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Volumn 30, Issue 6, 1998, Pages 745-759

Concomitant alterations in distribution of 70 kDA heat shock proteins, cytoskeleton and organelles in heat shocked 9L cells

Author keywords

Cell architecture; Cytoskeleton; Heat shock; Heat shock proteins; Organelles

Indexed keywords

ACTIN; HEAT SHOCK PROTEIN;

EID: 0031860326     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(97)00133-7     Document Type: Article
Times cited : (31)

References (55)
  • 1
    • 0027954495 scopus 로고
    • Heat-shock proteins as molecular chaperones
    • Becker J., Craig E.A. Heat-shock proteins as molecular chaperones. Eur. J. Biochem. 219:1994;11-23.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 11-23
    • Becker, J.1    Craig, E.A.2
  • 2
    • 0026162393 scopus 로고
    • Animal cell shape changes and gene expression
    • Ben-Ze'ev A. Animal cell shape changes and gene expression. Bioessays. 13:1991;207-212.
    • (1991) Bioessays , vol.13 , pp. 207-212
    • Ben-Ze'ev, A.1
  • 4
    • 0027509361 scopus 로고
    • The constitutive and stress inducible forms of hsp 70 exhibit functional similarities and interact with one another in an ATP-dependent fashion
    • Brown C.R., Martin R.L., Hansen W.J., Beckmann R.P., Welch W.J. The constitutive and stress inducible forms of hsp 70 exhibit functional similarities and interact with one another in an ATP-dependent fashion. J. Cell Biol. 120:1993;1101-1112.
    • (1993) J. Cell Biol. , vol.120 , pp. 1101-1112
    • Brown, C.R.1    Martin, R.L.2    Hansen, W.J.3    Beckmann, R.P.4    Welch, W.J.5
  • 5
    • 0024483266 scopus 로고
    • Fluorescent labeling of mitochondria
    • Y.-L. Wang, S.L. Taylor (Eds.), Fluorescence Microscopy of Living Cells in Culture, Part A: Fluorescent Analogs, Labeling Cells and Basic Microscopy, Academic Press, New York
    • L.B. Chen, Fluorescent labeling of mitochondria, in: Y.-L. Wang, S.L. Taylor (Eds.), Methods in Cell Biology, vol. 29: Fluorescence Microscopy of Living Cells in Culture, Part A: Fluorescent Analogs, Labeling Cells and Basic Microscopy, Academic Press, New York, 1989, pp. 103-123.
    • (1989) Methods in Cell Biology , vol.29 , pp. 103-123
    • Chen, L.B.1
  • 6
    • 0029871793 scopus 로고    scopus 로고
    • Modulation of protein phosphorylation and stress protein expression by okadaic acid on heat shock cells
    • Chen K.D., Chu J.J., Lai Y.K. Modulation of protein phosphorylation and stress protein expression by okadaic acid on heat shock cells. J. Cell. Biochem. 61:1996;255-265.
    • (1996) J. Cell. Biochem. , vol.61 , pp. 255-265
    • Chen, K.D.1    Chu, J.J.2    Lai, Y.K.3
  • 7
    • 0028328366 scopus 로고
    • Transient increase in vimentin phosphorylation and vimentin-HSC70 association in 9L rat brain tumor cells experiencing heat-shock
    • Cheng T.J., Lai Y.K. Transient increase in vimentin phosphorylation and vimentin-HSC70 association in 9L rat brain tumor cells experiencing heat-shock. J. Cell. Biochem. 54:1994;100-109.
    • (1994) J. Cell. Biochem. , vol.54 , pp. 100-109
    • Cheng, T.J.1    Lai, Y.K.2
  • 8
    • 0027226155 scopus 로고
    • Concomitant changes in mitochondria and intermediate filaments during heat shock and recovery of chicken embryo fibroblasts
    • Collier N.C., Sheetz M.P., Schlesinger M.J. Concomitant changes in mitochondria and intermediate filaments during heat shock and recovery of chicken embryo fibroblasts. J. Cell. Biochem. 52:1993;297-307.
    • (1993) J. Cell. Biochem. , vol.52 , pp. 297-307
    • Collier, N.C.1    Sheetz, M.P.2    Schlesinger, M.J.3
  • 9
    • 0029976264 scopus 로고    scopus 로고
    • The effects of hyperthermia on the cytoskeleton: A review
    • Coss R.A., Linnemans W.A.M. The effects of hyperthermia on the cytoskeleton: A review. Int. J. Hyperthermia. 12:1996;173-196.
    • (1996) Int. J. Hyperthermia , vol.12 , pp. 173-196
    • Coss, R.A.1    Linnemans, W.A.M.2
  • 10
    • 0024393778 scopus 로고
    • Peptide binding and release by proteins implicated as catalysis of protein assembly
    • Flynn G.C., Cappell T.G., Rothman J.E. Peptide binding and release by proteins implicated as catalysis of protein assembly. Science. 245:1989;385-390.
    • (1989) Science , vol.245 , pp. 385-390
    • Flynn, G.C.1    Cappell, T.G.2    Rothman, J.E.3
  • 11
    • 0026920473 scopus 로고
    • Heat shock protein HSP90 and its association with the cytoskeleton: A morphological study
    • Fostinis Y., Theodoropoulos P.A., Gravanis A., Stournaras C. Heat shock protein HSP90 and its association with the cytoskeleton: A morphological study. Biochem. Cell Biol. 70:1992;779-786.
    • (1992) Biochem. Cell Biol. , vol.70 , pp. 779-786
    • Fostinis, Y.1    Theodoropoulos, P.A.2    Gravanis, A.3    Stournaras, C.4
  • 12
    • 0028283501 scopus 로고
    • Intermediate filament: Structure, dynamics, function, and disease
    • Fuchs E., Weber K. Intermediate filament: Structure, dynamics, function, and disease. Annu. Rev. Biochem. 63:1994;345-382.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 345-382
    • Fuchs, E.1    Weber, K.2
  • 13
    • 0017834489 scopus 로고
    • Intranuclear actin bundles induced by dimethyl sulfoxide in interphase nucleus of Dictyostelium
    • Fukui Y. Intranuclear actin bundles induced by dimethyl sulfoxide in interphase nucleus of Dictyostelium. J. Cell Biol. 76:1978;146-157.
    • (1978) J. Cell Biol. , vol.76 , pp. 146-157
    • Fukui, Y.1
  • 14
    • 0027333423 scopus 로고
    • Role of the major heat shock proteins as molecular chaperones
    • Georgopoulos C., Welch W.J. Role of the major heat shock proteins as molecular chaperones. Annu. Rev. Cell Biol. 9:1993;601-634.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 601-634
    • Georgopoulos, C.1    Welch, W.J.2
  • 15
    • 0024461263 scopus 로고
    • β-internexin is a microtubule-associated protein identical to the 70-kDa heat-stock cognate protein and the clathrin uncoating ATPase
    • Green L.A.D., Liem R.K.H. β-Internexin is a microtubule-associated protein identical to the 70-kDa heat-stock cognate protein and the clathrin uncoating ATPase. J. Biol. Chem. 264:1989;15210-15215.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15210-15215
    • Green, L.A.D.1    Liem, R.K.H.2
  • 16
    • 0019494188 scopus 로고
    • Cellular-responses to stress: Comparison of a family of 71-kDa proteins rapidly synthesized in rat-tissue slices and canavanine-treated cells in culture
    • Hightower L.E., White F.P. Cellular-responses to stress: Comparison of a family of 71-kDa proteins rapidly synthesized in rat-tissue slices and canavanine-treated cells in culture. J. Cell. Physiol. 108:1981;261-275.
    • (1981) J. Cell. Physiol. , vol.108 , pp. 261-275
    • Hightower, L.E.1    White, F.P.2
  • 17
    • 0019480519 scopus 로고
    • Monitoring of relative mitochondrial membrane potential in living cells by fluorescence microscopy
    • Johnson L.V., Walsh M.L., Bockus B.J., Chen L.B. Monitoring of relative mitochondrial membrane potential in living cells by fluorescence microscopy. J. Cell Biol. 88:1981;526-535.
    • (1981) J. Cell Biol. , vol.88 , pp. 526-535
    • Johnson, L.V.1    Walsh, M.L.2    Bockus, B.J.3    Chen, L.B.4
  • 18
    • 0025261707 scopus 로고
    • Microtubules, membrane traffic, and cell organization
    • Kelly R.B. Microtubules, membrane traffic, and cell organization. Cell. 61:1990;5-7.
    • (1990) Cell , vol.61 , pp. 5-7
    • Kelly, R.B.1
  • 19
    • 0028967465 scopus 로고
    • Intermediate filaments: New protein, some answers, more questions
    • Klymkowsky M.W. Intermediate filaments: New protein, some answers, more questions. Curr. Opin. Cell Biol. 7:1995;46-54.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 46-54
    • Klymkowsky, M.W.1
  • 20
    • 0025267442 scopus 로고
    • Role of microtubules in the organization of the Golgi apparatus
    • Kreis T.E. Role of microtubules in the organization of the Golgi apparatus. Cell Motil. Cytoskeleton. 15:1990;67-70.
    • (1990) Cell Motil. Cytoskeleton , vol.15 , pp. 67-70
    • Kreis, T.E.1
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0024345716 scopus 로고
    • Heat shock resistance conferred by expression human hsp70 gene in rodent cells
    • Landry J., Chretien P., Lambert H., Hicker E., Weber L.A. Heat shock resistance conferred by expression human hsp70 gene in rodent cells. J. Cell Biol. 109:1989;7-15.
    • (1989) J. Cell Biol. , vol.109 , pp. 7-15
    • Landry, J.1    Chretien, P.2    Lambert, H.3    Hicker, E.4    Weber, L.A.5
  • 23
    • 0026675676 scopus 로고
    • Induction of HSP70 is associated with vincristine resistance in heat-shock 9L rat brain tumor cells
    • Lee W.C., Lin K.Y., Chen K.D., Lai Y.K. Induction of HSP70 is associated with vincristine resistance in heat-shock 9L rat brain tumor cells. Br. J. Cancer. 66:1992;653-659.
    • (1992) Br. J. Cancer , vol.66 , pp. 653-659
    • Lee, W.C.1    Lin, K.Y.2    Chen, K.D.3    Lai, Y.K.4
  • 24
    • 0027200844 scopus 로고
    • Induction of vimentin modification and vimentin-HSP72 association by withangulatin A in 9L rat brain tumor cells
    • Lee W.C., Lee Y.C., Perng M.D., Chen C.M., Lai Y.K. Induction of vimentin modification and vimentin-HSP72 association by withangulatin A in 9L rat brain tumor cells. J. Cell. Biochem. 52:1993;253-265.
    • (1993) J. Cell. Biochem. , vol.52 , pp. 253-265
    • Lee, W.C.1    Lee, Y.C.2    Perng, M.D.3    Chen, C.M.4    Lai, Y.K.5
  • 25
    • 0028906838 scopus 로고
    • Integrity of intermediate filaments is associated with the development of acquired thermotolerance in 9L rat brain tumor cells
    • Lee Y.C., Lai Y.K. Integrity of intermediate filaments is associated with the development of acquired thermotolerance in 9L rat brain tumor cells. J. Cell. Biochem. 57:1995;150-162.
    • (1995) J. Cell. Biochem. , vol.57 , pp. 150-162
    • Lee, Y.C.1    Lai, Y.K.2
  • 26
    • 0011205729 scopus 로고
    • Correlation between the synthesis of heat shock proteins and the development of thermotolerance in Chinese hamster fibroblasts
    • Li C.G., Werb Z. Correlation between the synthesis of heat shock proteins and the development of thermotolerance in Chinese hamster fibroblasts. Proc. Natl. Acad. Sci. USA. 79:1982;3918-3922.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3918-3922
    • Li, C.G.1    Werb, Z.2
  • 27
    • 0028931927 scopus 로고
    • The 70-kDa heat shock proteins associate with glandular intermediate filaments in an ATP-dependent manner
    • Liao J., Lowthert L.A., Ghori N., Omary M.B. The 70-kDa heat shock proteins associate with glandular intermediate filaments in an ATP-dependent manner. J. Biol. Chem. 270:1995;915-922.
    • (1995) J. Biol. Chem. , vol.270 , pp. 915-922
    • Liao, J.1    Lowthert, L.A.2    Ghori, N.3    Omary, M.B.4
  • 29
    • 0021802475 scopus 로고
    • A vital stain for the Golgi apparatus
    • Lipsky N.G., Pabano R.E. A vital stain for the Golgi apparatus. Science. 228:1985;745-747.
    • (1985) Science , vol.228 , pp. 745-747
    • Lipsky, N.G.1    Pabano, R.E.2
  • 30
    • 0026734257 scopus 로고
    • Expression of human HSP70 in rat fibroblast enhances cell-survival and facilitates recovery from translational and transcriptional inhibition following heat-shock
    • Liu R.Y., Li X.C., Li L.G., Li G.C. Expression of human HSP70 in rat fibroblast enhances cell-survival and facilitates recovery from translational and transcriptional inhibition following heat-shock. Cancer Res. 52:1992;3667-3673.
    • (1992) Cancer Res. , vol.52 , pp. 3667-3673
    • Liu, R.Y.1    Li, X.C.2    Li, L.G.3    Li, G.C.4
  • 31
    • 0028228643 scopus 로고
    • A possible role for stable microtubules in intracellular transport from the endoplasmic reticulum to the Golgi apparatus
    • Mizuno M., Singer S.J. A possible role for stable microtubules in intracellular transport from the endoplasmic reticulum to the Golgi apparatus. J. Cell Sci. 107:1994;1321-1331.
    • (1994) J. Cell Sci. , vol.107 , pp. 1321-1331
    • Mizuno, M.1    Singer, S.J.2
  • 32
    • 0028973450 scopus 로고
    • Microtubule nucleation by gamma-tubulin-containing rings in the centrosome
    • Moritz M., Braunfeld M.B., Sedat J.W., Alberts B., Agard D.A. Microtubule nucleation by gamma-tubulin-containing rings in the centrosome. Nature. 378:1995;638-640.
    • (1995) Nature , vol.378 , pp. 638-640
    • Moritz, M.1    Braunfeld, M.B.2    Sedat, J.W.3    Alberts, B.4    Agard, D.A.5
  • 33
    • 0027143990 scopus 로고
    • Effect of ATP on the release of hsp70 and hsp40 from the nucleus in heat-shock HeLa cells
    • Ohtsuka K., Utsumi K.R., Kaneda T., Hattori H. Effect of ATP on the release of hsp70 and hsp40 from the nucleus in heat-shock HeLa cells. Exp. Cell Res. 209:1993;357-366.
    • (1993) Exp. Cell Res. , vol.209 , pp. 357-366
    • Ohtsuka, K.1    Utsumi, K.R.2    Kaneda, T.3    Hattori, H.4
  • 34
    • 0019200479 scopus 로고
    • Dimethlsulfoxide and the ionophore A23187 affect the arrangement of actin and induce nuclear actin paracrystals in PtK2 cells
    • Osborn M., Weber K. Dimethlsulfoxide and the ionophore A23187 affect the arrangement of actin and induce nuclear actin paracrystals in PtK2 cells. Exp. Cell Res. 129:1980;103-114.
    • (1980) Exp. Cell Res. , vol.129 , pp. 103-114
    • Osborn, M.1    Weber, K.2
  • 35
    • 0021467944 scopus 로고
    • Changes in chromatin and the phosphorylation of nuclear proteins during heat shock of Achlya ambisexualis
    • Pekkala D., Heath B., Silver J.C. Changes in chromatin and the phosphorylation of nuclear proteins during heat shock of Achlya ambisexualis. J. Cell Biol. 104:1984;1198-1205.
    • (1984) J. Cell Biol. , vol.104 , pp. 1198-1205
    • Pekkala, D.1    Heath, B.2    Silver, J.C.3
  • 36
    • 0022969885 scopus 로고
    • Speculations on the functions of the major heat shock and glucose-regulated proteins
    • Pelham H.R.B. Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell. 46:1986;959-961.
    • (1986) Cell , vol.46 , pp. 959-961
    • Pelham, H.R.B.1
  • 37
    • 0002193920 scopus 로고
    • Functions of the hsp70 protein family: An overview
    • R.I. Morimoto, A. Tissieres, C. Georgopoulos (Eds.), Cold Spring Harbor, New York
    • H.R.B. Pelham, Functions of the hsp70 protein family: An overview, in: R.I. Morimoto, A. Tissieres, C. Georgopoulos (Eds.), Stress Protein in Biology and Medicine, Cold Spring Harbor, New York, 1990.
    • (1990) Stress Protein in Biology and Medicine
    • Pelham, H.R.B.1
  • 38
    • 0022555884 scopus 로고
    • Actin and actin-binding proteins. A critical evaluation of mechanisms and functions
    • Pollard T.D., Cooper J.A. Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Annu. Rev. Biochem. 55:1986;987-1035.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 987-1035
    • Pollard, T.D.1    Cooper, J.A.2
  • 39
    • 0029110225 scopus 로고
    • Molecular chaperones and intracellular protein translocation
    • Rassow J., Pfanner N. Molecular chaperones and intracellular protein translocation. Rev. Physiol. Biochem. Pharmacol. 126:1995;199-264.
    • (1995) Rev. Physiol. Biochem. Pharmacol. , vol.126 , pp. 199-264
    • Rassow, J.1    Pfanner, N.2
  • 40
    • 0028965273 scopus 로고
    • Partner proteins determine multiple functions of Hsp70
    • Rassow J., Voo W., Pfanner N. Partner proteins determine multiple functions of Hsp70. Trends Cell Biol. 5:1995;207-212.
    • (1995) Trends Cell Biol. , vol.5 , pp. 207-212
    • Rassow, J.1    Voo, W.2    Pfanner, N.3
  • 41
    • 0028964437 scopus 로고
    • Cytoskeletal control of gene expression: Depolymerization of microtubule activates NF-kappa B
    • Rosette C., Karin M. Cytoskeletal control of gene expression: Depolymerization of microtubule activates NF-kappa B. J. Cell Biol. 128:1995;1111-1119.
    • (1995) J. Cell Biol. , vol.128 , pp. 1111-1119
    • Rosette, C.1    Karin, M.2
  • 42
    • 0019209780 scopus 로고
    • Reversible translocation of cytoplasmic actin into the nucleus caused by dimethyl sulfoxide
    • Sanger J.W., Sanger J.M., Kreis T.E., Jockusch B.M. Reversible translocation of cytoplasmic actin into the nucleus caused by dimethyl sulfoxide. Proc. Natl. Acad. Sci. USA. 77:1980;5268-5272.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5268-5272
    • Sanger, J.W.1    Sanger, J.M.2    Kreis, T.E.3    Jockusch, B.M.4
  • 43
    • 0021677114 scopus 로고
    • Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbruch chromosome
    • Scheer U., Hinssen H., Franke W.W., Jockusch B.M. Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbruch chromosome. Cell. 39:1984;111-122.
    • (1984) Cell , vol.39 , pp. 111-122
    • Scheer, U.1    Hinssen, H.2    Franke, W.W.3    Jockusch, B.M.4
  • 44
    • 0025803568 scopus 로고
    • Recent insights into the assembly, dynamics, and function of intermediate filament networks
    • Skalli O., Goldman R.D. Recent insights into the assembly, dynamics, and function of intermediate filament networks. Cell Motil. Cytoskeleton. 19:1988;67-79.
    • (1988) Cell Motil. Cytoskeleton , vol.19 , pp. 67-79
    • Skalli, O.1    Goldman, R.D.2
  • 45
    • 0021748350 scopus 로고
    • Localization of endoplasmic reticulum in living and glutaraldehyde fixed cells with fluorescent dyes
    • Terasaki M., Song J.D., Wong J.R., Weiss M., Chen L.B. Localization of endoplasmic reticulum in living and glutaraldehyde fixed cells with fluorescent dyes. Cell. 38:1984;101-108.
    • (1984) Cell , vol.38 , pp. 101-108
    • Terasaki, M.1    Song, J.D.2    Wong, J.R.3    Weiss, M.4    Chen, L.B.5
  • 46
    • 0020429331 scopus 로고
    • Molecular and cellular effects of heat shock and related treatments of mammalian tissue-culture cells
    • Thomas G.P., Welch W.J., Mathews M.B., Feramisco J.R. Molecular and cellular effects of heat shock and related treatments of mammalian tissue-culture cells. Cold Spring Harbor Symp. Quant. Biol. 46:1982;985-996.
    • (1982) Cold Spring Harbor Symp. Quant. Biol. , vol.46 , pp. 985-996
    • Thomas, G.P.1    Welch, W.J.2    Mathews, M.B.3    Feramisco, J.R.4
  • 48
    • 0000166773 scopus 로고
    • Complex regulation of heat shock-responsive and glucose-responsive genes in human cells
    • Watowich S.S., Morimoto R.I. Complex regulation of heat shock-responsive and glucose-responsive genes in human cells. Mol. Cell Biol. 8:1988;393-405.
    • (1988) Mol. Cell Biol. , vol.8 , pp. 393-405
    • Watowich, S.S.1    Morimoto, R.I.2
  • 50
    • 0026460892 scopus 로고
    • Mammalian stress response: Cell physiology, structure/function of stress proteins and implication for medicine and disease
    • Welch W.J. Mammalian stress response: Cell physiology, structure/function of stress proteins and implication for medicine and disease. Physiol. Rev. 72:1992;1063-1081.
    • (1992) Physiol. Rev. , vol.72 , pp. 1063-1081
    • Welch, W.J.1
  • 51
    • 0021844164 scopus 로고
    • Disruption of the three cytoskeletal networks in mammalian cells does not affect transcription, translation, or protein translocation changes induced by heat shock
    • Welch W.J., Feramisco J.R. Disruption of the three cytoskeletal networks in mammalian cells does not affect transcription, translation, or protein translocation changes induced by heat shock. Mol. Cell. Biol. 5:1985;1571-1581.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 1571-1581
    • Welch, W.J.1    Feramisco, J.R.2
  • 52
    • 0023924167 scopus 로고
    • Characterization of the thermotolerant cell. II. Effects on the intracellular distribution of heat-shock protein 70, intermediate filaments and small nuclear ribonucleoprotein complexes
    • Welch W.J., Mizzen L.A. Characterization of the thermotolerant cell. II. Effects on the intracellular distribution of heat-shock protein 70, intermediate filaments and small nuclear ribonucleoprotein complexes. J. Cell Biol. 106:1988;1117-1130.
    • (1988) J. Cell Biol. , vol.106 , pp. 1117-1130
    • Welch, W.J.1    Mizzen, L.A.2
  • 53
    • 0022379715 scopus 로고
    • Morphological study of the mammalian stress response: Characterization of changes in cytoplasmic organelles, cytoskeleton, and nucleoli and appearance of intranuclear acting filaments in rat fibroblasts after heat shock treatment
    • Welch W.J., Suhan J.P. Morphological study of the mammalian stress response: Characterization of changes in cytoplasmic organelles, cytoskeleton, and nucleoli and appearance of intranuclear acting filaments in rat fibroblasts after heat shock treatment. J. Cell Biol. 101:1985;1198-1211.
    • (1985) J. Cell Biol. , vol.101 , pp. 1198-1211
    • Welch, W.J.1    Suhan, J.P.2
  • 54
    • 0022976650 scopus 로고
    • Cellular and biochemical events in mammalian cells during and after recovery from physiological stress
    • Welch W.J., Suhan J.P. Cellular and biochemical events in mammalian cells during and after recovery from physiological stress. J. Cell. Biol. 103:1986;2035-2053.
    • (1986) J. Cell. Biol. , vol.103 , pp. 2035-2053
    • Welch, W.J.1    Suhan, J.P.2
  • 55
    • 0022272967 scopus 로고
    • The mammalian stress response and the cytoskeleton: Alterations in intermediate filaments
    • Welch W.J., Feramisco J.R., Blose S.H. The mammalian stress response and the cytoskeleton: Alterations in intermediate filaments. Ann. N. Y. Acad. Sci. 455:1985;57-67.
    • (1985) Ann. N. Y. Acad. Sci. , vol.455 , pp. 57-67
    • Welch, W.J.1    Feramisco, J.R.2    Blose, S.H.3


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