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Volumn 19, Issue 13, 2012, Pages 2038-2050

UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) inhibitors: A new class of antibacterial agents

Author keywords

Biosynthesis; FtsH; Gram negative bacteria; Lipid A; LpxC; LpxC Inhibitors; MDR; Structure

Indexed keywords

ANTIINFECTIVE AGENT; HYDROXAMIC ACID DERIVATIVE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE; URP 3 O (3 HYDROXYMYRISTOYL) N ACETYLGLUCOSAMINE DEACETYLASE;

EID: 84860535850     PISSN: 09298673     EISSN: 1875533X     Source Type: Journal    
DOI: 10.2174/092986712800167374     Document Type: Article
Times cited : (33)

References (64)
  • 1
    • 22144459368 scopus 로고    scopus 로고
    • Anticbiotic resistence - The problem intensifies
    • Levy, S. B. Anticbiotic resistence-the problem intensifies. Adv. Drug Deliv. Riv., 2005, 57(10), 1446-1450.
    • (2005) Adv. Drug Deliv. Riv. , vol.57 , Issue.10 , pp. 1446-1450
    • Levy, S.B.1
  • 2
    • 10944272743 scopus 로고    scopus 로고
    • Antibacterial resistance worldwide: Causes, challenges and responses
    • Levy, S. B.; Marshall, B. Antibacterial resistance worldwide: causes, challenges and responses. Nat. Med., 2004, 10(12), 122-129.
    • (2004) Nat. Med. , vol.10 , Issue.12 , pp. 122-129
    • Levy, S.B.1    Marshall, B.2
  • 3
    • 24344467083 scopus 로고    scopus 로고
    • Multi-resistant gram-negative organisms in Maryland: A statewide survey of resistant Acinetobacter baumannii
    • Wright M. O. Multi-resistant gram-negative organisms in Maryland: a statewide survey of resistant Acinetobacter baumannii. Am. J. Infect Control, 2005, 33(7), 419-421.
    • (2005) Am. J. Infect Control , vol.33 , Issue.7 , pp. 419-421
    • Wright, M.O.1
  • 4
    • 33646837531 scopus 로고    scopus 로고
    • Resistance in gram-negative bacteria: Enterobacteriaceae
    • Paterson, D. L. Resistance in gram-negative bacteria: Enterobacteriaceae. Am. J. Med., 2006, 119(6), S20-8.
    • (2006) Am. J. Med. , vol.119 , Issue.6
    • Paterson, D.L.1
  • 5
    • 70349971143 scopus 로고    scopus 로고
    • New screens and targets in antibacterial drug discovery
    • Shannon, B. F.; Eric, D. B. New screens and targets in antibacterial drug discovery. Curr. Opin. Microbiol, 2009, 12(5), 497-504.
    • (2009) Curr. Opin. Microbiol , vol.12 , Issue.5 , pp. 497-504
    • Shannon, B.F.1    Eric, D.B.2
  • 6
    • 0345839252 scopus 로고    scopus 로고
    • Where will new antibiotics come from?
    • Walsh, C. where will new antibiotics come from? Nat. Rev. Microbiol, 2003, 1(1), 65-70.
    • (2003) Nat. Rev. Microbiol , vol.1 , Issue.1 , pp. 65-70
    • Walsh, C.1
  • 7
    • 0036791627 scopus 로고    scopus 로고
    • New (and not so new) antibacterial targets-from where and when will the novel drugs come?
    • Projan, S. J. New (and not so new) antibacterial targets-from where and when will the novel drugs come? Curr. Opin. Pharm., 2002, 2(5), 513-522.
    • (2002) Curr. Opin. Pharm. , vol.2 , Issue.5 , pp. 513-522
    • Projan . S, J.1
  • 8
    • 0036792157 scopus 로고    scopus 로고
    • Antimicrobials: New solutions badly needed
    • Projan, S. J.; Youngman, P. J. Antimicrobials: New solutions badly needed. Curr. Opin. Microbiol, 2002, 5(5), 463-465.
    • (2002) Curr. Opin. Microbiol , vol.5 , Issue.5 , pp. 463-465
    • Projan, S.J.1    Youngman, P.J.2
  • 9
    • 0027255391 scopus 로고
    • Bacterial endotoxins: Extraordinary lipids that activate eucaryotic signal transduction
    • Raetz, C. R. Bacterial endotoxins: extraordinary lipids that activate eucaryotic signal transduction. Journal of bacteriology, 1993, 175(18), 5745-5743.
    • (1993) Journal of Bacteriology , vol.175 , Issue.18 , pp. 5745-5743
    • Raetz, C.R.1
  • 10
    • 0026604214 scopus 로고
    • The lipid A biosynthesis mutation lpxA2 of Escherichia coli results in drastic antibiotic supersusceptibility
    • Vuorio, R.; Vaara M. The lipid A biosynthesis mutation lpxA2 of Escherichia coli results in drastic antibiotic supersusceptibility. Antimicrobial Agents and Chemotherapy, 1992, 36(4), 826-829.
    • (1992) Antimicrobial Agents and Chemotherapy , vol.36 , Issue.4 , pp. 826-829
    • Vuorio, R.1    Vaara, M.2
  • 11
    • 0031922619 scopus 로고    scopus 로고
    • Antibacterial and anti-inflammatory agents that target endotoxin
    • DOI 10.1016/S0966-842X(98)01230-X, PII S0966842X9801230X
    • Wyckoff, T. J.; Raetz, C. R.; Jackman, J. E. Antibacterial and antiinflammatory agents that target endotoxin. Trends in Microbiology, 1998, 6(4), 154-159. (Pubitemid 28202433)
    • (1998) Trends in Microbiology , vol.6 , Issue.4 , pp. 154-159
    • Wyckoff, T.J.O.1    Raetz, C.R.H.2    Jackman, J.E.3
  • 14
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido, H.; Vaara, M. Molecular basis of bacterial outer membrane permeability. Microbiol Rev., 1985, 49(1), 1-32. (Pubitemid 15134118)
    • (1985) Microbiological Reviews , vol.49 , Issue.1 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 15
    • 0027409501 scopus 로고
    • Outer membrane permeability barrier to azithromycin, clarithromycin, and roxithromycin in gram-negative enteric bacteria
    • Vaara, M. Outer membrane permeability barrier to azithromycin, clarithromycin, and roxithromycin in gram-negative enteric bacteria. Antimicrobial Agents and Chemotherapy, 1993, 37(2), 354-356. (Pubitemid 23046584)
    • (1993) Antimicrobial Agents and Chemotherapy , vol.37 , Issue.2 , pp. 354-356
    • Vaara, M.1
  • 16
    • 0024294319 scopus 로고
    • Biosynthesis of lipid A in Escherichia coli: Identification of UDP-3-O-(R-3-hydroxymyristoyl)-R-D-glucosamine as a precursor of UDP-N2-O3-bis-(R-3-hydroxymyristoyl)-R-D-glucosamine
    • Anderson, M. S.; Robertson, A. D.; Macher, I.; Raetz, C. R. Biosynthesis of lipid A in Escherichia coli: Identification of UDP-3-O-(R-3-hydroxymyristoyl) -R-D-glucosamine as a precursor of UDP-N2-O3-bis-(R-3-hydroxymyristoyl)-R-D- glucosamine. Biochemistry,1988, 27(6), 1908-1917.
    • (1988) Biochemistry , vol.27 , Issue.6 , pp. 1908-1917
    • Anderson, M.S.1    Robertson, A.D.2    MacHer, I.3    Raetz, C.R.4
  • 17
    • 0027304442 scopus 로고
    • UDP-N-acetylglucosamine acyltransferase of Escherichia coli. The first step of endotoxin biosynthesis is thermodynamically unfavorable
    • Anderson, M. S.; Bull, H. G.; Galloway, S. M.; Kelly, T. M.; Mohan, S.; Radika, K.; Raetz, C. R. UDP-Nacetylglucosamine acyltransferase of Escherichia coli: The first step of endotoxin biosynthesis is thermodynamically unfavorable, J. Biol. Chem., 1993, 268(26), 19858-19865. (Pubitemid 23270781)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.26 , pp. 19858-19865
    • Anderson, M.S.1    Bull, H.G.2    Galloway, S.M.3    Kelly, T.M.4    Mohan, S.5    Radika, K.6    Raetz, C.R.H.7
  • 18
    • 0141535260 scopus 로고    scopus 로고
    • Targeting metalloenzymes: A strategy that works
    • DOI 10.1016/S1471-4892(03)00115-2, PII S1471489203001152
    • White, R. J.; Margolis, P. S.; Trias, J.; Yuan, Z. Targeting metalloenzymes: A strategy that works. Curr. Opin. Pharmacol, 2003, 3(5), 502-507. (Pubitemid 37221130)
    • (2003) Current Opinion in Pharmacology , vol.3 , Issue.5 , pp. 502-507
    • White, R.J.1    Margolis, P.S.2    Trias, J.3    Yuan, Z.4
  • 21
    • 0042123525 scopus 로고    scopus 로고
    • Structure of the LpxC deacetylase with a bound substrate-analog inhibitor
    • DOI 10.1038/nsb948
    • Coggins, B. E.; Li, X. C.; McClerren, A. L.; Hindsqual, O.; Raetz, C. R.; Zhou, P. Structure of the LpxC deacetylase with a bound substrate-analog inhibitor. Nature Structural Biology, 2003, 10(8), 645-651. (Pubitemid 36944718)
    • (2003) Nature Structural Biology , vol.10 , Issue.8 , pp. 645-651
    • Coggins, B.E.1    Li, X.2    McClerren, A.L.3    Hindsgaul, O.4    Raetz, C.R.H.5    Zhou, P.6
  • 22
    • 13444287735 scopus 로고    scopus 로고
    • a analysis of an active site histidine: Insights into the mechanism and inhibitor design
    • DOI 10.1021/bi047820z
    • Coggins, B. E.; McClerren, A. L.; Jiang, L.; Li, X. C.; Rudolph, J.; Hindsgual, O.; Raetz, C. R.; Zhou, P. Refined solution structure of the LpxCTU-514 complex and pKa analysis of an active site histidine: insights into the mechanism and inhibitor design. Biochemistry, 2005, 44(4), 1114-1126. (Pubitemid 40208991)
    • (2005) Biochemistry , vol.44 , Issue.4 , pp. 1114-1126
    • Coggins, B.E.1    McClerren, A.L.2    Jiang, L.3    Li, X.4    Rudolph, J.5    Hindsgaul, O.6    Raetz, C.R.H.7    Zhou, P.8
  • 24
    • 39549112496 scopus 로고    scopus 로고
    • Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitor
    • DOI 10.1110/ps.073324108
    • Mochalkin, I.; Knafels, J. D.; Lightle, S. Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitor. Protein Science, 2008, 17(3), 450-457. (Pubitemid 351281545)
    • (2008) Protein Science , vol.17 , Issue.3 , pp. 450-457
    • Mochalkin, I.1    Knafels, J.D.2    Lightle, S.3
  • 25
    • 33845951202 scopus 로고    scopus 로고
    • Binding of uridine 5′-diphosphate in the "basic patch" of the zinc deacetylase LpxC and implications for substrate binding
    • DOI 10.1021/bi0619021
    • Gennadios, H.; Christianson, D. W. Binding of uridine 5′-diphosphate in the "basic patch" of the zinc deacetylase LpxC and implications for substrate binding. Biochemistry, 2006, 45(51), 15216-15223. (Pubitemid 46032448)
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15216-15223
    • Gennadios, H.A.1    Christianson, D.W.2
  • 26
    • 39449115488 scopus 로고    scopus 로고
    • Mechanism and inhibition of LpxC: An essential zincdependent deacetylase of bacterial Lipid A synthesis
    • Brab, A. W.; Zou, P. Mechanism and inhibition of LpxC: an essential zincdependent deacetylase of bacterial Lipid A synthesis. Curr. Pharm. Bio., 2008, 9: 9-15.
    • (2008) Curr. Pharm. Bio. , vol.9 , pp. 9-15
    • Brab, A.W.1    Zou, P.2
  • 28
    • 20444469255 scopus 로고    scopus 로고
    • UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism
    • DOI 10.1074/jbc.M413560200
    • Hernick, M.; Gennadios, H. A.; Whittington, D. A.; Rusche, K. M.; Christianson, D. W.; Fierke, C. A. UDP-3-O-((R)-3-hydroxymyristoyl)- Nacetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism. Journal of Biological Chemistry, 2005, 280(17), 16969-16978. (Pubitemid 41389158)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 16969-16978
    • Hernick, M.1    Gennadios, H.A.2    Whittington, D.A.3    Rusche, K.M.4    Christianson, D.W.5    Fierke, C.A.6
  • 29
    • 13444269024 scopus 로고    scopus 로고
    • Kinetic analysis of the zinc-dependent deacetylase in the lipid A biosynthetic pathway
    • DOI 10.1021/bi048001h
    • McClerren, A. L.; Zhou, P.; Guan, Z. Q.; Raetz, C. R.; Rudolph, J. Kinetic analysis of the znc-dependent deacetylase in the Lipid A biosynthetic pathway. Biochemistry, 2005, 44(4), 1106-1113. (Pubitemid 40208990)
    • (2005) Biochemistry , vol.44 , Issue.4 , pp. 1106-1113
    • McClerren, A.L.1    Zhou, P.2    Guan, Z.3    Raetz, C.R.H.4    Rudolph, J.5
  • 30
    • 9744244982 scopus 로고    scopus 로고
    • Zinc hydrolases: The mechanisms of zinc-dependent deacetylases
    • DOI 10.1016/j.abb.2004.08.006, PII S0003986104004503
    • Hernick, M.; Fierke, C. A. Zinc hydrolases: the mechanisms of zincdependent deacetylases. Arch. Biochem. Biophys., 2005, 433(1), 71-84. (Pubitemid 39586584)
    • (2005) Archives of Biochemistry and Biophysics , vol.433 , Issue.1 , pp. 71-84
    • Hernick, M.1    Fierke, C.A.2
  • 31
    • 45949084971 scopus 로고    scopus 로고
    • DFT investigation on the mechanism of the deacetylation reaction catalyzed by LpxC
    • Robinet, J. J.; Gauld, J. M. DFT investigation on the mechanism of the deacetylation reaction catalyzed by LpxC. J. Phys. Chem., 2008, 112(11), 3462-3469.
    • (2008) J. Phys. Chem. , vol.112 , Issue.11 , pp. 3462-3469
    • Robinet, J.J.1    Gauld, J.M.2
  • 32
    • 33745602267 scopus 로고    scopus 로고
    • Mechanistic inferences from the binding of ligands to LpxC, a metal-dependent deacetylase
    • DOI 10.1021/bi060823m
    • Gennadios, H. A.; Whittington, D. A.; Li, X. C.; Fierke, C. A.; Christianson, D. W. Mechanistic inferences from the binding of ligands to LpxC, a metaldependent deacetylase. Biochemistry, 2006, 45(26), 7940-7948. (Pubitemid 43993217)
    • (2006) Biochemistry , vol.45 , Issue.26 , pp. 7940-7948
    • Gennadios, H.A.1    Whittington, D.A.2    Li, X.3    Fierke, C.A.4    Christianson, D.W.5
  • 33
    • 0345523771 scopus 로고    scopus 로고
    • Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli
    • DOI 10.1046/j.1365-2958.1999.01221.x
    • Ogura, T.; Inoue, K.; Tatsuta, T.; Suzaki, T.; Karata, K.; Young, K.; Su, L. H.; Fierke, C. A.; Jackman, J. E.; Raetz, C. R.; Coleman, J.; Tomoyasu, T.; Matsuzawa, H. Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli. Mol. Microbiol., 1999, 31(3), 833-844. (Pubitemid 29057286)
    • (1999) Molecular Microbiology , vol.31 , Issue.3 , pp. 833-844
    • Ogura, T.1    Inoue, K.2    Tatsuta, T.3    Suzaki, T.4    Karata, K.5    Young, K.6    Su, L.-H.7    Fierke, C.A.8    Jackman, J.E.9    Raetz, C.R.H.10    Coleman, J.11    Tomoyasu, T.12    Matsuzawa, H.13
  • 35
    • 0344824655 scopus 로고    scopus 로고
    • Proteolysis in bacteria regulatory circuits
    • Susan, G. Proteolysis in bacteria regulatory circuits. Annu. Rev. Cell Dev. Biol., 2003, 19, 565-587.
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 565-587
    • Susan, G.1
  • 36
    • 25844525796 scopus 로고    scopus 로고
    • Cellular functions, mechanism of action, and regulation of FtsH protease
    • DOI 10.1146/annurev.micro.59.030804.121316
    • Ito, K.; Akiyama, Y. Celluar functions, mechanism of action, and regulation of FtsH protease. Annu. Rev. Microbio., 2005, 59, 211-231. (Pubitemid 41507430)
    • (2005) Annual Review of Microbiology , vol.59 , pp. 211-231
    • Ito, K.1    Akiyama, Y.2
  • 37
    • 33645085050 scopus 로고    scopus 로고
    • The C-terminal end of LpxC is required for degradation by the FtsH protease
    • Führer, F.; Langklotz, S.; Narberhaus, F. The C-terminal end of LpxC is required for degradation by the FtsH protease. Molecular Microbiology, 2006, 59(3), 1025-1036.
    • (2006) Molecular Microbiology , vol.59 , Issue.3 , pp. 1025-1036
    • Führer, F.1    Langklotz, S.2    Narberhaus, F.3
  • 38
    • 34547938709 scopus 로고    scopus 로고
    • Sequence and Length Recognition of the C-terminal Turnover Element of LpxC, a Soluble Substrate of the Membrane-bound FtsH Protease
    • DOI 10.1016/j.jmb.2007.06.083, PII S0022283607008947
    • Führer, F.; Müller, A.; Baumann, H.; Langklotz S.; Kutscher, B.; Narberhaus, F. Sequence and length recognition of the C-terminal turnover element of LpxC: a soluble substrate of the membrane-bound FtsH protease. J. Mol. Biol., 2007, 372(2), 485-496. (Pubitemid 47267962)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.2 , pp. 485-496
    • Fuhrer, F.1    Muller, A.2    Baumann, H.3    Langklotz, S.4    Kutscher, B.5    Narberhaus, F.6
  • 39
    • 55749093837 scopus 로고    scopus 로고
    • Dual role of FtsH in regulating lipopolysaccharide biosynthesis in Escherichia coli
    • Katz, C.; Ron, E. Z. Dual role of FtsH in regulating lipopolysaccharide biosynthesis in Escherichia coli. Journal of Bacteriology, 2008, 190(21), 7117-7122.
    • (2008) Journal of Bacteriology , vol.190 , Issue.21 , pp. 7117-7122
    • Katz, C.1    Ron, E.Z.2
  • 40
    • 79951634603 scopus 로고    scopus 로고
    • Control of lipopolysaccharide biosynthesis by FtsH-mediated proteolysis of LpxC is conserved in Enterobacteria but not in all Gram-negative bacteria
    • Langklotz, S.; Schakermann, M.;Narberhaus, F. Control of lipopolysaccharide biosynthesis by FtsH-mediated proteolysis of LpxC is conserved in Enterobacteria but not in all Gram-negative bacteria. Journal of Bacteriology, 2011, 193(5), 1090-1097.
    • (2011) Journal of Bacteriology , vol.193 , Issue.5 , pp. 1090-1097
    • Langklotz, S.1    Schakermann, M.2    Narberhaus, F.3
  • 46
    • 0037068502 scopus 로고    scopus 로고
    • Inhibition of the antibacterial target UDP-(3-O-acyl)-N-acetylglucosamine deacetylase (LpxC): Isoxazoline zinc amidase inhibitors bearing diverse metal binding groups
    • DOI 10.1021/jm020183v
    • Pirrung, M. C.; Tumey, L. N.; Raetz, C. R.; Jackman, J. E.; Snehalatha, K.; McClerren, A. L.; Fierke, C. A.; Gantt, S. L.; Rusche, K. M. Inhibition of the antibacterial target UDP-(3-O-acyl)-N-acetylglucosamine deacetylase (LpxC): isoxazoline zinc amidase inhibitors bearing diverse metal binding groups. J. Med. Chem., 2002, 45(19), 4359-4370. (Pubitemid 35025582)
    • (2002) Journal of Medicinal Chemistry , vol.45 , Issue.19 , pp. 4359-4370
    • Pirrung, M.C.1    Tumey, L.N.2    Raetz, C.R.H.3    Jackman, J.E.4    Snehalatha, K.5    McClerren, A.L.6    Fierke, C.A.7    Gantt, S.L.8    Rusche, K.M.9
  • 47
    • 0037433247 scopus 로고    scopus 로고
    • High-throughput catch-and-release synthesis of oxazoline hydroxamates. Structure-activity relationships in novel inhibitors of Escherichia coli LpxC: In vitro enzyme inhibition and antibacterial properties
    • DOI 10.1021/ja0209114
    • Pirrung, M. C.; Tumey, L. N.; McClerren, A. L.; Raetz, C. R. High-Throughput Catch-and-Release Synthesis of Oxazoline Hydroxamates. Structure-activity relationships in novel inhibitors of Escherichia coli LpxC: in vitro enzyme inhibition and antibacterial properties. J. Am. Chem. Soc., 2003, 125(6), 1575-1586. (Pubitemid 36206239)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.6 , pp. 1575-1586
    • Pirrung, M.C.1    Tumey, L.N.2    McClerren, A.L.3    Raetz, C.R.H.4
  • 49
    • 29244445498 scopus 로고    scopus 로고
    • A slow, tight-binding inhibitor of the zinc-dependent deacetylase LpxC of lipid a biosynthesis with antibiotic activity comparable to ciprofloxacin
    • DOI 10.1021/bi0518186
    • McClerren, A. L.; Endsly, S.; Bowman, J. L.; Adersen, N. H.; Guan, Z. Q.; Rudolph, J.; Raetz, C. R. A slow, tight-binding inhibitor of the zincdependent deacetylase LpxC of Lipid A biosynthesis with antibiotic activity comparable to Ciprofloxacin. Biochemistry, 2005, 44(50), 16574-16583. (Pubitemid 41832039)
    • (2005) Biochemistry , vol.44 , Issue.50 , pp. 16574-16583
    • McClerren, A.L.1    Endsley, S.2    Bowman, J.L.3    Andersen, N.H.4    Guan, Z.5    Rudolph, J.6    Raetz, C.R.H.7
  • 50
    • 33947676835 scopus 로고    scopus 로고
    • Inhibition of lipid A biosynthesis as the primary mechanism of CHIR-090 antibiotic activity in Escherichia coli
    • DOI 10.1021/bi6025165
    • Barb, A. W.; McClerren, A. L.; Snehelatha K.; Reynolds, C. M.; Zhou, P.; Raetz, C. R. Inhibition of Lipid A biosynthesis as the primary mechanism of CHIR-090 antibiotic activity in Escherichia coli. Biochemistry, 2007, 46(12), 3793-3802. (Pubitemid 46493479)
    • (2007) Biochemistry , vol.46 , Issue.12 , pp. 3793-3802
    • Barb, A.W.1    McClerren, A.L.2    Snehelatha, K.3    Reynolds, C.M.4    Zhou, P.5    Raetz, C.R.H.6
  • 51
    • 78651346930 scopus 로고    scopus 로고
    • Structure of the metal-dependent deacetylase LpxC from Yersinia enterocolitica complexed with the potent inhibitor CHIR-090
    • Cole, K. E.; Gattis, S. G.; Angell, H. D.; Fierke, C. A.; Christianson, D. W. Structure of the metal-dependent deacetylase LpxC from Yersinia enterocolitica complexed with the potent inhibitor CHIR-090. Biochemistry, 2011, 50(2), 258-265.
    • (2011) Biochemistry , vol.50 , Issue.2 , pp. 258-265
    • Cole, K.E.1    Gattis, S.G.2    Angell, H.D.3    Fierke, C.A.4    Christianson, D.W.5
  • 55
    • 39449127018 scopus 로고    scopus 로고
    • Role of sulfonamide group in matrix metalloproteinase inhibitors
    • DOI 10.2174/092986708783497300
    • Cheng, X. C.; Wang, Q; Fang, H.; Xu W. F. Role of sulfonamide group in matrix metalloproteinase inhibitors. Curr. Med. Chem., 2008, 15(4), 368-373. (Pubitemid 351266942)
    • (2008) Current Medicinal Chemistry , vol.15 , Issue.4 , pp. 368-373
    • Cheng, X.-C.1    Wang, Q.2    Fang, H.3    Xu, W.-F.4
  • 57
    • 47349084576 scopus 로고    scopus 로고
    • Progress in the development of matrix metalloproteinase inhibitors
    • DOI 10.2174/092986708784567680
    • Tu, G. G.; Xu, W. F.; Huang, H. M.; Li, S. H. Progress in the Development of Matrix Metalloproteinase Inhibitors. Curr. Med. Chem., 2008, 15(4), 1388-1395. (Pubitemid 351997789)
    • (2008) Current Medicinal Chemistry , vol.15 , Issue.14 , pp. 1388-1395
    • Tu, G.G.1    Xu, W.F.2    Huang, H.M.3    Lib, S.H.4
  • 58
    • 58149384690 scopus 로고    scopus 로고
    • Aminopeptidase N (APN/CD13) as a target for anticancer agent design
    • Zhang, X. P.; Xu, W. F. Aminopeptidase N (APN/CD13) as a target for anticancer agent design. Curr. Med. Chem., 2008, 15(27), 2850-2865.
    • (2008) Curr. Med. Chem. , vol.15 , Issue.27 , pp. 2850-2865
    • Zhang, X.P.1    Xu, W.F.2
  • 59
    • 0024375849 scopus 로고
    • Phosphonate analogues of carboxypeptidase A substrates are potent transition-state analogue inhibitors
    • Hanson, J. E.; Kaplan, A. P.; Bartlett, P. A. Phosphonate analogues of carboxypeptidase A substrates are potent transition-state analogue inhibitors. Biochemistry, 1989, 28(15), 6294-6305. (Pubitemid 19202018)
    • (1989) Biochemistry , vol.28 , Issue.15 , pp. 6294-6305
    • Hanson, J.E.1    Kaplan, A.P.2    Bartlett, P.A.3
  • 60
    • 0023667724 scopus 로고
    • Slow-and fast-binding inhibitors of thermolysin display different modes of binding: Crystallographic analysis of extended phosphonamidate transition-state analogues
    • Holden, H. M.; Tronrud, D. E.; Monzingo, A. F.; Weaver, L. H.; Matthews, B. W. Slow-and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues. Biochemistry, 1987, 26(26), 8542-8553.
    • (1987) Biochemistry , vol.26 , Issue.26 , pp. 8542-8553
    • Holden, H.M.1    Tronrud, D.E.2    Monzingo, A.F.3    Weaver, L.H.4    Matthews, B.W.5
  • 62
    • 67649386512 scopus 로고    scopus 로고
    • A new class of UDP-3-O-(R-3-hydroxymyristol)-Nacetylglucosamine deacetylase (LpxC) inhibitors for the treatment of Gramnegative infections: PCT application WO 2008027466
    • Cuny, G. D. A new class of UDP-3-O-(R-3-hydroxymyristol)- Nacetylglucosamine deacetylase (LpxC) inhibitors for the treatment of Gramnegative infections: PCT application WO 2008027466. Expert Opin. Ther. Patents, 2009, 19(6), 893-899.
    • (2009) Expert Opin. Ther. Patents , vol.19 , Issue.6 , pp. 893-899
    • Cuny, G.D.1
  • 63
    • 33847654341 scopus 로고    scopus 로고
    • Amphipathic benzoic acid derivatives: Synthesis and binding in the hydrophobic tunnel of the zinc deacetylase LpxC
    • DOI 10.1016/j.bmc.2007.01.044, PII S0968089607000727
    • Shin, H.; Gennadios, H. A.; Whittington, D. A.; Christianson, D. W. Amphipathic benzoic acid derivatives: Synthesis and binding in the hydrophobic tunnel of the zinc deacetylase LpxC. Bioorg. Med. Chem., 2007, 15(7), 2617-2623. (Pubitemid 46367709)
    • (2007) Bioorganic and Medicinal Chemistry , vol.15 , Issue.7 , pp. 2617-2623
    • Shin, H.1    Gennadios, H.A.2    Whittington, D.A.3    Christianson, D.W.4


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