메뉴 건너뛰기




Volumn 276, Issue 5 45-5, 1999, Pages

Role of tyrosine phosphorylation in the reassembly of occludin and other tight junction proteins

Author keywords

ATP depletion; Cytoskeleton; Occludin; Tyrosine phosphorylation; Zonula occludens 1

Indexed keywords

ADENOSINE TRIPHOSPHATE; GENISTEIN; OCCLUDIN; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE INHIBITOR;

EID: 0033004247     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.1999.276.5.f737     Document Type: Article
Times cited : (197)

References (56)
  • 2
    • 0023918616 scopus 로고
    • Characterization of ZO-1: A protein component of the tight junction from mouse liver and Madin-Darby canine kidney cells
    • Anderson, J. M., B. R. Stevenson, L. A. Jesaitis, D. A. Goodenough, and M. S. Mooseker. Characterization of ZO-1: a protein component of the tight junction from mouse liver and Madin-Darby canine kidney cells. J. Cell Biol. 106: 1141-1149, 1988.
    • (1988) J. Cell Biol. , vol.106 , pp. 1141-1149
    • Anderson, J.M.1    Stevenson, B.R.2    Jesaitis, L.A.3    Goodenough, D.A.4    Mooseker, M.S.5
  • 3
    • 0028609124 scopus 로고
    • ATP depletion: A novel method to study junctional properties in epithelial tissues. I. Rearrangement of the actin cytoskeleton
    • Bacallao, R., A. Garfinkel, S. Monke, G. Zampighi, and L. J. Mandel. ATP depletion: a novel method to study junctional properties in epithelial tissues. I. Rearrangement of the actin cytoskeleton. J. Cell Sci. 107: 3301-3313, 1994.
    • (1994) J. Cell Sci. , vol.107 , pp. 3301-3313
    • Bacallao, R.1    Garfinkel, A.2    Monke, S.3    Zampighi, G.4    Mandel, L.J.5
  • 5
    • 0029908483 scopus 로고    scopus 로고
    • The tight junction protein ZO-2 contains three PDZ (PSD-95/Discs-large/ZO-1) domains and an alternatively spliced region
    • Beatch, M., L. A. Jesaitis, W. J. Gallin, D. Goodenough, and B. R. Stevenson. The tight junction protein ZO-2 contains three PDZ (PSD-95/Discs-large/ZO-1) domains and an alternatively spliced region. J. Biol. Chem. 271: 25723-25726, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25723-25726
    • Beatch, M.1    Jesaitis, L.A.2    Gallin, W.J.3    Goodenough, D.4    Stevenson, B.R.5
  • 7
    • 0030029894 scopus 로고    scopus 로고
    • Protein trafficking and polarity in kidney epithelium: From cell biology to physiology
    • Brown, D., and J. L. Stow. Protein trafficking and polarity in kidney epithelium: from cell biology to physiology. Physiol. Rev. 76: 245-297, 1996.
    • (1996) Physiol. Rev. , vol.76 , pp. 245-297
    • Brown, D.1    Stow, J.L.2
  • 9
    • 0028017451 scopus 로고
    • Regulation of mitogenesis, motogenesis, and tubulogenesis by hepatocyte growth factor in renal collecting duct cells
    • Renal Fluid Electrolyte Physiol. 36
    • Cantley, L. G., E. J. G. Barros, M. Gandhi, M. Rauchman, and S. K. Nigam. Regulation of mitogenesis, motogenesis, and tubulogenesis by hepatocyte growth factor in renal collecting duct cells. Am. J. Physiol. 267 (Renal Fluid Electrolyte Physiol. 36): F271-F280, 1994.
    • (1994) Am. J. Physiol. , vol.267
    • Cantley, L.G.1    Barros, E.J.G.2    Gandhi, M.3    Rauchman, M.4    Nigam, S.K.5
  • 10
    • 0030713369 scopus 로고    scopus 로고
    • On the design and analysis of multicenter trials in acute renal failure
    • Chertow, G. M. On the design and analysis of multicenter trials in acute renal failure. Am. J. Kidney Dis. 30: S96-S101, 1997.
    • (1997) Am. J. Kidney Dis. , vol.30
    • Chertow, G.M.1
  • 11
    • 0029122307 scopus 로고
    • Phosphorylation of the tight junction cingulin and the effects of protein kinase inhibitors and activators in MDCK epithelial cells
    • Citi, S., and N. Denisenko. Phosphorylation of the tight junction cingulin and the effects of protein kinase inhibitors and activators in MDCK epithelial cells. J. Cell Sci. 108: 2917-2926, 1995.
    • (1995) J. Cell Sci. , vol.108 , pp. 2917-2926
    • Citi, S.1    Denisenko, N.2
  • 12
    • 0031893838 scopus 로고    scopus 로고
    • Molecular structure and assembly of the tight junction
    • Renal Physiol. 43
    • Denker, B. M., and S. K. Nigam. Molecular structure and assembly of the tight junction. Am. J. Physiol. 274 (Renal Physiol. 43): F1-F9, 1998.
    • (1998) Am. J. Physiol. , vol.274
    • Denker, B.M.1    Nigam, S.K.2
  • 13
    • 0029862538 scopus 로고    scopus 로고
    • Involvement of a heterotrimeric G protein a subunit in tight junction biogenesis
    • Denker, B. M., C. Saha, S. Khawaja, and S. K. Nigam. Involvement of a heterotrimeric G protein a subunit in tight junction biogenesis. J. Biol. Chem. 271: 25750-25753, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25750-25753
    • Denker, B.M.1    Saha, C.2    Khawaja, S.3    Nigam, S.K.4
  • 14
    • 0028355697 scopus 로고
    • Method for recovering ATP content and mitochondrial function after chemical anoxia in renal cell cultures
    • Cell Physiol. 35
    • Doctor, R. B., R. Bacallao, and L. J. Mandel. Method for recovering ATP content and mitochondrial function after chemical anoxia in renal cell cultures. Am. J. Physiol. 266 (Cell Physiol. 35): C1803-C1811, 1994.
    • (1994) Am. J. Physiol. , vol.266
    • Doctor, R.B.1    Bacallao, R.2    Mandel, L.J.3
  • 15
    • 0029883798 scopus 로고    scopus 로고
    • Identification of isoforms of G proteins and PKC that colocalized tight junctions
    • Dodane, V., and B. Kachar. Identification of isoforms of G proteins and PKC that colocalized tight junctions. J. Membr. Biol. 149: 199-209, 1996.
    • (1996) J. Membr. Biol. , vol.149 , pp. 199-209
    • Dodane, V.1    Kachar, B.2
  • 16
  • 17
    • 0032491391 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton
    • Fanning, A. S., B. J. Jameson, L. A. Jesaitis, and J. M. Anderson. The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton. J. Biol. Chem. 273: 29745-29753, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29745-29753
    • Fanning, A.S.1    Jameson, B.J.2    Jesaitis, L.A.3    Anderson, J.M.4
  • 18
    • 0032053707 scopus 로고    scopus 로고
    • Oxygen radicals and signaling
    • Finkel, T. Oxygen radicals and signaling. Curr. Opin. Cell Biol. 10: 248-253, 1998.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 248-253
    • Finkel, T.1
  • 19
    • 0028298272 scopus 로고
    • Alterations in epithelial polarity and the pathogenesis of disease states
    • Fish, E. M., and B. A. Molitoris. Alterations in epithelial polarity and the pathogenesis of disease states. N. Engl. J. Med. 330: 1580-1588, 1994.
    • (1994) N. Engl. J. Med. , vol.330 , pp. 1580-1588
    • Fish, E.M.1    Molitoris, B.A.2
  • 20
    • 0030764263 scopus 로고    scopus 로고
    • Insulin-like growth factor I preserves renal function postoperatively
    • Renal Physiol. 41
    • Franklin, S. C., M. Moulton, G. A. Sicard, M. R. Hammerman, and S. B. Miller. Insulin-like growth factor I preserves renal function postoperatively. Am. J. Physiol. 272 (Renal Physiol. 41): F257-F259, 1997.
    • (1997) Am. J. Physiol. , vol.272
    • Franklin, S.C.1    Moulton, M.2    Sicard, G.A.3    Hammerman, M.R.4    Miller, S.B.5
  • 21
    • 0032577975 scopus 로고    scopus 로고
    • Claudin-1 and claudin-2: Novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin
    • Furuse, M., K. Fujita, T. Hiiragi, K. Fujimoto, and S. Tsukita. Claudin-1 and claudin-2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin. J. Cell Biol. 141: 1539-1550, 1998.
    • (1998) J. Cell Biol. , vol.141 , pp. 1539-1550
    • Furuse, M.1    Fujita, K.2    Hiiragi, T.3    Fujimoto, K.4    Tsukita, S.5
  • 22
    • 0028110309 scopus 로고
    • Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions
    • Furuse, M., M. Itoh, T. Hirase, A. Nagafuchi, S. Yonemura, S. Tsukita, and S. Tsukita. Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions. J. Cell Biol. 127: 1617-1626, 1994.
    • (1994) J. Cell Biol. , vol.127 , pp. 1617-1626
    • Furuse, M.1    Itoh, M.2    Hirase, T.3    Nagafuchi, A.4    Yonemura, S.5    Tsukita, S.6    Tsukita, S.7
  • 23
    • 0030056968 scopus 로고    scopus 로고
    • Cell adhesion: The molecular basis of tissue architecture and morphogenesis
    • Gumbiner, B. M. Cell adhesion: the molecular basis of tissue architecture and morphogenesis. Cell 84: 345-357, 1996.
    • (1996) Cell , vol.84 , pp. 345-357
    • Gumbiner, B.M.1
  • 24
    • 0030950861 scopus 로고    scopus 로고
    • Growth factor and cytokines in acute renal failure
    • Harris, R. C. Growth factor and cytokines in acute renal failure. Adv. Ren. Replace. Ther. 4: 43-53, 1997.
    • (1997) Adv. Ren. Replace. Ther. , vol.4 , pp. 43-53
    • Harris, R.C.1
  • 25
    • 0032489875 scopus 로고    scopus 로고
    • ZO-3, a novel member of the MAGUK protein family found at the tight junction, interactions with ZO-1 and occludin
    • Haskins, J., L. Gu, E. S. Wittchen, J. Hibbard, and B. R. Stevenson. ZO-3, a novel member of the MAGUK protein family found at the tight junction, interactions with ZO-1 and occludin. J. Cell Biol. 141: 199-208, 1998.
    • (1998) J. Cell Biol. , vol.141 , pp. 199-208
    • Haskins, J.1    Gu, L.2    Wittchen, E.S.3    Hibbard, J.4    Stevenson, B.R.5
  • 27
    • 0030738023 scopus 로고    scopus 로고
    • Biologically active peptides in acute renal failure: Recent clinical trials
    • Hirsberg, R. Biologically active peptides in acute renal failure: recent clinical trials. Nephrol. Dial. Transplant. 12: 1563-1566, 1997.
    • (1997) Nephrol. Dial. Transplant. , vol.12 , pp. 1563-1566
    • Hirsberg, R.1
  • 28
    • 0028922237 scopus 로고
    • Epidermal growth factor induces tyrosine phosphorylation and reorganization of the tight junction protein ZO-1 in A431 cells
    • Itallie, C. M. V., M. S. Balda, and J. M. Anderson. Epidermal growth factor induces tyrosine phosphorylation and reorganization of the tight junction protein ZO-1 in A431 cells. J. Cell Sci. 108: 1735-1742, 1995.
    • (1995) J. Cell Sci. , vol.108 , pp. 1735-1742
    • Itallie, C.M.V.1    Balda, M.S.2    Anderson, J.M.3
  • 29
    • 0025888954 scopus 로고
    • A 220-kDa undercoat-constitutive protein: Its specific localization at cadherin-based cell-cell adhesion sites
    • Itoh, M., S. Yonemura, A. Nagafuchi, S. Tsukita, and S. Tsukita. A 220-kDa undercoat-constitutive protein: its specific localization at cadherin-based cell-cell adhesion sites. J. Cell Biol. 115: 1449-1462, 1991.
    • (1991) J. Cell Biol. , vol.115 , pp. 1449-1462
    • Itoh, M.1    Yonemura, S.2    Nagafuchi, A.3    Tsukita, S.4    Tsukita, S.5
  • 30
  • 31
    • 0029840160 scopus 로고    scopus 로고
    • Symplekin, a novel type of tight junction plaque protein
    • Keon, B. H., S. Schäfer, C. Kuhn, C. Grund, and W. W. Franke. Symplekin, a novel type of tight junction plaque protein. J. Cell Biol. 134: 1003-1018, 1996.
    • (1996) J. Cell Biol. , vol.134 , pp. 1003-1018
    • Keon, B.H.1    Schäfer, S.2    Kuhn, C.3    Grund, C.4    Franke, W.W.5
  • 32
    • 0029143156 scopus 로고
    • Tight junction, membrane-associated guanylate kinases and cell signaling
    • Kim, S. K. Tight junction, membrane-associated guanylate kinases and cell signaling. Curr. Opin. Cell Biol. 7: 641-649, 1995.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 641-649
    • Kim, S.K.1
  • 33
    • 0028055171 scopus 로고
    • Functional and cytoskeletal changes induced by sublethal injury in proximal tubular epithelial cells
    • Renal Fluid Electrolyte Physiol. 35
    • Kroshian, V. M., A. M. Sheridan, and W. Lieberthal. Functional and cytoskeletal changes induced by sublethal injury in proximal tubular epithelial cells. Am. J. Physiol. 266 (Renal Fluid Electrolyte Physiol. 35): F21-F30, 1994.
    • (1994) Am. J. Physiol. , vol.266
    • Kroshian, V.M.1    Sheridan, A.M.2    Lieberthal, W.3
  • 34
    • 0028953668 scopus 로고
    • Increased Tyr phosphorylation of ZO-1 during modification of tight junctions between glomerular foot processes
    • Renal Fluid Electrolyte Physiol. 37
    • Kurihara, H., J. M. Anderson, and M. G. Farquhar. Increased Tyr phosphorylation of ZO-1 during modification of tight junctions between glomerular foot processes. Am. J. Physiol. 268 (Renal Fluid Electrolyte Physiol. 37): F514-F524, 1995.
    • (1995) Am. J. Physiol. , vol.268
    • Kurihara, H.1    Anderson, J.M.2    Farquhar, M.G.3
  • 35
    • 0027339375 scopus 로고
    • Uncoupling of the molecular "fence" and paracellular "gate" functions in epithelial tight junctions
    • Mandel, L. J., R. Bacallao, and G. Zampighi. Uncoupling of the molecular "fence" and paracellular "gate" functions in epithelial tight junctions. Nature 361: 552-555, 1993.
    • (1993) Nature , vol.361 , pp. 552-555
    • Mandel, L.J.1    Bacallao, R.2    Zampighi, G.3
  • 37
    • 0031944250 scopus 로고    scopus 로고
    • Molecular architecture of tight junction
    • Mitic, L. L., and J. M. Anderson. Molecular architecture of tight junction. Annu. Rev. Physiol. 60: 121-142, 1998.
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 121-142
    • Mitic, L.L.1    Anderson, J.M.2
  • 38
    • 0029859715 scopus 로고    scopus 로고
    • Cellular ATP depletion induces disruption of the spectrin cytoskeletal network
    • Renal Fluid Electrolyte Physiol. 40
    • Molitoris, B. A., R. Dahl, and M. Hosford. Cellular ATP depletion induces disruption of the spectrin cytoskeletal network. Am. J. Physiol. 271 (Renal Fluid Electrolyte Physiol. 40): F790-F798, 1996.
    • (1996) Am. J. Physiol. , vol.271
    • Molitoris, B.A.1    Dahl, R.2    Hosford, M.3
  • 39
    • 0030953448 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in signal transduction
    • Neel, B. G., and N. K. Tonks. Protein tyrosine phosphatases in signal transduction. Curr. Opin. Cell Biol. 9: 193-204, 1997.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 193-204
    • Neel, B.G.1    Tonks, N.K.2
  • 40
    • 0026338562 scopus 로고
    • The role of phosphorylation in development of tight junctions in cultured renal epithelial (MDCK) cells
    • Nigam, S. K., N. Denisenko, E. Rodriguez-Boulan, and S. Citi. The role of phosphorylation in development of tight junctions in cultured renal epithelial (MDCK) cells. Biochem. Biophys. Res. Commun. 181: 548-553, 1991.
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 548-553
    • Nigam, S.K.1    Denisenko, N.2    Rodriguez-Boulan, E.3    Citi, S.4
  • 42
    • 0032550221 scopus 로고    scopus 로고
    • Occludin-deficient embryonic stem cells can differentiate into polarized epithelial cells bearing tight junctions
    • Saitou, M., K. Fujimoto, Y. Doi, M. Itoh, T. Fujimoto, M. Furuse, H. Takano, T. Noda, and S. Tsukita. Occludin-deficient embryonic stem cells can differentiate into polarized epithelial cells bearing tight junctions. J. Cell Biol. 141: 397-408, 1998.
    • (1998) J. Cell Biol. , vol.141 , pp. 397-408
    • Saitou, M.1    Fujimoto, K.2    Doi, Y.3    Itoh, M.4    Fujimoto, T.5    Furuse, M.6    Takano, H.7    Noda, T.8    Tsukita, S.9
  • 43
    • 0030982357 scopus 로고    scopus 로고
    • Possible involvement of phosphorylation of occludin in tight junction formation
    • Sakakibara, A., M. Furuse, M. Saitou, Y. Ando-Akatsuka, and S. Tsukita. Possible involvement of phosphorylation of occludin in tight junction formation. J. Cell Biol. 137: 1393-1401, 1997.
    • (1997) J. Cell Biol. , vol.137 , pp. 1393-1401
    • Sakakibara, A.1    Furuse, M.2    Saitou, M.3    Ando-Akatsuka, Y.4    Tsukita, S.5
  • 44
    • 0028931103 scopus 로고
    • Evidence that tyrosine phosphorylation may increase tight junction permeability
    • Staddon, J. M., K. Herrenknecht, C. Smales, and L. L. Rubin. Evidence that tyrosine phosphorylation may increase tight junction permeability. J. Cell Sci. 108: 609-619, 1995.
    • (1995) J. Cell Sci. , vol.108 , pp. 609-619
    • Staddon, J.M.1    Herrenknecht, K.2    Smales, C.3    Rubin, L.L.4
  • 45
    • 0027970874 scopus 로고
    • Protein-tyrosine phosphatases
    • Stone, R. L., and J. E. Dixon. Protein-tyrosine phosphatases. J. Biol. Chem. 269: 31323-31326, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31323-31326
    • Stone, R.L.1    Dixon, J.E.2
  • 46
    • 0029019364 scopus 로고
    • Development of tubular nephron
    • Stuart, R. O., and S. K. Nigam. Development of tubular nephron. Semin. Nephrol. 15: 315-326, 1995.
    • (1995) Semin. Nephrol. , vol.15 , pp. 315-326
    • Stuart, R.O.1    Nigam, S.K.2
  • 47
    • 0029041046 scopus 로고
    • Regulated assembly of tight junctions by protein kinase C
    • Stuart, R. O., and S. K. Nigam. Regulated assembly of tight junctions by protein kinase C. Proc. Natl. Acad. Sci. USA 92: 6072-6076, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6072-6076
    • Stuart, R.O.1    Nigam, S.K.2
  • 48
    • 0029967354 scopus 로고    scopus 로고
    • Dependence of epithelial intercellular junction biogenesis on thapsigargin-sensitive intracellular calcium stores
    • Stuart, R. O., A. Sun, K. T. Bush, and S. K. Nigam. Dependence of epithelial intercellular junction biogenesis on thapsigargin-sensitive intracellular calcium stores. J. Biol. Chem. 271: 13636-13641, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13636-13641
    • Stuart, R.O.1    Sun, A.2    Bush, K.T.3    Nigam, S.K.4
  • 49
    • 0029615381 scopus 로고
    • V-src kinase shifts the cadherin-based cell adhesion from the strong to the weak state and b catenin is not required for the shift
    • Takeda, H., A. Nagafuchi, S. Yonemura, S. Tsukita, J. Behrens, W. Birchimeier, and S. Tsukita. V-src kinase shifts the cadherin-based cell adhesion from the strong to the weak state and b catenin is not required for the shift. J. Cell Biol. 131: 1839-1847, 1995.
    • (1995) J. Cell Biol. , vol.131 , pp. 1839-1847
    • Takeda, H.1    Nagafuchi, A.2    Yonemura, S.3    Tsukita, S.4    Behrens, J.5    Birchimeier, W.6    Tsukita, S.7
  • 50
    • 0028819708 scopus 로고
    • Effects of tyrosine phosphorylation on tight junction in temperature-sensitive v-src-transfected MDCK cells
    • Takeda, H., and S. Tsukita. Effects of tyrosine phosphorylation on tight junction in temperature-sensitive v-src-transfected MDCK cells. Cell Struct. Funct. 20: 387-393, 1995.
    • (1995) Cell Struct. Funct. , vol.20 , pp. 387-393
    • Takeda, H.1    Tsukita, S.2
  • 52
    • 0030946064 scopus 로고    scopus 로고
    • Tight junction proteins form large complexes and associate with the cytoskeleton in an ATP depletion model for reversible junction assembly
    • Tsukamoto, T., and S. K. Nigam. Tight junction proteins form large complexes and associate with the cytoskeleton in an ATP depletion model for reversible junction assembly. J. Biol. Chem. 272: 16133-16139, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16133-16139
    • Tsukamoto, T.1    Nigam, S.K.2
  • 54
    • 0031425958 scopus 로고    scopus 로고
    • Phosphorylation of occludin correlates with occludin localization and function at the tight junction
    • Cell Physiol. 42
    • Wong, V. Phosphorylation of occludin correlates with occludin localization and function at the tight junction. Am. J. Physiol. 273 (Cell Physiol. 42): C1859-C1867, 1997.
    • (1997) Am. J. Physiol. , vol.273
    • Wong, V.1
  • 55
    • 0028008838 scopus 로고
    • A small rab GTPase is distributed in cytoplasmic vesicles in non polarized cells but colocalizes with the tight junction marker ZO-1 in polarized epithelial cells
    • Zahraoui, A., G. Joberty, M. Arpin, J. J. Fontaine, R. Hellio, A. Tavitian, and D. Louvard. A small rab GTPase is distributed in cytoplasmic vesicles in non polarized cells but colocalizes with the tight junction marker ZO-1 in polarized epithelial cells. J. Cell Biol. 124: 101-115, 1994.
    • (1994) J. Cell Biol. , vol.124 , pp. 101-115
    • Zahraoui, A.1    Joberty, G.2    Arpin, M.3    Fontaine, J.J.4    Hellio, R.5    Tavitian, A.6    Louvard, D.7
  • 56
    • 0028109285 scopus 로고
    • Localization of the 7H6 antigen at tight junctions correlates with the paracellular barrier function of MDCK cells
    • Zhong, Y., K. Enomoto, H. Isomura, N. Sawada, T. Minase, M. Oyamada, Y. Konishi, and M. Mori. Localization of the 7H6 antigen at tight junctions correlates with the paracellular barrier function of MDCK cells. Exp. Cell Res. 214: 614-620, 1994.
    • (1994) Exp. Cell Res. , vol.214 , pp. 614-620
    • Zhong, Y.1    Enomoto, K.2    Isomura, H.3    Sawada, N.4    Minase, T.5    Oyamada, M.6    Konishi, Y.7    Mori, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.