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Volumn 11, Issue 2, 1999, Pages 226-232

Multiple signals converging on NF-κB

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; DNA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INHIBITOR PROTEIN; INTERLEUKIN 1BETA; PHOSPHOTRANSFERASE; TRANSCRIPTION FACTOR; TUMOR NECROSIS FACTOR ALPHA;

EID: 0032939903     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(99)80030-1     Document Type: Article
Times cited : (451)

References (50)
  • 1
    • 0029874138 scopus 로고    scopus 로고
    • The NF-κB and IκB proteins: New discoveries and insights
    • Baldwin A.S. The NF-κB and IκB proteins: new discoveries and insights. Annu Rev Immunol. 14:1996;649-681.
    • (1996) Annu Rev Immunol , vol.14 , pp. 649-681
    • Baldwin, A.S.1
  • 2
    • 0028985037 scopus 로고
    • NF-κB and Rel proteins in innate immunity
    • Kopp E., Ghosh S. NF-κB and Rel proteins in innate immunity. Adv Immunol. 58:1995;1-27.
    • (1995) Adv Immunol , vol.58 , pp. 1-27
    • Kopp, E.1    Ghosh, S.2
  • 3
    • 0030271387 scopus 로고    scopus 로고
    • NF-κB: Ten years after
    • Baeuerle P.A., Baltimore D. NF-κB: ten years after. Cell. 87:1996;13-20.
    • (1996) Cell , vol.87 , pp. 13-20
    • Baeuerle, P.A.1    Baltimore, D.2
  • 4
    • 0028174061 scopus 로고
    • Function and activation of NF-κB in the immune system
    • Baeuerle P.A., Henkel T. Function and activation of NF-κB in the immune system. Annu Rev Immunol. 12:1994;141-179.
    • (1994) Annu Rev Immunol , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkel, T.2
  • 5
    • 0031906550 scopus 로고    scopus 로고
    • Signal transduction through NF-κB
    • May M.J., Ghosh S. Signal transduction through NF-κB. Immunol Today. 19:1998;80-88.
    • (1998) Immunol Today , vol.19 , pp. 80-88
    • May, M.J.1    Ghosh, S.2
  • 6
    • 0030899121 scopus 로고    scopus 로고
    • IκB epsilon, a novel member of the IκB family, controls RelA and cRel NF-κB activity
    • Whiteside S.T., Epinat J.C., Rice N.R., Israel A. IκB epsilon, a novel member of the IκB family, controls RelA and cRel NF-κB activity. EMBO J. 16:1997;1413-1426.
    • (1997) EMBO J , vol.16 , pp. 1413-1426
    • Whiteside, S.T.1    Epinat, J.C.2    Rice, N.R.3    Israel, A.4
  • 7
    • 0026523562 scopus 로고
    • Intramolecular masking of the nuclear location signal and dimerization domain in the precursor for the p50 NF-κB subunit
    • Henkel T., Zabel U., Van Zee K., Muller J.M., Fanning E., Baeuerle P. Intramolecular masking of the nuclear location signal and dimerization domain in the precursor for the p50 NF-κB subunit. Cell. 68:1992;1121-1133.
    • (1992) Cell , vol.68 , pp. 1121-1133
    • Henkel, T.1    Zabel, U.2    Van Zee, K.3    Muller, J.M.4    Fanning, E.5    Baeuerle, P.6
  • 8
    • 0030747128 scopus 로고    scopus 로고
    • NF-κB as a frequent target for immunosuppressive and anti-inflammatory molecules
    • Baeuerle P.A., Baichwal V.R. NF-κB as a frequent target for immunosuppressive and anti-inflammatory molecules. Adv Immunol. 65:1997;111-136.
    • (1997) Adv Immunol , vol.65 , pp. 111-136
    • Baeuerle, P.A.1    Baichwal, V.R.2
  • 10
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
    • First report of the biochemical purification of the IκB kinase complex and the identification of a kinase component responsible for cytokine-inducible phosphorylation of IκB. The authors show that the IKK complex has an apparent relative molecular of greater than 700 kDa and established that its activation kinetics in response to pro-inflammatory cytokines correlates with that of IκB phosphorylation.
    • DiDonato J.A., Hayakawa M., Rothwarf D.M., Zandi E., Karin M. A cytokine-responsive IκB kinase that activates the transcription factor NF-κB. Nature. 388:1997;853-862. First report of the biochemical purification of the IκB kinase complex and the identification of a kinase component responsible for cytokine-inducible phosphorylation of IκB. The authors show that the IKK complex has an apparent relative molecular of greater than 700 kDa and established that its activation kinetics in response to pro-inflammatory cytokines correlates with that of IκB phosphorylation.
    • (1997) Nature , vol.388 , pp. 853-862
    • Didonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5
  • 11
    • 0030613551 scopus 로고    scopus 로고
    • The IκB kinase complex (IKK) contains two kinase subunits, IKKα and IKKβ, necessary for IκB phosphorylation and NF-κB activation
    • Zandi E., Rothwarf D.M., Delhasse M., Hayakawa M., Karin M. The IκB kinase complex (IKK) contains two kinase subunits, IKKα and IKKβ, necessary for IκB phosphorylation and NF-κB activation. Cell. 91:1997;243-252.
    • (1997) Cell , vol.91 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhasse, M.3    Hayakawa, M.4    Karin, M.5
  • 12
    • 0030685825 scopus 로고    scopus 로고
    • IKK-1 and IKK-2: Cytokine-activated IκB kinases essential for NF-κB activation
    • Further characterization of the IκB kinase complex, termed the IKK signalsome, and the identification of a second IκB kinase component, termed IKK2. The authors also demonstrated that IKK2 plays a more critical role than IKK1 in the TNFα-mediated activation of the NF-κB signal transduction pathway.
    • Mercurio F., Zhu H., Murray B.W., Shevchenko A., Bennett B.L., Li J., Young D., Barbosa M., Mann M., Manning A.M., Rao A. IKK-1 and IKK-2: cytokine-activated IκB kinases essential for NF-κB activation. Science. 278:1997;860-866. Further characterization of the IκB kinase complex, termed the IKK signalsome, and the identification of a second IκB kinase component, termed IKK2. The authors also demonstrated that IKK2 plays a more critical role than IKK1 in the TNFα-mediated activation of the NF-κB signal transduction pathway.
    • (1997) Science , vol.278 , pp. 860-866
    • Mercurio, F.1    Zhu, H.2    Murray, B.W.3    Shevchenko, A.4    Bennett, B.L.5    Li, J.6    Young, D.7    Barbosa, M.8    Mann, M.9    Manning, A.M.10    Rao, A.11
  • 13
    • 0030611595 scopus 로고    scopus 로고
    • IκB kinase-β: NF-κB activation and complex formation with IκB kinase-κ And NIK
    • Woronicz J.D., Gao X., Cao Z., Rothe M., Goeddel D.V. IκB kinase-β: NF-κB activation and complex formation with IκB kinase-κ and NIK. Science. 278:1997;866-869.
    • (1997) Science , vol.278 , pp. 866-869
    • Woronicz, J.D.1    Gao, X.2    Cao, Z.3    Rothe, M.4    Goeddel, D.V.5
  • 14
    • 0030613758 scopus 로고    scopus 로고
    • NF-κB activation: The IκB kinase revealed?
    • Stancovski I., Baltimore D. NF-κB activation: the IκB kinase revealed? Cell. 91:1997;299-302.
    • (1997) Cell , vol.91 , pp. 299-302
    • Stancovski, I.1    Baltimore, D.2
  • 15
    • 0030613646 scopus 로고    scopus 로고
    • Catalysis by a multiprotein IκB kinase complex
    • Maniatis T. Catalysis by a multiprotein IκB kinase complex. Science. 278:1997;818-819.
    • (1997) Science , vol.278 , pp. 818-819
    • Maniatis, T.1
  • 17
    • 0028970734 scopus 로고
    • Stimulation-dependent IκB phosphorylation marks the NF-κB inhibitor for degradation via the ubiquitin-proteasome pathway
    • Alkalay I., Yaron A., Hatzubai A., Orian A., Ciechanover A., Ben-Neriah Y. Stimulation-dependent IκB phosphorylation marks the NF-κB inhibitor for degradation via the ubiquitin-proteasome pathway. Proc Natl Acad Sci USA. 92:1995;10599-10603.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10599-10603
    • Alkalay, I.1    Yaron, A.2    Hatzubai, A.3    Orian, A.4    Ciechanover, A.5    Ben-Neriah, Y.6
  • 18
    • 0030731146 scopus 로고    scopus 로고
    • Inhibition of NF-κB cellular function via specific targeting of the IκB ubiquitin ligase
    • Elucidation of the mechanism by which phosphorylated IκB is targeted for site-specific ubiquitination and subsequent degradation. The authors precisely defined the ubiquitin ligase substrate recognition motif of the IκBs and demonstrated that introduction of short phosphopeptides based on this motif into cells abrogates stimulus-dependent activation of the NF-κB pathway.
    • Yaron A., Gonen H., Alkalay I., Hatzubai A., Jung S., Beyth S., Mercurio F., Manning A.M., Ciechanover A., Ben-Neriah Y. Inhibition of NF-κB cellular function via specific targeting of the IκB ubiquitin ligase. EMBO J. 16:1997;101-107. Elucidation of the mechanism by which phosphorylated IκB is targeted for site-specific ubiquitination and subsequent degradation. The authors precisely defined the ubiquitin ligase substrate recognition motif of the IκBs and demonstrated that introduction of short phosphopeptides based on this motif into cells abrogates stimulus-dependent activation of the NF-κB pathway.
    • (1997) EMBO J , vol.16 , pp. 101-107
    • Yaron, A.1    Gonen, H.2    Alkalay, I.3    Hatzubai, A.4    Jung, S.5    Beyth, S.6    Mercurio, F.7    Manning, A.M.8    Ciechanover, A.9    Ben-Neriah, Y.10
  • 19
    • 0029146930 scopus 로고
    • Signal-induced site-specific phosphorylation targets IκB α to the ubiquitin-proteasome pathway
    • Chen Z., Hagler J., Palombella V.J., Melandri F., Scherer D., Ballard D., Maniatis T. Signal-induced site-specific phosphorylation targets IκB α to the ubiquitin-proteasome pathway. Genes Dev. 9:1995;1586-1597.
    • (1995) Genes Dev , vol.9 , pp. 1586-1597
    • Chen, Z.1    Hagler, J.2    Palombella, V.J.3    Melandri, F.4    Scherer, D.5    Ballard, D.6    Maniatis, T.7
  • 20
    • 0031285250 scopus 로고    scopus 로고
    • Activation of the IκB α complex by MEKK1, a kinase of the JNK pathway
    • Identification of mitogen-activated protein kinase kinase kinase-1 as an upstream activator of the IκB kinase complex.
    • Lee F.S., Hagler J., Chen Z.J., Maniatis T. Activation of the IκB α complex by MEKK1, a kinase of the JNK pathway. Cell. 88:1997;213-222. Identification of mitogen-activated protein kinase kinase kinase-1 as an upstream activator of the IκB kinase complex.
    • (1997) Cell , vol.88 , pp. 213-222
    • Lee, F.S.1    Hagler, J.2    Chen, Z.J.3    Maniatis, T.4
  • 21
    • 0031017618 scopus 로고    scopus 로고
    • MAP3K-related kinase involved in NF-κB induction by TNF, CD95 and IL-1
    • Identification of NF-κB-inducing kinase (NIK) as an upstream activator of the IκB kinase complex in response to TNFα, IL-1 and FasL.
    • Malinin N.L., Boldin M.P., Kovalenko A.V., Wallach D. MAP3K-related kinase involved in NF-κB induction by TNF, CD95 and IL-1. Nature. 385:1997;540-544. Identification of NF-κB-inducing kinase (NIK) as an upstream activator of the IκB kinase complex in response to TNFα, IL-1 and FasL.
    • (1997) Nature , vol.385 , pp. 540-544
    • Malinin, N.L.1    Boldin, M.P.2    Kovalenko, A.V.3    Wallach, D.4
  • 22
    • 0032583947 scopus 로고    scopus 로고
    • NF-κB-inducing kinase activates IKKα by phosphorylation of Ser176
    • Ling L., Cao Z., Goeddel D.V. NF-κB-inducing kinase activates IKKα by phosphorylation of Ser176. Proc Natl Acad Sci USA. 95:1998;3792-3797.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3792-3797
    • Ling, L.1    Cao, Z.2    Goeddel, D.V.3
  • 23
    • 0032583949 scopus 로고    scopus 로고
    • Differential regulation of IκB kinase α and β by two upstream kinases, NF-κB-inducing kinase and mitogen-activated protein kinase/ERK kinase kinase-1
    • Nakano H., Shindo M., Sakon S., Nishinaka S., Mihara M., Yagita H., Okumura K. Differential regulation of IκB kinase α and β by two upstream kinases, NF-κB-inducing kinase and mitogen-activated protein kinase/ERK kinase kinase-1. Proc Natl Acad Sci USA. 95:1998;3537-3542.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3537-3542
    • Nakano, H.1    Shindo, M.2    Sakon, S.3    Nishinaka, S.4    Mihara, M.5    Yagita, H.6    Okumura, K.7
  • 25
    • 0031597368 scopus 로고    scopus 로고
    • Coordinate regulation of IκB kinases by mitogen-activated protein kinase kinase kinase 1 and NF-κB-inducing kinase
    • Nemoto S., DiDonato J.A., Lin A. Coordinate regulation of IκB kinases by mitogen-activated protein kinase kinase kinase 1 and NF-κB-inducing kinase. Mol Cell Biol. 18:1998;7336-7343.
    • (1998) Mol Cell Biol , vol.18 , pp. 7336-7343
    • Nemoto, S.1    Didonato, J.A.2    Lin, A.3
  • 26
    • 0032515035 scopus 로고    scopus 로고
    • Role of IKK1 and IKK2 in lipopolysaccharide signaling in human monocytic cells
    • O'Connell M.A., Bennett B.L., Mercurio F., Manning A., Mackman N. Role of IKK1 and IKK2 in lipopolysaccharide signaling in human monocytic cells. J Biol Chem. 273:1998;30410-30414.
    • (1998) J Biol Chem , vol.273 , pp. 30410-30414
    • O'Connell, M.A.1    Bennett, B.L.2    Mercurio, F.3    Manning, A.4    Mackman, N.5
  • 27
    • 0032568792 scopus 로고    scopus 로고
    • Complementation cloning of NEMO, a component of the IκB kinase complex essential for NF-κB activation
    • Identification of NF-κB essential modulator NEMO as a non-kinase component of the IκB kinase complex required for efficient activation of IKK2.
    • Yamaoka S., Courtois G., Bessia C., Whiteside S., Weil R., Agou F., Kirk H.E., Kay R.J., Israël A. Complementation cloning of NEMO, a component of the IκB kinase complex essential for NF-κB activation. Cell. 93:1998;1231-1240. Identification of NF-κB essential modulator NEMO as a non-kinase component of the IκB kinase complex required for efficient activation of IKK2.
    • (1998) Cell , vol.93 , pp. 1231-1240
    • Yamaoka, S.1    Courtois, G.2    Bessia, C.3    Whiteside, S.4    Weil, R.5    Agou, F.6    Kirk, H.E.7    Kay, R.J.8    Israël, A.9
  • 28
    • 0032589935 scopus 로고    scopus 로고
    • IKKAP-1, a novel regulator of NF-κB activation, reveals heterogeneity in IκB complexes
    • Identification and biochemical characterization of distinct IκB kinase complexes, comprised of different IKK dimers, within cells. It was demonstrated that high molecular weight IκBα kinase complexes (greater than 700 kDa) exist in vivo that contain IKK2, but not IKK1, which display TNFα-dependent activation. This finding suggests that IKK1 knock out mice would retain the ability to elicit stimulus-dependent activation of the NF-κB pathway.
    • Mercurio F., Murray B., Bennett B.L., Pascaul G., Shevchenko A., Zhu H., Young D., Li J., Mann M., Manning A. IKKAP-1, a novel regulator of NF-κB activation, reveals heterogeneity in IκB complexes. Mol Cell Biol. 19:1999;1526-1538. Identification and biochemical characterization of distinct IκB kinase complexes, comprised of different IKK dimers, within cells. It was demonstrated that high molecular weight IκBα kinase complexes (greater than 700 kDa) exist in vivo that contain IKK2, but not IKK1, which display TNFα-dependent activation. This finding suggests that IKK1 knock out mice would retain the ability to elicit stimulus-dependent activation of the NF-κB pathway.
    • (1999) Mol Cell Biol , vol.19 , pp. 1526-1538
    • Mercurio, F.1    Murray, B.2    Bennett, B.L.3    Pascaul, G.4    Shevchenko, A.5    Zhu, H.6    Young, D.7    Li, J.8    Mann, M.9    Manning, A.10
  • 29
    • 0032541657 scopus 로고    scopus 로고
    • IKK-γ is an essential regulatory subunit of the IκB kinase complex
    • This work is the first to report the purification and characterization of IKKγ, a core component of the IKK complex. The authors demonstrate that IKKγ directly associates with IKKβ (IKK2) and mediates an essential step in the stimulus-dependent activation of IKK activity.
    • Rothwarf D.M., Zandi E., Natoli G., Karin M. IKK-γ is an essential regulatory subunit of the IκB kinase complex. Nature. 395:1998;297-300. This work is the first to report the purification and characterization of IKKγ, a core component of the IKK complex. The authors demonstrate that IKKγ directly associates with IKKβ (IKK2) and mediates an essential step in the stimulus-dependent activation of IKK activity.
    • (1998) Nature , vol.395 , pp. 297-300
    • Rothwarf, D.M.1    Zandi, E.2    Natoli, G.3    Karin, M.4
  • 30
    • 0031888055 scopus 로고    scopus 로고
    • Interaction of an adenovirus E3 14.7-kilodalton protein with a novel tumor necrosis factor-alpha-inducible cellular protein containing leuine zipper motifs
    • Li Y., Kang J., Horwitz M.S. Interaction of an adenovirus E3 14.7-kilodalton protein with a novel tumor necrosis factor-alpha-inducible cellular protein containing leuine zipper motifs. Mol Cell Biol. 18:1998;1601-1610.
    • (1998) Mol Cell Biol , vol.18 , pp. 1601-1610
    • Li, Y.1    Kang, J.2    Horwitz, M.S.3
  • 31
    • 0032541670 scopus 로고    scopus 로고
    • IKAP is a scaffold protein of the IκB kinase complex
    • Cohen L., Henzel W.J., Baeuerle P.A. IKAP is a scaffold protein of the IκB kinase complex. Nature. 395:1998;292-296.
    • (1998) Nature , vol.395 , pp. 292-296
    • Cohen, L.1    Henzel, W.J.2    Baeuerle, P.A.3
  • 33
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteosome pathway: On protein death and cell life
    • Ciechanover A. The ubiquitin-proteosome pathway: on protein death and cell life. EMBO J. 17:1998;7151-7160.
    • (1998) EMBO J , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 35
    • 0028170265 scopus 로고
    • Activation of NF-κB in vivo is regulated by multiple phosphorylations
    • Naumann M., Scheidereit C. Activation of NF-κB in vivo is regulated by multiple phosphorylations. EMBO J. 13:1994;4597-4607.
    • (1994) EMBO J , vol.13 , pp. 4597-4607
    • Naumann, M.1    Scheidereit, C.2
  • 36
    • 0032491485 scopus 로고    scopus 로고
    • Activation of nuclear factor-κB-dependent transcription by tumor necrosis factor-alpha is mediated through phosphorylation of RelA/p65 on serine 529
    • Wang D., Baldwin A.S. Activation of nuclear factor-κB-dependent transcription by tumor necrosis factor-alpha is mediated through phosphorylation of RelA/p65 on serine 529. J Biol Chem. 273:1998;29411-29416.
    • (1998) J Biol Chem , vol.273 , pp. 29411-29416
    • Wang, D.1    Baldwin, A.S.2
  • 37
    • 0030991201 scopus 로고    scopus 로고
    • The transcriptional activity of NF-κB is regulated by the IκB-associated PKAc subunit through a cyclic AMP-independent mechanism
    • Zhong H., Yang H.S., Erdjument-Bromage H., Tempst P., Ghosh S. The transcriptional activity of NF-κB is regulated by the IκB-associated PKAc subunit through a cyclic AMP-independent mechanism. Cell. 89:1997;413-424.
    • (1997) Cell , vol.89 , pp. 413-424
    • Zhong, H.1    Yang, H.S.2    Erdjument-Bromage, H.3    Tempst, P.4    Ghosh, S.5
  • 38
    • 0030614504 scopus 로고    scopus 로고
    • Regulation of NF-κB by cyclin-dependent kinases associated with the p300 coactivator
    • Perkins N.D., Felzien L.K., Betts J.C., Leung K., Beach D.H., Nabel G.J. Regulation of NF-κB by cyclin-dependent kinases associated with the p300 coactivator. Science. 275:1997;523-527.
    • (1997) Science , vol.275 , pp. 523-527
    • Perkins, N.D.1    Felzien, L.K.2    Betts, J.C.3    Leung, K.4    Beach, D.H.5    Nabel, G.J.6
  • 39
    • 0032039076 scopus 로고    scopus 로고
    • Phosphorylation of NF-κB p65 by PKA9stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300
    • Zhong H., Voll R.E., Ghosh S. Phosphorylation of NF-κB p65 by PKA9stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300. Mol Cell. 1:1998;661-671.
    • (1998) Mol Cell , vol.1 , pp. 661-671
    • Zhong, H.1    Voll, R.E.2    Ghosh, S.3
  • 40
    • 0344801229 scopus 로고    scopus 로고
    • Targeting the NF-κB activation pathway for gene regulating drugs
    • Manning A. Targeting the NF-κB activation pathway for gene regulating drugs. Curr Opin Drug Disc Dev. 1:1998;147-156.
    • (1998) Curr Opin Drug Disc Dev , vol.1 , pp. 147-156
    • Manning, A.1
  • 41
    • 0018906664 scopus 로고
    • A dorso-ventral shift embryonic primordia in a new maternal-effect mutant of Drosophila
    • Nusslein-Volhard C., Lohs-Schardin M., Sander K., Cremer C. A dorso-ventral shift embryonic primordia in a new maternal-effect mutant of Drosophila. Nature. 283:1980;474-476.
    • (1980) Nature , vol.283 , pp. 474-476
    • Nusslein-Volhard, C.1    Lohs-Schardin, M.2    Sander, K.3    Cremer, C.4
  • 42
    • 0026045994 scopus 로고
    • The dorsal morphogen gradient regulates the mesoderm determinant twist in early Drosophila embryos
    • Jiang J., Kosman D., Ip Y.T., Levine M. The dorsal morphogen gradient regulates the mesoderm determinant twist in early Drosophila embryos. Genes Dev. 5:1991;1881-1891.
    • (1991) Genes Dev , vol.5 , pp. 1881-1891
    • Jiang, J.1    Kosman, D.2    Ip, Y.T.3    Levine, M.4
  • 43
    • 0027189976 scopus 로고
    • The interplay between multiple enhancer and silencer elements defines the pattern of decapentaplegic expression
    • Huang J.D., Schwyter D.H., Shirokawa J.M., Courey A.J. The interplay between multiple enhancer and silencer elements defines the pattern of decapentaplegic expression. Genes Dev. 7:1993;694-704.
    • (1993) Genes Dev , vol.7 , pp. 694-704
    • Huang, J.D.1    Schwyter, D.H.2    Shirokawa, J.M.3    Courey, A.J.4
  • 44
    • 0028933142 scopus 로고
    • Twist is required in head mesenchyme for cranial neural tube morphogensis
    • Chen Z.F., Behringer R.R. Twist is required in head mesenchyme for cranial neural tube morphogensis. Genes Dev. 9:1995;686-699.
    • (1995) Genes Dev , vol.9 , pp. 686-699
    • Chen, Z.F.1    Behringer, R.R.2
  • 47
    • 0032499286 scopus 로고    scopus 로고
    • Role of Rel/NF-κB transcription factors during the outgrowth of vertebrate limb
    • Kanegae Y., Tavares A.T., Izpisua-Belmonte J.C., Verma I. Role of Rel/NF-κB transcription factors during the outgrowth of vertebrate limb. Nature. 392:1998;611-614.
    • (1998) Nature , vol.392 , pp. 611-614
    • Kanegae, Y.1    Tavares, A.T.2    Izpisua-Belmonte, J.C.3    Verma, I.4
  • 48
    • 0032498962 scopus 로고    scopus 로고
    • Inhibition of NF-κB in disruption of the apical ectodermal ridge and aberrant limb morphogenesis
    • Bushdid P., Brantley D., Yull F., Blaeuer G., Hoffman L., Niswander L., Kerr L. Inhibition of NF-κB in disruption of the apical ectodermal ridge and aberrant limb morphogenesis. Nature. 392:1998;615-619.
    • (1998) Nature , vol.392 , pp. 615-619
    • Bushdid, P.1    Brantley, D.2    Yull, F.3    Blaeuer, G.4    Hoffman, L.5    Niswander, L.6    Kerr, L.7


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