메뉴 건너뛰기




Volumn 255, Issue 3, 1998, Pages 552-562

Evidence that Hsc70 negatively modulates the activation of the heme-regulated eIP-2α kinase in rabbit reticulocyte lysate

Author keywords

Heat and oxidative stress; Heme regulated EIF 2 kinase; Hsc70; Rabbit reticulocyte lysate; Translational control

Indexed keywords

HEAT SHOCK PROTEIN 70; PHOSPHOTRANSFERASE;

EID: 0032146164     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2550552.x     Document Type: Article
Times cited : (31)

References (55)
  • 1
    • 0030997120 scopus 로고    scopus 로고
    • Hsp90 is obligatory for the heme-regulated eIF-2α kinase to aquire and maintain an activable conformation
    • Uma, S., Hartson, S. D., Chen, J.-J. & Matts, R. L. (1997) Hsp90 is obligatory for the heme-regulated eIF-2α kinase to aquire and maintain an activable conformation, J. Biol. Chem. 272, 11648-11656.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11648-11656
    • Uma, S.1    Hartson, S.D.2    Chen, J.-J.3    Matts, R.L.4
  • 2
    • 0000257134 scopus 로고
    • Translational regulation in reticulocytes: The role of heme-regulated eIF-2α kinase
    • (Ilan, J., ed.) Plenum Press, New York
    • Chen, J.-J. (1993) Translational regulation in reticulocytes: the role of heme-regulated eIF-2α kinase, in Translational regulation of gene expression 2 (Ilan, J., ed.) pp. 349-372, Plenum Press, New York.
    • (1993) Translational Regulation of Gene Expression , vol.2 , pp. 349-372
    • Chen, J.-J.1
  • 3
    • 0028935374 scopus 로고
    • Regulation of protein synthesis by heme-regulated eIF-2α kinase
    • Chen, J.-J. & London, I. M. (1995) Regulation of protein synthesis by heme-regulated eIF-2α kinase, Trends in Biochem. Sci. 20, 105-108.
    • (1995) Trends in Biochem. Sci. , vol.20 , pp. 105-108
    • Chen, J.-J.1    London, I.M.2
  • 4
    • 0000002161 scopus 로고
    • Binding of Met-tRNA
    • (Trachsel, H., ed.) CRC Press, Boca Raton FL
    • Jackson, R. J. (1991) Binding of Met-tRNA, in Translation in eukaryotes (Trachsel, H., ed.) pp. 193-229, CRC Press, Boca Raton FL.
    • (1991) Translation in Eukaryotes , pp. 193-229
    • Jackson, R.J.1
  • 5
    • 77956925190 scopus 로고
    • Regulation of protein synthesis
    • (Boyer, P. D. & Krebs, E. G., eds) Academic Press, New York
    • London, I. M., Levin, D. H., Matts, R. L., Thomas, N. S. B., Petryshyn, R. & Chen, J. J. (1987) Regulation of protein synthesis, in The enzymes (Boyer, P. D. & Krebs, E. G., eds) vol. 18, pp. 359-380, Academic Press, New York.
    • (1987) The Enzymes , vol.18 , pp. 359-380
    • London, I.M.1    Levin, D.H.2    Matts, R.L.3    Thomas, N.S.B.4    Petryshyn, R.5    Chen, J.J.6
  • 6
    • 0021164835 scopus 로고
    • The regulation of initiation of protein synthesis by phosphorylation of eIF-2alpha and the role of reversing factor in the recycling of eIF-2
    • Matts, R. L. & London, I. M. (1984) The regulation of initiation of protein synthesis by phosphorylation of eIF-2alpha and the role of reversing factor in the recycling of eIF-2, J. Biol. Chem. 259, 6708-6711.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6708-6711
    • Matts, R.L.1    London, I.M.2
  • 7
    • 0021352831 scopus 로고
    • Mechanism of translational control by partial phosphorylation of the α subunit of eukaryotic initiation factor 2
    • Siekierka, J., Manne, V. & Ochoa, S. (1984) Mechanism of translational control by partial phosphorylation of the α subunit of eukaryotic initiation factor 2, Proc. Natl Acad. Sci. USA 81, 352-356.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 352-356
    • Siekierka, J.1    Manne, V.2    Ochoa, S.3
  • 8
    • 0002949973 scopus 로고
    • The control of protein synthesis in rabbit reticulocyte lysates
    • Hunt, T. (1979) The control of protein synthesis in rabbit reticulocyte lysates, Miami Winter Symp. 16, 321-345.
    • (1979) Miami Winter Symp. , vol.16 , pp. 321-345
    • Hunt, T.1
  • 9
    • 0022494945 scopus 로고
    • Modulators of the eukaryotic heat shock response
    • Lanks, K. W. (1986) Modulators of the eukaryotic heat shock response, Exp. Cell Res. 165, 1-10.
    • (1986) Exp. Cell Res. , vol.165 , pp. 1-10
    • Lanks, K.W.1
  • 10
    • 0025832056 scopus 로고
    • Translational control in mammalian cells
    • Hershey, J. W. B. (1991) Translational control in mammalian cells, Annu. Rev. Biochem. 60, 717-755.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 717-755
    • Hershey, J.W.B.1
  • 11
    • 0011263157 scopus 로고
    • Adjustment of translation to special physiological conditions
    • (Trachsel, H., ed.) CRC Press, Boca Raton FL
    • Pain, V. M. & Clemens, M. J. (1991) Adjustment of translation to special physiological conditions, in Translation in eukaryotes (Trachsel, H., ed.) pp. 293-324, CRC Press, Boca Raton FL.
    • (1991) Translation in Eukaryotes , pp. 293-324
    • Pain, V.M.1    Clemens, M.J.2
  • 12
    • 0031009879 scopus 로고    scopus 로고
    • The role of the 90-kDa heat-shock protein and its associated cohorts in stabilizing the heme-regulated eIF-2α kinase in rabbit reticulocye lysates during heat stress
    • Xu, Z., Pal, J. K., Thulasiraman, V., Hahn, H. P., Chen, J.-J. & Matts, R. L. (1997) The role of the 90-kDa heat-shock protein and its associated cohorts in stabilizing the heme-regulated eIF-2α kinase in rabbit reticulocye lysates during heat stress, Eur. J. Biochem. 246, 461-470.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 461-470
    • Xu, Z.1    Pal, J.K.2    Thulasiraman, V.3    Hahn, H.P.4    Chen, J.-J.5    Matts, R.L.6
  • 13
    • 0019405290 scopus 로고
    • Relationship between phosphorylation and activity of heme-regulated eukaryotic initiation factor 2α kinase
    • Fagard, R. & London, I. M. (1981) Relationship between phosphorylation and activity of heme-regulated eukaryotic initiation factor 2α kinase, Proc. Natl Acad. Sci. USA 78, 866-870.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 866-870
    • Fagard, R.1    London, I.M.2
  • 14
    • 0026760078 scopus 로고
    • The relationship between protein synthesis and heat-shock proteins levels in rabbit reticulocyte lysates
    • Matts, R. L. & Hurst, R. (1992) The relationship between protein synthesis and heat-shock proteins levels in rabbit reticulocyte lysates, J. Biol. Chem. 267, 18168-18174.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18168-18174
    • Matts, R.L.1    Hurst, R.2
  • 15
    • 0027282654 scopus 로고
    • Denatured proteins inhibit translation in hemin-supplemented rabbit reticulocyte lysate by inducing the activation of the heme-regulated eIF-2α kinase
    • Matts, R. L., Hurst, R. & Xu, Z., (1993) Denatured proteins inhibit translation in hemin-supplemented rabbit reticulocyte lysate by inducing the activation of the heme-regulated eIF-2α kinase, Biochemistry 32, 7323-7328.
    • (1993) Biochemistry , vol.32 , pp. 7323-7328
    • Matts, R.L.1    Hurst, R.2    Xu, Z.3
  • 17
    • 0017180204 scopus 로고
    • Control of protein synthesis by hemin: Isolation and characterization of a supernatant factor from rabbit reticulocyte lysate
    • Gross, M. (1976) Control of protein synthesis by hemin: isolation and characterization of a supernatant factor from rabbit reticulocyte lysate, Biochim. Biophys. Acta 447, 445-459.
    • (1976) Biochim. Biophys. Acta , vol.447 , pp. 445-459
    • Gross, M.1
  • 18
    • 0015527030 scopus 로고
    • Control of globin synthesis: The role of heme
    • Hunt, T., Vanderhoff, G. & London, I. M. (1972) Control of globin synthesis: the role of heme, J. Mol. Biol. 66, 471-481.
    • (1972) J. Mol. Biol. , vol.66 , pp. 471-481
    • Hunt, T.1    Vanderhoff, G.2    London, I.M.3
  • 19
    • 0025866988 scopus 로고
    • Toxic heavy metal ions activate the heme-regulated eukaryotic initiation factor-2-alpha kinase by inhibiting the capacity of hemin-supplemented reticulocyte lysates to reduce disulfide bonds
    • Matts, R. L., Schatz, J. R., Hurst, R. & Kagen, R. (1991) Toxic heavy metal ions activate the heme-regulated eukaryotic initiation factor-2-alpha kinase by inhibiting the capacity of hemin-supplemented reticulocyte lysates to reduce disulfide bonds, J. Biol. Chem. 266, 12695-12702.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12695-12702
    • Matts, R.L.1    Schatz, J.R.2    Hurst, R.3    Kagen, R.4
  • 20
    • 0023633792 scopus 로고
    • Inhibition of rabbit reticulocyte lysate protein synthesis by heavy metal ions involves the phosphorylation of the alpha-subunit of the eukaryotic initiation factor 2
    • Hurst, R., Schatz, J. R. & Matts, R. L. (1987) Inhibition of rabbit reticulocyte lysate protein synthesis by heavy metal ions involves the phosphorylation of the alpha-subunit of the eukaryotic initiation factor 2, J. Biol. Chem. 262, 15939-15945.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15939-15945
    • Hurst, R.1    Schatz, J.R.2    Matts, R.L.3
  • 21
    • 0024271276 scopus 로고
    • Specific interaction between a subset of the p53 protein family and heat-shock proteins hsp72/hsc73 in a human osteosarcoma cell line
    • Ehrhart, J. C., Duthu, A., Ullrich, S., Appella, E. & May, P. (1988) Specific interaction between a subset of the p53 protein family and heat-shock proteins hsp72/hsc73 in a human osteosarcoma cell line, Oncogene 3, 595-603.
    • (1988) Oncogene , vol.3 , pp. 595-603
    • Ehrhart, J.C.1    Duthu, A.2    Ullrich, S.3    Appella, E.4    May, P.5
  • 22
    • 0018175885 scopus 로고
    • Evidence that glucose 6-phosphate regulates protein synthesis initiation in reticulocyte lysates
    • Ernst, V., Levin, D. H. & London, I. M. (1978) Evidence that glucose 6-phosphate regulates protein synthesis initiation in reticulocyte lysates, J. Biol. Chem. 253, 7163-7172.
    • (1978) J. Biol. Chem. , vol.253 , pp. 7163-7172
    • Ernst, V.1    Levin, D.H.2    London, I.M.3
  • 23
    • 0024331965 scopus 로고
    • Evaluation of protein phosphorylation state by a combination of vertical slab gel isoelectric focusing and immunoblotting
    • Maurides, P. A., Akkaraju, G. R. & Jagus, R. (1989) Evaluation of protein phosphorylation state by a combination of vertical slab gel isoelectric focusing and immunoblotting, Anal. Biochem. 183, 144-151.
    • (1989) Anal. Biochem. , vol.183 , pp. 144-151
    • Maurides, P.A.1    Akkaraju, G.R.2    Jagus, R.3
  • 24
    • 0023665208 scopus 로고
    • Phosphorylation of eukaryotic initiation factor 2 during physiological stress which affect protein synthesis
    • Scorsone, K. A., Panniers, R., Rowlands, A. G. & Henshaw, E. C. (1987) Phosphorylation of eukaryotic initiation factor 2 during physiological stress which affect protein synthesis, J. Biol. Chem. 262, 14538-14543.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14538-14543
    • Scorsone, K.A.1    Panniers, R.2    Rowlands, A.G.3    Henshaw, E.C.4
  • 25
    • 0026778841 scopus 로고
    • Interactions of the heme-regulated eIF-2α kinase with heat-shock proteins' in rabbit reticulocyte lysates
    • Matts, R. L., Xu, Z., Pal, J. K. & Chen, J.-J. (1992) Interactions of the heme-regulated eIF-2α kinase with heat-shock proteins' in rabbit reticulocyte lysates, J. Biol. Chem. 267, 18160-18167.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18160-18167
    • Matts, R.L.1    Xu, Z.2    Pal, J.K.3    Chen, J.-J.4
  • 26
    • 0030928059 scopus 로고    scopus 로고
    • Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells
    • Eggers, D. K., Welch, W. J. & Hansen, W. J. (1997) Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells, Mol. Cell. Biol. 8, 1559-1573.
    • (1997) Mol. Cell. Biol. , vol.8 , pp. 1559-1573
    • Eggers, D.K.1    Welch, W.J.2    Hansen, W.J.3
  • 27
    • 0026523153 scopus 로고
    • Interactions of liver Grp78 and Escherichia coli recombinant Grp78 with ATP: Multiple species and disaggregation
    • Carlino, A., Toledo, H., Skaleris, D., DeLisio, R., Weissbach, H. & Brot, N. (1992) Interactions of liver Grp78 and Escherichia coli recombinant Grp78 with ATP: Multiple species and disaggregation, Proc. Natl Acad. Sci. USA 89, 2081-2085.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 2081-2085
    • Carlino, A.1    Toledo, H.2    Skaleris, D.3    Delisio, R.4    Weissbach, H.5    Brot, N.6
  • 29
    • 0021280391 scopus 로고
    • An enzyme that removes clathrin coats: Purification of an uncoating ATPase
    • Schlossman, D. M., Schmid, S. L., Braell, W. A. & Rothman, J. E. (1984) An enzyme that removes clathrin coats: purification of an uncoating ATPase, J. Cell Biol. 99, 723-733.
    • (1984) J. Cell Biol. , vol.99 , pp. 723-733
    • Schlossman, D.M.1    Schmid, S.L.2    Braell, W.A.3    Rothman, J.E.4
  • 30
    • 0022346828 scopus 로고
    • ATP catalyzes the sequestration of clathrin during enzymatic uncoating
    • Schmid, S. L., Braell, W. A. & Rothman, J. E. (1985) ATP catalyzes the sequestration of clathrin during enzymatic uncoating, J. Biol. Chem. 260, 10057-10062.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10057-10062
    • Schmid, S.L.1    Braell, W.A.2    Rothman, J.E.3
  • 32
    • 0029118986 scopus 로고
    • Polymerization of 70-kDa heat-shock protein by yeast DnaJ in ATP
    • King, C., Eisenberg, E. & Greene, L. (1995) Polymerization of 70-kDa heat-shock protein by yeast DnaJ in ATP, J. Biol. Chem. 270, 22535-22540.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22535-22540
    • King, C.1    Eisenberg, E.2    Greene, L.3
  • 33
    • 0029953178 scopus 로고    scopus 로고
    • Effect of constitutive 70-kDa heat-shock protein polymerization on its interaction with protein substrate
    • Gao, B., Eisenberg, E. & Greene, L. (1996) Effect of constitutive 70-kDa heat-shock protein polymerization on its interaction with protein substrate, J. Biol. Chem. 271, 16792-16797.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16792-16797
    • Gao, B.1    Eisenberg, E.2    Greene, L.3
  • 37
    • 0003028958 scopus 로고
    • Heat shock, protein phosphorylation and the control of translation in rabbit reticulocytcs, reticulocyte lysates and HeLa cells
    • (Schlesinger, M. J., Ashburner, M. & Tissieries, A., eds) Cold Spring Harbor Press, Cold Spring Harbor NY
    • Ernst, V., Baum, E. Z. & Reddy, R. (1982) Heat shock, protein phosphorylation and the control of translation in rabbit reticulocytcs, reticulocyte lysates and HeLa cells, in Heat shock: from bacteria to man (Schlesinger, M. J., Ashburner, M. & Tissieries, A., eds) pp. 215-225, Cold Spring Harbor Press, Cold Spring Harbor NY.
    • (1982) Heat Shock: From Bacteria to Man , pp. 215-225
    • Ernst, V.1    Baum, E.Z.2    Reddy, R.3
  • 38
    • 0018428421 scopus 로고
    • In situ phosphorylation of the α-subunit of eukaryotic initiation factor 2 in reticulocyte lysate inhibited by heme deficiency, double-stranded RNA, oxidized glutathione, or heme-regulated protein kinase
    • Ernst, V., Levin, D. H. & London, I. M. (1979) In situ phosphorylation of the α-subunit of eukaryotic initiation factor 2 in reticulocyte lysate inhibited by heme deficiency, double-stranded RNA, oxidized glutathione, or heme-regulated protein kinase, Proc. Natl Acad. Sci. USA 76, 2118-2122.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 2118-2122
    • Ernst, V.1    Levin, D.H.2    London, I.M.3
  • 40
    • 0021103648 scopus 로고
    • The use of affinity chromatography on 2′5′ ADP-Sepharose reveals a requirement for NADPH, thioredoxin and thioredoxin reductase for the maintenance of high protein synthesis activity in rabbit reticulocye lysates
    • Hunt, T., Herbert, P., Cambell, E. A., Delidakis, C. & Jackson, R. J. (1983) The use of affinity chromatography on 2′5′ ADP-Sepharose reveals a requirement for NADPH, thioredoxin and thioredoxin reductase for the maintenance of high protein synthesis activity in rabbit reticulocye lysates, Eur. J. Biochem. 131, 303-311.
    • (1983) Eur. J. Biochem. , vol.131 , pp. 303-311
    • Hunt, T.1    Herbert, P.2    Cambell, E.A.3    Delidakis, C.4    Jackson, R.J.5
  • 41
    • 0020622118 scopus 로고
    • Roles of sugar phosphates and thiol reducing systems in the control of reticulocyte protein synthesis
    • Jackson, R. J., Herbert, P., Cambell, E. A. & Hunt, T. (1983) Roles of sugar phosphates and thiol reducing systems in the control of reticulocyte protein synthesis, Eur. J. Biochem. 131, 313-324.
    • (1983) Eur. J. Biochem. , vol.131 , pp. 313-324
    • Jackson, R.J.1    Herbert, P.2    Cambell, E.A.3    Hunt, T.4
  • 42
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman, J., Nimmesgern, E., Ohtsuka, K. & Hartl, F. U. (1994) Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 370, 111-117.
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hartl, F.U.4
  • 43
    • 0025303147 scopus 로고
    • Interaction of hsp70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckman, R. P., Mizzen, L. A. & Welch, W. J. (1990) Interaction of hsp70 with newly synthesized proteins: Implications for protein folding and assembly, Science 248, 850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckman, R.P.1    Mizzen, L.A.2    Welch, W.J.3
  • 44
    • 0027048776 scopus 로고
    • Recycling and phosphorylation of eukaryotic initiation factor 2 on 60S subunits of 80S initiation complexes and polyribosomes
    • Ramaiah, K. V. A., Dhindsa, R. S., Chen, J.-J., London, I. M. & Levin, D. (1992) Recycling and phosphorylation of eukaryotic initiation factor 2 on 60S subunits of 80S initiation complexes and polyribosomes, Proc. Natl Acad. Sci. USA 89, 12063-12067.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 12063-12067
    • Ramaiah, K.V.A.1    Dhindsa, R.S.2    Chen, J.-J.3    London, I.M.4    Levin, D.5
  • 45
    • 0026699920 scopus 로고
    • Effects of hemin and porphyrin compounds on intersubunit disulfide formation of heme-regulated eIF-2α kinase and the regulation of protein synthesis in reticulocyte lysates
    • Yang, J. M., London, I. M. & Chen, J.-J. (1992) Effects of hemin and porphyrin compounds on intersubunit disulfide formation of heme-regulated eIF-2α kinase and the regulation of protein synthesis in reticulocyte lysates, J. Biol. Chem. 267, 20519-20524.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20519-20524
    • Yang, J.M.1    London, I.M.2    Chen, J.-J.3
  • 46
    • 0024333869 scopus 로고
    • Disulfide bond formation in the regulation of eIF-2α kinase by heme
    • Chen, J.-J., Yang, J. M., Petryshyn, R., Kosower, N. & London, I. M. (1989) Disulfide bond formation in the regulation of eIF-2α kinase by heme, J. Biol. Chem. 264, 9559-9564.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9559-9564
    • Chen, J.-J.1    Yang, J.M.2    Petryshyn, R.3    Kosower, N.4    London, I.M.5
  • 47
    • 0028931814 scopus 로고
    • Effect of oxidizing agents and haemin on the phosphorylation of eukaryotic elongation factor 2 in rabbit reticulocyte lysates
    • Nilsson, A. & Nygard, O. (1995) Effect of oxidizing agents and haemin on the phosphorylation of eukaryotic elongation factor 2 in rabbit reticulocyte lysates, Biochim. Biophys. Acta 1260, 200-206.
    • (1995) Biochim. Biophys. Acta , vol.1260 , pp. 200-206
    • Nilsson, A.1    Nygard, O.2
  • 48
    • 0027319027 scopus 로고
    • Expression of a phosphorylation-resistant eukaryotic initiation factor 2α subunit mitigates heat shock inhibition of protein synthesis
    • Murtha-Riel, P., Davies, M. V., Scherer, J. B., Choi, S. J., Hershey, J. W. B. & Kaufman, R. J. (1993) Expression of a phosphorylation-resistant eukaryotic initiation factor 2α subunit mitigates heat shock inhibition of protein synthesis, J. Biol. Chem. 268, 12946-12951.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12946-12951
    • Murtha-Riel, P.1    Davies, M.V.2    Scherer, J.B.3    Choi, S.J.4    Hershey, J.W.B.5    Kaufman, R.J.6
  • 49
    • 0021228666 scopus 로고
    • Heat shock induced translational alterations in HeLa cells: Initiation factor modifications and the inhibition of translation
    • Duncan, R. & Hershey, J. W. B. (1984) Heat shock induced translational alterations in HeLa cells: Initiation factor modifications and the inhibition of translation, J. Biol. Chem. 259, 11882-11889.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11882-11889
    • Duncan, R.1    Hershey, J.W.B.2
  • 50
    • 0023387397 scopus 로고
    • Translation repression by chemical inducers of the stress response occurs by different pathways
    • Duncan, R. & Hershey, J. W. B. (1987) Translation repression by chemical inducers of the stress response occurs by different pathways, Arch. Biochem. Biophys. 256, 651-661.
    • (1987) Arch. Biochem. Biophys. , vol.256 , pp. 651-661
    • Duncan, R.1    Hershey, J.W.B.2
  • 51
    • 0024437487 scopus 로고
    • Protein synthesis and protein phosphorylation during heat stress, recovery, and adaptation
    • Duncan, R. F. & Hershey, J. W. B. (1989) Protein synthesis and protein phosphorylation during heat stress, recovery, and adaptation, J. Cell Biol. 109, 1467-1481.
    • (1989) J. Cell Biol. , vol.109 , pp. 1467-1481
    • Duncan, R.F.1    Hershey, J.W.B.2
  • 52
    • 0028938425 scopus 로고
    • Activation of the double-stranded RNA-regulated protein kinase by depletion of endoplasmic reticular calcium stores
    • Prostko, C. R., Dholakia, J. N., Brostrom, M. A. & Brostrom, C. O. (1995) Activation of the double-stranded RNA-regulated protein kinase by depletion of endoplasmic reticular calcium stores, J. Biol. Chem. 270, 6211-6215.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6211-6215
    • Prostko, C.R.1    Dholakia, J.N.2    Brostrom, M.A.3    Brostrom, C.O.4
  • 53
    • 0028963278 scopus 로고
    • Independent signaling of grp78 gene transcription and phosphorylation of eukaryotic initiation factor 2-alpha by the stressed endoplasmic reticulum
    • Brostrom, M. A., Prostko, C. R., Gmitter, D. & Brostrom, C. O. (1995) Independent signaling of grp78 gene transcription and phosphorylation of eukaryotic initiation factor 2-alpha by the stressed endoplasmic reticulum, J. Biol. Chem. 270, 4127-4132.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4127-4132
    • Brostrom, M.A.1    Prostko, C.R.2    Gmitter, D.3    Brostrom, C.O.4
  • 55
    • 0022455341 scopus 로고
    • Protection of Chinese hamster ovary cells from hyperthermic killing by cycloheximide or puromycin
    • Lee, Y. J. & Dewey, W. C. (1986) Protection of Chinese hamster ovary cells from hyperthermic killing by cycloheximide or puromycin, Radiat. Res. 106, 98-110.
    • (1986) Radiat. Res. , vol.106 , pp. 98-110
    • Lee, Y.J.1    Dewey, W.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.