메뉴 건너뛰기




Volumn 411, Issue 3-4, 2010, Pages 190-197

A sensitive fluorescence-based assay for the detection of ExoU-mediated PLA2 activity

Author keywords

ExoU; PED6; Phospholipase A2; Pseudomonas aeruginosa

Indexed keywords

BACTERIAL PROTEIN; GLUTAMATE SODIUM; METHYL ARACHIDONYL FLUOROPHOSPHONATE; PHOSPHOLIPASE A1; PHOSPHOLIPASE A2 INHIBITOR; PROTEIN EXOU; SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG;

EID: 72449131834     PISSN: 00098981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cca.2009.10.025     Document Type: Article
Times cited : (23)

References (45)
  • 1
    • 0141453241 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa bacteremia: risk factors for mortality and influence of delayed receipt of effective antimicrobial therapy on clinical outcome
    • Kang C.I., Kim S.H., Kim H.B., et al. Pseudomonas aeruginosa bacteremia: risk factors for mortality and influence of delayed receipt of effective antimicrobial therapy on clinical outcome. Clin Infect Dis 37 6 (2003 Sep 15) 745-751
    • (2003) Clin Infect Dis , vol.37 , Issue.6 , pp. 745-751
    • Kang, C.I.1    Kim, S.H.2    Kim, H.B.3
  • 2
    • 33748432273 scopus 로고    scopus 로고
    • Severe pseudomonal infections
    • Mutlu G.M., and Wunderink R.G. Severe pseudomonal infections. Curr Opin Crit Care 12 5 (2006 Oct) 458-463
    • (2006) Curr Opin Crit Care , vol.12 , Issue.5 , pp. 458-463
    • Mutlu, G.M.1    Wunderink, R.G.2
  • 3
    • 63349107361 scopus 로고    scopus 로고
    • Clinical impact of imipenem-resistant Pseudomonas aeruginosa bloodstream infections
    • Suarez C., Pena C., Tubau F., et al. Clinical impact of imipenem-resistant Pseudomonas aeruginosa bloodstream infections. J Infect 58 4 (2009 Apr) 285-290
    • (2009) J Infect , vol.58 , Issue.4 , pp. 285-290
    • Suarez, C.1    Pena, C.2    Tubau, F.3
  • 4
    • 15544389065 scopus 로고    scopus 로고
    • Role of the type III secreted exoenzymes S, T, and Y in systemic spread of Pseudomonas aeruginosa PAO1 in vivo
    • Vance R.E., Rietsch A., and Mekalanos J.J. Role of the type III secreted exoenzymes S, T, and Y in systemic spread of Pseudomonas aeruginosa PAO1 in vivo. Infect Immun 73 3 (2005 Mar) 1706-1713
    • (2005) Infect Immun , vol.73 , Issue.3 , pp. 1706-1713
    • Vance, R.E.1    Rietsch, A.2    Mekalanos, J.J.3
  • 5
    • 33846284918 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa chronic colonization in cystic fibrosis patients
    • Murray T.S., Egan M., and Kazmierczak B.I. Pseudomonas aeruginosa chronic colonization in cystic fibrosis patients. Curr Opin Pediatr 19 1 (2007 Feb) 83-88
    • (2007) Curr Opin Pediatr , vol.19 , Issue.1 , pp. 83-88
    • Murray, T.S.1    Egan, M.2    Kazmierczak, B.I.3
  • 6
    • 33646016635 scopus 로고    scopus 로고
    • Nosocomial bacterial pneumonia in HIV-infected patients: risk factors for adverse outcome and implications for rational empiric antibiotic therapy
    • Franzetti F., Grassini A., Piazza M., et al. Nosocomial bacterial pneumonia in HIV-infected patients: risk factors for adverse outcome and implications for rational empiric antibiotic therapy. Infection 34 1 (2006 Feb) 9-16
    • (2006) Infection , vol.34 , Issue.1 , pp. 9-16
    • Franzetti, F.1    Grassini, A.2    Piazza, M.3
  • 7
    • 34447322825 scopus 로고    scopus 로고
    • The impact of nosocomially-acquired resistant Pseudomonas aeruginosa infection in a burn unit
    • Armour A.D., Shankowsky H.A., Swanson T., Lee J., and Tredget E.E. The impact of nosocomially-acquired resistant Pseudomonas aeruginosa infection in a burn unit. J Trauma 63 1 (2007 Jul) 164-171
    • (2007) J Trauma , vol.63 , Issue.1 , pp. 164-171
    • Armour, A.D.1    Shankowsky, H.A.2    Swanson, T.3    Lee, J.4    Tredget, E.E.5
  • 8
    • 65549088935 scopus 로고    scopus 로고
    • Cooperation and virulence of clinical Pseudomonas aeruginosa populations
    • Kohler T., Buckling A., and van Delden C. Cooperation and virulence of clinical Pseudomonas aeruginosa populations. Proc Natl Acad Sci USA 106 15 (Apr 14, 2009) 6339-6344
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.15 , pp. 6339-6344
    • Kohler, T.1    Buckling, A.2    van Delden, C.3
  • 9
    • 48249107970 scopus 로고    scopus 로고
    • Ventilator-associated pneumonia in an adult clinical-surgical intensive care unit of a Brazilian university hospital: incidence, risk factors, etiology, and antibiotic resistance
    • Rocha L.A., Vilela C.A., Cezario R.C., Almeida A.B., and Gontijo Filho P. Ventilator-associated pneumonia in an adult clinical-surgical intensive care unit of a Brazilian university hospital: incidence, risk factors, etiology, and antibiotic resistance. Braz J Infect Dis 12 1 (Feb 2008) 80-85
    • (2008) Braz J Infect Dis , vol.12 , Issue.1 , pp. 80-85
    • Rocha, L.A.1    Vilela, C.A.2    Cezario, R.C.3    Almeida, A.B.4    Gontijo Filho, P.5
  • 10
    • 0034468607 scopus 로고    scopus 로고
    • Review of the incidence and prognosis of Pseudomonas aeruginosa infections in cancer patients in the 1990s
    • Maschmeyer G., and Braveny I. Review of the incidence and prognosis of Pseudomonas aeruginosa infections in cancer patients in the 1990s. Eur J Clin Microbiol Infect Dis 19 12 (Dec 2000) 915-925
    • (2000) Eur J Clin Microbiol Infect Dis , vol.19 , Issue.12 , pp. 915-925
    • Maschmeyer, G.1    Braveny, I.2
  • 11
    • 0032702557 scopus 로고    scopus 로고
    • Bacterial phospholipases and pathogenesis
    • Schmiel D.H., and Miller V.L. Bacterial phospholipases and pathogenesis. Microbes Infect 1 13 (Nov 1999) 1103-1112
    • (1999) Microbes Infect , vol.1 , Issue.13 , pp. 1103-1112
    • Schmiel, D.H.1    Miller, V.L.2
  • 12
    • 33846688692 scopus 로고    scopus 로고
    • Secreted bacterial phospholipase A2 enzymes: better living through phospholipolysis
    • Sitkiewicz I., Stockbauer K.E., and Musser J.M. Secreted bacterial phospholipase A2 enzymes: better living through phospholipolysis. Trends Microbiol 15 2 (Feb 2007) 63-69
    • (2007) Trends Microbiol , vol.15 , Issue.2 , pp. 63-69
    • Sitkiewicz, I.1    Stockbauer, K.E.2    Musser, J.M.3
  • 13
    • 33750722808 scopus 로고    scopus 로고
    • Bacterial protein toxins and lipids: role in toxin targeting and activity
    • Geny B., and Popoff M.R. Bacterial protein toxins and lipids: role in toxin targeting and activity. Biol Cell 98 11 (Nov 2006) 633-651
    • (2006) Biol Cell , vol.98 , Issue.11 , pp. 633-651
    • Geny, B.1    Popoff, M.R.2
  • 14
    • 0031872389 scopus 로고    scopus 로고
    • Phospholipase A of Yersinia enterocolitica contributes to pathogenesis in a mouse model
    • Schmiel D.H., Wagar E., Karamanou L., Weeks D., and Miller V.L. Phospholipase A of Yersinia enterocolitica contributes to pathogenesis in a mouse model. Infect Immun 66 8 (Aug 1998) 3941-3951
    • (1998) Infect Immun , vol.66 , Issue.8 , pp. 3941-3951
    • Schmiel, D.H.1    Wagar, E.2    Karamanou, L.3    Weeks, D.4    Miller, V.L.5
  • 15
    • 0035877065 scopus 로고    scopus 로고
    • Type III protein secretion is associated with death in lower respiratory and systemic Pseudomonas aeruginosa infections
    • Roy-Burman A., Savel R.H., Racine S., et al. Type III protein secretion is associated with death in lower respiratory and systemic Pseudomonas aeruginosa infections. J Infect Dis 183 12 (Jun 15, 2001) 1767-1774
    • (2001) J Infect Dis , vol.183 , Issue.12 , pp. 1767-1774
    • Roy-Burman, A.1    Savel, R.H.2    Racine, S.3
  • 16
    • 0038376087 scopus 로고    scopus 로고
    • The mechanism of action of the Pseudomonas aeruginosa-encoded type III cytotoxin, ExoU
    • Sato H., Frank D.W., Hillard C.J., et al. The mechanism of action of the Pseudomonas aeruginosa-encoded type III cytotoxin, ExoU. EMBO J 22 12 (Jun 16, 2003) 2959-2969
    • (2003) EMBO J , vol.22 , Issue.12 , pp. 2959-2969
    • Sato, H.1    Frank, D.W.2    Hillard, C.J.3
  • 17
    • 0142135037 scopus 로고    scopus 로고
    • In vivo phospholipase activity of the Pseudomonas aeruginosa cytotoxin ExoU and protection of mammalian cells with phospholipase A2 inhibitors
    • Phillips R.M., Six D.A., Dennis E.A., and Ghosh P. In vivo phospholipase activity of the Pseudomonas aeruginosa cytotoxin ExoU and protection of mammalian cells with phospholipase A2 inhibitors. J Biol Chem 278 42 (Oct 17, 2003) 41,326-41,332
    • (2003) J Biol Chem , vol.278 , Issue.42
    • Phillips, R.M.1    Six, D.A.2    Dennis, E.A.3    Ghosh, P.4
  • 18
    • 4444342607 scopus 로고    scopus 로고
    • ExoU is a potent intracellular phospholipase
    • Sato H., and Frank D.W. ExoU is a potent intracellular phospholipase. Mol Microbiol 53 5 (Sep 2004) 1279-1290
    • (2004) Mol Microbiol , vol.53 , Issue.5 , pp. 1279-1290
    • Sato, H.1    Frank, D.W.2
  • 19
    • 33646374906 scopus 로고    scopus 로고
    • A C-terminal domain targets the Pseudomonas aeruginosa cytotoxin ExoU to the plasma membrane of host cells
    • Rabin S.D., Veesenmeyer J.L., Bieging K.T., and Hauser A.R. A C-terminal domain targets the Pseudomonas aeruginosa cytotoxin ExoU to the plasma membrane of host cells. Infect Immun 74 5 (May 2006) 2552-2561
    • (2006) Infect Immun , vol.74 , Issue.5 , pp. 2552-2561
    • Rabin, S.D.1    Veesenmeyer, J.L.2    Bieging, K.T.3    Hauser, A.R.4
  • 20
    • 33748672064 scopus 로고    scopus 로고
    • Identification of superoxide dismutase as a cofactor for the pseudomonas type III toxin, ExoU
    • Sato H., Feix J.B., and Frank D.W. Identification of superoxide dismutase as a cofactor for the pseudomonas type III toxin, ExoU. Biochemistry 45 34 (Aug 29, 2006) 10,368-10,375
    • (2006) Biochemistry , vol.45 , Issue.34
    • Sato, H.1    Feix, J.B.2    Frank, D.W.3
  • 21
    • 13244295376 scopus 로고    scopus 로고
    • Characterization of phospholipase activity of the Pseudomonas aeruginosa type III cytotoxin, ExoU
    • Sato H., Feix J.B., Hillard C.J., and Frank D.W. Characterization of phospholipase activity of the Pseudomonas aeruginosa type III cytotoxin, ExoU. J Bacteriol 187 3 (Feb 2005) 1192-1195
    • (2005) J Bacteriol , vol.187 , Issue.3 , pp. 1192-1195
    • Sato, H.1    Feix, J.B.2    Hillard, C.J.3    Frank, D.W.4
  • 22
    • 11144265658 scopus 로고    scopus 로고
    • Functional regions of the Pseudomonas aeruginosa cytotoxin ExoU
    • Rabin S.D., and Hauser A.R. Functional regions of the Pseudomonas aeruginosa cytotoxin ExoU. Infect Immun 73 1 (Jan 2005) 573-582
    • (2005) Infect Immun , vol.73 , Issue.1 , pp. 573-582
    • Rabin, S.D.1    Hauser, A.R.2
  • 23
    • 0033066577 scopus 로고    scopus 로고
    • Biological effects of Pseudomonas aeruginosa type III-secreted proteins on CHO cells
    • Vallis A.J., Finck-Barbancon V., Yahr T.L., and Frank D.W. Biological effects of Pseudomonas aeruginosa type III-secreted proteins on CHO cells. Infect Immun 67 4 (Apr 1999) 2040-2044
    • (1999) Infect Immun , vol.67 , Issue.4 , pp. 2040-2044
    • Vallis, A.J.1    Finck-Barbancon, V.2    Yahr, T.L.3    Frank, D.W.4
  • 24
    • 0030868998 scopus 로고    scopus 로고
    • ExoU expression by Pseudomonas aeruginosa correlates with acute cytotoxicity and epithelial injury
    • Finck-Barbancon V., Goranson J., Zhu L., et al. ExoU expression by Pseudomonas aeruginosa correlates with acute cytotoxicity and epithelial injury. Mol Microbiol 25 3 (Aug 1997) 547-557
    • (1997) Mol Microbiol , vol.25 , Issue.3 , pp. 547-557
    • Finck-Barbancon, V.1    Goranson, J.2    Zhu, L.3
  • 25
    • 0029914812 scopus 로고    scopus 로고
    • Genetic relationship between the 53- and 49-kilodalton forms of exoenzyme S from Pseudomonas aeruginosa
    • Yahr T.L., Barbieri J.T., and Frank D.W. Genetic relationship between the 53- and 49-kilodalton forms of exoenzyme S from Pseudomonas aeruginosa. J Bacteriol 178 5 (Mar 1996) 1412-1419
    • (1996) J Bacteriol , vol.178 , Issue.5 , pp. 1412-1419
    • Yahr, T.L.1    Barbieri, J.T.2    Frank, D.W.3
  • 26
    • 77049313195 scopus 로고
    • Acetylornithinase of Escherichia coli: partial purification and some properties
    • Vogel H.J., and Bonner D.M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem 218 1 (Jan 1956) 97-106
    • (1956) J Biol Chem , vol.218 , Issue.1 , pp. 97-106
    • Vogel, H.J.1    Bonner, D.M.2
  • 27
    • 0015910040 scopus 로고
    • Exotoxins of Pseudomonas aeruginosa. I. Factors that influence the production of exotoxin A
    • Liu P.V. Exotoxins of Pseudomonas aeruginosa. I. Factors that influence the production of exotoxin A. J Infect Dis 128 4 (Oct 1973) 506-513
    • (1973) J Infect Dis , vol.128 , Issue.4 , pp. 506-513
    • Liu, P.V.1
  • 28
    • 0345504899 scopus 로고
    • Pseudomonas aeruginosa exoenzyme S: an adenosine diphosphate ribosyltransferase distinct from toxin A
    • Iglewski B.H., Sadoff J., Bjorn M.J., and Maxwell E.S. Pseudomonas aeruginosa exoenzyme S: an adenosine diphosphate ribosyltransferase distinct from toxin A. Proc Natl Acad Sci USA 75 7 (Jul 1978) 3211-3215
    • (1978) Proc Natl Acad Sci USA , vol.75 , Issue.7 , pp. 3211-3215
    • Iglewski, B.H.1    Sadoff, J.2    Bjorn, M.J.3    Maxwell, E.S.4
  • 29
    • 0017076808 scopus 로고
    • Pseudomonas aeruginosa exotoxin: purification by preparative polyacrylamide gel electrophoresis and the development of a highly specific antitoxin serum
    • Callahan L.T. Pseudomonas aeruginosa exotoxin: purification by preparative polyacrylamide gel electrophoresis and the development of a highly specific antitoxin serum. Infect Immun 14 1 (Jul 1976) 55-61
    • (1976) Infect Immun , vol.14 , Issue.1 , pp. 55-61
    • Callahan, L.T.1
  • 30
    • 3142769080 scopus 로고    scopus 로고
    • Origins of delays in monolayer kinetics: phospholipase A2 paradigm
    • Cajal Y., Berg O.G., and Jain M.K. Origins of delays in monolayer kinetics: phospholipase A2 paradigm. Biochemistry 43 28 (Jul 20, 2004) 9256-9264
    • (2004) Biochemistry , vol.43 , Issue.28 , pp. 9256-9264
    • Cajal, Y.1    Berg, O.G.2    Jain, M.K.3
  • 31
    • 0020482178 scopus 로고
    • Origin of the latency phase during the action of phospholipase A2 on unmodified phosphatidylcholine vesicles
    • Apitz-Castro R., Jain M.K., and De Haas G.H. Origin of the latency phase during the action of phospholipase A2 on unmodified phosphatidylcholine vesicles. Biochim Biophys Acta 688 2 (Jun 14, 1982) 349-356
    • (1982) Biochim Biophys Acta , vol.688 , Issue.2 , pp. 349-356
    • Apitz-Castro, R.1    Jain, M.K.2    De Haas, G.H.3
  • 32
    • 0030702957 scopus 로고    scopus 로고
    • Thermodynamic and kinetic basis of interfacial activation: resolution of binding and allosteric effects on pancreatic phospholipase A2 at zwitterionic interfaces
    • Berg O.G., Rogers J., Yu B.Z., Yao J., Romsted L.S., and Jain M.K. Thermodynamic and kinetic basis of interfacial activation: resolution of binding and allosteric effects on pancreatic phospholipase A2 at zwitterionic interfaces. Biochemistry 36 47 (Nov 25, 1997) 14,512-14,530
    • (1997) Biochemistry , vol.36 , Issue.47
    • Berg, O.G.1    Rogers, J.2    Yu, B.Z.3    Yao, J.4    Romsted, L.S.5    Jain, M.K.6
  • 33
    • 33847704986 scopus 로고    scopus 로고
    • Pseudolipasin A is a specific inhibitor for phospholipase A2 activity of Pseudomonas aeruginosa cytotoxin ExoU
    • Lee V.T., Pukatzki S., Sato H., et al. Pseudolipasin A is a specific inhibitor for phospholipase A2 activity of Pseudomonas aeruginosa cytotoxin ExoU. Infect Immun 75 3 (Mar 2007) 1089-1098
    • (2007) Infect Immun , vol.75 , Issue.3 , pp. 1089-1098
    • Lee, V.T.1    Pukatzki, S.2    Sato, H.3
  • 34
    • 33745621121 scopus 로고    scopus 로고
    • Eukaryotic localization, activation and ubiquitinylation of a bacterial type III secreted toxin
    • Stirling F.R., Cuzick A., Kelly S.M., Oxley D., and Evans T.J. Eukaryotic localization, activation and ubiquitinylation of a bacterial type III secreted toxin. Cell Microbiol 8 8 (Aug 2006) 1294-1309
    • (2006) Cell Microbiol , vol.8 , Issue.8 , pp. 1294-1309
    • Stirling, F.R.1    Cuzick, A.2    Kelly, S.M.3    Oxley, D.4    Evans, T.J.5
  • 35
    • 0015991171 scopus 로고
    • Physical chemical studies of short-chain lecithin homologues. I. Influence of the chain length of the fatty acid ester and of electrolytes on the critical micelle concentration
    • Tausk R.J., Karmiggelt J., Oudshoorn C., and Overbeek J.T. Physical chemical studies of short-chain lecithin homologues. I. Influence of the chain length of the fatty acid ester and of electrolytes on the critical micelle concentration. Biophys Chem 1 3 (Feb 1974) 175-183
    • (1974) Biophys Chem , vol.1 , Issue.3 , pp. 175-183
    • Tausk, R.J.1    Karmiggelt, J.2    Oudshoorn, C.3    Overbeek, J.T.4
  • 36
    • 2542478793 scopus 로고    scopus 로고
    • The critical micelle concentrations of lysophosphatidic acid and sphingosylphosphorylcholine
    • Li Z., Mintzer E., and Bittman R. The critical micelle concentrations of lysophosphatidic acid and sphingosylphosphorylcholine. Chem Phys Lipids 130 2 (Jul 2004) 197-201
    • (2004) Chem Phys Lipids , vol.130 , Issue.2 , pp. 197-201
    • Li, Z.1    Mintzer, E.2    Bittman, R.3
  • 37
    • 0000989532 scopus 로고
    • Effect of electrolyte and urea on micelle formation
    • Schick M. Effect of electrolyte and urea on micelle formation. J Phys Chem 68 12 (1964) 3585-3592
    • (1964) J Phys Chem , vol.68 , Issue.12 , pp. 3585-3592
    • Schick, M.1
  • 38
    • 33847803878 scopus 로고
    • Micelle formation by ionic surfactants. II. Specificity of head groups, micelle structure
    • Stigter D. Micelle formation by ionic surfactants. II. Specificity of head groups, micelle structure. J Phys Chem 78 24 (11/01, 1974) 2480-2485
    • (1974) J Phys Chem , vol.78 , Issue.24 , pp. 2480-2485
    • Stigter, D.1
  • 39
    • 13344265911 scopus 로고
    • Counterions and micelle size. I. Light scattering by solutions of dodecyltrimethylammonium salts
    • Anacker E.W., and Ghose H.M. Counterions and micelle size. I. Light scattering by solutions of dodecyltrimethylammonium salts. J Phys Chem 67 8 (08/01, 1963) 1713-1716
    • (1963) J Phys Chem , vol.67 , Issue.8 , pp. 1713-1716
    • Anacker, E.W.1    Ghose, H.M.2
  • 40
    • 0021109735 scopus 로고
    • Effect of lipid phase transition on the binding of anions to dimyristoylphosphatidylcholine liposomes
    • Tatulian S.A. Effect of lipid phase transition on the binding of anions to dimyristoylphosphatidylcholine liposomes. Biochim Biophys Acta 736 2 (Dec 21, 1983) 189-195
    • (1983) Biochim Biophys Acta , vol.736 , Issue.2 , pp. 189-195
    • Tatulian, S.A.1
  • 41
    • 0034633952 scopus 로고    scopus 로고
    • Structural basis of the anionic interface preference and kcat* activation of pancreatic phospholipase A2
    • Yu B.Z., Poi M.J., Ramagopal U.A., et al. Structural basis of the anionic interface preference and kcat* activation of pancreatic phospholipase A2. Biochemistry 39 40 (Oct 10, 2000) 12,312-12,323
    • (2000) Biochemistry , vol.39 , Issue.40
    • Yu, B.Z.1    Poi, M.J.2    Ramagopal, U.A.3
  • 42
    • 0033551220 scopus 로고    scopus 로고
    • Contributions of residues of pancreatic phospholipase A2 to interfacial binding, catalysis, and activation
    • Yu B.Z., Rogers J., Tsai M.D., Pidgeon C., and Jain M.K. Contributions of residues of pancreatic phospholipase A2 to interfacial binding, catalysis, and activation. Biochemistry 38 15 (Apr 13, 1999) 4875-4884
    • (1999) Biochemistry , vol.38 , Issue.15 , pp. 4875-4884
    • Yu, B.Z.1    Rogers, J.2    Tsai, M.D.3    Pidgeon, C.4    Jain, M.K.5
  • 43
    • 0032580962 scopus 로고    scopus 로고
    • Cationic residues 53 and 56 control the anion-induced interfacial k*cat activation of pancreatic phospholipase A2
    • Rogers J., Yu B.Z., Tsai M.D., Berg O.G., and Jain M.K. Cationic residues 53 and 56 control the anion-induced interfacial k*cat activation of pancreatic phospholipase A2. Biochemistry 37 26 (Jun 30, 1998) 9549-9556
    • (1998) Biochemistry , vol.37 , Issue.26 , pp. 9549-9556
    • Rogers, J.1    Yu, B.Z.2    Tsai, M.D.3    Berg, O.G.4    Jain, M.K.5
  • 44
    • 0027192943 scopus 로고
    • Metal ion and salt effects on the phospholipase A2, lysophospholipase, and transacylase activities of human cytosolic phospholipase A2
    • Reynolds L.J., Hughes L.L., Louis A.I., Kramer R.M., and Dennis E.A. Metal ion and salt effects on the phospholipase A2, lysophospholipase, and transacylase activities of human cytosolic phospholipase A2. Biochim Biophys Acta 1167 3 (Apr 23, 1993) 272-280
    • (1993) Biochim Biophys Acta , vol.1167 , Issue.3 , pp. 272-280
    • Reynolds, L.J.1    Hughes, L.L.2    Louis, A.I.3    Kramer, R.M.4    Dennis, E.A.5
  • 45
    • 2442624720 scopus 로고    scopus 로고
    • Monomeric Cu, Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis
    • Rakhit R., Crow J.P., Lepock J.R., Kondejewski L.H., Cashman N.R., and Chakrabartty A. Monomeric Cu, Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis. J Biol Chem 279 15 (Apr 9, 2004) 15,499-15,504
    • (2004) J Biol Chem , vol.279 , Issue.15
    • Rakhit, R.1    Crow, J.P.2    Lepock, J.R.3    Kondejewski, L.H.4    Cashman, N.R.5    Chakrabartty, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.