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Volumn 62, Issue , 2008, Pages 47-54

Phosphoinositide-specific phospholipase C in mammalian cells: Structure, properties, and function;Fosfolipaza C zalezna od fosfatydyloinozytolu w komórkach ssaków-budowa, włas̈ciwos̈ci i funkcja

Author keywords

Isoforms PLC ; Phospholipase C (PLC); PLC ; PLC ; PLC ; PLC ; PLC ; Regulatory activities of PLC; Signal transduction

Indexed keywords

ION CHANNEL; ISOPROTEIN; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE PHOSPHODIESTERASE;

EID: 40749118944     PISSN: 00325449     EISSN: 17322693     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (8)

References (64)
  • 2
  • 6
    • 20544462579 scopus 로고    scopus 로고
    • G-protein-activated phospholipase C-b, new partners for cell polarity proteins Par3 and Par6
    • Cai Y., Stafford L.J., Bryan B.A., Mitchell D., Liu M.: G-protein-activated phospholipase C-b, new partners for cell polarity proteins Par3 and Par6. Oncogene, 2005; 24: 4293-4300
    • (2005) Oncogene , vol.24 , pp. 4293-4300
    • Cai, Y.1    Stafford, L.J.2    Bryan, B.A.3    Mitchell, D.4    Liu, M.5
  • 7
    • 30944456676 scopus 로고    scopus 로고
    • The latest phospholipase C, PLC-h, is implicated in neronal function
    • Cockcroft S.: The latest phospholipase C, PLC-h, is implicated in neronal function. Trends Biochem. Sci., 2006; 31: 4-7
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 4-7
    • Cockcroft, S.1
  • 8
    • 0034677631 scopus 로고    scopus 로고
    • PIP2 i PIP3: Complex roles at the cell surface
    • Czech M.P.: PIP2 i PIP3: complex roles at the cell surface. Cell, 2000; 100: 603-606
    • (2000) Cell , vol.100 , pp. 603-606
    • Czech, M.P.1
  • 9
    • 0036214044 scopus 로고    scopus 로고
    • The ERBB receptor family: A therapeutic target for cancer
    • de Bono J.S., Rowinsky E.K.: The ErbB receptor family: A therapeutic target for cancer. Trends Mol. Med., 2002; 8: S19-S26
    • (2002) Trends Mol. Med. , vol.8 , pp. S19-S26
    • De Bono, J.S.1    Rowinsky, E.K.2
  • 10
    • 34548559192 scopus 로고    scopus 로고
    • In the ventral tegmental area, the membrane-mediated actions of progestins for lordosis of hormone-primed hamsters involve phospholipase C and protein kinase C
    • Frye C.A., Walf A.A.: In the ventral tegmental area, the membrane-mediated actions of progestins for lordosis of hormone-primed hamsters involve phospholipase C and protein kinase C. J. Neuroendocrinol., 2007; 19: 717-724
    • (2007) J. Neuroendocrinol. , vol.19 , pp. 717-724
    • Frye, C.A.1    Walf, A.A.2
  • 11
    • 0036217935 scopus 로고    scopus 로고
    • Structure, regulation, and function of phospholipase C isozymes
    • Fukami K.: Structure, regulation, and function of phospholipase C isozymes. J. Biochem., 2002, 131: 293-299
    • (2002) J. Biochem. , vol.131 , pp. 293-299
    • Fukami, K.1
  • 12
    • 0031955881 scopus 로고    scopus 로고
    • Increased activity of phospholipase C in aorta of spontaneously hypertensive rats correlates with decreased sphingomyelin: Total phospholipid ratio
    • Gryckiewicz E., Dettlaff A., Pawelczyk T.: Increased activity of phospholipase C in aorta of spontaneously hypertensive rats correlates with decreased sphingomyelin: total phospholipid ratio. Cell. Mol. Biol. Lett., 1998; 3: 3-11
    • (1998) Cell. Mol. Biol. Lett. , vol.3 , pp. 3-11
    • Gryckiewicz, E.1    Dettlaff, A.2    Pawelczyk, T.3
  • 13
    • 12544250874 scopus 로고    scopus 로고
    • Phospholipase Cb2 binds to and inhibits phospholipase Cd1
    • Guo Y., Rebecchi M., Scarlata S.: Phospholipase Cb2 binds to and inhibits phospholipase Cd1. J. Biol. Chem., 2005; 280: 1438-1447
    • (2005) J. Biol. Chem. , vol.280 , pp. 1438-1447
    • Guo, Y.1    Rebecchi, M.2    Scarlata, S.3
  • 14
    • 33745143631 scopus 로고    scopus 로고
    • Ga12/13-and Rho-dependent activation of phospholipase C-e by lysophosphatidic acid and trombin receptors
    • Hains M.D., Wing M.R., Maddileti S., Siderovski D.P., Harden T.K.: Ga12/13-and Rho-dependent activation of phospholipase C-e by lysophosphatidic acid and trombin receptors. Mol. Pharmacol., 2006; 69: 2068-2075
    • (2006) Mol. Pharmacol. , vol.69 , pp. 2068-2075
    • Hains, M.D.1    Wing, M.R.2    Maddileti, S.3    Siderovski, D.P.4    Harden, T.K.5
  • 15
    • 24344475560 scopus 로고    scopus 로고
    • Phospholipase C in living cells: Activation, inhibition, Ca+2 requirement, and regulation of M current
    • Horowitz L.F., Hirdes W., Suh B.C., Hilgemann D.W., Mackie K., Hille B.: Phospholipase C in living cells: Activation, inhibition, Ca+2 requirement, and regulation of M current. J. Gen. Physiol., 2005; 126: 243-262
    • (2005) J. Gen. Physiol. , vol.126 , pp. 243-262
    • Horowitz, L.F.1    Hirdes, W.2    Suh, B.C.3    Hilgemann, D.W.4    Mackie, K.5    Hille, B.6
  • 16
    • 16844362568 scopus 로고    scopus 로고
    • The interaction of phospholipase C-beta3 with shank2 regulates mGluR-mediated calcium signal
    • Hwang J.I., Kim H.S., Lee J.R., Kim E., Ryu S.H., Suh P.G.: The interaction of phospholipase C-beta3 with shank2 regulates mGluR-mediated calcium signal. J. Biol. Chem., 2005; 280: 12467-12473
    • (2005) J. Biol. Chem. , vol.280 , pp. 12467-12473
    • Hwang, J.I.1    Kim, H.S.2    Lee, J.R.3    Kim, E.4    Ryu, S.H.5    Suh, P.G.6
  • 17
    • 22144495354 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel phospholipase C, PLC-h
    • Hwang J.I., Oh Y.S., Shin K.J., Kim H., Ryu S.H., Suh P.G.: Molecular cloning and characterization of a novel phospholipase C, PLC-h. Biochem. J., 2005; 389: 181-186
    • (2005) Biochem. J. , vol.389 , 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
  • 18
    • 0037040173 scopus 로고    scopus 로고
    • Mutations in the carboxyl-terminal domain of phospholipase C-b1 delineate the dimer interface and a potential Gaq interaction site
    • Ilkaeva O., Kinch L.N., Paulssen R.H., Ross E.M.: Mutations in the carboxyl-terminal domain of phospholipase C-b1 delineate the dimer interface and a potential Gaq interaction site. J. Biol. Chem., 2002; 277: 4294-4300
    • (2002) J. Biol. Chem. , vol.277 , pp. 4294-4300
    • Ilkaeva, O.1    Kinch, L.N.2    Paulssen, R.H.3    Ross, E.M.4
  • 20
    • 33745228758 scopus 로고    scopus 로고
    • Nuclear inositide signalling-expansion, structures and clarification
    • Irvine R.F.: Nuclear inositide signalling-expansion, structures and clarification. Biochim. Biophys. Acta, 2006; 1761: 505-508
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 505-508
    • Irvine, R.F.1
  • 21
    • 33646340970 scopus 로고    scopus 로고
    • G-protein-coupled receptor agonists activate endogenous phospholipase C-e and phospholipase C-a3 in a temporally distinct manner
    • Kelley G.G., Kaproth-Joslin K.A., Reks S.E., Smrcka A.V., Wojcikiewicz R.J.: G-protein-coupled receptor agonists activate endogenous phospholipase C-e and phospholipase C-a3 in a temporally distinct manner. J. Biol. Chem., 2006; 281: 2639-2648
    • (2006) J. Biol. Chem. , vol.281 , pp. 2639-2648
    • Kelley, G.G.1    Kaproth-Joslin, K.A.2    Reks, S.E.3    Smrcka, A.V.4    Wojcikiewicz, R.J.5
  • 22
    • 0037357899 scopus 로고    scopus 로고
    • Phospholipase C activity in skin fibroblasts obtained from patients with essential hypertension
    • Kosugi T., Osanai T., Kamada T., Nakano T., Okumura K.: Phospholipase C activity in skin fibroblasts obtained from patients with essential hypertension. J. Hypertens., 2003; 21: 583-590
    • (2003) J. Hypertens. , vol.21 , pp. 583-590
    • Kosugi, T.1    Osanai, T.2    Kamada, T.3    Nakano, T.4    Okumura, K.5
  • 24
    • 0029741298 scopus 로고    scopus 로고
    • Inverse regulation of estrogen receptor and epidermal growth factor receptor gene expression in MCF-7 breast cancer cells treated with phorbol ester
    • Lee C.S., deFazio A., Ormandy C.J., Sutherland R.L.: Inverse regulation of estrogen receptor and epidermal growth factor receptor gene expression in MCF-7 breast cancer cells treated with phorbol ester. J. Steroid Biochem. Mol. Biol., 1996; 58: 267-275
    • (1996) J. Steroid Biochem. Mol. Biol. , vol.58 , pp. 267-275
    • Lee, C.S.1    DeFazio, A.2    Ormandy, C.J.3    Sutherland, R.L.4
  • 25
    • 0038281249 scopus 로고    scopus 로고
    • Phosphoinositide recognition domains
    • Lemmon M.A.: Phosphoinositide recognition domains. Traffic, 2003; 4: 201-213
    • (2003) Traffic , vol.4 , pp. 201-213
    • Lemmon, M.A.1
  • 26
    • 2942627762 scopus 로고    scopus 로고
    • Phospholipase C d-4 overexpression upregulates ErbBl/2 expression, Erk Signaling pathway, and proliferation in MCF-7 cells
    • Leung D.W., Tompkins C., Brewer J., Ball A., Coon M., Morris V., Waggoner D., Singer J. W.: Phospholipase C d-4 overexpression upregulates ErbBl/2 expression, Erk Signaling pathway, and proliferation in MCF-7 cells. Mol. Cancer, 2004; 3: 1-15
    • (2004) Mol. Cancer , vol.3 , pp. 1-15
    • Leung, D.W.1    Tompkins, C.2    Brewer, J.3    Ball, A.4    Coon, M.5    Morris, V.6    Waggoner, D.7    Singer, J.W.8
  • 28
    • 0034421837 scopus 로고    scopus 로고
    • Phospholipase C isoforms, cytoskeletal organization, and vascular smooth muscle differentiation
    • Lymn J.S., Hughes A.D.: Phospholipase C isoforms, cytoskeletal organization, and vascular smooth muscle differentiation. News Physiol. Sci., 2000; 15: 41-45
    • (2000) News Physiol. Sci. , vol.15 , pp. 41-45
    • Lymn, J.S.1    Hughes, A.D.2
  • 32
    • 0037197775 scopus 로고    scopus 로고
    • Enhanced activity of variant phospholipase C-d1 protein (R257H) detected in patients with coronary artery spasm
    • Nakano T., Osanai T., Tomita H., Sekimata M., Homma Y., Okumura K.: Enhanced activity of variant phospholipase C-d1 protein (R257H) detected in patients with coronary artery spasm. Circulation, 2002; 105: 2024-2029
    • (2002) Circulation , vol.105 , pp. 2024-2029
    • Nakano, T.1    Osanai, T.2    Tomita, H.3    Sekimata, M.4    Homma, Y.5    Okumura, K.6
  • 33
    • 2342627142 scopus 로고    scopus 로고
    • Isozymes delta of phosphoinositidespecific phospholipase C and their role in signal transduction in the cell
    • Ochocka A.M., Pawelczyk T.: Isozymes delta of phosphoinositidespecific phospholipase C and their role in signal transduction in the cell. Acta Biochim. Polon., 2003; 50: 1097-1110
    • (2003) Acta Biochim. Polon. , vol.50 , pp. 1097-1110
    • Ochocka, A.M.1    Pawelczyk, T.2
  • 34
    • 0347593996 scopus 로고    scopus 로고
    • Requirement for Ras guanine nucleotide releasing protein 3 in coupling phospholipase C-g2 to Ras in B cell receptor signaling
    • Oh-hora M., Johmura S., Hashimoto A., Hikida M., Kurosaki T.: Requirement for Ras guanine nucleotide releasing protein 3 in coupling phospholipase C-g2 to Ras in B cell receptor signaling. J. Exp. Med., 2003; 198: 1841-1851
    • (2003) J. Exp. Med. , vol.198 , pp. 1841-1851
    • Oh-Hora, M.1    Johmura, S.2    Hashimoto, A.3    Hikida, M.4    Kurosaki, T.5
  • 35
    • 0032610756 scopus 로고    scopus 로고
    • Isozymes delta of phosphoinositide-specific phospholipase C
    • Pawelczyk T.: Isozymes delta of phosphoinositide-specific phospholipase C. Acta Biochem. Polon., 1999; 46: 91-98
    • (1999) Acta Biochem. Polon. , vol.46 , pp. 91-98
    • Pawelczyk, T.1
  • 36
    • 17544392380 scopus 로고    scopus 로고
    • Przekazywanie sygnau w komórce z udziaem fosfatydyloinozytoloswoistych fosfolipaz C
    • Paweczyk T.: Przekazywanie sygnau w komórce z udziaem fosfatydyloinozytoloswoistych fosfolipaz C. Post. Hig. Med. Dow.,1999; 53: 173-182
    • (1999) Post. Hig. Med. Dow. , vol.53 , pp. 173-182
    • Paweczyk, T.1
  • 37
    • 0037201967 scopus 로고    scopus 로고
    • Multiple roles of pleckstrin homology domains in phospholipase Cb function
    • Philip F., Guo Y., Scarlata S.: Multiple roles of pleckstrin homology domains in phospholipase Cb function. FEBS Lett., 2002; 531: 28-32
    • (2002) FEBS Lett. , vol.531 , pp. 28-32
    • Philip, F.1    Guo, Y.2    Scarlata, S.3
  • 38
    • 1642534405 scopus 로고    scopus 로고
    • A potentially critical role of phospholipases in central nervous system ischemic, traumatic, and neurodegenerative disorders
    • Phillis J.W., O'Regan M.H.: A potentially critical role of phospholipases in central nervous system ischemic, traumatic, and neurodegenerative disorders. Brain Res. Brain Res. Rev., 2004; 44: 13-47
    • (2004) Brain Res. Brain Res. Rev. , vol.44 , pp. 13-47
    • Phillis, J.W.1    O'Regan, M.H.2
  • 40
    • 0033779101 scopus 로고    scopus 로고
    • Structure, function, and control of phosphoinositide-specific phospholipase C
    • Rebecchi M.J., Pentyala S.N.: Structure, function, and control of phosphoinositide-specific phospholipase C. Physiol. Rev., 2000; 80: 1291-1335
    • (2000) Physiol. Rev. , vol.80 , pp. 1291-1335
    • Rebecchi, M.J.1    Pentyala, S.N.2
  • 41
    • 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
  • 42
    • 11144277290 scopus 로고    scopus 로고
    • Phospholipase Cz causes Ca2+ oscillations and parthenogenetic activation of human oocytes
    • Rogers N.T., Hobson E., Pickering S., Lai F.A., Braude P., Swann K.: Phospholipase Cz causes Ca2+ oscillations and parthenogenetic activation of human oocytes. Reproduction, 2004; 128: 697-702
    • (2004) Reproduction , vol.128 , pp. 697-702
    • Rogers, N.T.1    Hobson, E.2    Pickering, S.3    Lai, F.A.4    Braude, P.5    Swann, K.6
  • 43
    • 33845940377 scopus 로고    scopus 로고
    • Structural determinants for phosphatidic acid regulation of phospholipase C-b1
    • Ross E.M., Mateu D., Gomes A.V., Arana C., Tran T., Litosch I.: Structural determinants for phosphatidic acid regulation of phospholipase C-b1. J. Biol. Chem., 2006; 281: 33087-33094
    • (2006) J. Biol. Chem. , vol.281 , pp. 33087-33094
    • Ross, E.M.1    Mateu, D.2    Gomes, A.V.3    Arana, C.4    Tran, T.5    Litosch, I.6
  • 44
    • 79958823169 scopus 로고    scopus 로고
    • Fosfolipazy A w komórkach ssaków-budowa, waciwoci, rola fizjologiczna i patologiczna
    • Sadurska B., Szumio M.: Fosfolipazy A w komórkach ssaków-budowa, waciwoci, rola fizjologiczna i patologiczna. Post. Hig. Med. Dow., 2005; 59: 116-123
    • (2005) Post. Hig. Med. Dow. , vol.59 , pp. 116-123
    • Sadurska, B.1    Szumio, M.2
  • 45
    • 0043130467 scopus 로고    scopus 로고
    • Inositol-specific phospholipase C in low and fast proliferating hepatoma cell lines
    • Santi P., Solimando L., Zini N., Santi S., Riccio M., Guidotti L.: Inositol-specific phospholipase C in low and fast proliferating hepatoma cell lines. Int. Oncol., 2003; 22: 1147-1153
    • (2003) Int. Oncol. , vol.22 , pp. 1147-1153
    • Santi, P.1    Solimando, L.2    Zini, N.3    Santi, S.4    Riccio, M.5    Guidotti, L.6
  • 47
    • 9144254020 scopus 로고    scopus 로고
    • Rho A activates purified phospholipase C-e by a guanine nucleotide-dependent mechanizm
    • Seifert J.P., Wing M.R., Snyder J.T., Gershburg S., Sondek J., Harden T.K.: Rho A activates purified phospholipase C-e by a guanine nucleotide-dependent mechanizm. J. Biol. Chem., 2004; 279: 47992-47997
    • (2004) J. Biol. Chem. , vol.279 , pp. 47992-47997
    • Seifert, J.P.1    Wing, M.R.2    Snyder, J.T.3    Gershburg, S.4    Sondek, J.5    Harden, T.K.6
  • 50
    • 20444477143 scopus 로고    scopus 로고
    • Regulation of phospholipase C-d1 through direct interactions with the small GTPase Ra1 and calmodulin
    • Sidhu R.S., Clough R.R., Bhullar R.P.: Regulation of phospholipase C-d1 through direct interactions with the small GTPase Ra1 and calmodulin. J. Biol. Chem., 2005; 280: 21933-21941
    • (2005) J. Biol. Chem. , vol.280 , pp. 21933-21941
    • Sidhu, R.S.1    Clough, R.R.2    Bhullar, R.P.3
  • 51
    • 0038756655 scopus 로고    scopus 로고
    • The pleckstrin homology domain of phospholipase C-b2 as an effector site for Rac
    • Snyder J.T., Singer A.U., Wing M.R., Harden T.K., Sondek J.: The pleckstrin homology domain of phospholipase C-b2 as an effector site for Rac. J. Biol. Chem., 2003; 278: 21099-21104
    • (2003) J. Biol. Chem. , vol.278 , pp. 21099-21104
    • Snyder, J.T.1    Singer, A.U.2    Wing, M.R.3    Harden, T.K.4    Sondek, J.5
  • 53
    • 20444434117 scopus 로고    scopus 로고
    • Identification of a novel class of mammalian phosphoinositol-specific phospholipase C enzymes
    • Stewart A.J., Mukherjee J., Roberts S.J., Lester D., Farquharson C.: Identification of a novel class of mammalian phosphoinositol-specific phospholipase C enzymes. Int. J. Mol. Med., 2005; 15: 117-121
    • (2005) Int. J. Mol. Med. , vol.15 , pp. 117-121
    • Stewart, A.J.1    Mukherjee, J.2    Roberts, S.J.3    Lester, D.4    Farquharson, C.5
  • 55
    • 38449094474 scopus 로고    scopus 로고
    • Biaka RasGRP-czynniki aktywujce Ras
    • Szamaek M., Baer-Dubowska W.: Biaka RasGRP-czynniki aktywujce Ras. Post. Biochem., 2007; 53: 112-120
    • (2007) Post. Biochem. , vol.53 , pp. 112-120
    • Szamaek, M.1    Baer-Dubowska, W.2
  • 56
    • 33846084349 scopus 로고    scopus 로고
    • Fosfolipaza D w komórkach ssaków-budowa, waciwoci, rola fizjologiczna i patologiczna
    • Szumio M., Rahden-Staroñ I.: Fosfolipaza D w komórkach ssaków-budowa, waciwoci, rola fizjologiczna i patologiczna. Post. Hig. Med. Dow., 2006; 60: 421-430
    • (2006) Post. Hig. Med. Dow. , vol.60 , pp. 421-430
    • Szumio, M.1    Rahden-Staroñ, I.2
  • 57
    • 0037135287 scopus 로고    scopus 로고
    • Analysis of gene expression following spinal cord injury in rat using complementary DNA microarray
    • Tachibana T., Noguchi K., Ruda M.A.: Analysis of gene expression following spinal cord injury in rat using complementary DNA microarray. Neurosci. Lett., 2002; 327:133-137
    • (2002) Neurosci. Lett. , vol.327 , pp. 133-137
    • Tachibana, T.1    Noguchi, K.2    Ruda, M.A.3
  • 58
    • 0037244266 scopus 로고    scopus 로고
    • Lamin expression in normal human skin, actinic keratosis, squamous cell carcinoma and basal cell carcinoma
    • Tilli C.M., Ramaekers F.C., Broers J.L., Hutchison C.J., Neumann H.A.: Lamin expression in normal human skin, actinic keratosis, squamous cell carcinoma and basal cell carcinoma. Br. J. Dermatol., 2003; 148: 102-109
    • (2003) Br. J. Dermatol. , vol.148 , pp. 102-109
    • Tilli, C.M.1    Ramaekers, F.C.2    Broers, J.L.3    Hutchison, C.J.4    Neumann, H.A.5
  • 59
    • 0032728220 scopus 로고    scopus 로고
    • Mammalian phosphoinositide-specific phospholipase C
    • Williams R.L.: Mammalian phosphoinositide-specific phospholipase C. Biochim. Biophys. Acta, 1999; 1441: 255-267
    • (1999) Biochim. Biophys. Acta , vol.1441 , pp. 255-267
    • Williams, R.L.1
  • 60
    • 2342514426 scopus 로고    scopus 로고
    • PLC-e: A shared effector protein in Ras-, Rho-, and Gabg-mediated signaling
    • Wing M.R., Bourdon D.M., Harden T.K.: PLC-e: A shared effector protein in Ras-, Rho-, and Gabg-mediated signaling. Mol. Interv., 2003; 5: 273-280
    • (2003) Mol. Interv. , vol.5 , pp. 273-280
    • Wing, M.R.1    Bourdon, D.M.2    Harden, T.K.3
  • 61
  • 62
    • 0036374208 scopus 로고    scopus 로고
    • Regulation of the intracellular localization of phosphoinositide-specific phospholipase C-d1
    • Yagisawa H., Yamaga M., Okada M., Sasaki K., Fujii M.: Regulation of the intracellular localization of phosphoinositide-specific phospholipase C-d1. Advan. Enzyme Regul., 2002; 42: 261-284
    • (2002) Advan. Enzyme Regul. , vol.42 , pp. 261-284
    • Yagisawa, H.1    Yamaga, M.2    Okada, M.3    Sasaki, K.4    Fujii, M.5
  • 63
    • 0038311944 scopus 로고    scopus 로고
    • Phosphoinositide regulation of the actin cytoskeleton
    • Yin H.L., Janmey P.A.: Phosphoinositide regulation of the actin cytoskeleton. Annu. Rev. Physiol., 2003; 65: 761-789
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 761-789
    • Yin, H.L.1    Janmey, P.A.2
  • 64
    • 27744467849 scopus 로고    scopus 로고
    • Molecular cloning and characterization of PLC-h2
    • Zhou Y., Wing M.R., Sondek J., Harden T.K.: Molecular cloning and characterization of PLC-h2. Biochem. J., 2005; 391: 667-676
    • (2005) Biochem. J. , vol.391 , pp. 667-676
    • Zhou, Y.1    Wing, M.R.2    Sondek, J.3    Harden, T.K.4


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