메뉴 건너뛰기




Volumn 312, Issue 7, 2006, Pages 1205-1217

Involvement of Golgi-associated Lyn tyrosine kinase in the translocation of annexin II to the endoplasmic reticulum under oxidative stress

Author keywords

Annexin II; Endoplasmic reticulum (ER); Golgi; HeLa; Hydrogen peroxide; Lyn; Signal transduction; Src family kinases; Trafficking; Tyrosine phosphorylation

Indexed keywords

LIPOCORTIN 2; PROTEIN KINASE LYN; SUCROSE; TYROSINE;

EID: 33645243620     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2006.02.003     Document Type: Article
Times cited : (64)

References (71)
  • 1
    • 0032915392 scopus 로고    scopus 로고
    • Epidermal growth factor receptors: Critical mediators of multiple receptor pathways
    • P.O. Hackel, E. Zwick, N. Prenzel, and A. Ullrich Epidermal growth factor receptors: critical mediators of multiple receptor pathways Curr. Opin. Cell Biol. 11 1999 184 189
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 184-189
    • Hackel, P.O.1    Zwick, E.2    Prenzel, N.3    Ullrich, A.4
  • 2
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix and the cytoskeleton
    • B. Geiger, A. Bershadsky, R. Pankov, and K.M. Yamada Transmembrane crosstalk between the extracellular matrix and the cytoskeleton Nat. Rev., Mol. Cell Biol. 2 2001 793 805
    • (2001) Nat. Rev., Mol. Cell Biol. , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 5
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of Src
    • M.T. Brown, and J.A. Cooper Regulation, substrates and functions of Src Biochim. Biophys. Acta 1287 1996 121 149
    • (1996) Biochim. Biophys. Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 6
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • S.M. Thomas, and J.S. Brugge Cellular functions regulated by Src family kinases Annu. Rev. Cell Dev. Biol. 13 1997 513 609
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 7
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • P. Blume-Jensen, and T. Hunter Oncogenic kinase signalling Nature 411 2001 355 365
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 8
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: The fats of the matter
    • M.D. Resh Myristylation and palmitylation of Src family members: the fats of the matter Cell 76 1994 411 413
    • (1994) Cell , vol.76 , pp. 411-413
    • Resh, M.D.1
  • 9
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • M.D. Resh Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins Biochim. Biophys. Acta 1451 1999 1 16
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 10
    • 0027315182 scopus 로고
    • T cell antigen receptor signal transduction: A tale of tails and cytoplasmic protein-tyrosine kinases
    • A. Weiss T cell antigen receptor signal transduction: a tale of tails and cytoplasmic protein-tyrosine kinases Cell 73 1993 209 212
    • (1993) Cell , vol.73 , pp. 209-212
    • Weiss, A.1
  • 11
    • 0032931978 scopus 로고    scopus 로고
    • Src-related protein tyrosine kinases in hematopoiesis
    • S.J. Corey, and S.M. Anderson Src-related protein tyrosine kinases in hematopoiesis Blood 93 1999 1 14
    • (1999) Blood , vol.93 , pp. 1-14
    • Corey, S.J.1    Anderson, S.M.2
  • 12
    • 0034603197 scopus 로고    scopus 로고
    • New roles for Src kinases in control of cell survival and angiogenesis
    • J. Schlessinger New roles for Src kinases in control of cell survival and angiogenesis Cell 100 2000 293 296
    • (2000) Cell , vol.100 , pp. 293-296
    • Schlessinger, J.1
  • 14
    • 0025605786 scopus 로고
    • Immunolocalization of the cellular src protein in interphase and mitotic NIH c-src overexpresser cells
    • T. David-Pfeuty, and Y. Nouvian-Dooghe Immunolocalization of the cellular src protein in interphase and mitotic NIH c-src overexpresser cells J. Cell Biol. 111 1990 3097 3116
    • (1990) J. Cell Biol. , vol.111 , pp. 3097-3116
    • David-Pfeuty, T.1    Nouvian-Dooghe, Y.2
  • 16
    • 0028279060 scopus 로고
    • Distinct intracellular localization of Lck and Fyn protein tyrosine kinases in human T lymphocytes
    • S.C. Ley, M. Marsh, C.R. Bebbington, K. Proudfoot, and P. Jordan Distinct intracellular localization of Lck and Fyn protein tyrosine kinases in human T lymphocytes J. Cell Biol. 125 1994 639 649
    • (1994) J. Cell Biol. , vol.125 , pp. 639-649
    • Ley, S.C.1    Marsh, M.2    Bebbington, C.R.3    Proudfoot, K.4    Jordan, P.5
  • 17
    • 0029071799 scopus 로고
    • hck is located on the secretory granules in human neutrophils and translocates towards the phagosome during cell activation
    • hck is located on the secretory granules in human neutrophils and translocates towards the phagosome during cell activation Biochem. J. 309 1995 657 665
    • (1995) Biochem. J. , vol.309 , pp. 657-665
    • Mohn, H.1    Le Cabec, V.2    Fischer, S.3    Maridonneau-Parini, I.4
  • 18
    • 0033519347 scopus 로고    scopus 로고
    • lck travels to the plasma membrane via the exocytic pathway
    • lck travels to the plasma membrane via the exocytic pathway J. Cell Biol. 145 1999 457 468
    • (1999) J. Cell Biol. , vol.145 , pp. 457-468
    • Bijlmakers, M.J.E.1    Marsh, M.2
  • 19
    • 2942640590 scopus 로고    scopus 로고
    • Trafficking of Lyn through the Golgi caveolin involves the charged residues on αe and αi helices in the kinase domain
    • K. Kasahara, Y. Nakayama, K. Ikeda, Y. Fukushima, D. Matsuda, S. Horimoto, and N. Yamaguchi Trafficking of Lyn through the Golgi caveolin involves the charged residues on αE and αI helices in the kinase domain J. Cell Biol. 165 2004 641 652
    • (2004) J. Cell Biol. , vol.165 , pp. 641-652
    • Kasahara, K.1    Nakayama, Y.2    Ikeda, K.3    Fukushima, Y.4    Matsuda, D.5    Horimoto, S.6    Yamaguchi, N.7
  • 22
    • 0025913788 scopus 로고
    • Specific proto-oncogenic tyrosine kinases of src family are enriched in cell-to-cell adherens junctions where the level of tyrosine phosphorylation is elevated
    • S. Tsukita, K. Oishi, T. Akiyama, Y. Yamanashi, T. Yamamoto, and S. Tsukita Specific proto-oncogenic tyrosine kinases of src family are enriched in cell-to-cell adherens junctions where the level of tyrosine phosphorylation is elevated J. Cell Biol. 113 1991 867 879
    • (1991) J. Cell Biol. , vol.113 , pp. 867-879
    • Tsukita, S.1    Oishi, K.2    Akiyama, T.3    Yamanashi, Y.4    Yamamoto, T.5    Tsukita, S.6
  • 23
    • 0032540356 scopus 로고    scopus 로고
    • Overexpression of C-terminal Src kinase homologous kinase suppresses activation of Lyn tyrosine kinase required for VLA5-mediated Dami cell spreading
    • A. Hirao, X.L. Huang, T. Suda, and N. Yamaguchi Overexpression of C-terminal Src kinase homologous kinase suppresses activation of Lyn tyrosine kinase required for VLA5-mediated Dami cell spreading J. Biol. Chem. 273 1998 10004 10010
    • (1998) J. Biol. Chem. , vol.273 , pp. 10004-10010
    • Hirao, A.1    Huang, X.L.2    Suda, T.3    Yamaguchi, N.4
  • 24
    • 0033531214 scopus 로고    scopus 로고
    • The AMPA receptor interacts with and signals through the protein tyrosine kinase Lyn
    • T. Hayashi, H. Umemori, M. Mishina, and T. Yamamoto The AMPA receptor interacts with and signals through the protein tyrosine kinase Lyn Nature 397 1999 72 76
    • (1999) Nature , vol.397 , pp. 72-76
    • Hayashi, T.1    Umemori, H.2    Mishina, M.3    Yamamoto, T.4
  • 26
    • 0029067675 scopus 로고
    • Golgi retention mechanism of β-1,4-galactosyltransferase: Membrane-spanning domain-dependent homodimerization and association with α- And β-tubulins
    • N. Yamaguchi, and M.N. Fukuda Golgi retention mechanism of β-1,4-galactosyltransferase: membrane-spanning domain-dependent homodimerization and association with α- and β-tubulins J. Biol. Chem. 270 1995 12170 12176
    • (1995) J. Biol. Chem. , vol.270 , pp. 12170-12176
    • Yamaguchi, N.1    Fukuda, M.N.2
  • 27
    • 0035020726 scopus 로고    scopus 로고
    • Overexpression of the Csk homologous kinase (Chk tyrosine kinase) induces multinucleation: A possible role for chromosome-associated Chk in chromosome dynamics
    • N. Yamaguchi, Y. Nakayama, T. Urakami, S. Suzuki, T. Nakamura, T. Suda, and N. Oku Overexpression of the Csk homologous kinase (Chk tyrosine kinase) induces multinucleation: a possible role for chromosome-associated Chk in chromosome dynamics J. Cell Sci. 114 2001 1631 1641
    • (2001) J. Cell Sci. , vol.114 , pp. 1631-1641
    • Yamaguchi, N.1    Nakayama, Y.2    Urakami, T.3    Suzuki, S.4    Nakamura, T.5    Suda, T.6    Oku, N.7
  • 30
    • 0037392942 scopus 로고    scopus 로고
    • The specificities of protein kinase inhibitors: An update
    • J. Bain, H. McLauchlan, M. Elliott, and P. Cohen The specificities of protein kinase inhibitors: an update Biochem. J. 371 2003 199 204
    • (2003) Biochem. J. , vol.371 , pp. 199-204
    • Bain, J.1    McLauchlan, H.2    Elliott, M.3    Cohen, P.4
  • 31
    • 0029068249 scopus 로고
    • Activation of the Lck tyrosine protein kinase by hydrogen peroxide requires the phosphorylation of Tyr-394
    • J.S. Hardwick, and B.M. Sefton Activation of the Lck tyrosine protein kinase by hydrogen peroxide requires the phosphorylation of Tyr-394 Proc. Natl. Acad. Sci. U. S. A. 92 1995 4527 4531
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 4527-4531
    • Hardwick, J.S.1    Sefton, B.M.2
  • 32
    • 14644433076 scopus 로고    scopus 로고
    • Multi-lobulation of the nucleus in prolonged S phase by nuclear expression of Chk tyrosine kinase
    • Y. Nakayama, and N. Yamaguchi Multi-lobulation of the nucleus in prolonged S phase by nuclear expression of Chk tyrosine kinase Exp. Cell Res. 304 2005 570 581
    • (2005) Exp. Cell Res. , vol.304 , pp. 570-581
    • Nakayama, Y.1    Yamaguchi, N.2
  • 33
    • 0030997718 scopus 로고    scopus 로고
    • Translocation of the Csk homologous kinase (Chk/Hyl) controls activity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulated platelets
    • A. Hirao, I. Hamaguchi, T. Suda, and N. Yamaguchi Translocation of the Csk homologous kinase (Chk/Hyl) controls activity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulated platelets EMBO J. 16 1997 2342 2351
    • (1997) EMBO J. , vol.16 , pp. 2342-2351
    • Hirao, A.1    Hamaguchi, I.2    Suda, T.3    Yamaguchi, N.4
  • 34
    • 0033060256 scopus 로고    scopus 로고
    • Induction of cell shape changes through activation of the interleukin-3 common ß chain receptor by the RON receptor-type tyrosine kinase
    • A. Mera, M. Suga, M. Ando, T. Suda, and N. Yamaguchi Induction of cell shape changes through activation of the interleukin-3 common ß chain receptor by the RON receptor-type tyrosine kinase J. Biol. Chem. 274 1999 15766 15774
    • (1999) J. Biol. Chem. , vol.274 , pp. 15766-15774
    • Mera, A.1    Suga, M.2    Ando, M.3    Suda, T.4    Yamaguchi, N.5
  • 35
    • 0029737640 scopus 로고    scopus 로고
    • Systematic peptide fragmentation of polyvinylidene difluoride (PVDF)-immobilized proteins prior to microsequencing
    • A. Iwamatsu, and N. Yoshida-Kubomura Systematic peptide fragmentation of polyvinylidene difluoride (PVDF)-immobilized proteins prior to microsequencing J. Biochem. 120 1996 29 34
    • (1996) J. Biochem. , vol.120 , pp. 29-34
    • Iwamatsu, A.1    Yoshida-Kubomura, N.2
  • 36
    • 0036135495 scopus 로고    scopus 로고
    • The ATP-dependent lon protease of Salmonella enterica serovar Typhimurium regulates invasion and expression of genes carried on Salmonella pathogenicity island 1
    • A. Takaya, T. Tomoyasu, A. Tokumitsu, M. Morioka, and T. Yamamoto The ATP-dependent lon protease of Salmonella enterica serovar Typhimurium regulates invasion and expression of genes carried on Salmonella pathogenicity island 1 J. Bacteriol. 184 2002 224 232
    • (2002) J. Bacteriol. , vol.184 , pp. 224-232
    • Takaya, A.1    Tomoyasu, T.2    Tokumitsu, A.3    Morioka, M.4    Yamamoto, T.5
  • 37
    • 0029959639 scopus 로고    scopus 로고
    • STK/RON receptor tyrosine kinase mediates both apoptotic and growth signals via the multifunctional docking site conserved among the HGF receptor family
    • A. Iwama, N. Yamaguchi, and T. Suda STK/RON receptor tyrosine kinase mediates both apoptotic and growth signals via the multifunctional docking site conserved among the HGF receptor family EMBO J. 15 1996 5866 5875
    • (1996) EMBO J. , vol.15 , pp. 5866-5875
    • Iwama, A.1    Yamaguchi, N.2    Suda, T.3
  • 38
    • 0033152305 scopus 로고    scopus 로고
    • A common signaling pathway via Syk and Lyn tyrosine kinases generated from capping of the sialomucins CD34 and CD43 in immature hematopoietic cells
    • J. Tada, M. Omine, T. Suda, and N. Yamaguchi A common signaling pathway via Syk and Lyn tyrosine kinases generated from capping of the sialomucins CD34 and CD43 in immature hematopoietic cells Blood 93 1999 3723 3735
    • (1999) Blood , vol.93 , pp. 3723-3735
    • Tada, J.1    Omine, M.2    Suda, T.3    Yamaguchi, N.4
  • 39
    • 0028031044 scopus 로고
    • Identification of the plakoglobin-binding domain in desmoglein and its role in plaque assembly and intermediate filament anchorage
    • S.M. Troyanovsky, R.B. Troyanovsky, L.G. Eshkind, V.A. Krutovskikh, R.E. Leube, and W.W. Franke Identification of the plakoglobin-binding domain in desmoglein and its role in plaque assembly and intermediate filament anchorage J. Cell Biol. 127 1994 151 160
    • (1994) J. Cell Biol. , vol.127 , pp. 151-160
    • Troyanovsky, S.M.1    Troyanovsky, R.B.2    Eshkind, L.G.3    Krutovskikh, V.A.4    Leube, R.E.5    Franke, W.W.6
  • 40
    • 0025894092 scopus 로고
    • Cadherin cell adhesion receptors as a morphogenetic regulator
    • M. Takeichi Cadherin cell adhesion receptors as a morphogenetic regulator Science 251 1991 1451 1455
    • (1991) Science , vol.251 , pp. 1451-1455
    • Takeichi, M.1
  • 41
    • 0033521010 scopus 로고    scopus 로고
    • Cortical actin organization: Lessons from ERM (Ezrin/Radixin/Moesin) proteins
    • S. Tsukita, and S. Yonemura Cortical actin organization: lessons from ERM (Ezrin/Radixin/Moesin) proteins J. Biol. Chem. 274 1999 34507 34510
    • (1999) J. Biol. Chem. , vol.274 , pp. 34507-34510
    • Tsukita, S.1    Yonemura, S.2
  • 45
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • R.D. Klausner, J.G. Donaldson, and J. Lippincott-Schwarts Brefeldin A: insights into the control of membrane traffic and organelle structure J. Cell Biol. 116 1992 1071 1080
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwarts, J.3
  • 46
    • 0021135281 scopus 로고
    • Associations of elements of the Golgi apparatus with microtubules
    • A.A. Rogalski, and S.J. Singer Associations of elements of the Golgi apparatus with microtubules J. Cell Biol. 99 1984 1092 1100
    • (1984) J. Cell Biol. , vol.99 , pp. 1092-1100
    • Rogalski, A.A.1    Singer, S.J.2
  • 47
    • 7944235830 scopus 로고    scopus 로고
    • Src-family kinases in B-cell development and signaling
    • S.B. Gauld, and J.C. Cambier Src-family kinases in B-cell development and signaling Oncogene 23 2004 8001 8006
    • (2004) Oncogene , vol.23 , pp. 8001-8006
    • Gauld, S.B.1    Cambier, J.C.2
  • 49
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • K. Simons, and E. Ikonen Functional rafts in cell membranes Nature 387 1997 569 572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 50
    • 0035018581 scopus 로고    scopus 로고
    • Floating the raft hypothesis for immune receptors: Access to rafts controls receptor signaling and trafficking
    • M.L. Dykstra, A. Cherukuri, and S.K. Pierce Floating the raft hypothesis for immune receptors: access to rafts controls receptor signaling and trafficking Traffic 2 2001 160 166
    • (2001) Traffic , vol.2 , pp. 160-166
    • Dykstra, M.L.1    Cherukuri, A.2    Pierce, S.K.3
  • 51
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • D.A. Brown, and E. London Functions of lipid rafts in biological membranes Annu. Rev. Cell Dev. Biol. 14 1998 111 136
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 52
    • 0344462719 scopus 로고    scopus 로고
    • Redox regulation of signal transduction in mammalian cells
    • P. Herrlich, and F.D. Böhmer Redox regulation of signal transduction in mammalian cells Biochem. Pharmacol. 59 2000 35 41
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 35-41
    • Herrlich, P.1    Böhmer, F.D.2
  • 53
    • 0037376674 scopus 로고    scopus 로고
    • Oxidant signals and oxidative stress
    • T. Finkel Oxidant signals and oxidative stress Curr. Opin. Cell Biol. 15 2003 247 254
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 247-254
    • Finkel, T.1
  • 54
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • T.C. Meng, T. Fukada, and N.K. Tonks Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo Mol. Cell 9 2002 387 399
    • (2002) Mol. Cell , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3
  • 57
    • 0033407492 scopus 로고    scopus 로고
    • Annexin II: A mediator of the plasmin/plasminogen activator system
    • K.A. Hajjar, and S. Krishnan Annexin II: a mediator of the plasmin/plasminogen activator system Trends Cardiovasc. Med. 9 1999 128 138
    • (1999) Trends Cardiovasc. Med. , vol.9 , pp. 128-138
    • Hajjar, K.A.1    Krishnan, S.2
  • 58
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: From structure to function
    • V. Gerke, and S.E. Moss Annexins: from structure to function Physiol. Rev. 82 2001 331 371
    • (2001) Physiol. Rev. , vol.82 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 60
    • 0030062726 scopus 로고    scopus 로고
    • Modulation of the rat alveolar macrophage respiratory burst by hydroperoxides is calcium dependent
    • C.R. Hoyal, E. Gozal, H. Zhou, K. Foldenauer, and H.J. Forman Modulation of the rat alveolar macrophage respiratory burst by hydroperoxides is calcium dependent Arch. Biochem. Biophys. 326 1996 166 171
    • (1996) Arch. Biochem. Biophys. , vol.326 , pp. 166-171
    • Hoyal, C.R.1    Gozal, E.2    Zhou, H.3    Foldenauer, K.4    Forman, H.J.5
  • 63
    • 0034695002 scopus 로고    scopus 로고
    • Modes of annexin-membrane interactions analyzed by employing chimeric annexin proteins
    • J. König, and V. Gerke Modes of annexin-membrane interactions analyzed by employing chimeric annexin proteins Biochim. Biophys. Acta 1498 2000 174 180
    • (2000) Biochim. Biophys. Acta , vol.1498 , pp. 174-180
    • König, J.1    Gerke, V.2
  • 64
    • 0034839237 scopus 로고    scopus 로고
    • Association of annexin 2 with recycling endosomes requires either calcium- or cholesterol-stabilized membrane domains
    • D. Zeuschner, W. Stoorvogel, and V. Gerke Association of annexin 2 with recycling endosomes requires either calcium- or cholesterol-stabilized membrane domains Eur. J. Cell Biol. 80 2001 499 507
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 499-507
    • Zeuschner, D.1    Stoorvogel, W.2    Gerke, V.3
  • 65
    • 0033822975 scopus 로고    scopus 로고
    • Biophysical and molecular properties of annexin-formed channels
    • J.I. Kourie, and H.B. Wood Biophysical and molecular properties of annexin-formed channels Prog. Biophys. Mol. Biol. 73 2000 91 134
    • (2000) Prog. Biophys. Mol. Biol. , vol.73 , pp. 91-134
    • Kourie, J.I.1    Wood, H.B.2
  • 66
    • 0037054555 scopus 로고    scopus 로고
    • Retinoic acid stimulates annexin-mediated growth plate chondrocyte mineralization
    • W. Wang, and T. Kirsch Retinoic acid stimulates annexin-mediated growth plate chondrocyte mineralization J. Cell Biol. 157 2002 1061 1069
    • (2002) J. Cell Biol. , vol.157 , pp. 1061-1069
    • Wang, W.1    Kirsch, T.2
  • 67
    • 0037423193 scopus 로고    scopus 로고
    • 2+ influx regulates growth plate chondrocyte maturation and apoptosis
    • 2+ influx regulates growth plate chondrocyte maturation and apoptosis J. Biol. Chem. 278 2003 3762 3769
    • (2003) J. Biol. Chem. , vol.278 , pp. 3762-3769
    • Wang, W.1    Xu, J.2    Kirsch, T.3
  • 69
    • 0025635905 scopus 로고
    • Calcium-activated endonexin II forms calcium channels across acidic phospholipid bilayer membranes
    • E. Rojas, H.B. Pollard, H.T. Haigler, C. Parra, and A.L. Burns Calcium-activated endonexin II forms calcium channels across acidic phospholipid bilayer membranes J. Biol. Chem. 265 1990 21207 21215
    • (1990) J. Biol. Chem. , vol.265 , pp. 21207-21215
    • Rojas, E.1    Pollard, H.B.2    Haigler, H.T.3    Parra, C.4    Burns, A.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.