메뉴 건너뛰기




Volumn 7, Issue 4, 1997, Pages 343-360

The nuclear matrix: A target for heat shock effects and a determinant for stress response

Author keywords

Heat shock; Nuclear matrix; Stress responses

Indexed keywords

HEAT SHOCK PROTEIN 70;

EID: 0031393659     PISSN: 10454403     EISSN: None     Source Type: Journal    
DOI: 10.1615/critreveukargeneexpr.v7.i4.30     Document Type: Review
Times cited : (37)

References (177)
  • 1
    • 0344832765 scopus 로고
    • Intracellular structure and nucleocytoplasmic transport
    • Berezney R and Jeon KW (eds): Academic Press
    • Agutter PS (1995): Intracellular structure and nucleocytoplasmic transport. In Berezney R and Jeon KW (eds): "Nuclear Matrix: Structural and Functional Organization." Academic Press.
    • (1995) Nuclear Matrix: Structural and Functional Organization
    • Agutter, P.S.1
  • 2
    • 0024438224 scopus 로고
    • Protein import through the nuclear pore complex is a multistep process
    • Akey CW, Goldfarb DS (1989): Protein import through the nuclear pore complex is a multistep process. J Cell Biol 109:971-982.
    • (1989) J Cell Biol , vol.109 , pp. 971-982
    • Akey, C.W.1    Goldfarb, D.S.2
  • 3
    • 0023697402 scopus 로고
    • Dynamic changes in the structure and intracellular locale of the mammalian low molecular weight heat shock protein
    • Arrigo A-P, Suhan JP, Welch WJ (1988): Dynamic changes in the structure and intracellular locale of the mammalian low molecular weight heat shock protein. Mol Cell Biol 8:5059-5071.
    • (1988) Mol Cell Biol , vol.8 , pp. 5059-5071
    • Arrigo, A.-P.1    Suhan, J.P.2    Welch, W.J.3
  • 4
    • 0018382014 scopus 로고
    • The induction of gene activity in Drosophila by heat shock
    • Ashburner M, Bonner JJ (1979): The induction of gene activity in Drosophila by heat shock. Cell 17:241-254.
    • (1979) Cell , vol.17 , pp. 241-254
    • Ashburner, M.1    Bonner, J.J.2
  • 6
    • 0024319521 scopus 로고
    • Large scale chromatin structural domains within mitotic and interphase chromosomes in vivo and in vitro
    • Belmont AS, Braunfeld MB, Sedat JW, Agard DA (1989): Large scale chromatin structural domains within mitotic and interphase chromosomes in vivo and in vitro. Chromosoma 98:129-143.
    • (1989) Chromosoma , vol.98 , pp. 129-143
    • Belmont, A.S.1    Braunfeld, M.B.2    Sedat, J.W.3    Agard, D.A.4
  • 8
    • 0029977376 scopus 로고    scopus 로고
    • Reducing the radiation-induced G2 delay causes HeLa cells to undergo apoptosis instead of mitotic death
    • Bernhard EJ, Muschel RJ, Bakanauskas VJ, McKenna WG (1996): Reducing the radiation-induced G2 delay causes HeLa cells to undergo apoptosis instead of mitotic death. Int J Radiat Biol 69:575-584.
    • (1996) Int J Radiat Biol , vol.69 , pp. 575-584
    • Bernhard, E.J.1    Muschel, R.J.2    Bakanauskas, V.J.3    McKenna, W.G.4
  • 9
    • 0024094652 scopus 로고
    • Thermal stabilization of putative karyoskeletal protein-enriched fractions of Saccharomyces cerevisiae
    • Berrios S, Fisher PA (1988): Thermal stabilization of putative karyoskeletal protein-enriched fractions of Saccharomyces cerevisiae. Mol Cell Biol 8:4573-4575.
    • (1988) Mol Cell Biol , vol.8 , pp. 4573-4575
    • Berrios, S.1    Fisher, P.A.2
  • 10
    • 0018391697 scopus 로고
    • The effect of hyperthermia on the protein content of HeLa nuclei: A flow cytometric analysis
    • Blair OC, Winward RT, Roti Roti JL (1979): The effect of hyperthermia on the protein content of HeLa nuclei: A flow cytometric analysis. Radiat Res 78:474-484.
    • (1979) Radiat Res , vol.78 , pp. 474-484
    • Blair, O.C.1    Winward, R.T.2    Roti Roti, J.L.3
  • 11
    • 0021742214 scopus 로고
    • Inhibition by hyperthermia of repair synthesis and chromatin reassembly of ultraviolet-induced damage to DNA
    • Bodell WJ, Cleaver JE, Roti Roti JL (1984): Inhibition by hyperthermia of repair synthesis and chromatin reassembly of ultraviolet-induced damage to DNA. Radiat Res 100:87-95.
    • (1984) Radiat Res , vol.100 , pp. 87-95
    • Bodell, W.J.1    Cleaver, J.E.2    Roti Roti, J.L.3
  • 12
    • 0021905437 scopus 로고
    • DNA repair in an active gene, removal of pyrimidine dimers from the DHFR gene of CHO cells is much more efficient than in the genome overall
    • Bohr VA, Smith CA, Okumoto DS, Hanawalt PC (1985): DNA repair in an active gene, removal of pyrimidine dimers from the DHFR gene of CHO cells is much more efficient than in the genome overall. Cell 40:359-369.
    • (1985) Cell , vol.40 , pp. 359-369
    • Bohr, V.A.1    Smith, C.A.2    Okumoto, D.S.3    Hanawalt, P.C.4
  • 13
    • 0022999212 scopus 로고
    • The chicken ubiquitin gene contains a heat shock promoter and expresses an unstable mRNa in heat-shocked cells
    • Bond U, Schlessinger MJ (1986): The chicken ubiquitin gene contains a heat shock promoter and expresses an unstable mRNA in heat-shocked cells. Mol Cell Biol 6:4602-4610.
    • (1986) Mol Cell Biol , vol.6 , pp. 4602-4610
    • Bond, U.1    Schlessinger, M.J.2
  • 14
    • 0026739006 scopus 로고
    • Reduction of levels of nuclear-associated protein in heated cells by cycloheximide, D2O, and thermotolerance
    • Borrelli MJ, Stafford DM, Rausch CM, Lepock JR, Lee JY, Corry PM (1992): Reduction of levels of nuclear-associated protein in heated cells by cycloheximide, D2O, and thermotolerance. Radiat Res 131:204-213.
    • (1992) Radiat Res , vol.131 , pp. 204-213
    • Borrelli, M.J.1    Stafford, D.M.2    Rausch, C.M.3    Lepock, J.R.4    Lee, J.Y.5    Corry, P.M.6
  • 15
    • 0030007686 scopus 로고    scopus 로고
    • Excess protein in nuclei isolated from heat-shocked cells results from a reduced extractability of nuclear proteins
    • Borrelli MJ, Lepock JR, Frey HE, Lee YJ, Corry PM (1996): Excess protein in nuclei isolated from heat-shocked cells results from a reduced extractability of nuclear proteins. J Cell Physiol 167:369-379.
    • (1996) J Cell Physiol , vol.167 , pp. 369-379
    • Borrelli, M.J.1    Lepock, J.R.2    Frey, H.E.3    Lee, Y.J.4    Corry, P.M.5
  • 16
    • 0344832762 scopus 로고
    • Chromatin domains and prediction of MAR sequences
    • Berezney R, Jeon KW (eds): Academic Press
    • Boulikas T (1995): Chromatin domains and prediction of MAR sequences. In Berezney R, Jeon KW (eds): "Nuclear matrix: Structural and Functional Organization." Academic Press.
    • (1995) Nuclear Matrix: Structural and Functional Organization
    • Boulikas, T.1
  • 17
    • 0027480459 scopus 로고
    • Possible role of localized protein denaturation in the mechanism of induction of thermotolerance by heat, sodium-arsenite and ethanol
    • Burgman PWJJ, Kampinga HH, Konings AWT (1993): Possible role of localized protein denaturation in the mechanism of induction of thermotolerance by heat, sodium-arsenite and ethanol. Int J Hypertherm 151-162.
    • (1993) Int J Hypertherm , pp. 151-162
    • Burgman, P.W.J.J.1    Kampinga, H.H.2    Konings, A.W.T.3
  • 18
    • 0026655566 scopus 로고
    • Heat induced protein denaturation in the particulate fraction of HeLa S3 cells: Effect of thermotolerance
    • Burgman PWJJ, Konings AWT (1992): Heat induced protein denaturation in the particulate fraction of HeLa S3 cells: Effect of thermotolerance. J Cell Physiol 153:88-94.
    • (1992) J Cell Physiol , vol.153 , pp. 88-94
    • Burgman, P.W.J.J.1    Konings, A.W.T.2
  • 20
    • 0027395056 scopus 로고
    • Content of nonhistone protein in nuclei after hyperthermic treatment
    • Chu GL, Ross G, Wong RSI, Warters R, Dewey WC (1993): Content of nonhistone protein in nuclei after hyperthermic treatment. J Cell Physiol 154:217-221.
    • (1993) J Cell Physiol , vol.154 , pp. 217-221
    • Chu, G.L.1    Ross, G.2    Wong, R.S.I.3    Warters, R.4    Dewey, W.C.5
  • 21
    • 0344401237 scopus 로고    scopus 로고
    • The ubiquitin-mediated proteolytic system: Involvement of molecular chaperones, degradation of oncoproteins, and activation of transcriptional regulators
    • LX, "Protein Kinesis"
    • Ciechanover A, Laszlo A, Bercovich B, Stancovski I, BenNeriah Y, Orian A (1996): The ubiquitin-mediated proteolytic system: Involvement of molecular chaperones, degradation of oncoproteins, and activation of transcriptional regulators. Cold Spring Harbor Symposium, LX, "Protein Kinesis".
    • (1996) Cold Spring Harbor Symposium
    • Ciechanover, A.1    Laszlo, A.2    Bercovich, B.3    Stancovski, I.4    Benneriah, Y.5    Orian, A.6
  • 22
    • 0021046130 scopus 로고
    • Actively transcribed genes are associated with the nuclear matrix
    • Ciejek EM, Tsai MJ, O'Malley BW (1983): Actively transcribed genes are associated with the nuclear matrix. Nature 306:607-609.
    • (1983) Nature , vol.306 , pp. 607-609
    • Ciejek, E.M.1    Tsai, M.J.2    O'Malley, B.W.3
  • 23
    • 0019448593 scopus 로고
    • Recovery of CHO cells from hyperthermic potentiation to X-rays: Repair of DNA and chromatin
    • Clark EP, Dewey WC, Lett JT (1981): Recovery of CHO cells from hyperthermic potentiation to X-rays: Repair of DNA and chromatin. Radiat Res 85:302-313.
    • (1981) Radiat Res , vol.85 , pp. 302-313
    • Clark, E.P.1    Dewey, W.C.2    Lett, J.T.3
  • 24
    • 0022553738 scopus 로고
    • Chromosomal loop anchorage of the kappa immunoglobulin gene occurs next to the enhancer in a region containing Topoisomerase II sites
    • Cockerill PN, Garrard WT (1986): Chromosomal loop anchorage of the kappa immunoglobulin gene occurs next to the enhancer in a region containing Topoisomerase II sites. Cell 44:273-282.
    • (1986) Cell , vol.44 , pp. 273-282
    • Cockerill, P.N.1    Garrard, W.T.2
  • 25
    • 0023819489 scopus 로고
    • Heat sensitization of G1 and S phase cells by procaine HCL. II. Toxicity and probability of dividing following treatment
    • Coss RA, Dewey WC (1988): Heat sensitization of G1 and S phase cells by procaine HCL. II. Toxicity and probability of dividing following treatment. Int J Hypertherm 4:687-697.
    • (1988) Int J Hypertherm , vol.4 , pp. 687-697
    • Coss, R.A.1    Dewey, W.C.2
  • 26
    • 0027323456 scopus 로고
    • Chaperones: Helpers along the pathways to protein folding
    • Craig EA (1993): Chaperones: helpers along the pathways to protein folding. Science 260:1902-1903.
    • (1993) Science , vol.260 , pp. 1902-1903
    • Craig, E.A.1
  • 27
    • 0030789171 scopus 로고    scopus 로고
    • Heat effects on the repair of DNA double-strand breaks in CHO cells
    • Dahm-Daphi J, Brammer I, Dikomey E (1997): Heat effects on the repair of DNA double-strand breaks in CHO cells. Int J Radiat Biol 72:171-179.
    • (1997) Int J Radiat Biol , vol.72 , pp. 171-179
    • Dahm-Daphi, J.1    Brammer, I.2    Dikomey, E.3
  • 28
    • 0029060051 scopus 로고
    • The nuclear pore complex
    • Davis LI (1995): The nuclear pore complex. Annu Rev Biochem 64:865-896.
    • (1995) Annu Rev Biochem , vol.64 , pp. 865-896
    • Davis, L.I.1
  • 30
    • 0024510540 scopus 로고
    • RNA metabolism in nuclei: Adenovirus and heat shock alter intranuclear RNA compartmentalization
    • Denome RM, Werner EA, Patterson RJ (1989): RNA metabolism in nuclei: adenovirus and heat shock alter intranuclear RNA compartmentalization. Nucl Acids Res 17:2081-2098.
    • (1989) Nucl Acids Res , vol.17 , pp. 2081-2098
    • Denome, R.M.1    Werner, E.A.2    Patterson, R.J.3
  • 31
    • 0028823224 scopus 로고
    • Correlation between thermal radiosensitization and slowly rejoined DNA strand breaks in CHO cells
    • Dikomey E, Jung H (1995): Correlation between thermal radiosensitization and slowly rejoined DNA strand breaks in CHO cells. Int J Radiat Biol 68:227-233.
    • (1995) Int J Radiat Biol , vol.68 , pp. 227-233
    • Dikomey, E.1    Jung, H.2
  • 33
    • 0029795408 scopus 로고    scopus 로고
    • Flow cytometric analysis of nuclear matrix proteins: Method and potential applications
    • Dynlacht JR, Henthorn J, O'N an C, Dunn ST, Story MD (1996b): Flow cytometric analysis of nuclear matrix proteins: Method and potential applications. Cytometry 24:348-359.
    • (1996) Cytometry , vol.24 , pp. 348-359
    • Dynlacht, J.R.1    Henthorn, J.2    O'N An, C.3    Dunn, S.T.4    Story, M.D.5
  • 35
    • 0023442466 scopus 로고
    • Deficiency in DNA repair in mouse lymphoma strain L5178Y-S
    • Evans HH, Ricanati M, Horng MF (1987): Deficiency in DNA repair in mouse lymphoma strain L5178Y-S. Proc Natl Acad Sci USA 84:7562-7566.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7562-7566
    • Evans, H.H.1    Ricanati, M.2    Horng, M.F.3
  • 36
    • 0028362691 scopus 로고
    • Nuclear transport
    • Fabre E, Hurt EC (1994): Nuclear transport. Curr Biol 6:335-342.
    • (1994) Curr Biol , vol.6 , pp. 335-342
    • Fabre, E.1    Hurt, E.C.2
  • 38
    • 0017928015 scopus 로고
    • Chromatin
    • Felsenfeld G (1978): Chromatin. Nature 271:115-122.
    • (1978) Nature , vol.271 , pp. 115-122
    • Felsenfeld, G.1
  • 39
    • 0024977940 scopus 로고
    • Heat shock-induced appearance of RNA polymerase II in karyoskeletal protein-enriched (nuclear "matrix") fractions correlates with transcription shut-down in Drosophilia melanogaster
    • Fisher PA, Lin L, McConnell M, Greenleaf A, Lee J-M, Smith DE (1989): Heat shock-induced appearance of RNA polymerase II in karyoskeletal protein-enriched (nuclear "matrix") fractions correlates with transcription shut-down in Drosophilia melanogaster. J Biol Chem 265:3464-3469.
    • (1989) J Biol Chem , vol.265 , pp. 3464-3469
    • Fisher, P.A.1    Lin, L.2    McConnell, M.3    Greenleaf, A.4    Lee, J.-M.5    Smith, D.E.6
  • 40
    • 0008888495 scopus 로고
    • Effects of thermal stress on the karyoskeleton - Insights into the possible role of karyoskeletal elements in DNA replication and transcription
    • Straus PR, Wilson SH (eds): Caldwell, New Jersey: Telford Press
    • Fisher PA (1990): Effects of thermal stress on the karyoskeleton - insights into the possible role of karyoskeletal elements in DNA replication and transcription. In Straus PR, Wilson SH (eds): "The Eukaryotic Nucleus." Caldwell, New Jersey: Telford Press.
    • (1990) The Eukaryotic Nucleus
    • Fisher, P.A.1
  • 41
  • 42
    • 0022602301 scopus 로고
    • Metaphase chromosome structure: Involvement of Topoisomerase II
    • Gasser SM, Laroche T, Falquet J et al. (1986): Metaphase chromosome structure: Involvement of Topoisomerase II. J Mol Biol 188:613-629.
    • (1986) J Mol Biol , vol.188 , pp. 613-629
    • Gasser, S.M.1    Laroche, T.2    Falquet, J.3
  • 43
    • 0029934811 scopus 로고    scopus 로고
    • The human hnRNP-M proteins: Structure and relation with early heat shock-induced splicing arrest and chromosome mapping
    • Gattoni R, Mahe D, Mahl P, Fischer N, Mattei M-G, Stevenin J, Fuchs J-P (1996): The human hnRNP-M proteins: structure and relation with early heat shock-induced splicing arrest and chromosome mapping. Nucl Acids Res 24:2535-2542.
    • (1996) Nucl Acids Res , vol.24 , pp. 2535-2542
    • Gattoni, R.1    Mahe, D.2    Mahl, P.3    Fischer, N.4    Mattei, M.-G.5    Stevenin, J.6    Fuchs, J.-P.7
  • 44
    • 0028228354 scopus 로고
    • Dynamic changes in the higher order chromatin organization of specific sequences revealed by in situ hybridization of nuclear halos
    • Gerdes MG, Carter KC, Moen Jr. PT, Lawrence JB (1994): Dynamic changes in the higher order chromatin organization of specific sequences revealed by in situ hybridization of nuclear halos. J Cell Biol 126:289-304.
    • (1994) J Cell Biol , vol.126 , pp. 289-304
    • Gerdes, M.G.1    Carter, K.C.2    Moen P.T., Jr.3    Lawrence, J.B.4
  • 45
    • 0028332328 scopus 로고
    • Nuclear matrix and the regulation of gene expression: Tissue specificity
    • Getzenberg RH (1994): Nuclear matrix and the regulation of gene expression: tissue specificity. J Cell Biochem 55:22-31.
    • (1994) J Cell Biochem , vol.55 , pp. 22-31
    • Getzenberg, R.H.1
  • 46
    • 0022348695 scopus 로고
    • Cell cycle-dependent repair of double-strand DNa breaks in a X-ray sensitive Chinese hamster cell
    • Giaccia A, Weinstein R, Hu J, Stamato TD (1985): Cell cycle-dependent repair of double-strand DNA breaks in a X-ray sensitive Chinese hamster cell. Somat Cell Mol Genet 5:485-491.
    • (1985) Somat Cell Mol Genet , vol.5 , pp. 485-491
    • Giaccia, A.1    Weinstein, R.2    Hu, J.3    Stamato, T.D.4
  • 47
    • 0022508558 scopus 로고
    • Topoisomerase I interacts with transcribed regions in Drosophila cells
    • Gilmour DS, Pflugfelder G, Wang JC et al. (1986): Topoisomerase I interacts with transcribed regions in Drosophila cells. Cell 44:401-407.
    • (1986) Cell , vol.44 , pp. 401-407
    • Gilmour, D.S.1    Pflugfelder, G.2    Wang, J.C.3
  • 48
    • 0022622393 scopus 로고
    • Novobiocin inhibits RNa polymerase II transcription in vitro by a mechanism distinct from DNa Topoisomerase II
    • Gottesfeld JM (1986): Novobiocin inhibits RNA polymerase II transcription in vitro by a mechanism distinct from DNA Topoisomerase II. Nucl Acids Res 14:2075-2088.
    • (1986) Nucl Acids Res , vol.14 , pp. 2075-2088
    • Gottesfeld, J.M.1
  • 50
    • 0344401236 scopus 로고
    • Effect of thermotolerance on the cellular heat-radiation response
    • Urano M, Douple E (eds): The Netherlands: VSP
    • Henle KJ, Nagle WA, Moss AJ (1989): Effect of thermotolerance on the cellular heat-radiation response. In Urano M, Douple E (eds): "Hyperthermia and Oncology." The Netherlands: VSP.
    • (1989) Hyperthermia and Oncology
    • Henle, K.J.1    Nagle, W.A.2    Moss, A.J.3
  • 51
    • 0027222945 scopus 로고
    • Alterations in nuclear protein mass and macromolecular synthesis following heat shock
    • Higashikubo R, Roti Roti JL (1993): Alterations in nuclear protein mass and macromolecular synthesis following heat shock. Radiat Res 134:193-201.
    • (1993) Radiat Res , vol.134 , pp. 193-201
    • Higashikubo, R.1    Roti Roti, J.L.2
  • 52
    • 0025362616 scopus 로고
    • DNA supercoiling and eukaryotic transcription - Cause and effect
    • Hirose S, Ohta T (1990): DNA supercoiling and eukaryotic transcription - cause and effect. Cell Struct Func 15: 133-135.
    • (1990) Cell Struct Func , vol.15 , pp. 133-135
    • Hirose, S.1    Ohta, T.2
  • 53
    • 0023617425 scopus 로고
    • Protein disulfide cross-linking stabilizes a polyoma large T antigen-host protein complex on the nuclear matrix
    • Humphrey GW, Pigiet V (1987): Protein disulfide cross-linking stabilizes a polyoma large T antigen-host protein complex on the nuclear matrix. Exp Cell Res 171: 122-136.
    • (1987) Exp Cell Res , vol.171 , pp. 122-136
    • Humphrey, G.W.1    Pigiet, V.2
  • 54
    • 0022049377 scopus 로고
    • Transcription occurs at a nucleoskeleton
    • Jackson DA, Cook PR (1985): Transcription occurs at a nucleoskeleton. EMBO J 4:919-925.
    • (1985) EMBO J , vol.4 , pp. 919-925
    • Jackson, D.A.1    Cook, P.R.2
  • 55
    • 0031589513 scopus 로고    scopus 로고
    • Silencing and DNA repair connect
    • Jackson SP (1997): Silencing and DNA repair connect. Nature 388:829-830.
    • (1997) Nature , vol.388 , pp. 829-830
    • Jackson, S.P.1
  • 56
    • 0021949553 scopus 로고
    • Heat-induced alterations in DNA polymerase activity of HeLa cells and of isolated nuclei. Relation to survival
    • Kampinga HH, Jorritsma JBM, Konings AWT (1985): Heat-induced alterations in DNA polymerase activity of HeLa cells and of isolated nuclei. Relation to survival. Intl J Radiat Biol 47:29-40.
    • (1985) Intl J Radiat Biol , vol.47 , pp. 29-40
    • Kampinga, H.H.1    Jorritsma, J.B.M.2    Konings, A.W.T.3
  • 57
    • 0023605264 scopus 로고
    • Heat-induced nuclear protein binding and its relation to thermal cyctotoxicity
    • Kampinga HH, Luppes JG, Konings AWT (1987): Heat-induced nuclear protein binding and its relation to thermal cyctotoxicity. Im J Hyperthermia 3:459-465.
    • (1987) Im J Hyperthermia , vol.3 , pp. 459-465
    • Kampinga, H.H.1    Luppes, J.G.2    Konings, A.W.T.3
  • 58
    • 0023792418 scopus 로고
    • The interaction of heat and radiation affecting the ability of nuclear DNA to undergo supercoiling changes
    • Kampinga HH, Wright WD, Konings AWT, Roti Roti JL (1988): The interaction of heat and radiation affecting the ability of nuclear DNA to undergo supercoiling changes. Radiat Res 116:114-123.
    • (1988) Radiat Res , vol.116 , pp. 114-123
    • Kampinga, H.H.1    Wright, W.D.2    Konings, A.W.T.3    Roti Roti, J.L.4
  • 59
    • 0024550538 scopus 로고
    • The relationship of increased nuclear protein content induced by hyperthermia to killing of HeLa S3 cells
    • Kampinga HH, Turkel-Uygur N, Roti Roti JL, Konings AWT (1989a): The relationship of increased nuclear protein content induced by hyperthermia to killing of HeLa S3 cells. Radiat Res 117:511-522.
    • (1989) Radiat Res , vol.117 , pp. 511-522
    • Kampinga, H.H.1    Turkel-Uygur, N.2    Roti Roti, J.L.3    Konings, A.W.T.4
  • 61
    • 0027457953 scopus 로고
    • Thermotolerance in mammalian cells: Protein denaturation and aggregation, and stress proteins
    • Kampinga HH (1993): Thermotolerance in mammalian cells: Protein denaturation and aggregation, and stress proteins. J Cell Sci 104:11-18.
    • (1993) J Cell Sci , vol.104 , pp. 11-18
    • Kampinga, H.H.1
  • 62
    • 0027417616 scopus 로고
    • Association of HSP72 with the nuclear (TX-100-insoluble) fraction upon heating tolerant and non-tolerant HeLa S3 cells
    • Kampinga HH, Muller E, Brunsting JF, Heine L, Konings AWT, Issels RD (1993): Association of HSP72 with the nuclear (TX-100-insoluble) fraction upon heating tolerant and non-tolerant HeLa S3 cells. Int J Hyperther 9:89-98.
    • (1993) Int J Hyperther , vol.9 , pp. 89-98
    • Kampinga, H.H.1    Muller, E.2    Brunsting, J.F.3    Heine, L.4    Konings, A.W.T.5    Issels, R.D.6
  • 63
    • 0029082019 scopus 로고
    • Thermal protein denaturation and protein aggregation in cells made thermotolerant by various chemicals: Role of heat shock proteins
    • Kampinga HH, Brunsting JF, Stege GJJ, Burgman PWJJ, Konings AWT (1995): Thermal protein denaturation and protein aggregation in cells made thermotolerant by various chemicals: Role of heat shock proteins. Exp Cell Res 219:536-546.
    • (1995) Exp Cell Res , vol.219 , pp. 536-546
    • Kampinga, H.H.1    Brunsting, J.F.2    Stege, G.J.J.3    Burgman, P.W.J.J.4    Konings, A.W.T.5
  • 64
    • 0030817602 scopus 로고    scopus 로고
    • Correlation between slowly repairable double-strand breaks and thermal radiosensitization in the human HeLa S3 cell line
    • Kampinga HH, Hiemstra YS, Konings AWT, Dikomey E (1997): Correlation between slowly repairable double-strand breaks and thermal radiosensitization in the human HeLa S3 cell line. Int J Radiat Biol 72:293-301.
    • (1997) Int J Radiat Biol , vol.72 , pp. 293-301
    • Kampinga, H.H.1    Hiemstra, Y.S.2    Konings, A.W.T.3    Dikomey, E.4
  • 65
    • 0024325164 scopus 로고
    • DNA supercoiling changes in nucleoids from irradiated L5178Y-S and -R cells
    • Kapiszewska M, Wright WD, Lange CS, Roti Roti JL (1989): DNA supercoiling changes in nucleoids from irradiated L5178Y-S and -R cells. Radiat Res 119:569-575.
    • (1989) Radiat Res , vol.119 , pp. 569-575
    • Kapiszewska, M.1    Wright, W.D.2    Lange, C.S.3    Roti Roti, J.L.4
  • 66
    • 0030055021 scopus 로고    scopus 로고
    • Recruitment of damaged DNA to the nuclear matrix in hamster cells following ultraviolet irradiation
    • Koehler DR, Hanawalt PC (1996): Recruitment of damaged DNA to the nuclear matrix in hamster cells following ultraviolet irradiation. Nucl Acids Res 24:2877-2884.
    • (1996) Nucl Acids Res , vol.24 , pp. 2877-2884
    • Koehler, D.R.1    Hanawalt, P.C.2
  • 67
    • 0017331464 scopus 로고
    • Structure of chromatin
    • Kornberg RD (1977): Structure of chromatin. Annu Rev Biochem 46:931-954.
    • (1977) Annu Rev Biochem , vol.46 , pp. 931-954
    • Kornberg, R.D.1
  • 68
    • 0027161090 scopus 로고
    • Heat-induced morphological and biochemical changes in the nuclear lamina from Ehrlich ascites tumor cells in vivo
    • Krachmarov CP, Traub P (1993): Heat-induced morphological and biochemical changes in the nuclear lamina from Ehrlich ascites tumor cells in vivo. J Cell Biochem 52:308-319.
    • (1993) J Cell Biochem , vol.52 , pp. 308-319
    • Krachmarov, C.P.1    Traub, P.2
  • 69
    • 0016361516 scopus 로고
    • Actin is the naturally occurring inhibitor of deoxyribonuclease I
    • Lazarides E, Lindberg U (1974): Actin is the naturally occurring inhibitor of deoxyribonuclease I. Proc Natl Acad Sci USA 71:4742-4746.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 4742-4746
    • Lazarides, E.1    Lindberg, U.2
  • 70
    • 0026663886 scopus 로고
    • Initial characterization of heat-induced excess nuclear proteins in HeLa cells
    • Laszlo A, Wright W, Roti Roti JL (1992): Initial characterization of heat-induced excess nuclear proteins in HeLa cells. J Cell Physiol 151:519-532.
    • (1992) J Cell Physiol , vol.151 , pp. 519-532
    • Laszlo, A.1    Wright, W.2    Roti Roti, J.L.3
  • 71
    • 0026607443 scopus 로고
    • The effects of hyperthermia on mammalian cell structure and function
    • Laszlo A (1992): The effects of hyperthermia on mammalian cell structure and function. J Cell Prolif 25:59-87.
    • (1992) J Cell Prolif , vol.25 , pp. 59-87
    • Laszlo, A.1
  • 72
    • 0027407597 scopus 로고
    • Effect of amino acid analogs on the development of thermotolerance and on thermotolerant cells
    • Laszlo A, Li GC (1993): Effect of amino acid analogs on the development of thermotolerance and on thermotolerant cells. J Cell Physiol 154:419-432.
    • (1993) J Cell Physiol , vol.154 , pp. 419-432
    • Laszlo, A.1    Li, G.C.2
  • 73
    • 0025773250 scopus 로고
    • Mechanism(s) of heat killing: Accumulation of nascent polypeptides in the nucleus?
    • Lee YL, Borrelli MJ, Corry PM (1991): Mechanism(s) of heat killing: Accumulation of nascent polypeptides in the nucleus? Biochem Biophys Res Commun 176: 1525-1531.
    • (1991) Biochem Biophys Res Commun , vol.176 , pp. 1525-1531
    • Lee, Y.L.1    Borrelli, M.J.2    Corry, P.M.3
  • 74
    • 0020436703 scopus 로고
    • Involvement of membranes in cellular responses to hyperthermia
    • Lepock J (1982): Involvement of membranes in cellular responses to hyperthermia. Radiat Res 92:433-438.
    • (1982) Radiat Res , vol.92 , pp. 433-438
    • Lepock, J.1
  • 75
    • 0001625110 scopus 로고    scopus 로고
    • Protein denaturation during heat shock
    • Willis JS (ed): Connecticut: JAI Press
    • Lepock JR (1997): Protein denaturation during heat shock. In Willis JS (ed): "Advances in Molecular and Cell Biology," Vol. 1. Connecticut: JAI Press.
    • (1997) Advances in Molecular and Cell Biology , vol.1
    • Lepock, J.R.1
  • 76
    • 0020436703 scopus 로고
    • Involvement of membranes in cellular responses to hyperthermia
    • Lepock JR (1982): Involvement of membranes in cellular responses to hyperthermia. Radiat Res 92:433-438.
    • (1982) Radiat Res , vol.92 , pp. 433-438
    • Lepock, J.R.1
  • 77
    • 0022555843 scopus 로고
    • The heat shock response
    • Lindquist S (1986): The heat shock response. Annu Rev Biochem 55:1151-1191.
    • (1986) Annu Rev Biochem , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 78
    • 20244389811 scopus 로고
    • Characterization of a heat shock-induced insoluble complex in the nuclei of cells
    • Littlewood TD, Hancock DC, Evan GI (1987): Characterization of a heat shock-induced insoluble complex in the nuclei of cells. J Cell Sci 88:65-72.
    • (1987) J Cell Sci , vol.88 , pp. 65-72
    • Littlewood, T.D.1    Hancock, D.C.2    Evan, G.I.3
  • 79
    • 0023433855 scopus 로고
    • Supercoiling of the DNA template during transcription
    • Liu LF, Wang JC (1987): Supercoiling of the DNA template during transcription. Proc Natl Acad Sci USA 83:7024-7027.
    • (1987) Proc Natl Acad Sci USA , vol.83 , pp. 7024-7027
    • Liu, L.F.1    Wang, J.C.2
  • 80
    • 0026602826 scopus 로고
    • Cellular mechanisms associated with the lack of chronic thermotolerance development
    • Mackey MA, Anolik SL, Roti Roti JL (1992a): Cellular mechanisms associated with the lack of chronic thermotolerance development. Cancer Res 52:1101-1106.
    • (1992) Cancer Res , vol.52 , pp. 1101-1106
    • Mackey, M.A.1    Anolik, S.L.2    Roti Roti, J.L.3
  • 81
    • 0026655578 scopus 로고
    • Changes in heat and radiation sensitivity during long duration, moderate hyperthermia in HeLa S3 cells
    • Mackey MA, Anolik SL, Roti Roti JL (1992b): Changes in heat and radiation sensitivity during long duration, moderate hyperthermia in HeLa S3 cells. Int J Radiat Biol Oncol Phys 24:543-550.
    • (1992) Int J Radiat Biol Oncol Phys , vol.24 , pp. 543-550
    • Mackey, M.A.1    Anolik, S.L.2    Roti Roti, J.L.3
  • 83
    • 0028354550 scopus 로고
    • Dynamic changes in intracellular localization and isoforms of the 27 kD stress protein in human keratinocytes
    • McClaren M, Isseroff RR (1994): Dynamic changes in intracellular localization and isoforms of the 27 kD stress protein in human keratinocytes. J Invest Dermatol 102: 375-381.
    • (1994) J Invest Dermatol , vol.102 , pp. 375-381
    • McClaren, M.1    Isseroff, R.R.2
  • 84
    • 0023609206 scopus 로고
    • Heat shock-induced changes in the structural stability of proteinaceous elements in vivo and morphological effects in situ
    • McConnell M, Whalen AM, Smith DE, Fisher PA (1987): Heat shock-induced changes in the structural stability of proteinaceous elements in vivo and morphological effects in situ. J Cell Biol 105:1087-1098.
    • (1987) J Cell Biol , vol.105 , pp. 1087-1098
    • McConnell, M.1    Whalen, A.M.2    Smith, D.E.3    Fisher, P.A.4
  • 86
    • 0028891783 scopus 로고
    • Apoptosis, oncosis, and necrosis: An overview of cell death
    • Majnoj G, Joris I (1995): Apoptosis, oncosis, and necrosis: An overview of cell death. Am J Pathol 146:3-15.
    • (1995) Am J Pathol , vol.146 , pp. 3-15
    • Majnoj, G.1    Joris, I.2
  • 87
    • 0027995426 scopus 로고
    • Radiation sensitivity correlates with changes in DNA supercoiling and nucleoid protein content in cells of three Chinese hamster cell lines
    • Malyapa RS, Wright WD, Roti Roti JL (1994): Radiation sensitivity correlates with changes in DNA supercoiling and nucleoid protein content in cells of three Chinese hamster cell lines. Radiat Res 140:312-320.
    • (1994) Radiat Res , vol.140 , pp. 312-320
    • Malyapa, R.S.1    Wright, W.D.2    Roti Roti, J.L.3
  • 88
    • 0030024907 scopus 로고    scopus 로고
    • DNa supercoiling changes and nucleoid protein composition in a group of L5178Y cells of varying radiosensitivity
    • Malyapa RS, Wright WD, Roti Roti JL (1996a): DNA supercoiling changes and nucleoid protein composition in a group of L5178Y cells of varying radiosensitivity. Radiat Res 145:239-242.
    • (1996) Radiat Res , vol.145 , pp. 239-242
    • Malyapa, R.S.1    Wright, W.D.2    Roti Roti, J.L.3
  • 89
    • 0030586059 scopus 로고    scopus 로고
    • DNA supercoiling changes and nuclear matrix-associated proteins: Possible role in oncogene-mediated radioresistance
    • Malyapa RS, Wright WD, Taylor YC, Roti Roti JL (1996b): DNA supercoiling changes and nuclear matrix-associated proteins: Possible role in oncogene-mediated radioresistance. Int J Radiat Oncol Biol Phys 35:963-973.
    • (1996) Int J Radiat Oncol Biol Phys , vol.35 , pp. 963-973
    • Malyapa, R.S.1    Wright, W.D.2    Taylor, Y.C.3    Roti Roti, J.L.4
  • 90
    • 0023737554 scopus 로고
    • Brain enzyme histochemistry following stabilization by microwave irradiation
    • Marani E, Bolhuis P, Boon ME (1988): Brain enzyme histochemistry following stabilization by microwave irradiation. Histochem J 20:397-404.
    • (1988) Histochem J , vol.20 , pp. 397-404
    • Marani, E.1    Bolhuis, P.2    Boon, M.E.3
  • 91
    • 0026072171 scopus 로고
    • Heat-induced stabilization of the nuclear matrix, a morphological and biochemical analysis in murine erythroleukemia cells
    • Martelli AM, Falcieri E, Gobbi P, Manzoli L, Gilmour RS, Cocco L (1991): Heat-induced stabilization of the nuclear matrix, a morphological and biochemical analysis in murine erythroleukemia cells. Exp Cell Res 196:216-225.
    • (1991) Exp Cell Res , vol.196 , pp. 216-225
    • Martelli, A.M.1    Falcieri, E.2    Gobbi, P.3    Manzoli, L.4    Gilmour, R.S.5    Cocco, L.6
  • 92
    • 0029838246 scopus 로고    scopus 로고
    • hnRNP proteins and B23 are the major proteins of the internal nuclear matrix of HeLa S3 cells
    • Mattern KA, Humbel BM, Muijsers AO, deJong L, vanDriel R (1996): hnRNP proteins and B23 are the major proteins of the internal nuclear matrix of HeLa S3 cells. J Cell Biochem 62:275-289.
    • (1996) J Cell Biochem , vol.62 , pp. 275-289
    • Mattern, K.A.1    Humbel, B.M.2    Muijsers, A.O.3    DeJong, L.4    VanDriel, R.5
  • 93
    • 0027412012 scopus 로고
    • The response of Chinese hamster cells to low radiation doses: Evidence of enhanced sensitivity of cells to low radiation doses
    • Marples B, Joiner MC (1993): The response of Chinese hamster cells to low radiation doses: Evidence of enhanced sensitivity of cells to low radiation doses. Radiat Res 133:41-51.
    • (1993) Radiat Res , vol.133 , pp. 41-51
    • Marples, B.1    Joiner, M.C.2
  • 94
    • 0344832753 scopus 로고
    • Topoisomerase I identified by scleroderma 70 antisera: Enrichment of Topoisomerase I at the centromere in mouse mitotic cells before anaphase
    • Maul GG, French BT, vanVenroou WJ, et al. (1994): Topoisomerase I identified by scleroderma 70 antisera: Enrichment of Topoisomerase I at the centromere in mouse mitotic cells before anaphase. Proc Natl Acad Sci USA 83:5145-5149.
    • (1994) Proc Natl Acad Sci USA , vol.83 , pp. 5145-5149
    • Maul, G.G.1    French, B.T.2    VanVenroou, W.J.3
  • 95
    • 0029042717 scopus 로고
    • Mechanisms of nuclear protein import
    • Melchior F, Gerace L (1995): Mechanisms of nuclear protein import. Curr Biol 7:310-318.
    • (1995) Curr Biol , vol.7 , pp. 310-318
    • Melchior, F.1    Gerace, L.2
  • 96
    • 0023663101 scopus 로고
    • Selective removal of transcription blocking DNA damage from the transcribed strand of the mammalian DHFR gene
    • Mellon I, Spivak G, Hanawalt PC (1987): Selective removal of transcription blocking DNA damage from the transcribed strand of the mammalian DHFR gene. Cell 51:241-249.
    • (1987) Cell , vol.51 , pp. 241-249
    • Mellon, I.1    Spivak, G.2    Hanawalt, P.C.3
  • 97
    • 0024426244 scopus 로고
    • Induction of the Escherichia coli lactose operon selectively increases repair of its transcribed DNA strand
    • Mellon I, Hanawalt PC (1989): Induction of the Escherichia coli lactose operon selectively increases repair of its transcribed DNA strand. Nature 342:95-98.
    • (1989) Nature , vol.342 , pp. 95-98
    • Mellon, I.1    Hanawalt, P.C.2
  • 98
    • 0028829166 scopus 로고
    • Thermostability of a nuclear-targeted luciferase expressed in mammalian cells. Destabilizing influence of the intranuclear microenvironment
    • Michels AA, Nguyen VT, Konings AWT, Kampinga HH, Bensaude O (1995): Thermostability of a nuclear-targeted luciferase expressed in mammalian cells. Destabilizing influence of the intranuclear microenvironment. Eur J Biochem 234:382-389.
    • (1995) Eur J Biochem , vol.234 , pp. 382-389
    • Michels, A.A.1    Nguyen, V.T.2    Konings, A.W.T.3    Kampinga, H.H.4    Bensaude, O.5
  • 100
    • 0021675784 scopus 로고
    • Organization of the higher order chromatin loop: Specific DNA attachment sites on the nuclear scaffold
    • Mirkovitch J, Mirault M-E, Laemmli UK (1984): Organization of the higher order chromatin loop: specific DNA attachment sites on the nuclear scaffold. Cell 39:23-32.
    • (1984) Cell , vol.39 , pp. 23-32
    • Mirkovitch, J.1    Mirault, M.-E.2    Laemmli, U.K.3
  • 101
    • 0022447223 scopus 로고
    • Preferential association of acidic actin with nuclei and nuclear matrix from mouse leukemia L5178Y cells
    • Nakayasu H, Ueda K (1986): Preferential association of acidic actin with nuclei and nuclear matrix from mouse leukemia L5178Y cells. Exp Cell Res 163:327-336.
    • (1986) Exp Cell Res , vol.163 , pp. 327-336
    • Nakayasu, H.1    Ueda, K.2
  • 102
    • 0028223457 scopus 로고
    • Hyperthermia inhibits the repair of DNA double-strand breaks induced by ionizing radiation as determined by pulsed-field gel electrophoresis
    • Nevaldine B, Longo JA, Hahn PJ (1994): Hyperthermia inhibits the repair of DNA double-strand breaks induced by ionizing radiation as determined by pulsed-field gel electrophoresis. Int J Hypertherm 10:381-388.
    • (1994) Int J Hypertherm , vol.10 , pp. 381-388
    • Nevaldine, B.1    Longo, J.A.2    Hahn, P.J.3
  • 103
    • 0022471245 scopus 로고
    • Intracellular distribution of 73,000 and 72,000 dalton heat shock proteins in HeLa cells
    • Ohtsuka K, Nakamura H, Sato C (1986): Intracellular distribution of 73,000 and 72,000 dalton heat shock proteins in HeLa cells. Int J Hypertherm 2:267-275.
    • (1986) Int J Hypertherm , vol.2 , pp. 267-275
    • Ohtsuka, K.1    Nakamura, H.2    Sato, C.3
  • 104
    • 0026704984 scopus 로고
    • The relationship between hsp70 localization and heat resistance
    • Ohtsuka K, Laszlo A (1992): The relationship between hsp70 localization and heat resistance. Exp Cell Res 202:507-518.
    • (1992) Exp Cell Res , vol.202 , pp. 507-518
    • Ohtsuka, K.1    Laszlo, A.2
  • 105
    • 0025265544 scopus 로고
    • Prompt heat-shock and heat-shifted proteins associated with the nuclear matrix-intermediate filament scaffold in Drosophila melanogaster cells
    • Ornells DA, Penman S (1990): Prompt heat-shock and heat-shifted proteins associated with the nuclear matrix-intermediate filament scaffold in Drosophila melanogaster cells. J Cell Sci 95:393-404.
    • (1990) J Cell Sci , vol.95 , pp. 393-404
    • Ornells, D.A.1    Penman, S.2
  • 106
    • 0026178922 scopus 로고
    • Catalytic function of DNA Topoisomerase II
    • Osheroff N, Zechiedrich EL, Gale KC (1991): Catalytic function of DNA Topoisomerase II. BioEssays 13: 269-275.
    • (1991) BioEssays , vol.13 , pp. 269-275
    • Osheroff, N.1    Zechiedrich, E.L.2    Gale, K.C.3
  • 107
    • 0344832751 scopus 로고
    • Toward a molecular understanding of the structure and function of the nuclear pore complex
    • Berezney R, Jeon KW (eds): Academic Press
    • Pante N, Aebi U (1995): Toward a molecular understanding of the structure and function of the nuclear pore complex. In Berezney R, Jeon KW (eds): "Nuclear Matrix: Structural and Functional Organization." Academic Press.
    • (1995) Nuclear Matrix: Structural and Functional Organization
    • Pante, N.1    Aebi, U.2
  • 108
    • 0018858066 scopus 로고
    • A fixed site of DNA replication in eucaryotic cells
    • Pardoll DM, Vogelstein B, Coffey DS (1980): A fixed site of DNA replication in eucaryotic cells. Cell 19:527-536.
    • (1980) Cell , vol.19 , pp. 527-536
    • Pardoll, D.M.1    Vogelstein, B.2    Coffey, D.S.3
  • 109
    • 0021467944 scopus 로고
    • Changes in chromatin and the phosphorylation of nuclear proteins during heat shock of Achlya ambisexualis
    • Pekkala D, Heath IB, Silver JC (1984): Changes in chromatin and the phosphorylation of nuclear proteins during heat shock of Achlya ambisexualis. Mol Cell Biol 4: 1198-1205.
    • (1984) Mol Cell Biol , vol.4 , pp. 1198-1205
    • Pekkala, D.1    Heath, I.B.2    Silver, J.C.3
  • 111
    • 0022181017 scopus 로고
    • DNA Topoisomerase I mutants: Increased heterogeneity in linking number and other replicon-dependent changes in DNA supercoiling
    • Pruss GJ (1985): DNA Topoisomerase I mutants: Increased heterogeneity in linking number and other replicon-dependent changes in DNA supercoiling. J Mol Biol 185:51-63.
    • (1985) J Mol Biol , vol.185 , pp. 51-63
    • Pruss, G.J.1
  • 112
    • 0025247954 scopus 로고
    • Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components
    • Reichelt R, Holzenburg A, Buhle EL, Jarnik M, Engel A, Aebi U (1990): Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components. J Cell Biol 110:883-894.
    • (1990) J Cell Biol , vol.110 , pp. 883-894
    • Reichelt, R.1    Holzenburg, A.2    Buhle, E.L.3    Jarnik, M.4    Engel, A.5    Aebi, U.6
  • 113
    • 0020804195 scopus 로고
    • "Prompt" heat shock proteins: Translationally regulated synthesis of new proteins associated with the nuclear matrix-intermediate filaments as an early response to heat shock
    • Reiter T, Penman S (1983): "Prompt" heat shock proteins: translationally regulated synthesis of new proteins associated with the nuclear matrix-intermediate filaments as an early response to heat shock. Proc Natl Acad Sci USA 80:4737-4731.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 4737-14731
    • Reiter, T.1    Penman, S.2
  • 114
    • 0020599032 scopus 로고
    • Isolation of 3S androgen receptors from salt resistant fractions and nuclear matrices of prostatic nuclei after mild trypsin digestion
    • Rennie PS, Bruchovsky N, Cheng H (1983): Isolation of 3S androgen receptors from salt resistant fractions and nuclear matrices of prostatic nuclei after mild trypsin digestion. J Biol Chem 258:7623-7630.
    • (1983) J Biol Chem , vol.258 , pp. 7623-7630
    • Rennie, P.S.1    Bruchovsky, N.2    Cheng, H.3
  • 115
    • 0021338869 scopus 로고
    • Cycle progression and division of viable and non-viable Chinese hamster ovary cells following acute hyperthermia and their relationship to thermal tolerance decay
    • Rice GC, Gray JW, Dewey WC (1984): Cycle progression and division of viable and non-viable Chinese hamster ovary cells following acute hyperthermia and their relationship to thermal tolerance decay. Cancer Res 44:1802-1808.
    • (1984) Cancer Res , vol.44 , pp. 1802-1808
    • Rice, G.C.1    Gray, J.W.2    Dewey, W.C.3
  • 116
    • 0018192572 scopus 로고
    • The effects of hyperthermia on the protein to DNA ratio of isolated HeLa chromatin
    • Roti Roti JL, Winward RT (1978): The effects of hyperthermia on the protein to DNA ratio of isolated HeLa chromatin. Radiat Res 74:159-169.
    • (1978) Radiat Res , vol.74 , pp. 159-169
    • Roti Roti, J.L.1    Winward, R.T.2
  • 117
    • 0018407884 scopus 로고
    • The kinetics of increase in chromatin protein content in heated cells: A possible role in cell killing
    • Roti Roti JL, Henle KJ, Winward RT (1979): The kinetics of increase in chromatin protein content in heated cells: A possible role in cell killing. Radiat Res 78:522-531.
    • (1979) Radiat Res , vol.78 , pp. 522-531
    • Roti Roti, J.L.1    Henle, K.J.2    Winward, R.T.3
  • 118
    • 0018904841 scopus 로고
    • Factors affecting the heat-induced increase in protein content of chromatin
    • Roti Roti JL, Winward RT (1980): Factors affecting the heat-induced increase in protein content of chromatin. Radiat Res 81:138-144.
    • (1980) Radiat Res , vol.81 , pp. 138-144
    • Roti Roti, J.L.1    Winward, R.T.2
  • 119
    • 0023228268 scopus 로고
    • Visualization of DNA loops in nucleoids from HeLa cells: Assays for DNA damage and repair
    • Roti Roti JL, Wright WD (1987): Visualization of DNA loops in nucleoids from HeLa cells: Assays for DNA damage and repair. Cytometry 8:461-467.
    • (1987) Cytometry , vol.8 , pp. 461-467
    • Roti Roti, J.L.1    Wright, W.D.2
  • 121
    • 0028279478 scopus 로고
    • Heat-shock-induced changes in nuclear protein and cell killing in thermotolerant HeLa cells
    • Roti Roti JL, Turkel N (1994): Heat-shock-induced changes in nuclear protein and cell killing in thermotolerant HeLa cells. Radiat Res 138:286-290.
    • (1994) Radiat Res , vol.138 , pp. 286-290
    • Roti Roti, J.L.1    Turkel, N.2
  • 122
    • 0028022544 scopus 로고
    • Heat-induced changes in nuclear-associated proteins in normal and thermotolerant HeLa cells
    • Roti Roti JL, Turkel N (1994): Heat-induced changes in nuclear-associated proteins in normal and thermotolerant HeLa cells. Radiat Res 139:73-81.
    • (1994) Radiat Res , vol.139 , pp. 73-81
    • Roti Roti, J.L.1    Turkel, N.2
  • 124
    • 0023046695 scopus 로고
    • Both DNA Topoisomerases I and II relax 2 um plasmid DNA in living yeast cells
    • Saavedra RA, Huberman JA (1989): Both DNA Topoisomerases I and II relax 2 um plasmid DNA in living yeast cells. Cell 45:65-70.
    • (1989) Cell , vol.45 , pp. 65-70
    • Saavedra, R.A.1    Huberman, J.A.2
  • 125
    • 0027375419 scopus 로고
    • Heat-shock treatment selectively affects induction and repair of cyclobutane pyrimidine dimers in transcriptionally active genes in ultraviolet-irradiated human fibroblasts
    • Sakkers RJ, Filon AR, Brunsting JF, Kampinga HH, Mullenders LHF, Konings AWT (1993): Heat-shock treatment selectively affects induction and repair of cyclobutane pyrimidine dimers in transcriptionally active genes in ultraviolet-irradiated human fibroblasts. Radiat Res 135:343-350.
    • (1993) Radiat Res , vol.135 , pp. 343-350
    • Sakkers, R.J.1    Filon, A.R.2    Brunsting, J.F.3    Kampinga, H.H.4    Mullenders, L.H.F.5    Konings, A.W.T.6
  • 126
    • 0029016491 scopus 로고
    • Repair of UV-induced pyrimidine(6-4)pyrimidone photoproducts is selectively inhibited in transcriptionally active genes after heat treatment of human fibroblasts
    • Sakkers RJ, Filon AR, Kampinga HH, Konings AWT, Mullenders LHF (1995): Repair of UV-induced pyrimidine(6-4)pyrimidone photoproducts is selectively inhibited in transcriptionally active genes after heat treatment of human fibroblasts. Int J Radiat Biol 67: 495-499.
    • (1995) Int J Radiat Biol , vol.67 , pp. 495-499
    • Sakkers, R.J.1    Filon, A.R.2    Kampinga, H.H.3    Konings, A.W.T.4    Mullenders, L.H.F.5
  • 127
    • 0019209780 scopus 로고
    • Reversible translocation of cytoplasmic actin into the nucleus caused by dimethyl sulfoxide
    • Sanger JW, Sanger JM, Kreis TE, Jockusch BM (1980): Reversible translocation of cytoplasmic actin into the nucleus caused by dimethyl sulfoxide. Proc Natl Acad Sci USA 77:5268-5272.
    • (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
  • 128
    • 0028920432 scopus 로고
    • Selective inhibition of repair of active genes by hyperthermia is due to inhibition of global and transcription coupled repair pathways
    • Sakkers RJ, Filon AR, Brunsting JF, Kampinga HH, Konings AWT, Mullenders LHF (1995): Selective inhibition of repair of active genes by hyperthermia is due to inhibition of global and transcription coupled repair pathways. Carcinogenesis 16:743-748.
    • (1995) Carcinogenesis , vol.16 , pp. 743-748
    • Sakkers, R.J.1    Filon, A.R.2    Brunsting, J.F.3    Kampinga, H.H.4    Konings, A.W.T.5    Mullenders, L.H.F.6
  • 130
    • 0026643651 scopus 로고
    • The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate
    • Shi Y, Thomas JO (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
  • 131
    • 0029960517 scopus 로고    scopus 로고
    • In vivo nuclear transport kinetics in saccharomyces cerevisiae: A role for heat shock protein 70 during targeting and translocation
    • Shulga N, Roberts P, Gu, Z, Spitz L, Tabb MM, Nomura M, Goldfarb DS (1996): In vivo nuclear transport kinetics in saccharomyces cerevisiae: A role for heat shock protein 70 during targeting and translocation. J Cell Biol 135:329-339.
    • (1996) J Cell Biol , vol.135 , pp. 329-339
    • Shulga, N.1    Roberts, P.2    Gu, Z.3    Spitz, L.4    Tabb, M.M.5    Nomura, M.6    Goldfarb, D.S.7
  • 132
    • 0030724031 scopus 로고    scopus 로고
    • Compartmentalization of eukaryotic gene expression: Causes and effects
    • Singer RH, Green MR (1997): Compartmentalization of eukaryotic gene expression: Causes and effects. Cell 91:291-294.
    • (1997) Cell , vol.91 , pp. 291-294
    • Singer, R.H.1    Green, M.R.2
  • 133
    • 0028296271 scopus 로고
    • A preliminary investigation into the extent of increased radioresistance or hyper-radiosensitivity in cells of hamster cell lines known to be deficient in DNA repair
    • Skov K, Maples B, Matthews JB, Joiner MC, Zhou H (1994): A preliminary investigation into the extent of increased radioresistance or hyper-radiosensitivity in cells of hamster cell lines known to be deficient in DNA repair. Radiat Res 138:8126-129.
    • (1994) Radiat Res , vol.138 , pp. 8126-8129
    • Skov, K.1    Maples, B.2    Matthews, J.B.3    Joiner, M.C.4    Zhou, H.5
  • 134
    • 85088713013 scopus 로고
    • 3H thymnidine on low dose hypersensitivity
    • Fuciarelli AF, Zimbrick JD (eds): Columbus, OH: Battelle Press
    • 3H thymnidine on low dose hypersensitivity. In Fuciarelli AF, Zimbrick JD (eds): "Radiation Damage in DNA." Columbus, OH: Battelle Press.
    • (1995) Radiation Damage in DNA
    • Skov, K.1    Koch, C.2    Marples3
  • 135
    • 0023575750 scopus 로고
    • Biosynthesis and interconversion of Drosophilia nuclear lamin isoforms during normal growth and in response to heat shock
    • Smith DE, Gruenbaum Y, Berrios M, Fisher PA (1987): Biosynthesis and interconversion of Drosophilia nuclear lamin isoforms during normal growth and in response to heat shock. J Cell Biol 105:771-790.
    • (1987) J Cell Biol , vol.105 , pp. 771-790
    • Smith, D.E.1    Gruenbaum, Y.2    Berrios, M.3    Fisher, P.A.4
  • 136
    • 0020585842 scopus 로고
    • Isolation of a cell cycle dependent gamma ray-sensitive Chinese hamster ovary cell
    • Stamato TD, Weinstein R, Giaccia AJ, Mackenzie L (1983): Isolation of a cell cycle dependent gamma ray-sensitive Chinese hamster ovary cell. Somat Cell Genet 9: 165-173.
    • (1983) Somat Cell Genet , vol.9 , pp. 165-173
    • Stamato, T.D.1    Weinstein, R.2    Giaccia, A.J.3    Mackenzie, L.4
  • 137
  • 138
    • 0029799798 scopus 로고    scopus 로고
    • Functional irrelationships between nuclear structure and transcriptional control: Contributions to regulation of cell cycle- And tissue-specific gene expression
    • Stein GS, Stein JL, Lian JE, vanWijnen AJ, Montecino M (1996): Functional irrelationships between nuclear structure and transcriptional control: contributions to regulation of cell cycle- and tissue-specific gene expression. J Cell Biochem 62:198-209.
    • (1996) J Cell Biochem , vol.62 , pp. 198-209
    • Stein, G.S.1    Stein, J.L.2    Lian, J.E.3    VanWijnen, A.J.4    Montecino, M.5
  • 139
    • 0017841455 scopus 로고
    • Effect of hyperthermia on nonhistone proteins isolated with DNA
    • Tomasovic SP, Turner GN, Dewey WC (1978): Effect of hyperthermia on nonhistone proteins isolated with DNA. Radiat Res 73:535-552.
    • (1978) Radiat Res , vol.73 , pp. 535-552
    • Tomasovic, S.P.1    Turner, G.N.2    Dewey, W.C.3
  • 140
    • 0022423465 scopus 로고
    • Regulations of the eschericia coli DNA Topoisomerase I gene by DNA supercoiling
    • Tse-Dinh YC (1985): Regulations of the eschericia coli DNA Topoisomerase I gene by DNA supercoiling. Nucl Acids Res 13:4751-4763.
    • (1985) Nucl Acids Res , vol.13 , pp. 4751-4763
    • Tse-Dinh, Y.C.1
  • 141
    • 0030964526 scopus 로고    scopus 로고
    • Silencing factors participate in DNA repair and recombination in Saccharomyces cerevisiae
    • Tsukamoto Y, Kato J-I, Ikeda H (1997): Silencing factors participate in DNA repair and recombination in Saccharomyces cerevisiae. Nature 388:900-903.
    • (1997) Nature , vol.388 , pp. 900-903
    • Tsukamoto, Y.1    Kato, J.-I.2    Ikeda, H.3
  • 142
    • 0023939168 scopus 로고
    • The nuclear scaffold exhibits DNA-binding sites selective for supercoiled DNA
    • Tsutsui K, Tsutsui K, Muller MT (1988): The nuclear scaffold exhibits DNA-binding sites selective for supercoiled DNA. J Biol Chem 263:7235-7241.
    • (1988) J Biol Chem , vol.263 , pp. 7235-7241
    • Tsutsui, K.1    Tsutsui, K.2    Muller, M.T.3
  • 143
    • 0001262820 scopus 로고
    • Mitotic spindle pulls but fails to separate chromosomes in type II DNA Topoisomerase mutants: Uncoordinated mitosis
    • Uemura T, Yanagida M (1986): Mitotic spindle pulls but fails to separate chromosomes in type II DNA Topoisomerase mutants: uncoordinated mitosis. EMBO J 5: 1003-1010.
    • (1986) EMBO J , vol.5 , pp. 1003-1010
    • Uemura, T.1    Yanagida, M.2
  • 144
    • 0029904240 scopus 로고    scopus 로고
    • Heat-induced modifications in the association of specific proteins with the nuclear matrix
    • VanderWaal R, Thampy G, Wright WD, Roti Roti JL (1996): Heat-induced modifications in the association of specific proteins with the nuclear matrix. Radiat Res 145:746-753.
    • (1996) Radiat Res , vol.145 , pp. 746-753
    • VanderWaal, R.1    Thampy, G.2    Wright, W.D.3    Roti Roti, J.L.4
  • 145
    • 0030780845 scopus 로고    scopus 로고
    • A comparison of the modes and kinetics of heat-induced cell killing in HeLa and L5178Y cells
    • VanderWaal R, Malyapa RS, Higashikubo R, Roti Roti JL (1997): A comparison of the modes and kinetics of heat-induced cell killing in HeLa and L5178Y cells. Radiat Res 148:455-462.
    • (1997) Radiat Res , vol.148 , pp. 455-462
    • VanderWaal, R.1    Malyapa, R.S.2    Higashikubo, R.3    Roti Roti, J.L.4
  • 146
    • 0027722329 scopus 로고
    • Recent advances in nuclear matrix formation
    • Vemuri MC, Raju NN, Malhotra SU (1993): Recent advances in nuclear matrix formation. Cytobios 76: 117-128.
    • (1993) Cytobios , vol.76 , pp. 117-128
    • Vemuri, M.C.1    Raju, N.N.2    Malhotra, S.U.3
  • 147
    • 0026025804 scopus 로고
    • Division associated and division independent hyperthermic cell death: Comparison with other cytotoxic agents
    • Vidair CA, Dewey WC (1991): Division associated and division independent hyperthermic cell death: comparison with other cytotoxic agents. Int J Hypertherm 7:51-69.
    • (1991) Int J Hypertherm , vol.7 , pp. 51-69
    • Vidair, C.A.1    Dewey, W.C.2
  • 148
    • 0027450118 scopus 로고
    • Heat shock alters centrosome organization leading to mitotic dysfunction and cell death
    • Vidair CA, Doxsey SJ, Dewey WD (1993): Heat shock alters centrosome organization leading to mitotic dysfunction and cell death. J Cell Physiol 154:443-455.
    • (1993) J Cell Physiol , vol.154 , pp. 443-455
    • Vidair, C.A.1    Doxsey, S.J.2    Dewey, W.D.3
  • 149
    • 0019169859 scopus 로고
    • Supercoiled loops and eucaryotic DNA replication
    • Vogelstein B, Pardoll DM, Coffey DS (1980): Supercoiled loops and eucaryotic DNA replication. Cell 22:79-85.
    • (1980) Cell , vol.22 , pp. 79-85
    • Vogelstein, B.1    Pardoll, D.M.2    Coffey, D.S.3
  • 150
    • 0027157984 scopus 로고
    • Alterations in nuclear matrix ultrastructure of G1 mammalian cells following heat shock: Resinless section electron microscopy, biochemical and immunofluorescence studies
    • Wachberger PR, Coss RA (1993): Alterations in nuclear matrix ultrastructure of G1 mammalian cells following heat shock: resinless section electron microscopy, biochemical and immunofluorescence studies. J Cell Physiol 155:615-634.
    • (1993) J Cell Physiol , vol.155 , pp. 615-634
    • Wachberger, P.R.1    Coss, R.A.2
  • 151
    • 0028238341 scopus 로고
    • Recovery of nuclear matrix ultrastructure of interphase CHO cells after heat shock
    • Wachberger PR, Coss RA (1994): Recovery of nuclear matrix ultrastructure of interphase CHO cells after heat shock. J Cell Physiol 160:97-106.
    • (1994) J Cell Physiol , vol.160 , pp. 97-106
    • Wachberger, P.R.1    Coss, R.A.2
  • 152
    • 0023904316 scopus 로고
    • Action at a distance along a DNA
    • Wang JC, Giaever GN (1988): Action at a distance along a DNA. Science 240:300-304.
    • (1988) Science , vol.240 , pp. 300-304
    • Wang, J.C.1    Giaever, G.N.2
  • 153
    • 0342779999 scopus 로고
    • Template topology and transcription
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Wang JC (1992): Template topology and transcription. In "Transcriptional Regulation." Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (1992) Transcriptional Regulation
    • Wang, J.C.1
  • 154
    • 0343329774 scopus 로고    scopus 로고
    • Long-range effects in a supercoiled DNa domain generated by transcription in vitro
    • Wang Z, Droge P (1997): Long-range effects in a supercoiled DNA domain generated by transcription in vitro. J Mol Biol 271:499-510.
    • (1997) J Mol Biol , vol.271 , pp. 499-510
    • Wang, Z.1    Droge, P.2
  • 155
    • 0031081432 scopus 로고    scopus 로고
    • Untangling the role of DNA Topoisomerase II in mitotic chromosome structure and function
    • Warburton P, Earnshaw W (1997): Untangling the role of DNA Topoisomerase II in mitotic chromosome structure and function. BioEssays 19:97-99.
    • (1997) BioEssays , vol.19 , pp. 97-99
    • Warburton, P.1    Earnshaw, W.2
  • 156
    • 0018090095 scopus 로고
    • Production and Excision of 5′,6′-dihydroxydihydrothymine type products in the DNA of preheated cells
    • Warters RL, Roti Roti JL (1978): Production and Excision of 5′,6′-dihydroxydihydrothymine type products in the DNA of preheated cells. Int J Radiat Biol 34:381-384.
    • (1978) Int J Radiat Biol , vol.34 , pp. 381-384
    • Warters, R.L.1    Roti Roti, J.L.2
  • 157
    • 0018365335 scopus 로고
    • Excision of X-ray induced thymine damage in chromatin from heated cells
    • Warters RL, Roti Roti JL (1979): Excision of X-ray induced thymine damage in chromatin from heated cells. Radiat Res 79:113-121.
    • (1979) Radiat Res , vol.79 , pp. 113-121
    • Warters, R.L.1    Roti Roti, J.L.2
  • 158
    • 0020454467 scopus 로고
    • Hyperthermia and the cell nucleus
    • Warters RL, Roti Roti JL (1982): Hyperthermia and the cell nucleus. Radiat Res 92:458-462.
    • (1982) Radiat Res , vol.92 , pp. 458-462
    • Warters, R.L.1    Roti Roti, J.L.2
  • 159
    • 0022502908 scopus 로고
    • Heat shock (45°C) results in an increase on nuclear matrix protein mass in HeLa cells
    • Warters RL, Yasui LS, Sharma R, Roti Roti JL (1986): Heat shock (45°C) results in an increase on nuclear matrix protein mass in HeLa cells. Int J Radiat Biol 50:253-259.
    • (1986) Int J Radiat Biol , vol.50 , pp. 253-259
    • Warters, R.L.1    Yasui, L.S.2    Sharma, R.3    Roti Roti, J.L.4
  • 160
    • 0025139185 scopus 로고
    • Inhibition of replicon cluster ligation into chromsomal DNA at elevated temperatures
    • Warters RL, Lyons BW (1990): Inhibition of replicon cluster ligation into chromsomal DNA at elevated temperatures. J Cell Physiol 142:365-371.
    • (1990) J Cell Physiol , vol.142 , pp. 365-371
    • Warters, R.L.1    Lyons, B.W.2
  • 161
    • 0026592349 scopus 로고
    • Repair of DNA strand breaks at hyperthermic temperatures in Chinese hamster ovary cells
    • Warters R, Axtell J (1992): Repair of DNA strand breaks at hyperthermic temperatures in Chinese hamster ovary cells. Int J Radiat Biol 61:43-48.
    • (1992) Int J Radiat Biol , vol.61 , pp. 43-48
    • Warters, R.1    Axtell, J.2
  • 163
    • 0028361146 scopus 로고
    • Heat sensitivity of HeLa S3 cell DNA Topoisomerase II
    • Warters RL, Barrows LR (1994): Heat sensitivity of HeLa S3 cell DNA Topoisomerase II. J Cell Physiol 159: 468-474.
    • (1994) J Cell Physiol , vol.159 , pp. 468-474
    • Warters, R.L.1    Barrows, L.R.2
  • 164
    • 0021259444 scopus 로고
    • Nuclear and nucleolar localization of 72,000-dalton heat shock protein in heat shocked mammalian cells
    • Welch WJ, Feramisco JR (1984): Nuclear and nucleolar localization of 72,000-dalton heat shock protein in heat shocked mammalian cells. J Biol Chem 259:4501-4513.
    • (1984) J Biol Chem , vol.259 , pp. 4501-4513
    • Welch, W.J.1    Feramisco, J.R.2
  • 165
    • 0022379715 scopus 로고
    • Morphological study of the mammalian stress response: Characterization of changes on cytoplasmic organelles, cytoskeleton and nucleoli, and appearance of intranuclear actin filaments in rat fibroblasts after heat shock treatment
    • Welch WJ, Suhan JP (1985): Morphological study of the mammalian stress response: characterization of changes on cytoplasmic organelles, cytoskeleton and nucleoli, and appearance of intranuclear actin filaments in rat fibroblasts after heat shock treatment. J Cell Biol 101:1198-1211.
    • (1985) J Cell Biol , vol.101 , pp. 1198-1211
    • Welch, W.J.1    Suhan, J.P.2
  • 166
    • 0015000275 scopus 로고
    • Variation in sensitivity to heat shock during the cell cycle of Chinese hamster cells in vitro
    • Westra A, Dewey WC (1971): Variation in sensitivity to heat shock during the cell cycle of Chinese hamster cells in vitro. Int J Radiat Biol 19:467-477.
    • (1971) Int J Radiat Biol , vol.19 , pp. 467-477
    • Westra, A.1    Dewey, W.C.2
  • 167
    • 0024579710 scopus 로고
    • Heat-induced damage to HeLa S3 cells: Correlation of viability, permeability, osmosensitivity, phase-contrast light scanning electron and transmission electron microscopical findings
    • Wheatley DN, Kerr C, Gregory DW (1989): Heat-induced damage to HeLa S3 cells: correlation of viability, permeability, osmosensitivity, phase-contrast light scanning electron and transmission electron microscopical findings. Int J Hypertherm 5:145-162.
    • (1989) Int J Hypertherm , vol.5 , pp. 145-162
    • Wheatley, D.N.1    Kerr, C.2    Gregory, D.W.3
  • 168
    • 0026901006 scopus 로고
    • Failla Memorial Lecture: Is radiation all bad?
    • Wolff S (1992): Failla Memorial Lecture: Is radiation all bad? Radiat Res 131:117-123.
    • (1992) Radiat Res , vol.131 , pp. 117-123
    • Wolff, S.1
  • 169
    • 0027478378 scopus 로고
    • Critical steps for induction of chromosomal aberrations in CHO cells heated in S phase
    • Wong RSL, Kapp LN, Krishnaswamy G, Dewey WC (1993): Critical steps for induction of chromosomal aberrations in CHO cells heated in S phase. Radiat Res 133:52-59.
    • (1993) Radiat Res , vol.133 , pp. 52-59
    • Wong, R.S.L.1    Kapp, L.N.2    Krishnaswamy, G.3    Dewey, W.C.4
  • 170
    • 0017688585 scopus 로고
    • Higher order coiling of DNA in chromatin
    • Worcel A, Benyajati C (1977): Higher order coiling of DNA in chromatin. Cell 12:83-100.
    • (1977) Cell , vol.12 , pp. 83-100
    • Worcel, A.1    Benyajati, C.2
  • 171
  • 173
    • 0025242795 scopus 로고
    • Repair of radiation-induced DNA damage in thermotolerant and non-thermotolerant HeLa cells
    • Wynstra JH, Wright WD, Roti Roti JL (1990): Repair of radiation-induced DNA damage in thermotolerant and non-thermotolerant HeLa cells. Radiat Res 124:85-89.
    • (1990) Radiat Res , vol.124 , pp. 85-89
    • Wynstra, J.H.1    Wright, W.D.2    Roti Roti, J.L.3
  • 174
    • 0030046766 scopus 로고
    • Assessment of glucocorticoid receptor-heat shock protein 90 interactions in vivo during nucleocytoplasmic trafficking
    • Yang J, Defranco DB (1994): Assessment of glucocorticoid receptor-heat shock protein 90 interactions in vivo during nucleocytoplasmic trafficking. Mol Endocrinol 10:3-13.
    • (1994) Mol Endocrinol , vol.10 , pp. 3-13
    • Yang, J.1    Defranco, D.B.2
  • 175
    • 0002097103 scopus 로고
    • Post-translational regulation of heat shock protein synthesis in Drosophila
    • Morimoto RI, Tissieres A, Georgopoulos C (eds): Cold Spring Harbor, NY: Cold Spring Laboratory
    • Yost HJ, Petersen RB, Lindquist S (1990): Post-translational regulation of heat shock protein synthesis in Drosophila. In Morimoto RI, Tissieres A, Georgopoulos C (eds): "Stress Proteins in Biology and Medicine." Cold Spring Harbor, NY: Cold Spring Laboratory.
    • (1990) Stress Proteins in Biology and Medicine
    • Yost, H.J.1    Petersen, R.B.2    Lindquist, S.3
  • 176
    • 84977303966 scopus 로고
    • Supercoiled loops in the organization of replication and transcription in eukaryotes
    • Zehnbauer B, Vogelstein B (1985): Supercoiled loops in the organization of replication and transcription in eukaryotes. BioEssays 2:52-54.
    • (1985) BioEssays , vol.2 , pp. 52-54
    • Zehnbauer, B.1    Vogelstein, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.