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Volumn 9, Issue 8, 1998, Pages 1995-2010

IκB is a substrate for a selective pathway of lysosomal proteolysis

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; RECEPTOR PROTEIN; TRANSCRIPTION FACTOR; DNA BINDING PROTEIN; HYBRID PROTEIN; I KAPPA B; LAMP2 PROTEIN, HUMAN; LEUKOCYTE ANTIGEN; LYSOSOME ASSOCIATED MEMBRANE PROTEIN; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2; MEMBRANE PROTEIN; NF KAPPAB INHIBITOR ALPHA; NF-KAPPAB INHIBITOR ALPHA; UBIQUITIN;

EID: 0031595780     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.9.8.1995     Document Type: Article
Times cited : (134)

References (55)
  • 1
    • 0030586233 scopus 로고    scopus 로고
    • LAPTM5: A novel lysosomal-associated multispanning membrane protein preferentially expressed in hematopoietic cells
    • Adra, C.N., Zhu, S., Ko, J-L., et al. (1996). LAPTM5: a novel lysosomal-associated multispanning membrane protein preferentially expressed in hematopoietic cells. Genomics 35, 328-337.
    • (1996) Genomics , vol.35 , pp. 328-337
    • Adra, C.N.1    Zhu, S.2    Ko, J.-L.3
  • 2
    • 0030923854 scopus 로고    scopus 로고
    • Requirement for an intralysosomal hsc73 for a selective pathway of lysosomal proteolysis
    • Agarraberes, F., Terlecky, S.R., and Dice, J.F. (1997). Requirement for an intralysosomal hsc73 for a selective pathway of lysosomal proteolysis. J. Cell Biol. 137, 825-834.
    • (1997) J. Cell Biol. , vol.137 , pp. 825-834
    • Agarraberes, F.1    Terlecky, S.R.2    Dice, J.F.3
  • 3
    • 0028970734 scopus 로고
    • Stimulation-dependent IκBα phosphorylation marks the NF-κB inhibitor for degradation via the ubiquitin-proteasome pathway
    • Alkalay, L, Yaron, A., Hatzubai, A., Orian, A., Ciechanover, A., and Ben-Neriah, Y. (1995). Stimulation-dependent IκBα phosphorylation marks the NF-κB inhibitor for degradation via the ubiquitin-proteasome pathway. Proc. Natl. Acad. Sci. USA 92, 10599-10603.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10599-10603
    • Alkalay, L.1    Yaron, A.2    Hatzubai, A.3    Orian, A.4    Ciechanover, A.5    Ben-Neriah, Y.6
  • 4
    • 0027280820 scopus 로고
    • Uptake and degradation of glyceraldehyde-3-phosphate dehydrogenase by rat liver lysosomes
    • Aniento, F., Roche, E., Cuervo, A.M., and Knecht, E. (1993). Uptake and degradation of glyceraldehyde-3-phosphate dehydrogenase by rat liver lysosomes. J. Biol. Chem. 268, 10463-1070.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10463-11070
    • Aniento, F.1    Roche, E.2    Cuervo, A.M.3    Knecht, E.4
  • 5
    • 0030586367 scopus 로고    scopus 로고
    • Selective uptake and degradation of c-fos and v-fos by rat liver lysosomes
    • Aniento, F., Papavassiliou, A.G., Knecht, E., and Roche, E. (1996). Selective uptake and degradation of c-fos and v-fos by rat liver lysosomes. FEES Lett. 390, 47-52.
    • (1996) FEES Lett. , vol.390 , pp. 47-52
    • Aniento, F.1    Papavassiliou, A.G.2    Knecht, E.3    Roche, E.4
  • 6
    • 0030271387 scopus 로고    scopus 로고
    • NF-kappa B: Ten years after
    • Baeuerle, P.A., and Baltimore, D. (1996). NF-kappa B: ten years after. Cell 87, 13-20.
    • (1996) Cell , vol.87 , pp. 13-20
    • Baeuerle, P.A.1    Baltimore, D.2
  • 7
    • 0028174061 scopus 로고
    • Function and activation of NF-κB in the immune system
    • Baeuerle, P.A., and Henker, T. (1994). Function and activation of NF-κB in the immune system. Annu. Rev. Immunol. 12, 141-179.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henker, T.2
  • 8
    • 0029874138 scopus 로고    scopus 로고
    • The NF-kappa B and I kappa B proteins: New discoveries and insights
    • Baldwin, A.S., Jr. (1996). The NF-kappa B and I kappa B proteins: new discoveries and insights. Annu. Rev. Immunol. 14, 649-683.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 649-683
    • Baldwin Jr., A.S.1
  • 9
    • 0029059060 scopus 로고
    • Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-κB
    • Beg, A.A., Sha, W.C., Bronson, R.T., Ghosh, S., and Baltimore, D. (1995). Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-κB. Nature 376, 167-170.
    • (1995) Nature , vol.376 , pp. 167-170
    • Beg, A.A.1    Sha, W.C.2    Bronson, R.T.3    Ghosh, S.4    Baltimore, D.5
  • 10
    • 0016203040 scopus 로고
    • A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels
    • Bonner, W.N., and Laskey, R.A. (1974). A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur. J. Biochem. 46, 83-85.
    • (1974) Eur. J. Biochem. , vol.46 , pp. 83-85
    • Bonner, W.N.1    Laskey, R.A.2
  • 11
    • 0016367845 scopus 로고
    • Isolation of lysosomes from lymphoid tissues
    • Bowers, W.E. (1974). Isolation of lysosomes from lymphoid tissues. Methods Enzymol. 31, 353-356.
    • (1974) Methods Enzymol. , vol.31 , pp. 353-356
    • Bowers, W.E.1
  • 12
    • 0031570757 scopus 로고    scopus 로고
    • Calpain contributes to silica-induced IκB-alpha degradation and nuclear factor-κB activation
    • Chen, F., Lu, Y., Kuhn, D.C., Maki, M., Shi, X., Sun, S-C., and Demers, L.M. (1997). Calpain contributes to silica-induced IκB-alpha degradation and nuclear factor-κB activation. Arch. Biochem. Biophys. 342, 383-388.
    • (1997) Arch. Biochem. Biophys. , vol.342 , pp. 383-388
    • Chen, F.1    Lu, Y.2    Kuhn, D.C.3    Maki, M.4    Shi, X.5    Sun, S.-C.6    Demers, L.M.7
  • 13
    • 0023891846 scopus 로고
    • Peptide sequences that target proteins for enhanced degradation during serum withdrawal
    • Chiang, H.-L., and Dice, J.F. (1988). Peptide sequences that target proteins for enhanced degradation during serum withdrawal. J. Biol. Chem. 263, 6797-6805.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6797-6805
    • Chiang, H.-L.1    Dice, J.F.2
  • 14
    • 0024975155 scopus 로고
    • A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins
    • Chiang, H.-L., Terlecky, S.R., Plant, C.P., and Dice, J.F. (1989). A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 246, 382-385.
    • (1989) Science , vol.246 , pp. 382-385
    • Chiang, H.-L.1    Terlecky, S.R.2    Plant, C.P.3    Dice, J.F.4
  • 15
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo, A.M., and Dice, J.F. (1996). A receptor for the selective uptake and degradation of proteins by lysosomes. Science 273, 501-503.
    • (1996) Science , vol.273 , pp. 501-503
    • Cuervo, A.M.1    Dice, J.F.2
  • 16
    • 0031041902 scopus 로고    scopus 로고
    • A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins
    • Cuervo, A.M., Dice, J.F., and Knecht, E. (1997a). A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins. J. Biol. Chem. 272, 5606-5615.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5606-5615
    • Cuervo, A.M.1    Dice, J.F.2    Knecht, E.3
  • 17
    • 0013521519 scopus 로고    scopus 로고
    • Molecular chaperones and intracellular protein degradation with emphasis on a selective lysosomal pathway of proteolysis
    • ed. A.L. Fink and J. Goto, New York: Marcel Dekker
    • Cuervo, A.M., Hayes, S.A., and Dice, J.F. (1997b). Molecular chaperones and intracellular protein degradation with emphasis on a selective lysosomal pathway of proteolysis. In: Structure and Function of Molecular Chaperones: The Role of Chaperones in the Life Cycle of Proteins, ed. A.L. Fink and J. Goto, New York: Marcel Dekker, 491-509.
    • (1997) Structure and Function of Molecular Chaperones: The Role of Chaperones in the Life Cycle of Proteins , pp. 491-509
    • Cuervo, A.M.1    Hayes, S.A.2    Dice, J.F.3
  • 18
    • 0028848119 scopus 로고
    • Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation
    • Cuervo, A.M., Knecht, E., Terlecky, S.R., and Dice, J.F. (1995a). Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation. Am. J. Physiol. 269, C1200-C1208.
    • (1995) Am. J. Physiol. , vol.269
    • Cuervo, A.M.1    Knecht, E.2    Terlecky, S.R.3    Dice, J.F.4
  • 19
    • 0028797005 scopus 로고
    • Degradation of proteasomes by lysosomes in rat liver
    • Cuervo, A.M., Palmer, A., Rivett, A.J., and Knecht, E. (1995b). Degradation of proteasomes by lysosomes in rat liver. Eur. J. Biochem. 227, 792-800.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 792-800
    • Cuervo, A.M.1    Palmer, A.2    Rivett, A.J.3    Knecht, E.4
  • 20
    • 0027944153 scopus 로고
    • Selective binding and uptake of ribonuclease a and glyceraldehyde-3-phosphate dehydrogenase by isolated rat liver lysosomes
    • Cuervo, A.M., Terlecky, S.R., Dice, J.F., and Knecht, E. (1994). Selective binding and uptake of ribonuclease A and glyceraldehyde-3-phosphate dehydrogenase by isolated rat liver lysosomes. J. Biol. Chem. 269, 26374-26380.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26374-26380
    • Cuervo, A.M.1    Terlecky, S.R.2    Dice, J.F.3    Knecht, E.4
  • 21
    • 0025294506 scopus 로고
    • Peptide sequences that target cytosolic proteins for lysosomal proteolysis
    • Dice, J.F. (1990). Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends. Biochem. Sci. 15, 305-309.
    • (1990) Trends. Biochem. Sci. , vol.15 , pp. 305-309
    • Dice, J.F.1
  • 23
    • 0028222874 scopus 로고
    • Autophagy and related mechanisms of lysosome-mediated protein degradation
    • Dunn, W.A. (1994). Autophagy and related mechanisms of lysosome-mediated protein degradation. Trends Cell Biol. 4, 139-143.
    • (1994) Trends Cell Biol. , vol.4 , pp. 139-143
    • Dunn, W.A.1
  • 24
    • 0024238385 scopus 로고
    • Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Comparison of their deduced amino acid sequences
    • Fukuda, M., Viitala, J., Matteson, J., and Carlsson, S.R. (1988). Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Comparison of their deduced amino acid sequences. J. Biol. Chem. 263, 18920-18928.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18920-18928
    • Fukuda, M.1    Viitala, J.2    Matteson, J.3    Carlsson, S.R.4
  • 25
    • 0029999656 scopus 로고    scopus 로고
    • Bcl-2 down-regulates the activity of transcription factor NF-κB induced upon apoptosis
    • Grimm, S., Bauer, M.K.A., Baeuerle, P.A., and Schulze-Osthoff, K. (1996). Bcl-2 down-regulates the activity of transcription factor NF-κB induced upon apoptosis. J. Cell Biol. 134, 13-23.
    • (1996) J. Cell Biol. , vol.134 , pp. 13-23
    • Grimm, S.1    Bauer, M.K.A.2    Baeuerle, P.A.3    Schulze-Osthoff, K.4
  • 27
    • 0020669729 scopus 로고
    • Protein labeling by reductive alkylation
    • Jentoft, N., and Dearborn, D.G. (1983). Protein labeling by reductive alkylation. Methods Enzymol. 91, 570-579.
    • (1983) Methods Enzymol. , vol.91 , pp. 570-579
    • Jentoft, N.1    Dearborn, D.G.2
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0026690834 scopus 로고
    • Ubiquitin-activating enzyme, E1, is associated with maturation of autophagic vacuoles
    • Lenk, S.E., Dunn, W.A., Trausch, J.S., Ciechanover, A., and Schwartz, A.L. (1992). Ubiquitin-activating enzyme, E1, is associated with maturation of autophagic vacuoles. J. Cell Biol. 118, 301-308.
    • (1992) J. Cell Biol. , vol.118 , pp. 301-308
    • Lenk, S.E.1    Dunn, W.A.2    Trausch, J.S.3    Ciechanover, A.4    Schwartz, A.L.5
  • 32
    • 0022388390 scopus 로고
    • Lysosomal degradation of ribonuclease A and ribonuclease S-protein microinjected into the cytosol of human fibroblasts
    • McElligott, M.A., Miao, P., and Dice, J.F. (1985). Lysosomal degradation of ribonuclease A and ribonuclease S-protein microinjected into the cytosol of human fibroblasts. J. Biol. Chem. 260, 11986-11993.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11986-11993
    • McElligott, M.A.1    Miao, P.2    Dice, J.F.3
  • 33
    • 0028181648 scopus 로고
    • Enhanced I kappa B alpha degradation is responsible for constitutive NF-kappa B activity in mature murine B-cell lines
    • Miyamoto, S., Chiao, P.J., and Verma, I.M. (1994). Enhanced I kappa B alpha degradation is responsible for constitutive NF-kappa B activity in mature murine B-cell lines. Mol. Cell. Biol. 14, 3276-3282.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3276-3282
    • Miyamoto, S.1    Chiao, P.J.2    Verma, I.M.3
  • 34
    • 0031594708 scopus 로고    scopus 로고
    • Novel IκBα proteolytic pathway in WEHI231 immature B cells
    • Miyamoto, S., Seufzer, B.J., and Shumway, S.D. (1998). Novel IκBα proteolytic pathway in WEHI231 immature B cells. Mol. Cell. Biol. 18, 19-29.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 19-29
    • Miyamoto, S.1    Seufzer, B.J.2    Shumway, S.D.3
  • 35
    • 0019784780 scopus 로고
    • Degradation of proteins microinjected into IMR-90 human diploid fibroblasts
    • Neff, N.T., Bourret, L., Miao, P., and Dice, J.F. (1981). Degradation of proteins microinjected into IMR-90 human diploid fibroblasts. J. Cell Biol. 91, 184-194.
    • (1981) J. Cell Biol. , vol.91 , pp. 184-194
    • Neff, N.T.1    Bourret, L.2    Miao, P.3    Dice, J.F.4
  • 36
    • 0031172065 scopus 로고    scopus 로고
    • NF-kB: A crucial transcription factor for glial and neuronal cell function
    • O'Neill, L.A.J., and Kaltschmidt, C. (1997). NF-kB: a crucial transcription factor for glial and neuronal cell function. Trends Neuro-sci. 20, 252-256.
    • (1997) Trends Neuro-sci. , vol.20 , pp. 252-256
    • O'Neill, L.A.J.1    Kaltschmidt, C.2
  • 37
    • 0020710506 scopus 로고
    • A rapid and simplified method for the preparation of lysosomal membranes from rat liver
    • Ohsumi, Y., Ishikawa, T., and Kato, K. (1983). A rapid and simplified method for the preparation of lysosomal membranes from rat liver. J. Biochem. 93, 547-556.
    • (1983) J. Biochem. , vol.93 , pp. 547-556
    • Ohsumi, Y.1    Ishikawa, T.2    Kato, K.3
  • 38
    • 0002006941 scopus 로고
    • Inhibition of proteolytic enzymes
    • ed. R.J. Beynon and J.S. Bond, Oxford: IRL Press
    • Salvelsen, G., and Nagase, H. (1989). Inhibition of proteolytic enzymes. In: Proteolytic Enzymes, ed. R.J. Beynon and J.S. Bond, Oxford: IRL Press, 83-104.
    • (1989) Proteolytic Enzymes , pp. 83-104
    • Salvelsen, G.1    Nagase, H.2
  • 40
    • 0026590541 scopus 로고
    • Dithiocarbamates as potent inhibitors of nuclear factor κB activation in intact cells
    • Schreck, R., Meier, B., Manner, D.N., Droge, W., and Baeurle, P. (1992). Dithiocarbamates as potent inhibitors of nuclear factor κB activation in intact cells. J. Exp. Med. 175, 1181-1194.
    • (1992) J. Exp. Med. , vol.175 , pp. 1181-1194
    • Schreck, R.1    Meier, B.2    Manner, D.N.3    Droge, W.4    Baeurle, P.5
  • 41
    • 0027168948 scopus 로고
    • The p65 subunit of NF-κB regulates IκB by two distinct mechanisms
    • Scott, M.L., Fujita, T., Liou, H.C., Noalan, G.P., and Baltimore, D. (1993). The p65 subunit of NF-κB regulates IκB by two distinct mechanisms. Genes Dev. 7, 1266-1276.
    • (1993) Genes Dev. , vol.7 , pp. 1266-1276
    • Scott, M.L.1    Fujita, T.2    Liou, H.C.3    Noalan, G.P.4    Baltimore, D.5
  • 42
    • 0025239273 scopus 로고
    • Isolation of subcellular organelles
    • Storrie, B., and Madden, E.A. (1990). Isolation of subcellular organelles. Methods Enzymol. 182, 203-225.
    • (1990) Methods Enzymol. , vol.182 , pp. 203-225
    • Storrie, B.1    Madden, E.A.2
  • 43
    • 0030026562 scopus 로고    scopus 로고
    • Both amino- and carboxyl-terminal sequences within IκBα regulate its inducible degradation
    • Sun, S-C., Elwood, H., and Greene, W.C. (1996). Both amino-and carboxyl-terminal sequences within IκBα regulate its inducible degradation. Mol Cell. Biol. 16, 1058-1065.
    • (1996) Mol Cell. Biol. , vol.16 , pp. 1058-1065
    • Sun, S.-C.1    Elwood, H.2    Greene, W.C.3
  • 44
    • 0027168447 scopus 로고
    • NF-κB controls expression of inhibitor IκBα: Evidence for an inducible autoregulatory pathway
    • Sun, S-C., Ganchi, P.A., Ballard, D.W., and Greene, W.C. (1993). NF-κB controls expression of inhibitor IκBα: evidence for an inducible autoregulatory pathway. Science 259, 1912-1915.
    • (1993) Science , vol.259 , pp. 1912-1915
    • Sun, S.-C.1    Ganchi, P.A.2    Ballard, D.W.3    Greene, W.C.4
  • 45
    • 0029814276 scopus 로고    scopus 로고
    • Role of unphosphorylated, newly synthesized IκBβ in persistent activation of NF-κB
    • Suyang, H., Phillips, R., Douglas, I., and Ghosh, S. (1996). Role of unphosphorylated, newly synthesized IκBβ in persistent activation of NF-κB. Mol Cell. Biol. 16, 5444-5449.
    • (1996) Mol Cell. Biol. , vol.16 , pp. 5444-5449
    • Suyang, H.1    Phillips, R.2    Douglas, I.3    Ghosh, S.4
  • 46
    • 0026808914 scopus 로고
    • Protein and peptide binding and stimulation of in vitro lysosomal proteolysis by the 73-kDa heat shock cognate protein
    • Terlecky, S.R., Chiang, H.-L.,Olson, T.S., and Dice, J.F. (1992). Protein and peptide binding and stimulation of in vitro lysosomal proteolysis by the 73-kDa heat shock cognate protein. J. Biol. Chem. 267, 9202-9209.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9202-9209
    • Terlecky, S.R.1    Chiang, H.-L.2    Olson, T.S.3    Dice, J.F.4
  • 47
    • 0027379661 scopus 로고
    • Polypeptide import and degradation by isolated lysosomes
    • Terlecky, S.R., and Dice, J.F. (1993). Polypeptide import and degradation by isolated lysosomes. J. Biol. Chem. 268, 23490-23495.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23490-23495
    • Terlecky, S.R.1    Dice, J.F.2
  • 48
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedures and some applications
    • Towbin, H., Staehelin, T., and Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedures and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4353.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4353
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 49
    • 0029851617 scopus 로고    scopus 로고
    • Signal-induced degradation of IκBα: Association with NF-κB and the PEST sequence in Ikappa;Bα are not required
    • van Antwerp, D.J., and Verma, I.M. (1996). Signal-induced degradation of IκBα: association with NF-κB and the PEST sequence in Ikappa;Bα are not required. Mol Cell. Biol. 16, 6037-6045.
    • (1996) Mol Cell. Biol. , vol.16 , pp. 6037-6045
    • Van Antwerp, D.J.1    Verma, I.M.2
  • 51
    • 0028817585 scopus 로고
    • Multiorgan inflammation and hematopoietic abnormalities in mice with a targeted disruption of RelB, a member of the NF-κB/Rel family
    • Weith, F., Carrasco, D., Durham, S.K., Barton, D.S., Rizzo, C.A., Ryseck, R.P., Lira, S.A., and Bravo, R. (1995). Multiorgan inflammation and hematopoietic abnormalities in mice with a targeted disruption of RelB, a member of the NF-κB/Rel family. Cell 80, 331-340.
    • (1995) Cell , vol.80 , pp. 331-340
    • Weith, F.1    Carrasco, D.2    Durham, S.K.3    Barton, D.S.4    Rizzo, C.A.5    Ryseck, R.P.6    Lira, S.A.7    Bravo, R.8
  • 52
    • 0021922919 scopus 로고
    • Rapid purification of mammalian 70,000-dalton stress proteins: Affinity of the proteins for nucleotides
    • Welch, W.J., and Feramisco, J.R. (1985). Rapid purification of mammalian 70,000-dalton stress proteins: affinity of the proteins for nucleotides. Mol. Cell. Biol. 5, 1229-1237.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 1229-1237
    • Welch, W.J.1    Feramisco, J.R.2
  • 53
    • 0029736796 scopus 로고    scopus 로고
    • Bcl-2 and crmA have different effects on transformation, apoptosis and the stability of I kappa B-alpha in chicken spleen cells transformed by temperature-sensitive v-Rel oncoproteins
    • White, D.W., and Gilmore, T.D. (1996). Bcl-2 and crmA have different effects on transformation, apoptosis and the stability of I kappa B-alpha in chicken spleen cells transformed by temperature-sensitive v-Rel oncoproteins. Oncogene 13, 891-899.
    • (1996) Oncogene , vol.13 , pp. 891-899
    • White, D.W.1    Gilmore, T.D.2
  • 54
    • 0025801067 scopus 로고
    • Proteins containing peptide sequences related to KFERQ are selectively depleted in liver and heart, but not skeletal muscle, of fasted rats
    • Wing, S.S., Chiang, H.L., Goldberg, A.L., and Dice, J.F. (1991). Proteins containing peptide sequences related to KFERQ are selectively depleted in liver and heart, but not skeletal muscle, of fasted rats. Biochem. J. 275, 165-169.
    • (1991) Biochem. J. , vol.275 , pp. 165-169
    • Wing, S.S.1    Chiang, H.L.2    Goldberg, A.L.3    Dice, J.F.4
  • 55
    • 0031566233 scopus 로고    scopus 로고
    • The heat shock response inhibits inducible nitric oxide synthase gene expression by blocking I kappa-B degradation and NF-kappa B nuclear translocation
    • Wong, H.R., Ryan, M., and Wispe, J.R. (1997). The heat shock response inhibits inducible nitric oxide synthase gene expression by blocking I kappa-B degradation and NF-kappa B nuclear translocation. Biochem. Biophys. Res. Commun. 231, 257-263.
    • (1997) Biochem. Biophys. Res. Commun. , vol.231 , pp. 257-263
    • Wong, H.R.1    Ryan, M.2    Wispe, J.R.3


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