메뉴 건너뛰기




Volumn 206, Issue 6, 1997, Pages 397-406

Tissue-specific expression of an hsc90 gene and nuclear translocation of the HSC90-related protein during amphibian embryogenesis

Author keywords

Amphibian; Development; Heat shock proteins 90; Molecular chaperones

Indexed keywords

HEAT SHOCK PROTEIN 90; MESSENGER RNA; AMPHIBIAN PROTEIN;

EID: 0031020541     PISSN: 0949944X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004270050069     Document Type: Article
Times cited : (4)

References (65)
  • 1
    • 0028589101 scopus 로고
    • A role for HSP90 in cell cycle control: Weel tyrosine kinase activity requires interaction with HSP90
    • Aligue R, Akhavan-niak H, Russel P (1994) A role for HSP90 in cell cycle control: Weel tyrosine kinase activity requires interaction with HSP90. EMBO J 13:6099-6106
    • (1994) EMBO J , vol.13 , pp. 6099-6106
    • Aligue, R.1    Akhavan-niak, H.2    Russel, P.3
  • 2
    • 0029833883 scopus 로고    scopus 로고
    • Does the chaperone heat-shock protein HSP70 play a role in control of developmental processes?
    • Angelier N, Moreau N, Rodriguez-Martin ML, Prudhomme C (1996) Does the chaperone heat-shock protein HSP70 play a role in control of developmental processes? Int J Dev Biol 40: 521-529
    • (1996) Int J Dev Biol , vol.40 , pp. 521-529
    • Angelier, N.1    Moreau, N.2    Rodriguez-Martin, M.L.3    Prudhomme, C.4
  • 3
    • 0028858813 scopus 로고
    • Distinct roles of the molecular chaperone hsp90 in modulating dioxin receptor function via basic helix-loop-helix and PAS domains
    • Antonsson C, Whitelaw ML, McGuire J, Gustafsson JA, Poellinger L (1995) Distinct roles of the molecular chaperone hsp90 in modulating dioxin receptor function via basic helix-loop-helix and PAS domains. Mol Cell Biol 15:756-765
    • (1995) Mol Cell Biol , vol.15 , pp. 756-765
    • Antonsson, C.1    Whitelaw, M.L.2    McGuire, J.3    Gustafsson, J.A.4    Poellinger, L.5
  • 4
    • 0019023345 scopus 로고
    • Purification of mouse immunoglobulin heavy-chain messenger RNAs from myeloma tumor RNA
    • Auffray C, Rougeon F (1980) Purification of mouse immunoglobulin heavy-chain messenger RNAs from myeloma tumor RNA. Eur J Biochem 107:303-314
    • (1980) Eur J Biochem , vol.107 , pp. 303-314
    • Auffray, C.1    Rougeon, F.2
  • 5
    • 0022779172 scopus 로고
    • Translational activation of maternal mRNA encoding the heat-shock protein HSP90 during sea urchin embryogenesis
    • Bedard PA, Brandhorst BP (1986) Translational activation of maternal mRNA encoding the heat-shock protein HSP90 during sea urchin embryogenesis. Dev Biol 117:286-293
    • (1986) Dev Biol , vol.117 , pp. 286-293
    • Bedard, P.A.1    Brandhorst, B.P.2
  • 6
    • 0021092952 scopus 로고
    • Spontaneous high expression of heat-shock proteins in mouse embryonnal carcinoma cells and ectoderm from day 8 mouse embryo
    • Bensaüde O, Morange M (1983) Spontaneous high expression of heat-shock proteins in mouse embryonnal carcinoma cells and ectoderm from day 8 mouse embryo. EMBO J 2:173-177
    • (1983) EMBO J , vol.2 , pp. 173-177
    • Bensaüde, O.1    Morange, M.2
  • 9
    • 0024421221 scopus 로고
    • HSP82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures
    • Borkovich KA, Farelly FW, Finkelstein DB, Taulien J, Lindquist S (1989) HSP82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol Cell Biol 9:3919-3930
    • (1989) Mol Cell Biol , vol.9 , pp. 3919-3930
    • Borkovich, K.A.1    Farelly, F.W.2    Finkelstein, D.B.3    Taulien, J.4    Lindquist, S.5
  • 10
  • 12
    • 0028923673 scopus 로고
    • Evidence for a 90 kDa heat-shock protein gene expression in the amphibian oocyte
    • Coumailleau P, Billoud B, Sourrouille P, Moreau N, Angelier N (1995a) Evidence for a 90 kDa heat-shock protein gene expression in the amphibian oocyte. Dev Biol 168:247-258
    • (1995) Dev Biol , vol.168 , pp. 247-258
    • Coumailleau, P.1    Billoud, B.2    Sourrouille, P.3    Moreau, N.4    Angelier, N.5
  • 13
    • 0028823398 scopus 로고
    • Definition of a minimal domain of the dioxin receptor that is associated with hsp90 and maintains wild type ligand binding affinity and specificity
    • Coumailleau P, Poellinger L, Gustafsson JA, Whitelaw ML (1995b) Definition of a minimal domain of the dioxin receptor that is associated with hsp90 and maintains wild type ligand binding affinity and specificity. J Biol Chem 270:25291-25300
    • (1995) J Biol Chem , vol.270 , pp. 25291-25300
    • Coumailleau, P.1    Poellinger, L.2    Gustafsson, J.A.3    Whitelaw, M.L.4
  • 16
    • 0026578738 scopus 로고
    • Gene expression in the Caenorhabditis elegans Dauer larva: Developmental regulation of hsp90 and other genes
    • Dalley B, Golomb M (1992) Gene expression in the Caenorhabditis elegans Dauer larva: developmental regulation of hsp90 and other genes. Dev Biol 151:80-90
    • (1992) Dev Biol , vol.151 , pp. 80-90
    • Dalley, B.1    Golomb, M.2
  • 17
    • 0023068568 scopus 로고
    • Identification of the 90 kDa substrate of rat liver type II casein kinase with the heat-shock proteins which binds steroid receptors
    • Dougherty JJ, Rabideau DD, lannotti AM, Sullivan WP, Toft DO (1987) Identification of the 90 kDa substrate of rat liver type II casein kinase with the heat-shock proteins which binds steroid receptors. Biochem Biophys Acta 927:74-80
    • (1987) Biochem Biophys Acta , vol.927 , pp. 74-80
    • Dougherty, J.J.1    Rabideau, D.D.2    Lannotti, A.M.3    Sullivan, W.P.4    Toft, D.O.5
  • 18
    • 0021355126 scopus 로고
    • Complete sequence of the heat shock-inducible HSP90 gene of Saccharomyces cerevisiae
    • Farrelly FW, Finkelstein DB (1984) Complete sequence of the heat shock-inducible HSP90 gene of Saccharomyces cerevisiae. J Biol Chem 259:5745-5751
    • (1984) J Biol Chem , vol.259 , pp. 5745-5751
    • Farrelly, F.W.1    Finkelstein, D.B.2
  • 20
    • 0001942572 scopus 로고
    • Table chronologique du développement chez Pleurodeles waltlii
    • Gallien L, Durocher M (1957) Table chronologique du développement chez Pleurodeles waltlii. Bull Biol Fr Belg 91:97-114
    • (1957) Bull Biol Fr Belg , vol.91 , pp. 97-114
    • Gallien, L.1    Durocher, M.2
  • 21
    • 0021711644 scopus 로고
    • Progesterone receptor in the chick oviduct: An immunohistochemical study with antibodies to distinct receptor components
    • Gasc J, Renoir J, Radanyi C, Joab I, Tuohimaa P, Baulieu EE (1984) Progesterone receptor in the chick oviduct: an immunohistochemical study with antibodies to distinct receptor components. JCell Biol 99:1193
    • (1984) JCell Biol , vol.99 , pp. 1193
    • Gasc, J.1    Renoir, J.2    Radanyi, C.3    Joab, I.4    Tuohimaa, P.5    Baulieu, E.E.6
  • 22
    • 0025171925 scopus 로고
    • Nuclear localization of two steroid receptor associated proteins, HSP90 and P59
    • Gasc JM, Renoir JM, Faber LE, Delahaye F, Baulieu EE (1990) Nuclear localization of two steroid receptor associated proteins, HSP90 and P59. Exp Cell Res 186:362-367
    • (1990) Exp Cell Res , vol.186 , pp. 362-367
    • Gasc, J.M.1    Renoir, J.M.2    Faber, L.E.3    Delahaye, F.4    Baulieu, E.E.5
  • 24
    • 0026092207 scopus 로고
    • Stage and lineage-regulated expression of two HSP90 transcripts during mouse germ cell differentiation and embryogenesis
    • Gruppi CM, Zakeri ZF, Wolgemuth DJ (1991) Stage and lineage-regulated expression of two HSP90 transcripts during mouse germ cell differentiation and embryogenesis. Mol Reprod Dev 28:209-217
    • (1991) Mol Reprod Dev , vol.28 , pp. 209-217
    • Gruppi, C.M.1    Zakeri, Z.F.2    Wolgemuth, D.J.3
  • 25
    • 0028987872 scopus 로고
    • The arylhydrocarbon receptor complex
    • Hankinson O (1995) The arylhydrocarbon receptor complex. Annu Rev Pharmacol Toxicol 35:307-340
    • (1995) Annu Rev Pharmacol Toxicol , vol.35 , pp. 307-340
    • Hankinson, O.1
  • 26
    • 0026285616 scopus 로고
    • In situ hybridization: An improved whole-mount method for Xenopus embryos
    • Harland RM (1991) In situ hybridization: an improved whole-mount method for Xenopus embryos. Meth Cell Biol 36:685-695
    • (1991) Meth Cell Biol , vol.36 , pp. 685-695
    • Harland, R.M.1
  • 27
    • 0022339762 scopus 로고
    • Distribution of nuclear proteins during maturation of the xenopus oocyte
    • Hausen P, Wang YH, Dreyer C, Stick R (1985) Distribution of nuclear proteins during maturation of the xenopus oocyte. J Embryol Exp Morphol 89 Suppl.: 17-34
    • (1985) J Embryol Exp Morphol , vol.89 , Issue.SUPPL. , pp. 17-34
    • Hausen, P.1    Wang, Y.H.2    Dreyer, C.3    Stick, R.4
  • 28
    • 0027487094 scopus 로고
    • Immunolocalization of HSP70-related proteins constitutively expressed during Xenopus laevis oogenesis and development
    • Herberts C, Moreau N, Angelier N (1993) Immunolocalization of HSP70-related proteins constitutively expressed during Xenopus laevis oogenesis and development. Int J Dev Biol 37: 397-406
    • (1993) Int J Dev Biol , vol.37 , pp. 397-406
    • Herberts, C.1    Moreau, N.2    Angelier, N.3
  • 29
    • 0024364170 scopus 로고
    • Sequence and regulation of a gene encoding a human 89-kilodalton heat-shock protein
    • Hickey E, Brandon SE, Smale G, Lloyd D, Weber LA (1989) Sequence and regulation of a gene encoding a human 89-kilodalton heat-shock protein. Mol Cell Biol 9:2615-2626
    • (1989) Mol Cell Biol , vol.9 , pp. 2615-2626
    • Hickey, E.1    Brandon, S.E.2    Smale, G.3    Lloyd, D.4    Weber, L.A.5
  • 32
    • 0028171452 scopus 로고
    • hsp90α and HSP90β genes are present in the zebrafish and are differentially regulated in developing embryos
    • Krone PH, Sass JB (1994) hsp90α and HSP90β genes are present in the zebrafish and are differentially regulated in developing embryos. Biochem Biophys Res Commun 204:746-752
    • (1994) Biochem Biophys Res Commun , vol.204 , pp. 746-752
    • Krone, P.H.1    Sass, J.B.2
  • 33
    • 0022462428 scopus 로고
    • An ancient development induction: Heat-shock proteins induced in sporulation and oogenesis
    • Kurtz S, Rossi J, Petko L, Lindquist S (1986) An ancient development induction: heat-shock proteins induced in sporulation and oogenesis. Science 231:1154-1157
    • (1986) Science , vol.231 , pp. 1154-1157
    • Kurtz, S.1    Rossi, J.2    Petko, L.3    Lindquist, S.4
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0021708673 scopus 로고
    • Quantitation and intracellular localization of the 85 K heat-shock protein by using monoclonal and polyclonal antibodies
    • Lai BT, Chin NW, Stanek AE, Keh W, Lanks KW (1984) Quantitation and intracellular localization of the 85 K heat-shock protein by using monoclonal and polyclonal antibodies. Mol Cell Biol 4:2802-2810
    • (1984) Mol Cell Biol , vol.4 , pp. 2802-2810
    • Lai, B.T.1    Chin, N.W.2    Stanek, A.E.3    Keh, W.4    Lanks, K.W.5
  • 37
    • 0002024938 scopus 로고
    • The expression of heat shock genes during normal development in Drosophila melanogaster
    • Mason PJ, Hall LMC, Gausz J (1984) The expression of heat shock genes during normal development in Drosophila melanogaster. Mol Gen Genet 194:73-78
    • (1984) Mol Gen Genet , vol.194 , pp. 73-78
    • Mason, P.J.1    Hall, L.M.C.2    Gausz, J.3
  • 38
    • 0024468795 scopus 로고
    • Evidence for the association of the heme-regulated eIF-2a kinase with the 90 kDa heat-shock protein in rabbit reticulocyte lysate in situ
    • Matts RL, Hurst RH (1989) Evidence for the association of the heme-regulated eIF-2a kinase with the 90 kDa heat-shock protein in rabbit reticulocyte lysate in situ. J Biol Chem 264: 15542-15547
    • (1989) J Biol Chem , vol.264 , pp. 15542-15547
    • Matts, R.L.1    Hurst, R.H.2
  • 39
    • 0029611034 scopus 로고
    • The basic Helix-Loop-Helix/PAS factor SIM is associated with hsp90. Implication for regulation by interaction with partner factors
    • McGuire J, Coumailleau P, Whitelaw ML, Gustafsson JA, Poellinger L (1995) The basic Helix-Loop-Helix/PAS factor SIM is associated with hsp90. Implication for regulation by interaction with partner factors. J Biol Chem 270:31353-31357
    • (1995) J Biol Chem , vol.270 , pp. 31353-31357
    • McGuire, J.1    Coumailleau, P.2    Whitelaw, M.L.3    Gustafsson, J.A.4    Poellinger, L.5
  • 42
    • 0028046712 scopus 로고
    • Detection of heat-shock element-binding activities by gel shift assay during mouse preimplantation development
    • Mezger V, Renard JP, Christians E, Morange M (1994b) Detection of heat-shock element-binding activities by gel shift assay during mouse preimplantation development. Dev Biol 165:627-638
    • (1994) Dev Biol , vol.165 , pp. 627-638
    • Mezger, V.1    Renard, J.P.2    Christians, E.3    Morange, M.4
  • 43
    • 0026669310 scopus 로고
    • The 90-kDa heat-shock protein, HSP90, binds and protects casein kinase II from self-agregation and enhances its kinase activity
    • Miyata Y, Yahara I (1992) The 90-kDa heat-shock protein, HSP90, binds and protects casein kinase II from self-agregation and enhances its kinase activity. J Biol Chem 267:7042-7047
    • (1992) J Biol Chem , vol.267 , pp. 7042-7047
    • Miyata, Y.1    Yahara, I.2
  • 44
    • 0024542186 scopus 로고
    • Murine 86- and 84-kDa heat-shock proteins cDNA sequences, chromosome assignments, and evolutionary origins
    • Moore SK, Kozak C, Robinson E.A, Ullrich SJ, Appella E (1989) Murine 86- and 84-kDa heat-shock proteins cDNA sequences, chromosome assignments, and evolutionary origins. J Biol Chem 264:5343-5351
    • (1989) J Biol Chem , vol.264 , pp. 5343-5351
    • Moore, S.K.1    Kozak, C.2    Robinson, E.A.3    Ullrich, S.J.4    Appella, E.5
  • 45
    • 0027419466 scopus 로고
    • The Drosophila single-minded gene encodes a helix-loop-helix-protein that acts as a master regulator of CNS midline development
    • Nambu JR, Lewis JO, Crews ST (1993) The Drosophila single-minded gene encodes a helix-loop-helix-protein that acts as a master regulator of CNS midline development. Comp Biochem Physiol 104A:399-409
    • (1993) Comp Biochem Physiol , vol.104 A , pp. 399-409
    • Nambu, J.R.1    Lewis, J.O.2    Crews, S.T.3
  • 46
    • 0023024149 scopus 로고
    • Calmoduline-regulated binding of the 90 kDa heat-shock protein to actin filaments
    • Nishida E, Koyasu S, Sakai H, Yahara I (1986) Calmoduline-regulated binding of the 90 kDa heat-shock protein to actin filaments. J Biol Chem 261:16033-16036
    • (1986) J Biol Chem , vol.261 , pp. 16033-16036
    • Nishida, E.1    Koyasu, S.2    Sakai, H.3    Yahara, I.4
  • 47
    • 0016711037 scopus 로고
    • High resolution two dimensional electrophoresis of proteins
    • O' Farrell PH (1975) High resolution two dimensional electrophoresis of proteins. J Biol Chem 250:4007-4021
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O' Farrell, P.H.1
  • 48
    • 0025151698 scopus 로고
    • DNA sequencespecific binding activity of the heat shock transcription factor is heat-inducible before the midblastula transition of early Xenopus development
    • Ovsenek N, Heikkila JJ (1990) DNA sequencespecific binding activity of the heat shock transcription factor is heat-inducible before the midblastula transition of early Xenopus development. Development 110:427-433
    • (1990) Development , vol.110 , pp. 427-433
    • Ovsenek, N.1    Heikkila, J.J.2
  • 49
    • 0025815731 scopus 로고
    • Evidence that the 90 kDa heat-shock protein (HSP90) exists in cytosol in heteromeric complexes containing HSP70 and three other proteins with Mr of 63,000, 56,000 and 50,000
    • Perdew GH, Whitelaw ML (1991) Evidence that the 90 kDa heat-shock protein (HSP90) exists in cytosol in heteromeric complexes containing HSP70 and three other proteins with Mr of 63,000, 56,000 and 50,000. J Biol Chem 266:6708-6713
    • (1991) J Biol Chem , vol.266 , pp. 6708-6713
    • Perdew, G.H.1    Whitelaw, M.L.2
  • 51
    • 0027451956 scopus 로고
    • The role of heat-shock proteins in regulating the function, folding and trafficking of the glucocorticoid receptor
    • Pratt WB (1993) The role of heat-shock proteins in regulating the function, folding and trafficking of the glucocorticoid receptor. J Biol Chem 268:21455-21458
    • (1993) J Biol Chem , vol.268 , pp. 21455-21458
    • Pratt, W.B.1
  • 52
    • 0024442546 scopus 로고
    • Immunofluorescence colocalization of the 90 kDa heat-shock protein and microtubules in interphase and mitotic mammalian cells
    • Redmond T, Sanchez ER, Bresnick EH, Schlesinger MJ, Toft DO, Pratt WB, Welsh MJ (1989) Immunofluorescence colocalization of the 90 kDa heat-shock protein and microtubules in interphase and mitotic mammalian cells. Eur J Cell Biol 50:66-75
    • (1989) Eur J Cell Biol , vol.50 , pp. 66-75
    • Redmond, T.1    Sanchez, E.R.2    Bresnick, E.H.3    Schlesinger, M.J.4    Toft, D.O.5    Pratt, W.B.6    Welsh, M.J.7
  • 53
    • 0024456399 scopus 로고
    • Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells
    • Rothmann JE (1989) Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells. Cell 59: 591-601
    • (1989) Cell , vol.59 , pp. 591-601
    • Rothmann, J.E.1
  • 54
    • 0023766565 scopus 로고
    • Evidence that the 90-kilodalton heat-shock protein is associated with tubulin-containing complexes in L cell cytosol and in intact PtK cells
    • Sanchez ER, Redmond T, Scherrer LC, Bresnick EH, Welsh MJ, Pratt WB (1988) Evidence that the 90-kilodalton heat-shock protein is associated with tubulin-containing complexes in L cell cytosol and in intact PtK cells. Mol Endocrinol 2:756-760
    • (1988) Mol Endocrinol , vol.2 , pp. 756-760
    • Sanchez, E.R.1    Redmond, T.2    Scherrer, L.C.3    Bresnick, E.H.4    Welsh, M.J.5    Pratt, W.B.6
  • 55
    • 0025290187 scopus 로고
    • The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70 and 90-kilodalton heat-shock proteins
    • Sanchez ER, Faber LE, Henzel WJ, Pratt WB (1990) The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70 and 90-kilodalton heat-shock proteins. Biochemistry 29:5145-5152
    • (1990) Biochemistry , vol.29 , pp. 5145-5152
    • Sanchez, E.R.1    Faber, L.E.2    Henzel, W.J.3    Pratt, W.B.4
  • 56
    • 0030029444 scopus 로고    scopus 로고
    • Specific localization of zebrafish hsp90α mRNA to myoD-expressing cells suggests a role for hsp90α during normal muscle development
    • Sass JB, Weinberg ES, Krone PH (1996) Specific localization of zebrafish hsp90α mRNA to myoD-expressing cells suggests a role for hsp90α during normal muscle development. Mech Dev 54-195-204
    • (1996) Mech Dev , vol.54 , pp. 195-204
    • Sass, J.B.1    Weinberg, E.S.2    Krone, P.H.3
  • 57
    • 0026722373 scopus 로고
    • Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84)
    • Shaknovich R, Shue G, Kohtz DS (1992) Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84). Mol Cell Biol 12: 5059-5068
    • (1992) Mol Cell Biol , vol.12 , pp. 5059-5068
    • Shaknovich, R.1    Shue, G.2    Kohtz, D.S.3
  • 58
    • 0027980828 scopus 로고
    • Structural and functional aspects of basic helix-loop-helix protein folding by heat-shock protein 90
    • Shue G, Kohtz DS (1994) Structural and functional aspects of basic helix-loop-helix protein folding by heat-shock protein 90. J Biol Chem 269:2707-2711
    • (1994) J Biol Chem , vol.269 , pp. 2707-2711
    • Shue, G.1    Kohtz, D.S.2
  • 59
    • 0027433644 scopus 로고
    • Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstitutet in a cell-free system
    • Stancato LF, Chow YH, Hutchinson KA, Perdew GH, Joves R, Pratt WB (1993) Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstitutet in a cell-free system. J Biol Chem 268:21711-21716
    • (1993) J Biol Chem , vol.268 , pp. 21711-21716
    • Stancato, L.F.1    Chow, Y.H.2    Hutchinson, K.A.3    Perdew, G.H.4    Joves, R.5    Pratt, W.B.6
  • 60
    • 0021980039 scopus 로고
    • Double-stranded DNA induces the phosphorylation of several proteins including the 90 000 mol. wt. heat-shock protein in animal cell extracts
    • Walker AI, Hunt T, Jackson RJ, Anderson CW (1985) Double-stranded DNA induces the phosphorylation of several proteins including the 90 000 mol. wt. heat-shock protein in animal cell extracts. EMBO J 4:139-145
    • (1985) EMBO J , vol.4 , pp. 139-145
    • Walker, A.I.1    Hunt, T.2    Jackson, R.J.3    Anderson, C.W.4
  • 62
  • 64
    • 0022327612 scopus 로고
    • Steroid receptor regulated transcription of specific genes and gene networks
    • Yamamoto KR (1985) Steroid receptor regulated transcription of specific genes and gene networks. Annu Rev Genet 19:209-215
    • (1985) Annu Rev Genet , vol.19 , pp. 209-215
    • Yamamoto, K.R.1
  • 65
    • 0020578024 scopus 로고
    • Accumulation of a specific subset of D. melanogaster heat shock mRNAs in normal development without heat shock
    • Zimmerman JL, Petri W, Meselson M (1983) Accumulation of a specific subset of D. melanogaster heat shock mRNAs in normal development without heat shock. Cell 32:1161-1170
    • (1983) Cell , vol.32 , pp. 1161-1170
    • Zimmerman, J.L.1    Petri, W.2    Meselson, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.