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Volumn 5, Issue , 2008, Pages

Caspase-3-mediated cleavage of p65/RelA results in a carboxy-terminal fragment that inhibits IκBα and enhances HIV-1 replication in human T lymphocytes

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; I KAPPA B ALPHA; PHORBOL 13 ACETATE 12 MYRISTATE; PHYTOHEMAGGLUTININ; SYNAPTOTAGMIN I; TRANSCRIPTION FACTOR RELA; TUMOR NECROSIS FACTOR ALPHA; I KAPPA B; NF KAPPAB INHIBITOR ALPHA; NF-KAPPAB INHIBITOR ALPHA;

EID: 60049088876     PISSN: None     EISSN: 17424690     Source Type: Journal    
DOI: 10.1186/1742-4690-5-109     Document Type: Article
Times cited : (23)

References (57)
  • 1
    • 0035137882 scopus 로고    scopus 로고
    • Control of oncogenesis and cancer therapy resistance by the transcription factor NF-κB
    • 199203 11160144 10.1172/JCI11991
    • Baldwin AS Control of oncogenesis and cancer therapy resistance by the transcription factor NF-κB J Clin Invest 2001, 107:241-246 199203 11160144 10.1172/JCI11991
    • (2001) J Clin Invest , vol.107 , pp. 241-246
    • Baldwin, A.S.1
  • 2
    • 0031126702 scopus 로고    scopus 로고
    • Rel/NF-kappa B and I kappa B proteins: An overview
    • 10.1006/scbi.1997.0057 9299584
    • May MJ Ghosh S Rel/NF-kappa B and I kappa B proteins: An overview Semin Cancer Biol 1997, 8:63-73 10.1006/scbi.1997.0057 9299584
    • (1997) Semin Cancer Biol , vol.8 , pp. 63-73
    • May, M.J.1    Ghosh, S.2
  • 3
    • 0031126395 scopus 로고    scopus 로고
    • I kappa B proteins: Structure, function and regulation
    • 10.1006/scbi.1997.0058 9299585
    • Whiteside ST Israel A I kappa B proteins: Structure, function and regulation Semin Cancer Biol 1997, 8:75-82 10.1006/scbi.1997.0058 9299585
    • (1997) Semin Cancer Biol , vol.8 , pp. 75-82
    • Whiteside, S.T.1    Israel, A.2
  • 4
    • 0033516464 scopus 로고    scopus 로고
    • 3-deazaadenosine, a S-adenosylhomocysteine hydrolase inhibitor, has dual effects on NF-kappaB regulation. Inhibition of NF-kappaB transcriptional activity and promotion of IkappaBalpha degradation
    • 10.1074/jbc.274.27.18981 10383397
    • Jeong SY Ahn SG Lee JH Kim HS Kim JW Rhim H Jeong SW Kim IK 3-deazaadenosine, a S-adenosylhomocysteine hydrolase inhibitor, has dual effects on NF-kappaB regulation. Inhibition of NF-kappaB transcriptional activity and promotion of IkappaBalpha degradation J Biol Chem 1999, 274:18981-19898 10.1074/jbc.274.27.18981 10383397
    • (1999) J Biol Chem , vol.274 , pp. 18981-19898
    • Jeong, S.Y.1    Ahn, S.G.2    Lee, J.H.3    Kim, H.S.4    Kim, J.W.5    Rhim, H.6    Jeong, S.W.7    Kim, I.K.8
  • 5
    • 0033174072 scopus 로고    scopus 로고
    • Apoptosis overrides survival signals through a caspase-mediated dominant-negative NF-kappa B loop
    • 10.1038/12050 10559921
    • Levkau B Scatena M Giachelli CM Ross R Raines EW Apoptosis overrides survival signals through a caspase-mediated dominant-negative NF-kappa B loop Nat Cell Biol 1999, 1:227-233 10.1038/12050 10559921
    • (1999) Nat Cell Biol , vol.1 , pp. 227-233
    • Levkau, B.1    Scatena, M.2    Giachelli, C.M.3    Ross, R.4    Raines, E.W.5
  • 6
    • 0035816561 scopus 로고    scopus 로고
    • Caspase-3-mediated cleavage of the NF-kappa B subunit p65 at the NH2 terminus potentiates naphthoquinone analog-induced apoptosis
    • 10.1074/jbc.M101291200 11320092
    • Kang KH Lee KH Kim MY Choi KH Caspase-3-mediated cleavage of the NF-kappa B subunit p65 at the NH2 terminus potentiates naphthoquinone analog-induced apoptosis J Biol Chem 2001, 276:24638-24644 10.1074/ jbc.M101291200 11320092
    • (2001) J Biol Chem , vol.276 , pp. 24638-24644
    • Kang, K.H.1    Lee, K.H.2    Kim, M.Y.3    Choi, K.H.4
  • 7
    • 3142771914 scopus 로고    scopus 로고
    • Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor kappaB response
    • 2213320 15226358 10.1084/jem.20040196
    • Saccani S Marazzi I Beg AA Natoli G Degradation of promoter-bound p65/ RelA is essential for the prompt termination of the nuclear factor kappaB response J Exp Med 2004, 200:107-113 2213320 15226358 10.1084/ jem.20040196
    • (2004) J Exp Med , vol.200 , pp. 107-113
    • Saccani, S.1    Marazzi, I.2    Beg, A.A.3    Natoli, G.4
  • 8
    • 21244499051 scopus 로고    scopus 로고
    • Proteolytic cleavage of the p65-RelA subunit of NF-kappaB during poliovirus infection
    • 10.1074/jbc.M502303200 15845545
    • Neznanov N Chumakov KM Neznanova L Almasan A Banerjee AK Gudkov AV Proteolytic cleavage of the p65-RelA subunit of NF-kappaB during poliovirus infection J Biol Chem 2005, 280:24153-24158 10.1074/ jbc.M502303200 15845545
    • (2005) J Biol Chem , vol.280 , pp. 24153-24158
    • Neznanov, N.1    Chumakov, K.M.2    Neznanova, L.3    Almasan, A.4    Banerjee, A.K.5    Gudkov, A.V.6
  • 9
    • 0038771214 scopus 로고    scopus 로고
    • Modulation of NF-kappaB activity by exchange of dimers
    • 10.1016/S1097-2765(03)00227-2 12820969
    • Saccani S Pantano S Natoli G Modulation of NF-kappaB activity by exchange of dimers Mol Cell 2003, 11:1563-1574 10.1016/ S1097-2765(03)00227-2 12820969
    • (2003) Mol Cell , vol.11 , pp. 1563-1574
    • Saccani, S.1    Pantano, S.2    Natoli, G.3
  • 10
    • 0035139943 scopus 로고    scopus 로고
    • Hostile takeovers: Viral appropriation of the NF-kappaB pathway
    • 199181 11160127 10.1172/JCI11918
    • Hiscott J Kwon H Genin P Hostile takeovers: Viral appropriation of the NF-kappaB pathway J Clin Invest 2001, 107:143-151 199181 11160127 10.1172/JCI11918
    • (2001) J Clin Invest , vol.107 , pp. 143-151
    • Hiscott, J.1    Kwon, H.2    Genin, P.3
  • 11
    • 0023176085 scopus 로고
    • An inducible transcription factor activates expression of human immunodeficiency virus in T cells
    • 10.1038/326711a0 3031512
    • Nabel G Baltimore D An inducible transcription factor activates expression of human immunodeficiency virus in T cells Nature 1987, 326:711-713 10.1038/326711a0 3031512
    • (1987) Nature , vol.326 , pp. 711-713
    • Nabel, G.1    Baltimore, D.2
  • 12
    • 0029874138 scopus 로고    scopus 로고
    • The NF-kappa B and I kappa B proteins: New discoveries and insights
    • 10.1146/annurev.immunol.14.1.649 8717528
    • Baldwin AS Jr The NF-kappa B and I kappa B proteins: New discoveries and insights Annu Rev Immunol 1996, 14:649-681 10.1146/ annurev.immunol.14.1.649 8717528
    • (1996) Annu Rev Immunol , vol.14 , pp. 649-681
    • Baldwin Jr., A.S.1
  • 14
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-κB in preventing TNF-α-induced cell death
    • 10.1126/science.274.5288.782 8864118
    • Beg AA Baltimore D An essential role for NF-κB in preventing TNF-α-induced cell death Science 1996, 274:782-784 10.1126/ science.274.5288.782 8864118
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, A.A.1    Baltimore, D.2
  • 15
    • 0033947601 scopus 로고    scopus 로고
    • The pro- or anti-apoptotic function of NF-kappaB is determined by the nature of the apoptotic stimulus
    • 10.1046/j.1432-1327.2000.01421.x 10849002
    • Kaltschmidt B Kaltschmidt C Hofmann TG Hehner SP Dröge W Schmitz ML The pro- or anti-apoptotic function of NF-kappaB is determined by the nature of the apoptotic stimulus Eur J Biochem 2000, 267:3828-3835 10.1046/j.1432-1327.2000.01421.x 10849002
    • (2000) Eur J Biochem , vol.267 , pp. 3828-3835
    • Kaltschmidt, B.1    Kaltschmidt, C.2    Hofmann, T.G.3    Hehner, S.P.4    Dröge, W.5    Schmitz, M.L.6
  • 16
    • 0032032627 scopus 로고    scopus 로고
    • CD95 (Fas)-induced caspase-mediated proteolysis of NF-κB
    • 9500443
    • Ravi R Bedi A Fuchs EJ Bedi A CD95 (Fas)-induced caspase-mediated proteolysis of NF-κB Cancer Res 1998, 58:882-886 9500443
    • (1998) Cancer Res , vol.58 , pp. 882-886
    • Ravi, R.1    Bedi, A.2    Fuchs, E.J.3    Bedi, A.4
  • 18
    • 0028318159 scopus 로고
    • Leptomycin B targets a regulatory cascade of crm1, a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression
    • 8119981
    • Nishi K Yoshida M Fujiwara D Nishikawa M Horinouchi S Beppu T Leptomycin B targets a regulatory cascade of crm1, a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression J Biol Chem 1994, 269:6320-6324 8119981
    • (1994) J Biol Chem , vol.269 , pp. 6320-6324
    • Nishi, K.1    Yoshida, M.2    Fujiwara, D.3    Nishikawa, M.4    Horinouchi, S.5    Beppu, T.6
  • 19
    • 0032536519 scopus 로고    scopus 로고
    • Caspases are activated in a branched protease cascade & control distinct downstream processes in Fas-induced apoptosis
    • 2212161 9463409 10.1084/jem.187.4.587
    • Hirata H Takahashi A Kobayashi S Yonehara S Sawai H Okazaki T Yamamoto K Sasada M Caspases are activated in a branched protease cascade & control distinct downstream processes in Fas-induced apoptosis J Exp Med 1998, 187:587-600 2212161 9463409 10.1084/jem.187.4.587
    • (1998) J Exp Med , vol.187 , pp. 587-600
    • Hirata, H.1    Takahashi, A.2    Kobayashi, S.3    Yonehara, S.4    Sawai, H.5    Okazaki, T.6    Yamamoto, K.7    Sasada, M.8
  • 20
    • 0029894283 scopus 로고    scopus 로고
    • Activation of the CPP32 apoptotic protease by distinct signaling pathways with differential sensitivity to Bcl-xL
    • 10.1074/jbc.271.30.17601 8663611
    • Erhardt P Cooper GM Activation of the CPP32 apoptotic protease by distinct signaling pathways with differential sensitivity to Bcl-xL J Biol Chem 1996, 271:17601-17604 10.1074/jbc.271.30.17601 8663611
    • (1996) J Biol Chem , vol.271 , pp. 17601-17604
    • Erhardt, P.1    Cooper, G.M.2
  • 21
    • 0041666520 scopus 로고    scopus 로고
    • Caspase-3 activation is an early event and initiates apoptotic damage in a human leukemia cell line
    • 10.1023/A:1024121017841 12815279
    • Varghese J Khandre NS Sarin A Caspase-3 activation is an early event and initiates apoptotic damage in a human leukemia cell line Apoptosis 2003, 8:363-370 10.1023/A:1024121017841 12815279
    • (2003) Apoptosis , vol.8 , pp. 363-370
    • Varghese, J.1    Khandre, N.S.2    Sarin, A.3
  • 22
    • 0026652879 scopus 로고
    • The RxxRxRxxC motif conserved in all Rel/kappa B proteins is essential for the DNA-binding activity and redox regulation of the v-Rel oncoprotein
    • 364524 1620118
    • Kumar S Rabson AB Gelinas C The RxxRxRxxC motif conserved in all Rel/ kappa B proteins is essential for the DNA-binding activity and redox regulation of the v-Rel oncoprotein Mol Cell Biol 1992, 12:3094-3106 364524 1620118
    • (1992) Mol Cell Biol , vol.12 , pp. 3094-3106
    • Kumar, S.1    Rabson, A.B.2    Gelinas, C.3
  • 23
    • 0037482136 scopus 로고    scopus 로고
    • X-ray crystal structure of an IkappaBbeta·NF-kappaB p65 homodimer complex
    • 10.1074/jbc.M301022200 12686541
    • Malek S Huang DB Huxford T Ghosh S Ghosh G X-ray crystal structure of an IkappaBbeta·NF-kappaB p65 homodimer complex J Biol Chem 2003, 278:23094-23100 10.1074/jbc.M301022200 12686541
    • (2003) J Biol Chem , vol.278 , pp. 23094-23100
    • Malek, S.1    Huang, D.B.2    Huxford, T.3    Ghosh, S.4    Ghosh, G.5
  • 24
    • 0034040118 scopus 로고    scopus 로고
    • Reservoirs for HIV-1: Mechanisms for viral persistence in the presence of antiviral immune responses and antiretroviral therapy
    • 10.1146/annurev.immunol.18.1.665 10837072
    • Pierson T McArthur J Siliciano RF Reservoirs for HIV-1: Mechanisms for viral persistence in the presence of antiviral immune responses and antiretroviral therapy Annu Rev Immunol 2000, 18:665-708 10.1146/ annurev.immunol.18.1.665 10837072
    • (2000) Annu Rev Immunol , vol.18 , pp. 665-708
    • Pierson, T.1    McArthur, J.2    Siliciano, R.F.3
  • 26
    • 0024428086 scopus 로고
    • The NF-kappa B binding sites in the human immunodeficiency virus type 1 long terminal repeat are not required for virus infectivity
    • 251138 2795721
    • Leonard J Parrott C Buckler-White AJ Turner W Ross EK Martin MA Rabson AB The NF-kappa B binding sites in the human immunodeficiency virus type 1 long terminal repeat are not required for virus infectivity J Virol 1989, 63:4919-4924 251138 2795721
    • (1989) J Virol , vol.63 , pp. 4919-4924
    • Leonard, J.1    Parrott, C.2    Buckler-White, A.J.3    Turner, W.4    Ross, E.K.5    Martin, M.A.6    Rabson, A.B.7
  • 28
    • 0027209915 scopus 로고
    • A cooperative interaction between NF-kappa B and Sp1 is required for HIV enhancer activation
    • 413631 8253080
    • Perkins ND Edwards NL Duckett CS Agranoff AB Schmid RM Nabel GJ A cooperative interaction between NF-kappa B and Sp1 is required for HIV enhancer activation EMBO J 1993, 12:3551-3558 413631 8253080
    • (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    Nabel, G.J.6
  • 29
    • 0036892507 scopus 로고    scopus 로고
    • Novel effects of neutrophil-derived proteinase 3 and elastase on the vascular endothelium involve in vivo cleavage of NF-kappaB and proapoptotic changes in JNK, ERK, and p38 MAPK signaling pathways
    • 10.1097/01.ASN.0000034911.03334.C3 12444202
    • Preston GA Zarella CS Pendergraft WF 3rd Rudolph EH Yang JJ Sekura SB Jennette JC Falk RJ Novel effects of neutrophil-derived proteinase 3 and elastase on the vascular endothelium involve in vivo cleavage of NF-kappaB and proapoptotic changes in JNK, ERK, and p38 MAPK signaling pathways J Am Soc Nephrol 2002, 13:2840-2849 10.1097/ 01.ASN.0000034911.03334.C3 12444202
    • (2002) J Am Soc Nephrol , vol.13 , pp. 2840-2849
    • Preston, G.A.1    Zarella, C.S.2    Pendergraft III, W.F.3    Rudolph, E.H.4    Yang, J.J.5    Sekura, S.B.6    Jennette, J.C.7    Falk, R.J.8
  • 30
    • 0034665797 scopus 로고    scopus 로고
    • A caspase-3-like protease is involved in NF-kappaB activation induced by stimulation of N-methyl-D-aspartate receptors in rat striatum
    • 10.1016/S0169-328X(00)00147-9 11038244
    • Qin Z Wang Y Chasea TN A caspase-3-like protease is involved in NF-kappaB activation induced by stimulation of N-methyl-D-aspartate receptors in rat striatum Brain Res Mol Brain Res 2000, 80:111-122 10.1016/S0169-328X(00)00147-9 11038244
    • (2000) Brain Res Mol Brain Res , vol.80 , pp. 111-122
    • Qin, Z.1    Wang, Y.2    Chasea, T.N.3
  • 31
    • 22244449642 scopus 로고    scopus 로고
    • Caspase-mediated p65 cleavage promotes TRAIL-induced apoptosis
    • 10.1158/0008-5472.CAN-05-0472 16024612
    • Kim HS Chang I Kim JY Choi KH Lee MS Caspase-mediated p65 cleavage promotes TRAIL-induced apoptosis Cancer Res 2005, 65:6111-6119 10.1158/ 0008-5472.CAN-05-0472 16024612
    • (2005) Cancer Res , vol.65 , pp. 6111-6119
    • Kim, H.S.1    Chang, I.2    Kim, J.Y.3    Choi, K.H.4    Lee, M.S.5
  • 32
    • 0036479137 scopus 로고    scopus 로고
    • Phorbol 12-myristate 13-acetate inhibits death receptor-mediated apoptosis in Jurkat cells by disrupting recruitment of Fas-associated polypeptide with death domain
    • 10.1074/jbc.M107218200 11729181
    • Meng XW Heldebrant MP Kaufmann SH Phorbol 12-myristate 13-acetate inhibits death receptor-mediated apoptosis in Jurkat cells by disrupting recruitment of Fas-associated polypeptide with death domain J Biol Chem 2002, 277:3776-3783 10.1074/jbc.M107218200 11729181
    • (2002) J Biol Chem , vol.277 , pp. 3776-3783
    • Meng, X.W.1    Heldebrant, M.P.2    Kaufmann, S.H.3
  • 33
    • 0038514192 scopus 로고    scopus 로고
    • Combined action of ERK, NF kappa B mediates the protective effect of phorbol ester on Fas-induced apoptosis in Jurkat cells
    • 10.1074/jbc.M211556200 12551910
    • Engedal N Blomhoff HK Combined action of ERK, NF kappa B mediates the protective effect of phorbol ester on Fas-induced apoptosis in Jurkat cells J Biol Chem 2003, 278:10934-10941 10.1074/jbc.M211556200 12551910
    • (2003) J Biol Chem , vol.278 , pp. 10934-10941
    • Engedal, N.1    Blomhoff, H.K.2
  • 34
    • 0031929815 scopus 로고    scopus 로고
    • Activation of caspase-3-like enzymes in non-apoptotic T cells
    • 10.1002/(SICI)1521-4141(199803)28:03<891::AID-IMMU891>3.0.CO;2-X
    • Wilhelm S Wagner H Häcker G Activation of caspase-3-like enzymes in non-apoptotic T cells Eur J Immunol 1998, 28:891-900 10.1002/ (SICI)1521-4141(199803)28:03<891::AID-IMMU891>3.0.CO;2-X 9541584
    • (1998) Eur J Immunol , vol.28 , pp. 891-900
    • Wilhelm, S.1    Wagner, H.2    Häcker, G.3
  • 35
    • 0033378016 scopus 로고    scopus 로고
    • Early activation of caspases during T lymphocyte stimulation results in selective substrate cleavage in nonapoptotic cells
    • 2195712 10601362 10.1084/jem.190.12.1879
    • Alam A Cohen LY Aouad S Sékaly RP Early activation of caspases during T lymphocyte stimulation results in selective substrate cleavage in nonapoptotic cells J Exp Med 1999, 190:1879-1890 2195712 10601362 10.1084/jem.190.12.1879
    • (1999) J Exp Med , vol.190 , pp. 1879-1890
    • Alam, A.1    Cohen, L.Y.2    Aouad, S.3    Sékaly, R.P.4
  • 36
    • 0033386808 scopus 로고    scopus 로고
    • Caspase activation is required for T cell proliferation
    • 2195711 10601363 10.1084/jem.190.12.1891
    • Kennedy NJ Kataoka T Tschopp J Budd RC Caspase activation is required for T cell proliferation J Exp Med 1999, 190:1891-1896 2195711 10601363 10.1084/jem.190.12.1891
    • (1999) J Exp Med , vol.190 , pp. 1891-1896
    • Kennedy, N.J.1    Kataoka, T.2    Tschopp, J.3    Budd, R.C.4
  • 38
    • 12544256390 scopus 로고    scopus 로고
    • Nuclear translocation of caspase-3 is dependent on its proteolytic activation and recognition of a substrate-like proteins
    • 10.1074/jbc.C400538200 15569692
    • Kamada S Kikkawa U Tsujimoto Y Hunter T Nuclear translocation of caspase-3 is dependent on its proteolytic activation and recognition of a substrate-like proteins J Biol Chem 2004, 280:857-860 10.1074/ jbc.C400538200 15569692
    • (2004) J Biol Chem , vol.280 , pp. 857-860
    • Kamada, S.1    Kikkawa, U.2    Tsujimoto, Y.3    Hunter, T.4
  • 39
    • 0035349737 scopus 로고    scopus 로고
    • Protein kinase C activation by PMA rapidly induces apoptosis through caspase-3/CPP32 and serine proteases in a gastric cancer cell line
    • 11295059
    • Park IC Park MJ Rhee CH Lee JI Choe TB Jang JJ Lee SH Hong SI Protein kinase C activation by PMA rapidly induces apoptosis through caspase-3/ CPP32 and serine proteases in a gastric cancer cell line Int J Oncol 2001, 18:1077-1083 11295059
    • (2001) Int J Oncol , vol.18 , pp. 1077-1083
    • Park, I.C.1    Park, M.J.2    Rhee, C.H.3    Lee, J.I.4    Choe, T.B.5    Jang, J.J.6    Lee, S.H.7    Hong, S.I.8
  • 40
    • 0030994236 scopus 로고    scopus 로고
    • Evidence for CPP32 activation in the absence of apoptosis during T lymphocyte stimulation
    • 10.1074/jbc.272.21.13459 9153186
    • Miossec C Dutilleul V Fassy F Diu-Hercend A Evidence for CPP32 activation in the absence of apoptosis during T lymphocyte stimulation J Biol Chem 1997, 272:13459-13462 10.1074/jbc.272.21.13459 9153186
    • (1997) J Biol Chem , vol.272 , pp. 13459-13462
    • Miossec, C.1    Dutilleul, V.2    Fassy, F.3    Diu-Hercend, A.4
  • 41
    • 0032505751 scopus 로고    scopus 로고
    • Caspase-3-like activity is necessary for IL-2 release in activated Jurkat T-cells
    • 10.1006/excr.1998.4214 9770373
    • Posmantur R Wang KK Gilbertsen RB Caspase-3-like activity is necessary for IL-2 release in activated Jurkat T-cells Exp Cell Res 1998, 244:302-309 10.1006/excr.1998.4214 9770373
    • (1998) Exp Cell Res , vol.244 , pp. 302-309
    • Posmantur, R.1    Wang, K.K.2    Gilbertsen, R.B.3
  • 42
    • 0034801392 scopus 로고    scopus 로고
    • Caspase-mediated calcineurin activation contributes to IL-2 release during T cell activation
    • 10.1006/bbrc.2001.5278 11478781
    • Mukerjee N McGinnis KM Gnegy ME Wang KK Caspase-mediated calcineurin activation contributes to IL-2 release during T cell activation Biochem Biophys Res Commun 2001, 285:1192-1199 10.1006/bbrc.2001.5278 11478781
    • (2001) Biochem Biophys Res Commun , vol.285 , pp. 1192-1199
    • Mukerjee, N.1    McGinnis, K.M.2    Gnegy, M.E.3    Wang, K.K.4
  • 43
    • 0033565406 scopus 로고    scopus 로고
    • Inhibition of NF-kappa B activity in human T lymphocytes induces caspase-dependent apoptosis without detectable activation of caspase-1, -3
    • 10395645
    • Kolenko V Bloom T Rayman P Bukowski R His E Finke J Inhibition of NF-kappa B activity in human T lymphocytes induces caspase-dependent apoptosis without detectable activation of caspase-1, -3 J Immunol 1999, 163:590-598 10395645
    • (1999) J Immunol , vol.163 , pp. 590-598
    • Kolenko, V.1    Bloom, T.2    Rayman, P.3    Bukowski, R.4    His, E.5    Finke, J.6
  • 44
    • 0032556894 scopus 로고    scopus 로고
    • Crystal structure of p50/p65 heterodimer of transcription factor NF-kappaB bound to DNA
    • 10.1038/34356 9450761
    • Chen FE Huang DB Chen YQ Ghosh G Crystal structure of p50/p65 heterodimer of transcription factor NF-kappaB bound to DNA Nature 1998, 391:410-413 10.1038/34356 9450761
    • (1998) Nature , vol.391 , pp. 410-413
    • Chen, F.E.1    Huang, D.B.2    Chen, Y.Q.3    Ghosh, G.4
  • 45
    • 0027404184 scopus 로고
    • Mutational analysis of the p50 subunit of NF-kappa B and inhibition of NF-kappa B activity by trans-dominant p50 mutants
    • 237362 8416374
    • Bressler P Brown K Timmer W Bours V Siebenlist U Fauci AS Mutational analysis of the p50 subunit of NF-kappa B and inhibition of NF-kappa B activity by trans-dominant p50 mutants J Virol 1993, 67:288-293 237362 8416374
    • (1993) J Virol , vol.67 , pp. 288-293
    • Bressler, P.1    Brown, K.2    Timmer, W.3    Bours, V.4    Siebenlist, U.5    Fauci, A.S.6
  • 46
    • 34748850130 scopus 로고    scopus 로고
    • Basal shuttle of NF-kappaB/I kappaB alpha in resting T lymphocytes regulates HIV-1 LTR dependent expression
    • 1988826 17686171 10.1186/1742-4690-4-56
    • Coiras M López-Huertas MR Rullas J Mittelbrunn M Alcamí J Basal shuttle of NF-kappaB/I kappaB alpha in resting T lymphocytes regulates HIV-1 LTR dependent expression Retrovirology 2007, 4:56 1988826 17686171 10.1186/1742-4690-4-56
    • (2007) Retrovirology , vol.4 , pp. 56
    • Coiras, M.1    López-Huertas, M.R.2    Rullas, J.3    Mittelbrunn, M.4    Alcamí, J.5
  • 47
    • 0142105387 scopus 로고    scopus 로고
    • Genetic analysis of NF-kappaB/Rel transcription factors defines functional specificities
    • 213788 14532125 10.1093/emboj/cdg534
    • Hoffmann A Leung TH Baltimore D Genetic analysis of NF-kappaB/Rel transcription factors defines functional specificities EMBO J 2003, 22:5530-5539 213788 14532125 10.1093/emboj/cdg534
    • (2003) EMBO J , vol.22 , pp. 5530-5539
    • Hoffmann, A.1    Leung, T.H.2    Baltimore, D.3
  • 48
    • 0028986046 scopus 로고
    • Domain organization of I kappa B alpha and sites of interaction with NF-kappa B p65
    • 230444 7891711
    • Jaffray E Wood KM Hay RT Domain organization of I kappa B alpha and sites of interaction with NF-kappa B p65 Mol Cell Biol 1995, 15:2166-2172 230444 7891711
    • (1995) Mol Cell Biol , vol.15 , pp. 2166-2172
    • Jaffray, E.1    Wood, K.M.2    Hay, R.T.3
  • 49
    • 0027519680 scopus 로고
    • Phosphatidylcholine hydrolysis activates NF-kappa B, increases human immunodeficiency virus replication in human monocytes, T lymphocytes
    • 238097 8411362
    • Arenzana-Seisdedos F Fernandez B Dominguez I Jacque JM Thomas D Diaz-Meco MT Moscat J Virelizier JL Phosphatidylcholine hydrolysis activates NF-kappa B, increases human immunodeficiency virus replication in human monocytes, T lymphocytes J Virol 1993, 67:6596-6604 238097 8411362
    • (1993) J Virol , vol.67 , pp. 6596-6604
    • Arenzana-Seisdedos, F.1    Fernandez, B.2    Dominguez, I.3    Jacque, J.M.4    Thomas, D.5    Diaz-Meco, M.T.6    Moscat, J.7    Virelizier, J.L.8
  • 50
    • 0020531610 scopus 로고
    • High efficiency DNA-mediated transformation of primate cells
    • 10.1126/science.6306768 6306768
    • Gorman C Padmanabhan R Howard BH High efficiency DNA-mediated transformation of primate cells Science 1983, 221:551-553 10.1126/ science.6306768 6306768
    • (1983) Science , vol.221 , pp. 551-553
    • Gorman, C.1    Padmanabhan, R.2    Howard, B.H.3
  • 51
    • 0025738076 scopus 로고
    • Cloning of an NF-kappa B subunit which stimulates HIV transcription in synergy with p65
    • 10.1038/352733a0 1876189
    • Schmid RM Perkins ND Duckett CS Andrews PC Nabel GJ Cloning of an NF-kappa B subunit which stimulates HIV transcription in synergy with p65 Nature 1991, 352:733-736 10.1038/352733a0 1876189
    • (1991) Nature , vol.352 , pp. 733-736
    • Schmid, R.M.1    Perkins, N.D.2    Duckett, C.S.3    Andrews, P.C.4    Nabel, G.J.5
  • 52
    • 0022495870 scopus 로고
    • Production of acquired immunodeficiency syndrome-associated retrovirus in human and non-human cells transfected with an infectious molecular clone
    • Adachi A Gendelman HE Koening S Folks T Willey R Rabson A Martin MA Production of acquired immunodeficiency syndrome-associated retrovirus in human and non-human cells transfected with an infectious molecular clone J Virol 1988, 59:284-291
    • (1988) J Virol , vol.59 , pp. 284-291
    • Adachi, A.1    Gendelman, H.E.2    Koening, S.3    Folks, T.4    Willey, R.5    Rabson, A.6    Martin, M.A.7
  • 53
    • 33845974053 scopus 로고    scopus 로고
    • A new strategy based on recombinant viruses as a tool for assessing drug susceptibility of human Immunodeficiency virus type 1
    • 10.1002/jmv.20770 17177310
    • Garcia-Perez J Sanchez-Palomino S Perez-Olmeda M Fernandez B Alcami J A new strategy based on recombinant viruses as a tool for assessing drug susceptibility of human Immunodeficiency virus type 1 J Med Virol 2007, 79:127-137 10.1002/jmv.20770 17177310
    • (2007) J Med Virol , vol.79 , pp. 127-137
    • Garcia-Perez, J.1    Sanchez-Palomino, S.2    Perez-Olmeda, M.3    Fernandez, B.4    Alcami, J.5
  • 55
    • 0018247640 scopus 로고
    • Biochemical transfer of single-copy eucaryotic genes using total cellular DNA as donor
    • 10.1016/0092-8674(78)90254-4 210957
    • Wigler M Pellicer A Silverstein S Axel R Biochemical transfer of single-copy eucaryotic genes using total cellular DNA as donor Cell 1978, 14:725-731 10.1016/0092-8674(78)90254-4 210957
    • (1978) Cell , vol.14 , pp. 725-731
    • Wigler, M.1    Pellicer, A.2    Silverstein, S.3    Axel, R.4
  • 56
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 10.1016/0003-2697(76)90527-3 942051
    • Bradford MM A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal Biochem 1976, 72:248-254 10.1016/0003-2697(76)90527-3 942051
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1


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