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Volumn 143, Issue 11, 1997, Pages 3615-3624

Differential HSC70 expression during asexual development of Neurospora crassa

Author keywords

Conidiation; Developmental regulation; Heat shock; HSC70 HSP70; Neurospora crassa

Indexed keywords

8 BROMO CYCLIC AMP; CYCLIC AMP; HEAT SHOCK PROTEIN 70;

EID: 0030696207     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-143-11-3615     Document Type: Article
Times cited : (17)

References (60)
  • 1
    • 0027954495 scopus 로고
    • Heat-shock proteins as molecular chaperones
    • Becker, J. & Craig, E. A. (1994). Heat-shock proteins as molecular chaperones. Eur J Biochem 219, 11-23.
    • (1994) Eur J Biochem , vol.219 , pp. 11-23
    • Becker, J.1    Craig, E.A.2
  • 2
    • 0023515282 scopus 로고
    • Mechanisms of heat shock activation in higher eukaryotes
    • Bienz, M. & Pelham, H. R. B. (1987). Mechanisms of heat shock activation in higher eukaryotes. Adv Genet 24, 31-72.
    • (1987) Adv Genet , vol.24 , pp. 31-72
    • Bienz, M.1    Pelham, H.R.B.2
  • 3
    • 0023148754 scopus 로고
    • Differential expression of heat shock proteins and spontaneous synthesis of HSP70 during the life cycle of Blastocladiella emersonii
    • Bonato, M. C., Silvia, A. M., Gomes, S. L., Maia, J. C. & Juliani, M. H. (1987). Differential expression of heat shock proteins and spontaneous synthesis of HSP70 during the life cycle of Blastocladiella emersonii. Eur J Biochem 163, 211-220.
    • (1987) Eur J Biochem , vol.163 , pp. 211-220
    • Bonato, M.C.1    Silvia, A.M.2    Gomes, S.L.3    Maia, J.C.4    Juliani, M.H.5
  • 4
    • 0016203040 scopus 로고
    • A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels
    • Bonner, W. M. & Laskey, R. A. (1974). A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem 46, 83-88.
    • (1974) Eur J Biochem , vol.46 , pp. 83-88
    • Bonner, W.M.1    Laskey, R.A.2
  • 5
    • 0025307385 scopus 로고
    • Regulation of a yeast HSP70 gene by a cAMP responsive transcriptional control element
    • Boorstein, W. R. & Craig, E. A. (1990). Regulation of a yeast HSP70 gene by a cAMP responsive transcriptional control element. EMBO J 9, 2543-2553.
    • (1990) EMBO J , vol.9 , pp. 2543-2553
    • Boorstein, W.R.1    Craig, E.A.2
  • 6
    • 0027393628 scopus 로고
    • Oxidative injury rapidly activates the heat shock transcription factor but fails to increase levels of heat shock proteins
    • Bruce, J. L., Price, B. D., Coleman, C. N. & Calderwood, S. K. (1993). Oxidative injury rapidly activates the heat shock transcription factor but fails to increase levels of heat shock proteins. Cancer Res 53, 12-15.
    • (1993) Cancer Res , vol.53 , pp. 12-15
    • Bruce, J.L.1    Price, B.D.2    Coleman, C.N.3    Calderwood, S.K.4
  • 7
    • 0024292642 scopus 로고
    • CAMP-independent control of sporulation, glycogen metabolism, and heat shock resistance in Saccharomyces cerevisiae
    • Cameron, S., Levin, L., Zooler, M. & Wigler, M. (1988). cAMP-independent control of sporulation, glycogen metabolism, and heat shock resistance in Saccharomyces cerevisiae. Cell 53, 555-566.
    • (1988) Cell , vol.53 , pp. 555-566
    • Cameron, S.1    Levin, L.2    Zooler, M.3    Wigler, M.4
  • 8
    • 0026095265 scopus 로고
    • CAMP and cAMP-dependent protein kinase regulate the human heat shock protein 70 gene promoter activity
    • Choi, H.-S., Li, B., Lin, Z., Huang, E. & Liu, A. Y.-C (1991). cAMP and cAMP-dependent protein kinase regulate the human heat shock protein 70 gene promoter activity. J Biol Chem 266, 11858-11865.
    • (1991) J Biol Chem , vol.266 , pp. 11858-11865
    • Choi, H.-S.1    Li, B.2    Lin, Z.3    Huang, E.4    Liu, A.Y.-C.5
  • 9
    • 0028448479 scopus 로고
    • Expression of sunflower low-molecular-weight heat-shock proteins during embryogenesis and persistence after germination: Localization and possible functional implications
    • Coca, M. A., Almoguera, C. & Jordano, J. (1994). Expression of sunflower low-molecular-weight heat-shock proteins during embryogenesis and persistence after germination: localization and possible functional implications. Plant Mol Biol 25, 479-492.
    • (1994) Plant Mol Biol , vol.25 , pp. 479-492
    • Coca, M.A.1    Almoguera, C.2    Jordano, J.3
  • 10
    • 0023898306 scopus 로고
    • Cyclic AMP-dependent, constitutive thermotolerance in the adenylate cyclase-deficient cr-1 (crisp) mutant of Neurospora crassa
    • Cruz, A. K., Terenzi, H. F., Jorge, J. A. & Terenzi, H. F. (1988). Cyclic AMP-dependent, constitutive thermotolerance in the adenylate cyclase-deficient cr-1 (crisp) mutant of Neurospora crassa. Curr Genet 13, 451-454.
    • (1988) Curr Genet , vol.13 , pp. 451-454
    • Cruz, A.K.1    Terenzi, H.F.2    Jorge, J.A.3    Terenzi, H.F.4
  • 11
    • 0002953469 scopus 로고
    • Heat shock 70-kD proteins and lysosomal proteolysis
    • Edited by R. I. Morimoto, A. Tissieres & C. Georgopoulos. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory
    • Dice, J. F., Agarraberes, F., Kirven-Brooks, M., Terlecky, L. J. & Terlecky, S. R. (1994). Heat shock 70-kD proteins and lysosomal proteolysis. In The Biology of Heat Shock Proteins and Molecular Chaperones, pp. 137-152. Edited by R. I. Morimoto, A. Tissieres & C. Georgopoulos. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 137-152
    • Dice, J.F.1    Agarraberes, F.2    Kirven-Brooks, M.3    Terlecky, L.J.4    Terlecky, S.R.5
  • 12
    • 0028180628 scopus 로고
    • The yeast and mammalian Ras pathway control transcription of heat shock genes independently of heat shock transcription factor
    • Engelberg, D., Zandi, E., Parker, C. S. & Karin, M. (1994). The yeast and mammalian Ras pathway control transcription of heat shock genes independently of heat shock transcription factor. Mol Cell Biol 14, 4929-4937.
    • (1994) Mol Cell Biol , vol.14 , pp. 4929-4937
    • Engelberg, D.1    Zandi, E.2    Parker, C.S.3    Karin, M.4
  • 13
    • 0027787571 scopus 로고
    • Purification and partial amino acid sequence of the major 70,000-Dalton heat shock protein in Neurospora crassa
    • Fracella, F., Mohsenzadeh, S. & Rensing, L. (1993). Purification and partial amino acid sequence of the major 70,000-Dalton heat shock protein in Neurospora crassa. Exp Mycol 17, 362-367.
    • (1993) Exp Mycol , vol.17 , pp. 362-367
    • Fracella, F.1    Mohsenzadeh, S.2    Rensing, L.3
  • 14
    • 0028911832 scopus 로고
    • Dynamic protein-DNA architecture of a yeast heat shock promoter
    • Giardina, C. & Lis, J. T. (1995). Dynamic protein-DNA architecture of a yeast heat shock promoter. Mol Cell Biol 15, 2737-2744.
    • (1995) Mol Cell Biol , vol.15 , pp. 2737-2744
    • Giardina, C.1    Lis, J.T.2
  • 15
    • 0028117314 scopus 로고
    • Molecular chaperones in protein folding: The art of avoiding sticky situations
    • Hartl, F.-U., Hlodan, R. & Langer, T. (1994). Molecular chaperones in protein folding: the art of avoiding sticky situations. Trends Biochem Sci 19, 20-25.
    • (1994) Trends Biochem Sci , vol.19 , pp. 20-25
    • Hartl, F.-U.1    Hlodan, R.2    Langer, T.3
  • 16
    • 0025208339 scopus 로고
    • DNA binding of heat shock factor to the heat shock element is insufficient for transcriptional activation in murine erythroleukemia cells
    • Hensold, J. O., Hunt, C. R., Calderwood, S. K., Housman, D. E. & Kingston, R. E. (1990). DNA binding of heat shock factor to the heat shock element is insufficient for transcriptional activation in murine erythroleukemia cells. Mol Cell Biol 10, 1600-1608.
    • (1990) Mol Cell Biol , vol.10 , pp. 1600-1608
    • Hensold, J.O.1    Hunt, C.R.2    Calderwood, S.K.3    Housman, D.E.4    Kingston, R.E.5
  • 18
    • 0000049580 scopus 로고
    • Methionine synthesis in Neurospora. the isolation of cystathionine
    • Horowitz, N. H. (1947). Methionine synthesis in Neurospora. The isolation of cystathionine. J Biol Chem 171, 255-264.
    • (1947) J Biol Chem , vol.171 , pp. 255-264
    • Horowitz, N.H.1
  • 19
    • 0021746842 scopus 로고
    • A heat shock-resistant mutant of Saccharomyces cerevisiae shows constitutive synthesis of two heat shock proteins and altered growth
    • Iida, H. & Yahara, I. (1984). A heat shock-resistant mutant of Saccharomyces cerevisiae shows constitutive synthesis of two heat shock proteins and altered growth. J Cell Biol 99, 1441-1450.
    • (1984) J Cell Biol , vol.99 , pp. 1441-1450
    • Iida, H.1    Yahara, I.2
  • 20
    • 0027113344 scopus 로고
    • Effect of sodium salicylate on the human heat shock response
    • Jurivich, D., Sistonen, L., Kroes, R. & Morimoto, R. I. (1992). Effect of sodium salicylate on the human heat shock response. Science 255, 1243-1245.
    • (1992) Science , vol.255 , pp. 1243-1245
    • Jurivich, D.1    Sistonen, L.2    Kroes, R.3    Morimoto, R.I.4
  • 21
    • 0028816665 scopus 로고
    • The hsp70 gene family of Neurospora crassa: Cloning, sequence analysis, expression, and genetic mapping of the major stress-inducible member
    • Kapoor, M., Curle, C. A. & Runham, C. (1995). The hsp70 gene family of Neurospora crassa: cloning, sequence analysis, expression, and genetic mapping of the major stress-inducible member. J Bacteriol 177, 212-221.
    • (1995) J Bacteriol , vol.177 , pp. 212-221
    • Kapoor, M.1    Curle, C.A.2    Runham, C.3
  • 23
    • 0028960212 scopus 로고
    • Heat shock protein Hsp70 accelerates the recovery of heat-shocked mammalian cells through its modulation of heat shock transcription factor HSF1
    • Kim, D., Ouyang, H. & Li, G. C. (1995). Heat shock protein Hsp70 accelerates the recovery of heat-shocked mammalian cells through its modulation of heat shock transcription factor HSF1. Proc Natl Acad Sci USA 92, 2126-2130.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2126-2130
    • Kim, D.1    Ouyang, H.2    Li, G.C.3
  • 24
    • 0021752865 scopus 로고
    • Changing patterns of gene expression during sporulation in yeast
    • Kurtz, S. & Lindquist, S. (1984). Changing patterns of gene expression during sporulation in yeast. Proc Natl Acad Sci USA 81, 7323-7327.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 7323-7327
    • Kurtz, S.1    Lindquist, S.2
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (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
  • 26
    • 0027474070 scopus 로고
    • Dual control of heat shock response: Involvement of a constitutive heat shock element-binding factor
    • Liu, R. Y., Kim, D., Yang, S. H. & Li, G. C. (1993). Dual control of heat shock response: involvement of a constitutive heat shock element-binding factor. Proc Natl Acad Sci USA 90, 3078-3082.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3078-3082
    • Liu, R.Y.1    Kim, D.2    Yang, S.H.3    Li, G.C.4
  • 27
    • 0025965014 scopus 로고
    • Neurospora crassa clock-controlled genes are regulated at the level of transcription
    • Loros, J. J. & Dunlap, J. C. (1991). Neurospora crassa clock-controlled genes are regulated at the level of transcription. Mol Cell Biol 11, 558-563.
    • (1991) Mol Cell Biol , vol.11 , pp. 558-563
    • Loros, J.J.1    Dunlap, J.C.2
  • 28
    • 0027379498 scopus 로고
    • Identification of the heat shock protein of Neurospora crassa corresponding to the stress-inducible peroxidase
    • Machwe, A. & Kapoor, M. (1993). Identification of the heat shock protein of Neurospora crassa corresponding to the stress-inducible peroxidase. Biochem Biophys Res Commun 196, 692-698.
    • (1993) Biochem Biophys Res Commun , vol.196 , pp. 692-698
    • Machwe, A.1    Kapoor, M.2
  • 29
    • 0020576826 scopus 로고
    • Initiation of meiosis in yeast mutants defective in adenylate cyclase and cyclic AMP-dependent protein kinase
    • Matsumoto, K., Uno, I. & Ishikawa, T. (1983). Initiation of meiosis in yeast mutants defective in adenylate cyclase and cyclic AMP-dependent protein kinase. Cell 32, 417-423.
    • (1983) Cell , vol.32 , pp. 417-423
    • Matsumoto, K.1    Uno, I.2    Ishikawa, T.3
  • 30
    • 0016340825 scopus 로고
    • Mutations specifically blocking differentiation of macroconidia in Neurospora crassa
    • Matsuyama, S. S., Nelson, R. E. & Siegel, R. W. (1974). Mutations specifically blocking differentiation of macroconidia in Neurospora crassa. Dev Biol 41, 278-287.
    • (1974) Dev Biol , vol.41 , pp. 278-287
    • Matsuyama, S.S.1    Nelson, R.E.2    Siegel, R.W.3
  • 31
    • 0028263853 scopus 로고
    • Transcription of amphibian lampbrush chromosomes is disturbed by microinjection of HSP70 monoclonal antibodies
    • Moreau, N., Lain, M.-C, Billoud, B. & Angelier, N. (1994). Transcription of amphibian lampbrush chromosomes is disturbed by microinjection of HSP70 monoclonal antibodies. Exp Cell Res 211, 108-114.
    • (1994) Exp Cell Res , vol.211 , pp. 108-114
    • Moreau, N.1    Lain, M.-C.2    Billoud, B.3    Angelier, N.4
  • 32
    • 0026592050 scopus 로고
    • Transcriptional regulation of heat shock genes
    • Morimoto, R. I., Sarge, K. D. & Abravaya, K. (1992). Transcriptional regulation of heat shock genes. J Biol Chem 267, 21987-21990.
    • (1992) J Biol Chem , vol.267 , pp. 21987-21990
    • Morimoto, R.I.1    Sarge, K.D.2    Abravaya, K.3
  • 35
    • 0018609721 scopus 로고
    • A simple, versatile, sensitive and volume-independent method for quantitative protein determination which is independent of other external influences
    • Neuhoff, V., Philipp, K., Zimmer, H. G. & Mesecke, S. (1979). A simple, versatile, sensitive and volume-independent method for quantitative protein determination which is independent of other external influences. Hoppe-Seyler's Z Physiol Chem 360, 1657-1670.
    • (1979) Hoppe-Seyler's Z Physiol Chem , vol.360 , pp. 1657-1670
    • Neuhoff, V.1    Philipp, K.2    Zimmer, H.G.3    Mesecke, S.4
  • 36
    • 0026161705 scopus 로고
    • Photostimulation of conidiation in mutants of Neurospora crassa
    • Ninnemann, H. (1991). Photostimulation of conidiation in mutants of Neurospora crassa, Photochem Photobiol B-Biol 9, 189-199.
    • (1991) Photochem Photobiol B-Biol , vol.9 , pp. 189-199
    • Ninnemann, H.1
  • 37
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P. H. (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
  • 38
    • 0029087122 scopus 로고
    • Developmentally regulated expression of heat shock genes in Leptosphaeria maculans
    • Patterson, N. A. & Kapoor, M. (1995). Developmentally regulated expression of heat shock genes in Leptosphaeria maculans. Can J Biochem 41, 499-507.
    • (1995) Can J Biochem , vol.41 , pp. 499-507
    • Patterson, N.A.1    Kapoor, M.2
  • 39
    • 0028171863 scopus 로고
    • CAMP modulates stress protein synthesis in human monocytes-macrophages
    • Pizurki, L. & Polla, B. (1994). cAMP modulates stress protein synthesis in human monocytes-macrophages. J Cell Physiol 161, 169-177.
    • (1994) J Cell Physiol , vol.161 , pp. 169-177
    • Pizurki, L.1    Polla, B.2
  • 40
    • 0021810896 scopus 로고
    • The heat shock response of Neurospora crassa: Protein synthesis and induced thermotolerance
    • Plesofsky-Vig, N. & Brambl, R. (1985a). The heat shock response of Neurospora crassa: protein synthesis and induced thermotolerance. J Bacteriol 162, 1083-1091.
    • (1985) J Bacteriol , vol.162 , pp. 1083-1091
    • Plesofsky-Vig, N.1    Brambl, R.2
  • 41
    • 0022003149 scopus 로고
    • The heat shock response of fungi
    • Plesofsky-Vig, N. & Brambl, R. (1985b). The heat shock response of fungi. Exp Mycol 9, 187-194.
    • (1985) Exp Mycol , vol.9 , pp. 187-194
    • Plesofsky-Vig, N.1    Brambl, R.2
  • 42
    • 0025078939 scopus 로고
    • Gene sequence and analysis of hsp30, a small heat shock protein of Neurospora crassa which associates with mitochondria
    • Plesofsky-Vig, N. & Brambl, R. (1990). Gene sequence and analysis of hsp30, a small heat shock protein of Neurospora crassa which associates with mitochondria. J Biol Chem 265, 15432-15440.
    • (1990) J Biol Chem , vol.265 , pp. 15432-15440
    • Plesofsky-Vig, N.1    Brambl, R.2
  • 43
    • 0028025643 scopus 로고
    • Interaction between heat shock factor and Hsp70 is insufficient to suppress induction of DNA-binding activity in vivo
    • Rabindran, S. K., Wisniewski, J., Li, L., Li, G. C. & Wu, C. (1994). Interaction between heat shock factor and Hsp70 is insufficient to suppress induction of DNA-binding activity in vivo. Mol Cell Biol 14, 6552-6560.
    • (1994) Mol Cell Biol , vol.14 , pp. 6552-6560
    • Rabindran, S.K.1    Wisniewski, J.2    Li, L.3    Li, G.C.4    Wu, C.5
  • 44
    • 0024027150 scopus 로고
    • Molecular analysis of a Neurospora crassa gene expressed during conidiation
    • Roberts, A., Berlin, V., Hager, K. M. & Yanofsky, C. (1988). Molecular analysis of a Neurospora crassa gene expressed during conidiation. Mol Cell Biol 8, 2411-2418.
    • (1988) Mol Cell Biol , vol.8 , pp. 2411-2418
    • Roberts, A.1    Berlin, V.2    Hager, K.M.3    Yanofsky, C.4
  • 45
    • 0027027630 scopus 로고
    • Hsp80 of Neurospora crassa: CDNA cloning, gene mapping, and studies of mRNA accumulation under stress
    • Roychowdhury, H. S., Wong, D. & Kapoor, M. (1992). hsp80 of Neurospora crassa: cDNA cloning, gene mapping, and studies of mRNA accumulation under stress. Biochem Cell Biol 70, 1356-1367.
    • (1992) Biochem Cell Biol , vol.70 , pp. 1356-1367
    • Roychowdhury, H.S.1    Wong, D.2    Kapoor, M.3
  • 46
    • 0344501034 scopus 로고
    • Development in N. crassa
    • Edited by V. E. A. Russo, S. Brody, D. Cove & S. Ottolenghi. Heidelberg: Springer
    • Russo, V. E. A. & Pandit, N. N. (1992). Development in N. crassa. In Development - the Molecular Genetic Approach, pp. 88-102. Edited by V. E. A. Russo, S. Brody, D. Cove & S. Ottolenghi. Heidelberg: Springer.
    • (1992) Development - The Molecular Genetic Approach , pp. 88-102
    • Russo, V.E.A.1    Pandit, N.N.2
  • 47
    • 0026643651 scopus 로고
    • The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate
    • Shi, Y. & Thomas, J. O. (1992). The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate. Mol Cell Biol 12, 2186-2192.
    • (1992) Mol Cell Biol , vol.12 , pp. 2186-2192
    • Shi, Y.1    Thomas, J.O.2
  • 48
    • 0023079112 scopus 로고
    • Heat shock response of Saccharomyces cerevisiae mutants altered in cyclic AMP-dependent protein phosphorylation
    • Shin, D.-Y., Matsumoto, K., Iida, H., Uno, I. & Ishikawa, T. (1987). Heat shock response of Saccharomyces cerevisiae mutants altered in cyclic AMP-dependent protein phosphorylation. Mol Cell Biol 7, 244-250.
    • (1987) Mol Cell Biol , vol.7 , pp. 244-250
    • Shin, D.-Y.1    Matsumoto, K.2    Iida, H.3    Uno, I.4    Ishikawa, T.5
  • 49
    • 0024282785 scopus 로고
    • Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation
    • Sorger, P. K. & Pelham, H. R. B. (1988). Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation. Cell 54, 855-864.
    • (1988) Cell , vol.54 , pp. 855-864
    • Sorger, P.K.1    Pelham, H.R.B.2
  • 50
    • 0023643235 scopus 로고
    • Heat shock factor is regulated differently in yeast and HeLa cells
    • Sorger, P. K., Lewis, M. J. & Pelham, H. R. B. (1987). Heat shock factor is regulated differently in yeast and HeLa cells. Nature 329, 81-84.
    • (1987) Nature , vol.329 , pp. 81-84
    • Sorger, P.K.1    Lewis, M.J.2    Pelham, H.R.B.3
  • 51
    • 0024651274 scopus 로고
    • A morphological and genetic analysis of conidiophore development in Neurospora crassa
    • Springer, M. & Yanofsky, C. (1989). A morphological and genetic analysis of conidiophore development in Neurospora crassa. Genes Dev 3, 559-571.
    • (1989) Genes Dev , vol.3 , pp. 559-571
    • Springer, M.1    Yanofsky, C.2
  • 52
    • 0016240020 scopus 로고
    • A Neurospora crassa morphological mutant showing reduced adenylate cyclase activity
    • Terenzi, H., Flawia, M. & Torres, H. (1974). A Neurospora crassa morphological mutant showing reduced adenylate cyclase activity. Biochem Biophys Res Commun 58, 990-996.
    • (1974) Biochem Biophys Res Commun , vol.58 , pp. 990-996
    • Terenzi, H.1    Flawia, M.2    Torres, H.3
  • 53
    • 0029002553 scopus 로고
    • Redox imbalance at the start of each morphogenetic step of Neurospora crassa conidiation
    • Toledo, I., Rangel, P. & Hansberg, W. (1995). Redox imbalance at the start of each morphogenetic step of Neurospora crassa conidiation. Arch Biochem Biophys 319, 519-524.
    • (1995) Arch Biochem Biophys , vol.319 , pp. 519-524
    • Toledo, I.1    Rangel, P.2    Hansberg, W.3
  • 54
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. M. & Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76, 4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.M.2    Gordon, J.3
  • 55
    • 0026677814 scopus 로고
    • Isolation, partial amino acid sequence, and cellular distribution of heat-shock protein Hsp98 from Neurospora crassa
    • Vassilev, A. O., Plesofsky-Vig, N. & Brambl, R. (1992). Isolation, partial amino acid sequence, and cellular distribution of heat-shock protein Hsp98 from Neurospora crassa. Biochim Biophys Acta 1156, 1-6.
    • (1992) Biochim Biophys Acta , vol.1156 , pp. 1-6
    • Vassilev, A.O.1    Plesofsky-Vig, N.2    Brambl, R.3
  • 56
    • 0001963674 scopus 로고
    • A convenient growth medium for Neurospora (medium M)
    • Vogel, H. J. (1956). A convenient growth medium for Neurospora (medium M). Microb Genet Bull 13, 42-43.
    • (1956) Microb Genet Bull , vol.13 , pp. 42-43
    • Vogel, H.J.1
  • 57
    • 0027352499 scopus 로고
    • The disappearance of an HSC70 species in mung bean seed during germination: Sssssspurification and characterization of the protein
    • Wang, C. & Lin, B. L. (1993). The disappearance of an HSC70 species in mung bean seed during germination: sssssspurification and characterization of the protein. Plant Mol Biol 21, 317-329.
    • (1993) Plant Mol Biol , vol.21 , pp. 317-329
    • Wang, C.1    Lin, B.L.2
  • 58
    • 0024670024 scopus 로고
    • Yeast HSP70 RNA levels vary in response to the physiological status of the cell
    • Werner-Washburne, M., Becker, J., Kosic-Smithers, J. & Craig, E. A. (1989). Yeast HSP70 RNA levels vary in response to the physiological status of the cell. J Bacteriol 171, 2680-2688.
    • (1989) J Bacteriol , vol.171 , pp. 2680-2688
    • Werner-Washburne, M.1    Becker, J.2    Kosic-Smithers, J.3    Craig, E.A.4
  • 59
    • 0024411246 scopus 로고
    • E1a transactivation of the human HSP70 promoter is mediated through the basal transcriptional complex
    • Williams, G. T., McClanahan, T. L. & Morimoto, R. I. (1989). E1a transactivation of the human HSP70 promoter is mediated through the basal transcriptional complex. Mol Cell Biol 9, 2574-2587.
    • (1989) Mol Cell Biol , vol.9 , pp. 2574-2587
    • Williams, G.T.1    McClanahan, T.L.2    Morimoto, R.I.3
  • 60
    • 0023251292 scopus 로고
    • Detection of three protein binding sites in the serum-regulated promoter of the human gene encoding the 70-kDa heat shock protein
    • Wu, B. J., Kingston, R. E. & Morimoto, R. I. (1987). Detection of three protein binding sites in the serum-regulated promoter of the human gene encoding the 70-kDa heat shock protein. Proc Natl Acad Sci USA 84, 2203-2207.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 2203-2207
    • Wu, B.J.1    Kingston, R.E.2    Morimoto, R.I.3


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