) Pharmacotherapy , vol.29 , pp. 511-525
    • Vidaillac, C.1    Rybak, M.J.2
  • 30
    • 79954581843 scopus 로고    scopus 로고
    • Ceftaroline fosamil: A new broad-spectrum cephalosporin
    • Laudano, J.B. Ceftaroline fosamil: A new broad-spectrum cephalosporin. J. Antimicrob. Chemoth. 2011, 66 (Suppl. 3), iii11-iii18.
    • (2011) J. Antimicrob. Chemoth. , vol.66 , Issue.SUPPL. 3
    • Laudano, J.B.1
  • 31
    • 67049086953 scopus 로고    scopus 로고
    • In vitro activity of ceftaroline alone and in combination against clinical isolates of resistant gram-negative pathogens, including beta-lactamase-producing enterobacteriaceae and pseudomonas aeruginosa
    • Vidaillac, C.; Leonard, S.N.; Sader, H.S.; Jones, R.N.; Rybak, M.J. In vitro activity of ceftaroline alone and in combination against clinical isolates of resistant gram-negative pathogens, including beta-lactamase-producing Enterobacteriaceae and Pseudomonas aeruginosa. Antimicrob. Agents Ch. 2009, 53, 2360-2366.
    • (2009) Antimicrob. Agents Ch. , vol.53 , pp. 2360-2366
    • Vidaillac, C.1    Leonard, S.N.2    Sader, H.S.3    Jones, R.N.4    Rybak, M.J.5
  • 32
    • 78149464483 scopus 로고    scopus 로고
    • Cyclodimerization by ring-closing metathesis: Synthesis, computational, and biological evaluation of novel bis-azetidinyl-macrocycles
    • Sliwa, A.; Dive, G.; Habib Jiwan, J.-L.; Marchand-Brynaert, J. Cyclodimerization by ring-closing metathesis: Synthesis, Computational, And biological evaluation of novel bis-azetidinyl-macrocycles. Tetrahedron 2010, 66, 9519-9527.
    • (2010) Tetrahedron , vol.66 , pp. 9519-9527
    • Sliwa, A.1    Dive, G.2    Habib Jiwan, J.-L.3    Marchand-Brynaert, J.4
  • 33
    • 84857703117 scopus 로고    scopus 로고
    • Unprecedented inhibition of resistant penicillin binding proteins by bis-2-oxoazetidinyl macrocycles
    • Sliwa, A.; Dive, G.; Zervosen, A.; Verlaine, O.; Sauvage, E.; Marchand-Brynaert, J. Unprecedented inhibition of resistant penicillin binding proteins by bis-2-oxoazetidinyl macrocycles. Med. Chem. Commun. 2012, 3, 344-351.
    • (2012) Med. Chem. Commun. , vol.3 , pp. 344-351
    • Sliwa, A.1    Dive, G.2    Zervosen, A.3    Verlaine, O.4    Sauvage, E.5    Marchand-Brynaert, J.6
  • 34
    • 63849228551 scopus 로고    scopus 로고
    • Novel large-ring 1,3-bridged 2-azetidinones as potential inhibitors of penicillin-binding proteins
    • Urbach, A.; Dive, G.; Marchand-Brynaert, J. Novel Large-Ring 1,3-Bridged 2-Azetidinones as Potential Inhibitors of Penicillin-Binding Proteins. Eur. J. Org. Chem. 2009, 2009, 1757-1770.
    • (2009) Eur. J. Org. Chem. , vol.2009 , pp. 1757-1770
    • Urbach, A.1    Dive, G.2    Marchand-Brynaert, J.3
  • 35
    • 62549090567 scopus 로고    scopus 로고
    • Large ring 1,3-bridged 2-azetidinones: Experimental and theoretical studies
    • Urbach, A.; Dive, G.; Tinant, B.; Duval, V.; Marchand-Brynaert, J. Large ring 1,3-bridged 2-azetidinones: Experimental and theoretical studies. Eur. J. Med. Chem. 2009, 44, 2071-2080.
    • (2009) Eur. J. Med. Chem. , vol.44 , pp. 2071-2080
    • Urbach, A.1    Dive, G.2    Tinant, B.3    Duval, V.4    Marchand-Brynaert, J.5
  • 36
    • 0036829003 scopus 로고    scopus 로고
    • Structural basis for the beta lactam resistance of PBP2a from methicillin-resistant staphylococcus aureus
    • Lim, D.; Strynadka, N.C. Structural basis for the beta lactam resistance of PBP2a from methicillin-resistant Staphylococcus aureus. Nat. Struct. Biol. 2002, 9, 870-876.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 870-876
    • Lim, D.1    Strynadka, N.C.2
  • 37
    • 0035977042 scopus 로고    scopus 로고
    • Crystal structure of PBP2x from a highly penicillin-resistant streptococcus pneumoniae clinical isolate: A mosaic framework containing 83 mutations
    • Dessen, A.; Mouz, N.; Gordon, E.; Hopkins, J.; Dideberg, O. Crystal structure of PBP2x from a highly penicillin-resistant Streptococcus pneumoniae clinical isolate: A mosaic framework containing 83 mutations. J. Biol. Chem. 2001, 276, 45106-45112.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45106-45112
    • Dessen, A.1    Mouz, N.2    Gordon, E.3    Hopkins, J.4    Dideberg, O.5
  • 38
    • 0036628607 scopus 로고    scopus 로고
    • The 2.4 - A crystal structure of the penicillin-resistant penicillin-binding protein PBP5fm from enterococcus faecium in complex with benzylpenicillin
    • Sauvage, E.; Kerff, F.; Fonze, E.; Herman, R.; Schoot, B.; Marquette, J.P.; Taburet, Y.; Prevost, D.; Dumas, J.; Leonard, G.; et al. The 2.4-A crystal structure of the penicillin-resistant penicillin-binding protein PBP5fm from Enterococcus faecium in complex with benzylpenicillin. Cell. Mol. Life Sci. 2002, 59, 1223-1232.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1223-1232
    • Sauvage, E.1    Kerff, F.2    Fonze, E.3    Herman, R.4    Schoot, B.5    Marquette, J.P.6    Taburet, Y.7    Prevost, D.8    Dumas, J.9    Leonard, G.10
  • 39
    • 26944445052 scopus 로고    scopus 로고
    • Inactivators in competition: How to deal with them⋯ and not!
    • Frere, J.M.; Marchot, P. Inactivators in competition: How to deal with them⋯ and not! Biochem. Pharmacol. 2005, 70, 1417-1423.
    • (2005) Biochem. Pharmacol. , vol.70 , pp. 1417-1423
    • Frere, J.M.1    Marchot, P.2
  • 40
    • 0001930562 scopus 로고
    • Mode of action: Interaction with penicillin binding proteins
    • Page, M., Ed.; Chapman and Hall: Glasgow, Scotland
    • Frère, J.-M.; Nguyen-Disteche, M.; Coyette, J.; Joris, B. Mode of action: Interaction with penicillin binding proteins. In The Chemistry of beta-lactams; Page, M., Ed.; Chapman and Hall: Glasgow, Scotland, 1992; pp. 148-195.
    • (1992) The Chemistry of Beta-lactams , pp. 148-195
    • Frère, J.-M.1    Nguyen-Disteche, M.2    Coyette, J.3    Joris, B.4
  • 41
    • 0017087726 scopus 로고
    • Mode of interaction between beta-lactam antibiotics and the exocellular DD-carboxypeptidase - Transpeptidase from streptomyces R39
    • Fuad, N.; Frere, J.M.; Ghuysen, J.M.; Duez, C.; Iwatsubo, M. Mode of interaction between beta-lactam antibiotics and the exocellular DD-carboxypeptidase - transpeptidase from Streptomyces R39. Biochem. J. 1976, 155, 623-629.
    • (1976) Biochem. J. , vol.155 , pp. 623-629
    • Fuad, N.1    Frere, J.M.2    Ghuysen, J.M.3    Duez, C.4    Iwatsubo, M.5
  • 42
    • 0027198156 scopus 로고
    • Penicillin-binding protein 2x of streptococcus pneumoniae: Enzymic activities and interactions with beta-lactams
    • Jamin, M.; Damblon, C.; Millier, S.; Hakenbeck, R.; Frere, J.M. Penicillin-binding protein 2x of Streptococcus pneumoniae: Enzymic activities and interactions with beta-lactams. Biochem. J. 1993, 292, 735-741.
    • (1993) Biochem. J. , vol.292 , pp. 735-741
    • Jamin, M.1    Damblon, C.2    Millier, S.3    Hakenbeck, R.4    Frere, J.M.5
  • 43
    • 0027517627 scopus 로고
    • Penicillin binding protein 2x as a major contributor to intrinsic beta-lactam resistance of streptococcus pneumoniae
    • Jamin, M.; Hakenbeck, R.; Frere, J.M. Penicillin binding protein 2x as a major contributor to intrinsic beta-lactam resistance of Streptococcus pneumoniae. FEBS Lett. 1993, 331, 101-104.
    • (1993) FEBS Lett. , vol.331 , pp. 101-104
    • Jamin, M.1    Hakenbeck, R.2    Frere, J.M.3
  • 46
    • 0032908481 scopus 로고    scopus 로고
    • BOCILLIN FL, A sensitive and commercially available reagent for detection of penicillin-binding proteins
    • Zhao, G.; Meier, T.I.; Kahl, S.D.; Gee, K.R.; Blaszczak, L.C. BOCILLIN FL, A sensitive and commercially available reagent for detection of penicillin-binding proteins. Antimicrob. Agents Ch. 1999, 43, 1124-1128.
    • (1999) Antimicrob. Agents Ch. , vol.43 , pp. 1124-1128
    • Zhao, G.1    Meier, T.I.2    Kahl, S.D.3    Gee, K.R.4    Blaszczak, L.C.5
  • 47
    • 0028231058 scopus 로고
    • Use of biotinylated beta-lactams and chemiluminescence for study and purification of penicillin-binding proteins in bacteria
    • Dargis, M.; Malouin, F. Use of biotinylated beta-lactams and chemiluminescence for study and purification of penicillin-binding proteins in bacteria. Antimicrob. Agents Ch. 1994, 38, 973-980.
    • (1994) Antimicrob. Agents Ch. , vol.38 , pp. 973-980
    • Dargis, M.1    Malouin, F.2
  • 48
    • 0031974583 scopus 로고    scopus 로고
    • Soluble penicillin-binding protein 2a: Beta-lactam binding and inhibition by non-beta-lactams using a 96-well format
    • Toney, J.H.; Hammond, G.G.; Leiting, B.; Pryor, K.D.; Wu, J.K.; Cuca, G.C.; Pompliano, D.L. Soluble penicillin-binding protein 2a: Beta-lactam binding and inhibition by non-beta-lactams using a 96-well format. Anal. Biochem. 1998, 255, 113-119.
    • (1998) Anal. Biochem. , vol.255 , pp. 113-119
    • Toney, J.H.1    Hammond, G.G.2    Leiting, B.3    Pryor, K.D.4    Wu, J.K.5    Cuca, G.C.6    Pompliano, D.L.7
  • 49
    • 70449627031 scopus 로고    scopus 로고
    • A microtiter plate-based beta-lactam binding assay for inhibitors of high-molecular-mass penicillin-binding proteins
    • Stefanova, M.; Bobba, S.; Gutheil, W.G. A microtiter plate-based beta-lactam binding assay for inhibitors of high-molecular-mass penicillin-binding proteins. Anal. Biochem. 2010, 396, 164-166.
    • (2010) Anal. Biochem. , vol.396 , pp. 164-166
    • Stefanova, M.1    Bobba, S.2    Gutheil, W.G.3
  • 50
    • 79956298875 scopus 로고    scopus 로고
    • Microtiter plate-based assay for inhibitors of penicillin-binding protein 2a from methicillin-resistant staphylococcus aureus
    • Bobba, S.; Ponnaluri, V.K.; Mukherji, M.; Gutheil, W.G. Microtiter plate-based assay for inhibitors of penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Ch. 2011, 55, 2783-2787.
    • (2011) Antimicrob. Agents Ch. , vol.55 , pp. 2783-2787
    • Bobba, S.1    Ponnaluri, V.K.2    Mukherji, M.3    Gutheil, W.G.4
  • 51
    • 80054956493 scopus 로고    scopus 로고
    • A boronic-acid-based probe for fluorescence polarization assays with penicillin binding proteins and beta-lactamases
    • Inglis, S.R.; Strieker, M.; Rydzik, A.M.; Dessen, A.; Schofield, C.J. A boronic-acid-based probe for fluorescence polarization assays with penicillin binding proteins and beta-lactamases. Anal. Biochem. 2012, 420, 41-47.
    • (2012) Anal. Biochem. , vol.420 , pp. 41-47
    • Inglis, S.R.1    Strieker, M.2    Rydzik, A.M.3    Dessen, A.4    Schofield, C.J.5
  • 53
  • 54
    • 1442324697 scopus 로고    scopus 로고
    • Interactions between penicillin-binding proteins (PBPs) and two novel classes of PBP inhibitors, arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-ones
    • Zervosen, A.; Lu, W.P.; Chen, Z.; White, R.E.; Demuth, T.P., Jr.; Frere, J.M. Interactions between penicillin-binding proteins (PBPs) and two novel classes of PBP inhibitors, Arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-ones. Antimicrob. Agents Ch. 2004, 48, 961-969.
    • (2004) Antimicrob. Agents Ch. , vol.48 , pp. 961-969
    • Zervosen, A.1    Lu, W.P.2    Chen, Z.3    White, R.E.4    Demuth Jr., T.P.5    Frere, J.M.6
  • 55
    • 0024996497 scopus 로고
    • Chromogenic depsipeptide substrates for beta-lactamases and penicillin-sensitive DD-peptidases
    • Adam, M.; Damblon, C.; Plaitin, B.; Christiaens, L.; Frere, J.M. Chromogenic Depsipeptide Substrates for Beta-Lactamases and Penicillin-Sensitive DD-Peptidases. Biochem. J. 1990, 270, 525-529.
    • (1990) Biochem. J. , vol.270 , pp. 525-529
    • Adam, M.1    Damblon, C.2    Plaitin, B.3    Christiaens, L.4    Frere, J.M.5
  • 59
    • 0043195272 scopus 로고    scopus 로고
    • Novel fluorogenic substrates for imaging beta-lactamase gene expression
    • Gao, W.; Xing, B.; Tsien, R.Y.; Rao, J. Novel fluorogenic substrates for imaging beta-lactamase gene expression. J. Am. Chem. Soc. 2003, 125, 11146-11147.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11146-11147
    • Gao, W.1    Xing, B.2    Tsien, R.Y.3    Rao, J.4
  • 60
    • 16244375539 scopus 로고    scopus 로고
    • Cell-permeable near-infrared fluorogenic substrates for imaging beta-lactamase activity
    • Xing, B.; Khanamiryan, A.; Rao, J. Cell-permeable near-infrared fluorogenic substrates for imaging beta-lactamase activity. J. Am. Chem. Soc. 2005, 127, 4158-4159.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 4158-4159
    • Xing, B.1    Khanamiryan, A.2    Rao, J.3
  • 62
    • 33751321865 scopus 로고    scopus 로고
    • A detergent-based assay for the detection of promiscuous inhibitors
    • Feng, B.Y.; Shoichet, B.K. A detergent-based assay for the detection of promiscuous inhibitors. Nat. Protoc. 2006, 1, 550-553.
    • (2006) Nat. Protoc. , vol.1 , pp. 550-553
    • Feng, B.Y.1    Shoichet, B.K.2
  • 63
    • 33745188660 scopus 로고    scopus 로고
    • Screening in a spirit haunted world
    • Shoichet, B.K. Screening in a spirit haunted world. Drug Discov. Today 2006, 11, 607-615.
    • (2006) Drug Discov. Today , vol.11 , pp. 607-615
    • Shoichet, B.K.1
  • 64
    • 0017324044 scopus 로고
    • Serine proteases: Structure and mechanism of catalysis
    • Kraut, J. Serine proteases: Structure and mechanism of catalysis. Annu. Rev. Biochem. 1977, 46, 331-358.
    • (1977) Annu. Rev. Biochem. , vol.46 , pp. 331-358
    • Kraut, J.1
  • 65
    • 78649658087 scopus 로고    scopus 로고
    • Bridging cell wall biosynthesis and bacterial morphogenesis
    • Mattei, P.J.; Neves, D.; Dessen, A. Bridging cell wall biosynthesis and bacterial morphogenesis. Curr. Opin. Struct. Biol. 2010, 20, 749-755.
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 749-755
    • Mattei, P.J.1    Neves, D.2    Dessen, A.3
  • 66
    • 39149088656 scopus 로고    scopus 로고
    • The penicillin-binding proteins: Structure and role in peptidoglycan biosynthesis
    • Sauvage, E.; Kerff, F.; Terrak, M.; Ayala, J.A.; Charlier, P. The penicillin-binding proteins: Structure and role in peptidoglycan biosynthesis. FEMS Microbiol. Rev. 2008, 32, 234-258.
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 234-258
    • Sauvage, E.1    Kerff, F.2    Terrak, M.3    Ayala, J.A.4    Charlier, P.5
  • 67
    • 0037457830 scopus 로고    scopus 로고
    • Potential transition state analogue inhibitors for the penicillin-binding proteins
    • Pechenov, A.; Stefanova, M.E.; Nicholas, R.A.; Peddi, S.; Gutheil, W.G. Potential transition state analogue inhibitors for the penicillin-binding proteins. Biochemistry 2003, 42, 579-588.
    • (2003) Biochemistry , vol.42 , pp. 579-588
    • Pechenov, A.1    Stefanova, M.E.2    Nicholas, R.A.3    Peddi, S.4    Gutheil, W.G.5
  • 68
    • 20444369942 scopus 로고    scopus 로고
    • Crystal structure of escherichia coli penicillin-binding protein 5 bound to a tripeptide boronic acid inhibitor: A role for ser-110 in deacylation
    • Nicola, G.; Peddi, S.; Stefanova, M.; Nicholas, R.A.; Gutheil, W.G.; Davies, C. Crystal structure of Escherichia coli penicillin-binding protein 5 bound to a tripeptide boronic acid inhibitor: A role for Ser-110 in deacylation. Biochemistry 2005, 44, 8207-8217.
    • (2005) Biochemistry , vol.44 , pp. 8207-8217
    • Nicola, G.1    Peddi, S.2    Stefanova, M.3    Nicholas, R.A.4    Gutheil, W.G.5    Davies, C.6
  • 69
    • 77955041712 scopus 로고    scopus 로고
    • Crystal structure of a complex between the actinomadura R39 DD-peptidase and a peptidoglycan-mimetic boronate inhibitor: Interpretation of a transition state analogue in terms of catalytic mechanism
    • Dzhekieva, L.; Rocaboy, M.; Kerff, F.; Charlier, P.; Sauvage, E.; Pratt, R.F. Crystal structure of a complex between the Actinomadura R39 DD-peptidase and a peptidoglycan-mimetic boronate inhibitor: Interpretation of a transition state analogue in terms of catalytic mechanism. Biochemistry 2010, 49, 6411-6419.
    • (2010) Biochemistry , vol.49 , pp. 6411-6419
    • Dzhekieva, L.1    Rocaboy, M.2    Kerff, F.3    Charlier, P.4    Sauvage, E.5    Pratt, R.F.6
  • 72
    • 79952191452 scopus 로고    scopus 로고
    • Boronic acids in medicinal chemistry: Anticancer, antibacterial and antiviral applications
    • Trippier, P.C.; McGuigan, C. Boronic acids in medicinal chemistry: Anticancer, Antibacterial and antiviral applications. Med. Chem. Commun. 2010, 1, 183-198.
    • (2010) Med. Chem. Commun. , vol.1 , pp. 183-198
    • Trippier, P.C.1    McGuigan, C.2
  • 73
    • 0030847769 scopus 로고    scopus 로고
    • Structure-activity studies of the inhibition of serine beta-lactamases by phosphonate monoesters
    • Li, N.; Rahil, J.; Wright, M.E.; Pratt, R.F. Structure-activity studies of the inhibition of serine beta-lactamases by phosphonate monoesters. Bioorg. Med. Chem. 1997, 5, 1783-1788.
    • (1997) Bioorg. Med. Chem. , vol.5 , pp. 1783-1788
    • Li, N.1    Rahil, J.2    Wright, M.E.3    Pratt, R.F.4
  • 74
    • 0024370749 scopus 로고
    • Inhibition of a class C beta-lactamase by a specific phosphonate monoester
    • Pratt, R.F. Inhibition of a class C beta-lactamase by a specific phosphonate monoester. Science 1989, 246, 917-919.
    • (1989) Science , vol.246 , pp. 917-919
    • Pratt, R.F.1
  • 75
    • 0025849757 scopus 로고
    • Phosphonate monoester inhibitors of class A beta-lactamases
    • Rahil, J.; Pratt, R.F. Phosphonate monoester inhibitors of class A beta-lactamases. Biochem. J. 1991, 275, 793-795.
    • (1991) Biochem. J. , vol.275 , pp. 793-795
    • Rahil, J.1    Pratt, R.F.2
  • 76
    • 0027451306 scopus 로고
    • Structure of a phosphonate-inhibited beta-lactamase: An analog of the tetrahedral transition state/intermediate of beta-lactam hydrolysis
    • Chen, C.C.; Rahil, J.; Pratt, R.F.; Herzberg, O. Structure of a phosphonate-inhibited beta-lactamase: An analog of the tetrahedral transition state/intermediate of beta-lactam hydrolysis. J. Mol. Biol. 1993, 234, 165-178.
    • (1993) J. Mol. Biol. , vol.234 , pp. 165-178
    • Chen, C.C.1    Rahil, J.2    Pratt, R.F.3    Herzberg, O.4
  • 77
    • 0028224698 scopus 로고
    • Crystallographic structure of a phosphonate derivative of the enterobacter cloacae P99 cephalosporinase: Mechanistic interpretation of a beta-lactamase transition-state analog
    • Lobkovsky, E.; Billings, E.M.; Moews, P.C.; Rahil, J.; Pratt, R.F.; Knox, J.R. Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: Mechanistic interpretation of a beta-lactamase transition-state analog. Biochemistry 1994, 33, 6762-6772.
    • (1994) Biochemistry , vol.33 , pp. 6762-6772
    • Lobkovsky, E.1    Billings, E.M.2    Moews, P.C.3    Rahil, J.4    Pratt, R.F.5    Knox, J.R.6
  • 78
    • 0032562183 scopus 로고    scopus 로고
    • Crystal structure of an acylation transition-state analog of the TEM-1 beta-lactamase: Mechanistic implications for class A beta-lactamases
    • Maveyraud, L.; Pratt, R.F.; Samama, J.P. Crystal structure of an acylation transition-state analog of the TEM-1 beta-lactamase: Mechanistic implications for class A beta-lactamases. Biochemistry 1998, 37, 2622-2628.
    • (1998) Biochemistry , vol.37 , pp. 2622-2628
    • Maveyraud, L.1    Pratt, R.F.2    Samama, J.P.3
  • 79
    • 0035574578 scopus 로고    scopus 로고
    • Inverse acyl phosph(on)ates: Substrates or inhibitors of beta-lactam-recognizing enzymes?
    • Morrison, M.J.; Li, N.; Pratt, R.F. Inverse acyl phosph(on)ates: Substrates or inhibitors of beta-lactam-recognizing enzymes? Bioorg. Chem. 2001, 29, 271-281.
    • (2001) Bioorg. Chem. , vol.29 , pp. 271-281
    • Morrison, M.J.1    Li, N.2    Pratt, R.F.3
  • 80
    • 0032495765 scopus 로고    scopus 로고
    • Salicyloyl cyclic phosphate, a "Penicillin-like" inhibitor of β-lactamases
    • Pratt, R.F.; Hammar, N.J. Salicyloyl Cyclic Phosphate, a "Penicillin-Like" Inhibitor of β-Lactamases. J. Am. Chem. Soc. 1998, 120, 3004-3006.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3004-3006
    • Pratt, R.F.1    Hammar, N.J.2
  • 81
    • 2642588180 scopus 로고    scopus 로고
    • Toward better antibiotics: Crystallographic studies of a novel class of DD-peptidase/β-lactamase inhibitors
    • Silvaggi, N.R.; Kaur, K.; Adediran, S.A.; Pratt, R.F.; Kelly, J.A. Toward Better Antibiotics: Crystallographic Studies of a Novel Class of DD-Peptidase/β-Lactamase Inhibitors. Biochemistry 2004, 43, 7046-7053.
    • (2004) Biochemistry , vol.43 , pp. 7046-7053
    • Silvaggi, N.R.1    Kaur, K.2    Adediran, S.A.3    Pratt, R.F.4    Kelly, J.A.5
  • 82
    • 33745457342 scopus 로고    scopus 로고
    • Synthesis and evaluation of ketophosph(on)ates as beta-lactamase inhibitors
    • Perumal, S.K.; Pratt, R.F. Synthesis and evaluation of ketophosph(on)ates as beta-lactamase inhibitors. J. Org. Chem. 2006, 71, 4778-4785.
    • (2006) J. Org. Chem. , vol.71 , pp. 4778-4785
    • Perumal, S.K.1    Pratt, R.F.2
  • 83
    • 0037013989 scopus 로고    scopus 로고
    • PH, inhibitor, and substrate specificity studies on escherichia coli penicillin-binding protein 5
    • Stefanova, M.E.; Davies, C; Nicholas, R.A.; Gutheil, W.G. pH, Inhibitor, And substrate specificity studies on Escherichia coli penicillin-binding protein 5. Biochim. Biophys. Acta 2002, 1597, 292-300.
    • (2002) Biochim. Biophys. Acta , vol.1597 , pp. 292-300
    • Stefanova, M.E.1    Davies, C.2    Nicholas, R.A.3    Gutheil, W.G.4
  • 85
    • 0009588086 scopus 로고
    • Non-beta-lactam mimics of beta-lactam antibiotics
    • Page, M.I., Ed.; Chapman and Hall: London, UK
    • Jungheim, L.N.; Ternansky, R.J. Non-beta-lactam mimics of beta-lactam antibiotics. In The Chemistry of Beta-Lactams; Page, M.I., Ed.; Chapman and Hall: London, UK, 1992; pp. 306-324.
    • (1992) The Chemistry of Beta-Lactams; , pp. 306-324
    • Jungheim, L.N.1    Ternansky, R.J.2
  • 86
    • 0034597574 scopus 로고    scopus 로고
    • Hydrolytic stability versus ring size in lactams: Implications for the development of lactam antibiotics and other serine protease inhibitors
    • Imming, P.; Klar, B.; Dix, D. Hydrolytic stability versus ring size in lactams: Implications for the development of lactam antibiotics and other serine protease inhibitors. J. Med. Chem. 2000, 43, 4328-4331.
    • (2000) J. Med. Chem. , vol.43 , pp. 4328-4331
    • Imming, P.1    Klar, B.2    Dix, D.3
  • 87
    • 0026031407 scopus 로고
    • Gamma-lactam analogues of beta-lactam antibiotics
    • Baldwin, J.E.; Lynch, G.P.; Pitlik, J. Gamma-lactam analogues of beta-lactam antibiotics. J. Antibiot. 1991, 44, 1-24.
    • (1991) J. Antibiot. , vol.44 , pp. 1-24
    • Baldwin, J.E.1    Lynch, G.P.2    Pitlik, J.3
  • 88
    • 0000130893 scopus 로고
    • Non-beta-lactam analogs of penicillins and cephalosporins
    • Ohno, M., Lukais, G, Eds.; Springer-Verlag: Berlin, Germany
    • Marchand-Brynaert, J.; Ghosez, L. Non-beta-lactam analogs of penicillins and cephalosporins. In Recent Progress in the Chemical Synthesis of Antibiotics; Ohno, M., Lukais, G, Eds.; Springer-Verlag: Berlin, Germany, 1990; pp. 729-794.
    • (1990) Recent Progress in the Chemical Synthesis of Antibiotics; , pp. 729-794
    • Marchand-Brynaert, J.1    Ghosez, L.2
  • 94
    • 0023022549 scopus 로고
    • Structure of lactivicin, an antibiotic having a new nucleus and similar biological activities to β-lactam antibiotics
    • Harada, S.; Tsubotani, S.; Hida, T.; Ono, H.; Okazaki, H. Structure of lactivicin, An antibiotic having a new nucleus and similar biological activities to β-lactam antibiotics. Tetrahedron Lett. 1986, 27, 6229-6232.
    • (1986) Tetrahedron Lett. , vol.27 , pp. 6229-6232
    • Harada, S.1    Tsubotani, S.2    Hida, T.3    Ono, H.4    Okazaki, H.5
  • 95
    • 0024491605 scopus 로고
    • Lactivicin, A naturally occurring non-beta-lactam antibiotic having beta-lactam-like action: Biological activities and mode of action
    • Nozaki, Y.; Katayama, N.; Harada, S.; Ono, H.; Okazaki, H. Lactivicin, A naturally occurring non-beta-lactam antibiotic having beta-lactam-like action: Biological activities and mode of action. J. Antibiot. 1989, 42, 84-93.
    • (1989) J. Antibiot. , vol.42 , pp. 84-93
    • Nozaki, Y.1    Katayama, N.2    Harada, S.3    Ono, H.4    Okazaki, H.5
  • 99
    • 0025232007 scopus 로고
    • Synthesis and antibacterial activity of lactivicin derivatives
    • Tamura, N.; Matsushita, Y.; Kawano, Y.; Yoshioka, K. Synthesis and antibacterial activity of lactivicin derivatives. Chem. Pharm. Bull. 1990, 38, 116-122.
    • (1990) Chem. Pharm. Bull. , vol.38 , pp. 116-122
    • Tamura, N.1    Matsushita, Y.2    Kawano, Y.3    Yoshioka, K.4
  • 102
    • 70349816746 scopus 로고    scopus 로고
    • Discovery of new inhibitors of resistant streptococcus pneumoniae penicillin binding protein (PBP) 2x by structure-based virtual screening
    • Miguet, L.; Zervosen, A.; Gerards, T.; Pasha, F.A.; Luxen, A.; Disteche-Nguyen, M.; Thomas, A. Discovery of new inhibitors of resistant Streptococcus pneumoniae penicillin binding protein (PBP) 2x by structure-based virtual screening. J. Med. Chem. 2009, 52, 5926-5936.
    • (2009) J. Med. Chem. , vol.52 , pp. 5926-5936
    • Miguet, L.1    Zervosen, A.2    Gerards, T.3    Pasha, F.A.4    Luxen, A.5    Disteche-Nguyen, M.6    Thomas, A.7
  • 104
    • 84862860831 scopus 로고    scopus 로고
    • Exploration of the chemical space of novel naphthalene-sulfonamide and anthranilic acid-based inhibitors of penicillin-binding proteins
    • Sosic, I.; Turk, S.; Sinreith, M.; Trost, N.; Verlaine, O.; Amoroso, A.; Zervosen, A.; Luxen, A.; Joris, B.; Gobec, S. Exploration of the chemical space of novel naphthalene-sulfonamide and anthranilic acid-based inhibitors of penicillin-binding proteins. Acta Chim. Slov. 2012, 59, 380-388.
    • (2012) Acta Chim. Slov. , vol.59 , pp. 380-388
    • Sosic, I.1    Turk, S.2    Sinreith, M.3    Trost, N.4    Verlaine, O.5    Amoroso, A.6    Zervosen, A.7    Luxen, A.8    Joris, B.9    Gobec, S.10
  • 106
    • 84863815623 scopus 로고    scopus 로고
    • 4-quinolones as noncovalent inhibitors of high molecular mass penicillin-binding proteins
    • Shilabin, A.G.; Dzhekieva, L.; Misra, P.; Jayaram, B.; Pratt, R.F. 4-Quinolones as Noncovalent Inhibitors of High Molecular Mass Penicillin-Binding Proteins. ACS Med. Chem. Lett. 2012, 3, 592-595.
    • (2012) ACS Med. Chem. Lett. , vol.3 , pp. 592-595
    • Shilabin, A.G.1    Dzhekieva, L.2    Misra, P.3    Jayaram, B.4    Pratt, R.F.5


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