메뉴 건너뛰기




Volumn 4, Issue 4, 2009, Pages

Ste20-related proline/alanine-rich kinase (SPAK) regulated transcriptionally by hypersmolarity is involved in intestinal barrier function

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MESSENGER RNA; PHOSPHOTRANSFERASE; SMALL INTERFERING RNA; STE20 RELATED PROLINE ALANINE RICH KINASE; TRANSCRIPTION FACTOR SP1; UNCLASSIFIED DRUG; PROTEIN SERINE THREONINE KINASE; STK39 PROTEIN, HUMAN; STK39 PROTEIN, MOUSE;

EID: 64549084094     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0005049     Document Type: Article
Times cited : (26)

References (97)
  • 1
    • 0020040032 scopus 로고
    • Comparison of the composition of faecal fluid in Crohn's disease and ulcerative colitis
    • Schilli R, Breuer RI, Klein F, Dunn K, Gnaedinger A, et al. (1982) Comparison of the composition of faecal fluid in Crohn's disease and ulcerative colitis. Gut 23: 326-332.
    • (1982) Gut , vol.23 , pp. 326-332
    • Schilli, R.1    Breuer, R.I.2    Klein, F.3    Dunn, K.4    Gnaedinger, A.5
  • 2
    • 0024462586 scopus 로고
    • Intestinal permeability in patients with Crohn's disease and their healthy relatives
    • Katz KD, Hollander D, Vadheim CM, McElree C, Delahunty T, et al. (1989) Intestinal permeability in patients with Crohn's disease and their healthy relatives. Gastroenterology 97: 927-931.
    • (1989) Gastroenterology , vol.97 , pp. 927-931
    • Katz, K.D.1    Hollander, D.2    Vadheim, C.M.3    McElree, C.4    Delahunty, T.5
  • 3
    • 0025314386 scopus 로고
    • Cellular basis for defective electrolyte transport in inflamed human colon
    • Sandle GI, Higgs N, Crowe P, Marsh MN, Venkatesan S, et al. (1990) Cellular basis for defective electrolyte transport in inflamed human colon. Gastroenterology 99: 97-105.
    • (1990) Gastroenterology , vol.99 , pp. 97-105
    • Sandle, G.I.1    Higgs, N.2    Crowe, P.3    Marsh, M.N.4    Venkatesan, S.5
  • 4
    • 0024241538 scopus 로고
    • Organic anions and the diarrhea of inflammatory bowel disease
    • Vernia P, Gnaedinger A, Hauck W, Breuer RI (1988) Organic anions and the diarrhea of inflammatory bowel disease. Dig Dis Sci 33: 1353-1358.
    • (1988) Dig Dis Sci , vol.33 , pp. 1353-1358
    • Vernia, P.1    Gnaedinger, A.2    Hauck, W.3    Breuer, R.I.4
  • 5
    • 0023899587 scopus 로고
    • Neonatal necrotizing enterocolitis. Inflammatory bowel disease of the newborn
    • Cheromcha DP, Hyman PE (1988) Neonatal necrotizing enterocolitis. Inflammatory bowel disease of the newborn. Dig Dis Sci 33: 78S-84S.
    • (1988) Dig Dis Sci , vol.33
    • Cheromcha, D.P.1    Hyman, P.E.2
  • 6
    • 9444230614 scopus 로고    scopus 로고
    • Stimulation of matrix metalloproteinases by hyperosmolarity via a JNK pathway in human corneal epithelial cells
    • Li DQ, Chen Z, Song XJ, Luo L, Pflugfelder SC (2004) Stimulation of matrix metalloproteinases by hyperosmolarity via a JNK pathway in human corneal epithelial cells. Invest Ophthalmol Vis Sci 45: 4302-4311.
    • (2004) Invest Ophthalmol Vis Sci , vol.45 , pp. 4302-4311
    • Li, D.Q.1    Chen, Z.2    Song, X.J.3    Luo, L.4    Pflugfelder, S.C.5
  • 7
    • 0031569363 scopus 로고    scopus 로고
    • Hyperosmotic stress as a stimulant for proinflammatory cytokine production
    • Shapiro L, Dinarello CA (1997) Hyperosmotic stress as a stimulant for proinflammatory cytokine production. Exp Cell Res 231: 354-362.
    • (1997) Exp Cell Res , vol.231 , pp. 354-362
    • Shapiro, L.1    Dinarello, C.A.2
  • 8
    • 0032973284 scopus 로고    scopus 로고
    • Hyperosmolarity-induced interleukin-8 expression in human bronchial epithelial cells through p38 mitogen-activated protein kinase
    • Hashimoto S, Matsumoto K, Gon Y, Nakayama T, Takeshita I, et al. (1999) Hyperosmolarity-induced interleukin-8 expression in human bronchial epithelial cells through p38 mitogen-activated protein kinase. Am J Respir Crit Care Med 159: 634-640.
    • (1999) Am J Respir Crit Care Med , vol.159 , pp. 634-640
    • Hashimoto, S.1    Matsumoto, K.2    Gon, Y.3    Nakayama, T.4    Takeshita, I.5
  • 9
    • 0034710811 scopus 로고    scopus 로고
    • Reactive oxygen intermediates are involved in IL-8 production induced by hyperosmotic stress in human bronchial epithelial cells
    • Loitsch SM, von Mallinckrodt C, Kippenberger S, Steinhilber D, Wagner TO, et al. (2000) Reactive oxygen intermediates are involved in IL-8 production induced by hyperosmotic stress in human bronchial epithelial cells. Biochem Biophys Res Commun 276: 571-578.
    • (2000) Biochem Biophys Res Commun , vol.276 , pp. 571-578
    • Loitsch, S.M.1    von Mallinckrodt, C.2    Kippenberger, S.3    Steinhilber, D.4    Wagner, T.O.5
  • 10
    • 0036735192 scopus 로고    scopus 로고
    • Hyperosmotic stress induces nuclear factor-kappaB activation and interleukin-8 production in human intestinal epithelial cells
    • Nemeth ZH, Deitch EA, Szabo C, Hasko G (2002) Hyperosmotic stress induces nuclear factor-kappaB activation and interleukin-8 production in human intestinal epithelial cells. Am J Pathol 161: 987-996.
    • (2002) Am J Pathol , vol.161 , pp. 987-996
    • Nemeth, Z.H.1    Deitch, E.A.2    Szabo, C.3    Hasko, G.4
  • 11
    • 0030906945 scopus 로고    scopus 로고
    • High glucose and hyperosmolarity increase secretion of interleukin-1 beta in cultured human aortic endothelial cells
    • Asakawa H, Miyagawa J, Hanafusa T, Kuwajima M, Matsuzawa Y (1997) High glucose and hyperosmolarity increase secretion of interleukin-1 beta in cultured human aortic endothelial cells. J Diabetes Complications 11: 176-179.
    • (1997) J Diabetes Complications , vol.11 , pp. 176-179
    • Asakawa, H.1    Miyagawa, J.2    Hanafusa, T.3    Kuwajima, M.4    Matsuzawa, Y.5
  • 13
    • 31044455375 scopus 로고    scopus 로고
    • JNK and ERK MAP kinases mediate induction of IL-1beta, TNF-alpha and IL-8 following hyperosmolar stress in human limbal epithelial cells
    • Li DQ, Luo L, Chen Z, Kim HS, Song XJ, et al. (2006) JNK and ERK MAP kinases mediate induction of IL-1beta, TNF-alpha and IL-8 following hyperosmolar stress in human limbal epithelial cells. Exp Eye Res 82: 588-596.
    • (2006) Exp Eye Res , vol.82 , pp. 588-596
    • Li, D.Q.1    Luo, L.2    Chen, Z.3    Kim, H.S.4    Song, X.J.5
  • 14
    • 0036316490 scopus 로고    scopus 로고
    • Hyperosmotic stimuli inhibit VCAM-1 expression in cultured endothelial cells via effects on interferon regulatory factor-1 expression and activity
    • Ochi H, Masuda J, Gimbrone MA (2002) Hyperosmotic stimuli inhibit VCAM-1 expression in cultured endothelial cells via effects on interferon regulatory factor-1 expression and activity. Eur J Immunol 32: 1821-1831.
    • (2002) Eur J Immunol , vol.32 , pp. 1821-1831
    • Ochi, H.1    Masuda, J.2    Gimbrone, M.A.3
  • 16
    • 31044453568 scopus 로고    scopus 로고
    • Hyperosmolar saline is a proinflammatory stress on the mouse ocular surface
    • Luo L, Li DQ, Corrales RM, Pflugfelder SC (2005) Hyperosmolar saline is a proinflammatory stress on the mouse ocular surface. Eye Contact Lens 31: 186-193.
    • (2005) Eye Contact Lens , vol.31 , pp. 186-193
    • Luo, L.1    Li, D.Q.2    Corrales, R.M.3    Pflugfelder, S.C.4
  • 17
    • 0037974828 scopus 로고    scopus 로고
    • A convenient rabbit model of ocular epithelium damage induced by osmotic dehydration
    • Katsuyama I, Arakawa T (2003) A convenient rabbit model of ocular epithelium damage induced by osmotic dehydration. J Ocul Pharmacol Ther 19: 281-289.
    • (2003) J Ocul Pharmacol Ther , vol.19 , pp. 281-289
    • Katsuyama, I.1    Arakawa, T.2
  • 19
    • 0033605292 scopus 로고    scopus 로고
    • Signaling by the germinal center kinase family of protein kinases
    • Kyriakis JM (1999) Signaling by the germinal center kinase family of protein kinases. J Biol Chem 274: 5259-5262.
    • (1999) J Biol Chem , vol.274 , pp. 5259-5262
    • Kyriakis, J.M.1
  • 20
    • 0032928614 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase: Conservation of a three-kinase module from yeast to human
    • Widmann C, Gibson S, Jarpe MB, Johnson GL (1999) Mitogen-activated protein kinase: conservation of a three-kinase module from yeast to human. Physiol Rev 79: 143-180.
    • (1999) Physiol Rev , vol.79 , pp. 143-180
    • Widmann, C.1    Gibson, S.2    Jarpe, M.B.3    Johnson, G.L.4
  • 21
    • 0032054723 scopus 로고    scopus 로고
    • Signal transduction by the c-Jun N-terminal kinase (JNK)-from inflammation to development
    • Ip YT, Davis RJ (1998) Signal transduction by the c-Jun N-terminal kinase (JNK)-from inflammation to development. Curr Opin Cell Biol 10: 205-219.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 205-219
    • Ip, Y.T.1    Davis, R.J.2
  • 23
    • 0033954866 scopus 로고    scopus 로고
    • Deficiency of a STE20/PAK family kinase LOK leads to the acceleration of LFA-1 clustering and cell adhesion of activated lymphocytes
    • Endo J, Toyama-Sorimachi N, Taya C, Kuramochi-Miyagawa S, Nagata K, et al. (2000) Deficiency of a STE20/PAK family kinase LOK leads to the acceleration of LFA-1 clustering and cell adhesion of activated lymphocytes. FEBS Lett 468: 234-238.
    • (2000) FEBS Lett , vol.468 , pp. 234-238
    • Endo, J.1    Toyama-Sorimachi, N.2    Taya, C.3    Kuramochi-Miyagawa, S.4    Nagata, K.5
  • 24
    • 0037020101 scopus 로고    scopus 로고
    • Association of the Ste20-like kinase (SLK) with the microtubule. Role in Rac1-mediated regulation of actin dynamics during cell adhesion and spreading
    • Wagner S, Flood TA, O'Reilly P, Hume K, Sabourin LA (2002) Association of the Ste20-like kinase (SLK) with the microtubule. Role in Rac1-mediated regulation of actin dynamics during cell adhesion and spreading. J Biol Chem 277: 37685-37692.
    • (2002) J Biol Chem , vol.277 , pp. 37685-37692
    • Wagner, S.1    Flood, T.A.2    O'Reilly, P.3    Hume, K.4    Sabourin, L.A.5
  • 25
    • 8744274131 scopus 로고    scopus 로고
    • p21-activated kinase regulates endothelial permeability through modulation of contractility
    • Stockton RA, Schaefer E, Schwartz MA (2004) p21-activated kinase regulates endothelial permeability through modulation of contractility. J Biol Chem 279: 46621-46630.
    • (2004) J Biol Chem , vol.279 , pp. 46621-46630
    • Stockton, R.A.1    Schaefer, E.2    Schwartz, M.A.3
  • 26
    • 34250353521 scopus 로고    scopus 로고
    • Induction of vascular permeability: Beta PIX and GIT1 scaffold the activation of extracellular signal-regulated kinase by PAK
    • Stockton R, Reutershan J, Scott D, Sanders J, Ley K, et al. (2007) Induction of vascular permeability: beta PIX and GIT1 scaffold the activation of extracellular signal-regulated kinase by PAK. Mol Biol Cell 18: 2346-2355.
    • (2007) Mol Biol Cell , vol.18 , pp. 2346-2355
    • Stockton, R.1    Reutershan, J.2    Scott, D.3    Sanders, J.4    Ley, K.5
  • 28
    • 33847374563 scopus 로고    scopus 로고
    • Cloning and characterization of a new intestinal inflammation-associated colonic epithelial Ste20-related protein kinase isoform
    • Yan Y, Nguyen H, Dalmasso G, Sitaraman SV, Merlin D (2007) Cloning and characterization of a new intestinal inflammation-associated colonic epithelial Ste20-related protein kinase isoform. Biochim Biophys Acta 1769: 106-116.
    • (2007) Biochim Biophys Acta , vol.1769 , pp. 106-116
    • Yan, Y.1    Nguyen, H.2    Dalmasso, G.3    Sitaraman, S.V.4    Merlin, D.5
  • 29
    • 53149133900 scopus 로고    scopus 로고
    • Nuclear factor-kappaB is a critical mediator of Ste20-like proline-/alanine-rich kinase regulation in intestinal inflammation
    • Yan Y, Dalmasso G, Nguyen HT, Obertone TS, Charrier-Hisamuddin L, et al. (2008) Nuclear factor-kappaB is a critical mediator of Ste20-like proline-/alanine-rich kinase regulation in intestinal inflammation. Am J Pathol 173: 1013-1028.
    • (2008) Am J Pathol , vol.173 , pp. 1013-1028
    • Yan, Y.1    Dalmasso, G.2    Nguyen, H.T.3    Obertone, T.S.4    Charrier-Hisamuddin, L.5
  • 30
    • 0035341895 scopus 로고    scopus 로고
    • The Ste20 group kinases as regulators of MAP kinase cascades
    • Dan I, Watanabe NM, Kusumi A (2001) The Ste20 group kinases as regulators of MAP kinase cascades. Trends Cell Biol 11: 220-230.
    • (2001) Trends Cell Biol , vol.11 , pp. 220-230
    • Dan, I.1    Watanabe, N.M.2    Kusumi, A.3
  • 31
    • 1842524184 scopus 로고    scopus 로고
    • SPAK kinase is a substrate and target of PKCtheta in T-cell receptor-induced AP-1 activation pathway
    • Li Y, Hu J, Vita R, Sun B, Tabata H, et al. (2004) SPAK kinase is a substrate and target of PKCtheta in T-cell receptor-induced AP-1 activation pathway. Embo J 23: 1112-1122.
    • (2004) Embo J , vol.23 , pp. 1112-1122
    • Li, Y.1    Hu, J.2    Vita, R.3    Sun, B.4    Tabata, H.5
  • 32
    • 0037184942 scopus 로고    scopus 로고
    • Cation chloride cotransporters interact with the stress-related kinases Ste20-related proline-alanine-rich kinase (SPAK) and oxidative stress response 1 (OSR1)
    • Piechotta K, Lu J, Delpire E (2002) Cation chloride cotransporters interact with the stress-related kinases Ste20-related proline-alanine-rich kinase (SPAK) and oxidative stress response 1 (OSR1). J Biol Chem 277: 50812-50819.
    • (2002) J Biol Chem , vol.277 , pp. 50812-50819
    • Piechotta, K.1    Lu, J.2    Delpire, E.3
  • 33
    • 0042847432 scopus 로고    scopus 로고
    • PASK (proline-alanine-rich STE20-related kinase), a regulatory kinase of the Na-K-Cl cotransporter (NKCC1)
    • Dowd BF, Forbush B (2003) PASK (proline-alanine-rich STE20-related kinase), a regulatory kinase of the Na-K-Cl cotransporter (NKCC1). J Biol Chem 278: 27347-27353.
    • (2003) J Biol Chem , vol.278 , pp. 27347-27353
    • Dowd, B.F.1    Forbush, B.2
  • 34
    • 30644472724 scopus 로고    scopus 로고
    • Characterization of SPAK and OSR1, regulatory kinases of the Na-K-2Cl cotransporter
    • Gagnon KB, England R, Delpire E (2006) Characterization of SPAK and OSR1, regulatory kinases of the Na-K-2Cl cotransporter. Mol Cell Biol 26: 689-698.
    • (2006) Mol Cell Biol , vol.26 , pp. 689-698
    • Gagnon, K.B.1    England, R.2    Delpire, E.3
  • 35
    • 0031008850 scopus 로고    scopus 로고
    • Expression of the bumetanide-sensitive Na-K-Cl cotransporter BSC2 is differentially regulated by fluid mechanical and inflammatory cytokine stimuli in vascular endothelium
    • Topper JN, Wasserman SM, Anderson KR, Cai J, Falb D, et al. (1997) Expression of the bumetanide-sensitive Na-K-Cl cotransporter BSC2 is differentially regulated by fluid mechanical and inflammatory cytokine stimuli in vascular endothelium. J Clin Invest 99: 2941-2949.
    • (1997) J Clin Invest , vol.99 , pp. 2941-2949
    • Topper, J.N.1    Wasserman, S.M.2    Anderson, K.R.3    Cai, J.4    Falb, D.5
  • 36
    • 34250370467 scopus 로고    scopus 로고
    • Mice lacking NKCC1 are protected from development of bacteremia and hypothermic sepsis secondary to bacterial pneumonia
    • Nguyen M, Pace AJ, Koller BH (2007) Mice lacking NKCC1 are protected from development of bacteremia and hypothermic sepsis secondary to bacterial pneumonia. J Exp Med 204: 1383-1393.
    • (2007) J Exp Med , vol.204 , pp. 1383-1393
    • Nguyen, M.1    Pace, A.J.2    Koller, B.H.3
  • 37
    • 15544384004 scopus 로고    scopus 로고
    • Molecular physiology and pathophysiology of electroneutral cation-chloride cotransporters
    • Gamba G (2005) Molecular physiology and pathophysiology of electroneutral cation-chloride cotransporters. Physiol Rev 85: 423-493.
    • (2005) Physiol Rev , vol.85 , pp. 423-493
    • Gamba, G.1
  • 38
    • 0030005634 scopus 로고    scopus 로고
    • Changes in cytoskeletal actin content, F-actin distribution, and surface morphology during HL-60 cell volume regulation
    • Hallows KR, Law FY, Packman CH, Knauf PA (1996) Changes in cytoskeletal actin content, F-actin distribution, and surface morphology during HL-60 cell volume regulation. J Cell Physiol 167: 60-71.
    • (1996) J Cell Physiol , vol.167 , pp. 60-71
    • Hallows, K.R.1    Law, F.Y.2    Packman, C.H.3    Knauf, P.A.4
  • 39
    • 0033835798 scopus 로고    scopus 로고
    • Hypertonic inhibition of exocytosis in neutrophils: Central role for osmotic actin skeleton remodeling
    • Rizoli SB, Rotstein OD, Parodo J, Phillips MJ, Kapus A (2000) Hypertonic inhibition of exocytosis in neutrophils: central role for osmotic actin skeleton remodeling. Am J Physiol Cell Physiol 279: C619-633.
    • (2000) Am J Physiol Cell Physiol , vol.279
    • Rizoli, S.B.1    Rotstein, O.D.2    Parodo, J.3    Phillips, M.J.4    Kapus, A.5
  • 40
    • 0033525861 scopus 로고    scopus 로고
    • Regulatory sequences of the mouse villin gene that efficiently drive transgenic expression in immature and differentiated epithelial cells of small and large intestines
    • Pinto D, Robine S, Jaisser F, El Marjou FE, Louvard D (1999) Regulatory sequences of the mouse villin gene that efficiently drive transgenic expression in immature and differentiated epithelial cells of small and large intestines. J Biol Chem 274: 6476-6482.
    • (1999) J Biol Chem , vol.274 , pp. 6476-6482
    • Pinto, D.1    Robine, S.2    Jaisser, F.3    El Marjou, F.E.4    Louvard, D.5
  • 41
    • 0028861099 scopus 로고
    • Cloning and characterization of seven cDNAs for hyperosmolarity-responsive (HOR) genes of Saccharomyces cerevisiae
    • Hirayama T, Maeda T, Saito H, Shinozaki K (1995) Cloning and characterization of seven cDNAs for hyperosmolarity-responsive (HOR) genes of Saccharomyces cerevisiae. Mol Gen Genet 249: 127-138.
    • (1995) Mol Gen Genet , vol.249 , pp. 127-138
    • Hirayama, T.1    Maeda, T.2    Saito, H.3    Shinozaki, K.4
  • 42
    • 0942287240 scopus 로고    scopus 로고
    • Osmoregulation of taurine transporter function and expression in retinal pigment epithelial, ganglion, and muller cells
    • El-Sherbeny A, Naggar H, Miyauchi S, Ola MS, Maddox DM, et al. (2004) Osmoregulation of taurine transporter function and expression in retinal pigment epithelial, ganglion, and muller cells. Invest Ophthalmol Vis Sci 45: 694-701.
    • (2004) Invest Ophthalmol Vis Sci , vol.45 , pp. 694-701
    • El-Sherbeny, A.1    Naggar, H.2    Miyauchi, S.3    Ola, M.S.4    Maddox, D.M.5
  • 44
    • 0023007801 scopus 로고
    • Purification and biochemical characterization of the promoter-specific transcription factor, Sp1
    • Briggs MR, Kadonaga JT, Bell SP, Tjian R (1986) Purification and biochemical characterization of the promoter-specific transcription factor, Sp1. Science 234: 47-52.
    • (1986) Science , vol.234 , pp. 47-52
    • Briggs, M.R.1    Kadonaga, J.T.2    Bell, S.P.3    Tjian, R.4
  • 46
    • 0022541602 scopus 로고
    • Activation of the AIDS retrovirus promoter by the cellular transcription factor, Sp1
    • Jones KA, Kadonaga JT, Luciw PA, Tjian R (1986) Activation of the AIDS retrovirus promoter by the cellular transcription factor, Sp1. Science 232: 755-759.
    • (1986) Science , vol.232 , pp. 755-759
    • Jones, K.A.1    Kadonaga, J.T.2    Luciw, P.A.3    Tjian, R.4
  • 47
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-kappaB
    • Hayden MS, Ghosh S (2004) Signaling to NF-kappaB. Genes Dev 18: 2195-2224.
    • (2004) Genes Dev , vol.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 48
    • 33645312379 scopus 로고    scopus 로고
    • Circuitry of nuclear factor kappaB signaling
    • Hoffmann A, Baltimore D (2006) Circuitry of nuclear factor kappaB signaling. Immunol Rev 210: 171-186.
    • (2006) Immunol Rev , vol.210 , pp. 171-186
    • Hoffmann, A.1    Baltimore, D.2
  • 49
    • 0027384590 scopus 로고
    • NF-kappa B subunit-specific regulation of the interleukin-8 promoter
    • Kunsch C, Rosen CA (1993) NF-kappa B subunit-specific regulation of the interleukin-8 promoter. Mol Cell Biol 13: 6137-6146.
    • (1993) Mol Cell Biol , vol.13 , pp. 6137-6146
    • Kunsch, C.1    Rosen, C.A.2
  • 50
    • 0031897632 scopus 로고    scopus 로고
    • NF-kappa B and Rel proteins: Evolutionarily conserved mediators of immune responses
    • Ghosh S, May MJ, Kopp EB (1998) NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses. Annu Rev Immunol 16: 225-260.
    • (1998) Annu Rev Immunol , vol.16 , pp. 225-260
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 51
    • 0035164415 scopus 로고    scopus 로고
    • Toll-like receptor-mediated NF-kappaB activation: A phylogenetically conserved paradigm in innate immunity
    • Zhang G, Ghosh S (2001) Toll-like receptor-mediated NF-kappaB activation: a phylogenetically conserved paradigm in innate immunity. J Clin Invest 107: 13-19.
    • (2001) J Clin Invest , vol.107 , pp. 13-19
    • Zhang, G.1    Ghosh, S.2
  • 52
    • 0028879819 scopus 로고
    • Role of transcriptional activation of I kappa B alpha in mediation of immunosuppression by glucocorticoids
    • Scheinman RI, Cogswell PC, Lofquist AK, Baldwin AS Jr (1995) Role of transcriptional activation of I kappa B alpha in mediation of immunosuppression by glucocorticoids. Science 270: 283-286.
    • (1995) Science , vol.270 , pp. 283-286
    • Scheinman, R.I.1    Cogswell, P.C.2    Lofquist, A.K.3    Baldwin Jr, A.S.4
  • 53
    • 33845306274 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of IkappaBalpha and processing of p105 in Crohn disease and ulcerative colitis
    • Visekruna A, Joeris T, Seidel D, Kroesen A, Loddenkemper C, et al. (2006) Proteasome-mediated degradation of IkappaBalpha and processing of p105 in Crohn disease and ulcerative colitis. J Clin Invest 116: 3195-3203.
    • (2006) J Clin Invest , vol.116 , pp. 3195-3203
    • Visekruna, A.1    Joeris, T.2    Seidel, D.3    Kroesen, A.4    Loddenkemper, C.5
  • 54
    • 0027209915 scopus 로고
    • A cooperative interaction between NF-kappa B and Sp1 is required for HIV-1 enhancer activation
    • Perkins ND, Edwards NL, Duckett CS, Agranoff AB, Schmid RM, et al. (1993) A cooperative interaction between NF-kappa B and Sp1 is required for HIV-1 enhancer activation. Embo J 12: 3551-3558.
    • (1993) Embo J , vol.12 , pp. 3551-3558
    • Perkins, N.D.1    Edwards, N.L.2    Duckett, C.S.3    Agranoff, A.B.4    Schmid, R.M.5
  • 55
    • 0035929642 scopus 로고    scopus 로고
    • The hepatitis B virus X protein induces HIV-1 replication and transcription in synergy with T-cell activation signals: Functional roles of NF-kappaB/NF-AT and SP1-binding sites in the HIV-1 long terminal repeat promoter
    • Gomez-Gonzalo M, Carretero M, Rullas J, Lara-Pezzi E, Aramburu J, et al. (2001) The hepatitis B virus X protein induces HIV-1 replication and transcription in synergy with T-cell activation signals: functional roles of NF-kappaB/NF-AT and SP1-binding sites in the HIV-1 long terminal repeat promoter. J Biol Chem 276: 35435-35443.
    • (2001) J Biol Chem , vol.276 , pp. 35435-35443
    • Gomez-Gonzalo, M.1    Carretero, M.2    Rullas, J.3    Lara-Pezzi, E.4    Aramburu, J.5
  • 56
  • 57
    • 0027454228 scopus 로고
    • Association between proto-oncoprotein Rel and TATA-binding protein mediates transcriptional activation by NF-kappa B
    • Kerr LD, Ransone LJ, Wamsley P, Schmitt MJ, Boyer TG, et al. (1993) Association between proto-oncoprotein Rel and TATA-binding protein mediates transcriptional activation by NF-kappa B. Nature 365: 412-419.
    • (1993) Nature , vol.365 , pp. 412-419
    • Kerr, L.D.1    Ransone, L.J.2    Wamsley, P.3    Schmitt, M.J.4    Boyer, T.G.5
  • 58
    • 0027454545 scopus 로고
    • Differential regulation of vascular cell adhesion molecule 1 gene expression by specific NF-kappa B subunits in endothelial and epithelial cells
    • Shu HB, Agranoff AB, Nabel EG, Leung K, Duckett CS, et al. (1993) Differential regulation of vascular cell adhesion molecule 1 gene expression by specific NF-kappa B subunits in endothelial and epithelial cells. Mol Cell Biol 13: 6283-6289.
    • (1993) Mol Cell Biol , vol.13 , pp. 6283-6289
    • Shu, H.B.1    Agranoff, A.B.2    Nabel, E.G.3    Leung, K.4    Duckett, C.S.5
  • 59
    • 0028961951 scopus 로고
    • Endothelial interferon regulatory factor 1 cooperates with NF-kappa B as a transcriptional activator of vascular cell adhesion molecule 1
    • Neish AS, Read MA, Thanos D, Pine R, Maniatis T, et al. (1995) Endothelial interferon regulatory factor 1 cooperates with NF-kappa B as a transcriptional activator of vascular cell adhesion molecule 1. Mol Cell Biol 15: 2558-2569.
    • (1995) Mol Cell Biol , vol.15 , pp. 2558-2569
    • Neish, A.S.1    Read, M.A.2    Thanos, D.3    Pine, R.4    Maniatis, T.5
  • 60
    • 0028865771 scopus 로고
    • Triggering of the human interleukin-6 gene by interferon-gamma and tumor necrosis factor-alpha in monocytic cells involves cooperation between interferon regulatory factor-1, NF kappa B, and Sp1 transcription factors
    • Sanceau J, Kaisho T, Hirano T, Wietzerbin J (1995) Triggering of the human interleukin-6 gene by interferon-gamma and tumor necrosis factor-alpha in monocytic cells involves cooperation between interferon regulatory factor-1, NF kappa B, and Sp1 transcription factors. J Biol Chem 270: 27920-27931.
    • (1995) J Biol Chem , vol.270 , pp. 27920-27931
    • Sanceau, J.1    Kaisho, T.2    Hirano, T.3    Wietzerbin, J.4
  • 61
    • 0031935038 scopus 로고    scopus 로고
    • Functional interference of Sp1 and NF-kappaB through the same DNA binding site
    • Hirano F, Tanaka H, Hirano Y, Hiramoto M, Handa H, et al. (1998) Functional interference of Sp1 and NF-kappaB through the same DNA binding site. Mol Cell Biol 18: 1266-1274.
    • (1998) Mol Cell Biol , vol.18 , pp. 1266-1274
    • Hirano, F.1    Tanaka, H.2    Hirano, Y.3    Hiramoto, M.4    Handa, H.5
  • 62
    • 20244375068 scopus 로고    scopus 로고
    • Inhibition of interferon-gamma expression by osmotic shrinkage of peripheral blood lymphocytes
    • Lang KS, Weigert C, Braedel S, Fillon S, Palmada M, et al. (2003) Inhibition of interferon-gamma expression by osmotic shrinkage of peripheral blood lymphocytes. Am J Physiol Cell Physiol 284: C200-208.
    • (2003) Am J Physiol Cell Physiol , vol.284
    • Lang, K.S.1    Weigert, C.2    Braedel, S.3    Fillon, S.4    Palmada, M.5
  • 63
    • 0033783525 scopus 로고    scopus 로고
    • Dehydration activates an NF-kappaB-driven, COX2-dependent survival mechanism in renal medullary interstitial cells
    • Hao CM, Yull F, Blackwell T, Komhoff M, Davis LS, et al. (2000) Dehydration activates an NF-kappaB-driven, COX2-dependent survival mechanism in renal medullary interstitial cells. J Clin Invest 106: 973-982.
    • (2000) J Clin Invest , vol.106 , pp. 973-982
    • Hao, C.M.1    Yull, F.2    Blackwell, T.3    Komhoff, M.4    Davis, L.S.5
  • 64
    • 0028867899 scopus 로고
    • Immunosuppression by glucocorticoids: Inhibition of NF-kappa B activity through induction of I kappa B synthesis
    • Auphan N, DiDonato JA, Rosette C, Helmberg A, Karin M (1995) Immunosuppression by glucocorticoids: inhibition of NF-kappa B activity through induction of I kappa B synthesis. Science 270: 286-290.
    • (1995) Science , vol.270 , pp. 286-290
    • Auphan, N.1    DiDonato, J.A.2    Rosette, C.3    Helmberg, A.4    Karin, M.5
  • 65
    • 0024475227 scopus 로고
    • NF-kappa B: A pleiotropic mediator of inducible and tissue-specific gene control
    • Lenardo MJ, Baltimore D (1989) NF-kappa B: a pleiotropic mediator of inducible and tissue-specific gene control. Cell 58: 227-229.
    • (1989) Cell , vol.58 , pp. 227-229
    • Lenardo, M.J.1    Baltimore, D.2
  • 66
    • 0024516201 scopus 로고
    • The involvement of NF-kappa B in beta-interferon gene regulation reveals its role as widely inducible mediator of signal transduction
    • Lenardo MJ, Fan CM, Maniatis T, Baltimore D (1989) The involvement of NF-kappa B in beta-interferon gene regulation reveals its role as widely inducible mediator of signal transduction. Cell 57: 287-294.
    • (1989) Cell , vol.57 , pp. 287-294
    • Lenardo, M.J.1    Fan, C.M.2    Maniatis, T.3    Baltimore, D.4
  • 67
    • 0028167846 scopus 로고
    • Inhibition of NF-kappa B by sodium salicylate and aspirin
    • Kopp E, Ghosh S (1994) Inhibition of NF-kappa B by sodium salicylate and aspirin. Science 265: 956-959.
    • (1994) Science , vol.265 , pp. 956-959
    • Kopp, E.1    Ghosh, S.2
  • 68
    • 0030698128 scopus 로고    scopus 로고
    • Post-transcriptional regulation contributes to Drosophila clock gene mRNA cycling
    • So WV, Rosbash M (1997) Post-transcriptional regulation contributes to Drosophila clock gene mRNA cycling. Embo J 16: 7146-7155.
    • (1997) Embo J , vol.16 , pp. 7146-7155
    • So, W.V.1    Rosbash, M.2
  • 69
    • 0033111732 scopus 로고    scopus 로고
    • Both Erk and p38 kinases are necessary for cytokine gene transcription
    • Carter AB, Monick MM, Hunninghake GW (1999) Both Erk and p38 kinases are necessary for cytokine gene transcription. Am J Respir Cell Mol Biol 20: 751-758.
    • (1999) Am J Respir Cell Mol Biol , vol.20 , pp. 751-758
    • Carter, A.B.1    Monick, M.M.2    Hunninghake, G.W.3
  • 70
    • 0023928976 scopus 로고
    • Osmoregulation by slow changes in aldose reductase and rapid changes in sorbitol flux
    • Bagnasco SM, Murphy HR, Bedford JJ, Burg MB (1988) Osmoregulation by slow changes in aldose reductase and rapid changes in sorbitol flux. Am J Physiol 254: C788-792.
    • (1988) Am J Physiol , vol.254
    • Bagnasco, S.M.1    Murphy, H.R.2    Bedford, J.J.3    Burg, M.B.4
  • 71
    • 0024433666 scopus 로고
    • Osmotic regulation of aldose reductase protein synthesis in renal medullary cells
    • Moriyama T, Garcia-Perez A, Burg MB (1989) Osmotic regulation of aldose reductase protein synthesis in renal medullary cells. J Biol Chem 264: 16810-16814.
    • (1989) J Biol Chem , vol.264 , pp. 16810-16814
    • Moriyama, T.1    Garcia-Perez, A.2    Burg, M.B.3
  • 72
    • 27944470863 scopus 로고    scopus 로고
    • Luminal hyperosmolarity decreases Na transport and impairs barrier function of sheep rumen epithelium
    • Schweigel M, Freyer M, Leclercq S, Etschmann B, Lodemann U, et al. (2005) Luminal hyperosmolarity decreases Na transport and impairs barrier function of sheep rumen epithelium. J Comp Physiol [B] 175: 575-591.
    • (2005) J Comp Physiol , vol.175 , Issue.B , pp. 575-591
    • Schweigel, M.1    Freyer, M.2    Leclercq, S.3    Etschmann, B.4    Lodemann, U.5
  • 74
    • 0027936755 scopus 로고
    • A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells
    • Han J, Lee JD, Bibbs L, Ulevitch RJ (1994) A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science 265: 808-811.
    • (1994) Science , vol.265 , pp. 808-811
    • Han, J.1    Lee, J.D.2    Bibbs, L.3    Ulevitch, R.J.4
  • 75
    • 34247591361 scopus 로고    scopus 로고
    • Hyperosmolarity-induced apoptosis in human corneal epithelial cells is mediated by cytochrome c and MAPK pathways
    • Luo L, Li DQ, Pflugfelder SC (2007) Hyperosmolarity-induced apoptosis in human corneal epithelial cells is mediated by cytochrome c and MAPK pathways. Cornea 26: 452-460.
    • (2007) Cornea , vol.26 , pp. 452-460
    • Luo, L.1    Li, D.Q.2    Pflugfelder, S.C.3
  • 76
    • 0345447585 scopus 로고    scopus 로고
    • Proinflammatory cytokines disrupt epithelial barrier function by apoptosis-independent mechanisms
    • Bruewer M, Luegering A, Kucharzik T, Parkos CA, Madara JL, et al. (2003) Proinflammatory cytokines disrupt epithelial barrier function by apoptosis-independent mechanisms. J Immunol 171: 6164-6172.
    • (2003) J Immunol , vol.171 , pp. 6164-6172
    • Bruewer, M.1    Luegering, A.2    Kucharzik, T.3    Parkos, C.A.4    Madara, J.L.5
  • 77
    • 0030739208 scopus 로고    scopus 로고
    • Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis
    • Mosser DD, Caron AW, Bourget L, Denis-Larose C, Massie B (1997) Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis. Mol Cell Biol 17: 5317-5327.
    • (1997) Mol Cell Biol , vol.17 , pp. 5317-5327
    • Mosser, D.D.1    Caron, A.W.2    Bourget, L.3    Denis-Larose, C.4    Massie, B.5
  • 78
    • 0032483967 scopus 로고    scopus 로고
    • Role of MEKK1 in cell survival and activation of JNK and ERK pathways defined by targeted gene disruption
    • Yujiri T, Sather S, Fanger GR, Johnson GL (1998) Role of MEKK1 in cell survival and activation of JNK and ERK pathways defined by targeted gene disruption. Science 282: 1911-1914.
    • (1998) Science , vol.282 , pp. 1911-1914
    • Yujiri, T.1    Sather, S.2    Fanger, G.R.3    Johnson, G.L.4
  • 79
    • 0033972143 scopus 로고    scopus 로고
    • Mitogen-activated protein phosphorylation in endothelial cells exposed to hyperosmolar conditions
    • Duzgun SA, Rasque H, Kito H, Azuma N, Li W, et al. (2000) Mitogen-activated protein phosphorylation in endothelial cells exposed to hyperosmolar conditions. J Cell Biochem 76: 567-571.
    • (2000) J Cell Biochem , vol.76 , pp. 567-571
    • Duzgun, S.A.1    Rasque, H.2    Kito, H.3    Azuma, N.4    Li, W.5
  • 80
    • 0141866849 scopus 로고    scopus 로고
    • Aldose reductase induced by hyperosmotic stress mediates cardiomyocyte apoptosis: Differential effects of sorbitol and mannitol
    • Galvez AS, Ulloa JA, Chiong M, Criollo A, Eisner V, et al. (2003) Aldose reductase induced by hyperosmotic stress mediates cardiomyocyte apoptosis: differential effects of sorbitol and mannitol. J Biol Chem 278: 38484-38494.
    • (2003) J Biol Chem , vol.278 , pp. 38484-38494
    • Galvez, A.S.1    Ulloa, J.A.2    Chiong, M.3    Criollo, A.4    Eisner, V.5
  • 81
    • 28244493047 scopus 로고    scopus 로고
    • Transforming growth factor-beta regulation of epithelial tight junction proteins enhances barrier function and blocks enterohemorrhagic Escherichia coli O157:H7-induced increased permeability
    • Howe KL, Reardon C, Wang A, Nazli A, McKay DM (2005) Transforming growth factor-beta regulation of epithelial tight junction proteins enhances barrier function and blocks enterohemorrhagic Escherichia coli O157:H7-induced increased permeability. Am J Pathol 167: 1587-1597.
    • (2005) Am J Pathol , vol.167 , pp. 1587-1597
    • Howe, K.L.1    Reardon, C.2    Wang, A.3    Nazli, A.4    McKay, D.M.5
  • 82
    • 0034807581 scopus 로고    scopus 로고
    • Cytoskeletal regulation of pulmonary vascular permeability
    • Dudek SM, Garcia JG (2001) Cytoskeletal regulation of pulmonary vascular permeability. J Appl Physiol 91: 1487-1500.
    • (2001) J Appl Physiol , vol.91 , pp. 1487-1500
    • Dudek, S.M.1    Garcia, J.G.2
  • 83
    • 0020379140 scopus 로고
    • Role of endothelial cell cytoskeleton in control of endothelial permeability
    • Shasby DM, Shasby SS, Sullivan JM, Peach MJ (1982) Role of endothelial cell cytoskeleton in control of endothelial permeability. Circ Res 51: 657-661.
    • (1982) Circ Res , vol.51 , pp. 657-661
    • Shasby, D.M.1    Shasby, S.S.2    Sullivan, J.M.3    Peach, M.J.4
  • 84
    • 0038340589 scopus 로고    scopus 로고
    • Contribution of F-actin to barrier properties of the blood-joint pathway
    • Poli A, Coleman PJ, Mason RM, Levick JR (2002) Contribution of F-actin to barrier properties of the blood-joint pathway. Microcirculation 9: 419-430.
    • (2002) Microcirculation , vol.9 , pp. 419-430
    • Poli, A.1    Coleman, P.J.2    Mason, R.M.3    Levick, J.R.4
  • 85
    • 36048961354 scopus 로고    scopus 로고
    • Edaravone mimics sphingosine-1-phosphate-induced endothelial barrier enhancement in human microvascular endothelial cells
    • Omori K, Shikata Y, Sarai K, Watanabe N, Wada J, et al. (2007) Edaravone mimics sphingosine-1-phosphate-induced endothelial barrier enhancement in human microvascular endothelial cells. Am J Physiol Cell Physiol 293: C1523-1531.
    • (2007) Am J Physiol Cell Physiol , vol.293
    • Omori, K.1    Shikata, Y.2    Sarai, K.3    Watanabe, N.4    Wada, J.5
  • 86
    • 34447294255 scopus 로고    scopus 로고
    • Focal adhesion kinase controls pH-dependent epidermal barrier homeostasis by regulating actin-directed Na+/H+ exchanger 1 plasma membrane localization
    • Ilic D, Mao-Qiang M, Crumrine D, Dolganov G, Larocque N, et al. (2007) Focal adhesion kinase controls pH-dependent epidermal barrier homeostasis by regulating actin-directed Na+/H+ exchanger 1 plasma membrane localization. Am J Pathol 170: 2055-2067.
    • (2007) Am J Pathol , vol.170 , pp. 2055-2067
    • Ilic, D.1    Mao-Qiang, M.2    Crumrine, D.3    Dolganov, G.4    Larocque, N.5
  • 87
    • 34247621784 scopus 로고    scopus 로고
    • Molecular pathogenesis of inflammatory bowel disease: Genotypes, phenotypes and personalized medicine
    • Goyette P, Labbe C, Trinh TT, Xavier RJ, Rioux JD (2007) Molecular pathogenesis of inflammatory bowel disease: genotypes, phenotypes and personalized medicine. Ann Med 39: 177-199.
    • (2007) Ann Med , vol.39 , pp. 177-199
    • Goyette, P.1    Labbe, C.2    Trinh, T.T.3    Xavier, R.J.4    Rioux, J.D.5
  • 88
    • 4844229767 scopus 로고    scopus 로고
    • Review article: The aetiopathogenesis of inflammatory bowel disease-immunology and repair mechanisms
    • Dignass AU, Baumgart DC, Sturm A (2004) Review article: the aetiopathogenesis of inflammatory bowel disease-immunology and repair mechanisms. Aliment Pharmacol Ther 20 Suppl 4: 9-17.
    • (2004) Aliment Pharmacol Ther , vol.20 , Issue.SUPPL. 4 , pp. 9-17
    • Dignass, A.U.1    Baumgart, D.C.2    Sturm, A.3
  • 89
    • 2142813761 scopus 로고    scopus 로고
    • A porous defense: The leaky epithelial barrier in intestinal disease
    • Clayburgh DR, Shen L, Turner JR (2004) A porous defense: the leaky epithelial barrier in intestinal disease. Lab Invest 84: 282-291.
    • (2004) Lab Invest , vol.84 , pp. 282-291
    • Clayburgh, D.R.1    Shen, L.2    Turner, J.R.3
  • 90
    • 0032193226 scopus 로고    scopus 로고
    • p38 MAPK is required for CD40-induced gene expression and proliferation in B lymphocytes
    • Craxton A, Shu G, Graves JD, Saklatvala J, Krebs EG, et al. (1998) p38 MAPK is required for CD40-induced gene expression and proliferation in B lymphocytes. J Immunol 161: 3225-3236.
    • (1998) J Immunol , vol.161 , pp. 3225-3236
    • Craxton, A.1    Shu, G.2    Graves, J.D.3    Saklatvala, J.4    Krebs, E.G.5
  • 91
    • 9444228220 scopus 로고    scopus 로고
    • Inhibition of p38 MAP kinase- and RICK/NF-kappaB-signaling suppresses inflammatory bowel disease
    • Hollenbach E, Neumann M, Vieth M, Roessner A, Malfertheiner P, et al. (2004) Inhibition of p38 MAP kinase- and RICK/NF-kappaB-signaling suppresses inflammatory bowel disease. Faseb J 18: 1550-1552.
    • (2004) Faseb J , vol.18 , pp. 1550-1552
    • Hollenbach, E.1    Neumann, M.2    Vieth, M.3    Roessner, A.4    Malfertheiner, P.5
  • 92
    • 0027196277 scopus 로고
    • Mechanism of initiator-mediated transcription: Evidence for a functional interaction between the TATA-binding protein and DNA in the absence of a specific recognition sequence
    • Zenzie-Gregory B, Khachi A, Garraway IP, Smale ST (1993) Mechanism of initiator-mediated transcription: evidence for a functional interaction between the TATA-binding protein and DNA in the absence of a specific recognition sequence. Mol Cell Biol 13: 3841-3849.
    • (1993) Mol Cell Biol , vol.13 , pp. 3841-3849
    • Zenzie-Gregory, B.1    Khachi, A.2    Garraway, I.P.3    Smale, S.T.4
  • 93
    • 0028286781 scopus 로고
    • Sp1 is a critical factor for the monocytic specific expression of human CD14
    • Zhang DE, Hetherington CJ, Tan S, Dziennis SE, Gonzalez DA, et al. (1994) Sp1 is a critical factor for the monocytic specific expression of human CD14. J Biol Chem 269: 11425-11434.
    • (1994) J Biol Chem , vol.269 , pp. 11425-11434
    • Zhang, D.E.1    Hetherington, C.J.2    Tan, S.3    Dziennis, S.E.4    Gonzalez, D.A.5
  • 95
    • 0018909468 scopus 로고
    • Ribonucleic acid synthesis in embryonic chick muscle, rates of synthesis and half-lives of transfer and ribosomal RNA species
    • Nwagwu M, Nana M (1980) Ribonucleic acid synthesis in embryonic chick muscle, rates of synthesis and half-lives of transfer and ribosomal RNA species. J Embryol Exp Morphol 56: 253-267.
    • (1980) J Embryol Exp Morphol , vol.56 , pp. 253-267
    • Nwagwu, M.1    Nana, M.2
  • 96
    • 0035821249 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1-dependent induction of intestinal trefoil factor protects barrier function during hypoxia
    • Furuta GT, Turner JR, Taylor CT, Hershberg RM, Comerford K, et al. (2001) Hypoxia-inducible factor 1-dependent induction of intestinal trefoil factor protects barrier function during hypoxia. J Exp Med 193: 1027-1034.
    • (2001) J Exp Med , vol.193 , pp. 1027-1034
    • Furuta, G.T.1    Turner, J.R.2    Taylor, C.T.3    Hershberg, R.M.4    Comerford, K.5
  • 97
    • 33748477283 scopus 로고    scopus 로고
    • Selective ablation of matrix metalloproteinase-2 exacerbates experimental colitis: Contrasting role of gelatinases in the pathogenesis of colitis
    • Garg P, Rojas M, Ravi A, Bockbrader K, Epstein S, et al. (2006) Selective ablation of matrix metalloproteinase-2 exacerbates experimental colitis: contrasting role of gelatinases in the pathogenesis of colitis. J Immunol 177: 4103-4112.
    • (2006) J Immunol , vol.177 , pp. 4103-4112
    • Garg, P.1    Rojas, M.2    Ravi, A.3    Bockbrader, K.4    Epstein, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.