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Volumn 1441, Issue 2-3, 1999, Pages 237-254

Bacterial phosphatidylinositol-specific phospholipase C: Structure, function, and interaction with lipids

Author keywords

Catalytic mechanism; Phosphatidylinositol specific phospholipase C; Phosphodiesterase; Phosphoinositide specific phospholipase C; Phosphotransferase

Indexed keywords

ISOENZYME; PHOSPHOLIPASE C;

EID: 0032698808     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1388-1981(99)00153-5     Document Type: Review
Times cited : (102)

References (53)
  • 1
    • 0025976408 scopus 로고
    • Identification of phosphatidylinositol-specific phospholipase C activity in Listeria monocytogenes: A novel type of virulence factor?
    • Mengaud J., Braun-Breton C., Cossart P. Identification of phosphatidylinositol-specific phospholipase C activity in Listeria monocytogenes: a novel type of virulence factor? Mol. Microbiol. 5:1991;367-372.
    • (1991) Mol. Microbiol. , vol.5 , pp. 367-372
    • Mengaud, J.1    Braun-Breton, C.2    Cossart, P.3
  • 2
    • 0027360072 scopus 로고
    • Cloning, expression, and mutagenesis of phosphatidylinositol-specific phospholipase C from Staphylococcus aureus: A potential staphylococcal virulence factor
    • Daugherty S., Low M.G. Cloning, expression, and mutagenesis of phosphatidylinositol-specific phospholipase C from Staphylococcus aureus: a potential staphylococcal virulence factor. Infect. Immun. 61:1993;5078-5089.
    • (1993) Infect. Immun. , vol.61 , pp. 5078-5089
    • Daugherty, S.1    Low, M.G.2
  • 3
    • 0029028599 scopus 로고
    • Mammalian glycosylphosphatidylinositol-anchored proteins and intracellular precursors
    • Hirose S., Knez J.J., Medof M.E. Mammalian glycosylphosphatidylinositol-anchored proteins and intracellular precursors. Methods Enzymol. 250:1995;582-614.
    • (1995) Methods Enzymol. , vol.250 , pp. 582-614
    • Hirose, S.1    Knez, J.J.2    Medof, M.E.3
  • 4
    • 0032579314 scopus 로고    scopus 로고
    • Structural and mechanistic comparison of prokaryotic and eukaryotic phosphoinositide-specific phospholipases C
    • Heinz D.W., Essen L.O., Williams R.L. Structural and mechanistic comparison of prokaryotic and eukaryotic phosphoinositide-specific phospholipases C. J. Mol. Biol. 275:1998;635-650.
    • (1998) J. Mol. Biol. , vol.275 , pp. 635-650
    • Heinz, D.W.1    Essen, L.O.2    Williams, R.L.3
  • 5
    • 0032497846 scopus 로고    scopus 로고
    • Families of phosphoinositide-specific phospholipase C: Structure and function
    • Katan M. Families of phosphoinositide-specific phospholipase C: structure and function. Biochim. Biophys. Acta. 1436:1998;5-17.
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 5-17
    • Katan, M.1
  • 6
    • 0017086018 scopus 로고
    • Studies on phosphatidylinositol phosphodiesterase (phospholipase C type) of Bacillus cereus. I. purification, properties and phosphatase- releasing activity
    • Ikezawa H., Yamanegi M., Taguchi R., Miyashita T., Ohyabu T. Studies on phosphatidylinositol phosphodiesterase (phospholipase C type) of Bacillus cereus. I. purification, properties and phosphatase- releasing activity. Biochim. Biophys. Acta. 450:1976;154-164.
    • (1976) Biochim. Biophys. Acta , vol.450 , pp. 154-164
    • Ikezawa, H.1    Yamanegi, M.2    Taguchi, R.3    Miyashita, T.4    Ohyabu, T.5
  • 8
    • 0028373202 scopus 로고
    • Toward the mechanism of phosphoinositide-specific phospholipases C
    • Bruzik K.S., Tsai M.D. Toward the mechanism of phosphoinositide-specific phospholipases C. Bioorg. Med. Chem. 2:1994;49-72.
    • (1994) Bioorg. Med. Chem. , vol.2 , pp. 49-72
    • Bruzik, K.S.1    Tsai, M.D.2
  • 9
    • 0024971573 scopus 로고
    • Functional characteristics of phosphatidylinositol-specific phospholipases C from Bacillus cereus and Bacillus thuringiensis
    • Volwerk J.J., Koke J.A., Wetherwax P.B., Griffith O.H. Functional characteristics of phosphatidylinositol-specific phospholipases C from Bacillus cereus and Bacillus thuringiensis. FEMS Microbiol. Lett. 52:1989;237-241.
    • (1989) FEMS Microbiol. Lett. , vol.52 , pp. 237-241
    • Volwerk, J.J.1    Koke, J.A.2    Wetherwax, P.B.3    Griffith, O.H.4
  • 10
    • 0032496273 scopus 로고    scopus 로고
    • Catalytic domain of phosphoinositide-specific phospholipase C (PLC). Mutational analysis of residues within the active site and hydrophobic ridge of PLCδ1
    • Ellis M.V., James S.R., Perisic O., Downes C.P., Williams R.L., Katan M. Catalytic domain of phosphoinositide-specific phospholipase C (PLC). Mutational analysis of residues within the active site and hydrophobic ridge of PLCδ1. J. Biol. Chem. 273:1998;11650-11659.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11650-11659
    • Ellis, M.V.1    James, S.R.2    Perisic, O.3    Downes, C.P.4    Williams, R.L.5    Katan, M.6
  • 11
    • 0026754645 scopus 로고
    • Substrate stereospecificity of phosphatidylinositol-specific phospholipase C from Bacillus cereus examined using the resolved enantiomers of synthetic myo-inositol 1-(4-nitrophenyl phosphate)
    • Leigh A.J., Volwerk J.J., Griffith O.H., Keana J.F. Substrate stereospecificity of phosphatidylinositol-specific phospholipase C from Bacillus cereus examined using the resolved enantiomers of synthetic myo-inositol 1-(4-nitrophenyl phosphate). Biochemistry. 31:1992;8978-8983.
    • (1992) Biochemistry , vol.31 , pp. 8978-8983
    • Leigh, A.J.1    Volwerk, J.J.2    Griffith, O.H.3    Keana, J.F.4
  • 12
    • 0027203487 scopus 로고
    • Substrate requirements of bacterial phosphatidylinositol-specific phospholipase C
    • Lewis K.A., Garigapati V.R., Zhou C., Roberts M.F. Substrate requirements of bacterial phosphatidylinositol-specific phospholipase C. Biochemistry. 32:1993;8836-8841.
    • (1993) Biochemistry , vol.32 , pp. 8836-8841
    • Lewis, K.A.1    Garigapati, V.R.2    Zhou, C.3    Roberts, M.F.4
  • 13
    • 0028142014 scopus 로고
    • Are D- And L-chiro-phosphoinositides substrates of phosphatidylinositol-specific phospholipase C?
    • Bruzik K.S., Hakeem A.A., Tsai M.D. Are D- and L-chiro-phosphoinositides substrates of phosphatidylinositol-specific phospholipase C? Biochemistry. 33:1994;8367-8374.
    • (1994) Biochemistry , vol.33 , pp. 8367-8374
    • Bruzik, K.S.1    Hakeem, A.A.2    Tsai, M.D.3
  • 14
    • 0026717417 scopus 로고
    • Phospholipids chiral at phosphorus. Stereochemical mechanism for the formation of inositol 1-phosphate catalyzed by phosphatidylinositol-specific phospholipase C
    • Bruzik K.S., Morocho A.M., Jhon D.-Y., Rhee S.G., Tsai M.-D. Phospholipids chiral at phosphorus. Stereochemical mechanism for the formation of inositol 1-phosphate catalyzed by phosphatidylinositol-specific phospholipase C. Biochemistry. 31:1992;5183-5193.
    • (1992) Biochemistry , vol.31 , pp. 5183-5193
    • Bruzik, K.S.1    Morocho, A.M.2    Jhon, D.-Y.3    Rhee, S.G.4    Tsai, M.-D.5
  • 15
    • 0028276578 scopus 로고
    • The detection of phospholipase-resistant and -sensitive glycosyl-phosphatidylinositol membrane anchors by western blotting
    • Guther M.L., Cardoso de Almeida M.L., Rosenberry T.L., Ferguson M.A.J. The detection of phospholipase-resistant and -sensitive glycosyl-phosphatidylinositol membrane anchors by western blotting. Anal. Biochem. 219:1994;249-255.
    • (1994) Anal. Biochem. , vol.219 , pp. 249-255
    • Guther, M.L.1    Cardoso De Almeida, M.L.2    Rosenberry, T.L.3    Ferguson, M.A.J.4
  • 16
    • 0024316809 scopus 로고
    • The glycosyl-phosphatidylinositol anchor of membrane proteins
    • Low M.G. The glycosyl-phosphatidylinositol anchor of membrane proteins. Biochim. Biophys. Acta. 988:1989;427-454.
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 427-454
    • Low, M.G.1
  • 17
    • 0031590269 scopus 로고    scopus 로고
    • The surface glycoconjugates of trypanosomatid parasites
    • Ferguson M.A.J. The surface glycoconjugates of trypanosomatid parasites. Phil. Trans. R. Soc. Lond. B. 352:1997;1295-1302.
    • (1997) Phil. Trans. R. Soc. Lond. B , vol.352 , pp. 1295-1302
    • Ferguson, M.A.J.1
  • 18
    • 0028000871 scopus 로고
    • Proteins on the surface of the malaria parasite and cell invasion
    • Holder A.A. Proteins on the surface of the malaria parasite and cell invasion. Parasitology. 108:1994;S5-S18.
    • (1994) Parasitology , vol.108
    • Holder, A.A.1
  • 21
    • 0027461517 scopus 로고
    • Structural requirements of phosphatidylinositol-specific phospholipase C δ1 for enzyme activity
    • Ellis M.V., Carne A., Katan M. Structural requirements of phosphatidylinositol-specific phospholipase C δ1 for enzyme activity. Eur. J. Biochem. 213:1993;339-347.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 339-347
    • Ellis, M.V.1    Carne, A.2    Katan, M.3
  • 22
    • 0029137828 scopus 로고
    • The structure and evolution of α/β barrel proteins
    • Reardon D., Farber G.K. The structure and evolution of α/β barrel proteins. FASEB J. 9:1995;497-503.
    • (1995) FASEB J. , vol.9 , pp. 497-503
    • Reardon, D.1    Farber, G.K.2
  • 23
    • 0029121937 scopus 로고
    • Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol
    • Heinz D.W., Ryan M., Bullock T.L., Griffith O.H. Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol. EMBO J. 14:1995;3855-3863.
    • (1995) EMBO J. , vol.14 , pp. 3855-3863
    • Heinz, D.W.1    Ryan, M.2    Bullock, T.L.3    Griffith, O.H.4
  • 24
    • 0031576330 scopus 로고    scopus 로고
    • Crystal structure of the phosphatidylinositol-specific phospholipase C from the human pathogen Listeria monocytogenes
    • Moser J., Gerstel B., Meyer J.E., Chakraborty T., Wehland J., Heinz D.W. Crystal structure of the phosphatidylinositol-specific phospholipase C from the human pathogen Listeria monocytogenes. J. Mol. Biol. 273:1997;269-282.
    • (1997) J. Mol. Biol. , vol.273 , pp. 269-282
    • Moser, J.1    Gerstel, B.2    Meyer, J.E.3    Chakraborty, T.4    Wehland, J.5    Heinz, D.W.6
  • 26
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ
    • Essen L.O., Perisic O., Cheung R., Katan M., Williams R.L. Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ Nature. 380:1996;595-602.
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 27
    • 0029973194 scopus 로고    scopus 로고
    • Synthesis, structure activity relationships, and the effect of polyethylene glycol on inhibitors of phosphatidylinositol-specific phospholipase C from Bacillus cereus
    • Ryan M., Smith M.P., Vinod T.K., Lau W.L., Keana J.F.W., Griffith O.H. Synthesis, structure activity relationships, and the effect of polyethylene glycol on inhibitors of phosphatidylinositol-specific phospholipase C from Bacillus cereus. J. Med. Chem. 39:1996;4366-4376.
    • (1996) J. Med. Chem. , vol.39 , pp. 4366-4376
    • Ryan, M.1    Smith, M.P.2    Vinod, T.K.3    Lau, W.L.4    Keana, J.F.W.5    Griffith, O.H.6
  • 28
    • 0026006923 scopus 로고
    • Glycosyl-phosphatidylinositol anchored acetylcholinesterase as substrate for phosphatidylinositol-specific phospholipase C from Bacillus cereus
    • Stieger S., Brodbeck U. Glycosyl-phosphatidylinositol anchored acetylcholinesterase as substrate for phosphatidylinositol-specific phospholipase C from Bacillus cereus. Biochimie. 73:1991;1179-1186.
    • (1991) Biochimie , vol.73 , pp. 1179-1186
    • Stieger, S.1    Brodbeck, U.2
  • 29
    • 0030608855 scopus 로고    scopus 로고
    • a values of the histidine side chains of phosphatidylinositol-specific phospholipase C from Bacillus cereus by NMR spectroscopy and site-directed mutagenesis
    • a values of the histidine side chains of phosphatidylinositol-specific phospholipase C from Bacillus cereus by NMR spectroscopy and site-directed mutagenesis. Protein Sci. 6:1997;1937-1944.
    • (1997) Protein Sci. , vol.6 , pp. 1937-1944
    • Liu, T.1    Ryan, M.2    Dahlquist, F.W.3    Griffith, O.H.4
  • 30
    • 0032584280 scopus 로고    scopus 로고
    • Mechanism of phosphatidylinositol-specific phospholipase C: A unified view of the mechanism of catalysis
    • Hondal R.J., Zhao Z., Kravchuk A.V., Liao H., Riddle S.R., Yue X., Bruzik K.S., Tsai M.D. Mechanism of phosphatidylinositol-specific phospholipase C: a unified view of the mechanism of catalysis. Biochemistry. 37:1998;4568-4580.
    • (1998) Biochemistry , vol.37 , pp. 4568-4580
    • Hondal, R.J.1    Zhao, Z.2    Kravchuk, A.V.3    Liao, H.4    Riddle, S.R.5    Yue, X.6    Bruzik, K.S.7    Tsai, M.D.8
  • 31
    • 0344817090 scopus 로고    scopus 로고
    • Characterization of the histidine residues of B. cereus phosphatidylinositol-specifc phospholipase C by NMR
    • in: K.S. Bruzik (Ed.) American Chemical Society, Washington, DC
    • T. Liu, M. Ryan, F.W. Dahlquist, O.H. Griffith, Characterization of the histidine residues of B. cereus phosphatidylinositol-specifc phospholipase C by NMR, in: K.S. Bruzik (Ed.), Phosphoinositides: Chemistry, Biochemistry, and Biomedical Applications, American Chemical Society, Washington, DC, 1998, pp. 91-108.
    • (1998) Phosphoinositides: Chemistry, Biochemistry, and Biomedical Applications , pp. 91-108
    • Liu, T.1    Ryan, M.2    Dahlquist, F.W.3    Griffith, O.H.4
  • 32
    • 0030734269 scopus 로고    scopus 로고
    • NMR studies of the role of hydrogen bonding in the mechanism of triosephosphate isomerase
    • Harris T.K., Abeygunawardana C., Mildvan A.S. NMR studies of the role of hydrogen bonding in the mechanism of triosephosphate isomerase. Biochemistry. 36:1997;14661-14675.
    • (1997) Biochemistry , vol.36 , pp. 14661-14675
    • Harris, T.K.1    Abeygunawardana, C.2    Mildvan, A.S.3
  • 33
    • 0030937806 scopus 로고    scopus 로고
    • A new concept for the mechanism of action of chymotrypsin: The role of the low-barrier hydrogen bond
    • Cassidy C.S., Lin J., Frey P.A. A new concept for the mechanism of action of chymotrypsin: the role of the low-barrier hydrogen bond. Biochemistry. 36:1997;4576-4584.
    • (1997) Biochemistry , vol.36 , pp. 4576-4584
    • Cassidy, C.S.1    Lin, J.2    Frey, P.A.3
  • 34
    • 0002455712 scopus 로고
    • Mechanistic principles of enzyme-cleavage of phosphodiester bonds
    • in: S.M. Linn, R.S. Lloyd, R.J. Roberts (Eds.) Cold Spring Harbor Laboratory Press, New York
    • J.A. Gerlt, Mechanistic principles of enzyme-cleavage of phosphodiester bonds, in: S.M. Linn, R.S. Lloyd, R.J. Roberts (Eds.), Nucleases, 2nd ed., Cold Spring Harbor Laboratory Press, New York, 1993, pp. 1-34.
    • (1993) Nucleases, 2nd Ed. , pp. 1-34
    • Gerlt, J.A.1
  • 35
    • 0028806062 scopus 로고
    • Bovine pancreatic ribonuclease A as a model of an enzyme with multiple substrate binding sites
    • Nogues M.V., Vilanova M., Cuchillo C.M. Bovine pancreatic ribonuclease A as a model of an enzyme with multiple substrate binding sites. Biochim. Biophys. Acta. 1253:1995;16-24.
    • (1995) Biochim. Biophys. Acta , vol.1253 , pp. 16-24
    • Nogues, M.V.1    Vilanova, M.2    Cuchillo, C.M.3
  • 36
    • 0025356027 scopus 로고
    • Phospholipids chiral at phosphorus. Stereochemical mechanism of reactions catalyzed by phosphatidylinositide-specific phospholipase C from Bacillus cereus and guinea pig uterus
    • Lin G.L., Bennett C.F., Tsai M.D. Phospholipids chiral at phosphorus. Stereochemical mechanism of reactions catalyzed by phosphatidylinositide-specific phospholipase C from Bacillus cereus and guinea pig uterus. Biochemistry. 29:1990;2747-2757.
    • (1990) Biochemistry , vol.29 , pp. 2747-2757
    • Lin, G.L.1    Bennett, C.F.2    Tsai, M.D.3
  • 37
    • 0041558701 scopus 로고    scopus 로고
    • Probing the roles of active site residues in phosphatidylinositol-specific phospholipase C from Bacillus cereus by site-directed mutagenesis
    • Gässler C.S., Ryan M., Liu T., Griffith O.H., Heinz D.W. Probing the roles of active site residues in phosphatidylinositol-specific phospholipase C from Bacillus cereus by site-directed mutagenesis. Biochemistry. 36:1997;12802-12813.
    • (1997) Biochemistry , vol.36 , pp. 12802-12813
    • Gässler, C.S.1    Ryan, M.2    Liu, T.3    Griffith, O.H.4    Heinz, D.W.5
  • 38
    • 0030995602 scopus 로고    scopus 로고
    • Phosphatidylinositol-specific phospholipase C: Kinetic and stereochemical evidence for an interaction between arginine-69 and the phosphate group of phosphatidylinositol
    • Hondal R.J., Riddle S.R., Kravchuk A.V., Zhao Z., Liao H., Bruzik K.S., Tsai M.D. Phosphatidylinositol-specific phospholipase C: kinetic and stereochemical evidence for an interaction between arginine-69 and the phosphate group of phosphatidylinositol. Biochemistry. 36:1997;6633-6642.
    • (1997) Biochemistry , vol.36 , pp. 6633-6642
    • Hondal, R.J.1    Riddle, S.R.2    Kravchuk, A.V.3    Zhao, Z.4    Liao, H.5    Bruzik, K.S.6    Tsai, M.D.7
  • 39
    • 0033585566 scopus 로고    scopus 로고
    • Identification of a novel catalytic triad with dual functions in enzymatic cleavage of the P-O bond
    • Kubiak R.J., Hondal R.J., Yue X., Tsai M.-D., Bruzik K.S. Identification of a novel catalytic triad with dual functions in enzymatic cleavage of the P-O bond. J. Am. Chem. Soc. 121:1999;488-489.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 488-489
    • Kubiak, R.J.1    Hondal, R.J.2    Yue, X.3    Tsai, M.-D.4    Bruzik, K.S.5
  • 40
    • 0026733844 scopus 로고
    • Kinetics of Bacillus cereus phosphatidylinositol-specific phospholipase C with thiophosphate and fluorescent analogs of phosphatidylinositol
    • Hendrickson H.S., Hendrickson E.K., Johnson J.L., Khan T.H., Chial H.J. Kinetics of Bacillus cereus phosphatidylinositol-specific phospholipase C with thiophosphate and fluorescent analogs of phosphatidylinositol. Biochemistry. 31:1992;12169-12172.
    • (1992) Biochemistry , vol.31 , pp. 12169-12172
    • Hendrickson, H.S.1    Hendrickson, E.K.2    Johnson, J.L.3    Khan, T.H.4    Chial, H.J.5
  • 41
    • 0028215584 scopus 로고
    • Phosphatidylinositol-specific phospholipase C from Bacillus cereus at the lipid-water interface: Interfacial binding, catalysis, and activation
    • Volwerk J.J., Filthuth E., Griffith O.H., Jain M.K. Phosphatidylinositol-specific phospholipase C from Bacillus cereus at the lipid-water interface: interfacial binding, catalysis, and activation. Biochemistry. 33:1994;3464-3474.
    • (1994) Biochemistry , vol.33 , pp. 3464-3474
    • Volwerk, J.J.1    Filthuth, E.2    Griffith, O.H.3    Jain, M.K.4
  • 43
    • 0032541972 scopus 로고    scopus 로고
    • Nonessential activation and competitive inhibition of bacterial phosphatidylinositol-specific phospholipase C by short-chain phospholipids and analogues
    • Zhou C., Roberts M.F. Nonessential activation and competitive inhibition of bacterial phosphatidylinositol-specific phospholipase C by short-chain phospholipids and analogues. Biochemistry. 37:1998;16430-16439.
    • (1998) Biochemistry , vol.37 , pp. 16430-16439
    • Zhou, C.1    Roberts, M.F.2
  • 44
    • 0031020118 scopus 로고    scopus 로고
    • Activation of phosphatidylinositol-specific phospholipase C toward inositol 1,2-(cyclic)-phosphate
    • Zhou C., Wu Y., Roberts M.F. Activation of phosphatidylinositol-specific phospholipase C toward inositol 1,2-(cyclic)-phosphate. Biochemistry. 36:1997;347-355.
    • (1997) Biochemistry , vol.36 , pp. 347-355
    • Zhou, C.1    Wu, Y.2    Roberts, M.F.3
  • 45
    • 0029740871 scopus 로고    scopus 로고
    • Crystal structure of phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with glucosaminyl(α1→6)-D-myo-inositol, an essential fragment of GPI anchors
    • Heinz D.W., Ryan M., Smith M.P., Weaver L.H., Keana J.F.W., Griffith O.H. Crystal structure of phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with glucosaminyl(α1→6)-D-myo-inositol, an essential fragment of GPI anchors. Biochemistry. 35:1996;9496-9504.
    • (1996) Biochemistry , vol.35 , pp. 9496-9504
    • Heinz, D.W.1    Ryan, M.2    Smith, M.P.3    Weaver, L.H.4    Keana, J.F.W.5    Griffith, O.H.6
  • 47
    • 0028790095 scopus 로고
    • Anchoring of tryptophan and tyrosine analogs at the hydrocarbon-polar boundary in model membrane vesicles: Parallax analysis of fluorescence quenching induced by nitroxide-labeled phospholipids
    • Kachel K., Asuncion-Punzalan E., London E. Anchoring of tryptophan and tyrosine analogs at the hydrocarbon-polar boundary in model membrane vesicles: parallax analysis of fluorescence quenching induced by nitroxide-labeled phospholipids. Biochemistry. 34:1995;15475-15479.
    • (1995) Biochemistry , vol.34 , pp. 15475-15479
    • Kachel, K.1    Asuncion-Punzalan, E.2    London, E.3
  • 48
    • 0032558436 scopus 로고    scopus 로고
    • 2 has a dramatically increased ability to hydrolyze phosphatidylcholine vesicles and cell membranes
    • 2 has a dramatically increased ability to hydrolyze phosphatidylcholine vesicles and cell membranes. Biochemistry. 37:1998;13203-13211.
    • (1998) Biochemistry , vol.37 , pp. 13203-13211
    • Baker, S.F.1    Othman, R.2    Wilton, D.C.3
  • 49
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-949.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-949
    • Kraulis, P.J.1
  • 50
    • 0002709844 scopus 로고    scopus 로고
    • Swiss-PdbViewer: A fast and easy-to-use PDB viewer for Macintosh and PC
    • Guex N., Peitsch M.C. Swiss-PdbViewer: a fast and easy-to-use PDB viewer for Macintosh and PC. Protein Data Bank Q. Newslett. 77:1996;7.
    • (1996) Protein Data Bank Q. Newslett. , vol.77 , pp. 7
    • Guex, N.1    Peitsch, M.C.2
  • 53
    • 0019882643 scopus 로고
    • Preferred conformation and molecular packing of phosphatidylethanolamine and phosphatidylcholine
    • Hauser H., Pascher I., Pearson R.H., Sundell S. Preferred conformation and molecular packing of phosphatidylethanolamine and phosphatidylcholine. Biochim. Biophys. Acta. 650:1981;21-51.
    • (1981) Biochim. Biophys. Acta , vol.650 , pp. 21-51
    • Hauser, H.1    Pascher, I.2    Pearson, R.H.3    Sundell, S.4


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