메뉴 건너뛰기




Volumn 100, Issue , 2014, Pages 80-87

600ns pulse electric field-induced phosphatidylinositol4,5-bisphosphate depletion

Author keywords

Calcium; Electric pulse; Nanopore; Phospholipase C; PIP2 depletion

Indexed keywords

NANOPORES;

EID: 84908056261     PISSN: 15675394     EISSN: 1878562X     Source Type: Journal    
DOI: 10.1016/j.bioelechem.2014.01.006     Document Type: Article
Times cited : (36)

References (44)
  • 1
    • 84872116460 scopus 로고    scopus 로고
    • Primary pathways of intracellular Ca(2+) mobilization by nanosecond pulsed electric field
    • Semenov I., Xiao S., Pakhomov A.G. Primary pathways of intracellular Ca(2+) mobilization by nanosecond pulsed electric field. Biochim. Biophys. Acta 2013, 1828(3):981-989.
    • (2013) Biochim. Biophys. Acta , vol.1828 , Issue.3 , pp. 981-989
    • Semenov, I.1    Xiao, S.2    Pakhomov, A.G.3
  • 2
    • 84863831676 scopus 로고    scopus 로고
    • Resolving the spatial kinetics of electric pulse-induced ion release
    • Beier H.T., Roth C.C., Tolstykh G.T., et al. Resolving the spatial kinetics of electric pulse-induced ion release. Biochem. Biophys. Res. Commun. 2012, 423(4):863-866.
    • (2012) Biochem. Biophys. Res. Commun. , vol.423 , Issue.4 , pp. 863-866
    • Beier, H.T.1    Roth, C.C.2    Tolstykh, G.T.3
  • 3
    • 4344709630 scopus 로고    scopus 로고
    • Nanosecond pulsed electric fields modulate cell function through intracellular signal transduction mechanisms
    • Beebe S.J., Blackmore P.F., White J.A., et al. Nanosecond pulsed electric fields modulate cell function through intracellular signal transduction mechanisms. Physiol. Meas. 2004, 25(4):1077-1093.
    • (2004) Physiol. Meas. , vol.25 , Issue.4 , pp. 1077-1093
    • Beebe, S.J.1    Blackmore, P.F.2    White, J.A.3
  • 4
    • 84886073747 scopus 로고    scopus 로고
    • Nanosecond pulsed electric field thresholds for nanopore formation in neural cells
    • Roth C.C., Tolstykh G.P., Payne J.A., et al. Nanosecond pulsed electric field thresholds for nanopore formation in neural cells. J. Biomed. Opt. 2013, 18(3):035005.
    • (2013) J. Biomed. Opt. , vol.18 , Issue.3 , pp. 035005
    • Roth, C.C.1    Tolstykh, G.P.2    Payne, J.A.3
  • 5
    • 2542505368 scopus 로고    scopus 로고
    • Stimulation of capacitative calcium entry in HL-60 cells by nanosecond pulsed electric fields
    • White J.A., Blackmore P.F., Schoenbach K.H., et al. Stimulation of capacitative calcium entry in HL-60 cells by nanosecond pulsed electric fields. J. Biol. Chem. 2004, 279(22):22964-22972.
    • (2004) J. Biol. Chem. , vol.279 , Issue.22 , pp. 22964-22972
    • White, J.A.1    Blackmore, P.F.2    Schoenbach, K.H.3
  • 6
    • 34548010736 scopus 로고    scopus 로고
    • Membrane permeabilization and cell damage by ultrashort electric field shocks
    • Pakhomov A.G., Shevin R., White J.A., et al. Membrane permeabilization and cell damage by ultrashort electric field shocks. Arch. Biochem. Biophys. 2007, 465(1):109-118.
    • (2007) Arch. Biochem. Biophys. , vol.465 , Issue.1 , pp. 109-118
    • Pakhomov, A.G.1    Shevin, R.2    White, J.A.3
  • 7
    • 84867804698 scopus 로고    scopus 로고
    • Electric field exposure triggers and guides formation of pseudopod-like blebs in U937 monocytes
    • Rassokhin M.A., Pakhomov A.G. Electric field exposure triggers and guides formation of pseudopod-like blebs in U937 monocytes. J. Membr. Biol. 2012, 245(9):521-529.
    • (2012) J. Membr. Biol. , vol.245 , Issue.9 , pp. 521-529
    • Rassokhin, M.A.1    Pakhomov, A.G.2
  • 8
    • 0042704730 scopus 로고    scopus 로고
    • Nanosecond, high-intensity pulsed electric fields induce apoptosis in human cells
    • Beebe S.J., Fox P.M., Rec L.I., et al. Nanosecond, high-intensity pulsed electric fields induce apoptosis in human cells. FASEB J. 2003, 17(11):1493-1495.
    • (2003) FASEB J. , vol.17 , Issue.11 , pp. 1493-1495
    • Beebe, S.J.1    Fox, P.M.2    Rec, L.I.3
  • 9
    • 41149108475 scopus 로고    scopus 로고
    • Simulation studies of ultrashort, high-intensity electric pulse induced action potential block in whole-animal nerves
    • Joshi R.P., Mishra A., Song J., et al. Simulation studies of ultrashort, high-intensity electric pulse induced action potential block in whole-animal nerves. IEEE Trans. Biomed. Eng. 2008, 55(4):1391-1398.
    • (2008) IEEE Trans. Biomed. Eng. , vol.55 , Issue.4 , pp. 1391-1398
    • Joshi, R.P.1    Mishra, A.2    Song, J.3
  • 10
    • 22544474377 scopus 로고    scopus 로고
    • Phosphoinositide lipid second messengers: new paradigms for calcium channel modulation
    • Delmas P., Coste B., Gamper N., et al. Phosphoinositide lipid second messengers: new paradigms for calcium channel modulation. Neuron 2005, 47(2):179-182.
    • (2005) Neuron , vol.47 , Issue.2 , pp. 179-182
    • Delmas, P.1    Coste, B.2    Gamper, N.3
  • 11
    • 77957260583 scopus 로고    scopus 로고
    • Osmosensitivity through the PIP2 availability: just add water
    • Gamper N. Osmosensitivity through the PIP2 availability: just add water. J. Physiol. 2010, 588(Pt 19):3631-3632.
    • (2010) J. Physiol. , vol.588 , pp. 3631-3632
    • Gamper, N.1
  • 12
    • 36348965431 scopus 로고    scopus 로고
    • Regulation of ion transport proteins by membrane phosphoinositides
    • Gamper N., Shapiro M.S. Regulation of ion transport proteins by membrane phosphoinositides. Nat. Rev. Neurosci. 2007, 8(12):921-934.
    • (2007) Nat. Rev. Neurosci. , vol.8 , Issue.12 , pp. 921-934
    • Gamper, N.1    Shapiro, M.S.2
  • 13
    • 0034695461 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion
    • Raucher D., Stauffer T., Chen W., et al. Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion. Cell 2000, 100(2):221-228.
    • (2000) Cell , vol.100 , Issue.2 , pp. 221-228
    • Raucher, D.1    Stauffer, T.2    Chen, W.3
  • 14
    • 33645117795 scopus 로고    scopus 로고
    • Nanosecond pulsed electric fields cause melanomas to self-destruct
    • Nuccitelli R., Pliquett U., Chen X., et al. Nanosecond pulsed electric fields cause melanomas to self-destruct. Biochem. Biophys. Res. Commun. 2006, 343(2):351-360.
    • (2006) Biochem. Biophys. Res. Commun. , vol.343 , Issue.2 , pp. 351-360
    • Nuccitelli, R.1    Pliquett, U.2    Chen, X.3
  • 15
    • 84879301662 scopus 로고    scopus 로고
    • Activation of intracellular phosphoinositide signaling after a single 600 nanosecond electric pulse
    • Tolstykh G.P., Hope H.T., Roth C.C., et al. Activation of intracellular phosphoinositide signaling after a single 600 nanosecond electric pulse. Bioelectrochemistry 2013, 94C:23-29.
    • (2013) Bioelectrochemistry , vol.94 C , pp. 23-29
    • Tolstykh, G.P.1    Hope, H.T.2    Roth, C.C.3
  • 16
    • 79251498907 scopus 로고    scopus 로고
    • Dose-dependent thresholds of 10-ns electric pulse induced plasma membrane disruption and cytotoxicity in multiple cell lines
    • Ibey B.L., Roth C.C., Pakhomov A.G., et al. Dose-dependent thresholds of 10-ns electric pulse induced plasma membrane disruption and cytotoxicity in multiple cell lines. PLoS One 2011, 6(1):e15642.
    • (2011) PLoS One , vol.6 , Issue.1 , pp. e15642
    • Ibey, B.L.1    Roth, C.C.2    Pakhomov, A.G.3
  • 17
    • 0032498538 scopus 로고    scopus 로고
    • Green fluorescent protein (GFP)-tagged cysteine-rich domains from protein kinase C as fluorescent indicators for diacylglycerol signaling in living cells
    • Oancea E., Teruel M.N., Quest A.F., et al. Green fluorescent protein (GFP)-tagged cysteine-rich domains from protein kinase C as fluorescent indicators for diacylglycerol signaling in living cells. J. Cell Biol. 1998, 140(3):485-498.
    • (1998) J. Cell Biol. , vol.140 , Issue.3 , pp. 485-498
    • Oancea, E.1    Teruel, M.N.2    Quest, A.F.3
  • 18
    • 18144365177 scopus 로고    scopus 로고
    • The use of Chinese hamster ovary (CHO) cells in the study of ion channels
    • Gamper N., Stockand J.D., Shapiro M.S. The use of Chinese hamster ovary (CHO) cells in the study of ion channels. J. Pharmacol. Toxicol. Methods 2005, 51(3):177-185.
    • (2005) J. Pharmacol. Toxicol. Methods , vol.51 , Issue.3 , pp. 177-185
    • Gamper, N.1    Stockand, J.D.2    Shapiro, M.S.3
  • 19
    • 0026482162 scopus 로고
    • Thapsigargin, a high affinity and global inhibitor of intracellular Ca2+ transport ATPases
    • Inesi G., Sagara Y. Thapsigargin, a high affinity and global inhibitor of intracellular Ca2+ transport ATPases. Arch. Biochem. Biophys. 1992, 298(2):313-317.
    • (1992) Arch. Biochem. Biophys. , vol.298 , Issue.2 , pp. 313-317
    • Inesi, G.1    Sagara, Y.2
  • 20
    • 67349226349 scopus 로고    scopus 로고
    • Lipid nanopores can form a stable, ion channel-like conduction pathway in cell membrane
    • Pakhomov A.G., Bowman A.M., Ibey B.L., et al. Lipid nanopores can form a stable, ion channel-like conduction pathway in cell membrane. Biochem. Biophys. Res. Commun. 2009, 385(2):181-186.
    • (2009) Biochem. Biophys. Res. Commun. , vol.385 , Issue.2 , pp. 181-186
    • Pakhomov, A.G.1    Bowman, A.M.2    Ibey, B.L.3
  • 21
    • 0033214925 scopus 로고    scopus 로고
    • Muscarinic M1 receptors activate phosphoinositide turnover and Ca2+ mobilisation in rat sympathetic neurones, but this signalling pathway does not mediate M-current inhibition
    • del Rio E., Bevilacqua J.A., Marsh S.J., et al. Muscarinic M1 receptors activate phosphoinositide turnover and Ca2+ mobilisation in rat sympathetic neurones, but this signalling pathway does not mediate M-current inhibition. J. Physiol. 1999, 520(Pt 1):101-111.
    • (1999) J. Physiol. , vol.520 , pp. 101-111
    • del Rio, E.1    Bevilacqua, J.A.2    Marsh, S.J.3
  • 22
    • 24344475560 scopus 로고    scopus 로고
    • Phospholipase C in living cells: activation, inhibition, Ca2+ requirement, and regulation of M current
    • Horowitz L.F., Hirdes W., Suh B.C., et al. Phospholipase C in living cells: activation, inhibition, Ca2+ requirement, and regulation of M current. J. Gen. Physiol. 2005, 126(3):243-262.
    • (2005) J. Gen. Physiol. , vol.126 , Issue.3 , pp. 243-262
    • Horowitz, L.F.1    Hirdes, W.2    Suh, B.C.3
  • 23
    • 0036329140 scopus 로고    scopus 로고
    • 2-Aminoethoxydiphenyl borate (2-APB) is a reliable blocker of store-operated Ca2+ entry but an inconsistent inhibitor of InsP3-induced Ca2+ release
    • Bootman M.D., Collins T.J., Mackenzie L., et al. 2-Aminoethoxydiphenyl borate (2-APB) is a reliable blocker of store-operated Ca2+ entry but an inconsistent inhibitor of InsP3-induced Ca2+ release. FASEB J. 2002, 16(10):1145-1150.
    • (2002) FASEB J. , vol.16 , Issue.10 , pp. 1145-1150
    • Bootman, M.D.1    Collins, T.J.2    Mackenzie, L.3
  • 24
    • 0038420824 scopus 로고    scopus 로고
    • 2-Aminoethoxydiphenyl borate (2-APB) antagonises inositol 1,4,5-trisphosphate-induced calcium release, inhibits calcium pumps and has a use-dependent and slowly reversible action on store-operated calcium entry channels
    • Peppiatt C.M., Collins T.J., Mackenzie L., et al. 2-Aminoethoxydiphenyl borate (2-APB) antagonises inositol 1,4,5-trisphosphate-induced calcium release, inhibits calcium pumps and has a use-dependent and slowly reversible action on store-operated calcium entry channels. Cell Calcium 2003, 34(1):97-108.
    • (2003) Cell Calcium , vol.34 , Issue.1 , pp. 97-108
    • Peppiatt, C.M.1    Collins, T.J.2    Mackenzie, L.3
  • 25
    • 84878614881 scopus 로고    scopus 로고
    • Quantitative properties and receptor reserve of the IP(3) and calcium branch of G(q)-coupled receptor signaling
    • Dickson E.J., Falkenburger B.H., Hille B. Quantitative properties and receptor reserve of the IP(3) and calcium branch of G(q)-coupled receptor signaling. J. Gen. Physiol. 2013, 141(5):521-535.
    • (2013) J. Gen. Physiol. , vol.141 , Issue.5 , pp. 521-535
    • Dickson, E.J.1    Falkenburger, B.H.2    Hille, B.3
  • 26
    • 0030790118 scopus 로고    scopus 로고
    • Structure and function of inositol 1,4,5-trisphosphate receptor
    • Yoshida Y., Imai S. Structure and function of inositol 1,4,5-trisphosphate receptor. Jpn. J. Pharmacol. 1997, 74(2):125-137.
    • (1997) Jpn. J. Pharmacol. , vol.74 , Issue.2 , pp. 125-137
    • Yoshida, Y.1    Imai, S.2
  • 27
    • 0027473443 scopus 로고
    • Barium-induced exocytosis is due to internal calcium release and block of calcium efflux
    • Przywara D.A., Chowdhury P.S., Bhave S.V., et al. Barium-induced exocytosis is due to internal calcium release and block of calcium efflux. Proc. Natl. Acad. Sci. U. S. A. 1993, 90(2):557-561.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , Issue.2 , pp. 557-561
    • Przywara, D.A.1    Chowdhury, P.S.2    Bhave, S.V.3
  • 28
    • 0032547744 scopus 로고    scopus 로고
    • Visualization of phosphoinositides that bind pleckstrin homology domains: calcium- and agonist-induced dynamic changes and relationship to myo-[3H]inositol-labeled phosphoinositide pools
    • Varnai P., Balla T. Visualization of phosphoinositides that bind pleckstrin homology domains: calcium- and agonist-induced dynamic changes and relationship to myo-[3H]inositol-labeled phosphoinositide pools. J. Cell Biol. 1998, 143(2):501-510.
    • (1998) J. Cell Biol. , vol.143 , Issue.2 , pp. 501-510
    • Varnai, P.1    Balla, T.2
  • 29
    • 34547103866 scopus 로고    scopus 로고
    • Inositol triphosphate-mediated Ca2+ signals direct purinergic P2Y receptor regulation of neuronal ion channels
    • Zaika O., Tolstykh G.P., Jaffe D.B., et al. Inositol triphosphate-mediated Ca2+ signals direct purinergic P2Y receptor regulation of neuronal ion channels. J. Neurosci. 2007, 27(33):8914-8926.
    • (2007) J. Neurosci. , vol.27 , Issue.33 , pp. 8914-8926
    • Zaika, O.1    Tolstykh, G.P.2    Jaffe, D.B.3
  • 30
    • 0030995012 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C isozymes
    • Rhee S.G., Bae Y.S. Regulation of phosphoinositide-specific phospholipase C isozymes. J. Biol. Chem. 1997, 272(24):15045-15048.
    • (1997) J. Biol. Chem. , vol.272 , Issue.24 , pp. 15045-15048
    • Rhee, S.G.1    Bae, Y.S.2
  • 31
    • 0034927336 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C
    • Rhee S.G. Regulation of phosphoinositide-specific phospholipase C. Annu. Rev. Biochem. 2001, 70:281-312.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 281-312
    • Rhee, S.G.1
  • 32
    • 0032582525 scopus 로고    scopus 로고
    • Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals
    • Oancea E., Meyer T. Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals. Cell 1998, 95(3):307-318.
    • (1998) Cell , vol.95 , Issue.3 , pp. 307-318
    • Oancea, E.1    Meyer, T.2
  • 33
    • 63349090552 scopus 로고    scopus 로고
    • Phospholipase C-mediated hydrolysis of PIP2 releases ERM proteins from lymphocyte membrane
    • Hao J.J., Liu Y., Kruhlak K.E., et al. Phospholipase C-mediated hydrolysis of PIP2 releases ERM proteins from lymphocyte membrane. J. Cell Biol. 2009, 184(3):451-462.
    • (2009) J. Cell Biol. , vol.184 , Issue.3 , pp. 451-462
    • Hao, J.J.1    Liu, Y.2    Kruhlak, K.E.3
  • 34
    • 0035808040 scopus 로고    scopus 로고
    • The complex and intriguing lives of PIP2 with ion channels and transporters
    • Hilgemann D.W., Feng S., Nasuhoglu C. The complex and intriguing lives of PIP2 with ion channels and transporters. Sci. STKE 2001, 2001(111):RE19.
    • (2001) Sci. STKE , vol.2001 , Issue.111 , pp. RE19
    • Hilgemann, D.W.1    Feng, S.2    Nasuhoglu, C.3
  • 35
    • 0037518226 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate (PIP2) modulation of ATP and pH sensitivity in Kir channels. A tale of an active and a silent PIP2 site in the N terminus
    • Schulze D., Krauter T., Fritzenschaft H., et al. Phosphatidylinositol 4,5-bisphosphate (PIP2) modulation of ATP and pH sensitivity in Kir channels. A tale of an active and a silent PIP2 site in the N terminus. J. Biol. Chem. 2003, 278(12):10500-10505.
    • (2003) J. Biol. Chem. , vol.278 , Issue.12 , pp. 10500-10505
    • Schulze, D.1    Krauter, T.2    Fritzenschaft, H.3
  • 36
    • 0028986998 scopus 로고
    • Significance of PIP2 hydrolysis and regulation of phospholipase C isozymes
    • Lee S.B., Rhee S.G. Significance of PIP2 hydrolysis and regulation of phospholipase C isozymes. Curr. Opin. Cell Biol. 1995, 7(2):183-189.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , Issue.2 , pp. 183-189
    • Lee, S.B.1    Rhee, S.G.2
  • 37
    • 33646478114 scopus 로고    scopus 로고
    • Phosphatidylinositol-4,5-biphosphate (PIP2) differentially regulates the interaction of human erythrocyte protein 4.1 (4.1R) with membrane proteins
    • An X., Zhang G., Debnath A.J., et al. Phosphatidylinositol-4,5-biphosphate (PIP2) differentially regulates the interaction of human erythrocyte protein 4.1 (4.1R) with membrane proteins. Biochemistry 2006, 45(18):5725-5732.
    • (2006) Biochemistry , vol.45 , Issue.18 , pp. 5725-5732
    • An, X.1    Zhang, G.2    Debnath, A.J.3
  • 38
    • 84870936338 scopus 로고    scopus 로고
    • Electrochemical reaction and oxidation of lecithin under pulsed electric fields (PEF) processing
    • Zhao W., Yang R., Liang Q., et al. Electrochemical reaction and oxidation of lecithin under pulsed electric fields (PEF) processing. J. Agric. Food Chem. 2012, 60:12204-12209.
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 12204-12209
    • Zhao, W.1    Yang, R.2    Liang, Q.3
  • 39
    • 84865822749 scopus 로고    scopus 로고
    • Oxidative effects of nanosecond pulsed electric field exposure in cells and cell-free media
    • Pakhomova O.N., Khorokhorina V.A., Bowman A.M., et al. Oxidative effects of nanosecond pulsed electric field exposure in cells and cell-free media. Arch. Biochem. Biophys. 2012, 527(1):55-64.
    • (2012) Arch. Biochem. Biophys. , vol.527 , Issue.1 , pp. 55-64
    • Pakhomova, O.N.1    Khorokhorina, V.A.2    Bowman, A.M.3
  • 40
    • 36549026923 scopus 로고    scopus 로고
    • Long-lasting plasma membrane permeabilization in mammalian cells by nanosecond pulsed electric field (nsPEF)
    • Pakhomov A.G., Kolb J.A., White R.P., et al. Long-lasting plasma membrane permeabilization in mammalian cells by nanosecond pulsed electric field (nsPEF). Bioelectromagnetics 2007, 28(8):655-663.
    • (2007) Bioelectromagnetics , vol.28 , Issue.8 , pp. 655-663
    • Pakhomov, A.G.1    Kolb, J.A.2    White, R.P.3
  • 41
    • 85036258461 scopus 로고    scopus 로고
    • Mechanism for membrane electroporation irreversibility under high-intensity, ultrashort electrical pulse conditions
    • Joshi R.P., Schoenbach K.H. Mechanism for membrane electroporation irreversibility under high-intensity, ultrashort electrical pulse conditions. Phys. Rev. E Stat. Nonlin. Soft Matter Phys. 2002, 66(5 Pt 1):052901.
    • (2002) Phys. Rev. E Stat. Nonlin. Soft Matter Phys. , vol.66 , Issue.5 , pp. 052901
    • Joshi, R.P.1    Schoenbach, K.H.2
  • 42
    • 41349083707 scopus 로고    scopus 로고
    • Theoretical predictions of electromechanical deformation of cells subjected to high voltages for membrane electroporation
    • Joshi R.P., Hu Q., Schoenbach K.H., et al. Theoretical predictions of electromechanical deformation of cells subjected to high voltages for membrane electroporation. Phys. Rev. E Stat. Nonlin. Soft Matter Phys. 2002, 65(2 Pt 1):021913.
    • (2002) Phys. Rev. E Stat. Nonlin. Soft Matter Phys. , vol.65 , Issue.2 , pp. 021913
    • Joshi, R.P.1    Hu, Q.2    Schoenbach, K.H.3
  • 43
    • 78650131676 scopus 로고    scopus 로고
    • Bioelectric effects of intense ultrashort pulses
    • Joshi R.P., Schoenbach K.H. Bioelectric effects of intense ultrashort pulses. Crit. Rev. Biomed. Eng. 2010, 38(3):255-304.
    • (2010) Crit. Rev. Biomed. Eng. , vol.38 , Issue.3 , pp. 255-304
    • Joshi, R.P.1    Schoenbach, K.H.2
  • 44
    • 45849122833 scopus 로고    scopus 로고
    • A voltage-sensing phosphatase, Ci-VSP, which shares sequence identity with PTEN, dephosphorylates phosphatidylinositol 4,5-bisphosphate
    • Iwasaki H., Murata Y., Kim Y., et al. A voltage-sensing phosphatase, Ci-VSP, which shares sequence identity with PTEN, dephosphorylates phosphatidylinositol 4,5-bisphosphate. Proc. Natl. Acad. Sci. U. S. A. 2008, 105(23):7970-7975.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , Issue.23 , pp. 7970-7975
    • Iwasaki, H.1    Murata, Y.2    Kim, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.