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Volumn 19, Issue 9, 1999, Pages 5861-5871

Dual role for Hsc70 in the biogenesis and regulation of the heme- regulated kinase of the α subunit of eukaryotic translation initiation factor 2

Author keywords

[No Author keywords available]

Indexed keywords

CLOFIBRIC ACID; HEAT SHOCK PROTEIN; INITIATION FACTOR 2; PHOSPHOTRANSFERASE;

EID: 0032766645     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.19.9.5861     Document Type: Article
Times cited : (47)

References (58)
  • 1
    • 0025062963 scopus 로고
    • Identification of cytosolic peroxisome proliferator binding protein as a member of the heat shock protein hsp70 family
    • Alvares, K., A. Carrillo, P. M. Yuan, H. Kawano, R. I. Morimoto, and J. K. Reddy. 1990. Identification of cytosolic peroxisome proliferator binding protein as a member of the heat shock protein hsp70 family. Proc. Natl. Acad. Sci. USA 87:5293-5297.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5293-5297
    • Alvares, K.1    Carrillo, A.2    Yuan, P.M.3    Kawano, H.4    Morimoto, R.I.5    Reddy, J.K.6
  • 2
    • 0022455603 scopus 로고
    • Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes
    • Ananthan, J., A. R. Goldberg, and R. Voellmy. 1986. Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes. Science 232:252-258.
    • (1986) Science , vol.232 , pp. 252-258
    • Ananthan, J.1    Goldberg, A.R.2    Voellmy, R.3
  • 3
    • 0032489016 scopus 로고    scopus 로고
    • The hsp70 and hsp60 chaperone machines
    • Bakau, B., and A. L. Horwich. 1998. The hsp70 and hsp60 chaperone machines. Cell 92:351-356.
    • (1998) Cell , vol.92 , pp. 351-356
    • Bakau, B.1    Horwich, A.L.2
  • 4
    • 0025303147 scopus 로고
    • Interaction of hsp70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckman, R. P., L. A. Mizzen, and W. J. Welch. 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
  • 5
    • 0033610887 scopus 로고    scopus 로고
    • Characterization of the hemin-sensitive eukaryotic initiation factor 2α kinase from mouse nonerythroid cells
    • Berlanga, J. J., S. Herrero, and C. De Haro. 1998. Characterization of the hemin-sensitive eukaryotic initiation factor 2α kinase from mouse nonerythroid cells. J. Biol. Chem. 273:32340-32346.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32340-32346
    • Berlanga, J.J.1    Herrero, S.2    De Haro, C.3
  • 6
    • 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., C. R. Prostko, D. Gmitter, and C. O. Brostrom. 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
  • 7
    • 0028099817 scopus 로고
    • Regulation of 70-kDa heat-shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HDJ1a and HDJ1b
    • Cheetham, M. E., A. P. Jackson, and B. H. Anderton. 1994. Regulation of 70-kDa heat-shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HDJ1a and HDJ1b. Eur. J. Biochem. 226:99-107.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 99-107
    • Cheetham, M.E.1    Jackson, A.P.2    Anderton, B.H.3
  • 9
    • 0000257134 scopus 로고
    • Translational regulation in reticulocytes: The role of heme-regulated eIF-2α kinase
    • J. Ilan (ed.), Plenum Press, New York, N.Y.
    • Chen, J.-J. 1993. Translational regulation in reticulocytes: the role of heme-regulated eIF-2α kinase, p. 349-372. In J. Ilan (ed.), Translational regulation of gene expression 2. Plenum Press, New York, N.Y.
    • (1993) Translational Regulation of Gene Expression , vol.2 , pp. 349-372
    • Chen, J.-J.1
  • 10
    • 0028935374 scopus 로고
    • Regulation of protein synthesis by heme-regulated eIF-2a kinase
    • Chen, J.-J., and I. M. London. 1995. Regulation of protein synthesis by heme-regulated eIF-2a kinase. Trends Biochem. Sci. 20:105-108.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 105-108
    • Chen, J.-J.1    London, I.M.2
  • 11
    • 0024333869 scopus 로고
    • Disulfide bond formation in the regulation of eIF-2α kinase by heme
    • Chen, J.-J., J. M. Yang, R. Petryshyn, N. Kosower, and I. M. London. 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
  • 12
    • 0025967766 scopus 로고
    • Is hsp70 the cellular thermometer?
    • Craig, E. A. 1991. Is hsp70 the cellular thermometer? Trends Biochem. Sci. 16:135-140.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 135-140
    • Craig, E.A.1
  • 13
    • 0028353336 scopus 로고
    • DnaJ-like proteins: Molecular chaperones and specific regulators of hsp70
    • Cyr, D. M., T. Langer, and M. G. Douglas. 1994. DnaJ-like proteins: molecular chaperones and specific regulators of hsp70. Trends Biochem. Sci. 19:176-181.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 176-181
    • Cyr, D.M.1    Langer, T.2    Douglas, M.G.3
  • 14
    • 3543037553 scopus 로고    scopus 로고
    • HSP70-2 heat shock protein of mouse spermatogenic cells
    • Eddy, E. M. 1998. HSP70-2 heat shock protein of mouse spermatogenic cells. J. Exp. Zool. 282:261-271.
    • (1998) J. Exp. Zool. , vol.282 , pp. 261-271
    • Eddy, E.M.1
  • 15
    • 0030928059 scopus 로고    scopus 로고
    • Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells
    • Eggers, D. K., W. J. Welch, and W. J. Hansen. 1997. Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells. Mol. Biol. Cell 8:1559-1573.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1559-1573
    • Eggers, D.K.1    Welch, W.J.2    Hansen, W.J.3
  • 16
    • 0018175885 scopus 로고
    • Evidence that glucose 6-phosphate regulates protein synthesis initiation in reticulocyte lysates
    • Ernst, V., D. H. Levin, and I. M. London. 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
  • 17
    • 0019405290 scopus 로고
    • Relationship between phosphorylation and activity of heme-regulated initiation factor 2a kinase
    • Fagard, R., and I. M. London. 1981. Relationship between phosphorylation and activity of heme-regulated initiation factor 2a 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
  • 18
    • 0029887140 scopus 로고    scopus 로고
    • The human cytosolic molecular chaperones in hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
    • Freeman, B. C., and R. I. Morimoto. 1996. The human cytosolic molecular chaperones in hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. EMBO J. 15:2969-2979.
    • (1996) EMBO J. , vol.15 , pp. 2969-2979
    • Freeman, B.C.1    Morimoto, R.I.2
  • 19
    • 0029051966 scopus 로고
    • Identification of a regulatory motiff in hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1
    • Freeman, B. C., M. P. Myers, R. Schumacher, and R. I. Morimoto. 1995. Identification of a regulatory motiff in hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J. 14:2281-2292.
    • (1995) EMBO J. , vol.14 , pp. 2281-2292
    • Freeman, B.C.1    Myers, M.P.2    Schumacher, R.3    Morimoto, R.I.4
  • 20
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman, J., E. Nimmesgern, K. Ohtsuka, and F. U. Hartl. 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
  • 22
    • 0028070415 scopus 로고
    • Control of protein synthesis by hemin. Purification of a rabbit reticulocyte hsp 70 and characterization of its regulation of the activation of the hemin-controlled eIF-2(alpha) kinase
    • Gross, M., A. Olin, S. Hessefort, and S. Bender. 1994. Control of protein synthesis by hemin. Purification of a rabbit reticulocyte hsp 70 and characterization of its regulation of the activation of the hemin-controlled eIF-2(alpha) kinase. J. Biol. Chem. 269:22738-22748.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22738-22748
    • Gross, M.1    Olin, A.2    Hessefort, S.3    Bender, S.4
  • 23
    • 0344337133 scopus 로고    scopus 로고
    • Unpublished observations
    • Gu, Y., S. Uma, and R. L. Matts. 1996. Unpublished observations.
    • (1996)
    • Gu, Y.1    Uma, S.2    Matts, R.L.3
  • 24
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U. 1996. Molecular chaperones in cellular protein folding. Nature 381:571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 25
    • 0029796733 scopus 로고    scopus 로고
    • Hsp90-mediated folding of the lymphoid cell kinase p561ck
    • Hartson, S. D., D. J. Barrett, P. Burn, and R. L. Matts. 1996. Hsp90-mediated folding of the lymphoid cell kinase p561ck. Biochemistry 35:13451-13459.
    • (1996) Biochemistry , vol.35 , pp. 13451-13459
    • Hartson, S.D.1    Barrett, D.J.2    Burn, P.3    Matts, R.L.4
  • 26
    • 0028023828 scopus 로고
    • Association of Hsp90 with cellular Src-family kinases in a cell-free system correlates with altered kinase structure and function
    • Hartson, S. D., and R. L. Matts. 1994. Association of Hsp90 with cellular Src-family kinases in a cell-free system correlates with altered kinase structure and function. Biochemistry 33:8912-8920.
    • (1994) Biochemistry , vol.33 , pp. 8912-8920
    • Hartson, S.D.1    Matts, R.L.2
  • 27
    • 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
  • 28
    • 0038217763 scopus 로고    scopus 로고
    • Regulation of the heat shock cognate Hsc70 in the mammalian cell: The characterization of the anti-apototic protein BAG-1 provides novel insights
    • Hohfeld, J. 1998. Regulation of the heat shock cognate Hsc70 in the mammalian cell: the characterization of the anti-apototic protein BAG-1 provides novel insights. Biol. Chem. 379:269-274.
    • (1998) Biol. Chem. , vol.379 , pp. 269-274
    • Hohfeld, J.1
  • 29
    • 0028842615 scopus 로고
    • Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp90 reaction cycle
    • Hohfeld, J., Y. Minami, and F.-U. Hartl. 1995. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp90 reaction cycle. Cell 83:589-598.
    • (1995) Cell , vol.83 , pp. 589-598
    • Hohfeld, J.1    Minami, Y.2    Hartl, F.-U.3
  • 30
    • 0028309738 scopus 로고
    • Association of peroxisome proliferator-activated receptor and Hsp72
    • Huang, Q., K. Alvares, R. Chu, C. A. Bradfield, and J. K. Reddy. 1994. Association of peroxisome proliferator-activated receptor and Hsp72. J. Biol. Chem. 269:8493-8497.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8493-8497
    • Huang, Q.1    Alvares, K.2    Chu, R.3    Bradfield, C.A.4    Reddy, J.K.5
  • 31
    • 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
  • 32
    • 0015527030 scopus 로고
    • Control of globin synthesis: The role of heme
    • Hunt, T., G. Vanderhoff, and I. M. London. 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
  • 33
    • 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
  • 34
    • 0025289846 scopus 로고
    • Mechanism of drug-induced heat resistance: The role of protein degradation
    • Lee, Y. J., E. P. Armour, P. M. Corry, and W. C. Dewey. 1990. Mechanism of drug-induced heat resistance: the role of protein degradation. Int. J. Hyperthermia 6:591-595.
    • (1990) Int. J. Hyperthermia , vol.6 , pp. 591-595
    • Lee, Y.J.1    Armour, E.P.2    Corry, P.M.3    Dewey, W.C.4
  • 35
    • 0022455341 scopus 로고
    • Protection of Chinese hamster ovary cells from hyperthermic killing by cycloheximide or puromycin
    • Lee, Y. J., and W. C. Dewey. 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
  • 36
    • 77956925190 scopus 로고
    • Regulation of protein synthesis
    • P. D. Boyer and E. G. Krebs (ed.), Academic Press, New York, N.Y.
    • London, I. M., D. H. Levin, R. L. Matts, N. S. B. Thomas, R. Petryshyn, and J. J. Chen. 1987. Regulation of protein synthesis, p. 359-380. In P. D. Boyer and E. G. Krebs (ed.), The enzymes, 3rd ed., vol. XVIII. Academic Press, New York, N.Y.
    • (1987) The Enzymes, 3rd Ed. , 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
  • 37
    • 0026760078 scopus 로고
    • The relationship between protein synthesis and heat shock proteins levels in rabbit reticulocyte lysates
    • Matts, R. L., and R. Hurst. 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
  • 38
    • 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., R. Hurst, and Z. Xu. 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
  • 39
    • 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., and I. M. London. 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
  • 40
    • 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., J. R. Schatz, R. Hurst, and R. Kagen. 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
  • 41
    • 0026778841 scopus 로고
    • Interactions of the heme-regulated eIF-2α kinase with heat shock proteins in rabbit reticulocyte lysates
    • Matts, R. L., Z. Xu, J. K. Pal, and J.-J. Chen. 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
  • 42
    • 0024331965 scopus 로고
    • Evaluation of protein phosphorylation state by a combination of vertical slab gel isoelectric focusing and immunoblotting
    • Maurides, P. A., G. R. Akkaraju, and R. Jagus. 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
  • 43
    • 0028245588 scopus 로고
    • Cloning and characterization of cDNA encoding rat hemin-sensitive initiation factor-2-alpha (eIF-2-alpha) kinase: Evidence for multitissue expression
    • Mellor, H., K. M. Flowers, S. R. Kimball, and L. S. Jefferson. 1994. Cloning and characterization of cDNA encoding rat hemin-sensitive initiation factor-2-alpha (eIF-2-alpha) kinase: evidence for multitissue expression. J. Biol. Chem. 269:10201-10204.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10201-10204
    • Mellor, H.1    Flowers, K.M.2    Kimball, S.R.3    Jefferson, L.S.4
  • 45
    • 0029964506 scopus 로고    scopus 로고
    • Molecular cloning of human p48, a transient component of progesterone hormone receptor complexes and an hsp90-binding protein
    • Prapapanich, V., S. Chen, S. C. Nair, R. A. Rimerman, and D. F. Smith. 1996. Molecular cloning of human p48, a transient component of progesterone hormone receptor complexes and an hsp90-binding protein. Mol. Endocrinol. 10:420-431.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 420-431
    • Prapapanich, V.1    Chen, S.2    Nair, S.C.3    Rimerman, R.A.4    Smith, D.F.5
  • 46
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt, W. B., and D. O. Toft. 1997. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocrine Rev. 18:306-360.
    • (1997) Endocrine Rev. , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 48
    • 0023665208 scopus 로고
    • Phosphorylation of eukaryotic initiation factor 2 during physiological stress which affect protein synthesis
    • Scorsone, K. A., R. Panniers, A. G. Rowlands, and E. C. Henshaw. 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
  • 51
    • 0031614812 scopus 로고    scopus 로고
    • Luciferase renaturation assays of chaperones and chaperone antagonists
    • R. LaRossa (ed.), Humana Press, Inc., Totowa, N.J.
    • Thulasiraman, V., and R. L. Matts. 1997. Luciferase renaturation assays of chaperones and chaperone antagonists, p. 129-141. In R. LaRossa (ed.), Methods in molecular biology: bioluminescent protocols. Humana Press, Inc., Totowa, N.J.
    • (1997) Methods in Molecular Biology: Bioluminescent Protocols , pp. 129-141
    • Thulasiraman, V.1    Matts, R.L.2
  • 53
    • 0032146164 scopus 로고    scopus 로고
    • Evidence that Hsc70 negatively modulates the activation of the heme-regulated eIF-2α kinase in rabbit reticulocyte lysate
    • Thulasiraman, V., Z. Xu, S. Uma, Y. Gu, J.-J. Chen, and R. L. Matts. 1998. Evidence that Hsc70 negatively modulates the activation of the heme-regulated eIF-2α kinase in rabbit reticulocyte lysate. Eur. J. Biochem. 255:552-562.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 552-562
    • Thulasiraman, V.1    Xu, Z.2    Uma, S.3    Gu, Y.4    Chen, J.-J.5    Matts, R.L.6
  • 54
    • 0033521588 scopus 로고    scopus 로고
    • In vivo newly translated polypeptides are sequestered in a protected folding environment
    • Thulasiraman, V., C.-F. Yang, and J. Frydman. 1999. In vivo newly translated polypeptides are sequestered in a protected folding environment. EMBO J. 18:85-95.
    • (1999) EMBO J. , vol.18 , pp. 85-95
    • Thulasiraman, V.1    Yang, C.-F.2    Frydman, J.3
  • 55
    • 0030997120 scopus 로고    scopus 로고
    • Hsp90 is obligatory for the heme-regulated eIF-2α kinase to acquire and maintain an activable conformation
    • Uma, S., S. D. Hartson, J.-J. Chen, and R. L. Matts. 1997. Hsp90 is obligatory for the heme-regulated eIF-2α kinase to acquire 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
  • 56
    • 0345631600 scopus 로고    scopus 로고
    • Unpublished observations
    • 55a. Uma, S., and R. L. Matts. Unpublished observations.
    • Uma, S.1    Matts, R.L.2
  • 57
    • 0029937303 scopus 로고    scopus 로고
    • Bcl-2 interacting protein BAG-1, binds to and activates the kinase Raf-1
    • Wang, H.-G., S. Takayama, U. R. Rapp, and J. C. Reed. 1996. Bcl-2 interacting protein BAG-1, binds to and activates the kinase Raf-1. Proc. Natl. Acad. Sci. USA 93:7063-7068.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7063-7068
    • Wang, H.-G.1    Takayama, S.2    Rapp, U.R.3    Reed, J.C.4
  • 58
    • 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 reticulocyte lysates during heat stress
    • Xu, Z., J. K. Pal, V. Thulasiraman, H. P. Hahn, J.-J. Chen, and R. L. Matts. 1997. The role of the 90-kDa heat-shock protein and its associated cohorts in stabilizing the heme-regulated eIF-2α kinase in rabbit reticulocyte 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


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