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Volumn 15, Issue 1, 2010, Pages 62-71

Screening for antibacterial inhibitors of the UDP-3-O-(R-3- Hydroxymyristoyl)-N-Acetylglucosamine deacetylase (LpxC) using a high-throughput mass spectrometry assay

Author keywords

Label free; Mass spectrometry; Thermal stability shift; UDP 3 O (R 3 Hydroxymyristoyl) N acetylglucosamine deacetylase (LpxC)

Indexed keywords

ANTIBIOTIC AGENT; BACTERIUM LIPOPOLYSACCHARIDE; ENZYME INHIBITOR; PLASMID DNA; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE; URIDINE DIPHOSPHATE O (3 HYDROXYMYRISTOYL) N ACETYLGLUCOSAMINE DEACETYLASE;

EID: 77949363962     PISSN: 10870571     EISSN: 1552454X     Source Type: Journal    
DOI: 10.1177/1087057109352902     Document Type: Article
Times cited : (37)

References (24)
  • 3
    • 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
    • McClerren AL, Endsley S, Bowman JL, Andersen NH, Guan Z, Rudolph J, et al: A slow, tight-binding inhibitor of the zinc-dependent deacetylase LpxC of lipid A biosynthesis with antibiotic activity comparable to ciprofloxacin. Biochemistry 2005 44 16574-16583.
    • (2005) Biochemistry , vol.44 , pp. 16574-16583
    • McClerren, A.L.1    Endsley, S.2    Bowman, J.L.3    Andersen, N.H.4    Guan, Z.5    Rudolph, J.6
  • 4
    • 39449115488 scopus 로고    scopus 로고
    • Mechanism and inhibition of LpxC: An essential zincdependent deacetylase of bacterial lipid A synthesis
    • Barb AW, Zhou P: Mechanism and inhibition of LpxC: an essential zincdependent deacetylase of bacterial lipid A synthesis. Curr Pharm Biotechnol 2008 9 9-15.
    • (2008) Curr Pharm Biotechnol , vol.9 , pp. 9-15
    • Barb, A.W.1    Zhou, P.2
  • 5
    • 0032971984 scopus 로고    scopus 로고
    • UDP-3-O-(R-3-Hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme
    • Jackman JE, Raetz CR, Fierke CA: UDP-3-O-(R-3-Hydroxymyristoyl)-N- acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme. Biochemistry 1999 38 1902-1911.
    • (1999) Biochemistry , vol.38 , pp. 1902-1911
    • Jackman, J.E.1    Raetz, C.R.2    Fierke, C.A.3
  • 6
    • 47749124645 scopus 로고    scopus 로고
    • Zinc metalloproteins as medicinal targets
    • Anzellotti AI, Farrell NP: Zinc metalloproteins as medicinal targets. Chem Soc Rev 2008 37 1629-1651.
    • (2008) Chem Soc Rev , vol.37 , pp. 1629-1651
    • Anzellotti, A.I.1    Farrell, N.P.2
  • 7
    • 10844233846 scopus 로고    scopus 로고
    • A bioinorganic perspective on matrix metalloproteinase inhibition
    • Puerta DT, Cohen SM: A bioinorganic perspective on matrix metalloproteinase inhibition. Curr Top Med Chem 2004 4 1551-1573.
    • (2004) Curr Top Med Chem , vol.4 , pp. 1551-1573
    • Puerta, D.T.1    Cohen, S.M.2
  • 8
    • 0030985685 scopus 로고    scopus 로고
    • Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc deacetylase from Pseudomonas aeruginosa: A metalloamidase of the lipid A biosynthesis pathway
    • Hyland SA, Eveland SS, Anderson MS: Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc deacetylase from Pseudomonas aeruginosa: a metalloamidase of the lipid A biosynthesis pathway. J Bacteriol 1997 179 2029-2037.
    • (1997) J Bacteriol , vol.179 , pp. 2029-2037
    • Hyland, S.A.1    Eveland, S.S.2    Anderson, M.S.3
  • 9
    • 0034646694 scopus 로고    scopus 로고
    • Antibacterial agents that target lipid A biosynthesis in gram-negative bacteria: Inhibition of diverse UDP-3-O-(r-3-hydroxymyristoyl)-n- acetylglucosamine deacetylases by substrate analogs containing zinc binding motifs
    • Jackman JE, Fierke CA, Tumey LN, Pirrung M, Uchiyama T, Tahir SH, et al: Antibacterial agents that target lipid A biosynthesis in gram-negative bacteria: inhibition of diverse UDP-3-O-(r-3-hydroxymyristoyl)-n-acetylglucosamine deacetylases by substrate analogs containing zinc binding motifs. J Biol Chem 2000 275 11002-11009.
    • (2000) J Biol Chem , vol.275 , pp. 11002-11009
    • Jackman, J.E.1    Fierke, C.A.2    Tumey, L.N.3    Pirrung, M.4    Uchiyama, T.5    Tahir, S.H.6
  • 10
    • 0035869556 scopus 로고    scopus 로고
    • A fluorescencebased homogeneous assay for measuring activity of UDP-3-0-(Ähydroxymyristoyl)-N-acetylgluocosamine deactylase
    • Wang W, Maniar M, Jain R, Jacobs J, Trias J, Yuan Z: A fluorescencebased homogeneous assay for measuring activity of UDP-3-0-(Ähydroxymyristoyl)-N- acetylgluocosamine deactylase. Anal Biochem 2001 290 338-1334
    • (2001) Anal Biochem , vol.290 , pp. 338-1334
    • Wang, W.1    Maniar, M.2    Jain, R.3    Jacobs, J.4    Trias, J.5    Yuan, Z.6
  • 13
    • 4143121255 scopus 로고    scopus 로고
    • Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery
    • Lo MC, Aulabaugh A, Jin G, Cowling R, Bard J, Malamas M, et al: Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery. Anal Biochem 2004 332 153-159.
    • (2004) Anal Biochem , vol.332 , pp. 153-159
    • Lo, M.C.1    Aulabaugh, A.2    Jin, G.3    Cowling, R.4    Bard, J.5    Malamas, M.6
  • 14
    • 0000598101 scopus 로고    scopus 로고
    • A high-capacity scintillation proximity assay for the discovery and evaluation of ZAP-70 tandem SH2 domain antagonists
    • Sheets MP, Warrior UP, Yoon H, Mollison KW, Djuric SW, Trevillyan JM: A high-capacity scintillation proximity assay for the discovery and evaluation of ZAP-70 tandem SH2 domain antagonists. J Biomol Screen 1998 3 139-144.
    • (1998) J Biomol Screen , vol.3 , pp. 139-144
    • Sheets, M.P.1    Warrior, U.P.2    Yoon, H.3    Mollison, K.W.4    Djuric, S.W.5    Trevillyan, J.M.6
  • 15
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • Zhang JH, Chung TD, Oldenburg KR: A simple statistical parameter for use in evaluation and validation of high throughput screening assays. J Biomol Screen 1999 4 67-73.
    • (1999) J Biomol Screen , vol.4 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 16
    • 0025773010 scopus 로고
    • Leakage of periplasmic enzymes from envAl strains of Escherichia coli
    • Young K, Silver LL: Leakage of periplasmic enzymes from envAl strains of Escherichia coli. J Bacterial 1991 173 3609-3614.
    • (1991) J Bacterial , vol.173 , pp. 3609-3614
    • Young, K.1    Silver, L.L.2
  • 18
    • 20444444649 scopus 로고    scopus 로고
    • Mechanism of human SIRT1 activation by resveratrol
    • Borra MT, Smith BC, Denu JM: Mechanism of human SIRT1 activation by resveratrol. J Biol Chem 2005 280 17187-17195.
    • (2005) J Biol Chem , vol.280 , pp. 17187-17195
    • Borra, M.T.1    Smith, B.C.2    Denu, J.M.3
  • 19
    • 35348888354 scopus 로고    scopus 로고
    • Application of mass spectrometry technologies for the discovery of low-molecular weight modulators of enzymes and protein-protein interactions
    • Zehender H, Mayr LM: Application of mass spectrometry technologies for the discovery of low-molecular weight modulators of enzymes and protein-protein interactions. Curr Opin Chem Biol 2007 11 511-517.
    • (2007) Curr Opin Chem Biol , vol.11 , pp. 511-517
    • Zehender, H.1    Mayr, L.M.2
  • 20
    • 34249912663 scopus 로고    scopus 로고
    • High-throughput screening by mass spectrometry: Comparison with the scintillation proximity assay with a focused-file screen of AKT1/PKBa
    • Quercia AK, LaMarr WA, Myung J, Ozbal CC, Landro JA, Lumb KJ: High-throughput screening by mass spectrometry: comparison with the scintillation proximity assay with a focused-file screen of AKT1/PKBa. J Biomol Screen 2007 12 473-480.
    • (2007) J Biomol Screen , vol.12 , pp. 473-480
    • Quercia, A.K.1    Lamarr, W.A.2    Myung, J.3    Ozbal, C.C.4    Landro, J.A.5    Lumb, K.J.6
  • 21
    • 33645665186 scopus 로고    scopus 로고
    • Synergy and antagonism of promiscuous inhibition in multiple-compound mixtures
    • Feng BY, Shoichet BK: Synergy and antagonism of promiscuous inhibition in multiple-compound mixtures. J Med Chem 2006 49 2151-2154.
    • (2006) J Med Chem , vol.49 , pp. 2151-2154
    • Feng, B.Y.1    Shoichet, B.K.2
  • 22
    • 27144476168 scopus 로고    scopus 로고
    • Statistical evaluation of a self-deconvoluting matrix strategy for high-throughput screening of the CXCR3 receptor
    • Ferrand S, Schmid A, Engeloch C, Glickman JF: Statistical evaluation of a self-deconvoluting matrix strategy for high-throughput screening of the CXCR3 receptor. Assay Drug Dev Technol 2005 3 413-424.
    • (2005) Assay Drug Dev Technol , vol.3 , pp. 413-424
    • Ferrand, S.1    Schmid, A.2    Engeloch, C.3    Glickman, J.F.4
  • 23
    • 0346279807 scopus 로고    scopus 로고
    • Evaluation of fluorescent compound interference in 4 fluorescence polarization assays: 2 kinases, 1 protease, and 1 phosphatase
    • Turek-Etienne TC, Small EC, Soh SC, Xin TA, Gaitonde PV, Barrabee EB, et al: Evaluation of fluorescent compound interference in 4 fluorescence polarization assays: 2 kinases, 1 protease, and 1 phosphatase. J Biomol Screen 2003 8 176-184.
    • (2003) J Biomol Screen , vol.8 , pp. 176-184
    • Turek-Etienne, T.C.1    Small, E.C.2    Soh, S.C.3    Xin, T.A.4    Gaitonde, P.V.5    Barrabee, E.B.6
  • 24
    • 51149121262 scopus 로고    scopus 로고
    • Evaluation of an orthogonal pooling strategy for rapid high-throughput screening of proteases
    • Motlekar N, Diamond SL, Napper AD : Evaluation of an orthogonal pooling strategy for rapid high-throughput screening of proteases. Assay Drug Dev Technol 2008 6 395-405.
    • (2008) Assay Drug Dev Technol , vol.6 , pp. 395-405
    • Motlekar, N.1    Diamond, S.L.2    Napper, A.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.