메뉴 건너뛰기




Volumn 10, Issue 11, 2015, Pages 2589-2597

Discovery of Inhibitors for the Ether Lipid-Generating Enzyme AGPS as Anti-Cancer Agents

Author keywords

[No Author keywords available]

Indexed keywords

ALKYL GLYCERONE PHOSPHATE SYNTHASE; ALKYL GLYCERONE PHOSPHATE SYNTHASE INHIBITOR; ANTIMYCIN A1; ANTINEOPLASTIC AGENT; ENZYME INHIBITOR; ETHER LIPID; SYNTHETASE; UNCLASSIFIED DRUG; ZINC 69435460; ALKYLGLYCERONE-PHOSPHATE SYNTHASE; MOLECULAR LIBRARY; TRANSFERASE;

EID: 84947909618     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.5b00466     Document Type: Article
Times cited : (51)

References (23)
  • 2
    • 0014694666 scopus 로고
    • Occurrence and nature of O-alkyl and O-alk-1-enyl moieties of glycerol in lipids of morris transplanted hepatomas and normal rat liver
    • Snyder, F., Blank, M. L., and Morris, H. P. (1969) Occurrence and nature of O-alkyl and O-alk-1-enyl moieties of glycerol in lipids of morris transplanted hepatomas and normal rat liver Biochim. Biophys. Acta, Lipids Lipid Metab. 176, 502-510 10.1016/0005-2760(69)90217-3
    • (1969) Biochim. Biophys. Acta, Lipids Lipid Metab. , vol.176 , pp. 502-510
    • Snyder, F.1    Blank, M.L.2    Morris, H.P.3
  • 3
    • 0015365375 scopus 로고
    • Ether-lipids, glycerol phosphate dehydrogenase, and growth rate in tumors and cultured cells
    • Howard, B. V., Morris, H. P., and Bailey, J. M. (1972) Ether-lipids, glycerol phosphate dehydrogenase, and growth rate in tumors and cultured cells Cancer Res. 32, 1533-1538
    • (1972) Cancer Res. , vol.32 , pp. 1533-1538
    • Howard, B.V.1    Morris, H.P.2    Bailey, J.M.3
  • 4
    • 0017338402 scopus 로고
    • Ether-linked glycerolipids in human brain tumors
    • Albert, D. H. and Anderson, C. E. (1977) Ether-linked glycerolipids in human brain tumors Lipids 12, 188-192 10.1007/BF02533292
    • (1977) Lipids , vol.12 , pp. 188-192
    • Albert, D.H.1    Anderson, C.E.2
  • 5
    • 2642629663 scopus 로고
    • Tumorigenicity of cell lines with altered lipid composition
    • Roos, D. S. and Choppin, P. W. (1984) Tumorigenicity of cell lines with altered lipid composition Proc. Natl. Acad. Sci. U. S. A. 81, 7622-7626 10.1073/pnas.81.23.7622
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 7622-7626
    • Roos, D.S.1    Choppin, P.W.2
  • 6
    • 0018786755 scopus 로고
    • Stereochemical specificity of the biosynthesis of the alkyl ether bond in alkyl ether lipids
    • Davis, P. A. and Hajra, A. K. (1979) Stereochemical specificity of the biosynthesis of the alkyl ether bond in alkyl ether lipids J. Biol. Chem. 254, 4760-4763
    • (1979) J. Biol. Chem. , vol.254 , pp. 4760-4763
    • Davis, P.A.1    Hajra, A.K.2
  • 7
    • 0034096194 scopus 로고    scopus 로고
    • Alkyl-dihydroxyacetonephosphate synthase. Presence and role of flavin adenine dinucleotide
    • de Vet, E. C., Hilkes, Y. H., Fraaije, M. W., and van den Bosch, H. (2000) Alkyl-dihydroxyacetonephosphate synthase. Presence and role of flavin adenine dinucleotide J. Biol. Chem. 275, 6276-6283 10.1074/jbc.275.9.6276
    • (2000) J. Biol. Chem. , vol.275 , pp. 6276-6283
    • De Vet, E.C.1    Hilkes, Y.H.2    Fraaije, M.W.3    Van Den Bosch, H.4
  • 9
    • 84883819129 scopus 로고    scopus 로고
    • Ether lipid generating enzyme AGPS alters the balance of structural and signaling lipids to fuel cancer pathogenicity
    • Benjamin, D. I., Cozzo, A., Ji, X., Roberts, L. S., Louie, S. M., Mulvihill, M. M., Luo, K., and Nomura, D. K. (2013) Ether lipid generating enzyme AGPS alters the balance of structural and signaling lipids to fuel cancer pathogenicity Proc. Natl. Acad. Sci. U. S. A. 110, 14912-14917 10.1073/pnas.1310894110
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 14912-14917
    • Benjamin, D.I.1    Cozzo, A.2    Ji, X.3    Roberts, L.S.4    Louie, S.M.5    Mulvihill, M.M.6    Luo, K.7    Nomura, D.K.8
  • 10
    • 34249898356 scopus 로고    scopus 로고
    • The crucial step in ether phospholipid biosynthesis: Structural basis of a noncanonical reaction associated with a peroxisomal disorder
    • Razeto, A., Mattiroli, F., Carpanelli, E., Aliverti, A., Pandini, V., Coda, A., and Mattevi, A. (2007) The crucial step in ether phospholipid biosynthesis: structural basis of a noncanonical reaction associated with a peroxisomal disorder Structure 15, 683-692 10.1016/j.str.2007.04.009
    • (2007) Structure , vol.15 , pp. 683-692
    • Razeto, A.1    Mattiroli, F.2    Carpanelli, E.3    Aliverti, A.4    Pandini, V.5    Coda, A.6    Mattevi, A.7
  • 11
    • 65349155431 scopus 로고    scopus 로고
    • ThermoFAD, a Thermofluor®-adapted flavin ad hoc detection system for protein folding and ligand binding
    • Forneris, F., Orrù, R., Bonivento, D., Chiarelli, L. R., and Mattevi, A. (2009) ThermoFAD, a Thermofluor®-adapted flavin ad hoc detection system for protein folding and ligand binding FEBS J. 276, 2833-2840 10.1111/j.1742-4658.2009.07006.x
    • (2009) FEBS J. , vol.276 , pp. 2833-2840
    • Forneris, F.1    Orrù, R.2    Bonivento, D.3    Chiarelli, L.R.4    Mattevi, A.5
  • 13
    • 0015911233 scopus 로고
    • The mechanism of action of the respiratory inhibitor, antimycin
    • Slater, E. C. (1973) The mechanism of action of the respiratory inhibitor, antimycin Biochim. Biophys. Acta, Rev. Bioenerg. 301, 129-154 10.1016/0304-4173(73)90002-5
    • (1973) Biochim. Biophys. Acta, Rev. Bioenerg. , vol.301 , pp. 129-154
    • Slater, E.C.1
  • 14
    • 16344382388 scopus 로고    scopus 로고
    • Thermodynamic stability of carbonic anhydrase: Measurements of binding affinity and stoichiometry using ThermoFluor
    • Matulis, D., Kranz, J. K., Salemme, F. R., and Todd, M. J. (2005) Thermodynamic stability of carbonic anhydrase: measurements of binding affinity and stoichiometry using ThermoFluor Biochemistry 44, 5258-5266 10.1021/bi048135v
    • (2005) Biochemistry , vol.44 , pp. 5258-5266
    • Matulis, D.1    Kranz, J.K.2    Salemme, F.R.3    Todd, M.J.4
  • 15
    • 22544467474 scopus 로고    scopus 로고
    • Binding of the respiratory chain inhibitor antimycin to the mitochondrial bc1 complex: A new crystal structure reveals an altered intramolecular hydrogen-bonding pattern
    • Huang, L.-S., Cobessi, D., Tung, E. Y., and Berry, E. A. (2005) Binding of the respiratory chain inhibitor antimycin to the mitochondrial bc1 complex: a new crystal structure reveals an altered intramolecular hydrogen-bonding pattern J. Mol. Biol. 351, 573-597 10.1016/j.jmb.2005.05.053
    • (2005) J. Mol. Biol. , vol.351 , pp. 573-597
    • Huang, L.-S.1    Cobessi, D.2    Tung, E.Y.3    Berry, E.A.4
  • 16
    • 84937132767 scopus 로고    scopus 로고
    • Diacylglycerol metabolism and signaling is a driving force underlying FASN inhibitor sensitivity in cancer cells
    • Benjamin, D. I., Li, D. S., Lowe, W., Heuer, T., Kemble, G., and Nomura, D. K. (2015) Diacylglycerol metabolism and signaling is a driving force underlying FASN inhibitor sensitivity in cancer cells ACS Chem. Biol. 10, 1616 10.1021/acschembio.5b00240
    • (2015) ACS Chem. Biol. , vol.10 , pp. 1616
    • Benjamin, D.I.1    Li, D.S.2    Lowe, W.3    Heuer, T.4    Kemble, G.5    Nomura, D.K.6
  • 17
    • 73149109062 scopus 로고    scopus 로고
    • Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis
    • Nomura, D. K., Long, J. Z., Niessen, S., Hoover, H. S., Ng, S. W., and Cravatt, B. F. (2010) Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis Cell 140, 49-61 10.1016/j.cell.2009.11.027
    • (2010) Cell , vol.140 , pp. 49-61
    • Nomura, D.K.1    Long, J.Z.2    Niessen, S.3    Hoover, H.S.4    Ng, S.W.5    Cravatt, B.F.6
  • 20
    • 33845304296 scopus 로고    scopus 로고
    • Peroxisomal disorders: The single peroxisomal enzyme deficiencies
    • Wanders, R. J. A. and Waterham, H. R. (2006) Peroxisomal disorders: the single peroxisomal enzyme deficiencies Biochim. Biophys. Acta, Mol. Cell Res. 1763, 1707-1720 10.1016/j.bbamcr.2006.08.010
    • (2006) Biochim. Biophys. Acta, Mol. Cell Res. , vol.1763 , pp. 1707-1720
    • Wanders, R.J.A.1    Waterham, H.R.2
  • 21
    • 0000159569 scopus 로고    scopus 로고
    • Protein structure and the energetics of protein stability
    • Robertson, A. D. and Murphy, K. P. (1997) Protein structure and the energetics of protein stability Chem. Rev. 97, 1251-1268 10.1021/cr960383c
    • (1997) Chem. Rev. , vol.97 , pp. 1251-1268
    • Robertson, A.D.1    Murphy, K.P.2
  • 22
    • 0027371870 scopus 로고
    • Ether lipid-synthesis - Purification and identification of alkyl-dihydroxyacetone phosphate synthase from Guinea-pig liver
    • Zomer, A., Deweerd, W., Langeveld, J., and Vandenbosch, H. (1993) Ether lipid-synthesis-purification and identification of alkyl-dihydroxyacetone phosphate synthase from guinea-pig liver Biochim. Biophys. Acta, Lipids Lipid Metab. 1170, 189-196 10.1016/0005-2760(93)90070-P
    • (1993) Biochim. Biophys. Acta, Lipids Lipid Metab. , vol.1170 , pp. 189-196
    • Zomer, A.1    Deweerd, W.2    Langeveld, J.3    Vandenbosch, H.4
  • 23
    • 0014197890 scopus 로고
    • Acyl dihydroxyacetone phosphate. A rapidly labeled lipid in Guinea pig liver mitochondria
    • Hajra, A. K. and Agranoff, B. W. (1967) Acyl dihydroxyacetone phosphate. A rapidly labeled lipid in guinea pig liver mitochondria J. Biol. Chem. 242, 1074-1075
    • (1967) J. Biol. Chem. , vol.242 , pp. 1074-1075
    • Hajra, A.K.1    Agranoff, B.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.