메뉴 건너뛰기




Volumn 212, Issue 3, 2009, Pages 329-340

Signaling to the apical membrane and to the paracellular pathway: Changes in the cytosolic proteome of Aedes Malpighian tubules

Author keywords

Actin; Adducin; Annexin; Ca2+; cAMP; Endoplasmin; PKA; PKC; V type H+ ATPase

Indexed keywords

KININ; PROTEIN;

EID: 59149096813     PISSN: 00220949     EISSN: None     Source Type: Journal    
DOI: 10.1242/jeb.024646     Document Type: Article
Times cited : (21)

References (67)
  • 1
    • 0028799226 scopus 로고
    • Tight junctions and the molecular basis for regulation of paracellular permeability
    • Anderson, J. M. and Van Itallie, C. M. (1995). Tight junctions and the molecular basis for regulation of paracellular permeability. Am. J. Physiol. 269, G467-G475.
    • (1995) Am. J. Physiol , vol.269
    • Anderson, J.M.1    Van Itallie, C.M.2
  • 2
    • 0141920729 scopus 로고    scopus 로고
    • The claudin-like megatrachea is essential in septate junctions for the epithelial barrier function in Drosophila
    • Behr, M., Riedel, D. and Schuh, R. (2003). The claudin-like megatrachea is essential in septate junctions for the epithelial barrier function in Drosophila. Dev. Cell 5, 611-620.
    • (2003) Dev. Cell , vol.5 , pp. 611-620
    • Behr, M.1    Riedel, D.2    Schuh, R.3
  • 4
    • 0028916254 scopus 로고
    • Cactus protein degradation mediates Drosophila dorsal-ventral signaling
    • Belvin, M. P., Jin, Y. and Anderson, K. V. (1995). Cactus protein degradation mediates Drosophila dorsal-ventral signaling. Genes Dev. 9, 783-793.
    • (1995) Genes Dev , vol.9 , pp. 783-793
    • Belvin, M.P.1    Jin, Y.2    Anderson, K.V.3
  • 6
    • 0041831243 scopus 로고    scopus 로고
    • Regulation of tight junction permeability with switch-like speed
    • Beyenbach, K. W. (2003). Regulation of tight junction permeability with switch-like speed. Curr. Opin. Nephrol. Hypertens. 12, 543-550.
    • (2003) Curr. Opin. Nephrol. Hypertens , vol.12 , pp. 543-550
    • Beyenbach, K.W.1
  • 7
    • 0034041747 scopus 로고    scopus 로고
    • +-ATPase in electrogenesis and epithelial transport in Malpighian tubules
    • +-ATPase in electrogenesis and epithelial transport in Malpighian tubules. J. Exp. Biol. 203, 1459-1468.
    • (2000) J. Exp. Biol , vol.203 , pp. 1459-1468
    • Beyenbach, K.W.1    Pannabecker, T.L.2    Nagel, W.3
  • 8
    • 0344196934 scopus 로고    scopus 로고
    • Effects of putative diuretic factors on intracellular secondary messenger levels in the Malpighian tubules of Aedes aegypti
    • Cady, C. and Hagedorn, H. H. (1999). Effects of putative diuretic factors on intracellular secondary messenger levels in the Malpighian tubules of Aedes aegypti. J. Insect Physiol. 45, 327-337.
    • (1999) J. Insect Physiol , vol.45 , pp. 327-337
    • Cady, C.1    Hagedorn, H.H.2
  • 10
    • 0032101866 scopus 로고    scopus 로고
    • The concentration-dependence of CRF-like diuretic peptide: Mechanisms of action
    • Clark, T. M., Hayes, T. K., Holman, G. M. and Beyenbach, K. W. (1998). The concentration-dependence of CRF-like diuretic peptide: mechanisms of action. J. Exp. Biol. 201, 1753-1762.
    • (1998) J. Exp. Biol , vol.201 , pp. 1753-1762
    • Clark, T.M.1    Hayes, T.K.2    Holman, G.M.3    Beyenbach, K.W.4
  • 11
    • 0029010942 scopus 로고
    • Synergism between diuretic peptides controlling ion and fluid transport in insect malpighian tubules
    • Coast, G. M. (1995). Synergism between diuretic peptides controlling ion and fluid transport in insect malpighian tubules. Regul. Pept. 57, 283-296.
    • (1995) Regul. Pept , vol.57 , pp. 283-296
    • Coast, G.M.1
  • 12
    • 25844477132 scopus 로고    scopus 로고
    • Mosquito natriuretic peptide identified as a calcitonin-like diuretic hormone in Anopheles gambiae (Giles)
    • Coast, G. M., Garside, C. S., Webster, S. G., Schegg, K. M. and Schooley, D. A. (2005). Mosquito natriuretic peptide identified as a calcitonin-like diuretic hormone in Anopheles gambiae (Giles). J. Exp. Biol. 208, 3281-3291.
    • (2005) J. Exp. Biol , vol.208 , pp. 3281-3291
    • Coast, G.M.1    Garside, C.S.2    Webster, S.G.3    Schegg, K.M.4    Schooley, D.A.5
  • 14
    • 0033562951 scopus 로고    scopus 로고
    • Ligand-specific, transient interaction between integrins and calreticulin during cell adhesion to extracellular matrix proteins is dependent upon phosphorylation/ dephosphorylation events
    • Coppolino, M. G. and Dedhar, S. (1999). Ligand-specific, transient interaction between integrins and calreticulin during cell adhesion to extracellular matrix proteins is dependent upon phosphorylation/ dephosphorylation events. Biochem. J. 340, 41-50.
    • (1999) Biochem. J , vol.340 , pp. 41-50
    • Coppolino, M.G.1    Dedhar, S.2
  • 15
    • 0030978516 scopus 로고    scopus 로고
    • Calreticulin is essential for integrin-mediated calcium signalling and cell adhesion
    • Coppolino, M. G., Woodside, M. J., Demaurex, N., Grinstein, S., St-Arnaud, R. and Dedhar, S. (1997). Calreticulin is essential for integrin-mediated calcium signalling and cell adhesion. Nature 386, 843-847.
    • (1997) Nature , vol.386 , pp. 843-847
    • Coppolino, M.G.1    Woodside, M.J.2    Demaurex, N.3    Grinstein, S.4    St-Arnaud, R.5    Dedhar, S.6
  • 17
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies, S. P., Reddy, H., Caivano, M. and Cohen, P. (2000). Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351, 95-105.
    • (2000) Biochem. J , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 19
    • 0032577975 scopus 로고    scopus 로고
    • Claudin-1 and -2: Novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin
    • Furuse, M., Fujita, K., Hiiragi, T., Fujimoto, K. and Tsukita, S. (1998). Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin. J. Cell Biol. 141, 1539-1550.
    • (1998) J. Cell Biol , vol.141 , pp. 1539-1550
    • Furuse, M.1    Fujita, K.2    Hiiragi, T.3    Fujimoto, K.4    Tsukita, S.5
  • 20
    • 0023245565 scopus 로고
    • Modulation of spectrin-actin assembly by erythrocyte adducin
    • Gardner, K. and Bennett, V. (1987). Modulation of spectrin-actin assembly by erythrocyte adducin. Nature 328, 359-362.
    • (1987) Nature , vol.328 , pp. 359-362
    • Gardner, K.1    Bennett, V.2
  • 23
    • 0023612830 scopus 로고
    • Isolation, primary structure and synthesis of leucokinin-VII and VIII: The final members of the new family of cephalomyotropic peptides isolated from head extracts of Leucophaea maderae
    • Holman, G. M., Cook, B. J. and Nachman, R. J. (1987). Isolation, primary structure and synthesis of leucokinin-VII and VIII: the final members of the new family of cephalomyotropic peptides isolated from head extracts of Leucophaea maderae. Comp. Biochem. Physiol. 88, 31-34.
    • (1987) Comp. Biochem. Physiol , vol.88 , pp. 31-34
    • Holman, G.M.1    Cook, B.J.2    Nachman, R.J.3
  • 24
    • 0034733784 scopus 로고    scopus 로고
    • Modulation of tight junction function by G protein-coupled events
    • Hopkins, A. M., Li, D., Mrsny, R. J., Walsh, S. V. and Nusrat, A. (2000). Modulation of tight junction function by G protein-coupled events. Adv. Drug Deliv. Rev. 41, 329-340.
    • (2000) Adv. Drug Deliv. Rev , vol.41 , pp. 329-340
    • Hopkins, A.M.1    Li, D.2    Mrsny, R.J.3    Walsh, S.V.4    Nusrat, A.5
  • 25
    • 0037442918 scopus 로고    scopus 로고
    • Constitutive activation of Rho proteins by CNF-1 influences tight junction structure and epithelial barrier function
    • Hopkins, A. M., Walsh, S. V., Verkade, P., Boquet, P. and Nusrat, A. (2003). Constitutive activation of Rho proteins by CNF-1 influences tight junction structure and epithelial barrier function. J. Cell Sci. 116, 725-742.
    • (2003) J. Cell Sci , vol.116 , pp. 725-742
    • Hopkins, A.M.1    Walsh, S.V.2    Verkade, P.3    Boquet, P.4    Nusrat, A.5
  • 26
    • 29144533473 scopus 로고    scopus 로고
    • Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells
    • Ikenouchi, J., Furuse, M., Furuse, K., Sasaki, H. and Tsukita, S. (2005). Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells. J. Cell Biol. 171, 939-945.
    • (2005) J. Cell Biol , vol.171 , pp. 939-945
    • Ikenouchi, J.1    Furuse, M.2    Furuse, K.3    Sasaki, H.4    Tsukita, S.5
  • 28
  • 30
    • 0029063512 scopus 로고
    • +-ATPase in vivo
    • +-ATPase in vivo. J. Biol. Chem. 270, 17025-17032.
    • (1995) J. Biol. Chem , vol.270 , pp. 17025-17032
    • Kane, P.M.1
  • 31
    • 0032489531 scopus 로고    scopus 로고
    • Regulation of the association of adducin with actin filaments by Rho-associated kinase (Rho-kinase) and myosin phosphatase
    • Kimura, K., Fukata, Y., Matsuoka, Y., Bennett, V., Matsuura, Y., Okawa, K., Iwamatsu, A. and Kaibuchi, K. (1998). Regulation of the association of adducin with actin filaments by Rho-associated kinase (Rho-kinase) and myosin phosphatase. J. Biol. Chem. 273, 5542-5548.
    • (1998) J. Biol. Chem , vol.273 , pp. 5542-5548
    • Kimura, K.1    Fukata, Y.2    Matsuoka, Y.3    Bennett, V.4    Matsuura, Y.5    Okawa, K.6    Iwamatsu, A.7    Kaibuchi, K.8
  • 32
    • 0032563088 scopus 로고    scopus 로고
    • Adducin preferentially recruits spectrin to the fast growing ends of actin filaments in a complex requiring the MARCKS-related domain and a newly defined oligomerization domain
    • Li, X., Matsuoka, Y. and Bennett, V. (1998). Adducin preferentially recruits spectrin to the fast growing ends of actin filaments in a complex requiring the MARCKS-related domain and a newly defined oligomerization domain. J. Biol. Chem. 273, 19329-19338.
    • (1998) J. Biol. Chem , vol.273 , pp. 19329-19338
    • Li, X.1    Matsuoka, Y.2    Bennett, V.3
  • 33
    • 0031943571 scopus 로고    scopus 로고
    • Regulation of the movement of solutes across tight junctions
    • Madara, J. L. (1998). Regulation of the movement of solutes across tight junctions. Annu. Rev. Physiol. 60, 143-159.
    • (1998) Annu. Rev. Physiol , vol.60 , pp. 143-159
    • Madara, J.L.1
  • 34
    • 0032572559 scopus 로고    scopus 로고
    • Adducin is an in vivo substrate for protein kinase C: Phosphorylation in the MARCKS-related domain inhibits activity in promoting spectrin-actin complexes and occurs in many cells, including dendritic spines of neurons
    • Matsuoka, Y., Li, X. and Bennett, V. (1998). Adducin is an in vivo substrate for protein kinase C: phosphorylation in the MARCKS-related domain inhibits activity in promoting spectrin-actin complexes and occurs in many cells, including dendritic spines of neurons. J. Cell Biol. 142, 485-497.
    • (1998) J. Cell Biol , vol.142 , pp. 485-497
    • Matsuoka, Y.1    Li, X.2    Bennett, V.3
  • 36
    • 0035142938 scopus 로고    scopus 로고
    • Chloride channels in apical membrane patches of stellate cells of Malpighian tubules of Aedes aegypti
    • O'Connor, K. R. and Beyenbach, K. W. (2001). Chloride channels in apical membrane patches of stellate cells of Malpighian tubules of Aedes aegypti. J. Exp. Biol. 204, 367-378.
    • (2001) J. Exp. Biol , vol.204 , pp. 367-378
    • O'Connor, K.R.1    Beyenbach, K.W.2
  • 37
    • 0033976470 scopus 로고    scopus 로고
    • Modes of control of insect Malpighian tubules: Synergism, antagonism, cooperation and autonomous regulation
    • O'Donnell, M. J. and Spring, J. H. (2000). Modes of control of insect Malpighian tubules: Synergism, antagonism, cooperation and autonomous regulation. J. Insect Physiol. 46, 107-117.
    • (2000) J. Insect Physiol , vol.46 , pp. 107-117
    • O'Donnell, M.J.1    Spring, J.H.2
  • 38
    • 0242505385 scopus 로고    scopus 로고
    • Separate control of anion and cation transport in Malpighian tubules of Drosophila melanogaster
    • O'Donnell, M. J., Dow, J. A., Huesmann, G. R., Tublitz, N. J. and Maddrell, S. H. (1996). Separate control of anion and cation transport in Malpighian tubules of Drosophila melanogaster. J. Exp. Biol. 199, 1163-1175.
    • (1996) J. Exp. Biol , vol.199 , pp. 1163-1175
    • O'Donnell, M.J.1    Dow, J.A.2    Huesmann, G.R.3    Tublitz, N.J.4    Maddrell, S.H.5
  • 40
    • 0027414892 scopus 로고
    • Regulation of epithelial shunt conductance by the peptide leucokinin
    • Pannabecker, T. L., Hayes, T. K. and Beyenbach, K. W. (1993). Regulation of epithelial shunt conductance by the peptide leucokinin. J. Membr. Biol. 132, 63-76.
    • (1993) J. Membr. Biol , vol.132 , pp. 63-76
    • Pannabecker, T.L.1    Hayes, T.K.2    Beyenbach, K.W.3
  • 41
    • 0040755075 scopus 로고
    • Active transport of potassium by the Malpighian tubules of insects
    • Ramsay, J. A. (1953). Active transport of potassium by the Malpighian tubules of insects. J. Exp. Biol. 93, 358-369.
    • (1953) J. Exp. Biol , vol.93 , pp. 358-369
    • Ramsay, J.A.1
  • 42
    • 38349084073 scopus 로고    scopus 로고
    • Hormone-induced assembly and activation of V-ATPase in blowfly salivary glands is mediated by protein kinase A
    • Rein, J., Voss Blenau, W., Walz, B. and Baumann, O. (2008). Hormone-induced assembly and activation of V-ATPase in blowfly salivary glands is mediated by protein kinase A. Am. J. Physiol. Cell Physiol. 294, C56-C65.
    • (2008) Am. J. Physiol. Cell Physiol , vol.294
    • Rein, J.1    Voss Blenau, W.2    Walz, B.3    Baumann, O.4
  • 43
    • 48049120845 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of annexin A2 regulates Rho-mediated actin rearrangement and cell adhesion
    • Rescher, U., Ludwig, C., Konietzko, V., Kharitonenkov, A. and Gerke, V. (2008). Tyrosine phosphorylation of annexin A2 regulates Rho-mediated actin rearrangement and cell adhesion. J. Cell Sci. 121, 2177-2185.
    • (2008) J. Cell Sci , vol.121 , pp. 2177-2185
    • Rescher, U.1    Ludwig, C.2    Konietzko, V.3    Kharitonenkov, A.4    Gerke, V.5
  • 46
    • 44149105668 scopus 로고    scopus 로고
    • The tight junction protein complex undergoes rapid and continuous molecular remodeling at steady state
    • Shen, L., Weber, C. R. and Turner, J. R. (2008). The tight junction protein complex undergoes rapid and continuous molecular remodeling at steady state. J. Cell Biol. 181, 683-695.
    • (2008) J. Cell Biol , vol.181 , pp. 683-695
    • Shen, L.1    Weber, C.R.2    Turner, J.R.3
  • 47
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O. and Mann, M. (1996). Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68, 850-858.
    • (1996) Anal. Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 48
    • 0028973059 scopus 로고
    • Regulation of IkB alpha phosphorylation by PKC- and Ca(2+)-dependent signal transduction pathways
    • Steffan, N. M., Bren, G. D., Frantz, B., Tocci, M. J., O'Neill, E. A. and Paya, C. V. (1995). Regulation of IkB alpha phosphorylation by PKC- and Ca(2+)-dependent signal transduction pathways. J. Immunol. 155, 4685-4691.
    • (1995) J. Immunol , vol.155 , pp. 4685-4691
    • Steffan, N.M.1    Bren, G.D.2    Frantz, B.3    Tocci, M.J.4    O'Neill, E.A.5    Paya, C.V.6
  • 49
    • 0344851707 scopus 로고    scopus 로고
    • Rab proteins and endocytic trafficking: Potential targets for therapeutic intervention
    • Stein, M. P., Dong, J. and Wandinger-Ness, A. (2003). Rab proteins and endocytic trafficking: potential targets for therapeutic intervention. Adv. Drug Deliv. Rev. 55, 1421-1437.
    • (2003) Adv. Drug Deliv. Rev , vol.55 , pp. 1421-1437
    • Stein, M.P.1    Dong, J.2    Wandinger-Ness, A.3
  • 50
    • 0028898233 scopus 로고
    • Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits
    • Sumner, J. P., Dow, J. A., Earley, F. G., Klein, U., Jäger, D. and Wieczorek, H. (1995). Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits. J. Biol. Chem. 270, 5649-5653.
    • (1995) J. Biol. Chem , vol.270 , pp. 5649-5653
    • Sumner, J.P.1    Dow, J.A.2    Earley, F.G.3    Klein, U.4    Jäger, D.5    Wieczorek, H.6
  • 53
    • 0030887904 scopus 로고    scopus 로고
    • A single cDNA encodes all three Aedes leucokinins, which stimulate both fluid secretion by the Malpighian tubules and hindgut contractions
    • Veenstra, J. A., Pattillo, J. M. and Petzel, D. H. (1997). A single cDNA encodes all three Aedes leucokinins, which stimulate both fluid secretion by the Malpighian tubules and hindgut contractions. J. Biol. Chem. 272, 10402-10407.
    • (1997) J. Biol. Chem , vol.272 , pp. 10402-10407
    • Veenstra, J.A.1    Pattillo, J.M.2    Petzel, D.H.3
  • 55
    • 12544249243 scopus 로고    scopus 로고
    • The V-ATPase subunit C binds to polymeric F-actin as well as monomeric G-actin and induces cross-linking of actin filaments
    • Vitavska, O., Merzendorfer, H. and Wieczorek, H. (2005). The V-ATPase subunit C binds to polymeric F-actin as well as monomeric G-actin and induces cross-linking of actin filaments. J. Biol. Chem. 280, 1070-1076.
    • (2005) J. Biol. Chem , vol.280 , pp. 1070-1076
    • Vitavska, O.1    Merzendorfer, H.2    Wieczorek, H.3
  • 58
    • 1642458089 scopus 로고    scopus 로고
    • Sinuous is a Drosophila claudin required for septate junction organization and epithelial tube size control
    • Wu, V. M., Schulte, J., Hirschi, A., Tepass, U. and Beitel, G. J. (2004). Sinuous is a Drosophila claudin required for septate junction organization and epithelial tube size control. J. Cell Biol. 164, 313-323.
    • (2004) J. Cell Biol , vol.164 , pp. 313-323
    • Wu, V.M.1    Schulte, J.2    Hirschi, A.3    Tepass, U.4    Beitel, G.J.5
  • 59
    • 19644384999 scopus 로고    scopus 로고
    • Role of regucalcin in maintaining cell homeostasis and function (review)
    • Yamaguchi, M. (2005). Role of regucalcin in maintaining cell homeostasis and function (review). Int. J. Mol. Med. 15, 371-389.
    • (2005) Int. J. Mol. Med , vol.15 , pp. 371-389
    • Yamaguchi, M.1
  • 60
    • 34447253828 scopus 로고    scopus 로고
    • Development of an integrated approach for evaluation of 2-D gel image analysis: Impact of multiple proteins in single spots on comparative proteomics in conventional 2-D gel/MALDI workflow
    • Yang, Y., Thannhauser, T. W., Li, L. and Zhang, S. (2007). Development of an integrated approach for evaluation of 2-D gel image analysis: impact of multiple proteins in single spots on comparative proteomics in conventional 2-D gel/MALDI workflow. Electrophoresis 28, 2080-2094.
    • (2007) Electrophoresis , vol.28 , pp. 2080-2094
    • Yang, Y.1    Thannhauser, T.W.2    Li, L.3    Zhang, S.4
  • 61
    • 0035132401 scopus 로고    scopus 로고
    • Leucokinin and the modulation of the shunt pathway in Malpighian tubules
    • Yu, M. and Beyenbach, K. W. (2001). Leucokinin and the modulation of the shunt pathway in Malpighian tubules. J. Insect Physiol. 47, 263-276.
    • (2001) J. Insect Physiol , vol.47 , pp. 263-276
    • Yu, M.1    Beyenbach, K.W.2
  • 62
    • 0036721079 scopus 로고    scopus 로고
    • 2+-dependent signal pathway in principal cells of Aedes aegypti Malpighian tubules
    • 2+-dependent signal pathway in principal cells of Aedes aegypti Malpighian tubules. Am. J. Physiol. 283, F499-F508.
    • (2002) Am. J. Physiol , vol.283
    • Yu, M.J.1    Beyenbach, K.W.2
  • 63
    • 0842269977 scopus 로고    scopus 로고
    • Effects of leucokinin-VIII on Aedes Malpighian tubule segments lacking stellate cells
    • Yu, M. J. and Beyenbach, K. W. (2004). Effects of leucokinin-VIII on Aedes Malpighian tubule segments lacking stellate cells. J. Exp. Biol. 207, 519-526.
    • (2004) J. Exp. Biol , vol.207 , pp. 519-526
    • Yu, M.J.1    Beyenbach, K.W.2
  • 64
    • 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., Joberty, G., Arpin, M., Fontaine, J. J., Hellio, R., Tavitian, A. and Louvard, D. (1994). 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) 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
  • 66
    • 0030991201 scopus 로고    scopus 로고
    • The transcriptional activity of NF-kappaB is regulated by the IkappaB-associated PKAc subunit through a cyclic AMP-independent mechanism
    • Zhong, H., SuYang, H., Erdjument-Bromage, H., Tempst, P. and Ghosh, S. (1997). The transcriptional activity of NF-kappaB is regulated by the IkappaB-associated PKAc subunit through a cyclic AMP-independent mechanism. Cell 89, 413-424.
    • (1997) Cell , vol.89 , pp. 413-424
    • Zhong, H.1    SuYang, H.2    Erdjument-Bromage, H.3    Tempst, P.4    Ghosh, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.