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Volumn 21, Issue 4, 2002, Pages 391-421

The structure and function of pardaxin

Author keywords

Arachidonic acid; Calcium; Cell death; MAPK; Neurotoxin; Neurotransmitter release; Pardaxin; PIA2; Pore; Signal transduction; Structure; Tool

Indexed keywords

ARACHIDONIC ACID; CALCIUM; CELL ENZYME; DOPAMINE; ICOSANOID; ION CHANNEL; MITOGEN ACTIVATED PROTEIN KINASE; PARDAXIN; PHOSPHATIDYLETHANOLAMINE; PROSTAGLANDIN;

EID: 0036449590     PISSN: 07313837     EISSN: None     Source Type: Journal    
DOI: 10.1081/TXR-120014410     Document Type: Review
Times cited : (8)

References (79)
  • 1
    • 0027354448 scopus 로고
    • Storage and release of neurotransmitters
    • Kelly, R.B. Storage and release of neurotransmitters. Cell 1993, 72, 43.
    • (1993) Cell , vol.72 , pp. 43
    • Kelly, R.B.1
  • 2
    • 0026071367 scopus 로고
    • Cellular and molecular biology of the presynaptic nerve terminal
    • Trimble, W.S.; Linial, M.; Scheller, R.H. Cellular and molecular biology of the presynaptic nerve terminal. Annu. Rev. Neurosci. 1991, 14, 93.
    • (1991) Annu. Rev. Neurosci. , vol.14 , pp. 93
    • Trimble, W.S.1    Linial, M.2    Scheller, R.H.3
  • 3
    • 0030763651 scopus 로고    scopus 로고
    • SNARE proteins - Why so many? Why so few?
    • Linial, M. SNARE proteins - Why so many? Why so few? J. Neurochem. 1997, 69, 1781.
    • (1997) J. Neurochem. , vol.69 , pp. 1781
    • Linial, M.1
  • 5
    • 0009575404 scopus 로고    scopus 로고
    • W-toxins, Calcium Channels and Neurosecretion
    • Gutman, Y., Lazarovici, P., Eds.; Harwood Academic Publishers: Amsterdam, The Netherlands
    • Garcia, A.G.; Albillos, A.; Gandia, L.; Lopez, M.G.; Michelena, P.; Montiel, C. W-toxins, Calcium Channels and Neurosecretion. In Toxins and Signal Transduction; Gutman, Y., Lazarovici, P., Eds.; Harwood Academic Publishers: Amsterdam, The Netherlands, 1997; 155.
    • (1997) Toxins and Signal Transduction , pp. 155
    • Garcia, A.G.1    Albillos, A.2    Gandia, L.3    Lopez, M.G.4    Michelena, P.5    Montiel, C.6
  • 7
    • 0000907084 scopus 로고    scopus 로고
    • Clostridial Neurotoxins as Enzymes: Structure and Function
    • Linial, M., Grasso, A., Lazarovici, P., Eds.; Harwood Academic Publishers: Amsterdam, The Netherlands
    • Montecucco, C.; Pellizzari, R.; Rossetto, O.; Schiavo, G.; Tonello, F.; Washbourne, F. Clostridial Neurotoxins as Enzymes: Structure and Function. In Secretory Systems and Toxins; Linial, M., Grasso, A., Lazarovici, P., Eds.; Harwood Academic Publishers: Amsterdam, The Netherlands, 1998; 315.
    • (1998) Secretory Systems and Toxins , pp. 315
    • Montecucco, C.1    Pellizzari, R.2    Rossetto, O.3    Schiavo, G.4    Tonello, F.5    Washbourne, F.6
  • 8
    • 0002301108 scopus 로고
    • α-Latrotoxin as a Tool for Studying Ionic Channels and Transmitter Release Process
    • Dolly, O.J., Ed.; J. Wiley and Sons: Chichester, England
    • Grasso, A. α-Latrotoxin as a Tool for Studying Ionic Channels and Transmitter Release Process. In Neurotoxins in Neurochemistry; Dolly, O.J., Ed.; J. Wiley and Sons: Chichester, England, 1988; 67.
    • (1988) Neurotoxins in Neurochemistry , pp. 67
    • Grasso, A.1
  • 9
    • 0028300286 scopus 로고
    • Can exocytosis inudced by α-latrotoxin be explained solely by its channel-forming activity?
    • Surkova, I. Can exocytosis inudced by α-latrotoxin be explained solely by its channel-forming activity? Ann. N. Y. Acad. Sci. 1994, 710, 48.
    • (1994) Ann. N. Y. Acad. Sci. , vol.710 , pp. 48
    • Surkova, I.1
  • 10
    • 0001504255 scopus 로고    scopus 로고
    • Ionophore polypeptide toxins and signal transduction
    • Gutman, Y., Lazarovici, P., Eds.; Harwood Academic Publishers: Amsterdam, The Netherlands
    • Bloch-Shilderman, E.; Abu-Raya, S.; Lazarovici, P. Ionophore polypeptide toxins and signal transduction. In Toxins and Signal Transduction; Gutman, Y., Lazarovici, P., Eds.; Harwood Academic Publishers: Amsterdam, The Netherlands, 1997; 211.
    • (1997) Toxins and Signal Transduction , pp. 211
    • Bloch-Shilderman, E.1    Abu-Raya, S.2    Lazarovici, P.3
  • 11
    • 0002354047 scopus 로고
    • Cytolytic toxins
    • Shier, W.T., Mebs, D., Eds.; Marcel Dekker, Inc.: New York
    • Harvey, A.L. Cytolytic toxins. In Handbook of Toxinology; Shier, W.T., Mebs, D., Eds.; Marcel Dekker, Inc.: New York, 1990; 1.
    • (1990) Handbook of Toxinology , pp. 1
    • Harvey, A.L.1
  • 14
    • 0022869696 scopus 로고
    • Purification and pore forming activity of two hydrophobic polypeptides from the secretion of the Red Sea Moses sole (Pardachirus marmoratus)
    • Lazarovici, P.; Primor, N.; Loew, L.M. Purification and pore forming activity of two hydrophobic polypeptides from the secretion of the Red Sea Moses sole (Pardachirus marmoratus). J. Biol. Chem. 1986, 261, 16704.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16704
    • Lazarovici, P.1    Primor, N.2    Loew, L.M.3
  • 15
    • 0024292077 scopus 로고
    • Sequencing and synthesis of pardaxin, a polypeptide from the Red Sea Moses sole with ionophore activity
    • Shai, Y.; Fox, J.; Caratsch, C.; Shih, Y.; Edwards, C.; Lazarovici, P. Sequencing and synthesis of pardaxin, a polypeptide from the Red Sea Moses sole with ionophore activity. FEBS Lett. 1988, 242, 161.
    • (1988) FEBS Lett. , vol.242 , pp. 161
    • Shai, Y.1    Fox, J.2    Caratsch, C.3    Shih, Y.4    Edwards, C.5    Lazarovici, P.6
  • 17
    • 0021717207 scopus 로고
    • Pavonins: Shark-repelling ichthyotoxins from the defense secretion of the Pacific sole
    • Tachibana, K.; Sakaitanai, M.; Nakanishi, K. Pavonins: Shark-repelling ichthyotoxins from the defense secretion of the Pacific sole. Science 1986, 226, 703.
    • (1986) Science , vol.226 , pp. 703
    • Tachibana, K.1    Sakaitanai, M.2    Nakanishi, K.3
  • 18
    • 0001613365 scopus 로고
    • Mellitin-like peptide from the shark-repelling defense secretion of the sole Pardachirus pavoninus
    • Thompson, S.A.; Tachibana, K.; Nakanishi, K.; Kubota, I. Mellitin-like peptide from the shark-repelling defense secretion of the sole Pardachirus pavoninus. Science 1986, 233, 341.
    • (1986) Science , vol.233 , pp. 341
    • Thompson, S.A.1    Tachibana, K.2    Nakanishi, K.3    Kubota, I.4
  • 21
    • 0021152462 scopus 로고
    • Three-dimensional structure of membrane and surface proteins
    • Eisenberg, D. Three-dimensional structure of membrane and surface proteins. Ann. Rev. Biochem. 1984, 53, 595.
    • (1984) Ann. Rev. Biochem. , vol.53 , pp. 595
    • Eisenberg, D.1
  • 22
    • 0002159463 scopus 로고
    • Secondary structure, permeability and molecular modeling of pardaxin pores
    • Lazarovici, P.; Edwards, C.; Raghunathan, G.; Guy, H.R., Secondary structure, permeability and molecular modeling of pardaxin pores. J. Nat. Toxins 1992, 1, 1.
    • (1992) J. Nat. Toxins , vol.1 , pp. 1
    • Lazarovici, P.1    Edwards, C.2    Raghunathan, G.3    Guy, H.R.4
  • 23
    • 0002223128 scopus 로고
    • Surfactant and Channel-forming Activities of the Moses Sole Toxin
    • Bolis, L., Zadunaisky, J., Gilles, R., Eds.; Springer Verlag: Berlin
    • Moran, A.; Korchak, Z.; Moran, N.; Primor, N. Surfactant and Channel-forming Activities of the Moses Sole Toxin. In Toxins, Drugs and Pollutants in Marine Animals; Bolis, L., Zadunaisky, J., Gilles, R., Eds.; Springer Verlag: Berlin, 1984; 13.
    • (1984) Toxins, Drugs and Pollutants in Marine Animals , pp. 13
    • Moran, A.1    Korchak, Z.2    Moran, N.3    Primor, N.4
  • 24
    • 0029019523 scopus 로고
    • Ion selectivity of the channels formed by pardaxin, an ionophore, in bilayer membranes
    • Shi, J.L.; Edwards, C.; Lazarovici, P. Ion selectivity of the channels formed by pardaxin, an ionophore, in bilayer membranes. Nat. Toxins 1995, 3, 151.
    • (1995) Nat. Toxins , vol.3 , pp. 151
    • Shi, J.L.1    Edwards, C.2    Lazarovici, P.3
  • 25
    • 8244256998 scopus 로고
    • Structural Models of Membrane Insertion and Channel Formation by Antiparallel-helical Membrane Peptides
    • Pullman, E., Ed.; Magnes Found: Jerusalem
    • Guy, H.R.; Raghunathan, G. Structural Models of Membrane Insertion and Channel Formation by Antiparallel-helical Membrane Peptides. In Transport Through Membranes: Carriers, Channels and Pumps; Pullman, E., Ed.; Magnes Found: Jerusalem, 1989; 369.
    • (1989) Transport Through Membranes: Carriers, Channels and Pumps , pp. 369
    • Guy, H.R.1    Raghunathan, G.2
  • 26
    • 0025066770 scopus 로고
    • Models of delta-hemolysin membrane channels and crystal structures
    • Raghunathan, G.; Seetharamulu, P.; Brooks, B.; Guy, H.R. Models of delta-hemolysin membrane channels and crystal structures. Proteins 1990, 8, 213.
    • (1990) Proteins , vol.8 , pp. 213
    • Raghunathan, G.1    Seetharamulu, P.2    Brooks, B.3    Guy, H.R.4
  • 27
    • 0025334586 scopus 로고
    • Pursuing the structure and function of voltage-gated channels
    • Guy, H.R.; Conti, F. Pursuing the structure and function of voltage-gated channels. TINS 1990, 13, 201.
    • (1990) TINS , vol.13 , pp. 201
    • Guy, H.R.1    Conti, F.2
  • 28
    • 0026468486 scopus 로고
    • Structure and activity studies on pardaxin and analogues using model membranes of phosphatidylcholine
    • Barrow, C.J.; Nakanishi, K.; Tachibana, K. Structure and activity studies on pardaxin and analogues using model membranes of phosphatidylcholine. Biochem. Biophys. Acta 1992, 1112, 235.
    • (1992) Biochem. Biophys. Acta , vol.1112 , pp. 235
    • Barrow, C.J.1    Nakanishi, K.2    Tachibana, K.3
  • 29
    • 0025245504 scopus 로고
    • Channel formation properties of synthetic pardaxin and analogues
    • Shai, Y.; Nach, D.; Yanovsky, A. Channel formation properties of synthetic pardaxin and analogues. J. Biol. Chem. 1990, 265, 20202.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20202
    • Shai, Y.1    Nach, D.2    Yanovsky, A.3
  • 31
    • 0025748640 scopus 로고
    • pH-Dependent pore formation properties of pardaxin analogues
    • Shai, Y.; Hadari, Y.R.; Finkels, A. pH-Dependent pore formation properties of pardaxin analogues. J. Biol. Chem. 1991, 266, 22346.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22346
    • Shai, Y.1    Hadari, Y.R.2    Finkels, A.3
  • 32
    • 0028221653 scopus 로고
    • Pardaxin: Channel formation by shark repellant peptide from fish
    • Shai, Y. Pardaxin: Channel formation by shark repellant peptide from fish. Toxicology 1994, 87, 109.
    • (1994) Toxicology , vol.87 , pp. 109
    • Shai, Y.1
  • 33
    • 0026758174 scopus 로고
    • Aggregation and organization of pardaxin in phospholipid membranes
    • Rapaport, D.; Shai, Y. Aggregation and organization of pardaxin in phospholipid membranes. J. Biol. Chem. 1992, 267, 6502.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6502
    • Rapaport, D.1    Shai, Y.2
  • 35
    • 0023629686 scopus 로고
    • Presynaptic effects of the pardaxins, polypeptides isolated from the gland secretion of the flatfish Pardachirus marmoratus
    • Renner, P.; Caratsch, C.E.; Waser, P.G.; Lazarovici, P.; Primor, N. Presynaptic effects of the pardaxins, polypeptides isolated from the gland secretion of the flatfish Pardachirus marmoratus. Neuroscience 1987, 23, 319.
    • (1987) Neuroscience , vol.23 , pp. 319
    • Renner, P.1    Caratsch, C.E.2    Waser, P.G.3    Lazarovici, P.4    Primor, N.5
  • 36
    • 0027465996 scopus 로고
    • Calcium-dependent and independent acetylcholine release from electric organ synaptosomes by pardaxin: Evidence of a biphasic action of an excitatory neurotoxin
    • Arribas, M.; Blasi, J.; Lazarovici, P.; Marsal, J. Calcium-dependent and independent acetylcholine release from electric organ synaptosomes by pardaxin: Evidence of a biphasic action of an excitatory neurotoxin. J. Neurochem. 1993, 60, 552.
    • (1993) J. Neurochem. , vol.60 , pp. 552
    • Arribas, M.1    Blasi, J.2    Lazarovici, P.3    Marsal, J.4
  • 37
    • 0345704610 scopus 로고
    • Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor
    • Greene, L.A.; Tischler, A.S. Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor. Proc. Natl. Acad. Sci. U. S. A. 1976, 73, 2424.
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 2424
    • Greene, L.A.1    Tischler, A.S.2
  • 38
    • 0025773144 scopus 로고
    • Control of exocytosis in adrenal chromaffin cells
    • Burgoyne, R.D. Control of exocytosis in adrenal chromaffin cells. Biochem. Biophys. Acta 1991, 1071, 174.
    • (1991) Biochem. Biophys. Acta , vol.1071 , pp. 174
    • Burgoyne, R.D.1
  • 39
    • 0022342760 scopus 로고
    • Minimal requirements for exocytosis: A study using PC12 cells permeabilized with Staphylococcaltoxin
    • Ahnert-Hilger, G.; Bhakdi, S.; Gratzl, M. Minimal requirements for exocytosis: A study using PC12 cells permeabilized with Staphylococcaltoxin. J. Biol. Chem. 1985, 260, 12730.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12730
    • Ahnert-Hilger, G.1    Bhakdi, S.2    Gratzl, M.3
  • 40
    • 0028327453 scopus 로고
    • Challenging catecholamine exocytosis with pardaxin, an excitatory ionophore fish toxin
    • Lazarovici, P. Challenging catecholamine exocytosis with pardaxin, an excitatory ionophore fish toxin. J. Toxicol., Toxin Rev. 1994, 13, 45.
    • (1994) J. Toxicol., Toxin Rev. , vol.13 , pp. 45
    • Lazarovici, P.1
  • 41
    • 0026996702 scopus 로고
    • Pardaxin induces exocytosis in bovine adrenal medullary chromaffin cells independent of calcium
    • Lazarovici, P.; Lelkes, P.I. Pardaxin induces exocytosis in bovine adrenal medullary chromaffin cells independent of calcium. J. Pharmacol. Exp. Ther. 1992, 263, 1317.
    • (1992) J. Pharmacol. Exp. Ther. , vol.263 , pp. 1317
    • Lazarovici, P.1    Lelkes, P.I.2
  • 42
    • 0035985030 scopus 로고    scopus 로고
    • Pardaxin, an ionophore neurotoxin, induces PC12 cell death: Activation of stress kinases and production of reactive oxygen species
    • in press
    • Bloch-Shilderman, E.; Jiang, H.; Lazarovici, P. Pardaxin, an ionophore neurotoxin, induces PC12 cell death: Activation of stress kinases and production of reactive oxygen species. J. Nat. Toxins 2002 (in press).
    • (2002) J. Nat. Toxins
    • Bloch-Shilderman, E.1    Jiang, H.2    Lazarovici, P.3
  • 44
    • 0035127213 scopus 로고    scopus 로고
    • Involvement of extracellular signal-regulated kinase (ERK) in pardaxin-induced dopamine release from PC12 cells
    • Bloch-Shilderman, E.; Jiang, H.; Abu-Raya, S.; Linial, M.; Lazarovici, P. Involvement of extracellular signal-regulated kinase (ERK) in pardaxin-induced dopamine release from PC12 cells. J. Pharmacol. Exp. Ther. 2001, 296, 704.
    • (2001) J. Pharmacol. Exp. Ther. , vol.296 , pp. 704
    • Bloch-Shilderman, E.1    Jiang, H.2    Abu-Raya, S.3    Linial, M.4    Lazarovici, P.5
  • 47
    • 0027233448 scopus 로고
    • Signal transduction via the MAP kinases: Proceed at your own RSK
    • Blenis, J. Signal transduction via the MAP kinases: Proceed at your own RSK. Proc. Natl. Acad. Sci. U. S. A. 1993, 90, 5889.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 5889
    • Blenis, J.1
  • 48
    • 0031600501 scopus 로고    scopus 로고
    • Growth factors and mitogen-activated protein kinases
    • Force, T.; Bonventre, J.V., Growth factors and mitogen-activated protein kinases. Hypertension 1998, 31, 152.
    • (1998) Hypertension , vol.31 , pp. 152
    • Force, T.1    Bonventre, J.V.2
  • 50
    • 0031009434 scopus 로고    scopus 로고
    • Cdc42Hs, but not Rac1, inhibits serum-stimulated cell cycle progression at G1/S through a mechanism requiring p38/RK
    • Molnar, A.; Theodoras, A.M.; Zon, L.I.; Kyriakis, J.M. Cdc42Hs, but not Rac1, inhibits serum-stimulated cell cycle progression at G1/S through a mechanism requiring p38/RK. J. Biol. Chem. 1997, 272, 13229.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13229
    • Molnar, A.1    Theodoras, A.M.2    Zon, L.I.3    Kyriakis, J.M.4
  • 52
    • 0026997568 scopus 로고
    • Pardaxin-stimulated calcium uptake in PC12 cells is blocked by cadmium and is not mediated by L-type calcium channels
    • Nikodijevic, B.; Nikodijevic, D.; Lazarovici, P. Pardaxin-stimulated calcium uptake in PC12 cells is blocked by cadmium and is not mediated by L-type calcium channels. J. Basic Clin. Physiol. Pharmacol. 1992, 3, 359.
    • (1992) J. Basic Clin. Physiol. Pharmacol. , vol.3 , pp. 359
    • Nikodijevic, B.1    Nikodijevic, D.2    Lazarovici, P.3
  • 53
    • 0027270722 scopus 로고
    • Cytolysins increase intracellular calcium and induce eicosanoid release by pheochromocytoma PC12 cell cultures
    • Abu-Raya, S.; Trembovler, V.; Shohami, E.; Lazarovici, P. Cytolysins increase intracellular calcium and induce eicosanoid release by pheochromocytoma PC12 cell cultures. Nat. Toxins 1993, 1, 263.
    • (1993) Nat. Toxins , vol.1 , pp. 263
    • Abu-Raya, S.1    Trembovler, V.2    Shohami, E.3    Lazarovici, P.4
  • 54
    • 0022514851 scopus 로고
    • Increased 5-hydroxytryptamine and norepinephrine release from rat brain slices by the Red Sea flatfish toxin pardaxin
    • Wang, H.Y.; Friedman, E. Increased 5-hydroxytryptamine and norepinephrine release from rat brain slices by the Red Sea flatfish toxin pardaxin. J. Neurochem. 1986, 47, 56.
    • (1986) J. Neurochem. , vol.47 , pp. 56
    • Wang, H.Y.1    Friedman, E.2
  • 55
    • 0000025340 scopus 로고    scopus 로고
    • The role of calcium protein Kinase C, pertussis toxin substrates and eicosanoids on pardaxin-induced dopamine release from PC12 cells
    • Lazarovici, P., Spira, M., Zlotkin, E., Eds.; Alaken, Inc.: Ft. Collins, Colorado
    • Bloch-Shilderman, E.; Abu-Raya, S.; Rasouly, D.; Furman, O.; Trembovler, V.; Shavit, D.; Lelkes, P.I.; Shohami, E.; Gutman, Y.; Lazarovici, P. The Role of Calcium, Protein Kinase C, Pertussis Toxin Substrates and Eicosanoids on Pardaxin-Induced Dopamine Release from PC12 Cells. In Biochemical Aspects of Marine Pharmacology; Lazarovici, P., Spira, M., Zlotkin, E., Eds.; Alaken, Inc.: Ft. Collins, Colorado, 1996; 158.
    • (1996) Biochemical Aspects of Marine Pharmacology , pp. 158
    • Bloch-Shilderman, E.1    Abu-Raya, S.2    Rasouly, D.3    Furman, O.4    Trembovler, V.5    Shavit, D.6    Lelkes, P.I.7    Shohami, E.8    Gutman, Y.9    Lazarovici, P.10
  • 56
    • 0029123782 scopus 로고
    • Purine and pyrimidine nucleotides activate distinct signalling pathways in PC12 cells
    • De Souza, L.R.; Moore, H.; Raha, S.; Reed, J.K. Purine and pyrimidine nucleotides activate distinct signalling pathways in PC12 cells. J. Neurosci. Res. 1995, 41, 753.
    • (1995) J. Neurosci. Res. , vol.41 , pp. 753
    • De Souza, L.R.1    Moore, H.2    Raha, S.3    Reed, J.K.4
  • 60
    • 0022283382 scopus 로고
    • The final steps to toxic cell death
    • Shier, W.T. The final steps to toxic cell death. J. Toxicol., Toxin Rev. 1985, 4, 191.
    • (1985) J. Toxicol., Toxin Rev. , vol.4 , pp. 191
    • Shier, W.T.1
  • 61
    • 0027586519 scopus 로고
    • 2+/calmodulin-dependent protein kinases
    • 2+/calmodulin-dependent protein kinases. Curr. Opin. Cell Biol. 1993, 5, 247.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 247
    • Shulman, H.1
  • 62
    • 0026612475 scopus 로고
    • 2+ signaling pathways converge on CaM kinase in PC12 cells
    • 2+ signaling pathways converge on CaM kinase in PC12 cells. FEBS Lett. 1992, 304, 237.
    • (1992) FEBS Lett. , vol.304 , pp. 237
    • MacNicol, M.1    Shulman, H.2
  • 63
    • 0028115022 scopus 로고
    • Neurotrophin signal transduction by the trk receptor
    • Kaplan, D.R.; Stephens, R.M. Neurotrophin signal transduction by the trk receptor. J. Neurobiol. 1994, 25, 1404.
    • (1994) J. Neurobiol. , vol.25 , pp. 1404
    • Kaplan, D.R.1    Stephens, R.M.2
  • 64
    • 0025361550 scopus 로고
    • A 42-kD tyrosine kinase substrate linked to chromaffin cell secretion exhibits as associated MAP kinase activity and is highly related to a 42-kD mitogen-stimulated protein in fibroblasts
    • Ely, C.M.; Oddie, K.M.; Litz, J.S.; Rossomando, A.J.; Kanner, S.C.; Sturgill, T.W.; Parsons, S.J. A 42-kD tyrosine kinase substrate linked to chromaffin cell secretion exhibits as associated MAP kinase activity and is highly related to a 42-kD mitogen-stimulated protein in fibroblasts. J. Cell Biol. 1990, 110, 731.
    • (1990) J. Cell Biol. , vol.110 , pp. 731
    • Ely, C.M.1    Oddie, K.M.2    Litz, J.S.3    Rossomando, A.J.4    Kanner, S.C.5    Sturgill, T.W.6    Parsons, S.J.7
  • 65
    • 0026757051 scopus 로고
    • Activation of MAP kinases by calcium-dependent and calcium-independent pathways. Stimulation by thapsigargin and epidermal growth factor
    • Chao, T.S.; Byron, K.L.; Lee, K.M.; Villereal, M.; Rosner, M.R. Activation of MAP kinases by calcium-dependent and calcium-independent pathways. Stimulation by thapsigargin and epidermal growth factor. J. Biol. Chem. 1992, 267, 19876.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19876
    • Chao, T.S.1    Byron, K.L.2    Lee, K.M.3    Villereal, M.4    Rosner, M.R.5
  • 66
    • 0028277844 scopus 로고
    • Membrane depolarization and calcium influx stimulates MEK and MAP kinases via activation of Ras
    • Rosen, L.B.; Ginty, D.D.; Weber, M.J.; Greenberg, M.E. Membrane depolarization and calcium influx stimulates MEK and MAP kinases via activation of Ras. Neuron 1994, 12, 1207.
    • (1994) Neuron , vol.12 , pp. 1207
    • Rosen, L.B.1    Ginty, D.D.2    Weber, M.J.3    Greenberg, M.E.4
  • 67
    • 0028831997 scopus 로고
    • Calcium signaling
    • Clapman, D.E. Calcium signaling. Cell 1995, 80, 259.
    • (1995) Cell , vol.80 , pp. 259
    • Clapman, D.E.1
  • 69
    • 0031714391 scopus 로고    scopus 로고
    • Signaling from G-protein-coupled receptors to mitogen-activated protein (MAP)-kinase cascades
    • Lopez-Ilasaca, M. Signaling from G-protein-coupled receptors to mitogen-activated protein (MAP)-kinase cascades. Biochem. Pharmacol. 1998, 56, 269.
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 269
    • Lopez-Ilasaca, M.1
  • 70
    • 0029616354 scopus 로고
    • Calcium influx induces neurite growth through a Src-Ras signaling cassette
    • Rusanescu, G.; Qi, H.; Thomas, S.M.; Brugge, J.S.; Halegoua, S. Calcium influx induces neurite growth through a Src-Ras signaling cassette. Neuron 1995, 15, 1415.
    • (1995) Neuron , vol.15 , pp. 1415
    • Rusanescu, G.1    Qi, H.2    Thomas, S.M.3    Brugge, J.S.4    Halegoua, S.5
  • 72
    • 0027304229 scopus 로고
    • Arachidonic acid in cell signalling
    • Piomelli, D. Arachidonic acid in cell signalling. Curr. Opin. Cell Biol. 1993, 5, 274.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 274
    • Piomelli, D.1
  • 74
    • 0023851691 scopus 로고
    • Pardaxin induces aggregation, but not fusion of phosphatidylserine vesicles
    • Lelkes, P.I.; Lazarovici, P. Pardaxin induces aggregation, but not fusion of phosphatidylserine vesicles. FEBS Lett. 1988, 242, 161.
    • (1988) FEBS Lett. , vol.242 , pp. 161
    • Lelkes, P.I.1    Lazarovici, P.2
  • 75
    • 0023654425 scopus 로고
    • Evidence of protein kinase C involvement in phorbol diester-stimulated arachidonic acid release and prostaglandin synthesis
    • Parker, J.; Daniel, L.W.; White, M. Evidence of protein kinase C involvement in phorbol diester-stimulated arachidonic acid release and prostaglandin synthesis. J. Biol. Chem. 1987, 262, 385.
    • (1987) J. Biol. Chem. , vol.262 , pp. 385
    • Parker, J.1    Daniel, L.W.2    White, M.3
  • 76
    • 0026597207 scopus 로고
    • Bradykinin stimulates arachidonic acid release through the sequential actions of an Sn-1 diacylglycerol lipase and a monocyl glycerol lipase
    • Allen, A.C.; Gammon, C.M.; Ousley, A.H.; McCarthy, K.D.; Morell, P. Bradykinin stimulates arachidonic acid release through the sequential actions of an Sn-1 diacylglycerol lipase and a monocyl glycerol lipase. J. Neurochem. 1992, 58, 1130.
    • (1992) J. Neurochem. , vol.58 , pp. 1130
    • Allen, A.C.1    Gammon, C.M.2    Ousley, A.H.3    McCarthy, K.D.4    Morell, P.5
  • 77
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier, J.; Osguthorpe, D.J.; Robson, B. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 1978, 120, 97.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 78
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J.; Doolittle, R. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 1982, 157, 105.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105
    • Kyte, J.1    Doolittle, R.2
  • 79
    • 0020623947 scopus 로고
    • A computer progran for predicting protein antigenic determinants
    • Hopp, T.P.; Woods, K.R. A computer progran for predicting protein antigenic determinants. Mol. Immunol. 1982, 20, 483.
    • (1982) Mol. Immunol. , vol.20 , pp. 483
    • Hopp, T.P.1    Woods, K.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.