메뉴 건너뛰기




Volumn 103, Issue 5, 2004, Pages 1779-1786

Negative regulation of FcεRI-mediated mast cell activation by a ubiquitin-protein ligase Cbl-b

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CALCIUM ION; CYSTEINE; FC RECEPTOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN KINASE; LAT PROTEIN; LIPID; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOLIPASE C; PHOSPHOLIPASE C GAMMA; PROTEIN GAB2; PROTEIN KINASE LYN; PROTEIN KINASE SYK; STRESS ACTIVATED PROTEIN KINASE; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE CBL B; UNCLASSIFIED DRUG; BETA N ACETYLHEXOSAMINIDASE; CALCIUM; CARRIER PROTEIN; CBL PROTEIN; CBLB PROTEIN, HUMAN; CBLB PROTEIN, RAT; CHUK PROTEIN, HUMAN; ENZYME PRECURSOR; I KAPPA B KINASE; IKBKB PROTEIN, HUMAN; IKBKE PROTEIN, HUMAN; IMMUNOGLOBULIN E RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE 4; PHOSPHOPROTEIN; PROTEIN SERINE THREONINE KINASE; PROTEIN TYROSINE KINASE; RIBONUCLEASE; SIGNAL PEPTIDE; SIGNAL TRANSDUCING ADAPTOR PROTEIN; TYROSINE; UBIQUITIN;

EID: 1442308053     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2003-07-2260     Document Type: Article
Times cited : (71)

References (48)
  • 1
    • 0025951923 scopus 로고
    • Phosphorylation and dephosphorylation of the high-affinity receptor for immunoglobulin E immediately after receptor engagement and disengagement
    • Paolini R, Jouvin MH, Kinet JP. Phosphorylation and dephosphorylation of the high-affinity receptor for immunoglobulin E immediately after receptor engagement and disengagement. Nature. 1991;353:855-858.
    • (1991) Nature , vol.353 , pp. 855-858
    • Paolini, R.1    Jouvin, M.H.2    Kinet, J.P.3
  • 2
    • 0025946132 scopus 로고
    • Molecular cloning of a porcine gene syk that encodes a 72-kDa protein-tyrosine kinase showing high susceptibility to proteolysis
    • Taniguchi T, Kobayashi T, Kondo J, et al. Molecular cloning of a porcine gene syk that encodes a 72-kDa protein-tyrosine kinase showing high susceptibility to proteolysis. J Biol Chem. 1991;266:15790-15796.
    • (1991) J Biol Chem , vol.266 , pp. 15790-15796
    • Taniguchi, T.1    Kobayashi, T.2    Kondo, J.3
  • 3
    • 0034874786 scopus 로고    scopus 로고
    • Structure and function of Syk protein-tyrosine kinase
    • Sada K, Takano T, Yanagi S, Yamamura H. Structure and function of Syk protein-tyrosine kinase. J Biochem (Tokyo). 2001;130:177-186.
    • (2001) J Biochem (Tokyo) , vol.130 , pp. 177-186
    • Sada, K.1    Takano, T.2    Yanagi, S.3    Yamamura, H.4
  • 4
    • 0028905060 scopus 로고
    • Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE
    • Shiue L, Zoller MJ, Brugge JS. Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE. J Biol Chem. 1995;270:10498-10502.
    • (1995) J Biol Chem , vol.270 , pp. 10498-10502
    • Shiue, L.1    Zoller, M.J.2    Brugge, J.S.3
  • 5
    • 0031092657 scopus 로고    scopus 로고
    • Impaired tyrosine phosphorylation and Ca2+ mobilization, but not degranulation, in lyn-deficient bone marrow-derived mast cells
    • Nishizumi H, Yamamoto T. Impaired tyrosine phosphorylation and Ca2+ mobilization, but not degranulation, in lyn-deficient bone marrow-derived mast cells. J Immunol. 1997;158:2350-2355.
    • (1997) J Immunol , vol.158 , pp. 2350-2355
    • Nishizumi, H.1    Yamamoto, T.2
  • 6
    • 0030018183 scopus 로고    scopus 로고
    • Transfection of Syk protein tyrosine kinase reconstitutes high affinity IgE receptor-mediated degranulation in a Syk-negative variant of rat basophilic leukemia RBL-2H3 cells
    • Zhang J, Berenstein EH, Evans RL, Siraganian RP. Transfection of Syk protein tyrosine kinase reconstitutes high affinity IgE receptor-mediated degranulation in a Syk-negative variant of rat basophilic leukemia RBL-2H3 cells. J Exp Med. 1996;184:71-79.
    • (1996) J Exp Med , vol.184 , pp. 71-79
    • Zhang, J.1    Berenstein, E.H.2    Evans, R.L.3    Siraganian, R.P.4
  • 7
    • 0030472724 scopus 로고    scopus 로고
    • Critical role for the tyrosine kinase Syk in signalling through the high affinity IgE receptor of mast cells
    • Costello PS, Turner M, Walters AE, et al. Critical role for the tyrosine kinase Syk in signalling through the high affinity IgE receptor of mast cells. Oncogene. 1996;13:2595-2605.
    • (1996) Oncogene , vol.13 , pp. 2595-2605
    • Costello, P.S.1    Turner, M.2    Walters, A.E.3
  • 9
    • 0035282938 scopus 로고    scopus 로고
    • SH2 domain-mediated targeting, but not localization, of Syk in the plasma membrane is critical for FcεRI signaling
    • Sada K, Zhang J, Siraganian RP. SH2 domain-mediated targeting, but not localization, of Syk in the plasma membrane is critical for FcεRI signaling. Blood. 2001;97:1352-1359.
    • (2001) Blood , vol.97 , pp. 1352-1359
    • Sada, K.1    Zhang, J.2    Siraganian, R.P.3
  • 10
    • 0033678973 scopus 로고    scopus 로고
    • LAT is essential for Fc(ε)RI-mediated mast cell activation
    • Saitoh S, Arudchandran R, Manetz TS, et al. LAT is essential for Fc(ε)RI-mediated mast cell activation. Immunity. 2000;12:525-535.
    • (2000) Immunity , vol.12 , pp. 525-535
    • Saitoh, S.1    Arudchandran, R.2    Manetz, T.S.3
  • 11
    • 0035849822 scopus 로고    scopus 로고
    • Essential role for Gab2 in the allergic response
    • Gu H, Saito K, Klaman LD, et al. Essential role for Gab2 in the allergic response. Nature. 2001;412:186-190.
    • (2001) Nature , vol.412 , pp. 186-190
    • Gu, H.1    Saito, K.2    Klaman, L.D.3
  • 12
    • 0036347746 scopus 로고    scopus 로고
    • Fyn kinase initiates complementary signals required for IgE-dependent mast cell degranulation
    • Parravicini V, Gadina M, Kovarova M, et al. Fyn kinase initiates complementary signals required for IgE-dependent mast cell degranulation. Nat Immunol. 2002;3:741-748.
    • (2002) Nat Immunol , vol.3 , pp. 741-748
    • Parravicini, V.1    Gadina, M.2    Kovarova, M.3
  • 13
    • 0029006745 scopus 로고
    • Cloning and characterization of cbl-b: A SH3 binding protein with homology to the c-cbl proto-oncogene
    • Keane MM, Rivero-Lezcano OM, Mitchell JA, Robbins KC, Lipkowitz S. Cloning and characterization of cbl-b: a SH3 binding protein with homology to the c-cbl proto-oncogene. Oncogene. 1995;10:2367-2377.
    • (1995) Oncogene , vol.10 , pp. 2367-2377
    • Keane, M.M.1    Rivero-Lezcano, O.M.2    Mitchell, J.A.3    Robbins, K.C.4    Lipkowitz, S.5
  • 14
    • 0036499010 scopus 로고    scopus 로고
    • Cbl and Cbl-b in T-cell regulation
    • Liu YC, Gu H. Cbl and Cbl-b in T-cell regulation. Trends Immunol. 2002;23:140-143.
    • (2002) Trends Immunol , vol.23 , pp. 140-143
    • Liu, Y.C.1    Gu, H.2
  • 15
    • 0034642499 scopus 로고    scopus 로고
    • Negative regulation of lymphocyte activation and autoimmunity by the molecular adaptor Cbl-b
    • Bachmaier K, Krawczyk C, Kozieradzki I, et al. Negative regulation of lymphocyte activation and autoimmunity by the molecular adaptor Cbl-b. Nature. 2000;403:211-216.
    • (2000) Nature , vol.403 , pp. 211-216
    • Bachmaier, K.1    Krawczyk, C.2    Kozieradzki, I.3
  • 16
    • 0034642534 scopus 로고    scopus 로고
    • Cbl-b regulates the CD28 dependence of T-cell activation
    • Chiang YJ, Kole HK, Brown K, et al. Cbl-b regulates the CD28 dependence of T-cell activation. Nature. 2000;403:216-220.
    • (2000) Nature , vol.403 , pp. 216-220
    • Chiang, Y.J.1    Kole, H.K.2    Brown, K.3
  • 17
    • 0035895959 scopus 로고    scopus 로고
    • Cbl-b, a RING-type E3 ubiquitin ligase, targets phosphatidylinositol 3-kinase for ubiquitination in T cells
    • Fang D, Wang HY, Fang N, et al. Cbl-b, a RING-type E3 ubiquitin ligase, targets phosphatidylinositol 3-kinase for ubiquitination in T cells. J Biol Chem. 2001;276:4872-4878.
    • (2001) J Biol Chem , vol.276 , pp. 4872-4878
    • Fang, D.1    Wang, H.Y.2    Fang, N.3
  • 18
    • 0035555195 scopus 로고    scopus 로고
    • Proteolysis-independent regulation of PI3K by Cbl-b-mediated ubiquitination in T cells
    • Fang D, Liu YC. Proteolysis-independent regulation of PI3K by Cbl-b-mediated ubiquitination in T cells. Nat Immunol. 2001;2:870-875.
    • (2001) Nat Immunol , vol.2 , pp. 870-875
    • Fang, D.1    Liu, Y.C.2
  • 19
    • 15144353776 scopus 로고    scopus 로고
    • Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav
    • Han J, Luby-Phelps K, Das B, et al. Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav. Science. 1998;279:558-560.
    • (1998) Science , vol.279 , pp. 558-560
    • Han, J.1    Luby-Phelps, K.2    Das, B.3
  • 20
    • 0037944241 scopus 로고    scopus 로고
    • Cbl-b negatively regulates B cell antigen receptor signaling in mature B cells through ubiquitination of the tyrosine kinase Syk
    • Sohn HW, Gu H, Pierce SK. Cbl-b negatively regulates B cell antigen receptor signaling in mature B cells through ubiquitination of the tyrosine kinase Syk. J Exp Med. 2003;197:1511-1524.
    • (2003) J Exp Med , vol.197 , pp. 1511-1524
    • Sohn, H.W.1    Gu, H.2    Pierce, S.K.3
  • 21
    • 0036645535 scopus 로고    scopus 로고
    • Cbl-b positively regulates Btk-mediated activation of phospholipase C-γ2 in B cells
    • Yasuda T, Tezuka T, Maeda A, et al. Cbl-b positively regulates Btk-mediated activation of phospholipase C-γ2 in B cells. J Exp Med. 2002;196:51-63.
    • (2002) J Exp Med , vol.196 , pp. 51-63
    • Yasuda, T.1    Tezuka, T.2    Maeda, A.3
  • 22
    • 0030889218 scopus 로고    scopus 로고
    • The product of the protooncogene c-cbl: A negative regulator of the Syk tyrosine kinase
    • Ota Y, Samelson LE. The product of the protooncogene c-cbl: a negative regulator of the Syk tyrosine kinase. Science. 1997;276:418-420.
    • (1997) Science , vol.276 , pp. 418-420
    • Ota, Y.1    Samelson, L.E.2
  • 23
    • 0037020143 scopus 로고    scopus 로고
    • Activation of Syk tyrosine kinase is required for c-Cbl-mediated ubiquitination of Fcε RI and Syk in RBL cells
    • Paolini R, Molfetta R, Beitz LO, et al. Activation of Syk tyrosine kinase is required for c-Cbl-mediated ubiquitination of Fcε RI and Syk in RBL cells. J Biol Chem. 2002;277:36940-36947.
    • (2002) J Biol Chem , vol.277 , pp. 36940-36947
    • Paolini, R.1    Molfetta, R.2    Beitz, L.O.3
  • 24
    • 0036736779 scopus 로고    scopus 로고
    • Proteasome-dependent regulation of Syk tyrosine kinase levels in human basophils
    • Youssef LA, Wilson BS, Oliver JM. Proteasome-dependent regulation of Syk tyrosine kinase levels in human basophils. J Allergy Clin Immunol. 2002;110:366-373.
    • (2002) J Allergy Clin Immunol , vol.110 , pp. 366-373
    • Youssef, L.A.1    Wilson, B.S.2    Oliver, J.M.3
  • 25
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E. Functional rafts in cell membranes. Nature. 1997;387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 26
    • 0037154747 scopus 로고    scopus 로고
    • T cell receptor signaling precedes immunological synapse formation
    • Lee KH, Holdorf AD, Dustin ML, et al. T cell receptor signaling precedes immunological synapse formation. Science. 2002;295:1539-1542.
    • (2002) Science , vol.295 , pp. 1539-1542
    • Lee, K.H.1    Holdorf, A.D.2    Dustin, M.L.3
  • 27
    • 0035853045 scopus 로고    scopus 로고
    • Raft-partitioning of the ubiquitin ligases Cbl and Nedd4 upon IgE-triggered cell signaling
    • Lafont F, Simons K. Raft-partitioning of the ubiquitin ligases Cbl and Nedd4 upon IgE-triggered cell signaling. Proc Natl Acad Sci U S A. 2001;98:3180-3184.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 3180-3184
    • Lafont, F.1    Simons, K.2
  • 28
    • 0023930021 scopus 로고
    • Studies with a monoclonal antibody to the beta subunit of the receptor with high affinity for immunoglobulin E
    • Rivera J, Kinet JP, Kim J, Pucillo C, Metzger H. Studies with a monoclonal antibody to the beta subunit of the receptor with high affinity for immunoglobulin E. Mol Immunol. 1988;25:647-661.
    • (1988) Mol Immunol , vol.25 , pp. 647-661
    • Rivera, J.1    Kinet, J.P.2    Kim, J.3    Pucillo, C.4    Metzger, H.5
  • 29
    • 0033981831 scopus 로고    scopus 로고
    • Sequential requirements of the N-terminal palmitoylation site and SH2 domain of Src family kinases in the initiation and progression of FcεRI signaling
    • Honda Z, Suzuki T, Kono H, et al. Sequential requirements of the N-terminal palmitoylation site and SH2 domain of Src family kinases in the initiation and progression of FcεRI signaling. Mol Cell Biol. 2000;20:1759-1771.
    • (2000) Mol Cell Biol , vol.20 , pp. 1759-1771
    • Honda, Z.1    Suzuki, T.2    Kono, H.3
  • 30
    • 0035920225 scopus 로고    scopus 로고
    • Cbl-b-dependent coordinated degradation of the epidermal growth factor receptor signaling complex
    • Ettenberg SA, Magnifico A, Cuello M, et al. Cbl-b-dependent coordinated degradation of the epidermal growth factor receptor signaling complex. J Biol Chem. 2001;276:27677-27684.
    • (2001) J Biol Chem , vol.276 , pp. 27677-27684
    • Ettenberg, S.A.1    Magnifico, A.2    Cuello, M.3
  • 31
    • 0037105464 scopus 로고    scopus 로고
    • Regulation of Fcε RI-mediated degranulation by an adaptor protein 3BP2 in rat basophilic leukemia RBL-2H3 cells
    • Sada K, Miah SMS, Maeno K, et al. Regulation of Fcε RI-mediated degranulation by an adaptor protein 3BP2 in rat basophilic leukemia RBL-2H3 cells. Blood. 2002;100:2138-2144.
    • (2002) Blood , vol.100 , pp. 2138-2144
    • Sada, K.1    Miah, S.M.S.2    Maeno, K.3
  • 32
    • 0033976068 scopus 로고    scopus 로고
    • Point mutation of a tyrosine in the linker region of Syk results in a gain of function
    • Sada K, Zhang J, Siraganian RP. Point mutation of a tyrosine in the linker region of Syk results in a gain of function. J Immunol. 2000;164:338-344.
    • (2000) J Immunol , vol.164 , pp. 338-344
    • Sada, K.1    Zhang, J.2    Siraganian, R.P.3
  • 33
    • 0031041581 scopus 로고    scopus 로고
    • Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains
    • Field KA, Holowka D, Baird B. Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains. J Biol Chem. 1997;272:4276-4280.
    • (1997) J Biol Chem , vol.272 , pp. 4276-4280
    • Field, K.A.1    Holowka, D.2    Baird, B.3
  • 34
    • 0032142953 scopus 로고    scopus 로고
    • LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation
    • Zhang W, Trible RP, Samelson LE. LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity. 1998;9:239-246.
    • (1998) Immunity , vol.9 , pp. 239-246
    • Zhang, W.1    Trible, R.P.2    Samelson, L.E.3
  • 35
    • 0036569710 scopus 로고    scopus 로고
    • The adapter molecule Gab2 regulates Fc ε RI-mediated signal transduction in mast cells
    • Xie ZH, Ambudkar I, Siraganian RP. The adapter molecule Gab2 regulates Fc ε RI-mediated signal transduction in mast cells. J Immunol. 2002;168:4682-4691.
    • (2002) J Immunol , vol.168 , pp. 4682-4691
    • Xie, Z.H.1    Ambudkar, I.2    Siraganian, R.P.3
  • 36
    • 0041589313 scopus 로고    scopus 로고
    • Adaptor protein 3BP2 is a potential ligand of Src homology 2 and 3 domains of Lyn protein-tyrosine kinase
    • Maeno K, Sada K, Kyo S, et al. Adaptor protein 3BP2 is a potential ligand of Src homology 2 and 3 domains of Lyn protein-tyrosine kinase. J Biol Chem. 2003;278:24912-24920.
    • (2003) J Biol Chem , vol.278 , pp. 24912-24920
    • Maeno, K.1    Sada, K.2    Kyo, S.3
  • 37
    • 0142155218 scopus 로고    scopus 로고
    • Negative regulation of Lyn protein-tyrosine kinase by c-Cbl ubiquitin-protein ligase in Fcε RI-mediated mast cell activation
    • Kyo S, Sada K, Qu X, et al. Negative regulation of Lyn protein-tyrosine kinase by c-Cbl ubiquitin-protein ligase in Fcε RI-mediated mast cell activation. Genes Cells. 2003;8:825-836.
    • (2003) Genes Cells , vol.8 , pp. 825-836
    • Kyo, S.1    Sada, K.2    Qu, X.3
  • 38
    • 0033604543 scopus 로고    scopus 로고
    • Signalling through the high-affinity IgE receptor Fc εRI
    • Turner H, Kinet JP. Signalling through the high-affinity IgE receptor Fc εRI. Nature. 1999;402: B24-B30.
    • (1999) Nature , vol.402
    • Turner, H.1    Kinet, J.P.2
  • 39
    • 0028968751 scopus 로고
    • Substitution of an aspartic acid results in constitutive activation of c-kit receptor tyrosine kinase in a rat tumor mast cell line RBL-2H3
    • Tsujimura T, Furitsu T, Morimoto M, et al. Substitution of an aspartic acid results in constitutive activation of c-kit receptor tyrosine kinase in a rat tumor mast cell line RBL-2H3. Int Arch Allergy Immunol. 1995;106:377-385.
    • (1995) Int Arch Allergy Immunol , vol.106 , pp. 377-385
    • Tsujimura, T.1    Furitsu, T.2    Morimoto, M.3
  • 40
    • 0035383812 scopus 로고    scopus 로고
    • Signal transducer and activator of transcription 3 activation is required for Asp(816) mutant c-Kit-mediated cytokine-independent survival and proliferation in human leukemia cells
    • Ning ZQ, Li J, Arceci RJ. Signal transducer and activator of transcription 3 activation is required for Asp(816) mutant c-Kit-mediated cytokine-independent survival and proliferation in human leukemia cells. Blood. 2001;97:3559-3567.
    • (2001) Blood , vol.97 , pp. 3559-3567
    • Ning, Z.Q.1    Li, J.2    Arceci, R.J.3
  • 41
    • 0031906691 scopus 로고    scopus 로고
    • Wortmannin-sensitive phosphorylation, translocation, and activation of PLC-γ1, but not PLCγ2, in antigen-stimulated RBL-2H3 mast cells
    • Barker SA, Caldwell KK, Pfeiffer JR, Wilson BS. Wortmannin-sensitive phosphorylation, translocation, and activation of PLC-γ1, but not PLCγ2, in antigen-stimulated RBL-2H3 mast cells. Mol Biol Cell. 1998;9:483-496.
    • (1998) Mol Biol Cell , vol.9 , pp. 483-496
    • Barker, S.A.1    Caldwell, K.K.2    Pfeiffer, J.R.3    Wilson, B.S.4
  • 42
    • 0001764561 scopus 로고    scopus 로고
    • Vav1 regulates phospholipase cgamma activation and calcium responses in mast cells
    • Manetz TS, Gonzalez-Espinosa C, Arudchandran R, et al. Vav1 regulates phospholipase cgamma activation and calcium responses in mast cells. Mol Cell Biol. 2001;21:3763-3774.
    • (2001) Mol Cell Biol , vol.21 , pp. 3763-3774
    • Manetz, T.S.1    Gonzalez-Espinosa, C.2    Arudchandran, R.3
  • 43
    • 0032693516 scopus 로고    scopus 로고
    • SLP-76 deficiency impairs signaling via the high-affinity IgE receptor in mast cells
    • Pivniouk VI, Martin TR, Lu-Kuo JM, et al. SLP-76 deficiency impairs signaling via the high-affinity IgE receptor in mast cells. J Clin Invest. 1999;103:1737-1743.
    • (1999) J Clin Invest , vol.103 , pp. 1737-1743
    • Pivniouk, V.I.1    Martin, T.R.2    Lu-Kuo, J.M.3
  • 44
    • 0033534533 scopus 로고    scopus 로고
    • Adaptors and molecular scaffolds in immune cell signaling
    • Rudd CE. Adaptors and molecular scaffolds in immune cell signaling. Cell. 1999;96:5-8.
    • (1999) Cell , vol.96 , pp. 5-8
    • Rudd, C.E.1
  • 45
    • 0037459341 scopus 로고    scopus 로고
    • Variation on an Src-like theme
    • Harrison SC. Variation on an Src-like theme. Cell. 2003;112:737-740.
    • (2003) Cell , vol.112 , pp. 737-740
    • Harrison, S.C.1
  • 46
    • 0034977079 scopus 로고    scopus 로고
    • Mutations in the gene encoding c-Abl-binding protein SH3BP2 cause cherubism
    • Ueki Y, Tiziani V, Santanna C, et al. Mutations in the gene encoding c-Abl-binding protein SH3BP2 cause cherubism. Nat Genet. 2001;28:125-126.
    • (2001) Nat Genet , vol.28 , pp. 125-126
    • Ueki, Y.1    Tiziani, V.2    Santanna, C.3
  • 47
    • 0036234459 scopus 로고    scopus 로고
    • Missing pieces in the NF-κB puzzle
    • Ghosh S, Karin M. Missing pieces in the NF-κB puzzle. Cell. 2002;109(suppl):S81-S96.
    • (2002) Cell , vol.109 , Issue.SUPPL.
    • Ghosh, S.1    Karin, M.2
  • 48
    • 0037184348 scopus 로고    scopus 로고
    • NF-κB signaling. Many roads lead to madrid
    • Dixit V, Mak TW. NF-κB signaling. Many roads lead to madrid. Cell. 2002;111:615-619.
    • (2002) Cell , vol.111 , pp. 615-619
    • Dixit, V.1    Mak, T.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.