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Volumn 51, Issue 3, 2012, Pages 238-266

Phospholipases C and sphingomyelinases: Lipids as substrates and modulators of enzyme activity

Author keywords

Enzyme regulation; Lipid protein interactions; Phospholipase C; Sphingomyelinase; Vesicle aggregation; Vesicle fusion

Indexed keywords

CERAMIDE; CYTOCHROME C; DIACYLGLYCEROL; PHOSPHOLIPASE C; SPHINGOMYELIN PHOSPHODIESTERASE; TRIACYLGLYCEROL LIPASE;

EID: 84860665292     PISSN: 01637827     EISSN: 18732194     Source Type: Journal    
DOI: 10.1016/j.plipres.2012.03.002     Document Type: Review
Times cited : (53)

References (269)
  • 1
    • 23944484438 scopus 로고    scopus 로고
    • Modulation of PI-specific phospholipase C by membrane curvature and molecular order
    • H. Ahyayauch, A.V. Villar, A. Alonso, and F.M. Goni Modulation of PI-specific phospholipase C by membrane curvature and molecular order Biochemistry 44 34 2005 11592 11600
    • (2005) Biochemistry , vol.44 , Issue.34 , pp. 11592-11600
    • Ahyayauch, H.1    Villar, A.V.2    Alonso, A.3    Goni, F.M.4
  • 2
    • 0034700264 scopus 로고    scopus 로고
    • Lipids favoring inverted phase enhance the ability of aerolysin to permeabilize liposome bilayers
    • A. Alonso, F.M. Goni, and J.T. Buckley Lipids favoring inverted phase enhance the ability of aerolysin to permeabilize liposome bilayers Biochemistry 39 46 2000 14019 14024
    • (2000) Biochemistry , vol.39 , Issue.46 , pp. 14019-14024
    • Alonso, A.1    Goni, F.M.2    Buckley, J.T.3
  • 3
    • 0042563108 scopus 로고    scopus 로고
    • Using X-ray crystallography of the Asp55Asn mutant of the phosphatidylcholine-preferring phospholipase C from Bacillus cereus to support the mechanistic role of Asp55 as the general base
    • N.M. Antikainen, A.F. Monzingo, C.L. Franklin, J.D. Robertus, and S.F. Martin Using X-ray crystallography of the Asp55Asn mutant of the phosphatidylcholine-preferring phospholipase C from Bacillus cereus to support the mechanistic role of Asp55 as the general base Arch Biochem Biophys 417 1 2003 81 86
    • (2003) Arch Biochem Biophys , vol.417 , Issue.1 , pp. 81-86
    • Antikainen, N.M.1    Monzingo, A.F.2    Franklin, C.L.3    Robertus, J.D.4    Martin, S.F.5
  • 4
    • 29244466467 scopus 로고    scopus 로고
    • Diacylglycerol induces fusion of nuclear envelope membrane precursor vesicles
    • T. Barona, R.D. Byrne, T.R. Pettitt, M.J. Wakelam, B. Larijani, and D.L. Poccia Diacylglycerol induces fusion of nuclear envelope membrane precursor vesicles J Biol Chem 280 50 2005 41171 41177
    • (2005) J Biol Chem , vol.280 , Issue.50 , pp. 41171-41177
    • Barona, T.1    Byrne, R.D.2    Pettitt, T.R.3    Wakelam, M.J.4    Larijani, B.5    Poccia, D.L.6
  • 5
    • 0029981021 scopus 로고    scopus 로고
    • Dual inhibitory effect of gangliosides on phospholipase C-promoted fusion of lipidic vesicles
    • G. Basanez, G.D. Fidelio, F.M. Goni, B. Maggio, and A. Alonso Dual inhibitory effect of gangliosides on phospholipase C-promoted fusion of lipidic vesicles Biochemistry 35 23 1996 7506 7513
    • (1996) Biochemistry , vol.35 , Issue.23 , pp. 7506-7513
    • Basanez, G.1    Fidelio, G.D.2    Goni, F.M.3    Maggio, B.4    Alonso, A.5
  • 6
    • 0031567613 scopus 로고    scopus 로고
    • Poly(ethylene glycol)-lipid conjugates inhibit phospholipase C-induced lipid hydrolysis, liposome aggregation and fusion through independent mechanisms
    • G. Basanez, F.M. Goni, and A. Alonso Poly(ethylene glycol)-lipid conjugates inhibit phospholipase C-induced lipid hydrolysis, liposome aggregation and fusion through independent mechanisms FEBS Lett 411 2-3 1997 281 286
    • (1997) FEBS Lett , vol.411 , Issue.23 , pp. 281-286
    • Basanez, G.1    Goni, F.M.2    Alonso, A.3
  • 7
    • 0040703911 scopus 로고    scopus 로고
    • Effect of single chain lipids on phospholipase C-promoted vesicle fusion. A test for the stalk hypothesis of membrane fusion
    • G. Basanez, F.M. Goni, and A. Alonso Effect of single chain lipids on phospholipase C-promoted vesicle fusion. A test for the stalk hypothesis of membrane fusion Biochemistry 37 11 1998 3901 3908
    • (1998) Biochemistry , vol.37 , Issue.11 , pp. 3901-3908
    • Basanez, G.1    Goni, F.M.2    Alonso, A.3
  • 8
    • 0029859762 scopus 로고    scopus 로고
    • Origin of the lag period in the phospholipase C cleavage of phospholipids in membranes. Concomitant vesicle aggregation and enzyme activation
    • G. Basanez, J.L. Nieva, F.M. Goni, and A. Alonso Origin of the lag period in the phospholipase C cleavage of phospholipids in membranes. Concomitant vesicle aggregation and enzyme activation Biochemistry 35 48 1996 15183 15187
    • (1996) Biochemistry , vol.35 , Issue.48 , pp. 15183-15187
    • Basanez, G.1    Nieva, J.L.2    Goni, F.M.3    Alonso, A.4
  • 9
    • 0029863628 scopus 로고    scopus 로고
    • Diacylglycerol and the promotion of lamellar-hexagonal and lamellar-isotropic phase transitions in lipids: Implications for membrane fusion
    • G. Basanez, J.L. Nieva, E. Rivas, A. Alonso, and F.M. Goni Diacylglycerol and the promotion of lamellar-hexagonal and lamellar-isotropic phase transitions in lipids: implications for membrane fusion Biophys J 70 5 1996 2299 2306
    • (1996) Biophys J , vol.70 , Issue.5 , pp. 2299-2306
    • Basanez, G.1    Nieva, J.L.2    Rivas, E.3    Alonso, A.4    Goni, F.M.5
  • 10
    • 0141861184 scopus 로고    scopus 로고
    • Morphological changes induced by phospholipase C and by sphingomyelinase on large unilamellar vesicles: A cryo-transmission electron microscopy study of liposome fusion
    • G. Basanez, M.B. Ruiz-Arguello, A. Alonso, F.M. Goni, G. Karlsson, and K. Edwards Morphological changes induced by phospholipase C and by sphingomyelinase on large unilamellar vesicles: a cryo-transmission electron microscopy study of liposome fusion Biophys J 72 6 1997 2630 2637
    • (1997) Biophys J , vol.72 , Issue.6 , pp. 2630-2637
    • Basanez, G.1    Ruiz-Arguello, M.B.2    Alonso, A.3    Goni, F.M.4    Karlsson, G.5    Edwards, K.6
  • 11
    • 0023707810 scopus 로고
    • Mass action kinetics of virus-cell aggregation and fusion
    • J. Bentz, S. Nir, and D.G. Covell Mass action kinetics of virus-cell aggregation and fusion Biophys J 54 3 1988 449 462
    • (1988) Biophys J , vol.54 , Issue.3 , pp. 449-462
    • Bentz, J.1    Nir, S.2    Covell, D.G.3
  • 13
    • 0025365516 scopus 로고
    • Effect of sulfatide and gangliosides on phospholipase C and phospholipase A2 activity: A monolayer study
    • I.D. Bianco, G.D. Fidelio, and B. Maggio Effect of sulfatide and gangliosides on phospholipase C and phospholipase A2 activity: a monolayer study Biochim Biophys Acta 1026 2 1990 179 185
    • (1990) Biochim Biophys Acta , vol.1026 , Issue.2 , pp. 179-185
    • Bianco, I.D.1    Fidelio, G.D.2    Maggio, B.3
  • 14
    • 15944425766 scopus 로고    scopus 로고
    • A mitochondrial pool of sphingomyelin is involved in TNFalpha-induced Bax translocation to mitochondria
    • H. Birbes, C. Luberto, Y.T. Hsu, S. El Bawab, Y.A. Hannun, and L.M. Obeid A mitochondrial pool of sphingomyelin is involved in TNFalpha-induced Bax translocation to mitochondria Biochem J 386 Pt. 3 2005 445 451
    • (2005) Biochem J , vol.386 , Issue.PART 3 , pp. 445-451
    • Birbes, H.1    Luberto, C.2    Hsu, Y.T.3    El Bawab, S.4    Hannun, Y.A.5    Obeid, L.M.6
  • 15
    • 32044452411 scopus 로고    scopus 로고
    • Phospholipase cleavage of D- and L-chiro-glycosylphosphoinositides asymmetrically incorporated into liposomal membranes
    • J.B. Bonilla, M.B. Cid, F.X. Contreras, F.M. Goni, and M. Martin-Lomas Phospholipase cleavage of D- and L-chiro-glycosylphosphoinositides asymmetrically incorporated into liposomal membranes Chemistry 12 5 2006 1513 1528
    • (2006) Chemistry , vol.12 , Issue.5 , pp. 1513-1528
    • Bonilla, J.B.1    Cid, M.B.2    Contreras, F.X.3    Goni, F.M.4    Martin-Lomas, M.5
  • 16
    • 77955123824 scopus 로고    scopus 로고
    • Implication of sphingomyelin/ceramide molar ratio on the biological activity of sphingomyelinase
    • B. Boulgaropoulos, H. Amenitsch, P. Laggner, and G. Pabst Implication of sphingomyelin/ceramide molar ratio on the biological activity of sphingomyelinase Biophys J 99 2 2010 499 506
    • (2010) Biophys J , vol.99 , Issue.2 , pp. 499-506
    • Boulgaropoulos, B.1    Amenitsch, H.2    Laggner, P.3    Pabst, G.4
  • 17
    • 79551613763 scopus 로고    scopus 로고
    • PLC regulation: Emerging pictures for molecular mechanisms
    • T.D. Bunney, and M. Katan PLC regulation: emerging pictures for molecular mechanisms Trends Biochem Sci 36 2 2011 88 96
    • (2011) Trends Biochem Sci , vol.36 , Issue.2 , pp. 88-96
    • Bunney, T.D.1    Katan, M.2
  • 18
    • 64749102105 scopus 로고    scopus 로고
    • Structural insights into formation of an active signaling complex between Rac and phospholipase C gamma 2
    • T.D. Bunney, O. Opaleye, S.M. Roe, P. Vatter, R.W. Baxendale, and C. Walliser Structural insights into formation of an active signaling complex between Rac and phospholipase C gamma 2 Mol Cell 34 2 2009 223 233
    • (2009) Mol Cell , vol.34 , Issue.2 , pp. 223-233
    • Bunney, T.D.1    Opaleye, O.2    Roe, S.M.3    Vatter, P.4    Baxendale, R.W.5    Walliser, C.6
  • 19
    • 72149090172 scopus 로고    scopus 로고
    • Coexistence of immiscible mixtures of palmitoylsphingomyelin and palmitoylceramide in monolayers and bilayers
    • J.V. Busto, M.L. Fanani, L. De Tullio, J. Sot, B. Maggio, and F.M. Goni Coexistence of immiscible mixtures of palmitoylsphingomyelin and palmitoylceramide in monolayers and bilayers Biophys J 97 10 2009 2717 2726
    • (2009) Biophys J , vol.97 , Issue.10 , pp. 2717-2726
    • Busto, J.V.1    Fanani, M.L.2    De Tullio, L.3    Sot, J.4    Maggio, B.5    Goni, F.M.6
  • 20
    • 77958166326 scopus 로고    scopus 로고
    • Cholesterol displaces palmitoylceramide from its tight packing with palmitoylsphingomyelin in the absence of a liquid-disordered phase
    • J.V. Busto, J. Sot, J. Requejo-Isidro, F.M. Goni, and A. Alonso Cholesterol displaces palmitoylceramide from its tight packing with palmitoylsphingomyelin in the absence of a liquid-disordered phase Biophys J 99 4 2010 1119 1128
    • (2010) Biophys J , vol.99 , Issue.4 , pp. 1119-1128
    • Busto, J.V.1    Sot, J.2    Requejo-Isidro, J.3    Goni, F.M.4    Alonso, A.5
  • 21
    • 33947276115 scopus 로고    scopus 로고
    • PLCgamma is enriched on poly-phosphoinositide-rich vesicles to control nuclear envelope assembly
    • R.D. Byrne, M. Garnier-Lhomme, K. Han, M. Dowicki, N. Michael, and N. Totty PLCgamma is enriched on poly-phosphoinositide-rich vesicles to control nuclear envelope assembly Cell Signal 19 5 2007 913 922
    • (2007) Cell Signal , vol.19 , Issue.5 , pp. 913-922
    • Byrne, R.D.1    Garnier-Lhomme, M.2    Han, K.3    Dowicki, M.4    Michael, N.5    Totty, N.6
  • 22
    • 66449107842 scopus 로고    scopus 로고
    • Tyrosine kinase regulation of nuclear envelope assembly
    • R.D. Byrne, B. Larijani, and D.L. Poccia Tyrosine kinase regulation of nuclear envelope assembly Adv Enzyme Regul 49 1 2009 148 156
    • (2009) Adv Enzyme Regul , vol.49 , Issue.1 , pp. 148-156
    • Byrne, R.D.1    Larijani, B.2    Poccia, D.L.3
  • 23
    • 60349111961 scopus 로고    scopus 로고
    • Nuclear envelope formation in vitro: A sea urchin egg cell-free system
    • R.D. Byrne, V. Zhendre, B. Larijani, and D.L. Poccia Nuclear envelope formation in vitro: a sea urchin egg cell-free system Methods Mol Biol 464 2009 207 223
    • (2009) Methods Mol Biol , vol.464 , pp. 207-223
    • Byrne, R.D.1    Zhendre, V.2    Larijani, B.3    Poccia, D.L.4
  • 24
    • 0032745772 scopus 로고    scopus 로고
    • Phase behavior and molecular interactions in mixtures of ceramide with dipalmitoylphosphatidylcholine
    • D.C. Carrer, and B. Maggio Phase behavior and molecular interactions in mixtures of ceramide with dipalmitoylphosphatidylcholine J Lipid Res 40 11 1999 1978 1989
    • (1999) J Lipid Res , vol.40 , Issue.11 , pp. 1978-1989
    • Carrer, D.C.1    Maggio, B.2
  • 25
    • 34548629303 scopus 로고    scopus 로고
    • Formation of ceramide/sphingomyelin gel domains in the presence of an unsaturated phospholipid: A quantitative multiprobe approach
    • B.M. Castro, R.F. de Almeida, L.C. Silva, A. Fedorov, and M. Prieto Formation of ceramide/sphingomyelin gel domains in the presence of an unsaturated phospholipid: a quantitative multiprobe approach Biophys J 93 5 2007 1639 1650
    • (2007) Biophys J , vol.93 , Issue.5 , pp. 1639-1650
    • Castro, B.M.1    De Almeida, R.F.2    Silva, L.C.3    Fedorov, A.4    Prieto, M.5
  • 26
    • 73649100926 scopus 로고    scopus 로고
    • Sphingomyelinase-induced phase transformations: Causing morphology switches and multiple-time-domain ceramide generation in model raft membranes
    • L. Chao, A.P. Gast, T.A. Hatton, and K.F. Jensen Sphingomyelinase-induced phase transformations: causing morphology switches and multiple-time-domain ceramide generation in model raft membranes Langmuir 26 1 2010 344 356
    • (2010) Langmuir , vol.26 , Issue.1 , pp. 344-356
    • Chao, L.1    Gast, A.P.2    Hatton, T.A.3    Jensen, K.F.4
  • 27
    • 65449116519 scopus 로고    scopus 로고
    • Listeria monocytogenes phosphatidylinositol-specific phospholipase C: Kinetic activation and homing in on different interfaces
    • W. Chen, H. Goldfine, B. Ananthanarayanan, W. Cho, and M.F. Roberts Listeria monocytogenes phosphatidylinositol-specific phospholipase C: kinetic activation and homing in on different interfaces Biochemistry 48 16 2009 3578 3592
    • (2009) Biochemistry , vol.48 , Issue.16 , pp. 3578-3592
    • Chen, W.1    Goldfine, H.2    Ananthanarayanan, B.3    Cho, W.4    Roberts, M.F.5
  • 28
    • 0030586161 scopus 로고    scopus 로고
    • Non-bilayer lipids and biological fusion intermediates
    • L. Chernomordik Non-bilayer lipids and biological fusion intermediates Chem Phys Lipids 81 2 1996 203 213
    • (1996) Chem Phys Lipids , vol.81 , Issue.2 , pp. 203-213
    • Chernomordik, L.1
  • 29
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • L.V. Chernomordik, and M.M. Kozlov Protein-lipid interplay in fusion and fission of biological membranes Annu Rev Biochem 72 2003 175 207
    • (2003) Annu Rev Biochem , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 30
  • 31
    • 0027310309 scopus 로고
    • Proteolytic fragments of phosphoinositide-specific phospholipase C-delta 1. Catalytic and membrane binding properties
    • M.E. Cifuentes, L. Honkanen, and M.J. Rebecchi Proteolytic fragments of phosphoinositide-specific phospholipase C-delta 1. Catalytic and membrane binding properties J Biol Chem 268 16 1993 11586 11593
    • (1993) J Biol Chem , vol.268 , Issue.16 , pp. 11586-11593
    • Cifuentes, M.E.1    Honkanen, L.2    Rebecchi, M.J.3
  • 33
    • 79954509850 scopus 로고    scopus 로고
    • The neutral sphingomyelinase family: Identifying biochemical connections
    • C.J. Clarke, B.X. Wu, and Y.A. Hannun The neutral sphingomyelinase family: identifying biochemical connections Adv Enzyme Regul 51 1 2011 51 58
    • (2011) Adv Enzyme Regul , vol.51 , Issue.1 , pp. 51-58
    • Clarke, C.J.1    Wu, B.X.2    Hannun, Y.A.3
  • 34
    • 0022830221 scopus 로고
    • Cloning and expression in Escherichia coli and Staphylococcus aureus of the beta-lysin determinant from Staphylococcus aureus: Evidence that bacteriophage conversion of beta-lysin activity is caused by insertional inactivation of the beta-lysin determinant
    • D.C. Coleman, J.P. Arbuthnott, H.M. Pomeroy, and T.H. Birkbeck Cloning and expression in Escherichia coli and Staphylococcus aureus of the beta-lysin determinant from Staphylococcus aureus: evidence that bacteriophage conversion of beta-lysin activity is caused by insertional inactivation of the beta-lysin determinant Microb Pathog 1 6 1986 549 564
    • (1986) Microb Pathog , vol.1 , Issue.6 , pp. 549-564
    • Coleman, D.C.1    Arbuthnott, J.P.2    Pomeroy, H.M.3    Birkbeck, T.H.4
  • 35
    • 11244299268 scopus 로고    scopus 로고
    • Asymmetric addition of ceramides but not dihydroceramides promotes transbilayer (flip-flop) lipid motion in membranes
    • F.X. Contreras, G. Basanez, A. Alonso, A. Herrmann, and F.M. Goni Asymmetric addition of ceramides but not dihydroceramides promotes transbilayer (flip-flop) lipid motion in membranes Biophys J 88 1 2005 348 359
    • (2005) Biophys J , vol.88 , Issue.1 , pp. 348-359
    • Contreras, F.X.1    Basanez, G.2    Alonso, A.3    Herrmann, A.4    Goni, F.M.5
  • 36
    • 77951931341 scopus 로고    scopus 로고
    • Transbilayer (flip-flop) lipid motion and lipid scrambling in membranes
    • F.X. Contreras, L. Sanchez-Magraner, A. Alonso, and F.M. Goni Transbilayer (flip-flop) lipid motion and lipid scrambling in membranes FEBS Lett 584 9 2010 1779 1786
    • (2010) FEBS Lett , vol.584 , Issue.9 , pp. 1779-1786
    • Contreras, F.X.1    Sanchez-Magraner, L.2    Alonso, A.3    Goni, F.M.4
  • 37
    • 33744924717 scopus 로고    scopus 로고
    • Sphingosine increases the permeability of model and cell membranes
    • F.X. Contreras, J. Sot, A. Alonso, and F.M. Goni Sphingosine increases the permeability of model and cell membranes Biophys J 90 11 2006 4085 4092
    • (2006) Biophys J , vol.90 , Issue.11 , pp. 4085-4092
    • Contreras, F.X.1    Sot, J.2    Alonso, A.3    Goni, F.M.4
  • 38
    • 2542473164 scopus 로고    scopus 로고
    • Cholesterol modulation of sphingomyelinase activity at physiological temperatures
    • F.X. Contreras, J. Sot, M.B. Ruiz-Arguello, A. Alonso, and F.M. Goni Cholesterol modulation of sphingomyelinase activity at physiological temperatures Chem Phys Lipids 130 2 2004 127 134
    • (2004) Chem Phys Lipids , vol.130 , Issue.2 , pp. 127-134
    • Contreras, F.X.1    Sot, J.2    Ruiz-Arguello, M.B.3    Alonso, A.4    Goni, F.M.5
  • 39
    • 0141510031 scopus 로고    scopus 로고
    • Sphingomyelinase activity causes transbilayer lipid translocation in model and cell membranes
    • F.X. Contreras, A.V. Villar, A. Alonso, R.N. Kolesnick, and F.M. Goni Sphingomyelinase activity causes transbilayer lipid translocation in model and cell membranes J Biol Chem 278 39 2003 37169 37174
    • (2003) J Biol Chem , vol.278 , Issue.39 , pp. 37169-37174
    • Contreras, F.X.1    Villar, A.V.2    Alonso, A.3    Kolesnick, R.N.4    Goni, F.M.5
  • 40
    • 0037201936 scopus 로고    scopus 로고
    • Role of sphingomyelinase and ceramide in modulating rafts: Do biophysical properties determine biologic outcome?
    • A.E. Cremesti, F.M. Goni, and R. Kolesnick Role of sphingomyelinase and ceramide in modulating rafts: do biophysical properties determine biologic outcome? FEBS Lett 531 1 2002 47 53
    • (2002) FEBS Lett , vol.531 , Issue.1 , pp. 47-53
    • Cremesti, A.E.1    Goni, F.M.2    Kolesnick, R.3
  • 41
    • 0029944209 scopus 로고    scopus 로고
    • Inhibition by gangliosides of Bacillus cereus phospholipase C activity against monolayers, micelles and bilayer vesicles
    • J.J. Daniele, B. Maggio, I.D. Bianco, F.M. Goni, A. Alonso, and G.D. Fidelio Inhibition by gangliosides of Bacillus cereus phospholipase C activity against monolayers, micelles and bilayer vesicles Eur J Biochem 239 1 1996 105 110
    • (1996) Eur J Biochem , vol.239 , Issue.1 , pp. 105-110
    • Daniele, J.J.1    Maggio, B.2    Bianco, I.D.3    Goni, F.M.4    Alonso, A.5    Fidelio, G.D.6
  • 42
    • 70449309739 scopus 로고
    • The activation of surface films of lecithin by amphipathic molecules
    • R.M. Dawson, and A.D. Bangham The activation of surface films of lecithin by amphipathic molecules Biochem J 72 1959 493 496
    • (1959) Biochem J , vol.72 , pp. 493-496
    • Dawson, R.M.1    Bangham, A.D.2
  • 43
    • 0021737878 scopus 로고
    • Long-chain unsaturated diacylglycerols cause a perturbation in the structure of phospholipid bilayers rendering them susceptible to phospholipase attack
    • R.M. Dawson, R.F. Irvine, J. Bray, and P.J. Quinn Long-chain unsaturated diacylglycerols cause a perturbation in the structure of phospholipid bilayers rendering them susceptible to phospholipase attack Biochem Biophys Res Commun 125 2 1984 836 842
    • (1984) Biochem Biophys Res Commun , vol.125 , Issue.2 , pp. 836-842
    • Dawson, R.M.1    Irvine, R.F.2    Bray, J.3    Quinn, P.J.4
  • 44
    • 0141642121 scopus 로고    scopus 로고
    • Sphingomyelin/phosphatidylcholine/cholesterol phase diagram: Boundaries and composition of lipid rafts
    • R.F. de Almeida, A. Fedorov, and M. Prieto Sphingomyelin/ phosphatidylcholine/cholesterol phase diagram: boundaries and composition of lipid rafts Biophys J 85 4 2003 2406 2416
    • (2003) Biophys J , vol.85 , Issue.4 , pp. 2406-2416
    • De Almeida, R.F.1    Fedorov, A.2    Prieto, M.3
  • 45
    • 0031317790 scopus 로고    scopus 로고
    • Lipid polymorphism and biomembrane function
    • B. de Kruijff Lipid polymorphism and biomembrane function Curr Opin Chem Biol 1 4 1997 564 569
    • (1997) Curr Opin Chem Biol , vol.1 , Issue.4 , pp. 564-569
    • De Kruijff, B.1
  • 46
    • 33646489007 scopus 로고    scopus 로고
    • The pleckstrin homology domain of phospholipase Cbeta transmits enzymatic activation through modulation of the membrane-domain orientation
    • G. Drin, D. Douguet, and S. Scarlata The pleckstrin homology domain of phospholipase Cbeta transmits enzymatic activation through modulation of the membrane-domain orientation Biochemistry 45 18 2006 5712 5724
    • (2006) Biochemistry , vol.45 , Issue.18 , pp. 5712-5724
    • Drin, G.1    Douguet, D.2    Scarlata, S.3
  • 47
    • 34249317263 scopus 로고    scopus 로고
    • Stimulation of phospholipase Cbeta by membrane interactions, interdomain movement, and G protein binding-how many ways can you activate an enzyme?
    • G. Drin, and S. Scarlata Stimulation of phospholipase Cbeta by membrane interactions, interdomain movement, and G protein binding-how many ways can you activate an enzyme? Cell Signal 19 7 2007 1383 1392
    • (2007) Cell Signal , vol.19 , Issue.7 , pp. 1383-1392
    • Drin, G.1    Scarlata, S.2
  • 48
    • 33947197663 scopus 로고    scopus 로고
    • The epidemiology, pathogenesis and treatment of Pseudomonas aeruginosa infections
    • J.A. Driscoll, S.L. Brody, and M.H. Kollef The epidemiology, pathogenesis and treatment of Pseudomonas aeruginosa infections Drugs 67 3 2007 351 368
    • (2007) Drugs , vol.67 , Issue.3 , pp. 351-368
    • Driscoll, J.A.1    Brody, S.L.2    Kollef, M.H.3
  • 49
    • 0019977989 scopus 로고
    • Clostridium perfringens type A enterotoxin: Characterization of the amino-terminal region
    • L.K. Duffy, J.L. McDonel, B.A. McClane, and A. Kurosky Clostridium perfringens type A enterotoxin: characterization of the amino-terminal region Infection Immunity 38 1 1982 386 388
    • (1982) Infection Immunity , vol.38 , Issue.1 , pp. 386-388
    • Duffy, L.K.1    McDonel, J.L.2    McClane, B.A.3    Kurosky, A.4
  • 50
    • 77957861153 scopus 로고    scopus 로고
    • Spatial regulation of membrane fusion controlled by modification of phosphoinositides
    • F. Dumas, R.D. Byrne, B. Vincent, T.M. Hobday, D.L. Poccia, and B. Larijani Spatial regulation of membrane fusion controlled by modification of phosphoinositides PLoS One 5 8 2010 e12208
    • (2010) PLoS One , vol.5 , Issue.8 , pp. 12208
    • Dumas, F.1    Byrne, R.D.2    Vincent, B.3    Hobday, T.M.4    Poccia, D.L.5    Larijani, B.6
  • 51
    • 0021890825 scopus 로고
    • 2+-induced fusion and destabilization of liposomes
    • 2+-induced fusion and destabilization of liposomes Biochemistry 24 13 1985 3099 3106
    • (1985) Biochemistry , vol.24 , Issue.13 , pp. 3099-3106
    • Ellens, H.1    Bentz, J.2    Szoka, F.C.3
  • 52
    • 0022418382 scopus 로고
    • Diacylglycerols, lysolecithin, or hydrocarbons markedly alter the bilayer to hexagonal phase transition temperature of phosphatidylethanolamines
    • R.M. Epand Diacylglycerols, lysolecithin, or hydrocarbons markedly alter the bilayer to hexagonal phase transition temperature of phosphatidylethanolamines Biochemistry 24 25 1985 7092 7095
    • (1985) Biochemistry , vol.24 , Issue.25 , pp. 7092-7095
    • Epand, R.M.1
  • 53
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta
    • L.O. Essen, O. Perisic, R. Cheung, M. Katan, and R.L. Williams Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta Nature 380 6575 1996 595 602
    • (1996) Nature , vol.380 , Issue.6575 , pp. 595-602
    • Essen, L.O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 54
    • 79952256065 scopus 로고    scopus 로고
    • Membrane environment exerts an important influence on rac-mediated activation of phospholipase Cgamma2
    • K.L. Everett, A. Buehler, T.D. Bunney, A. Margineanu, R.W. Baxendale, and P. Vatter Membrane environment exerts an important influence on rac-mediated activation of phospholipase Cgamma2 Mol Cell Biol 31 6 2011 1240 1251
    • (2011) Mol Cell Biol , vol.31 , Issue.6 , pp. 1240-1251
    • Everett, K.L.1    Buehler, A.2    Bunney, T.D.3    Margineanu, A.4    Baxendale, R.W.5    Vatter, P.6
  • 55
    • 58849111812 scopus 로고    scopus 로고
    • Sphingomyelinase-induced domain shape relaxation driven by out-of-equilibrium changes of composition
    • M.L. Fanani, L. De Tullio, S. Hartel, J. Jara, and B. Maggio Sphingomyelinase-induced domain shape relaxation driven by out-of-equilibrium changes of composition Biophys J 96 1 2009 67 76
    • (2009) Biophys J , vol.96 , Issue.1 , pp. 67-76
    • Fanani, M.L.1    De Tullio, L.2    Hartel, S.3    Jara, J.4    Maggio, B.5
  • 56
    • 77954731500 scopus 로고    scopus 로고
    • The action of sphingomyelinase in lipid monolayers as revealed by microscopic image analysis
    • M.L. Fanani, S. Hartel, B. Maggio, L. De Tullio, J. Jara, and F. Olmos The action of sphingomyelinase in lipid monolayers as revealed by microscopic image analysis Biochim Biophys Acta 1798 7 2010 1309 1323
    • (2010) Biochim Biophys Acta , vol.1798 , Issue.7 , pp. 1309-1323
    • Fanani, M.L.1    Hartel, S.2    Maggio, B.3    De Tullio, L.4    Jara, J.5    Olmos, F.6
  • 57
    • 0036924185 scopus 로고    scopus 로고
    • Bidirectional control of sphingomyelinase activity and surface topography in lipid monolayers
    • M.L. Fanani, S. Hartel, R.G. Oliveira, and B. Maggio Bidirectional control of sphingomyelinase activity and surface topography in lipid monolayers Biophys J 83 6 2002 3416 3424
    • (2002) Biophys J , vol.83 , Issue.6 , pp. 3416-3424
    • Fanani, M.L.1    Hartel, S.2    Oliveira, R.G.3    Maggio, B.4
  • 58
    • 0031797186 scopus 로고    scopus 로고
    • Surface pressure-dependent cross-modulation of sphingomyelinase and phospholipase A2 in monolayers
    • M.L. Fanani, and B. Maggio Surface pressure-dependent cross-modulation of sphingomyelinase and phospholipase A2 in monolayers Lipids 33 11 1998 1079 1087
    • (1998) Lipids , vol.33 , Issue.11 , pp. 1079-1087
    • Fanani, M.L.1    Maggio, B.2
  • 59
    • 33750246866 scopus 로고    scopus 로고
    • Phase behavior of lipid mixtures
    • G.W. Feigenson Phase behavior of lipid mixtures Nat Chem Biol 2 11 2006 560 563
    • (2006) Nat Chem Biol , vol.2 , Issue.11 , pp. 560-563
    • Feigenson, G.W.1
  • 60
    • 0043092111 scopus 로고    scopus 로고
    • Optimizing the interfacial binding and activity of a bacterial phosphatidylinositol-specific phospholipase C
    • J. Feng, W.D. Bradley, and M.F. Roberts Optimizing the interfacial binding and activity of a bacterial phosphatidylinositol-specific phospholipase C J Biol Chem 278 27 2003 24651 24657
    • (2003) J Biol Chem , vol.278 , Issue.27 , pp. 24651-24657
    • Feng, J.1    Bradley, W.D.2    Roberts, M.F.3
  • 61
    • 0037205478 scopus 로고    scopus 로고
    • Role of tryptophan residues in interfacial binding of phosphatidylinositol-specific phospholipase C
    • J. Feng, H. Wehbi, and M.F. Roberts Role of tryptophan residues in interfacial binding of phosphatidylinositol-specific phospholipase C J Biol Chem 277 22 2002 19867 19875
    • (2002) J Biol Chem , vol.277 , Issue.22 , pp. 19867-19875
    • Feng, J.1    Wehbi, H.2    Roberts, M.F.3
  • 62
    • 0036645698 scopus 로고    scopus 로고
    • Biochemical identification of a neutral sphingomyelinase 1 (NSM1)-like enzyme as the major NSM activity in the DT40 B-cell line: Absence of a role in the apoptotic response to endoplasmic reticulum stress
    • A.C. Fensome, M. Josephs, M. Katan, and F. Rodrigues-Lima Biochemical identification of a neutral sphingomyelinase 1 (NSM1)-like enzyme as the major NSM activity in the DT40 B-cell line: absence of a role in the apoptotic response to endoplasmic reticulum stress Biochem J 365 Pt. 1 2002 69 77
    • (2002) Biochem J , vol.365 , Issue.PART 1 , pp. 69-77
    • Fensome, A.C.1    Josephs, M.2    Katan, M.3    Rodrigues-Lima, F.4
  • 63
    • 1042298781 scopus 로고    scopus 로고
    • Role of Clostridium perfringens phospholipase C in the pathogenesis of gas gangrene
    • M. Flores-Diaz, and A. Alape-Giron Role of Clostridium perfringens phospholipase C in the pathogenesis of gas gangrene Toxicon 42 8 2003 979 986
    • (2003) Toxicon , vol.42 , Issue.8 , pp. 979-986
    • Flores-Diaz, M.1    Alape-Giron, A.2
  • 64
    • 22844442011 scopus 로고    scopus 로고
    • A cellular deficiency of gangliosides causes hypersensitivity to Clostridium perfringens phospholipase C
    • M. Flores-Diaz, A. Alape-Giron, G. Clark, B. Catimel, Y. Hirabayashi, and E. Nice A cellular deficiency of gangliosides causes hypersensitivity to Clostridium perfringens phospholipase C J Biol Chem 280 29 2005 26680 26689
    • (2005) J Biol Chem , vol.280 , Issue.29 , pp. 26680-26689
    • Flores-Diaz, M.1    Alape-Giron, A.2    Clark, G.3    Catimel, B.4    Hirabayashi, Y.5    Nice, E.6
  • 65
    • 77956392921 scopus 로고    scopus 로고
    • Phospholipase C is a key enzyme regulating intracellular calcium and modulating the phosphoinositide balance
    • K. Fukami, S. Inanobe, K. Kanemaru, and Y. Nakamura Phospholipase C is a key enzyme regulating intracellular calcium and modulating the phosphoinositide balance Prog Lipid Res 49 4 2010 429 437
    • (2010) Prog Lipid Res , vol.49 , Issue.4 , pp. 429-437
    • Fukami, K.1    Inanobe, S.2    Kanemaru, K.3    Nakamura, Y.4
  • 66
    • 0028787055 scopus 로고
    • The pleckstrin homology domain of phospholipase C-delta 1 binds with high affinity to phosphatidylinositol 4,5-bisphosphate in bilayer membranes
    • P. Garcia, R. Gupta, S. Shah, A.J. Morris, S.A. Rudge, and S. Scarlata The pleckstrin homology domain of phospholipase C-delta 1 binds with high affinity to phosphatidylinositol 4,5-bisphosphate in bilayer membranes Biochemistry 34 49 1995 16228 16234
    • (1995) Biochemistry , vol.34 , Issue.49 , pp. 16228-16234
    • Garcia, P.1    Gupta, R.2    Shah, S.3    Morris, A.J.4    Rudge, S.A.5    Scarlata, S.6
  • 67
    • 0015924569 scopus 로고
    • Hydrolysis of sphingomyelin liposomes by sphingomyelinase
    • S. Gatt, A. Herzl, and Y. Barenholz Hydrolysis of sphingomyelin liposomes by sphingomyelinase FEBS Lett 30 3 1973 281 285
    • (1973) FEBS Lett , vol.30 , Issue.3 , pp. 281-285
    • Gatt, S.1    Herzl, A.2    Barenholz, Y.3
  • 68
    • 0025851289 scopus 로고
    • Purification and characterization of an extracellular 29-kilodalton phospholipase C from Listeria monocytogenes
    • C. Geoffroy, J. Raveneau, J.L. Beretti, A. Lecroisey, J.A. Vazquez-Boland, and J.E. Alouf Purification and characterization of an extracellular 29-kilodalton phospholipase C from Listeria monocytogenes Infect Immun 59 7 1991 2382 2388
    • (1991) Infect Immun , vol.59 , Issue.7 , pp. 2382-2388
    • Geoffroy, C.1    Raveneau, J.2    Beretti, J.L.3    Lecroisey, A.4    Vazquez-Boland, J.A.5    Alouf, J.E.6
  • 69
    • 0027303320 scopus 로고
    • Nonspecific phospholipase C of Listeria monocytogenes: Activity on phospholipids in Triton X-100-mixed micelles and in biological membranes
    • H. Goldfine, N.C. Johnston, and C. Knob Nonspecific phospholipase C of Listeria monocytogenes: activity on phospholipids in Triton X-100-mixed micelles and in biological membranes J Bacteriol 175 14 1993 4298 4306
    • (1993) J Bacteriol , vol.175 , Issue.14 , pp. 4298-4306
    • Goldfine, H.1    Johnston, N.C.2    Knob, C.3
  • 70
    • 44949238672 scopus 로고    scopus 로고
    • Diffusion coefficient of fluorescent phosphatidylinositol 4,5-bisphosphate in the plasma membrane of cells
    • U. Golebiewska, M. Nyako, W. Woturski, I. Zaitseva, and S. McLaughlin Diffusion coefficient of fluorescent phosphatidylinositol 4,5-bisphosphate in the plasma membrane of cells Mol Biol Cell 19 4 2008 1663 1669
    • (2008) Mol Biol Cell , vol.19 , Issue.4 , pp. 1663-1669
    • Golebiewska, U.1    Nyako, M.2    Woturski, W.3    Zaitseva, I.4    McLaughlin, S.5
  • 71
    • 0842282983 scopus 로고    scopus 로고
    • Ceramide-1-phosphate blocks apoptosis through inhibition of acid sphingomyelinase in macrophages
    • A. Gomez-Munoz, J.Y. Kong, B. Salh, and U.P. Steinbrecher Ceramide-1-phosphate blocks apoptosis through inhibition of acid sphingomyelinase in macrophages J Lipid Res 45 1 2004 99 105
    • (2004) J Lipid Res , vol.45 , Issue.1 , pp. 99-105
    • Gomez-Munoz, A.1    Kong, J.Y.2    Salh, B.3    Steinbrecher, U.P.4
  • 72
    • 0039518668 scopus 로고    scopus 로고
    • Structure and functional properties of diacylglycerols in membranes
    • F.M. Goni, and A. Alonso Structure and functional properties of diacylglycerols in membranes Prog Lipid Res 38 1 1999 1 48
    • (1999) Prog Lipid Res , vol.38 , Issue.1 , pp. 1-48
    • Goni, F.M.1    Alonso, A.2
  • 73
    • 0034442596 scopus 로고    scopus 로고
    • Membrane fusion induced by phospholipase C and sphingomyelinases
    • F.M. Goni, and A. Alonso Membrane fusion induced by phospholipase C and sphingomyelinases Biosci Rep 20 6 2000 443 463
    • (2000) Biosci Rep , vol.20 , Issue.6 , pp. 443-463
    • Goni, F.M.1    Alonso, A.2
  • 74
    • 0034707090 scopus 로고    scopus 로고
    • Spectroscopic techniques in the study of membrane solubilization, reconstitution and permeabilization by detergents
    • F.M. Goni, and A. Alonso Spectroscopic techniques in the study of membrane solubilization, reconstitution and permeabilization by detergents Biochim Biophys Acta 1508 1-2 2000 51 68
    • (2000) Biochim Biophys Acta , vol.1508 , Issue.12 , pp. 51-68
    • Goni, F.M.1    Alonso, A.2
  • 75
    • 0037201939 scopus 로고    scopus 로고
    • Sphingomyelinases: Enzymology and membrane activity
    • F.M. Goni, and A. Alonso Sphingomyelinases: enzymology and membrane activity FEBS Lett 531 1 2002 38 46
    • (2002) FEBS Lett , vol.531 , Issue.1 , pp. 38-46
    • Goni, F.M.1    Alonso, A.2
  • 76
    • 33845346790 scopus 로고    scopus 로고
    • Biophysics of sphingolipids I. Membrane properties of sphingosine, ceramides and other simple sphingolipids
    • F.M. Goni, and A. Alonso Biophysics of sphingolipids I. Membrane properties of sphingosine, ceramides and other simple sphingolipids Biochim Biophys Acta 1758 12 2006 1902 1921
    • (2006) Biochim Biophys Acta , vol.1758 , Issue.12 , pp. 1902-1921
    • Goni, F.M.1    Alonso, A.2
  • 77
    • 58149188064 scopus 로고    scopus 로고
    • Effects of ceramide and other simple sphingolipids on membrane lateral structure
    • F.M. Goni, and A. Alonso Effects of ceramide and other simple sphingolipids on membrane lateral structure Biochim Biophys Acta 1788 1 2009 169 177
    • (2009) Biochim Biophys Acta , vol.1788 , Issue.1 , pp. 169-177
    • Goni, F.M.1    Alonso, A.2
  • 78
    • 0042335762 scopus 로고    scopus 로고
    • Ceramide-mediated clustering is required for CD95-DISC formation
    • H. Grassme, A. Cremesti, R. Kolesnick, and E. Gulbins Ceramide-mediated clustering is required for CD95-DISC formation Oncogene 22 35 2003 5457 5470
    • (2003) Oncogene , vol.22 , Issue.35 , pp. 5457-5470
    • Grassme, H.1    Cremesti, A.2    Kolesnick, R.3    Gulbins, E.4
  • 79
    • 0030775369 scopus 로고    scopus 로고
    • Acidic sphingomyelinase mediates entry of N gonorrhoeae into nonphagocytic cells
    • H. Grassme, E. Gulbins, B. Brenner, K. Ferlinz, K. Sandhoff, and K. Harzer Acidic sphingomyelinase mediates entry of N gonorrhoeae into nonphagocytic cells Cell 91 5 1997 605 615
    • (1997) Cell , vol.91 , Issue.5 , pp. 605-615
    • Grassme, H.1    Gulbins, E.2    Brenner, B.3    Ferlinz, K.4    Sandhoff, K.5    Harzer, K.6
  • 80
    • 0035179629 scopus 로고    scopus 로고
    • Molecular mechanisms of bacteria induced apoptosis
    • H. Grassme, V. Jendrossek, and E. Gulbins Molecular mechanisms of bacteria induced apoptosis Apoptosis 6 6 2001 441 445
    • (2001) Apoptosis , vol.6 , Issue.6 , pp. 441-445
    • Grassme, H.1    Jendrossek, V.2    Gulbins, E.3
  • 81
    • 0032698808 scopus 로고    scopus 로고
    • Bacterial phosphatidylinositol-specific phospholipase C: Structure, function, and interaction with lipids
    • O.H. Griffith, and M. Ryan Bacterial phosphatidylinositol-specific phospholipase C: structure, function, and interaction with lipids Biochim Biophys Acta 1441 2-3 1999 237 254
    • (1999) Biochim Biophys Acta , vol.1441 , Issue.23 , pp. 237-254
    • Griffith, O.H.1    Ryan, M.2
  • 82
    • 0029976468 scopus 로고    scopus 로고
    • Use of site-directed mutagenesis to probe structure-function relationships of alpha-toxin from Clostridium perfringens
    • I. Guillouard, T. Garnier, and S.T. Cole Use of site-directed mutagenesis to probe structure-function relationships of alpha-toxin from Clostridium perfringens Infect Immun 64 7 1996 2440 2444
    • (1996) Infect Immun , vol.64 , Issue.7 , pp. 2440-2444
    • Guillouard, I.1    Garnier, T.2    Cole, S.T.3
  • 83
    • 41849084510 scopus 로고    scopus 로고
    • Role of helix B residues in interfacial activation of a bacterial phosphatidylinositol-specific phospholipase C
    • S. Guo, X. Zhang, B.A. Seaton, and M.F. Roberts Role of helix B residues in interfacial activation of a bacterial phosphatidylinositol-specific phospholipase C Biochemistry 47 14 2008 4201 4210
    • (2008) Biochemistry , vol.47 , Issue.14 , pp. 4201-4210
    • Guo, S.1    Zhang, X.2    Seaton, B.A.3    Roberts, M.F.4
  • 84
    • 77950473766 scopus 로고    scopus 로고
    • Differential regulation of phospholipase C-beta2 activity and membrane interaction by Galphaq, Gbeta1gamma2, and Rac2
    • O. Gutman, C. Walliser, T. Piechulek, P. Gierschik, and Y.I. Henis Differential regulation of phospholipase C-beta2 activity and membrane interaction by Galphaq, Gbeta1gamma2, and Rac2 J Biol Chem 285 6 2010 3905 3915
    • (2010) J Biol Chem , vol.285 , Issue.6 , pp. 3905-3915
    • Gutman, O.1    Walliser, C.2    Piechulek, T.3    Gierschik, P.4    Henis, Y.I.5
  • 85
    • 80052010597 scopus 로고    scopus 로고
    • A dynamic model of membrane-bound phospholipase Cbeta2 activation by Gbetagamma subunits
    • D.S. Han, U. Golebiewska, S. Stolzenberg, S.F. Scarlata, and H. Weinstein A dynamic model of membrane-bound phospholipase Cbeta2 activation by Gbetagamma subunits Mol Pharmacol 80 3 2011 434 445
    • (2011) Mol Pharmacol , vol.80 , Issue.3 , pp. 434-445
    • Han, D.S.1    Golebiewska, U.2    Stolzenberg, S.3    Scarlata, S.F.4    Weinstein, H.5
  • 86
    • 1642359646 scopus 로고    scopus 로고
    • Roles of curvature and hydrophobic interstice energy in fusion: Studies of lipid perturbant effects
    • M.E. Haque, and B.R. Lentz Roles of curvature and hydrophobic interstice energy in fusion: studies of lipid perturbant effects Biochemistry 43 12 2004 3507 3517
    • (2004) Biochemistry , vol.43 , Issue.12 , pp. 3507-3517
    • Haque, M.E.1    Lentz, B.R.2
  • 87
    • 66349113776 scopus 로고    scopus 로고
    • Phospholipase C isozymes as effectors of Ras superfamily GTPases
    • T.K. Harden, S.N. Hicks, and J. Sondek Phospholipase C isozymes as effectors of Ras superfamily GTPases J Lipid Res 50 Suppl. 2009 S243 S248
    • (2009) J Lipid Res , vol.50 , Issue.SUPPL.
    • Harden, T.K.1    Hicks, S.N.2    Sondek, J.3
  • 88
    • 11244344327 scopus 로고    scopus 로고
    • Shape transitions and lattice structuring of ceramide-enriched domains generated by sphingomyelinase in lipid monolayers
    • S. Hartel, M.L. Fanani, and B. Maggio Shape transitions and lattice structuring of ceramide-enriched domains generated by sphingomyelinase in lipid monolayers Biophys J 88 1 2005 287 304
    • (2005) Biophys J , vol.88 , Issue.1 , pp. 287-304
    • Hartel, S.1    Fanani, M.L.2    Maggio, B.3
  • 89
    • 0032579314 scopus 로고    scopus 로고
    • Structural and mechanistic comparison of prokaryotic and eukaryotic phosphoinositide-specific phospholipases C
    • D.W. Heinz, L.O. Essen, and R.L. Williams Structural and mechanistic comparison of prokaryotic and eukaryotic phosphoinositide-specific phospholipases C J Mol Biol 275 4 1998 635 650
    • (1998) J Mol Biol , vol.275 , Issue.4 , pp. 635-650
    • Heinz, D.W.1    Essen, L.O.2    Williams, R.L.3
  • 90
    • 0029121937 scopus 로고
    • Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol
    • D.W. Heinz, M. Ryan, T.L. Bullock, and O.H. Griffith Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol EMBO J 14 16 1995 3855 3863
    • (1995) EMBO J , vol.14 , Issue.16 , pp. 3855-3863
    • Heinz, D.W.1    Ryan, M.2    Bullock, T.L.3    Griffith, O.H.4
  • 91
    • 0029740871 scopus 로고    scopus 로고
    • Crystal structure of phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with glucosaminyl(alpha 1 → 6)-d-myo-inositol, an essential fragment of GPI anchors
    • D.W. Heinz, M. Ryan, M.P. Smith, L.H. Weaver, J.F. Keana, and O.H. Griffith Crystal structure of phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with glucosaminyl(alpha 1 → 6)-d-myo-inositol, an essential fragment of GPI anchors Biochemistry 35 29 1996 9496 9504
    • (1996) Biochemistry , vol.35 , Issue.29 , pp. 9496-9504
    • Heinz, D.W.1    Ryan, M.2    Smith, M.P.3    Weaver, L.H.4    Keana, J.F.5    Griffith, O.H.6
  • 92
    • 0026733844 scopus 로고
    • Kinetics of Bacillus cereus phosphatidylinositol-specific phospholipase C with thiophosphate and fluorescent analogs of phosphatidylinositol
    • H.S. Hendrickson, E.K. Hendrickson, J.L. Johnson, T.H. Khan, and H.J. Chial Kinetics of Bacillus cereus phosphatidylinositol-specific phospholipase C with thiophosphate and fluorescent analogs of phosphatidylinositol Biochemistry 31 48 1992 12169 12172
    • (1992) Biochemistry , vol.31 , Issue.48 , pp. 12169-12172
    • Hendrickson, H.S.1    Hendrickson, E.K.2    Johnson, J.L.3    Khan, T.H.4    Chial, H.J.5
  • 93
    • 79951581102 scopus 로고    scopus 로고
    • Characterization of inositol phospho-sphingolipid-phospholipase C 1 (Isc1) in Cryptococcus neoformans reveals unique biochemical features
    • J. Henry, A. Guillotte, C. Luberto, and M. Del Poeta Characterization of inositol phospho-sphingolipid-phospholipase C 1 (Isc1) in Cryptococcus neoformans reveals unique biochemical features FEBS Lett 585 4 2011 635 640
    • (2011) FEBS Lett , vol.585 , Issue.4 , pp. 635-640
    • Henry, J.1    Guillotte, A.2    Luberto, C.3    Del Poeta, M.4
  • 96
    • 0037150709 scopus 로고    scopus 로고
    • Pseudomonas-Candida interactions: An ecological role for virulence factors
    • D.A. Hogan, and R. Kolter Pseudomonas-Candida interactions: an ecological role for virulence factors Science 296 5576 2002 2229 2232
    • (2002) Science , vol.296 , Issue.5576 , pp. 2229-2232
    • Hogan, D.A.1    Kolter, R.2
  • 97
    • 0034087155 scopus 로고    scopus 로고
    • Vectorial budding of vesicles by asymmetrical enzymatic formation of ceramide in giant liposomes
    • J.M. Holopainen, M.I. Angelova, and P.K. Kinnunen Vectorial budding of vesicles by asymmetrical enzymatic formation of ceramide in giant liposomes Biophys J 78 2 2000 830 838
    • (2000) Biophys J , vol.78 , Issue.2 , pp. 830-838
    • Holopainen, J.M.1    Angelova, M.I.2    Kinnunen, P.K.3
  • 98
    • 0030868488 scopus 로고    scopus 로고
    • Lipid microdomains in dimyristoylphosphatidylcholine-ceramide liposomes
    • J.M. Holopainen, J.Y. Lehtonen, and P.K. Kinnunen Lipid microdomains in dimyristoylphosphatidylcholine-ceramide liposomes Chem Phys Lipids 88 1 1997 1 13
    • (1997) Chem Phys Lipids , vol.88 , Issue.1 , pp. 1-13
    • Holopainen, J.M.1    Lehtonen, J.Y.2    Kinnunen, P.K.3
  • 99
    • 0032535156 scopus 로고    scopus 로고
    • Sphingomyelinase induces lipid microdomain formation in a fluid phosphatidylcholine/sphingomyelin membrane
    • J.M. Holopainen, M. Subramanian, and P.K. Kinnunen Sphingomyelinase induces lipid microdomain formation in a fluid phosphatidylcholine/sphingomyelin membrane Biochemistry 37 50 1998 17562 17570
    • (1998) Biochemistry , vol.37 , Issue.50 , pp. 17562-17570
    • Holopainen, J.M.1    Subramanian, M.2    Kinnunen, P.K.3
  • 100
    • 0024976936 scopus 로고
    • High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus
    • E. Hough, L.K. Hansen, B. Birknes, K. Jynge, S. Hansen, and A. Hordvik High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus Nature 338 6213 1989 357 360
    • (1989) Nature , vol.338 , Issue.6213 , pp. 357-360
    • Hough, E.1    Hansen, L.K.2    Birknes, B.3    Jynge, K.4    Hansen, S.5    Hordvik, A.6
  • 101
    • 0029950232 scopus 로고    scopus 로고
    • Ceramide induces structural defects into phosphatidylcholine bilayers and activates phospholipase A2
    • H.W. Huang, E.M. Goldberg, and R. Zidovetzki Ceramide induces structural defects into phosphatidylcholine bilayers and activates phospholipase A2 Biochem Biophys Res Commun 220 3 1996 834 838
    • (1996) Biochem Biophys Res Commun , vol.220 , Issue.3 , pp. 834-838
    • Huang, H.W.1    Goldberg, E.M.2    Zidovetzki, R.3
  • 102
    • 0031851644 scopus 로고    scopus 로고
    • Ceramides perturb the structure of phosphatidylcholine bilayers and modulate the activity of phospholipase A2
    • H.W. Huang, E.M. Goldberg, and R. Zidovetzki Ceramides perturb the structure of phosphatidylcholine bilayers and modulate the activity of phospholipase A2 Eur Biophys J 27 4 1998 361 366
    • (1998) Eur Biophys J , vol.27 , Issue.4 , pp. 361-366
    • Huang, H.W.1    Goldberg, E.M.2    Zidovetzki, R.3
  • 103
    • 0032817224 scopus 로고    scopus 로고
    • Ceramides modulate protein kinase C activity and perturb the structure of phosphatidylcholine/phosphatidylserine bilayers
    • H.W. Huang, E.M. Goldberg, and R. Zidovetzki Ceramides modulate protein kinase C activity and perturb the structure of phosphatidylcholine/ phosphatidylserine bilayers Biophys J 77 3 1999 1489 1497
    • (1999) Biophys J , vol.77 , Issue.3 , pp. 1489-1497
    • Huang, H.W.1    Goldberg, E.M.2    Zidovetzki, R.3
  • 104
    • 22144495354 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel phospholipase C, PLC-eta
    • J.I. Hwang, Y.S. Oh, K.J. Shin, H. Kim, S.H. Ryu, and P.G. Suh Molecular cloning and characterization of a novel phospholipase C, PLC-eta Biochem J 389 Pt. 1 2005 181 186
    • (2005) Biochem J , vol.389 , Issue.PART 1 , pp. 181-186
    • Hwang, J.I.1    Oh, Y.S.2    Shin, K.J.3    Kim, H.4    Ryu, S.H.5    Suh, P.G.6
  • 105
    • 71749086311 scopus 로고    scopus 로고
    • End-products diacylglycerol and ceramide modulate membrane fusion induced by a phospholipase C/sphingomyelinase from Pseudomonas aeruginosa
    • M. Ibarguren, P.H. Bomans, P.M. Frederik, M. Stonehouse, A.I. Vasil, and M.L. Vasil End-products diacylglycerol and ceramide modulate membrane fusion induced by a phospholipase C/sphingomyelinase from Pseudomonas aeruginosa Biochim Biophys Acta 1798 1 2010 59 64
    • (2010) Biochim Biophys Acta , vol.1798 , Issue.1 , pp. 59-64
    • Ibarguren, M.1    Bomans, P.H.2    Frederik, P.M.3    Stonehouse, M.4    Vasil, A.I.5    Vasil, M.L.6
  • 106
    • 79953293517 scopus 로고    scopus 로고
    • Imaging the early stages of phospholipase C/sphingomyelinase activity on vesicles containing coexisting ordered-disordered and gel-fluid domains
    • M. Ibarguren, D.J. Lopez, L.R. Montes, J. Sot, A.I. Vasil, and M.L. Vasil Imaging the early stages of phospholipase C/sphingomyelinase activity on vesicles containing coexisting ordered-disordered and gel-fluid domains J Lipid Res 52 4 2011 635 645
    • (2011) J Lipid Res , vol.52 , Issue.4 , pp. 635-645
    • Ibarguren, M.1    Lopez, D.J.2    Montes, L.R.3    Sot, J.4    Vasil, A.I.5    Vasil, M.L.6
  • 107
    • 0017086018 scopus 로고
    • Studies on phosphatidylinositol phosphodiesterase (phospholipase C type) of Bacillus cereus. I. purification, properties and phosphatase-releasing activity
    • H. Ikezawa, M. Yamanegi, R. Taguchi, T. Miyashita, and T. Ohyabu Studies on phosphatidylinositol phosphodiesterase (phospholipase C type) of Bacillus cereus. I. purification, properties and phosphatase-releasing activity Biochim Biophys Acta 450 2 1976 154 164
    • (1976) Biochim Biophys Acta , vol.450 , Issue.2 , pp. 154-164
    • Ikezawa, H.1    Yamanegi, M.2    Taguchi, R.3    Miyashita, T.4    Ohyabu, T.5
  • 109
    • 0029075004 scopus 로고
    • Kinetic analysis of phospholipase C beta isoforms using phospholipid-detergent mixed micelles. Evidence for interfacial catalysis involving distinct micelle binding and catalytic steps
    • S.R. James, A. Paterson, T.K. Harden, and C.P. Downes Kinetic analysis of phospholipase C beta isoforms using phospholipid-detergent mixed micelles. Evidence for interfacial catalysis involving distinct micelle binding and catalytic steps J Biol Chem 270 20 1995 11872 11881
    • (1995) J Biol Chem , vol.270 , Issue.20 , pp. 11872-11881
    • James, S.R.1    Paterson, A.2    Harden, T.K.3    Downes, C.P.4
  • 110
    • 0035957680 scopus 로고    scopus 로고
    • Tyrosine 331 and phenylalanine 334 in Clostridium perfringens alpha-toxin are essential for cytotoxic activity
    • M. Jepson, H.L. Bullifent, D. Crane, M. Flores-Diaz, A. Alape-Giron, and P. Jayasekeera Tyrosine 331 and phenylalanine 334 in Clostridium perfringens alpha-toxin are essential for cytotoxic activity FEBS Lett 495 3 2001 172 177
    • (2001) FEBS Lett , vol.495 , Issue.3 , pp. 172-177
    • Jepson, M.1    Bullifent, H.L.2    Crane, D.3    Flores-Diaz, M.4    Alape-Giron, A.5    Jayasekeera, P.6
  • 111
    • 0032967308 scopus 로고    scopus 로고
    • Differences in the carboxy-terminal (Putative phospholipid binding) domains of Clostridium perfringens and Clostridium bifermentans phospholipases C influence the hemolytic and lethal properties of these enzymes
    • M. Jepson, A. Howells, H.L. Bullifent, B. Bolgiano, D. Crane, and J. Miller Differences in the carboxy-terminal (Putative phospholipid binding) domains of Clostridium perfringens and Clostridium bifermentans phospholipases C influence the hemolytic and lethal properties of these enzymes Infect Immun 67 7 1999 3297 3301
    • (1999) Infect Immun , vol.67 , Issue.7 , pp. 3297-3301
    • Jepson, M.1    Howells, A.2    Bullifent, H.L.3    Bolgiano, B.4    Crane, D.5    Miller, J.6
  • 113
    • 11144351960 scopus 로고    scopus 로고
    • Phosphorylation of glycosyl-phosphatidylinositol by phosphatidylinositol 3-kinase changes its properties as a substrate for phospholipases
    • D.R. Jones, C. Paneda, A.V. Villar, A. Alonso, F.M. Goni, and P. Butikofer Phosphorylation of glycosyl-phosphatidylinositol by phosphatidylinositol 3-kinase changes its properties as a substrate for phospholipases FEBS Lett 579 1 2005 59 65
    • (2005) FEBS Lett , vol.579 , Issue.1 , pp. 59-65
    • Jones, D.R.1    Paneda, C.2    Villar, A.V.3    Alonso, A.4    Goni, F.M.5    Butikofer, P.6
  • 114
    • 0031576840 scopus 로고    scopus 로고
    • Interfacial regulation of bacterial sphingomyelinase activity
    • M. Jungner, H. Ohvo, and J.P. Slotte Interfacial regulation of bacterial sphingomyelinase activity Biochim Biophys Acta 1344 3 1997 230 240
    • (1997) Biochim Biophys Acta , vol.1344 , Issue.3 , pp. 230-240
    • Jungner, M.1    Ohvo, H.2    Slotte, J.P.3
  • 115
    • 33644840483 scopus 로고    scopus 로고
    • New insights into the families of PLC enzymes: Looking back and going forward
    • M. Katan New insights into the families of PLC enzymes: looking back and going forward Biochem J 391 Pt. 3 2005 e7 e9
    • (2005) Biochem J , vol.391 , Issue.PART 3
    • Katan, M.1
  • 116
    • 0023065884 scopus 로고
    • Phospholipase C and the physical states of polar head groups of lipids
    • Y. Kimura Phospholipase C and the physical states of polar head groups of lipids J Membr Biol 96 2 1987 187 191
    • (1987) J Membr Biol , vol.96 , Issue.2 , pp. 187-191
    • Kimura, Y.1
  • 117
    • 23744471645 scopus 로고    scopus 로고
    • Spectroscopic characterization of the EF-hand domain of phospholipase C delta1: Identification of a lipid interacting domain
    • M. Kobayashi, Z. Gryczynski, J. Lukomska, J. Feng, M.F. Roberts, and J.R. Lakowicz Spectroscopic characterization of the EF-hand domain of phospholipase C delta1: identification of a lipid interacting domain Arch Biochem Biophys 440 2 2005 191 203
    • (2005) Arch Biochem Biophys , vol.440 , Issue.2 , pp. 191-203
    • Kobayashi, M.1    Gryczynski, Z.2    Lukomska, J.3    Feng, J.4    Roberts, M.F.5    Lakowicz, J.R.6
  • 118
    • 0033884050 scopus 로고    scopus 로고
    • Compartmentalization of ceramide signaling: Physical foundations and biological effects
    • R.N. Kolesnick, F.M. Goni, and A. Alonso Compartmentalization of ceramide signaling: physical foundations and biological effects J Cell Physiol 184 3 2000 285 300
    • (2000) J Cell Physiol , vol.184 , Issue.3 , pp. 285-300
    • Kolesnick, R.N.1    Goni, F.M.2    Alonso, A.3
  • 119
    • 0020726469 scopus 로고
    • Possible mechanism of membrane fusion
    • M.M. Kozlov, and V.S. Markin Possible mechanism of membrane fusion Biofizika 28 2 1983 242 247
    • (1983) Biofizika , vol.28 , Issue.2 , pp. 242-247
    • Kozlov, M.M.1    Markin, V.S.2
  • 120
    • 0021447259 scopus 로고
    • Phospholipase C from Clostridium perfringens: Preparation and characterization of homogeneous enzyme
    • E.L. Krug, and C. Kent Phospholipase C from Clostridium perfringens: preparation and characterization of homogeneous enzyme Arch Biochem Biophys 231 2 1984 400 410
    • (1984) Arch Biochem Biophys , vol.231 , Issue.2 , pp. 400-410
    • Krug, E.L.1    Kent, C.2
  • 121
    • 33744953581 scopus 로고    scopus 로고
    • Novel tumor necrosis factor-responsive mammalian neutral sphingomyelinase-3 is a C-tail-anchored protein
    • O. Krut, K. Wiegmann, H. Kashkar, B. Yazdanpanah, and M. Kronke Novel tumor necrosis factor-responsive mammalian neutral sphingomyelinase-3 is a C-tail-anchored protein J Biol Chem 281 19 2006 13784 13793
    • (2006) J Biol Chem , vol.281 , Issue.19 , pp. 13784-13793
    • Krut, O.1    Wiegmann, K.2    Kashkar, H.3    Yazdanpanah, B.4    Kronke, M.5
  • 122
    • 0032692212 scopus 로고    scopus 로고
    • Purification and characterization of recombinant human acid sphingomyelinase expressed in insect Sf21 cells
    • S. Lansmann, O. Bartelsen, and K. Sandhoff Purification and characterization of recombinant human acid sphingomyelinase expressed in insect Sf21 cells Methods Enzymol 311 2000 149 156
    • (2000) Methods Enzymol , vol.311 , pp. 149-156
    • Lansmann, S.1    Bartelsen, O.2    Sandhoff, K.3
  • 123
    • 66849126974 scopus 로고    scopus 로고
    • Nuclear envelope formation: Mind the gaps
    • B. Larijani, and D.L. Poccia Nuclear envelope formation: mind the gaps Annu Rev Biophys 38 2009 107 124
    • (2009) Annu Rev Biophys , vol.38 , pp. 107-124
    • Larijani, B.1    Poccia, D.L.2
  • 124
    • 0029863717 scopus 로고    scopus 로고
    • Evidence for the formation of microdomains in liquid crystalline large unilamellar vesicles caused by hydrophobic mismatch of the constituent phospholipids
    • J.Y. Lehtonen, J.M. Holopainen, and P.K. Kinnunen Evidence for the formation of microdomains in liquid crystalline large unilamellar vesicles caused by hydrophobic mismatch of the constituent phospholipids Biophys J 70 4 1996 1753 1760
    • (1996) Biophys J , vol.70 , Issue.4 , pp. 1753-1760
    • Lehtonen, J.Y.1    Holopainen, J.M.2    Kinnunen, P.K.3
  • 125
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • M.A. Lemmon Membrane recognition by phospholipid-binding domains Nat Rev Mol Cell Biol 9 2 2008 99 111
    • (2008) Nat Rev Mol Cell Biol , vol.9 , Issue.2 , pp. 99-111
    • Lemmon, M.A.1
  • 126
    • 0035976969 scopus 로고    scopus 로고
    • Acid sphingomyelinase-deficient macrophages have defective cholesterol trafficking and efflux
    • A.R. Leventhal, W. Chen, A.R. Tall, and I. Tabas Acid sphingomyelinase-deficient macrophages have defective cholesterol trafficking and efflux J Biol Chem 276 48 2001 44976 44983
    • (2001) J Biol Chem , vol.276 , Issue.48 , pp. 44976-44983
    • Leventhal, A.R.1    Chen, W.2    Tall, A.R.3    Tabas, I.4
  • 127
    • 0027203487 scopus 로고
    • Substrate requirements of bacterial phosphatidylinositol-specific phospholipase C
    • K.A. Lewis, V.R. Garigapati, C. Zhou, and M.F. Roberts Substrate requirements of bacterial phosphatidylinositol-specific phospholipase C Biochemistry 32 34 1993 8836 8841
    • (1993) Biochemistry , vol.32 , Issue.34 , pp. 8836-8841
    • Lewis, K.A.1    Garigapati, V.R.2    Zhou, C.3    Roberts, M.F.4
  • 128
    • 0035077616 scopus 로고    scopus 로고
    • Stimulation of acid sphingomyelinase activity by lysosomal lipids and sphingolipid activator proteins
    • T. Linke, G. Wilkening, S. Lansmann, H. Moczall, O. Bartelsen, and J. Weisgerber Stimulation of acid sphingomyelinase activity by lysosomal lipids and sphingolipid activator proteins Biol Chem 382 2 2001 283 290
    • (2001) Biol Chem , vol.382 , Issue.2 , pp. 283-290
    • Linke, T.1    Wilkening, G.2    Lansmann, S.3    Moczall, H.4    Bartelsen, O.5    Weisgerber, J.6
  • 129
    • 0016636779 scopus 로고
    • Purification by affinity chromatography of phospholipase C from Bacillus cereus
    • C. Little, B. Aurebekk, and A.B. Otnaess Purification by affinity chromatography of phospholipase C from Bacillus cereus FEBS Lett 52 2 1975 175 179
    • (1975) FEBS Lett , vol.52 , Issue.2 , pp. 175-179
    • Little, C.1    Aurebekk, B.2    Otnaess, A.B.3
  • 130
    • 0027407050 scopus 로고
    • Lipid vesicle fusion induced by phospholipase C activity in model bile
    • T.E. Little, H. Madani, S.P. Lee, and E.W. Kaler Lipid vesicle fusion induced by phospholipase C activity in model bile J Lipid Res 34 2 1993 211 217
    • (1993) J Lipid Res , vol.34 , Issue.2 , pp. 211-217
    • Little, T.E.1    Madani, H.2    Lee, S.P.3    Kaler, E.W.4
  • 131
    • 0033618352 scopus 로고    scopus 로고
    • Activation of phospholipase C delta1 through C2 domain by a Ca(2+)-enzyme-phosphatidylserine ternary complex
    • J.W. Lomasney, H.F. Cheng, S.R. Roffler, and K. King Activation of phospholipase C delta1 through C2 domain by a Ca(2+)-enzyme-phosphatidylserine ternary complex J Biol Chem 274 31 1999 21995 22001
    • (1999) J Biol Chem , vol.274 , Issue.31 , pp. 21995-22001
    • Lomasney, J.W.1    Cheng, H.F.2    Roffler, S.R.3    King, K.4
  • 132
    • 0029795505 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate binding to the pleckstrin homology domain of phospholipase C-delta1 enhances enzyme activity
    • J.W. Lomasney, H.F. Cheng, L.P. Wang, Y. Kuan, S. Liu, and S.W. Fesik Phosphatidylinositol 4,5-bisphosphate binding to the pleckstrin homology domain of phospholipase C-delta1 enhances enzyme activity J Biol Chem 271 41 1996 25316 25326
    • (1996) J Biol Chem , vol.271 , Issue.41 , pp. 25316-25326
    • Lomasney, J.W.1    Cheng, H.F.2    Wang, L.P.3    Kuan, Y.4    Liu, S.5    Fesik, S.W.6
  • 133
    • 78650298911 scopus 로고    scopus 로고
    • Multiple phospholipid substrates of phospholipase C/sphingomyelinase HR2 from Pseudomonas aeruginosa
    • D.J. Lopez, M.I. Collado, M. Ibarguren, A.I. Vasil, M.L. Vasil, and F.M. Goni Multiple phospholipid substrates of phospholipase C/sphingomyelinase HR2 from Pseudomonas aeruginosa Chem Phys Lipids 164 1 2011 78 82
    • (2011) Chem Phys Lipids , vol.164 , Issue.1 , pp. 78-82
    • Lopez, D.J.1    Collado, M.I.2    Ibarguren, M.3    Vasil, A.I.4    Vasil, M.L.5    Goni, F.M.6
  • 134
    • 84860439078 scopus 로고    scopus 로고
    • Accumulated bending energy elicits neutral sphingomyelinase activity in human red blood cells
    • doi:10.1016/j.bpj.2012.03.020
    • Lopez DJ, Egido-Gabas M, Lopez-Montero I, Busto JV, Casas J, Garnier M, et al. Accumulated bending energy elicits neutral sphingomyelinase activity in human red blood cells. Biophys J, (2012). doi:10.1016/j.bpj.2012.03.020.
    • (2012) Biophys J
    • Lopez, D.J.1    Egido-Gabas, M.2    Lopez-Montero, I.3    Busto, J.V.4    Casas, J.5    Garnier, M.6
  • 135
    • 0041856515 scopus 로고    scopus 로고
    • Purification, characterization, and identification of a sphingomyelin synthase from Pseudomonas aeruginosa. PlcH is a multifunctional enzyme
    • C. Luberto, M.J. Stonehouse, E.A. Collins, N. Marchesini, S. El-Bawab, and A.I. Vasil Purification, characterization, and identification of a sphingomyelin synthase from Pseudomonas aeruginosa. PlcH is a multifunctional enzyme J Biol Chem 278 35 2003 32733 32743
    • (2003) J Biol Chem , vol.278 , Issue.35 , pp. 32733-32743
    • Luberto, C.1    Stonehouse, M.J.2    Collins, E.A.3    Marchesini, N.4    El-Bawab, S.5    Vasil, A.I.6
  • 136
    • 0027304585 scopus 로고
    • Phospholipase C-induced aggregation and fusion of cholesterol-lecithin small unilamellar vesicles
    • A.S. Luk, E.W. Kaler, and S.P. Lee Phospholipase C-induced aggregation and fusion of cholesterol-lecithin small unilamellar vesicles Biochemistry 32 27 1993 6965 6973
    • (1993) Biochemistry , vol.32 , Issue.27 , pp. 6965-6973
    • Luk, A.S.1    Kaler, E.W.2    Lee, S.P.3
  • 137
    • 2342570273 scopus 로고    scopus 로고
    • Acid and neutral sphingomyelinases: Roles and mechanisms of regulation
    • N. Marchesini, and Y.A. Hannun Acid and neutral sphingomyelinases: roles and mechanisms of regulation Biochem Cell Biol 82 1 2004 27 44
    • (2004) Biochem Cell Biol , vol.82 , Issue.1 , pp. 27-44
    • Marchesini, N.1    Hannun, Y.A.2
  • 138
    • 0038529730 scopus 로고    scopus 로고
    • Biochemical properties of mammalian neutral sphingomyelinase 2 and its role in sphingolipid metabolism
    • N. Marchesini, C. Luberto, and Y.A. Hannun Biochemical properties of mammalian neutral sphingomyelinase 2 and its role in sphingolipid metabolism J Biol Chem 278 16 2003 13775 13783
    • (2003) J Biol Chem , vol.278 , Issue.16 , pp. 13775-13783
    • Marchesini, N.1    Luberto, C.2    Hannun, Y.A.3
  • 139
    • 0033955871 scopus 로고    scopus 로고
    • PH-regulated activation and release of a bacteria-associated phospholipase C during intracellular infection by Listeria monocytogenes
    • H. Marquis, and E.J. Hager PH-regulated activation and release of a bacteria-associated phospholipase C during intracellular infection by Listeria monocytogenes Mol Microbiol 35 2 2000 289 298
    • (2000) Mol Microbiol , vol.35 , Issue.2 , pp. 289-298
    • Marquis, H.1    Hager, E.J.2
  • 140
    • 2942522547 scopus 로고    scopus 로고
    • Membrane restructuring by Bordetella pertussis adenylate cyclase toxin, a member of the RTX toxin family
    • C. Martin, M.A. Requero, J. Masin, I. Konopasek, F.M. Goni, and P. Sebo Membrane restructuring by Bordetella pertussis adenylate cyclase toxin, a member of the RTX toxin family J Bacteriol 186 12 2004 3760 3765
    • (2004) J Bacteriol , vol.186 , Issue.12 , pp. 3760-3765
    • Martin, C.1    Requero, M.A.2    Masin, J.3    Konopasek, I.4    Goni, F.M.5    Sebo, P.6
  • 141
    • 0034724255 scopus 로고    scopus 로고
    • The choline binding site of phospholipase C (Bacillus cereus): Insights into substrate specificity
    • S.F. Martin, B.C. Follows, P.J. Hergenrother, and B.K. Trotter The choline binding site of phospholipase C (Bacillus cereus): insights into substrate specificity Biochemistry 39 12 2000 3410 3415
    • (2000) Biochemistry , vol.39 , Issue.12 , pp. 3410-3415
    • Martin, S.F.1    Follows, B.C.2    Hergenrother, P.J.3    Trotter, B.K.4
  • 142
    • 0033963013 scopus 로고    scopus 로고
    • Solution conformations of short-chain phosphatidylcholine. Substrates of the phosphatidylcholine-preferring PLC of Bacillus cereus
    • S.F. Martin, and G.E. Pitzer Solution conformations of short-chain phosphatidylcholine. Substrates of the phosphatidylcholine-preferring PLC of Bacillus cereus Biochim Biophys Acta 1464 1 2000 104 112
    • (2000) Biochim Biophys Acta , vol.1464 , Issue.1 , pp. 104-112
    • Martin, S.F.1    Pitzer, G.E.2
  • 143
    • 50049084765 scopus 로고    scopus 로고
    • Thematic review series: Sphingolipids. ISC1 (inositol phosphosphingolipid-phospholipase C), the yeast homologue of neutral sphingomyelinases
    • N. Matmati, and Y.A. Hannun Thematic review series: sphingolipids. ISC1 (inositol phosphosphingolipid-phospholipase C), the yeast homologue of neutral sphingomyelinases J Lipid Res 49 5 2008 922 928
    • (2008) J Lipid Res , vol.49 , Issue.5 , pp. 922-928
    • Matmati, N.1    Hannun, Y.A.2
  • 144
    • 1642293929 scopus 로고    scopus 로고
    • Ceramide selectively displaces cholesterol from ordered lipid domains (rafts): Implications for lipid raft structure and function
    • London E. Megha Ceramide selectively displaces cholesterol from ordered lipid domains (rafts): implications for lipid raft structure and function J Biol Chem 279 11 2004 9997 10004
    • (2004) J Biol Chem , vol.279 , Issue.11 , pp. 9997-10004
    • Megha, L.E.1
  • 146
    • 12144291717 scopus 로고    scopus 로고
    • Membrane fusion induced by the catalytic activity of a phospholipase C/sphingomyelinase from Listeria monocytogenes
    • L.R. Montes, F.M. Goni, N.C. Johnston, H. Goldfine, and A. Alonso Membrane fusion induced by the catalytic activity of a phospholipase C/sphingomyelinase from Listeria monocytogenes Biochemistry 43 12 2004 3688 3695
    • (2004) Biochemistry , vol.43 , Issue.12 , pp. 3688-3695
    • Montes, L.R.1    Goni, F.M.2    Johnston, N.C.3    Goldfine, H.4    Alonso, A.5
  • 147
    • 34948837283 scopus 로고    scopus 로고
    • Leakage-free membrane fusion induced by the hydrolytic activity of PlcHR(2), a novel phospholipase C/sphingomyelinase from Pseudomonas aeruginosa
    • L.R. Montes, M. Ibarguren, F.M. Goni, M. Stonehouse, M.L. Vasil, and A. Alonso Leakage-free membrane fusion induced by the hydrolytic activity of PlcHR(2), a novel phospholipase C/sphingomyelinase from Pseudomonas aeruginosa Biochim Biophys Acta 1768 10 2007 2365 2372
    • (2007) Biochim Biophys Acta , vol.1768 , Issue.10 , pp. 2365-2372
    • Montes, L.R.1    Ibarguren, M.2    Goni, F.M.3    Stonehouse, M.4    Vasil, M.L.5    Alonso, A.6
  • 148
    • 54849418609 scopus 로고    scopus 로고
    • Ceramide-enriched membrane domains in red blood cells and the mechanism of sphingomyelinase-induced hot-cold hemolysis
    • L.R. Montes, D.J. Lopez, J. Sot, L.A. Bagatolli, M.J. Stonehouse, and M.L. Vasil Ceramide-enriched membrane domains in red blood cells and the mechanism of sphingomyelinase-induced hot-cold hemolysis Biochemistry 47 43 2008 11222 11230
    • (2008) Biochemistry , vol.47 , Issue.43 , pp. 11222-11230
    • Montes, L.R.1    Lopez, D.J.2    Sot, J.3    Bagatolli, L.A.4    Stonehouse, M.J.5    Vasil, M.L.6
  • 149
    • 0037023765 scopus 로고    scopus 로고
    • Membrane restructuring via ceramide results in enhanced solute efflux
    • L.R. Montes, M.B. Ruiz-Arguello, F.M. Goni, and A. Alonso Membrane restructuring via ceramide results in enhanced solute efflux J Biol Chem 277 14 2002 11788 11794
    • (2002) J Biol Chem , vol.277 , Issue.14 , pp. 11788-11794
    • Montes, L.R.1    Ruiz-Arguello, M.B.2    Goni, F.M.3    Alonso, A.4
  • 150
    • 0031584854 scopus 로고    scopus 로고
    • Lipid domains and orthorhombic phases in model stratum corneum: Evidence from Fourier transform infrared spectroscopy studies
    • D.J. Moore, M.E. Rerek, and R. Mendelsohn Lipid domains and orthorhombic phases in model stratum corneum: evidence from Fourier transform infrared spectroscopy studies Biochem Biophys Res Commun 231 3 1997 797 801
    • (1997) Biochem Biophys Res Commun , vol.231 , Issue.3 , pp. 797-801
    • Moore, D.J.1    Rerek, M.E.2    Mendelsohn, R.3
  • 151
    • 0024278361 scopus 로고
    • A new kinetic approach for studying phospholipase C (Clostridium perfringens alpha toxin) activity on phospholipid monolayers
    • H. Moreau, G. Pieroni, C. Jolivet-Reynaud, J.E. Alouf, and R. Verger A new kinetic approach for studying phospholipase C (Clostridium perfringens alpha toxin) activity on phospholipid monolayers Biochemistry 27 7 1988 2319 2323
    • (1988) Biochemistry , vol.27 , Issue.7 , pp. 2319-2323
    • Moreau, H.1    Pieroni, G.2    Jolivet-Reynaud, C.3    Alouf, J.E.4    Verger, R.5
  • 152
    • 0031576330 scopus 로고    scopus 로고
    • Crystal structure of the phosphatidylinositol-specific phospholipase C from the human pathogen Listeria monocytogenes
    • J. Moser, B. Gerstel, J.E. Meyer, T. Chakraborty, J. Wehland, and D.W. Heinz Crystal structure of the phosphatidylinositol-specific phospholipase C from the human pathogen Listeria monocytogenes J Mol Biol 273 1 1997 269 282
    • (1997) J Mol Biol , vol.273 , Issue.1 , pp. 269-282
    • Moser, J.1    Gerstel, B.2    Meyer, J.E.3    Chakraborty, T.4    Wehland, J.5    Heinz, D.W.6
  • 153
    • 0029986712 scopus 로고    scopus 로고
    • Membrane-damaging action of Clostridium perfringens alpha-toxin on phospholipid liposomes
    • M. Nagahama, K. Michiue, and J. Sakurai Membrane-damaging action of Clostridium perfringens alpha-toxin on phospholipid liposomes Biochim Biophys Acta 1280 1 1996 120 126
    • (1996) Biochim Biophys Acta , vol.1280 , Issue.1 , pp. 120-126
    • Nagahama, M.1    Michiue, K.2    Sakurai, J.3
  • 154
    • 0028916854 scopus 로고
    • Site-directed mutagenesis of histidine residues in Clostridium perfringens alpha-toxin
    • M. Nagahama, Y. Okagawa, T. Nakayama, E. Nishioka, and J. Sakurai Site-directed mutagenesis of histidine residues in Clostridium perfringens alpha-toxin J Bacteriol 177 5 1995 1179 1185
    • (1995) J Bacteriol , vol.177 , Issue.5 , pp. 1179-1185
    • Nagahama, M.1    Okagawa, Y.2    Nakayama, T.3    Nishioka, E.4    Sakurai, J.5
  • 155
    • 35848957936 scopus 로고    scopus 로고
    • Effect of unsaturated bonds in the sn-2 acyl chain of phosphatidylcholine on the membrane-damaging action of Clostridium perfringens alpha-toxin toward liposomes
    • M. Nagahama, A. Otsuka, M. Oda, R.K. Singh, Z.M. Ziora, and H. Imagawa Effect of unsaturated bonds in the sn-2 acyl chain of phosphatidylcholine on the membrane-damaging action of Clostridium perfringens alpha-toxin toward liposomes Biochim Biophys Acta 1768 11 2007 2940 2945
    • (2007) Biochim Biophys Acta , vol.1768 , Issue.11 , pp. 2940-2945
    • Nagahama, M.1    Otsuka, A.2    Oda, M.3    Singh, R.K.4    Ziora, Z.M.5    Imagawa, H.6
  • 156
    • 29644435330 scopus 로고    scopus 로고
    • Role of tyrosine-57 and -65 in membrane-damaging and sphingomyelinase activities of Clostridium perfringens alpha-toxin
    • M. Nagahama, A. Otsuka, and J. Sakurai Role of tyrosine-57 and -65 in membrane-damaging and sphingomyelinase activities of Clostridium perfringens alpha-toxin Biochim Biophys Acta 1762 1 2006 110 114
    • (2006) Biochim Biophys Acta , vol.1762 , Issue.1 , pp. 110-114
    • Nagahama, M.1    Otsuka, A.2    Sakurai, J.3
  • 158
    • 0029024958 scopus 로고
    • Topological properties of two cubic phases of a phospholipid:cholesterol: diacylglycerol aqueous system and their possible implications in the phospholipase C-induced liposome fusion
    • J.L. Nieva, A. Alonso, G. Basanez, F.M. Goni, A. Gulik, and R. Vargas Topological properties of two cubic phases of a phospholipid:cholesterol: diacylglycerol aqueous system and their possible implications in the phospholipase C-induced liposome fusion FEBS Lett 368 1 1995 143 147
    • (1995) FEBS Lett , vol.368 , Issue.1 , pp. 143-147
    • Nieva, J.L.1    Alonso, A.2    Basanez, G.3    Goni, F.M.4    Gulik, A.5    Vargas, R.6
  • 159
    • 0024457473 scopus 로고
    • Liposome fusion catalytically induced by phospholipase C
    • J.L. Nieva, F.M. Goni, and A. Alonso Liposome fusion catalytically induced by phospholipase C Biochemistry 28 18 1989 7364 7367
    • (1989) Biochemistry , vol.28 , Issue.18 , pp. 7364-7367
    • Nieva, J.L.1    Goni, F.M.2    Alonso, A.3
  • 160
    • 0027466246 scopus 로고
    • Phospholipase C-promoted membrane fusion. Retroinhibition by the end-product diacylglycerol
    • J.L. Nieva, F.M. Goni, and A. Alonso Phospholipase C-promoted membrane fusion. Retroinhibition by the end-product diacylglycerol Biochemistry 32 4 1993 1054 1058
    • (1993) Biochemistry , vol.32 , Issue.4 , pp. 1054-1058
    • Nieva, J.L.1    Goni, F.M.2    Alonso, A.3
  • 161
    • 0032842762 scopus 로고    scopus 로고
    • Alkaline sphingomyelinases and ceramidases of the gastrointestinal tract
    • A. Nilsson, and R.D. Duan Alkaline sphingomyelinases and ceramidases of the gastrointestinal tract Chem Phys Lipids 102 1-2 1999 97 105
    • (1999) Chem Phys Lipids , vol.102 , Issue.12 , pp. 97-105
    • Nilsson, A.1    Duan, R.D.2
  • 162
    • 34447521411 scopus 로고    scopus 로고
    • Binding of phosphoinositide-specific phospholipase C-zeta (PLC-zeta) to phospholipid membranes: Potential role of an unstructured cluster of basic residues
    • M. Nomikos, A. Mulgrew-Nesbitt, P. Pallavi, G. Mihalyne, I. Zaitseva, and K. Swann Binding of phosphoinositide-specific phospholipase C-zeta (PLC-zeta) to phospholipid membranes: potential role of an unstructured cluster of basic residues J Biol Chem 282 22 2007 16644 16653
    • (2007) J Biol Chem , vol.282 , Issue.22 , pp. 16644-16653
    • Nomikos, M.1    Mulgrew-Nesbitt, A.2    Pallavi, P.3    Mihalyne, G.4    Zaitseva, I.5    Swann, K.6
  • 163
    • 0037120891 scopus 로고    scopus 로고
    • Observation of topical catalysis by sphingomyelinase coupled to microspheres
    • T.A. Nurminen, J.M. Holopainen, H. Zhao, and P.K. Kinnunen Observation of topical catalysis by sphingomyelinase coupled to microspheres J Am Chem Soc 124 41 2002 12129 12134
    • (2002) J Am Chem Soc , vol.124 , Issue.41 , pp. 12129-12134
    • Nurminen, T.A.1    Holopainen, J.M.2    Zhao, H.3    Kinnunen, P.K.4
  • 164
    • 4544332732 scopus 로고    scopus 로고
    • Effects of Clostridium perfringens alpha-toxin (PLC) and perfringolysin O (PFO) on cytotoxicity to macrophages, on escape from the phagosomes of macrophages, and on persistence of C. perfringens in host tissues
    • D.K. O'Brien, and S.B. Melville Effects of Clostridium perfringens alpha-toxin (PLC) and perfringolysin O (PFO) on cytotoxicity to macrophages, on escape from the phagosomes of macrophages, and on persistence of C. perfringens in host tissues Infect Immun 72 9 2004 5204 5215
    • (2004) Infect Immun , vol.72 , Issue.9 , pp. 5204-5215
    • O'Brien, D.K.1    Melville, S.B.2
  • 165
    • 1842425716 scopus 로고    scopus 로고
    • Clostridium perfringens alpha-toxin activates the sphingomyelin metabolism system in sheep erythrocytes
    • S. Ochi, M. Oda, H. Matsuda, S. Ikari, and J. Sakurai Clostridium perfringens alpha-toxin activates the sphingomyelin metabolism system in sheep erythrocytes J Biol Chem 279 13 2004 12181 12189
    • (2004) J Biol Chem , vol.279 , Issue.13 , pp. 12181-12189
    • Ochi, S.1    Oda, M.2    Matsuda, H.3    Ikari, S.4    Sakurai, J.5
  • 167
    • 50049087984 scopus 로고    scopus 로고
    • The relationship between the metabolism of sphingomyelin species and the hemolysis of sheep erythrocytes induced by Clostridium perfringens alpha-toxin
    • M. Oda, T. Matsuno, R. Shiihara, S. Ochi, R. Yamauchi, and Y. Saito The relationship between the metabolism of sphingomyelin species and the hemolysis of sheep erythrocytes induced by Clostridium perfringens alpha-toxin J Lipid Res 49 5 2008 1039 1047
    • (2008) J Lipid Res , vol.49 , Issue.5 , pp. 1039-1047
    • Oda, M.1    Matsuno, T.2    Shiihara, R.3    Ochi, S.4    Yamauchi, R.5    Saito, Y.6
  • 168
    • 0037195915 scopus 로고    scopus 로고
    • Structural requirements for selective binding of ISC1 to anionic phospholipids
    • Y. Okamoto, S. Vaena De Avalos, and Y.A. Hannun Structural requirements for selective binding of ISC1 to anionic phospholipids J Biol Chem 277 48 2002 46470 46477
    • (2002) J Biol Chem , vol.277 , Issue.48 , pp. 46470-46477
    • Okamoto, Y.1    Vaena De Avalos, S.2    Hannun, Y.A.3
  • 169
    • 34250338204 scopus 로고    scopus 로고
    • Ceramidase enhances phospholipase C-induced hemolysis by Pseudomonas aeruginosa
    • N. Okino, and M. Ito Ceramidase enhances phospholipase C-induced hemolysis by Pseudomonas aeruginosa J Biol Chem 282 9 2007 6021 6030
    • (2007) J Biol Chem , vol.282 , Issue.9 , pp. 6021-6030
    • Okino, N.1    Ito, M.2
  • 170
    • 0032582694 scopus 로고    scopus 로고
    • Sphingomyelinase induces aggregation and fusion, but phospholipase A2 only aggregation, of low density lipoprotein (LDL) particles. Two distinct mechanisms leading to increased binding strength of LDL to human aortic proteoglycans
    • K. Oorni, J.K. Hakala, A. Annila, M. Ala-Korpela, and P.T. Kovanen Sphingomyelinase induces aggregation and fusion, but phospholipase A2 only aggregation, of low density lipoprotein (LDL) particles. Two distinct mechanisms leading to increased binding strength of LDL to human aortic proteoglycans J Biol Chem 273 44 1998 29127 29134
    • (1998) J Biol Chem , vol.273 , Issue.44 , pp. 29127-29134
    • Oorni, K.1    Hakala, J.K.2    Annila, A.3    Ala-Korpela, M.4    Kovanen, P.T.5
  • 171
    • 23244438374 scopus 로고    scopus 로고
    • Sphingomyelinase induces aggregation and fusion of small very low-density lipoprotein and intermediate-density lipoprotein particles and increases their retention to human arterial proteoglycans
    • K. Oorni, P. Posio, M. Ala-Korpela, M. Jauhiainen, and P.T. Kovanen Sphingomyelinase induces aggregation and fusion of small very low-density lipoprotein and intermediate-density lipoprotein particles and increases their retention to human arterial proteoglycans Arterioscler Thromb Vasc Biol 25 8 2005 1678 1683
    • (2005) Arterioscler Thromb Vasc Biol , vol.25 , Issue.8 , pp. 1678-1683
    • Oorni, K.1    Posio, P.2    Ala-Korpela, M.3    Jauhiainen, M.4    Kovanen, P.T.5
  • 172
    • 27144515597 scopus 로고    scopus 로고
    • Crystal structure of SmcL, a bacterial neutral sphingomyelinase C from Listeria
    • A.E. Openshaw, P.R. Race, H.J. Monzo, J.A. Vazquez-Boland, and M.J. Banfield Crystal structure of SmcL, a bacterial neutral sphingomyelinase C from Listeria J Biol Chem 280 2005 35011 35017
    • (2005) J Biol Chem , vol.280 , pp. 35011-35017
    • Openshaw, A.E.1    Race, P.R.2    Monzo, H.J.3    Vazquez-Boland, J.A.4    Banfield, M.J.5
  • 173
    • 0024987613 scopus 로고
    • Molecular comparison of a nonhemolytic and a hemolytic phospholipase C from Pseudomonas aeruginosa
    • R.M. Ostroff, A.I. Vasil, and M.L. Vasil Molecular comparison of a nonhemolytic and a hemolytic phospholipase C from Pseudomonas aeruginosa J Bacteriol 172 10 1990 5915 5923
    • (1990) J Bacteriol , vol.172 , Issue.10 , pp. 5915-5923
    • Ostroff, R.M.1    Vasil, A.I.2    Vasil, M.L.3
  • 175
    • 0033000398 scopus 로고    scopus 로고
    • Liposomes containing sphingomyelin and cholesterol: Detergent solubilization and infrared spectroscopic studies
    • S.K. Patra, A. Alonso, J.L.R. Arrondo, and F.M. Goni Liposomes containing sphingomyelin and cholesterol: detergent solubilization and infrared spectroscopic studies J Liposome Res 9 1999 247 260
    • (1999) J Liposome Res , vol.9 , pp. 247-260
    • Patra, S.K.1    Alonso, A.2    Arrondo, J.L.R.3    Goni, F.M.4
  • 176
    • 61449152986 scopus 로고    scopus 로고
    • Phosphatidylinositol metabolism and membrane fusion
    • D. Poccia, and B. Larijani Phosphatidylinositol metabolism and membrane fusion Biochem J 418 2 2009 233 246
    • (2009) Biochem J , vol.418 , Issue.2 , pp. 233-246
    • Poccia, D.1    Larijani, B.2
  • 177
  • 178
    • 15444377640 scopus 로고    scopus 로고
    • Intramolecular interaction between phosphorylated tyrosine-783 and the C-terminal Src homology 2 domain activates phospholipase C-gamma1
    • B. Poulin, F. Sekiya, and S.G. Rhee Intramolecular interaction between phosphorylated tyrosine-783 and the C-terminal Src homology 2 domain activates phospholipase C-gamma1 Proc Natl Acad Sci USA 102 12 2005 4276 4281
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.12 , pp. 4276-4281
    • Poulin, B.1    Sekiya, F.2    Rhee, S.G.3
  • 179
    • 67650227918 scopus 로고    scopus 로고
    • Correlation of vesicle binding and phospholipid dynamics with phospholipase C activity: Insights into phosphatidylcholine activation and surface dilution inhibition
    • M. Pu, X. Fang, A.G. Redfield, A. Gershenson, and M.F. Roberts Correlation of vesicle binding and phospholipid dynamics with phospholipase C activity: insights into phosphatidylcholine activation and surface dilution inhibition J Biol Chem 284 24 2009 16099 16107
    • (2009) J Biol Chem , vol.284 , Issue.24 , pp. 16099-16107
    • Pu, M.1    Fang, X.2    Redfield, A.G.3    Gershenson, A.4    Roberts, M.F.5
  • 180
    • 77956256450 scopus 로고    scopus 로고
    • Defining specific lipid binding sites for a peripheral membrane protein in situ using subtesla field-cycling NMR
    • M. Pu, A. Orr, A.G. Redfield, and M.F. Roberts Defining specific lipid binding sites for a peripheral membrane protein in situ using subtesla field-cycling NMR J Biol Chem 285 35 2010 26916 26922
    • (2010) J Biol Chem , vol.285 , Issue.35 , pp. 26916-26922
    • Pu, M.1    Orr, A.2    Redfield, A.G.3    Roberts, M.F.4
  • 181
    • 67651230535 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy of phosphatidylinositol-specific phospholipase C monitors the interplay of substrate and activator lipid binding
    • M. Pu, M.F. Roberts, and A. Gershenson Fluorescence correlation spectroscopy of phosphatidylinositol-specific phospholipase C monitors the interplay of substrate and activator lipid binding Biochemistry 48 29 2009 6835 6845
    • (2009) Biochemistry , vol.48 , Issue.29 , pp. 6835-6845
    • Pu, M.1    Roberts, M.F.2    Gershenson, A.3
  • 182
    • 0032485866 scopus 로고    scopus 로고
    • Phosphatidylcholine activation of bacterial phosphatidylinositol-specific phospholipase C toward PI vesicles
    • X. Qian, C. Zhou, and M.F. Roberts Phosphatidylcholine activation of bacterial phosphatidylinositol-specific phospholipase C toward PI vesicles Biochemistry 37 18 1998 6513 6522
    • (1998) Biochemistry , vol.37 , Issue.18 , pp. 6513-6522
    • Qian, X.1    Zhou, C.2    Roberts, M.F.3
  • 183
    • 0024423426 scopus 로고
    • Isolation of cDNA clones encoding human acid sphingomyelinase: Occurrence of alternatively processed transcripts
    • L.E. Quintern, E.H. Schuchman, O. Levran, M. Suchi, K. Ferlinz, and H. Reinke Isolation of cDNA clones encoding human acid sphingomyelinase: occurrence of alternatively processed transcripts EMBO J 8 9 1989 2469 2473
    • (1989) EMBO J , vol.8 , Issue.9 , pp. 2469-2473
    • Quintern, L.E.1    Schuchman, E.H.2    Levran, O.3    Suchi, M.4    Ferlinz, K.5    Reinke, H.6
  • 185
    • 33745608423 scopus 로고    scopus 로고
    • Characterization of the kinetics of phospholipase C activity toward mixed micelles of sodium deoxycholate and dimyristoylphosphatidylcholine
    • R. Ranganathan, C.M. Tcacenco, R. Rosseto, and J. Hajdu Characterization of the kinetics of phospholipase C activity toward mixed micelles of sodium deoxycholate and dimyristoylphosphatidylcholine Biophys Chem 122 2 2006 79 89
    • (2006) Biophys Chem , vol.122 , Issue.2 , pp. 79-89
    • Ranganathan, R.1    Tcacenco, C.M.2    Rosseto, R.3    Hajdu, J.4
  • 186
    • 68949102501 scopus 로고    scopus 로고
    • Phospholipid reorientation at the lipid/water interface measured by high resolution 31P field cycling NMR spectroscopy
    • M.F. Roberts, A.G. Redfield, and U. Mohanty Phospholipid reorientation at the lipid/water interface measured by high resolution 31P field cycling NMR spectroscopy Biophys J 97 1 2009 132 141
    • (2009) Biophys J , vol.97 , Issue.1 , pp. 132-141
    • Roberts, M.F.1    Redfield, A.G.2    Mohanty, U.3
  • 187
    • 0034623231 scopus 로고    scopus 로고
    • Structural requirements for catalysis and membrane targeting of mammalian enzymes with neutral sphingomyelinase and lysophospholipid phospholipase C activities. Analysis by chemical modification and site-directed mutagenesis
    • F. Rodrigues-Lima, A.C. Fensome, M. Josephs, J. Evans, R.J. Veldman, and M. Katan Structural requirements for catalysis and membrane targeting of mammalian enzymes with neutral sphingomyelinase and lysophospholipid phospholipase C activities. Analysis by chemical modification and site-directed mutagenesis J Biol Chem 275 36 2000 28316 28325
    • (2000) J Biol Chem , vol.275 , Issue.36 , pp. 28316-28325
    • Rodrigues-Lima, F.1    Fensome, A.C.2    Josephs, M.3    Evans, J.4    Veldman, R.J.5    Katan, M.6
  • 188
    • 34249816501 scopus 로고    scopus 로고
    • Sperm phospholipases and acrosomal exocytosis
    • E.R. Roldan, and Q.X. Shi Sperm phospholipases and acrosomal exocytosis Front Biosci 12 2007 89 104
    • (2007) Front Biosci , vol.12 , pp. 89-104
    • Roldan, E.R.1    Shi, Q.X.2
  • 189
    • 33845940377 scopus 로고    scopus 로고
    • Structural determinants for phosphatidic acid regulation of phospholipase C-beta1
    • E.M. Ross, D. Mateu, A.V. Gomes, C. Arana, T. Tran, and I. Litosch Structural determinants for phosphatidic acid regulation of phospholipase C-beta1 J Biol Chem 281 44 2006 33087 33094
    • (2006) J Biol Chem , vol.281 , Issue.44 , pp. 33087-33094
    • Ross, E.M.1    Mateu, D.2    Gomes, A.V.3    Arana, C.4    Tran, T.5    Litosch, I.6
  • 190
    • 22544470314 scopus 로고    scopus 로고
    • Caspase-dependent and -independent activation of acid sphingomyelinase signaling
    • J.A. Rotolo, J. Zhang, M. Donepudi, H. Lee, Z. Fuks, and R. Kolesnick Caspase-dependent and -independent activation of acid sphingomyelinase signaling J Biol Chem 280 28 2005 26425 26434
    • (2005) J Biol Chem , vol.280 , Issue.28 , pp. 26425-26434
    • Rotolo, J.A.1    Zhang, J.2    Donepudi, M.3    Lee, H.4    Fuks, Z.5    Kolesnick, R.6
  • 191
    • 0029981159 scopus 로고    scopus 로고
    • Different effects of enzyme-generated ceramides and diacylglycerols in phospholipid membrane fusion and leakage
    • M.B. Ruiz-Arguello, G. Basanez, F.M. Goni, and A. Alonso Different effects of enzyme-generated ceramides and diacylglycerols in phospholipid membrane fusion and leakage J Biol Chem 271 43 1996 26616 26621
    • (1996) J Biol Chem , vol.271 , Issue.43 , pp. 26616-26621
    • Ruiz-Arguello, M.B.1    Basanez, G.2    Goni, F.M.3    Alonso, A.4
  • 192
    • 0001504371 scopus 로고    scopus 로고
    • Vesicle membrane fusion induced by the concerted activities of sphingomyelinase and phospholipase C
    • M.B. Ruiz-Arguello, F.M. Goni, and A. Alonso Vesicle membrane fusion induced by the concerted activities of sphingomyelinase and phospholipase C J Biol Chem 273 36 1998 22977 22982
    • (1998) J Biol Chem , vol.273 , Issue.36 , pp. 22977-22982
    • Ruiz-Arguello, M.B.1    Goni, F.M.2    Alonso, A.3
  • 193
    • 0040110294 scopus 로고    scopus 로고
    • Phospholipase C hydrolysis of phospholipids in bilayers of mixed lipid compositions
    • M.B. Ruiz-Arguello, F.M. Goni, and A. Alonso Phospholipase C hydrolysis of phospholipids in bilayers of mixed lipid compositions Biochemistry 37 33 1998 11621 11628
    • (1998) Biochemistry , vol.37 , Issue.33 , pp. 11621-11628
    • Ruiz-Arguello, M.B.1    Goni, F.M.2    Alonso, A.3
  • 194
    • 0344563465 scopus 로고    scopus 로고
    • Effect of sublytic concentrations of sodium cholate on phospholipase C hydrolysis of phospholipid bilayers
    • M.B. Ruiz-Arguello, M.P. Veiga, A. Alonso, and F.M. Goni Effect of sublytic concentrations of sodium cholate on phospholipase C hydrolysis of phospholipid bilayers J Colloid Interface Sci 219 1 1999 163 167
    • (1999) J Colloid Interface Sci , vol.219 , Issue.1 , pp. 163-167
    • Ruiz-Arguello, M.B.1    Veiga, M.P.2    Alonso, A.3    Goni, F.M.4
  • 195
    • 0036008307 scopus 로고    scopus 로고
    • Sphingomyelinase cleavage of sphingomyelin in pure and mixed lipid membranes. Influence of the physical state of the sphingolipid
    • M.B. Ruiz-Arguello, M.P. Veiga, J.L. Arrondo, F.M. Goni, and A. Alonso Sphingomyelinase cleavage of sphingomyelin in pure and mixed lipid membranes. Influence of the physical state of the sphingolipid Chem Phys Lipids 114 1 2002 11 20
    • (2002) Chem Phys Lipids , vol.114 , Issue.1 , pp. 11-20
    • Ruiz-Arguello, M.B.1    Veiga, M.P.2    Arrondo, J.L.3    Goni, F.M.4    Alonso, A.5
  • 196
    • 0037058952 scopus 로고    scopus 로고
    • Listeria monocytogenes phosphatidylinositol-specific phospholipase C: Activation and allostery
    • M. Ryan, T.O. Zaikova, J.F. Keana, H. Goldfine, and O.H. Griffith Listeria monocytogenes phosphatidylinositol-specific phospholipase C: activation and allostery Biophys Chem 101-102 2002 347 358
    • (2002) Biophys Chem , vol.101-102 , pp. 347-358
    • Ryan, M.1    Zaikova, T.O.2    Keana, J.F.3    Goldfine, H.4    Griffith, O.H.5
  • 197
    • 0005226914 scopus 로고    scopus 로고
    • Characterization of acidic and neutral sphingomyelinase activities in crude extracts of HL-60 cells
    • D. Samet, and Y. Barenholz Characterization of acidic and neutral sphingomyelinase activities in crude extracts of HL-60 cells Chem Phys Lipids 102 1-2 1999 65 77
    • (1999) Chem Phys Lipids , vol.102 , Issue.12 , pp. 65-77
    • Samet, D.1    Barenholz, Y.2
  • 198
    • 0033621471 scopus 로고    scopus 로고
    • Function of the cloned putative neutral sphingomyelinase as lyso-platelet activating factor-phospholipase C
    • H. Sawai, N. Domae, N. Nagan, and Y.A. Hannun Function of the cloned putative neutral sphingomyelinase as lyso-platelet activating factor-phospholipase C J Biol Chem 274 53 1999 38131 38139
    • (1999) J Biol Chem , vol.274 , Issue.53 , pp. 38131-38139
    • Sawai, H.1    Domae, N.2    Nagan, N.3    Hannun, Y.A.4
  • 199
    • 0034670379 scopus 로고    scopus 로고
    • Identification of ISC1 (YER019w) as inositol phosphosphingolipid phospholipase C in Saccharomyces cerevisiae
    • H. Sawai, Y. Okamoto, C. Luberto, C. Mao, A. Bielawska, and N. Domae Identification of ISC1 (YER019w) as inositol phosphosphingolipid phospholipase C in Saccharomyces cerevisiae J Biol Chem 275 50 2000 39793 39798
    • (2000) J Biol Chem , vol.275 , Issue.50 , pp. 39793-39798
    • Sawai, H.1    Okamoto, Y.2    Luberto, C.3    Mao, C.4    Bielawska, A.5    Domae, N.6
  • 200
    • 0014083339 scopus 로고
    • Sphingomyelinase in normal human spleens and in spleens from subjects with Niemann-Pick disease
    • P.B. Schneider, and E.P. Kennedy Sphingomyelinase in normal human spleens and in spleens from subjects with Niemann-Pick disease J Lipid Res 8 3 1967 202 209
    • (1967) J Lipid Res , vol.8 , Issue.3 , pp. 202-209
    • Schneider, P.B.1    Kennedy, E.P.2
  • 201
    • 3543026271 scopus 로고    scopus 로고
    • Mechanism of tyrosine phosphorylation and activation of phospholipase C-gamma 1. Tyrosine 783 phosphorylation is not sufficient for lipase activation
    • F. Sekiya, B. Poulin, Y.J. Kim, and S.G. Rhee Mechanism of tyrosine phosphorylation and activation of phospholipase C-gamma 1. Tyrosine 783 phosphorylation is not sufficient for lipase activation J Biol Chem 279 31 2004 32181 32190
    • (2004) J Biol Chem , vol.279 , Issue.31 , pp. 32181-32190
    • Sekiya, F.1    Poulin, B.2    Kim, Y.J.3    Rhee, S.G.4
  • 203
    • 0029129260 scopus 로고
    • Structural and thermotropic properties of synthetic C16:0 (palmitoyl) ceramide: Effect of hydration
    • J. Shah, J.M. Atienza, R.I. Duclos Jr., A.V. Rawlings, Z. Dong, and G.G. Shipley Structural and thermotropic properties of synthetic C16:0 (palmitoyl) ceramide: effect of hydration J Lipid Res 36 9 1995 1936 1944
    • (1995) J Lipid Res , vol.36 , Issue.9 , pp. 1936-1944
    • Shah, J.1    Atienza, J.M.2    Duclos, Jr.R.I.3    Rawlings, A.V.4    Dong, Z.5    Shipley, G.G.6
  • 204
    • 34247875979 scopus 로고    scopus 로고
    • Dimer structure of an interfacially impaired phosphatidylinositol- specific phospholipase C
    • C. Shao, X. Shi, H. Wehbi, C. Zambonelli, J.F. Head, and B.A. Seaton Dimer structure of an interfacially impaired phosphatidylinositol-specific phospholipase C J Biol Chem 282 12 2007 9228 9235
    • (2007) J Biol Chem , vol.282 , Issue.12 , pp. 9228-9235
    • Shao, C.1    Shi, X.2    Wehbi, H.3    Zambonelli, C.4    Head, J.F.5    Seaton, B.A.6
  • 205
    • 0022919911 scopus 로고
    • Isolation and properties of a phosphatidylcholine-specific phospholipase C from bull seminal plasma
    • R.G. Sheikhnejad, and P.N. Srivastava Isolation and properties of a phosphatidylcholine-specific phospholipase C from bull seminal plasma J Biol Chem 261 16 1986 7544 7549
    • (1986) J Biol Chem , vol.261 , Issue.16 , pp. 7544-7549
    • Sheikhnejad, R.G.1    Srivastava, P.N.2
  • 206
    • 67650123206 scopus 로고    scopus 로고
    • Modulation of Bacillus thuringiensis phosphatidylinositol-specific phospholipase C activity by mutations in the putative dimerization interface
    • X. Shi, C. Shao, X. Zhang, C. Zambonelli, A.G. Redfield, and J.F. Head Modulation of Bacillus thuringiensis phosphatidylinositol-specific phospholipase C activity by mutations in the putative dimerization interface J Biol Chem 284 23 2009 15607 15618
    • (2009) J Biol Chem , vol.284 , Issue.23 , pp. 15607-15618
    • Shi, X.1    Shao, C.2    Zhang, X.3    Zambonelli, C.4    Redfield, A.G.5    Head, J.F.6
  • 207
    • 0027362739 scopus 로고
    • Energetics of intermediates in membrane fusion: Comparison of stalk and inverted micellar intermediate mechanisms
    • D.P. Siegel Energetics of intermediates in membrane fusion: comparison of stalk and inverted micellar intermediate mechanisms Biophys J 65 5 1993 2124 2140
    • (1993) Biophys J , vol.65 , Issue.5 , pp. 2124-2140
    • Siegel, D.P.1
  • 208
    • 0030783371 scopus 로고    scopus 로고
    • The mechanism of lamellar-to-inverted hexagonal phase transitions in phosphatidylethanolamine: Implications for membrane fusion mechanisms
    • D.P. Siegel, and R.M. Epand The mechanism of lamellar-to-inverted hexagonal phase transitions in phosphatidylethanolamine: implications for membrane fusion mechanisms Biophys J 73 6 1997 3089 3111
    • (1997) Biophys J , vol.73 , Issue.6 , pp. 3089-3111
    • Siegel, D.P.1    Epand, R.M.2
  • 209
    • 3042776328 scopus 로고    scopus 로고
    • The gaussian curvature elastic modulus of N-monomethylated dioleoylphosphatidylethanolamine: Relevance to membrane fusion and lipid phase behavior
    • D.P. Siegel, and M.M. Kozlov The gaussian curvature elastic modulus of N-monomethylated dioleoylphosphatidylethanolamine: relevance to membrane fusion and lipid phase behavior Biophys J 87 1 2004 366 374
    • (2004) Biophys J , vol.87 , Issue.1 , pp. 366-374
    • Siegel, D.P.1    Kozlov, M.M.2
  • 210
    • 67649410710 scopus 로고    scopus 로고
    • Lipid raft composition modulates sphingomyelinase activity and ceramide-induced membrane physical alterations
    • L.C. Silva, A.H. Futerman, and M. Prieto Lipid raft composition modulates sphingomyelinase activity and ceramide-induced membrane physical alterations Biophys J 96 8 2009 3210 3222
    • (2009) Biophys J , vol.96 , Issue.8 , pp. 3210-3222
    • Silva, L.C.1    Futerman, A.H.2    Prieto, M.3
  • 211
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • K. Simons, and E. Ikonen Functional rafts in cell membranes Nature 387 6633 1997 569 572
    • (1997) Nature , vol.387 , Issue.6633 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 212
    • 58149164862 scopus 로고    scopus 로고
    • Kinetics of bacterial phospholipase C activity at micellar interfaces: Effect of substrate aggregate microstructure and a model for the kinetic parameters
    • J. Singh, R. Ranganathan, and J. Hajdu Kinetics of bacterial phospholipase C activity at micellar interfaces: effect of substrate aggregate microstructure and a model for the kinetic parameters J Phys Chem B 112 51 2008 16741 16751
    • (2008) J Phys Chem B , vol.112 , Issue.51 , pp. 16741-16751
    • Singh, J.1    Ranganathan, R.2    Hajdu, J.3
  • 213
    • 0037178790 scopus 로고    scopus 로고
    • Ceramide channels increase the permeability of the mitochondrial outer membrane to small proteins
    • L.J. Siskind, R.N. Kolesnick, and M. Colombini Ceramide channels increase the permeability of the mitochondrial outer membrane to small proteins J Biol Chem 277 30 2002 26796 26803
    • (2002) J Biol Chem , vol.277 , Issue.30 , pp. 26796-26803
    • Siskind, L.J.1    Kolesnick, R.N.2    Colombini, M.3
  • 214
    • 0029013962 scopus 로고
    • Lateral domain formation in mixed monolayers containing cholesterol and dipalmitoylphosphatidylcholine or N-palmitoylsphingomyelin
    • J.P. Slotte Lateral domain formation in mixed monolayers containing cholesterol and dipalmitoylphosphatidylcholine or N-palmitoylsphingomyelin Biochim Biophys Acta 1235 2 1995 419 427
    • (1995) Biochim Biophys Acta , vol.1235 , Issue.2 , pp. 419-427
    • Slotte, J.P.1
  • 215
    • 0028828198 scopus 로고
    • The two distinct phospholipases C of Listeria monocytogenes have overlapping roles in escape from a vacuole and cell-to-cell spread
    • G.A. Smith, H. Marquis, S. Jones, N.C. Johnston, D.A. Portnoy, and H. Goldfine The two distinct phospholipases C of Listeria monocytogenes have overlapping roles in escape from a vacuole and cell-to-cell spread Infect Immun 63 11 1995 4231 4237
    • (1995) Infect Immun , vol.63 , Issue.11 , pp. 4231-4237
    • Smith, G.A.1    Marquis, H.2    Jones, S.3    Johnston, N.C.4    Portnoy, D.A.5    Goldfine, H.6
  • 216
    • 33646179776 scopus 로고    scopus 로고
    • Detergent-resistant, ceramide-enriched domains in sphingomyelin/ceramide bilayers
    • J. Sot, L.A. Bagatolli, F.M. Goni, and A. Alonso Detergent-resistant, ceramide-enriched domains in sphingomyelin/ceramide bilayers Biophys J 90 3 2006 903 914
    • (2006) Biophys J , vol.90 , Issue.3 , pp. 903-914
    • Sot, J.1    Bagatolli, L.A.2    Goni, F.M.3    Alonso, A.4
  • 217
    • 51249103180 scopus 로고    scopus 로고
    • Cholesterol displacement by ceramide in sphingomyelin-containing liquid-ordered domains, and generation of gel regions in giant lipidic vesicles
    • J. Sot, M. Ibarguren, J.V. Busto, L.R. Montes, F.M. Goni, and A. Alonso Cholesterol displacement by ceramide in sphingomyelin-containing liquid-ordered domains, and generation of gel regions in giant lipidic vesicles FEBS Lett 582 21-22 2008 3230 3236
    • (2008) FEBS Lett , vol.582 , Issue.2122 , pp. 3230-3236
    • Sot, J.1    Ibarguren, M.2    Busto, J.V.3    Montes, L.R.4    Goni, F.M.5    Alonso, A.6
  • 218
    • 77951910348 scopus 로고    scopus 로고
    • Ceramide-rich platforms in transmembrane signaling
    • B. Stancevic, and R. Kolesnick Ceramide-rich platforms in transmembrane signaling FEBS Lett 584 9 2010 1728 1740
    • (2010) FEBS Lett , vol.584 , Issue.9 , pp. 1728-1740
    • Stancevic, B.1    Kolesnick, R.2
  • 220
    • 0036721021 scopus 로고    scopus 로고
    • A novel cell entry pathway for a DAF-using human enterovirus is dependent on lipid rafts
    • A.D. Stuart, H.E. Eustace, T.A. McKee, and T.D. Brown A novel cell entry pathway for a DAF-using human enterovirus is dependent on lipid rafts J Virol 76 18 2002 9307 9322
    • (2002) J Virol , vol.76 , Issue.18 , pp. 9307-9322
    • Stuart, A.D.1    Eustace, H.E.2    McKee, T.A.3    Brown, T.D.4
  • 221
    • 46249091922 scopus 로고    scopus 로고
    • Multiple roles of phosphoinositide-specific phospholipase C isozymes
    • P.G. Suh, J.I. Park, L. Manzoli, L. Cocco, J.C. Peak, and M. Katan Multiple roles of phosphoinositide-specific phospholipase C isozymes BMB Rep 41 6 2008 415 434
    • (2008) BMB Rep , vol.41 , Issue.6 , pp. 415-434
    • Suh, P.G.1    Park, J.I.2    Manzoli, L.3    Cocco, L.4    Peak, J.C.5    Katan, M.6
  • 223
    • 0032868934 scopus 로고    scopus 로고
    • Secretory sphingomyelinase
    • I. Tabas Secretory sphingomyelinase Chem Phys Lipids 102 1-2 1999 123 130
    • (1999) Chem Phys Lipids , vol.102 , Issue.12 , pp. 123-130
    • Tabas, I.1
  • 224
    • 0019344439 scopus 로고
    • Phospholipase C from Clostridium perfringens
    • T. Takahashi, T. Sugahara, and A. Ohsaka Phospholipase C from Clostridium perfringens Methods in Enzymol 71 Pt. C 1981 710 725
    • (1981) Methods in Enzymol , vol.71 , Issue.PART C , pp. 710-725
    • Takahashi, T.1    Sugahara, T.2    Ohsaka, A.3
  • 226
    • 0030921454 scopus 로고    scopus 로고
    • Phosphoinositide binding specificity among phospholipase C isozymes as determined by photo-cross-linking to novel substrate and product analogs
    • E. Tall, G. Dorman, P. Garcia, L. Runnels, S. Shah, and J. Chen Phosphoinositide binding specificity among phospholipase C isozymes as determined by photo-cross-linking to novel substrate and product analogs Biochemistry 36 23 1997 7239 7248
    • (1997) Biochemistry , vol.36 , Issue.23 , pp. 7239-7248
    • Tall, E.1    Dorman, G.2    Garcia, P.3    Runnels, L.4    Shah, S.5    Chen, J.6
  • 227
    • 3142746012 scopus 로고    scopus 로고
    • Lipidic pore formation by the concerted action of proapoptotic BAX and tBID
    • O. Terrones, B. Antonsson, H. Yamaguchi, H.G. Wang, J. Liu, and R.M. Lee Lipidic pore formation by the concerted action of proapoptotic BAX and tBID J Biol Chem 279 29 2004 30081 30091
    • (2004) J Biol Chem , vol.279 , Issue.29 , pp. 30081-30091
    • Terrones, O.1    Antonsson, B.2    Yamaguchi, H.3    Wang, H.G.4    Liu, J.5    Lee, R.M.6
  • 228
    • 2042499658 scopus 로고    scopus 로고
    • Acid sphingomyelinase and inhibition by phosphate ion: Role of inhibition by phosphatidyl-myo-inositol 3,4,5-triphosphate in oligodendrocyte cell signaling
    • F.D. Testai, M.A. Landek, R. Goswami, M. Ahmed, and G. Dawson Acid sphingomyelinase and inhibition by phosphate ion: role of inhibition by phosphatidyl-myo-inositol 3,4,5-triphosphate in oligodendrocyte cell signaling J Neurochem 89 3 2004 636 644
    • (2004) J Neurochem , vol.89 , Issue.3 , pp. 636-644
    • Testai, F.D.1    Landek, M.A.2    Goswami, R.3    Ahmed, M.4    Dawson, G.5
  • 229
    • 0027231710 scopus 로고
    • Bacterial phospholipases C
    • R.W. Titball Bacterial phospholipases C Microbiol Rev 57 2 1993 347 366
    • (1993) Microbiol Rev , vol.57 , Issue.2 , pp. 347-366
    • Titball, R.W.1
  • 230
    • 0032584153 scopus 로고    scopus 로고
    • Cloned mammalian neutral sphingomyelinase: Functions in sphingolipid signaling?
    • S. Tomiuk, K. Hofmann, M. Nix, M. Zumbansen, and W. Stoffel Cloned mammalian neutral sphingomyelinase: functions in sphingolipid signaling? Proc Natl Acad Sci USA 95 7 1998 3638 3643
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.7 , pp. 3638-3643
    • Tomiuk, S.1    Hofmann, K.2    Nix, M.3    Zumbansen, M.4    Stoffel, W.5
  • 231
    • 71749099593 scopus 로고    scopus 로고
    • Influence of membrane curvature on the structure of the membrane-associated pleckstrin homology domain of phospholipase C-delta1
    • N. Uekama, T. Aoki, T. Maruoka, S. Kurisu, A. Hatakeyama, and S. Yamaguchi Influence of membrane curvature on the structure of the membrane-associated pleckstrin homology domain of phospholipase C-delta1 Biochim Biophys Acta 1788 12 2009 2575 2583
    • (2009) Biochim Biophys Acta , vol.1788 , Issue.12 , pp. 2575-2583
    • Uekama, N.1    Aoki, T.2    Maruoka, T.3    Kurisu, S.4    Hatakeyama, A.5    Yamaguchi, S.6
  • 232
    • 33845628549 scopus 로고    scopus 로고
    • Phosphatidylserine induces functional and structural alterations of the membrane-associated pleckstrin homology domain of phospholipase C-delta1
    • N. Uekama, T. Sugita, M. Okada, H. Yagisawa, and S. Tuzi Phosphatidylserine induces functional and structural alterations of the membrane-associated pleckstrin homology domain of phospholipase C-delta1 FEBS J 274 1 2007 177 187
    • (2007) FEBS J , vol.274 , Issue.1 , pp. 177-187
    • Uekama, N.1    Sugita, T.2    Okada, M.3    Yagisawa, H.4    Tuzi, S.5
  • 234
    • 63649103381 scopus 로고    scopus 로고
    • Phospholipase C and sphingomyelinase activities of the Clostridium perfringens alpha-toxin
    • P. Urbina, M. Flores-Diaz, A. Alape-Giron, A. Alonso, and F.M. Goni Phospholipase C and sphingomyelinase activities of the Clostridium perfringens alpha-toxin Chem Phys Lipids 159 1 2009 51 57
    • (2009) Chem Phys Lipids , vol.159 , Issue.1 , pp. 51-57
    • Urbina, P.1    Flores-Diaz, M.2    Alape-Giron, A.3    Alonso, A.4    Goni, F.M.5
  • 235
    • 78649800698 scopus 로고
    • Effects of bilayer composition and physical properties on the phospholipase C and sphingomyelinase activities of Clostridium perfringens alpha-toxin
    • P. Urbina, M. Flores-Diaz, A. Alape-Giron, A. Alonso, and F.M. Goni Effects of bilayer composition and physical properties on the phospholipase C and sphingomyelinase activities of Clostridium perfringens alpha-toxin Biochim Biophys Acta 1 1808 279 286
    • (1808) Biochim Biophys Acta , vol.1 , pp. 279-286
    • Urbina, P.1    Flores-Diaz, M.2    Alape-Giron, A.3    Alonso, A.4    Goni, F.M.5
  • 236
    • 41649103930 scopus 로고    scopus 로고
    • Fusogenicity of membranes: The impact of acid sphingomyelinase on innate immune responses
    • O. Utermohlen, J. Herz, M. Schramm, and M. Kronke Fusogenicity of membranes: the impact of acid sphingomyelinase on innate immune responses Immunobiology 213 3-4 2008 307 314
    • (2008) Immunobiology , vol.213 , Issue.34 , pp. 307-314
    • Utermohlen, O.1    Herz, J.2    Schramm, M.3    Kronke, M.4
  • 237
    • 0345505643 scopus 로고    scopus 로고
    • Severe impairment in early host defense against Listeria monocytogenes in mice deficient in acid sphingomyelinase
    • O. Utermohlen, U. Karow, J. Lohler, and M. Kronke Severe impairment in early host defense against Listeria monocytogenes in mice deficient in acid sphingomyelinase J Immunol 170 5 2003 2621 2628
    • (2003) J Immunol , vol.170 , Issue.5 , pp. 2621-2628
    • Utermohlen, O.1    Karow, U.2    Lohler, J.3    Kronke, M.4
  • 238
    • 14844293078 scopus 로고    scopus 로고
    • The phosphatidylglycerol/cardiolipin biosynthetic pathway is required for the activation of inositol phosphosphingolipid phospholipase C, Isc1p, during growth of Saccharomyces cerevisiae
    • S. Vaena de Avalos, X. Su, M. Zhang, Y. Okamoto, W. Dowhan, and Y.A. Hannun The phosphatidylglycerol/cardiolipin biosynthetic pathway is required for the activation of inositol phosphosphingolipid phospholipase C, Isc1p, during growth of Saccharomyces cerevisiae J Biol Chem 280 8 2005 7170 7177
    • (2005) J Biol Chem , vol.280 , Issue.8 , pp. 7170-7177
    • Vaena De Avalos, S.1    Su, X.2    Zhang, M.3    Okamoto, Y.4    Dowhan, W.5    Hannun, Y.A.6
  • 240
    • 0026285735 scopus 로고
    • Phospholipase C: Molecular biology and contribution to the pathogenesis of Pseudomonas aeruginosa
    • M.L. Vasil, L.M. Graham, R.M. Ostroff, V.D. Shortridge, and A.I. Vasil Phospholipase C: molecular biology and contribution to the pathogenesis of Pseudomonas aeruginosa Antibiot Chemother 44 1991 34 47
    • (1991) Antibiot Chemother , vol.44 , pp. 34-47
    • Vasil, M.L.1    Graham, L.M.2    Ostroff, R.M.3    Shortridge, V.D.4    Vasil, A.I.5
  • 241
    • 0030903343 scopus 로고    scopus 로고
    • Phospholipid metabolism in boar spermatozoa and role of diacylglycerol species in the de novo formation of phosphatidylcholine
    • J.M. Vazquez, and E.R. Roldan Phospholipid metabolism in boar spermatozoa and role of diacylglycerol species in the de novo formation of phosphatidylcholine Mol Reprod Dev 47 1 1997 105 112
    • (1997) Mol Reprod Dev , vol.47 , Issue.1 , pp. 105-112
    • Vazquez, J.M.1    Roldan, E.R.2
  • 242
    • 0026502412 scopus 로고
    • Nucleotide sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell-to-cell spread
    • J.A. Vazquez-Boland, C. Kocks, S. Dramsi, H. Ohayon, C. Geoffroy, and J. Mengaud Nucleotide sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell-to-cell spread Infect Immun 60 1 1992 219 230
    • (1992) Infect Immun , vol.60 , Issue.1 , pp. 219-230
    • Vazquez-Boland, J.A.1    Kocks, C.2    Dramsi, S.3    Ohayon, H.4    Geoffroy, C.5    Mengaud, J.6
  • 244
    • 0032939644 scopus 로고    scopus 로고
    • Ceramides in phospholipid membranes: Effects on bilayer stability and transition to nonlamellar phases
    • M.P. Veiga, J.L. Arrondo, F.M. Goni, and A. Alonso Ceramides in phospholipid membranes: effects on bilayer stability and transition to nonlamellar phases Biophys J 76 1 Pt. 1 1999 342 350
    • (1999) Biophys J , vol.76 , Issue.1 PART 1 , pp. 342-350
    • Veiga, M.P.1    Arrondo, J.L.2    Goni, F.M.3    Alonso, A.4
  • 245
    • 0034700313 scopus 로고    scopus 로고
    • Leaky vesicle fusion induced by phosphatidylinositol-specific phospholipase C: Observation of mixing of vesicular inner monolayers
    • A.V. Villar, A. Alonso, and F.M. Goni Leaky vesicle fusion induced by phosphatidylinositol-specific phospholipase C: observation of mixing of vesicular inner monolayers Biochemistry 39 46 2000 14012 14018
    • (2000) Biochemistry , vol.39 , Issue.46 , pp. 14012-14018
    • Villar, A.V.1    Alonso, A.2    Goni, F.M.3
  • 246
    • 0035815365 scopus 로고    scopus 로고
    • Diacylglycerol effects on phosphatidylinositol-specific phospholipase C activity and vesicle fusion
    • A.V. Villar, F.M. Goni, and A. Alonso Diacylglycerol effects on phosphatidylinositol-specific phospholipase C activity and vesicle fusion FEBS Lett 494 1-2 2001 117 120
    • (2001) FEBS Lett , vol.494 , Issue.12 , pp. 117-120
    • Villar, A.V.1    Goni, F.M.2    Alonso, A.3
  • 247
    • 0344701068 scopus 로고    scopus 로고
    • Phospholipase cleavage of glycosylphosphatidylinositol reconstituted in liposomal membranes
    • A.V. Villar, F.M. Goni, A. Alonso, D.R. Jones, Y. Leon, and I. Varela-Nieto Phospholipase cleavage of glycosylphosphatidylinositol reconstituted in liposomal membranes FEBS Lett 432 3 1998 150 154
    • (1998) FEBS Lett , vol.432 , Issue.3 , pp. 150-154
    • Villar, A.V.1    Goni, F.M.2    Alonso, A.3    Jones, D.R.4    Leon, Y.5    Varela-Nieto, I.6
  • 248
    • 0028215584 scopus 로고
    • Phosphatidylinositol-specific phospholipase C from Bacillus cereus at the lipid-water interface: Interfacial binding, catalysis, and activation
    • J.J. Volwerk, E. Filthuth, O.H. Griffith, and M.K. Jain Phosphatidylinositol-specific phospholipase C from Bacillus cereus at the lipid-water interface: interfacial binding, catalysis, and activation Biochemistry 33 12 1994 3464 3474
    • (1994) Biochemistry , vol.33 , Issue.12 , pp. 3464-3474
    • Volwerk, J.J.1    Filthuth, E.2    Griffith, O.H.3    Jain, M.K.4
  • 249
    • 0025109107 scopus 로고
    • Phosphatidylinositol-specific phospholipase C from Bacillus cereus combines intrinsic phosphotransferase and cyclic phosphodiesterase activities: A 31P NMR study
    • J.J. Volwerk, M.S. Shashidhar, A. Kuppe, and O.H. Griffith Phosphatidylinositol-specific phospholipase C from Bacillus cereus combines intrinsic phosphotransferase and cyclic phosphodiesterase activities: a 31P NMR study Biochemistry 29 35 1990 8056 8062
    • (1990) Biochemistry , vol.29 , Issue.35 , pp. 8056-8062
    • Volwerk, J.J.1    Shashidhar, M.S.2    Kuppe, A.3    Griffith, O.H.4
  • 250
    • 0027957538 scopus 로고
    • Diacylglycerol and hexadecane increase divalent cation-induced lipid mixing rates between phosphatidylserine large unilamellar vesicles
    • A. Walter, P.L. Yeagle, and D.P. Siegel Diacylglycerol and hexadecane increase divalent cation-induced lipid mixing rates between phosphatidylserine large unilamellar vesicles Biophys J 66 2 Pt. 1 1994 366 376
    • (1994) Biophys J , vol.66 , Issue.2 PART 1 , pp. 366-376
    • Walter, A.1    Yeagle, P.L.2    Siegel, D.P.3
  • 251
    • 0037216849 scopus 로고    scopus 로고
    • Sphingolipid partitioning into ordered domains in cholesterol-free and cholesterol-containing lipid bilayers
    • T.Y. Wang, and J.R. Silvius Sphingolipid partitioning into ordered domains in cholesterol-free and cholesterol-containing lipid bilayers Biophys J 84 1 2003 367 378
    • (2003) Biophys J , vol.84 , Issue.1 , pp. 367-378
    • Wang, T.Y.1    Silvius, J.R.2
  • 252
    • 24644469893 scopus 로고    scopus 로고
    • Listeria monocytogenes phosphatidylinositol-specific phospholipase C has evolved for virulence by greatly reduced activity on GPI anchors
    • Z. Wei, L.A. Zenewicz, and H. Goldfine Listeria monocytogenes phosphatidylinositol-specific phospholipase C has evolved for virulence by greatly reduced activity on GPI anchors Proc Natl Acad Sci USA 102 36 2005 12927 12931
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.36 , pp. 12927-12931
    • Wei, Z.1    Zenewicz, L.A.2    Goldfine, H.3
  • 253
    • 80053456720 scopus 로고    scopus 로고
    • The correlation between multidomain enzymes and multiple activation mechanisms. The case of phospholipase Cbeta and its membrane interactions
    • H. Weinstein, and S. Scarlata The correlation between multidomain enzymes and multiple activation mechanisms. The case of phospholipase Cbeta and its membrane interactions Biochim Biophys Acta 1808 12 2011 2940 2947
    • (2011) Biochim Biophys Acta , vol.1808 , Issue.12 , pp. 2940-2947
    • Weinstein, H.1    Scarlata, S.2
  • 254
    • 0032728220 scopus 로고    scopus 로고
    • Mammalian phosphoinositide-specific phospholipase C
    • R.L. Williams Mammalian phosphoinositide-specific phospholipase C Biochim Biophys Acta 1441 2-3 1999 255 267
    • (1999) Biochim Biophys Acta , vol.1441 , Issue.23 , pp. 255-267
    • Williams, R.L.1
  • 255
    • 79959356986 scopus 로고    scopus 로고
    • Identification of novel anionic phospholipid binding domains in neutral sphingomyelinase 2 with selective binding preference
    • B.X. Wu, C.J. Clarke, N. Matmati, D. Montefusco, N. Bartke, and Y.A. Hannun Identification of novel anionic phospholipid binding domains in neutral sphingomyelinase 2 with selective binding preference J Biol Chem 286 25 2011 22362 22371
    • (2011) J Biol Chem , vol.286 , Issue.25 , pp. 22362-22371
    • Wu, B.X.1    Clarke, C.J.2    Matmati, N.3    Montefusco, D.4    Bartke, N.5    Hannun, Y.A.6
  • 256
    • 77952937382 scopus 로고    scopus 로고
    • Identification and characterization of murine mitochondria-associated neutral sphingomyelinase (MA-nSMase), the mammalian sphingomyelin phosphodiesterase 5
    • B.X. Wu, V. Rajagopalan, P.L. Roddy, C.J. Clarke, and Y.A. Hannun Identification and characterization of murine mitochondria-associated neutral sphingomyelinase (MA-nSMase), the mammalian sphingomyelin phosphodiesterase 5 J Biol Chem 285 23 2010 17993 18002
    • (2010) J Biol Chem , vol.285 , Issue.23 , pp. 17993-18002
    • Wu, B.X.1    Rajagopalan, V.2    Roddy, P.L.3    Clarke, C.J.4    Hannun, Y.A.5
  • 257
    • 32944473705 scopus 로고    scopus 로고
    • Intestinal alkaline sphingomyelinase hydrolyses and inactivates platelet-activating factor by a phospholipase C activity
    • J. Wu, A. Nilsson, B.A. Jonsson, H. Stenstad, W. Agace, and Y. Cheng Intestinal alkaline sphingomyelinase hydrolyses and inactivates platelet-activating factor by a phospholipase C activity Biochem J 394 Pt. 1 2006 299 308
    • (2006) Biochem J , vol.394 , Issue.PART 1 , pp. 299-308
    • Wu, J.1    Nilsson, A.2    Jonsson, B.A.3    Stenstad, H.4    Agace, W.5    Cheng, Y.6
  • 258
    • 0030930320 scopus 로고    scopus 로고
    • Phosphoinositide-specific phospholipase C delta1 activity toward micellar substrates, inositol 1,2-cyclic phosphate, and other water-soluble substrates: A sequential mechanism and allosteric activation
    • Y. Wu, O. Perisic, R.L. Williams, M. Katan, and M.F. Roberts Phosphoinositide-specific phospholipase C delta1 activity toward micellar substrates, inositol 1,2-cyclic phosphate, and other water-soluble substrates: a sequential mechanism and allosteric activation Biochemistry 36 37 1997 11223 11233
    • (1997) Biochemistry , vol.36 , Issue.37 , pp. 11223-11233
    • Wu, Y.1    Perisic, O.2    Williams, R.L.3    Katan, M.4    Roberts, M.F.5
  • 259
    • 67749120148 scopus 로고    scopus 로고
    • A novel mitochondrial sphingomyelinase in zebrafish cells
    • T. Yabu, A. Shimuzu, and M. Yamashita A novel mitochondrial sphingomyelinase in zebrafish cells J Biol Chem 284 30 2009 20349 20363
    • (2009) J Biol Chem , vol.284 , Issue.30 , pp. 20349-20363
    • Yabu, T.1    Shimuzu, A.2    Yamashita, M.3
  • 260
    • 0024059792 scopus 로고
    • Nucleotide sequence and expression in Escherichia coli of the gene coding for sphingomyelinase of Bacillus cereus
    • A. Yamada, N. Tsukagoshi, S. Udaka, T. Sasaki, S. Makino, and S. Nakamura Nucleotide sequence and expression in Escherichia coli of the gene coding for sphingomyelinase of Bacillus cereus Eur J Biochem/FEBS 175 2 1988 213 220
    • (1988) Eur J Biochem/FEBS , vol.175 , Issue.2 , pp. 213-220
    • Yamada, A.1    Tsukagoshi, N.2    Udaka, S.3    Sasaki, T.4    Makino, S.5    Nakamura, S.6
  • 261
    • 77954709548 scopus 로고    scopus 로고
    • The acid sphingomyelinase/ceramide pathway: Biomedical significance and mechanisms of regulation
    • Y.H. Zeidan, and Y.A. Hannun The acid sphingomyelinase/ceramide pathway: biomedical significance and mechanisms of regulation Curr Mol Med 10 5 2010 454 466
    • (2010) Curr Mol Med , vol.10 , Issue.5 , pp. 454-466
    • Zeidan, Y.H.1    Hannun, Y.A.2
  • 262
    • 20444405028 scopus 로고    scopus 로고
    • Phosphatidylinositol-specific phospholipase C of Bacillus anthracis down-modulates the immune response
    • L.A. Zenewicz, Z. Wei, H. Goldfine, and H. Shen Phosphatidylinositol- specific phospholipase C of Bacillus anthracis down-modulates the immune response J Immunol 174 12 2005 8011 8016
    • (2005) J Immunol , vol.174 , Issue.12 , pp. 8011-8016
    • Zenewicz, L.A.1    Wei, Z.2    Goldfine, H.3    Shen, H.4
  • 264
    • 74549205784 scopus 로고    scopus 로고
    • Degradation of host sphingomyelin is essential for Leishmania virulence
    • O. Zhang, M.C. Wilson, W. Xu, F.F. Hsu, J. Turk, and F.M. Kuhlmann Degradation of host sphingomyelin is essential for Leishmania virulence PLoS Pathog 5 12 2009 e1000692
    • (2009) PLoS Pathog , vol.5 , Issue.12 , pp. 1000692
    • Zhang, O.1    Wilson, M.C.2    Xu, W.3    Hsu, F.F.4    Turk, J.5    Kuhlmann, F.M.6
  • 265
  • 266
    • 0030847158 scopus 로고    scopus 로고
    • Allosteric activation of phosphatidylinositol-specific phospholipase C: Specific phospholipid binding anchors the enzyme to the interface
    • C. Zhou, X. Qian, and M.F. Roberts Allosteric activation of phosphatidylinositol-specific phospholipase C: specific phospholipid binding anchors the enzyme to the interface Biochemistry 36 33 1997 10089 10097
    • (1997) Biochemistry , vol.36 , Issue.33 , pp. 10089-10097
    • Zhou, C.1    Qian, X.2    Roberts, M.F.3
  • 267
    • 0032541972 scopus 로고    scopus 로고
    • Nonessential activation and competitive inhibition of bacterial phosphatidylinositol-specific phospholipase C by short-chain phospholipids and analogues
    • C. Zhou, and M.F. Roberts Nonessential activation and competitive inhibition of bacterial phosphatidylinositol-specific phospholipase C by short-chain phospholipids and analogues Biochemistry 37 46 1998 16430 16439
    • (1998) Biochemistry , vol.37 , Issue.46 , pp. 16430-16439
    • Zhou, C.1    Roberts, M.F.2
  • 268
    • 0031020118 scopus 로고    scopus 로고
    • Activation of phosphatidylinositol-specific phospholipase C toward inositol 1,2-(cyclic)-phosphate
    • C. Zhou, Y. Wu, and M.F. Roberts Activation of phosphatidylinositol- specific phospholipase C toward inositol 1,2-(cyclic)-phosphate Biochemistry 36 2 1997 347 355
    • (1997) Biochemistry , vol.36 , Issue.2 , pp. 347-355
    • Zhou, C.1    Wu, Y.2    Roberts, M.F.3
  • 269
    • 0031711951 scopus 로고    scopus 로고
    • Modulation of enzymatic activity and biological function of Listeria monocytogenes broad-range phospholipase C by amino acid substitutions and by replacement with the Bacillus cereus ortholog
    • W.R. Zuckert, H. Marquis, and H. Goldfine Modulation of enzymatic activity and biological function of Listeria monocytogenes broad-range phospholipase C by amino acid substitutions and by replacement with the Bacillus cereus ortholog Infect Immun 66 10 1998 4823 4831
    • (1998) Infect Immun , vol.66 , Issue.10 , pp. 4823-4831
    • Zuckert, W.R.1    Marquis, H.2    Goldfine, H.3


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