메뉴 건너뛰기




Volumn 164, Issue 4, 2011, Pages 292-299

Changes in PLA 2 activity after interacting with anti-inflammatory drugs and model membranes: Evidence for the involvement of tryptophan residues

Author keywords

ADIFAB; Liposomes; NSAIDs; PLA 2 inhibition; Tryptophan fluorescence quenching and circular dichroism

Indexed keywords

FATTY ACID BINDING PROTEIN; MELOXICAM; NIMESULIDE; NONSTEROID ANTIINFLAMMATORY AGENT; PHOSPHOLIPASE A2; TENOXICAM; TRYPTOPHAN;

EID: 79957795877     PISSN: 00093084     EISSN: 18732941     Source Type: Journal    
DOI: 10.1016/j.chemphyslip.2011.03.003     Document Type: Article
Times cited : (17)

References (61)
  • 1
    • 0030479448 scopus 로고    scopus 로고
    • Conformational changes associated with activation of beevenomphospholipase A(2)
    • Tokyo
    • Ahmed, T., Kelly, S.M., Lawrence, A.J., Mezna, M., Price, N.C., 1996. Conformational changes associated with activation of beevenomphospholipase A(2). J. Biochem. (Tokyo) 120, 1224-1231.
    • (1996) J. Biochem. , vol.120 , pp. 1224-1231
    • Ahmed, T.1    Kelly, S.M.2    Lawrence, A.J.3    Mezna, M.4    Price, N.C.5
  • 2
    • 0023735595 scopus 로고
    • Probing the role of substrate conformation in phospholipase-A2 action on aggregated phospholipids using constrained phosphatidylcholine analogs
    • Barlow, P.N., Lister, M.D., Sigler, P.B., Dennis, E.A., 1988. Probing the role of substrate conformation in phospholipase-A2 action on aggregated phospholipids using constrained phosphatidylcholine analogs. J. Biol. Chem. 263, 12954-12958.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12954-12958
    • Barlow, P.N.1    Lister, M.D.2    Sigler, P.B.3    Dennis, E.A.4
  • 3
    • 0031015166 scopus 로고    scopus 로고
    • Fluorescence spectroscopy as a tool to investigate protein interactions
    • Brown, M.P., Royer, C., 1997. Fluorescence spectroscopy as a tool to investigate protein interactions. Curr. Opin. Biotechnol. 8, 45-49.
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 45-49
    • Brown, M.P.1    Royer, C.2
  • 4
    • 0028973599 scopus 로고
    • Modulation of phospholipase A2: Identification of an inactive membrane-bound state
    • Burack, W.R., Gadd, M.E., Biltonen, R.L., 1995. Modulation of phospholipase A(2) - identification of an inactive membrane-bound state. Biochemistry 34, 14819-14828. (Pubitemid 3002538)
    • (1995) Biochemistry , vol.34 , Issue.45 , pp. 14819-14828
    • Burack, W.R.1    Gadd, M.E.2    Biltonen, R.L.3
  • 5
    • 67650540778 scopus 로고    scopus 로고
    • Location of inhibitors bound to group IVA phospholipase A2 determined by molecular dynamics and deuterium exchange mass spectrometry
    • Burke, J.E., Babakhani, A., Gorfe, A.A., Kokotos, G., Li, S., Woods Jr., V.L., McCammon, J.A., Dennis, E.A., 2009. Location of inhibitors bound to group IVA phospholipase A2 determined by molecular dynamics and deuterium exchange mass spectrometry. J. Am. Chem. Soc. 131, 8083-8091.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 8083-8091
    • Burke, J.E.1    Babakhani, A.2    Gorfe, A.A.3    Kokotos, G.4    Li, S.5    Woods Jr., V.L.6    McCammon, J.A.7    Dennis, E.A.8
  • 8
    • 77749298786 scopus 로고    scopus 로고
    • Differentiating oxicam nonsteroidal anti-inflammatory drugs in phosphoglyceride monolayers
    • Czapla, K., Korchowiec, B., Rogalska, E., 2010. Differentiating oxicam nonsteroidal anti-inflammatory drugs in phosphoglyceride monolayers. Langmuir 26, 3485-3492.
    • (2010) Langmuir , vol.26 , pp. 3485-3492
    • Czapla, K.1    Korchowiec, B.2    Rogalska, E.3
  • 9
    • 0034604593 scopus 로고    scopus 로고
    • Investigations of lipid-protein interactions on monolayers of chain-substituted phosphatidylcholines
    • Dahmen-Levison, U., Brezesinski, G., Mohwald, H., Jakob, J., Nuhn, P., 2000. Investigations of lipid-protein interactions on monolayers of chain-substituted phosphatidylcholines. Angew. Chem. Int. Ed. 39, 2775-2778.
    • (2000) Angew. Chem. Int. Ed. , vol.39 , pp. 2775-2778
    • Dahmen-Levison, U.1    Brezesinski, G.2    Mohwald, H.3    Jakob, J.4    Nuhn, P.5
  • 10
    • 0034132322 scopus 로고    scopus 로고
    • Phospholipase A2 in eicosanoid generation
    • Dennis, E.A., 2000. Phospholipase A2 in eicosanoid generation. Am. J. Respir. Crit. Care Med. 161, S32-S35.
    • (2000) Am. J. Respir. Crit. Care Med. , vol.161
    • Dennis, E.A.1
  • 11
    • 0642373219 scopus 로고    scopus 로고
    • Partition and location of nimesulide in EPC liposomes: A spectrophotometric and fluorescence study
    • Ferreira, H., Lucio, M., de Castro, B., Gameiro, P., Lima, J., Reis, S., 2003. Partition and location of nimesulide in EPC liposomes: a spectrophotometric and fluorescence study. Anal. Bioanal. Chem. 377, 293-298.
    • (2003) Anal. Bioanal. Chem. , vol.377 , pp. 293-298
    • Ferreira, H.1    Lucio, M.2    De Castro, B.3    Gameiro, P.4    Lima, J.5    Reis, S.6
  • 12
    • 22144452566 scopus 로고    scopus 로고
    • Effects of diclofenac on EPC liposome membrane properties
    • Ferreira, H., Lucio, M., Lima, J., Matos, C., Reis, S., 2005a. Effects of diclofenac on EPC liposome membrane properties. Anal. Bioanal. Chem. 382, 1256-1264.
    • (2005) Anal. Bioanal. Chem. , vol.382 , pp. 1256-1264
    • Ferreira, H.1    Lucio, M.2    Lima, J.3    Matos, C.4    Reis, S.5
  • 13
    • 21344456131 scopus 로고    scopus 로고
    • Interaction of clonixin with EPC liposomes used as membrane models
    • Ferreira, H., Lucio, M., Lima, J., Matos, C., Reis, S., 2005b. Interaction of clonixin with EPC liposomes used as membrane models. J. Pharm. Sci. 94, 1277-1287.
    • (2005) J. Pharm. Sci. , vol.94 , pp. 1277-1287
    • Ferreira, H.1    Lucio, M.2    Lima, J.3    Matos, C.4    Reis, S.5
  • 14
    • 47749112015 scopus 로고    scopus 로고
    • Insights on calcium-independent phospholipid membrane damage by Lys49-PLA(2) using tryptophan scanning mutagenesis of bothropstoxin-I from Bothrops jararacussu
    • Ferreira, T.L., Ruller, R., Chioato, L., Ward, R.J., 2008. Insights on calcium-independent phospholipid membrane damage by Lys49-PLA(2) using tryptophan scanning mutagenesis of bothropstoxin-I from Bothrops jararacussu. Biochimie 90, 1397-1406.
    • (2008) Biochimie , vol.90 , pp. 1397-1406
    • Ferreira, T.L.1    Ruller, R.2    Chioato, L.3    Ward, R.J.4
  • 15
    • 0040182776 scopus 로고    scopus 로고
    • 2with phosphatidylcholine-phosphatidylglycerol mixed lipids
    • DOI 10.1021/bi000322f
    • Gadd, M.E., Biltonen, R.L., 2000. Characterization of the interaction of phospholipase A(2) with phosphatidylcholine-phosphatidylglycerol mixed lipids. Biochemistry 39, 9623-9631. (Pubitemid 30626812)
    • (2000) Biochemistry , vol.39 , Issue.32 , pp. 9623-9631
    • Gadd, M.E.1    Biltonen, R.L.2
  • 17
    • 23044484743 scopus 로고    scopus 로고
    • The role of phospholipases in lipid modification and atherosclerosis
    • Ghesquiere, S.A.I., Hofker, M.H., de Winther, M.P.J., 2005. The role of phospholipases in lipid modification and atherosclerosis. Cardiovasc. Toxicol. 5, 161-182.
    • (2005) Cardiovasc. Toxicol. , vol.5 , pp. 161-182
    • Ghesquiere, S.A.I.1    Hofker, M.H.2    De Winther, M.P.J.3
  • 18
    • 77952978246 scopus 로고    scopus 로고
    • Interfacial binding dynamics of bee venom phospholipase A(2) investigated by dynamic light scattering and quartz crystal microbalance
    • Jackman, J.A., Cho, N.J., Duran, R.S., Frank, C.W., 2010. Interfacial binding dynamics of bee venom phospholipase A(2) investigated by dynamic light scattering and quartz crystal microbalance. Langmuir 26, 4103-4112.
    • (2010) Langmuir , vol.26 , pp. 4103-4112
    • Jackman, J.A.1    Cho, N.J.2    Duran, R.S.3    Frank, C.W.4
  • 19
    • 33845208604 scopus 로고    scopus 로고
    • Alpha-lipoic acid: An inhibitor of secretory phospholipase A(2) with anti-inflammatory activity
    • Jameel, N.M., Shekhar, M.A., Vishwanath, B.S., 2006. alpha-lipoic acid: an inhibitor of secretory phospholipase A(2) with anti-inflammatory activity. Life Sci. 80, 146-153.
    • (2006) Life Sci. , vol.80 , pp. 146-153
    • Jameel, N.M.1    Shekhar, M.A.2    Vishwanath, B.S.3
  • 20
    • 1042275605 scopus 로고    scopus 로고
    • 2 enzymes
    • DOI 10.1016/j.toxicon.2003.11.002
    • Kini, R.M., 2003. Excitement ahead: structure, function and mechanism of snake venom phospholipase A(2) enzymes. Toxicon 42, 827-840. (Pubitemid 38201486)
    • (2003) Toxicon , vol.42 , Issue.8 , pp. 827-840
    • Kini, R.M.1
  • 23
    • 0029017689 scopus 로고
    • Interaction of free fatty-acids with phospholipid-bilayers
    • Langner, M., Isac, T., Hui, S.W., 1995. Interaction of free fatty-acids with phospholipid-bilayers. Biochim. Biophys. Acta Biomembr. 1236, 73-80.
    • (1995) Biochim. Biophys. Acta Biomembr. , vol.1236 , pp. 73-80
    • Langner, M.1    Isac, T.2    Hui, S.W.3
  • 24
    • 37749054322 scopus 로고    scopus 로고
    • Molecular basis of phospholipase A(2) activity toward phospholipids with sn-1 substitutions
    • Linderoth, L., Andresen, T.L., Jorgensen, K., Madsen, R., Peters, G.H., 2008. Molecular basis of phospholipase A(2) activity toward phospholipids with sn-1 substitutions. Biophys. J. 94, 14-26.
    • (2008) Biophys. J. , vol.94 , pp. 14-26
    • Linderoth, L.1    Andresen, T.L.2    Jorgensen, K.3    Madsen, R.4    Peters, G.H.5
  • 25
    • 0033616731 scopus 로고    scopus 로고
    • Evidence for a regulatory role of cholesterol superlattices in the hydrolytic activity of secretory phospholipase A2 in lipid membranes
    • Liu, F., Chong, P.L.G., 1999. Evidence for a regulatory role of cholesterol superlattices in the hydrolytic activity of secretory phospholipase A2 in lipid membranes. Biochemistry 38, 3867-3873.
    • (1999) Biochemistry , vol.38 , pp. 3867-3873
    • Liu, F.1    Chong, P.L.G.2
  • 26
    • 0028978839 scopus 로고
    • Phospholipase A(2) engineering - Probing the structural and functional roles of N-terminal residues with site-directed mutagenesis, X-ray, and NMR
    • Liu, X.H., Zhu, H.X., Huang, B.H., Rogers, J., Yu, B.Z., Kumar, A., Jain, M.K., Sundaralingam, M., Tsai, M.D., 1995. Phospholipase A(2) engineering - probing the structural and functional roles of N-terminal residues with site-directed mutagenesis, X-ray, and NMR. Biochemistry 34, 7322-7334.
    • (1995) Biochemistry , vol.34 , pp. 7322-7334
    • Liu, X.H.1    Zhu, H.X.2    Huang, B.H.3    Rogers, J.4    Yu, B.Z.5    Kumar, A.6    Jain, M.K.7    Sundaralingam, M.8    Tsai, M.D.9
  • 27
    • 42449162322 scopus 로고    scopus 로고
    • Binding of nonsteroidal anti-inflammatory drugs to DPPC: Structure and thermodynamic aspects
    • DOI 10.1021/la703584s
    • Lucio, M., Bringezu, F., Reis, S., Lima, J.L.F.C., Brezesinski, G., 2008. Binding of nonsteroidal anti-inflammatory drugs to DPPC: structure and thermodynamic aspects. Langmuir 24, 4132-4139. (Pubitemid 351569020)
    • (2008) Langmuir , vol.24 , Issue.8 , pp. 4132-4139
    • Lucio, M.1    Bringezu, F.2    Reis, S.3    Lima, J.L.F.C.4    Brezesinski, G.5
  • 28
    • 19244378715 scopus 로고    scopus 로고
    • Influence of some anti-inflammatory drugs in membrane fluidity studied by fluorescence anisotropy measurements
    • Lucio, M., Ferreira, H., Lima, J., Matos, C., de Castro, B., Reis, S., 2004. Influence of some anti-inflammatory drugs in membrane fluidity studied by fluorescence anisotropy measurements. Phys. Chem. Chem. Phys. 6, 1493-1498.
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 1493-1498
    • Lucio, M.1    Ferreira, H.2    Lima, J.3    Matos, C.4    De Castro, B.5    Reis, S.6
  • 29
    • 34447558471 scopus 로고    scopus 로고
    • Use of liposomes to evaluate the role of membrane interactions on antioxidant activity
    • Lucio, M., Ferreira, H., Lima, J.L.F.C., Reis, S., 2007. Use of liposomes to evaluate the role of membrane interactions on antioxidant activity. Anal. Chim. Acta 597, 163-170.
    • (2007) Anal. Chim. Acta , vol.597 , pp. 163-170
    • Lucio, M.1    Ferreira, H.2    Lima, J.L.F.C.3    Reis, S.4
  • 31
    • 73649118166 scopus 로고    scopus 로고
    • Phospholipase A2 inhibitors as potential therapeutic agents for the treatment of inflammatory diseases
    • Magrioti, V., Kokotos, G., 2010. Phospholipase A2 inhibitors as potential therapeutic agents for the treatment of inflammatory diseases. Expert Opin. Ther. Pat. 20, 1-18.
    • (2010) Expert Opin. Ther. Pat. , vol.20 , pp. 1-18
    • Magrioti, V.1    Kokotos, G.2
  • 32
    • 75549084522 scopus 로고    scopus 로고
    • Effects of the nonsteroidal anti-inflammatory drug naproxen on human erythrocytes and on cell membrane molecular models
    • Manrique-Moreno, M., Suwalsky, M., Villena, F., Garidel, P., 2010. Effects of the nonsteroidal anti-inflammatory drug naproxen on human erythrocytes and on cell membrane molecular models. Biophys. Chem. 147, 53-58.
    • (2010) Biophys. Chem. , vol.147 , pp. 53-58
    • Manrique-Moreno, M.1    Suwalsky, M.2    Villena, F.3    Garidel, P.4
  • 33
    • 72949099544 scopus 로고    scopus 로고
    • Non-steroidal anti-inflammatory drug induced membrane fusion: Concentration and temperature effects
    • Mondal, S., Sarkar, M., 2009. Non-steroidal anti-inflammatory drug induced membrane fusion: concentration and temperature effects. J. Phys. Chem. B 113, 16323-16331.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 16323-16331
    • Mondal, S.1    Sarkar, M.2
  • 34
    • 65649144271 scopus 로고    scopus 로고
    • The membrane-activity of ibuprofen, diclofenac, and naproxen: A physico-chemical study with lecithin phospholipids
    • Moreno, M.M., Garidel, P., Suwalsky, M., Howe, J., Brandenburg, K., 2009. The membrane-activity of ibuprofen, diclofenac, and naproxen: a physico-chemical study with lecithin phospholipids. Biochim. Biophys. Acta, Biomembr. 1788, 1296-1303.
    • (2009) Biochim. Biophys. Acta, Biomembr. , vol.1788 , pp. 1296-1303
    • Moreno, M.M.1    Garidel, P.2    Suwalsky, M.3    Howe, J.4    Brandenburg, K.5
  • 35
    • 77957244309 scopus 로고    scopus 로고
    • Molecular docking and 3D-QSAR CoMFA studies on indole inhibitors of GIIA secreted phospholipase A(2)
    • Mouchlis, V.D., Mavromoustakos, T.M., Kokotos, G., 2010. Molecular docking and 3D-QSAR CoMFA studies on indole inhibitors of GIIA secreted phospholipase A(2). J. Chem. Inf. Model. 50, 1589-1601.
    • (2010) J. Chem. Inf. Model. , vol.50 , pp. 1589-1601
    • Mouchlis, V.D.1    Mavromoustakos, T.M.2    Kokotos, G.3
  • 36
    • 33750037284 scopus 로고    scopus 로고
    • 2
    • DOI 10.1021/bi061440r
    • Nemec, K.N., Pande, A.H., Qin, S., Urbauer, R.J.B., Tan, S.H., Moe, D., Tatulian, S.A., 2006. Structural and functional effects of tryptophans inserted into the membrane-binding and substrate-binding sites of human group IIA phospholipase A(2). Biochemistry 45, 12448-12460. (Pubitemid 44583687)
    • (2006) Biochemistry , vol.45 , Issue.41 , pp. 12448-12460
    • Nemec, K.N.1    Pande, A.H.2    Qin, S.3    Urbauer, R.J.B.4    Tan, S.5    Moe, D.6    Tatulian, S.A.7
  • 37
    • 79952397326 scopus 로고    scopus 로고
    • Effects of non-steroidal anti-inflammatory drugs on the structure of lipid bilayers: Therapeutical aspects
    • Nunes, C., Brezesinski, G., Lima, J.L.F.C., Reis, S., Lucio, M., 2011. Effects of non-steroidal anti-inflammatory drugs on the structure of lipid bilayers: therapeutical aspects. Soft Matter..
    • (2011) Soft Matter..
    • Nunes, C.1    Brezesinski, G.2    Lima, J.L.F.C.3    Reis, S.4    Lucio, M.5
  • 38
    • 0030603978 scopus 로고    scopus 로고
    • Human non-pancreatic (group II) secreted phospholipase A(2) expressed from a synthetic gene in Escherichia coli: Characterisation of N-terminal mutants
    • Othman, R., Baker, S., Li, Y., Worrall, A.F., Wilton, D.C., 1996. Human non-pancreatic (group II) secreted phospholipase A(2) expressed from a synthetic gene in Escherichia coli: Characterisation of N-terminal mutants. Biochim. Biophys. Acta, Lipids Lipid Metab. 1303, 92-102.
    • (1996) Biochim. Biophys. Acta, Lipids Lipid Metab. , vol.1303 , pp. 92-102
    • Othman, R.1    Baker, S.2    Li, Y.3    Worrall, A.F.4    Wilton, D.C.5
  • 39
    • 33750087241 scopus 로고    scopus 로고
    • 2and functional implications
    • DOI 10.1021/bi060898q
    • Pande, A.H., Qin, S., Nemec, K.N., He, X.M., Tatulian, S.A., 2006. Isoform-specific-embrane insertion of secretory phospholipase A(2) and functional implications. Biochemistry 45, 12436-12447. (Pubitemid 44583686)
    • (2006) Biochemistry , vol.45 , Issue.41 , pp. 12436-12447
    • Pande, A.H.1    Qin, S.2    Nemec, K.N.3    He, X.4    Tatulian, S.A.5
  • 40
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher, S.W., Glockner, J., 1981. Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20, 33-37.
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glockner, J.2
  • 41
    • 27744595554 scopus 로고    scopus 로고
    • Evidence for the regulatory role of the N-terminal helix of secretory phospholipase A(2) from studies on native and chimeric proteins
    • Qin, S., Pande, A.H., Nemec, K.N., He, X.M., Tatulian, S.A., 2005. Evidence for the regulatory role of the N-terminal helix of secretory phospholipase A(2) from studies on native and chimeric proteins. J. Biol. Chem. 280, 36773-36783.
    • (2005) J. Biol. Chem. , vol.280 , pp. 36773-36783
    • Qin, S.1    Pande, A.H.2    Nemec, K.N.3    He, X.M.4    Tatulian, S.A.5
  • 42
    • 7044269246 scopus 로고    scopus 로고
    • The N-terminal alpha-helix of pancreatic phospholipase A(2) determines productive-mode orientation of the enzyme at the membrane surface
    • Qin, S., Pande, A.H., Nemec, K.N., Tatulian, S.A., 2004. The N-terminal alpha-helix of pancreatic phospholipase A(2) determines productive-mode orientation of the enzyme at the membrane surface. J. Mol. Biol. 344, 71-89.
    • (2004) J. Mol. Biol. , vol.344 , pp. 71-89
    • Qin, S.1    Pande, A.H.2    Nemec, K.N.3    Tatulian, S.A.4
  • 43
    • 0029076177 scopus 로고
    • Continuous measurement of phospholipase a(2) activity using the fluorescent-probe ADIFAB
    • Richieri, G.V., Kleinfeld, A.M., 1995. Continuous measurement of phospholipase a(2) activity using the fluorescent-probe ADIFAB. Anal. Biochem. 229, 256-263.
    • (1995) Anal. Biochem. , vol.229 , pp. 256-263
    • Richieri, G.V.1    Kleinfeld, A.M.2
  • 44
    • 0027089776 scopus 로고
    • A fluorescently labeled intestinal fatty-acid binding-protein - Interactions with fatty-acids and its use in monitoring free fatty-acids
    • Richieri, G.V., Ogata, R.T., Kleinfeld, A.M., 1992. A fluorescently labeled intestinal fatty-acid binding-protein - interactions with fatty-acids and its use in monitoring free fatty-acids. J. Biol. Chem. 267, 23495-23501.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23495-23501
    • Richieri, G.V.1    Ogata, R.T.2    Kleinfeld, A.M.3
  • 45
    • 0032904864 scopus 로고    scopus 로고
    • The measurement of free fatty acid concentration with the fluorescent probe ADIFAB: A practical guide for the use of the ADIFAB probe
    • Richieri, G.V., Ogata, R.T., Kleinfeld, A.M., 1999. The measurement of free fatty acid concentration with the fluorescent probe ADIFAB: a practical guide for the use of the ADIFAB probe. Mol. Cell. Biochem. 192, 87-94.
    • (1999) Mol. Cell. Biochem. , vol.192 , pp. 87-94
    • Richieri, G.V.1    Ogata, R.T.2    Kleinfeld, A.M.3
  • 46
    • 70449685768 scopus 로고    scopus 로고
    • Physico-chemical studies of molecular interactions between non-ionic surfactants and bovine serum albumin
    • Ruiz-Pena, M., Oropesa-Nunez, R., Pons, T., Louro, S.R., Perez-Gramatges, A., 2010. Physico-chemical studies of molecular interactions between non-ionic surfactants and bovine serum albumin. Colloids Surf. B 75, 282-289.
    • (2010) Colloids Surf. B , vol.75 , pp. 282-289
    • Ruiz-Pena, M.1    Oropesa-Nunez, R.2    Pons, T.3    Louro, S.R.4    Perez-Gramatges, A.5
  • 47
    • 0027955031 scopus 로고
    • The substrate specificities of four different lysophospholipases as determined by a novel fluorescence assay
    • She, H.S., Garsetti, D.E., Steiner, M.R., Egan, R.W., Clark, M.A., 1994. The substrate specificities of 4 different lysophospholipases as determined by a novel fluorescence assay. Biochem. J. 298, 23-29. (Pubitemid 24061537)
    • (1994) Biochemical Journal , vol.298 , Issue.1 , pp. 23-29
    • She, H.S.1    Garsetti, D.E.2    Steiner, M.R.3    Egan, R.W.4    Clark, M.A.5
  • 48
    • 0015793995 scopus 로고
    • Lateral phase separation in phospholipid membranes
    • Shimshick, E.J., McConnell, H.M., 1973. Lateral phase separation in phospholipid membranes. Biochemistry 12, 2351-2360.
    • (1973) Biochemistry , vol.12 , pp. 2351-2360
    • Shimshick, E.J.1    McConnell, H.M.2
  • 50
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N., Woody, R.W., 2000. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287, 252-260.
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 51
    • 0033534175 scopus 로고    scopus 로고
    • 2
    • Sumandea, M., Das, S., Sumandea, C., Cho, W., 1999. Roles of aromatic residues in high interfacial activity of Naja naja atra phospholipase A(2). Biochemistry 38, 16290-16297. (Pubitemid 129520551)
    • (1999) Biochemistry , vol.38 , Issue.49 , pp. 16290-16297
    • Sumandea, M.1    Das, S.2    Sumandea, C.3    Cho, W.4
  • 52
    • 0037339369 scopus 로고    scopus 로고
    • Structural effects of covalent inhibition of phospholipase A(2) suggest allosteric coupling between membrane binding and catalytic sites
    • Tatulian, S.A., 2003. Structural effects of covalent inhibition of phospholipase A(2) suggest allosteric coupling between membrane binding and catalytic sites. Biophys. J. 84, 1773-1783.
    • (2003) Biophys. J. , vol.84 , pp. 1773-1783
    • Tatulian, S.A.1
  • 53
    • 0031584275 scopus 로고    scopus 로고
    • Structural changes in a secretory phospholipase A(2) induced by membrane binding: A clue to interfacial activation?
    • Tatulian, S.A., Biltonen, R.L.,Tamm,L.K., 1997. Structural changes in a secretory phospholipase A(2) induced by membrane binding: a clue to interfacial activation? J Mol. Biol. 268, 809-815.
    • (1997) J Mol. Biol. , vol.268 , pp. 809-815
    • Tatulian, S.A.1    Biltonen, R.L.2    Tamm, L.K.3
  • 54
    • 14344260441 scopus 로고    scopus 로고
    • 2 hydrolysis of supported phospholipid bilayers: A neutron reflectivity and ellipsometry study
    • DOI 10.1021/bi047727a
    • Vacklin, H.P., Tiberg, F., Fragneto, G., Thomas, R.K., 2005. Phospholipase A(2) hydrolysis of supported phospholipid bilayers: a neutron reflectivity and ellipsornetry study. Biochemistry 44, 2811-2821. (Pubitemid 40293657)
    • (2005) Biochemistry , vol.44 , Issue.8 , pp. 2811-2821
    • Vacklin, H.P.1    Tiberg, F.2    Fragneto, G.3    Thomas, R.K.4
  • 55
    • 0035028745 scopus 로고    scopus 로고
    • Mechanisms of tryptophan fluorescence shifts in proteins
    • Vivian, J.T., Callis, P.R., 2001. Mechanisms of tryptophan fluorescence shifts in proteins. Biophys. J. 80, 2093-2109. (Pubitemid 32401976)
    • (2001) Biophysical Journal , vol.80 , Issue.5 , pp. 2093-2109
    • Vivian, J.T.1    Callis, P.R.2
  • 56
    • 38149115365 scopus 로고    scopus 로고
    • Liquid-liquid immiscibility in model membranes activates secretory phospholipase A(2)
    • Wagner, K., Desbat, B., Brezesinski, G., 2008. Liquid-liquid immiscibility in model membranes activates secretory phospholipase A(2). Biochim. Biophys. Acta. Biomembr. 1778, 166-174.
    • (2008) Biochim. Biophys. Acta. Biomembr. , vol.1778 , pp. 166-174
    • Wagner, K.1    Desbat, B.2    Brezesinski, G.3
  • 57
    • 61549109876 scopus 로고    scopus 로고
    • Meloxicam and meloxicam-beta-cyclodextrin complex in model membranes: Effects on the properties and enzymatic lipolysis of phospholipid monolayers in relation to anti-inflammatory activity
    • Wieclaw, K., Korchowiec, B., Corvis, Y., Korchowiec, J., Guermouche, H., Rogalska, E., 2009. Meloxicam and meloxicam-beta-cyclodextrin complex in model membranes: effects on the properties and enzymatic lipolysis of phospholipid monolayers in relation to anti-inflammatory activity. Langmuir 25, 1417-1426.
    • (2009) Langmuir , vol.25 , pp. 1417-1426
    • Wieclaw, K.1    Korchowiec, B.2    Corvis, Y.3    Korchowiec, J.4    Guermouche, H.5    Rogalska, E.6
  • 59
    • 0027248903 scopus 로고
    • 2
    • Yu, B.Z., Berg, O.G., Jain, M.K., 1993. The divalent-cation is obligatory for the binding of ligands to the catalytic site of secreted phospholipase-A(2). Biochemistry 32, 6485-6492. (Pubitemid 23208834)
    • (1993) Biochemistry , vol.32 , Issue.25 , pp. 6485-6492
    • Yu, B.-Z.1    Berg, O.G.2    Jain, M.K.3
  • 60
    • 0033551220 scopus 로고    scopus 로고
    • Contributions of residues of pancreatic phospholipase A(2) to interfacial binding, catalysis, and activation
    • Yu, B.Z., Rogers, J., Tsai, M.D., Pidgeon, C., Jain, M.K., 1999. Contributions of residues of pancreatic phospholipase A(2) to interfacial binding, catalysis, and activation. Biochemistry 38, 4875-4884.
    • (1999) Biochemistry , vol.38 , pp. 4875-4884
    • Yu, B.Z.1    Rogers, J.2    Tsai, M.D.3    Pidgeon, C.4    Jain, M.K.5
  • 61
    • 0026795513 scopus 로고
    • Synthetic model proteins - Positional effects of interchain hydrophobic interactions on stability of 2-stranded alpha-helical coiled-coils
    • Zhou, N.E., Kay, C.M., Hodges, R.S., 1992. Synthetic model proteins - positional effects of interchain hydrophobic interactions on stability of 2-stranded alpha-helical coiled-coils. J. Biol. Chem. 267, 2664-2670.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2664-2670
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.