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Volumn 156, Issue 1, 2010, Pages 19-33

Heat shock protein gene expression and function in amphibian model systems

Author keywords

A6 cells; Development; Heat shock factor 1; In situ hybridization; mRNA; Protein aggregation; Rana; Xenopus

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 110; HEAT SHOCK PROTEIN 47; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90;

EID: 77549088070     PISSN: 10956433     EISSN: 15314332     Source Type: Journal    
DOI: 10.1016/j.cbpa.2010.01.024     Document Type: Review
Times cited : (69)

References (192)
  • 1
    • 0036461694 scopus 로고    scopus 로고
    • Xenopus small heat shock proteins, Hsp30C and Hsp30D, maintain heat- and chemically denatured luciferase in a folding-competent state
    • Abdulle R., Mohindra A., Fernando P., and Heikkila J.J. Xenopus small heat shock proteins, Hsp30C and Hsp30D, maintain heat- and chemically denatured luciferase in a folding-competent state. Cell Stress Chaperones 7 (2002) 6-16
    • (2002) Cell Stress Chaperones , vol.7 , pp. 6-16
    • Abdulle, R.1    Mohindra, A.2    Fernando, P.3    Heikkila, J.J.4
  • 2
    • 0343238332 scopus 로고    scopus 로고
    • Heat-inducible expression of a reporter gene detected by transient assay in zebrafish
    • Adam A., Bartfai R., Lele Z., Krone P.H., and Orban L. Heat-inducible expression of a reporter gene detected by transient assay in zebrafish. Exp. Cell Res. 256 (2000) 282-290
    • (2000) Exp. Cell Res. , vol.256 , pp. 282-290
    • Adam, A.1    Bartfai, R.2    Lele, Z.3    Krone, P.H.4    Orban, L.5
  • 3
    • 0036905925 scopus 로고    scopus 로고
    • Enhanced accumulation of constitutive heat shock protein mRNA is an initial response of eye tissue to mild hyperthermia in vivo in adult Xenopus laevis
    • Ali A., and Heikkila J.J. Enhanced accumulation of constitutive heat shock protein mRNA is an initial response of eye tissue to mild hyperthermia in vivo in adult Xenopus laevis. Can. J. Physiol. Pharmacol. 80 (2002) 1119-1123
    • (2002) Can. J. Physiol. Pharmacol. , vol.80 , pp. 1119-1123
    • Ali, A.1    Heikkila, J.J.2
  • 4
    • 0027225560 scopus 로고
    • Expression of endogenous and microinjected hsp30 genes in early Xenopus laevis embryos
    • Ali A., Krone P., and Heikkila J.J. Expression of endogenous and microinjected hsp30 genes in early Xenopus laevis embryos. Dev. Genet. 14 (1993) 42-50
    • (1993) Dev. Genet. , vol.14 , pp. 42-50
    • Ali, A.1    Krone, P.2    Heikkila, J.J.3
  • 5
    • 0028055601 scopus 로고
    • (dA-dC)n. (dG-Dt)n repeats mark the boundaries of a recent insertion event into a subgroup of Xenopus laevis hsp30 promoters
    • Ali A., Krone P.H., and Heikkila J.J. (dA-dC)n. (dG-Dt)n repeats mark the boundaries of a recent insertion event into a subgroup of Xenopus laevis hsp30 promoters. Genome 37 (1994) 512-515
    • (1994) Genome , vol.37 , pp. 512-515
    • Ali, A.1    Krone, P.H.2    Heikkila, J.J.3
  • 6
    • 0030112708 scopus 로고    scopus 로고
    • Evaluation of stress-inducible hsp90 gene expression as a potential molecular biomarker in Xenopus laevis
    • Ali A., Krone P.H., Pearson D.S., and Heikkila J.J. Evaluation of stress-inducible hsp90 gene expression as a potential molecular biomarker in Xenopus laevis. Cell Stress Chaperones 1 (1996) 62-69
    • (1996) Cell Stress Chaperones , vol.1 , pp. 62-69
    • Ali, A.1    Krone, P.H.2    Pearson, D.S.3    Heikkila, J.J.4
  • 7
    • 8544229307 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA encoding a Xenopus 70 kDa heat shock cognate protein, Hsc70.I
    • Ali A., Salter-Cid L., Flajnik M., and Heikkila J.J. Isolation and characterization of a cDNA encoding a Xenopus 70 kDa heat shock cognate protein, Hsc70.I. Comp. Biochem. Physiol. 1 (1996) 62-69
    • (1996) Comp. Biochem. Physiol. , vol.1 , pp. 62-69
    • Ali, A.1    Salter-Cid, L.2    Flajnik, M.3    Heikkila, J.J.4
  • 8
    • 0010981026 scopus 로고    scopus 로고
    • Molecular cloning of a cDNA encoding a Xenopus laevis 70-kDa heat shock cognate protein, hsc70.II
    • Ali A., Salter-Cid L., Flajnik M., and Heikkila J.J. Molecular cloning of a cDNA encoding a Xenopus laevis 70-kDa heat shock cognate protein, hsc70.II. Biochim. Biophys. Acta 1309 (1996) 174-178
    • (1996) Biochim. Biophys. Acta , vol.1309 , pp. 174-178
    • Ali, A.1    Salter-Cid, L.2    Flajnik, M.3    Heikkila, J.J.4
  • 9
    • 0031445745 scopus 로고    scopus 로고
    • Preferential activation of HSF-binding activity and hsp70 gene expression in Xenopus heart after mild hyperthermia
    • Ali A., Fernando P., Smith W.L., Ovsenek N., Lepock J.R., and Heikkila J.J. Preferential activation of HSF-binding activity and hsp70 gene expression in Xenopus heart after mild hyperthermia. Cell Stress Chaperones 2 (1997) 229-237
    • (1997) Cell Stress Chaperones , vol.2 , pp. 229-237
    • Ali, A.1    Fernando, P.2    Smith, W.L.3    Ovsenek, N.4    Lepock, J.R.5    Heikkila, J.J.6
  • 10
    • 0031866191 scopus 로고    scopus 로고
    • HSP90 interacts with and regulates the activity of heat shock factor 1 in Xenopus oocytes
    • Ali A., Bharadwaj S., O'Carrol R., and Ovsenek N. HSP90 interacts with and regulates the activity of heat shock factor 1 in Xenopus oocytes. Mol. Cell. Biol. 18 (1998) 4949-4960
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4949-4960
    • Ali, A.1    Bharadwaj, S.2    O'Carrol, R.3    Ovsenek, N.4
  • 11
    • 0027971019 scopus 로고
    • Histone acetylation influences both gene expression and development of Xenopus laevis
    • Almouzni G., Khochbin S., Dimitrov S., and Wolffe A.P. Histone acetylation influences both gene expression and development of Xenopus laevis. Dev. Biol. 165 (1994) 654-669
    • (1994) Dev. Biol. , vol.165 , pp. 654-669
    • Almouzni, G.1    Khochbin, S.2    Dimitrov, S.3    Wolffe, A.P.4
  • 12
    • 0022455603 scopus 로고
    • Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes
    • Ananthan J., Goldberg A.L., and Voellmy R. Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes. Science 232 (1986) 522-524
    • (1986) Science , vol.232 , pp. 522-524
    • Ananthan, J.1    Goldberg, A.L.2    Voellmy, R.3
  • 14
    • 0031962486 scopus 로고    scopus 로고
    • Small stress proteins: chaperones that act as regulators of intracellular redox state and programmed cell death
    • Arrigo A.-P. Small stress proteins: chaperones that act as regulators of intracellular redox state and programmed cell death. J. Biol. Chem. 379 (1998) 19-26
    • (1998) J. Biol. Chem. , vol.379 , pp. 19-26
    • Arrigo, A.-P.1
  • 15
    • 0002241311 scopus 로고
    • Expression and function of the low-molecular weight heat shock proteins
    • Morimoto R.I., Tissieres A., and Georgopoulos C. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Arrigo A.-P., and Landry J. Expression and function of the low-molecular weight heat shock proteins. In: Morimoto R.I., Tissieres A., and Georgopoulos C. (Eds). The Biology of Heat Shock Proteins and Molecular Chaperones (1994), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. 335-373
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 335-373
    • Arrigo, A.-P.1    Landry, J.2
  • 16
    • 0030112452 scopus 로고    scopus 로고
    • Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells
    • Baler R., Zou J., and Voellmy R. Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells. Cell Stress Chaperones 1 (1996) 33-39
    • (1996) Cell Stress Chaperones , vol.1 , pp. 33-39
    • Baler, R.1    Zou, J.2    Voellmy, R.3
  • 17
    • 0021884257 scopus 로고
    • Heat shock response in Xenopus oocytes during meiotic maturation and activation
    • Baltus E., and Hanocq-Quertier J. Heat shock response in Xenopus oocytes during meiotic maturation and activation. Cell Differ. 16 (1985) 161-168
    • (1985) Cell Differ. , vol.16 , pp. 161-168
    • Baltus, E.1    Hanocq-Quertier, J.2
  • 18
    • 66349109329 scopus 로고    scopus 로고
    • Overexpression of the transcription factor Msx1 is insufficient to drive complete regeneration of refractory stage Xenopus laevis hindlimbs
    • Barker D.M., and Beck C.W. Overexpression of the transcription factor Msx1 is insufficient to drive complete regeneration of refractory stage Xenopus laevis hindlimbs. Dev. Dyn. 238 (2009) 1366-1378
    • (2009) Dev. Dyn. , vol.238 , pp. 1366-1378
    • Barker, D.M.1    Beck, C.W.2
  • 19
    • 0042196121 scopus 로고    scopus 로고
    • Molecular pathways needed for regeneration of spinal cord and muscle in a vertebrate
    • Beck C.W., Christen B., and Slack J.M.W. Molecular pathways needed for regeneration of spinal cord and muscle in a vertebrate. Dev. Cell 5 (2003) 429-439
    • (2003) Dev. Cell , vol.5 , pp. 429-439
    • Beck, C.W.1    Christen, B.2    Slack, J.M.W.3
  • 20
    • 0029830036 scopus 로고    scopus 로고
    • Degradation and endoplasmic reticulum retention of unassembled α- and β-subunits of Na, K-ATPase correlate with interaction of BiP
    • Beggah A., Mathews P., Beguin P., and Geering K. Degradation and endoplasmic reticulum retention of unassembled α- and β-subunits of Na, K-ATPase correlate with interaction of BiP. J. Biol. Chem. 271 (1996) 20895-20902
    • (1996) J. Biol. Chem. , vol.271 , pp. 20895-20902
    • Beggah, A.1    Mathews, P.2    Beguin, P.3    Geering, K.4
  • 21
    • 0032510285 scopus 로고    scopus 로고
    • Induction of the DNA-binding and transcriptional activities of heat shock factor 1 is uncoupled in Xenopus oocytes
    • Bharadwaj S., Hnatov A., Ali A., and Ovsenek N. Induction of the DNA-binding and transcriptional activities of heat shock factor 1 is uncoupled in Xenopus oocytes. Biochim. Biophys. Acta 1402 (1998) 79-85
    • (1998) Biochim. Biophys. Acta , vol.1402 , pp. 79-85
    • Bharadwaj, S.1    Hnatov, A.2    Ali, A.3    Ovsenek, N.4
  • 22
    • 0033499798 scopus 로고    scopus 로고
    • Multiple components of the HSP90 chaperone complex function in regulation of heat shock factor 1 in vivo
    • Bharadwaj S., Ali A., and Ovsenek N. Multiple components of the HSP90 chaperone complex function in regulation of heat shock factor 1 in vivo. Mol. Cell. Biol. 19 (1999) 8033-8041
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8033-8041
    • Bharadwaj, S.1    Ali, A.2    Ovsenek, N.3
  • 23
    • 0021436060 scopus 로고
    • Developmental control of the heat shock response in Xenopus
    • Bienz M. Developmental control of the heat shock response in Xenopus. Proc. Natl. Acad. Sci. U. S. A. 81 (1984) 3138-3142
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 3138-3142
    • Bienz, M.1
  • 24
    • 0021526790 scopus 로고
    • Xenopus hsp70 genes are constitutively expressed in injected oocytes
    • Bienz M. Xenopus hsp70 genes are constitutively expressed in injected oocytes. EMBO J. 3 (1984) 2477-2483
    • (1984) EMBO J. , vol.3 , pp. 2477-2483
    • Bienz, M.1
  • 25
    • 0020156128 scopus 로고
    • The heat shock response in Xenopus oocytes is controlled at the translational level
    • Bienz M., and Gurdon J.B. The heat shock response in Xenopus oocytes is controlled at the translational level. Cell 29 (1982) 811-819
    • (1982) Cell , vol.29 , pp. 811-819
    • Bienz, M.1    Gurdon, J.B.2
  • 26
    • 0027438122 scopus 로고
    • Constitutive expression of a somatic heat-inducible hsp70 gene during amphibian oogenesis
    • Billoud B., Rodriguez-Martin M.-L., Beerard L., Moreau N., and Angelier N. Constitutive expression of a somatic heat-inducible hsp70 gene during amphibian oogenesis. Development 119 (1993) 921-932
    • (1993) Development , vol.119 , pp. 921-932
    • Billoud, B.1    Rodriguez-Martin, M.-L.2    Beerard, L.3    Moreau, N.4    Angelier, N.5
  • 27
    • 0022000263 scopus 로고
    • Ubiquitin is a heat shock protein in chicken embryo fibroblasts
    • Bond U., and Schlesinger M.J. Ubiquitin is a heat shock protein in chicken embryo fibroblasts. Mol. Cell. Biol. 5 (1985) 949-956
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 949-956
    • Bond, U.1    Schlesinger, M.J.2
  • 28
    • 0032586878 scopus 로고    scopus 로고
    • Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function
    • Bova M.P., Yaron O., Huang Q.L., Ding L.L., Haley D.A., Stewart P.I., and Horwitz J. Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 6137-6142
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 6137-6142
    • Bova, M.P.1    Yaron, O.2    Huang, Q.L.3    Ding, L.L.4    Haley, D.A.5    Stewart, P.I.6    Horwitz, J.7
  • 29
    • 0023657397 scopus 로고
    • Determinants of messenger RNA stability
    • Brawerman G. Determinants of messenger RNA stability. Cell 48 (1987) 5-6
    • (1987) Cell , vol.48 , pp. 5-6
    • Brawerman, G.1
  • 30
    • 0031328320 scopus 로고    scopus 로고
    • Effect of herbimycin A on hsp30 and hsp70 heat shock protein gene expression in Xenopus cultured cells
    • Briant D., Ohan N., and Heikkila J.J. Effect of herbimycin A on hsp30 and hsp70 heat shock protein gene expression in Xenopus cultured cells. Biochem. Cell Biol. 75 (1997) 777-782
    • (1997) Biochem. Cell Biol. , vol.75 , pp. 777-782
    • Briant, D.1    Ohan, N.2    Heikkila, J.J.3
  • 32
    • 37249005420 scopus 로고    scopus 로고
    • Small heat shock protein Hsp27 is required for proper heart tube formation
    • Brown D.D., Christine K.S., Showell C., and Conlon F.L. Small heat shock protein Hsp27 is required for proper heart tube formation. Genesis 45 (2007) 667-678
    • (2007) Genesis , vol.45 , pp. 667-678
    • Brown, D.D.1    Christine, K.S.2    Showell, C.3    Conlon, F.L.4
  • 33
    • 0021341103 scopus 로고
    • Procollagen is more stable in cellulo than in vitro
    • Bruckner P., and Eikenberry E.F. Procollagen is more stable in cellulo than in vitro. Eur. J. Biochem. 140 (1984) 397-399
    • (1984) Eur. J. Biochem. , vol.140 , pp. 397-399
    • Bruckner, P.1    Eikenberry, E.F.2
  • 35
    • 0344874548 scopus 로고    scopus 로고
    • Cryopreservation of Xenopus transgenic lines
    • Buchholz D.R., Fu L., and Shi Y.-B. Cryopreservation of Xenopus transgenic lines. Mol. Reprod. Dev. 67 (2004) 65-69
    • (2004) Mol. Reprod. Dev. , vol.67 , pp. 65-69
    • Buchholz, D.R.1    Fu, L.2    Shi, Y.-B.3
  • 36
    • 0031897554 scopus 로고    scopus 로고
    • Purification and characterization of small heat shock proteins
    • Buchner J., Ehrnsperger M., Gaestel M., and Walke S. Purification and characterization of small heat shock proteins. Methods Enzymol. 290 (1998) 339-349
    • (1998) Methods Enzymol. , vol.290 , pp. 339-349
    • Buchner, J.1    Ehrnsperger, M.2    Gaestel, M.3    Walke, S.4
  • 37
    • 0027079934 scopus 로고
    • Thyroid hormone-induced gene expression changes in the developing frog limb
    • Buckbinder L., and Brown D.D. Thyroid hormone-induced gene expression changes in the developing frog limb. J. Biol. Chem. 267 (1992) 25786-25791
    • (1992) J. Biol. Chem. , vol.267 , pp. 25786-25791
    • Buckbinder, L.1    Brown, D.D.2
  • 38
    • 0035745996 scopus 로고    scopus 로고
    • Adjusting the thermostat: the threshold induction temperature for the heat-shock response in intertidal mussels (genus Mytilus) changes as a function of thermal history
    • Buckley B.A., Owen M.-E., and Hofmann G.E. Adjusting the thermostat: the threshold induction temperature for the heat-shock response in intertidal mussels (genus Mytilus) changes as a function of thermal history. J. Exp. Biol. 204 (2001) 3571-3579
    • (2001) J. Exp. Biol. , vol.204 , pp. 3571-3579
    • Buckley, B.A.1    Owen, M.-E.2    Hofmann, G.E.3
  • 39
    • 77549086526 scopus 로고    scopus 로고
    • Carlone, R.L., Fraser, G.A.D. 1989. An examination of heat shock and trauma-induced proteins in the regenerating forelimb of the newt, Notophthalmus viridescens. In: Kiotsis, V., Kovssoulakkos, S., Wallace, H., Eds. Recent Trends in Regeneration Research (V. Kiotsis, S. Kovssoulakkos, H. Wallace, eds.) Plenum Publishing, New York, pp. 17-25.
    • Carlone, R.L., Fraser, G.A.D. 1989. An examination of heat shock and trauma-induced proteins in the regenerating forelimb of the newt, Notophthalmus viridescens. In: Kiotsis, V., Kovssoulakkos, S., Wallace, H., Eds. Recent Trends in Regeneration Research (V. Kiotsis, S. Kovssoulakkos, H. Wallace, eds.) Plenum Publishing, New York, pp. 17-25.
  • 40
    • 0027351293 scopus 로고
    • Retinoic acid stimulates the synthesis of a novel heat shock protein in the regenerating forelimb of the newt
    • Carlone R.L., Boulianne R.P., Vijh K.M., Karn H., and Fraser G.A.D. Retinoic acid stimulates the synthesis of a novel heat shock protein in the regenerating forelimb of the newt. Biochem. Cell Biol. 71 (1993) 43-50
    • (1993) Biochem. Cell Biol. , vol.71 , pp. 43-50
    • Carlone, R.L.1    Boulianne, R.P.2    Vijh, K.M.3    Karn, H.4    Fraser, G.A.D.5
  • 41
    • 0006722030 scopus 로고
    • Patterns of protein synthesis in oocytes and early embryos of Rana esculenta complex
    • Chen P.S., and Stumm-Zollinger E. Patterns of protein synthesis in oocytes and early embryos of Rana esculenta complex. Roux's Arch. Dev. Biol. 195 (1986) 1-9
    • (1986) Roux's Arch. Dev. Biol. , vol.195 , pp. 1-9
    • Chen, P.S.1    Stumm-Zollinger, E.2
  • 42
    • 23844509529 scopus 로고    scopus 로고
    • Protein phosphatase 5 is a negative modulator of heat shock factor 1
    • Conde R., Xavier J., McLoughlin C., Chinkers M., and Ovsenek N. Protein phosphatase 5 is a negative modulator of heat shock factor 1. J. Biol. Chem. 280 (2005) 28989-28996
    • (2005) J. Biol. Chem. , vol.280 , pp. 28989-28996
    • Conde, R.1    Xavier, J.2    McLoughlin, C.3    Chinkers, M.4    Ovsenek, N.5
  • 43
    • 0034329435 scopus 로고    scopus 로고
    • HSP70 is involved in the control of chromosomal transcription in the amphibian oocyte
    • Corporeau C.D.-F., Angelier N., and Penrad-Mobayed M. HSP70 is involved in the control of chromosomal transcription in the amphibian oocyte. Exp. Cell Res. 260 (2000) 222-232
    • (2000) Exp. Cell Res. , vol.260 , pp. 222-232
    • Corporeau, C.D.-F.1    Angelier, N.2    Penrad-Mobayed, M.3
  • 44
    • 0028923673 scopus 로고
    • Evidence for a 90 kDa heat-shock protein gene expression in the amphibian oocyte
    • Coumailleau P., Billoud B., Sourrouille P., Moreau N., and Angelier N. Evidence for a 90 kDa heat-shock protein gene expression in the amphibian oocyte. Dev. Biol. 168 (1995) 247-258
    • (1995) Dev. Biol. , vol.168 , pp. 247-258
    • Coumailleau, P.1    Billoud, B.2    Sourrouille, P.3    Moreau, N.4    Angelier, N.5
  • 45
    • 0019830493 scopus 로고
    • Trauma-induced protein in rat tissues: a physiological role for a heat shock protein
    • Currie R.W., and White F.P. Trauma-induced protein in rat tissues: a physiological role for a heat shock protein. Science 214 (1981) 72-73
    • (1981) Science , vol.214 , pp. 72-73
    • Currie, R.W.1    White, F.P.2
  • 46
    • 0023792172 scopus 로고
    • Heat shock gene expression in Xenopus laevis A6 cells in response to heat shock and sodium arsenite treatments
    • Darasch S., Mosser D.D., Bols N.C., and Heikkila J.J. Heat shock gene expression in Xenopus laevis A6 cells in response to heat shock and sodium arsenite treatments. Biochem. Cell Biol. 66 (1988) 862-870
    • (1988) Biochem. Cell Biol. , vol.66 , pp. 862-870
    • Darasch, S.1    Mosser, D.D.2    Bols, N.C.3    Heikkila, J.J.4
  • 47
    • 0024498280 scopus 로고
    • The developmental expression of the heat-shock response in Xenopus laevis
    • Davis R.E., and King M.L. The developmental expression of the heat-shock response in Xenopus laevis. Development 105 (1989) 213-222
    • (1989) Development , vol.105 , pp. 213-222
    • Davis, R.E.1    King, M.L.2
  • 48
    • 0034979631 scopus 로고    scopus 로고
    • Isolation and characterization of a novel member of the relaxin/insulin family from the testis of the frog Rana esculenta
    • De Rienzo G., Aniello F., Branno M., and Minucci S. Isolation and characterization of a novel member of the relaxin/insulin family from the testis of the frog Rana esculenta. Endocrinology 142 (2001) 3231-3238
    • (2001) Endocrinology , vol.142 , pp. 3231-3238
    • De Rienzo, G.1    Aniello, F.2    Branno, M.3    Minucci, S.4
  • 49
    • 0031559751 scopus 로고    scopus 로고
    • Molecular cloning of a cDNA encoding the amphibian Pleurodeles waltl 70-kDa heat shock cognate protein
    • Delelis-Fanien C., Penrad-Mobayed M., and Angelier N. Molecular cloning of a cDNA encoding the amphibian Pleurodeles waltl 70-kDa heat shock cognate protein. Biochem. Biophys. Res. Commun. 238 (1997) 159-164
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 159-164
    • Delelis-Fanien, C.1    Penrad-Mobayed, M.2    Angelier, N.3
  • 50
    • 0028178722 scopus 로고
    • αA- and βB-crystallin in the retina: association with the post-golgi compartment of frog retinal photoreceptors
    • Deretic D., Aebersold R.J., Morrison H.D., and Papermaster D.S. αA- and βB-crystallin in the retina: association with the post-golgi compartment of frog retinal photoreceptors. J. Biol. Chem. 269 (1994) 16853-16861
    • (1994) J. Biol. Chem. , vol.269 , pp. 16853-16861
    • Deretic, D.1    Aebersold, R.J.2    Morrison, H.D.3    Papermaster, D.S.4
  • 51
    • 0034754210 scopus 로고    scopus 로고
    • Heat shock protein hyperexpression on chorioretinal layers after transpupillary thermotherapy
    • Desmettre T., Maurage C.A., and Mordon S. Heat shock protein hyperexpression on chorioretinal layers after transpupillary thermotherapy. Invest. Opthalmol. Vis. Sci. 42 (2001) 2976-2980
    • (2001) Invest. Opthalmol. Vis. Sci. , vol.42 , pp. 2976-2980
    • Desmettre, T.1    Maurage, C.A.2    Mordon, S.3
  • 52
    • 77950866609 scopus 로고    scopus 로고
    • The role of Hsp27 and actin in the regulation of movement in human cancer cells responding to heat shock
    • Doshi B.M., Hightower L.E., and Lee J. The role of Hsp27 and actin in the regulation of movement in human cancer cells responding to heat shock. Cell Stress Chaperones 14 (2009) 445-457
    • (2009) Cell Stress Chaperones , vol.14 , pp. 445-457
    • Doshi, B.M.1    Hightower, L.E.2    Lee, J.3
  • 53
    • 0021676865 scopus 로고
    • Multiple ubiquitin mRNAs during Xenopus laevis development contain tandem repeats of 76 amino acid coding sequence
    • Dworkin-Rastl E., Shrutkowski A., and Dworkin M.B. Multiple ubiquitin mRNAs during Xenopus laevis development contain tandem repeats of 76 amino acid coding sequence. Cell 39 (1984) 321-325
    • (1984) Cell , vol.39 , pp. 321-325
    • Dworkin-Rastl, E.1    Shrutkowski, A.2    Dworkin, M.B.3
  • 54
    • 0023146149 scopus 로고
    • Heat shock protein induction and induced thermal tolerance are independent in adult salamanders
    • Easton D.P., Rutledge P.S., and Spotila J.R. Heat shock protein induction and induced thermal tolerance are independent in adult salamanders. J. Exp. Zool. 241 (1987) 263-267
    • (1987) J. Exp. Zool. , vol.241 , pp. 263-267
    • Easton, D.P.1    Rutledge, P.S.2    Spotila, J.R.3
  • 55
    • 0033625965 scopus 로고    scopus 로고
    • The hsp110 and Grp170 stress proteins: newly recognized relatives of the Hsp70s
    • Easton D.P., Kaneko Y., and Subjeck J.R. The hsp110 and Grp170 stress proteins: newly recognized relatives of the Hsp70s. Cell Stress Chaperones 5 (2000) 276-290
    • (2000) Cell Stress Chaperones , vol.5 , pp. 276-290
    • Easton, D.P.1    Kaneko, Y.2    Subjeck, J.R.3
  • 56
    • 0028340597 scopus 로고
    • Retrograde axonal transport of locally synthesized proteins, e.g., actin and heat shock protein 70, in regenerating adult frog sciatic sensory axons
    • Edbladh M., Ekstrom P.A.R., and Edstrom A. Retrograde axonal transport of locally synthesized proteins, e.g., actin and heat shock protein 70, in regenerating adult frog sciatic sensory axons. J. Neurosci. Res. 38 (1994) 424-432
    • (1994) J. Neurosci. Res. , vol.38 , pp. 424-432
    • Edbladh, M.1    Ekstrom, P.A.R.2    Edstrom, A.3
  • 58
    • 0033636879 scopus 로고    scopus 로고
    • Functional characterization of Xenopus small heat shock protein, Hsp30C: the carboxyl end is required for stability and chaperone activity
    • Fernando P., and Heikkila J.J. Functional characterization of Xenopus small heat shock protein, Hsp30C: the carboxyl end is required for stability and chaperone activity. Cell Stress Chaperones 5 (2000) 148-159
    • (2000) Cell Stress Chaperones , vol.5 , pp. 148-159
    • Fernando, P.1    Heikkila, J.J.2
  • 59
    • 0036753798 scopus 로고    scopus 로고
    • Mutation or deletion of the C-terminal tail affects the function and structure of Xenopus laevis small heat shock protein, hsp30
    • Fernando P., Abdulle R., Mohindra A., Guillemette J.G., and Heikkila J.J. Mutation or deletion of the C-terminal tail affects the function and structure of Xenopus laevis small heat shock protein, hsp30. Comp. Biochem. Physiol. B. 133 (2002) 95-103
    • (2002) Comp. Biochem. Physiol. B. , vol.133 , pp. 95-103
    • Fernando, P.1    Abdulle, R.2    Mohindra, A.3    Guillemette, J.G.4    Heikkila, J.J.5
  • 60
    • 0037622070 scopus 로고    scopus 로고
    • Phosphorylation-dependent structural alterations in the small hsp30 chaperone are associated with cellular recovery
    • Fernando P., Megeny L.A., and Heikkila J.J. Phosphorylation-dependent structural alterations in the small hsp30 chaperone are associated with cellular recovery. Exp. Cell Res. 286 (2003) 175-185
    • (2003) Exp. Cell Res. , vol.286 , pp. 175-185
    • Fernando, P.1    Megeny, L.A.2    Heikkila, J.J.3
  • 61
    • 0034599722 scopus 로고    scopus 로고
    • Hsp90 is required for c-Mos activation and biphasic MAP kinase activation in Xenopus oocytes
    • Fisher D.L., Mandart E., and Doree M. Hsp90 is required for c-Mos activation and biphasic MAP kinase activation in Xenopus oocytes. EMBO J. 19 (2000) 1516-1524
    • (2000) EMBO J. , vol.19 , pp. 1516-1524
    • Fisher, D.L.1    Mandart, E.2    Doree, M.3
  • 63
    • 0029051966 scopus 로고
    • Identification of a regulatory motif in HSP70 that affects ATPase activity, substrate binding and interaction with HDJ-1
    • Freeman B.C., Myers M.P., Schumacher R., and Morimoto R.I. Identification of a regulatory motif in HSP70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J. 14 (1995) 2281-2292
    • (1995) EMBO J. , vol.14 , pp. 2281-2292
    • Freeman, B.C.1    Myers, M.P.2    Schumacher, R.3    Morimoto, R.I.4
  • 64
    • 33748601203 scopus 로고    scopus 로고
    • Examination of the expression of the heat shock protein gene, hsp110, in Xenopus laevis cultured cells and embryos
    • Gauley J., and Heikkila J.J. Examination of the expression of the heat shock protein gene, hsp110, in Xenopus laevis cultured cells and embryos. Comp. Biochem. Physiol. 145 (2006) 225-234
    • (2006) Comp. Biochem. Physiol. , vol.145 , pp. 225-234
    • Gauley, J.1    Heikkila, J.J.2
  • 65
    • 77549083150 scopus 로고    scopus 로고
    • Intracellular localization of the heat shock protein, HSP110, in Xenopus laevis A6 kidney epithelial cells
    • Gauley J., Young J.T., and Heikkila J.J. Intracellular localization of the heat shock protein, HSP110, in Xenopus laevis A6 kidney epithelial cells. Comp. Biochem. Physiol. 153 (2008) 417-427
    • (2008) Comp. Biochem. Physiol. , vol.153 , pp. 417-427
    • Gauley, J.1    Young, J.T.2    Heikkila, J.J.3
  • 66
    • 19444382840 scopus 로고    scopus 로고
    • Intracellular localization of Xenopus small heat shock protein, hsp30, in A6 kidney epithelial cells
    • Gellalchew M., and Heikkila J.J. Intracellular localization of Xenopus small heat shock protein, hsp30, in A6 kidney epithelial cells. Cell Biol. Int. 29 (2005) 221-227
    • (2005) Cell Biol. Int. , vol.29 , pp. 221-227
    • Gellalchew, M.1    Heikkila, J.J.2
  • 67
    • 0031042615 scopus 로고    scopus 로고
    • Distinct stress-inducible and developmentally regulated heat shock transcription factors in Xenopus oocytes
    • Gordon S., Bharadwaj S., Hnatov A., Ali A., and Ovsenek N. Distinct stress-inducible and developmentally regulated heat shock transcription factors in Xenopus oocytes. Dev. Biol. 181 (1997) 47-63
    • (1997) Dev. Biol. , vol.181 , pp. 47-63
    • Gordon, S.1    Bharadwaj, S.2    Hnatov, A.3    Ali, A.4    Ovsenek, N.5
  • 68
    • 0038660679 scopus 로고    scopus 로고
    • Lowered temperature set point for activation of the cellular stress response in T-lymphocytes
    • Gothard L.Q., Ruffner M.E., Woodward J.G., Park-Sarge O.-K., and Sarge K.D. Lowered temperature set point for activation of the cellular stress response in T-lymphocytes. J. Biol. Chem. 278 (2003) 9322-9326
    • (2003) J. Biol. Chem. , vol.278 , pp. 9322-9326
    • Gothard, L.Q.1    Ruffner, M.E.2    Woodward, J.G.3    Park-Sarge, O.-K.4    Sarge, K.D.5
  • 69
    • 0033938049 scopus 로고    scopus 로고
    • Expression and characterization of Xenopus type I collagen alpha 1 (COL1A1) during embryonic development
    • Goto T., Katada T., Kinoshita T., and Kubota H.Y. Expression and characterization of Xenopus type I collagen alpha 1 (COL1A1) during embryonic development. Dev. Growth Differ. 42 (2000) 249-256
    • (2000) Dev. Growth Differ. , vol.42 , pp. 249-256
    • Goto, T.1    Katada, T.2    Kinoshita, T.3    Kubota, H.Y.4
  • 70
    • 63849295666 scopus 로고    scopus 로고
    • Tumorigenesis and anti-tumour immune responses in Xenopus
    • Goyos A., and Robert J. Tumorigenesis and anti-tumour immune responses in Xenopus. Front. Biosci. 14 (2009) 167-176
    • (2009) Front. Biosci. , vol.14 , pp. 167-176
    • Goyos, A.1    Robert, J.2
  • 71
    • 0031922636 scopus 로고    scopus 로고
    • Control of gene expression in Xenopus early development
    • Hair A., Prioleau M.N., Vassetzky Y., and Mechali M. Control of gene expression in Xenopus early development. Dev. Genet. 22 (1998) 122-131
    • (1998) Dev. Genet. , vol.22 , pp. 122-131
    • Hair, A.1    Prioleau, M.N.2    Vassetzky, Y.3    Mechali, M.4
  • 72
    • 31344465486 scopus 로고    scopus 로고
    • Examination of the stress-induced expression of the collagen binding heat shock protein, hsp47, in Xenopus laevis cultured cells and embryos
    • Hamilton A.M., and Heikkila J.J. Examination of the stress-induced expression of the collagen binding heat shock protein, hsp47, in Xenopus laevis cultured cells and embryos. Comp. Biochem. Physiol. 143 (2006) 133-141
    • (2006) Comp. Biochem. Physiol. , vol.143 , pp. 133-141
    • Hamilton, A.M.1    Heikkila, J.J.2
  • 73
    • 0031441063 scopus 로고    scopus 로고
    • Characteristic expression of high molecular mass heat shock protein HSP105 during mouse embryo development
    • Hatayama T., Takigawa T., Takeuchi S., and Shiota K. Characteristic expression of high molecular mass heat shock protein HSP105 during mouse embryo development. Cell Struct. Funct. 22 (1997) 517-525
    • (1997) Cell Struct. Funct. , vol.22 , pp. 517-525
    • Hatayama, T.1    Takigawa, T.2    Takeuchi, S.3    Shiota, K.4
  • 74
    • 0742304949 scopus 로고    scopus 로고
    • Expression and function of small heat shock protein genes during Xenopus development
    • Heikkila J.J. Expression and function of small heat shock protein genes during Xenopus development. Semin. Cell Dev. Biol. 14 (2003) 259-266
    • (2003) Semin. Cell Dev. Biol. , vol.14 , pp. 259-266
    • Heikkila, J.J.1
  • 75
    • 18844366526 scopus 로고    scopus 로고
    • Regulation and function of small heat shock protein genes during amphibian development
    • Heikkila J.J. Regulation and function of small heat shock protein genes during amphibian development. J. Cell. Biochem. 93 (2004) 672-680
    • (2004) J. Cell. Biochem. , vol.93 , pp. 672-680
    • Heikkila, J.J.1
  • 76
    • 0021223780 scopus 로고
    • Different environmental stresses can activate the expression of a heat shock gene in rabbit blastocyst
    • Heikkila J.J., and Schultz G.A. Different environmental stresses can activate the expression of a heat shock gene in rabbit blastocyst. Gamete Res. 10 (1984) 45-56
    • (1984) Gamete Res. , vol.10 , pp. 45-56
    • Heikkila, J.J.1    Schultz, G.A.2
  • 77
    • 0020440738 scopus 로고
    • Expression of a set of fish genes following heat or metal ion exposure
    • Heikkila J.J., Schultz G.A., Iatrou K., and Gedamu L. Expression of a set of fish genes following heat or metal ion exposure. J. Biol. Chem. 257 (1982) 12000-12005
    • (1982) J. Biol. Chem. , vol.257 , pp. 12000-12005
    • Heikkila, J.J.1    Schultz, G.A.2    Iatrou, K.3    Gedamu, L.4
  • 78
    • 0021917408 scopus 로고
    • Acquisition of the heat shock response and thermotolerance during early development of Xenopus laevis
    • Heikkila J.J., Kloc M., Bury J., Schultz G.A., and Browder L.W. Acquisition of the heat shock response and thermotolerance during early development of Xenopus laevis. Dev. Biol. 107 (1985) 483-489
    • (1985) Dev. Biol. , vol.107 , pp. 483-489
    • Heikkila, J.J.1    Kloc, M.2    Bury, J.3    Schultz, G.A.4    Browder, L.W.5
  • 79
    • 0023278120 scopus 로고
    • Heat and sodium arsenite act synergistically on the induction of heat shock gene expression in Xenopus laevis A6 cells
    • Heikkila J.J., Darasch S.P., Mosser D.D., and Bols N.C. Heat and sodium arsenite act synergistically on the induction of heat shock gene expression in Xenopus laevis A6 cells. Biochem. Cell Biol. 65 (1987) 310-316
    • (1987) Biochem. Cell Biol. , vol.65 , pp. 310-316
    • Heikkila, J.J.1    Darasch, S.P.2    Mosser, D.D.3    Bols, N.C.4
  • 80
    • 0023243914 scopus 로고
    • Examination of heat shock protein mRNA accumulation in early Xenopus laevis embryos
    • Heikkila J.J., Ovsenek N., and Krone P.H. Examination of heat shock protein mRNA accumulation in early Xenopus laevis embryos. Biochem. Cell Biol. 65 (1987) 87-94
    • (1987) Biochem. Cell Biol. , vol.65 , pp. 87-94
    • Heikkila, J.J.1    Ovsenek, N.2    Krone, P.H.3
  • 81
    • 0030766710 scopus 로고    scopus 로고
    • Heat shock protein gene expression during Xenopus development
    • Heikkila J.J., Ohan N., Tam Y., and Ali A. Heat shock protein gene expression during Xenopus development. Cell. Mol. Life Sci. 53 (1997) 114-121
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 114-121
    • Heikkila, J.J.1    Ohan, N.2    Tam, Y.3    Ali, A.4
  • 82
    • 33745484796 scopus 로고    scopus 로고
    • Analysis of molecular chaperones using a Xenopus oocyte protein refolding assay
    • Heikkila J.J., Kaldis A., and Abdulle R. Analysis of molecular chaperones using a Xenopus oocyte protein refolding assay. Methods Mol. Biol. 322 (2006) 213-222
    • (2006) Methods Mol. Biol. , vol.322 , pp. 213-222
    • Heikkila, J.J.1    Kaldis, A.2    Abdulle, R.3
  • 83
    • 34249106456 scopus 로고    scopus 로고
    • The use of the Xenopus oocyte as a model system to analyze the expression and function of eukaryotic heat shock proteins
    • Heikkila J.J., Kaldis A., Morrow G., and Tanguay R.M. The use of the Xenopus oocyte as a model system to analyze the expression and function of eukaryotic heat shock proteins. Biotechnol. Adv. 25 (2007) 385-395
    • (2007) Biotechnol. Adv. , vol.25 , pp. 385-395
    • Heikkila, J.J.1    Kaldis, A.2    Morrow, G.3    Tanguay, R.M.4
  • 84
    • 0029919023 scopus 로고    scopus 로고
    • Characterization of a Rana catesbeiana HSP30 gene and its expression in the liver of this amphibian during both spontaneous and thyroid hormone-induced metamorphosis
    • Helbing C., Gallimore C., and Atkinson B.G. Characterization of a Rana catesbeiana HSP30 gene and its expression in the liver of this amphibian during both spontaneous and thyroid hormone-induced metamorphosis. Dev. Genet. 18 (1996) 223-233
    • (1996) Dev. Genet. , vol.18 , pp. 223-233
    • Helbing, C.1    Gallimore, C.2    Atkinson, B.G.3
  • 85
    • 0027487094 scopus 로고
    • Immunolocalization of hsp70-related proteins constitutively expressed during Xenopus laevis oogenesis and development
    • Herberts C., Moreau N., and Angelier N. Immunolocalization of hsp70-related proteins constitutively expressed during Xenopus laevis oogenesis and development. Int. J. Dev. Biol. 37 (1993) 397-406
    • (1993) Int. J. Dev. Biol. , vol.37 , pp. 397-406
    • Herberts, C.1    Moreau, N.2    Angelier, N.3
  • 86
    • 3543001076 scopus 로고    scopus 로고
    • Identification of Xenopus heat shock transcription factor-2: conserved role of sumoylation in regulating deoxyribonucleic acid-binding activity of heat shock transcription factor-2 proteins
    • Hilgarth R.S., Murphy L.A., O'Connor C.M., Clark J.A., Park-Sarge O.-K., and Sarge K.D. Identification of Xenopus heat shock transcription factor-2: conserved role of sumoylation in regulating deoxyribonucleic acid-binding activity of heat shock transcription factor-2 proteins. Cell Stress Chaperones 9 (2004) 214-220
    • (2004) Cell Stress Chaperones , vol.9 , pp. 214-220
    • Hilgarth, R.S.1    Murphy, L.A.2    O'Connor, C.M.3    Clark, J.A.4    Park-Sarge, O.-K.5    Sarge, K.D.6
  • 88
    • 0023368195 scopus 로고
    • Transcript levels and translational control of hsp70 synthesis in Xenopus oocytes
    • Horrell A., Shuttleworth J., and Colman A. Transcript levels and translational control of hsp70 synthesis in Xenopus oocytes. Genes Dev. 1 (1987) 433-444
    • (1987) Genes Dev. , vol.1 , pp. 433-444
    • Horrell, A.1    Shuttleworth, J.2    Colman, A.3
  • 89
    • 0027153286 scopus 로고
    • Structure of the gene encoding the mouse 47-KDa heat shock protein (HSP47)
    • Hosokawa N., Takechi H., Yokota S., Kirayoshi K., and Nagata K. Structure of the gene encoding the mouse 47-KDa heat shock protein (HSP47). Gene 126 (1993) 187-193
    • (1993) Gene , vol.126 , pp. 187-193
    • Hosokawa, N.1    Takechi, H.2    Yokota, S.3    Kirayoshi, K.4    Nagata, K.5
  • 91
    • 7444257956 scopus 로고    scopus 로고
    • Molecular chaperone function of the Rana catesbeiana small heat shock protein, Hsp30
    • Kaldis A., Atkinson B.G., and Heikkila J.J. Molecular chaperone function of the Rana catesbeiana small heat shock protein, Hsp30. Comp. Biochem. Physiol. 139 (2004) 175-182
    • (2004) Comp. Biochem. Physiol. , vol.139 , pp. 175-182
    • Kaldis, A.1    Atkinson, B.G.2    Heikkila, J.J.3
  • 93
    • 0026937338 scopus 로고
    • Properties of heat shock transcription factor in Xenopus embryos
    • Karn H., Ovsenek N., and Heikkila J.J. Properties of heat shock transcription factor in Xenopus embryos. Biochem. Cell Biol. 70 (1992) 1006-1013
    • (1992) Biochem. Cell Biol. , vol.70 , pp. 1006-1013
    • Karn, H.1    Ovsenek, N.2    Heikkila, J.J.3
  • 94
    • 2342496707 scopus 로고    scopus 로고
    • Hsp25, a member of the Hsp30 family, promotes inclusion formation in response to stress
    • Katoh Y., Fujimoto M., Nakamura K., Inouye S., Sugahara K., Izu H., and Nakai A. Hsp25, a member of the Hsp30 family, promotes inclusion formation in response to stress. FEBS Lett. 565 (2004) 28-32
    • (2004) FEBS Lett. , vol.565 , pp. 28-32
    • Katoh, Y.1    Fujimoto, M.2    Nakamura, K.3    Inouye, S.4    Sugahara, K.5    Izu, H.6    Nakai, A.7
  • 95
    • 0032527991 scopus 로고    scopus 로고
    • Proteasome inhibition leads to the activation of all members of the heat shock factor family
    • Kawazoe Y., Nakai A., Tanabe M., and Nagata K. Proteasome inhibition leads to the activation of all members of the heat shock factor family. Eur. J. Biochem. 255 (1998) 356-362
    • (1998) Eur. J. Biochem. , vol.255 , pp. 356-362
    • Kawazoe, Y.1    Nakai, A.2    Tanabe, M.3    Nagata, K.4
  • 96
    • 0021036415 scopus 로고
    • Cold- and heat-shock induction of new gene expression in cultured amphibian cells
    • Ketola-Pirie C.A., and Atkinson B.G. Cold- and heat-shock induction of new gene expression in cultured amphibian cells. Can. J. Biochem. Cell Biol. 61 (1983) 462-471
    • (1983) Can. J. Biochem. Cell Biol. , vol.61 , pp. 462-471
    • Ketola-Pirie, C.A.1    Atkinson, B.G.2
  • 97
    • 0023613813 scopus 로고
    • The events of the midblastula transition in Xenopus are regulated by changes in the cell cycle
    • Kimelman D., Kirschner M., and Scherson T. The events of the midblastula transition in Xenopus are regulated by changes in the cell cycle. Cell 48 (1987) 399-407
    • (1987) Cell , vol.48 , pp. 399-407
    • Kimelman, D.1    Kirschner, M.2    Scherson, T.3
  • 98
    • 0023156466 scopus 로고
    • Do Xenopus oocytes have a heat shock response?
    • King M.L., and Davis R.E. Do Xenopus oocytes have a heat shock response?. Dev. Biol. 119 (1987) 532-539
    • (1987) Dev. Biol. , vol.119 , pp. 532-539
    • King, M.L.1    Davis, R.E.2
  • 99
    • 0029806183 scopus 로고    scopus 로고
    • Transgenic Xenopus embryos from sperm nuclear transplantations reveal FGF signaling requirements during gastrulation
    • Kroll K.L., and Amaya E. Transgenic Xenopus embryos from sperm nuclear transplantations reveal FGF signaling requirements during gastrulation. Development 122 (1996) 3173-3183
    • (1996) Development , vol.122 , pp. 3173-3183
    • Kroll, K.L.1    Amaya, E.2
  • 100
    • 0023911049 scopus 로고
    • Analysis of hsp30, hsp70, and ubiquitin gene expression in Xenopus laevis tadpoles
    • Krone P.H., and Heikkila J.J. Analysis of hsp30, hsp70, and ubiquitin gene expression in Xenopus laevis tadpoles. Development 103 (1988) 59-67
    • (1988) Development , vol.103 , pp. 59-67
    • Krone, P.H.1    Heikkila, J.J.2
  • 101
    • 0024411412 scopus 로고
    • Expression of microinjected hsp70/CAT and hsp30/CAT chimeric genes in developing Xenopus laevis embryos
    • Krone P.H., and Heikkila J.J. Expression of microinjected hsp70/CAT and hsp30/CAT chimeric genes in developing Xenopus laevis embryos. Development 106 (1989) 271-281
    • (1989) Development , vol.106 , pp. 271-281
    • Krone, P.H.1    Heikkila, J.J.2
  • 102
    • 0026537572 scopus 로고
    • Comparison of the regulatory and structural regions of the Xenopus laevis small heat shock protein encoding gene family
    • Krone P.H., Snow A., Ali A., Pasternak J.J., and Heikkila J.J. Comparison of the regulatory and structural regions of the Xenopus laevis small heat shock protein encoding gene family. Gene 110 (1992) 159-166
    • (1992) Gene , vol.110 , pp. 159-166
    • Krone, P.H.1    Snow, A.2    Ali, A.3    Pasternak, J.J.4    Heikkila, J.J.5
  • 103
    • 0030579097 scopus 로고    scopus 로고
    • Evidence for the existence of a novel mechanism for the nuclear import of HSC70
    • Lamian V., Small G.M., and Feldherr C.M. Evidence for the existence of a novel mechanism for the nuclear import of HSC70. Exp. Cell Res. 228 (1996) 84-91
    • (1996) Exp. Cell Res. , vol.228 , pp. 84-91
    • Lamian, V.1    Small, G.M.2    Feldherr, C.M.3
  • 104
    • 0032757495 scopus 로고    scopus 로고
    • Spatial pattern of constitutive and heat shock-induced expression of the small heat shock protein gene family, Hsp30, in Xenopus laevis tailbud embryos
    • Lang L., Miskovic D., Fernando P., and Heikkila J.J. Spatial pattern of constitutive and heat shock-induced expression of the small heat shock protein gene family, Hsp30, in Xenopus laevis tailbud embryos. Dev. Genet. 25 (1999) 265-374
    • (1999) Dev. Genet. , vol.25 , pp. 265-374
    • Lang, L.1    Miskovic, D.2    Fernando, P.3    Heikkila, J.J.4
  • 105
    • 0033954189 scopus 로고    scopus 로고
    • Stress-induced, tissue-specific enrichment of hsp70 mRNA accumulation in Xenopus laevis embryos
    • Lang L., Miskovic D., Lo M., and Heikkila J.J. Stress-induced, tissue-specific enrichment of hsp70 mRNA accumulation in Xenopus laevis embryos. Cell Stress Chaperones 5 (2000) 36-44
    • (2000) Cell Stress Chaperones , vol.5 , pp. 36-44
    • Lang, L.1    Miskovic, D.2    Lo, M.3    Heikkila, J.J.4
  • 107
    • 0002858113 scopus 로고    scopus 로고
    • Proteasome inhibitors cause induction of heat shock proteins and trehalose, which together confer thermotolerance in Saccharomyces cerevisiae
    • Lee D.H., and Goldberg A.L. Proteasome inhibitors cause induction of heat shock proteins and trehalose, which together confer thermotolerance in Saccharomyces cerevisiae. Mol. Cell. Biol. 18 (1998) 30-38
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 30-38
    • Lee, D.H.1    Goldberg, A.L.2
  • 108
    • 0029161913 scopus 로고
    • Pharmacological modulation of heat shock factor 1 by anti-inflammatory drugs results in protection against stress-induced cellular damage
    • Lee B.S., Chen J., Angelidis C., Jurivich D.A., and Morimoto R.I. Pharmacological modulation of heat shock factor 1 by anti-inflammatory drugs results in protection against stress-induced cellular damage. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 7207-7211
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 7207-7211
    • Lee, B.S.1    Chen, J.2    Angelidis, C.3    Jurivich, D.A.4    Morimoto, R.I.5
  • 109
    • 22244478592 scopus 로고    scopus 로고
    • Expression of heat shock protein 70 during limb development and regeneration in the axolotl
    • Levesque M., Guimond J.-C., Pilote M., Leclerc S., Moldovan F., and Roy S. Expression of heat shock protein 70 during limb development and regeneration in the axolotl. Dev. Dyn. 233 (2005) 1525-1534
    • (2005) Dev. Dyn. , vol.233 , pp. 1525-1534
    • Levesque, M.1    Guimond, J.-C.2    Pilote, M.3    Leclerc, S.4    Moldovan, F.5    Roy, S.6
  • 110
    • 0029122585 scopus 로고
    • Sequence analysis of frog α-crystallin cDNA and its deduced primary structure: comparison of αA subunit chains among different vertebrate species
    • Lu S.-F., Pan F.-M., and Chiou S.-H. Sequence analysis of frog α-crystallin cDNA and its deduced primary structure: comparison of αA subunit chains among different vertebrate species. Biochem. Biophys. Res. Commun. 210 (1995) 974-981
    • (1995) Biochem. Biophys. Res. Commun. , vol.210 , pp. 974-981
    • Lu, S.-F.1    Pan, F.-M.2    Chiou, S.-H.3
  • 111
    • 0028883722 scopus 로고
    • Sequence analysis of frog αB crystallin cDNA: sequence homology and evolutionary comparison of αA, αB and heat shock proteins
    • Lu S.-F., Pan F.-M., and Chiou S.-H. Sequence analysis of frog αB crystallin cDNA: sequence homology and evolutionary comparison of αA, αB and heat shock proteins. Biochem. Biophys. Res. Commun. 216 (1995) 881-891
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 881-891
    • Lu, S.-F.1    Pan, F.-M.2    Chiou, S.-H.3
  • 112
    • 0033927557 scopus 로고    scopus 로고
    • Structure and function of small heat shock/α-crystallin proteins: established concepts and emerging ideas
    • MacRae T.H. Structure and function of small heat shock/α-crystallin proteins: established concepts and emerging ideas. Cell. Mol. Life Sci. 57 (2000) 899-913
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 899-913
    • MacRae, T.H.1
  • 113
    • 0025052137 scopus 로고
    • Identification of two HSP70-related Xenopus oocyte proteins that are capable of recycling across the nuclear envelope
    • Mandell R.B., and Feldherr C.M. Identification of two HSP70-related Xenopus oocyte proteins that are capable of recycling across the nuclear envelope. J. Cell Biol. 111 (1990) 1775-1783
    • (1990) J. Cell Biol. , vol.111 , pp. 1775-1783
    • Mandell, R.B.1    Feldherr, C.M.2
  • 114
    • 34748887784 scopus 로고    scopus 로고
    • Examination of KNK437- and quercetin-mediated inhibition of heat shock-induced heat shock protein gene expression in Xenopus laevis cultured cells
    • Manwell L.A., and Heikkila J.J. Examination of KNK437- and quercetin-mediated inhibition of heat shock-induced heat shock protein gene expression in Xenopus laevis cultured cells. Comp. Biochem. Physiol. 148 (2007) 521-530
    • (2007) Comp. Biochem. Physiol. , vol.148 , pp. 521-530
    • Manwell, L.A.1    Heikkila, J.J.2
  • 115
    • 0027288286 scopus 로고
    • The induction of pyruvate kinase synthesis by heat shock in Xenopus laevis embryos
    • Marsden M., Nickells R.W., Kapoor M., and Browder L.W. The induction of pyruvate kinase synthesis by heat shock in Xenopus laevis embryos. Dev. Genet. 14 (1993) 51-57
    • (1993) Dev. Genet. , vol.14 , pp. 51-57
    • Marsden, M.1    Nickells, R.W.2    Kapoor, M.3    Browder, L.W.4
  • 117
    • 0031006855 scopus 로고    scopus 로고
    • Xenopus heat shock factor 1 is a nuclear protein before heat stress
    • Mercier P.A., Foksa J., Ovsenek N., and Westwood J.T. Xenopus heat shock factor 1 is a nuclear protein before heat stress. J. Biol. Chem. 272 (1997) 14147-14151
    • (1997) J. Biol. Chem. , vol.272 , pp. 14147-14151
    • Mercier, P.A.1    Foksa, J.2    Ovsenek, N.3    Westwood, J.T.4
  • 118
    • 12344292410 scopus 로고    scopus 로고
    • Temporal and spatial manipulation of gene expression in Xenopus embryos by injection of heat shock promoter-containing plasmids
    • Michiue T., and Asashima M. Temporal and spatial manipulation of gene expression in Xenopus embryos by injection of heat shock promoter-containing plasmids. Dev. Dyn. 232 (2005) 369-376
    • (2005) Dev. Dyn. , vol.232 , pp. 369-376
    • Michiue, T.1    Asashima, M.2
  • 119
    • 0028260658 scopus 로고
    • Characterization of denatured protein inducers of the heat shock (stress) response in Xenopus laevis oocytes
    • Mifflin L.C., and Cohen R.E. Characterization of denatured protein inducers of the heat shock (stress) response in Xenopus laevis oocytes. J. Biol. Chem. 269 (1994) 15710-15717
    • (1994) J. Biol. Chem. , vol.269 , pp. 15710-15717
    • Mifflin, L.C.1    Cohen, R.E.2
  • 120
    • 0033050547 scopus 로고    scopus 로고
    • Constitutive and stress-inducible expression of the endoplasmic reticulum heat shock protein 70 gene family member, immunoglobulin-binding protein (BiP), during Xenopus laevis early development
    • Miskovic D., and Heikkila J.J. Constitutive and stress-inducible expression of the endoplasmic reticulum heat shock protein 70 gene family member, immunoglobulin-binding protein (BiP), during Xenopus laevis early development. Dev. Genet. 25 (1999) 31-39
    • (1999) Dev. Genet. , vol.25 , pp. 31-39
    • Miskovic, D.1    Heikkila, J.J.2
  • 121
    • 0030889987 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA encoding a Xenopus immunoglobulin binding protein, BiP (Grp78)
    • Miskovic D., Salter-Cid L., Ohan N., Flajnik M., and Heikkila J.J. Isolation and characterization of a cDNA encoding a Xenopus immunoglobulin binding protein, BiP (Grp78). Comp. Biochem. Physiol. 116B (1997) 227-234
    • (1997) Comp. Biochem. Physiol. , vol.116 B , pp. 227-234
    • Miskovic, D.1    Salter-Cid, L.2    Ohan, N.3    Flajnik, M.4    Heikkila, J.J.5
  • 122
    • 0032946166 scopus 로고    scopus 로고
    • Lens regeneration in Xenopus is not a mere repeat of lens development, with respect to crystallin gene expression
    • Mizuno N., Mochii M., Takahashi T.C., Eguchi G., and Okada T.S. Lens regeneration in Xenopus is not a mere repeat of lens development, with respect to crystallin gene expression. Differentiation 64 (1999) 143-149
    • (1999) Differentiation , vol.64 , pp. 143-149
    • Mizuno, N.1    Mochii, M.2    Takahashi, T.C.3    Eguchi, G.4    Okada, T.S.5
  • 123
    • 0012978847 scopus 로고    scopus 로고
    • Expression of crystallin genes inembryonic and regerating newt lenses
    • Mizuno N., Agata K., Sawada K., Mochii M., and Eguchi G. Expression of crystallin genes inembryonic and regerating newt lenses. Dev. Growth Differ. 44 (2002) 251-256
    • (2002) Dev. Growth Differ. , vol.44 , pp. 251-256
    • Mizuno, N.1    Agata, K.2    Sawada, K.3    Mochii, M.4    Eguchi, G.5
  • 124
    • 0028263853 scopus 로고
    • Transcription of amphibian lampbrush chromosomes is disturbed by microinjection of HSP70 monoclonal antibodies
    • Moreau N., Laine M.C., Billoud B., and Angelier N. Transcription of amphibian lampbrush chromosomes is disturbed by microinjection of HSP70 monoclonal antibodies. Exp. Cell Res. 211 (1994) 108-114
    • (1994) Exp. Cell Res. , vol.211 , pp. 108-114
    • Moreau, N.1    Laine, M.C.2    Billoud, B.3    Angelier, N.4
  • 125
    • 0031800886 scopus 로고    scopus 로고
    • Cell-cycle-dependent nuclear translocation of HSP70 in amphibian embryonic cells
    • Moreau N., Prudhomme C., and Angelier N. Cell-cycle-dependent nuclear translocation of HSP70 in amphibian embryonic cells. Int. J. Dev. Biol. 42 (1998) 633-636
    • (1998) Int. J. Dev. Biol. , vol.42 , pp. 633-636
    • Moreau, N.1    Prudhomme, C.2    Angelier, N.3
  • 126
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto R.I. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev. 12 (1998) 3788-3796
    • (1998) Genes Dev. , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 127
    • 6344285893 scopus 로고    scopus 로고
    • Hydrogen peroxide induces heat shock protein and proto-oncogene mRNA accumulation in Xenopus laevis A6 kidney epithelial cells
    • Muller M., Gauley J., and Heikkila J.J. Hydrogen peroxide induces heat shock protein and proto-oncogene mRNA accumulation in Xenopus laevis A6 kidney epithelial cells. Can. J. Physiol. Pharamcol. 82 (2004) 523-529
    • (2004) Can. J. Physiol. Pharamcol. , vol.82 , pp. 523-529
    • Muller, M.1    Gauley, J.2    Heikkila, J.J.3
  • 128
    • 34547612593 scopus 로고    scopus 로고
    • Expression of the small heat shock protein gene, hsp30, in Rana catesbeiana fibroblasts
    • Mulligan-Tuttle A., and Heikkila J.J. Expression of the small heat shock protein gene, hsp30, in Rana catesbeiana fibroblasts. Comp. Biochem. Physiol. 148 (2007) 308-316
    • (2007) Comp. Biochem. Physiol. , vol.148 , pp. 308-316
    • Mulligan-Tuttle, A.1    Heikkila, J.J.2
  • 129
    • 0025630059 scopus 로고
    • Heat shock protein 70 gene expression in intact salamanders (Eurycea bislineata) in response to calibrated heat shocks and to high temperatures encountered in the field
    • Near J.C., Easton D.P., Rutledge P.S., Dickinson D.P., and Spotila J.R. Heat shock protein 70 gene expression in intact salamanders (Eurycea bislineata) in response to calibrated heat shocks and to high temperatures encountered in the field. J. Exp. Zool. 256 (1990) 303-314
    • (1990) J. Exp. Zool. , vol.256 , pp. 303-314
    • Near, J.C.1    Easton, D.P.2    Rutledge, P.S.3    Dickinson, D.P.4    Spotila, J.R.5
  • 130
    • 0025100983 scopus 로고
    • An essential member of the HSP70 gene family of Saccharomyces cerevisiae is homologous to immunoglobulin heavy chain binding protein
    • Nicholson R.C., Williiams D.B., and Moran L.A. An essential member of the HSP70 gene family of Saccharomyces cerevisiae is homologous to immunoglobulin heavy chain binding protein. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 1159-1163
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 1159-1163
    • Nicholson, R.C.1    Williiams, D.B.2    Moran, L.A.3
  • 131
    • 0024110669 scopus 로고
    • A role for glyceraldehyde-3-phosphate dehydrogenase in the development of thermotolerance in Xenopus laevis embryos
    • Nickells R.W., and Browder L.W. A role for glyceraldehyde-3-phosphate dehydrogenase in the development of thermotolerance in Xenopus laevis embryos. J. Cell Biol. 107 (1988) 1901-1909
    • (1988) J. Cell Biol. , vol.107 , pp. 1901-1909
    • Nickells, R.W.1    Browder, L.W.2
  • 132
    • 47749112824 scopus 로고    scopus 로고
    • Population origin, development and temperature of development affect the amounts of HSP70, HSP90 and the putative hypoxia-inducible factor in the tadpoles of the common frog Rana temporaria
    • Nikinmaa M., Leveelahti L., Dahl E., Rissanen E., Rytkonen K.T., and Laurila A. Population origin, development and temperature of development affect the amounts of HSP70, HSP90 and the putative hypoxia-inducible factor in the tadpoles of the common frog Rana temporaria. J. Exp. Biol. 211 (2008) 1999-20004
    • (2008) J. Exp. Biol. , vol.211 , pp. 1999-20004
    • Nikinmaa, M.1    Leveelahti, L.2    Dahl, E.3    Rissanen, E.4    Rytkonen, K.T.5    Laurila, A.6
  • 133
    • 0030929973 scopus 로고    scopus 로고
    • Low-molecular-weight heat shock proteins in a desert fish (Poeciliopsis lucida): homologs of human Hsp27 and Xenopus Hsp30
    • Norris C.E., Brown M.A., Hickey E., Weber L.A., and Hightower L.E. Low-molecular-weight heat shock proteins in a desert fish (Poeciliopsis lucida): homologs of human Hsp27 and Xenopus Hsp30. Mol. Biol. Evol. 14 (1997) 115-129
    • (1997) Mol. Biol. Evol. , vol.14 , pp. 115-129
    • Norris, C.E.1    Brown, M.A.2    Hickey, E.3    Weber, L.A.4    Hightower, L.E.5
  • 134
    • 0029052774 scopus 로고
    • Involvement of differential gene expression and messenger RNA stability in the developmental regulation of the Hsp30 gene family in heat shocked Xenopus laevis embryos
    • Ohan N.W., and Heikkila J.J. Involvement of differential gene expression and messenger RNA stability in the developmental regulation of the Hsp30 gene family in heat shocked Xenopus laevis embryos. Dev. Genet. 17 (1995) 176-184
    • (1995) Dev. Genet. , vol.17 , pp. 176-184
    • Ohan, N.W.1    Heikkila, J.J.2
  • 135
    • 0031895813 scopus 로고    scopus 로고
    • Heat shock-induced assembly of Hsp30 family members into high molecular weight aggregates in Xenopus laevis cultured cells
    • Ohan N.W., Tam Y., Fernando P., and Heikkila J.J. Heat shock-induced assembly of Hsp30 family members into high molecular weight aggregates in Xenopus laevis cultured cells. Comp. Biochem. Physiol. B. 119 (1998) 381-389
    • (1998) Comp. Biochem. Physiol. B. , vol.119 , pp. 381-389
    • Ohan, N.W.1    Tam, Y.2    Fernando, P.3    Heikkila, J.J.4
  • 136
    • 0032460390 scopus 로고    scopus 로고
    • Characterization of a novel group of basic small heat shock proteins in Xenopus laevis A6 kidney epithelial cells
    • Ohan N.W., Tam Y., Fernando P., and Heikkila J.J. Characterization of a novel group of basic small heat shock proteins in Xenopus laevis A6 kidney epithelial cells. Biochem. Cell Biol. 76 (1998) 665-671
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 665-671
    • Ohan, N.W.1    Tam, Y.2    Fernando, P.3    Heikkila, J.J.4
  • 137
    • 0038692918 scopus 로고    scopus 로고
    • Effect of histone deacetylase inhibitors on heat shock protein gene expression during Xenopus development
    • Ovakim D.H., and Heikkila J.J. Effect of histone deacetylase inhibitors on heat shock protein gene expression during Xenopus development. Genesis 36 (2003) 88-96
    • (2003) Genesis , vol.36 , pp. 88-96
    • Ovakim, D.H.1    Heikkila, J.J.2
  • 138
    • 0023712261 scopus 로고
    • Heat shock-induced accumulation of ubiquitin mRNA in Xenopus laevis is developmentally regulated
    • Ovsenek N., and Heikkila J.J. Heat shock-induced accumulation of ubiquitin mRNA in Xenopus laevis is developmentally regulated. Dev. Biol. 12 (1988) 582-585
    • (1988) Dev. Biol. , vol.12 , pp. 582-585
    • Ovsenek, N.1    Heikkila, J.J.2
  • 139
    • 0025151698 scopus 로고
    • DNA sequence-specific binding activity of the heat shock transcription factor is heat-inducible before midblastula transition of early Xenopus development
    • Ovsenek N., and Heikkila J.J. DNA sequence-specific binding activity of the heat shock transcription factor is heat-inducible before midblastula transition of early Xenopus development. Development 110 (1990) 427-433
    • (1990) Development , vol.110 , pp. 427-433
    • Ovsenek, N.1    Heikkila, J.J.2
  • 140
    • 0025282426 scopus 로고
    • Cis-acting sequences and trans-acting factors required for constitutive expression of a microinjected HSP70 gene after the midblastula transition of Xenopus laevis embryogenesis
    • Ovsenek N., Williams G.T., Morimoto R.I., and Heikkila J.J. Cis-acting sequences and trans-acting factors required for constitutive expression of a microinjected HSP70 gene after the midblastula transition of Xenopus laevis embryogenesis. Dev. Genet. 11 (1990) 97-109
    • (1990) Dev. Genet. , vol.11 , pp. 97-109
    • Ovsenek, N.1    Williams, G.T.2    Morimoto, R.I.3    Heikkila, J.J.4
  • 141
    • 0023336183 scopus 로고
    • The yeast ubiquitin genes: a family of natural gene fusions
    • Ozkaynak E., Finley D., Solomon M.J., and Varshavsky A. The yeast ubiquitin genes: a family of natural gene fusions. EMBO J. 6 (1987) 1429-1439
    • (1987) EMBO J. , vol.6 , pp. 1429-1439
    • Ozkaynak, E.1    Finley, D.2    Solomon, M.J.3    Varshavsky, A.4
  • 142
    • 0027135501 scopus 로고
    • The function of heat shock proteins in stress tolerance: degradation and reactivation of the damaged proteins
    • Parsell D.A., and Lindquist S. The function of heat shock proteins in stress tolerance: degradation and reactivation of the damaged proteins. Annu. Rev. Genet. 27 (1993) 437-496
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 143
    • 48249122392 scopus 로고    scopus 로고
    • Identification of genes associated with regenerative success of Xenopus laevis hindlimbs
    • Pearl E.J., Barker D., Day R.C., and Beck C.W. Identification of genes associated with regenerative success of Xenopus laevis hindlimbs. BMC Dev. Biol. 8 (2008) 66
    • (2008) BMC Dev. Biol. , vol.8 , pp. 66
    • Pearl, E.J.1    Barker, D.2    Day, R.C.3    Beck, C.W.4
  • 144
    • 41149111451 scopus 로고    scopus 로고
    • The Hsp90 molecular chaperone: an open and shut case for treatment
    • Pearl L.H., Prodromou C., and Workman P. The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem. J. 410 (2008) 439-453
    • (2008) Biochem. J. , vol.410 , pp. 439-453
    • Pearl, L.H.1    Prodromou, C.2    Workman, P.3
  • 145
    • 0024755682 scopus 로고
    • Regulation of HSP70 synthesis by messenger RNA degradation
    • Petersen R.B., and Lindquist S. Regulation of HSP70 synthesis by messenger RNA degradation. Cell Regul. 1 (1989) 135-149
    • (1989) Cell Regul. , vol.1 , pp. 135-149
    • Petersen, R.B.1    Lindquist, S.2
  • 146
    • 0032818314 scopus 로고    scopus 로고
    • Heat shock-induced acquisition of thermotolerance at the levels of cell survival and translation in Xenopus A6 kidney epithelial cells
    • Phang D., Joyce E.M., and Heikkila J.J. Heat shock-induced acquisition of thermotolerance at the levels of cell survival and translation in Xenopus A6 kidney epithelial cells. Biochem. Cell Biol. 77 (1999) 141-151
    • (1999) Biochem. Cell Biol. , vol.77 , pp. 141-151
    • Phang, D.1    Joyce, E.M.2    Heikkila, J.J.3
  • 147
    • 0030767303 scopus 로고    scopus 로고
    • Conditions for a heat shock response during oogenesis and embryogenesis of the amphibian Pleurodeles waltl
    • Prudhomme C., Moreau N., and Angelier N. Conditions for a heat shock response during oogenesis and embryogenesis of the amphibian Pleurodeles waltl. Dev. Growth Differ. 39 (1997) 477-484
    • (1997) Dev. Growth Differ. , vol.39 , pp. 477-484
    • Prudhomme, C.1    Moreau, N.2    Angelier, N.3
  • 148
    • 0033016166 scopus 로고    scopus 로고
    • Fatal attraction: when chaperones turn harlot
    • Quinlan R., and Van Den Ijssel P. Fatal attraction: when chaperones turn harlot. Nat. Med. 5 (1999) 25-26
    • (1999) Nat. Med. , vol.5 , pp. 25-26
    • Quinlan, R.1    Van Den Ijssel, P.2
  • 149
    • 0037409604 scopus 로고    scopus 로고
    • Evolution of heat shock protein and immunity
    • Robert J. Evolution of heat shock protein and immunity. Dev. Comp. Immunol. 27 (2003) 449-464
    • (2003) Dev. Comp. Immunol. , vol.27 , pp. 449-464
    • Robert, J.1
  • 150
    • 0035133401 scopus 로고    scopus 로고
    • Phylogenetic conservation of the molecular and immunological properties of the chaperones gp96 and hsp70
    • Robert J., Menoret A., Basu S., Cohen N., and Srivastava P.K. Phylogenetic conservation of the molecular and immunological properties of the chaperones gp96 and hsp70. Eur. J. Immunol. 31 (2001) 186-195
    • (2001) Eur. J. Immunol. , vol.31 , pp. 186-195
    • Robert, J.1    Menoret, A.2    Basu, S.3    Cohen, N.4    Srivastava, P.K.5
  • 151
    • 72449129648 scopus 로고    scopus 로고
    • Xenopus, a Unique Comparative Model to Explore the Role of Certain Heat Shock Proteins and Non-classical MHC Class Ib Gene Products in Immune Surveillance
    • Robert J., Goyos A., and Nedelkovska H. Xenopus, a Unique Comparative Model to Explore the Role of Certain Heat Shock Proteins and Non-classical MHC Class Ib Gene Products in Immune Surveillance. Immunol. Res. 45 (2009) 114-122
    • (2009) Immunol. Res. , vol.45 , pp. 114-122
    • Robert, J.1    Goyos, A.2    Nedelkovska, H.3
  • 152
    • 0020965134 scopus 로고
    • Amphibian oocytes respond to heat shock after the induction of meiotic maturation by hormones
    • Rojas C., and Allende J.E. Amphibian oocytes respond to heat shock after the induction of meiotic maturation by hormones. Biochem. Int. 6 (1983) 517-525
    • (1983) Biochem. Int. , vol.6 , pp. 517-525
    • Rojas, C.1    Allende, J.E.2
  • 154
    • 0002073445 scopus 로고
    • Heat shock proteins from the lungless salamanders Eurycea bislineata and Desmognathus ochrophaeus
    • Rutledge P.S., Easton D.P., and Spotila J.R. Heat shock proteins from the lungless salamanders Eurycea bislineata and Desmognathus ochrophaeus. Comp. Biochem. Physiol. 88B (1987) 13-18
    • (1987) Comp. Biochem. Physiol. , vol.88 B , pp. 13-18
    • Rutledge, P.S.1    Easton, D.P.2    Spotila, J.R.3
  • 155
    • 0035650655 scopus 로고    scopus 로고
    • An essential role of histone deacetylases in postembryonic organ transformations in Xenopus laevis
    • Sachs L.M., Amano T., and Shi Y.B. An essential role of histone deacetylases in postembryonic organ transformations in Xenopus laevis. Int. J. Mol. Med. 8 (2001) 595-601
    • (2001) Int. J. Mol. Med. , vol.8 , pp. 595-601
    • Sachs, L.M.1    Amano, T.2    Shi, Y.B.3
  • 156
    • 34648857577 scopus 로고    scopus 로고
    • Different localization of HSP105 family proteins in mammalian cells
    • Saito Y., Yamagishi N., and Hatayama T. Different localization of HSP105 family proteins in mammalian cells. Exp. Cell Res. 313 (2007) 3707-3717
    • (2007) Exp. Cell Res. , vol.313 , pp. 3707-3717
    • Saito, Y.1    Yamagishi, N.2    Hatayama, T.3
  • 157
    • 0028366401 scopus 로고
    • Hsp70 genes are linked to the Xenopus major histocompatibility complex
    • Salter-Cid L., Kasahara M., and Flajnik M.F. Hsp70 genes are linked to the Xenopus major histocompatibility complex. Immunogenetics 39 (1994) 1-7
    • (1994) Immunogenetics , vol.39 , pp. 1-7
    • Salter-Cid, L.1    Kasahara, M.2    Flajnik, M.F.3
  • 159
    • 0029154777 scopus 로고
    • Male germ cell-specific alteration in temperature set point of the cellular stress response
    • Sarge K.D. Male germ cell-specific alteration in temperature set point of the cellular stress response. J. Biol. Chem. 270 (1995) 18745-18748
    • (1995) J. Biol. Chem. , vol.270 , pp. 18745-18748
    • Sarge, K.D.1
  • 160
    • 0028241317 scopus 로고
    • Expression of heat shock factor 2 in mouse testis: potential role as a regulator of heat shock protein gene expression during spermatogenesis
    • Sarge K.D., Park-Sarge O.K., Kirby J.D., Mayo K.E., and Moromoto R.I. Expression of heat shock factor 2 in mouse testis: potential role as a regulator of heat shock protein gene expression during spermatogenesis. Biol. Reprod. 50 (1994) 1334-1343
    • (1994) Biol. Reprod. , vol.50 , pp. 1334-1343
    • Sarge, K.D.1    Park-Sarge, O.K.2    Kirby, J.D.3    Mayo, K.E.4    Moromoto, R.I.5
  • 161
    • 33748785716 scopus 로고    scopus 로고
    • HSP90β is involved in signaling prolactin-induced apoptosis in newt testis
    • Saribek B., Jin Y., Saigo M., Ko E., and Abe S. HSP90β is involved in signaling prolactin-induced apoptosis in newt testis. Biochem. Biophys. Res. Commun. 349 (2006) 1190-1197
    • (2006) Biochem. Biophys. Res. Commun. , vol.349 , pp. 1190-1197
    • Saribek, B.1    Jin, Y.2    Saigo, M.3    Ko, E.4    Abe, S.5
  • 162
    • 0037086682 scopus 로고    scopus 로고
    • A novel function for the 90 kDa heat shock protein (Hsp90): facilitating nuclear export of 60S ribosomal subunits
    • Schlatter H., Langer T., Rosmus S., Onneken M.L., and Fasold H. A novel function for the 90 kDa heat shock protein (Hsp90): facilitating nuclear export of 60S ribosomal subunits. Biochem. J. 362 (2002) 675-684
    • (2002) Biochem. J. , vol.362 , pp. 675-684
    • Schlatter, H.1    Langer, T.2    Rosmus, S.3    Onneken, M.L.4    Fasold, H.5
  • 163
    • 43249109174 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress responses
    • Schroder M. Endoplasmic reticulum stress responses. Cell. Mol. Life Sci. 65 (2008) 862-894
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 862-894
    • Schroder, M.1
  • 164
    • 25444445362 scopus 로고    scopus 로고
    • Interaction between constitutively expressed heat shock protein, Hsc70, and cysteine string protein is important for cortical granule exocytosis in Xenopus oocytes
    • Smith G.B., Umbach J.A., Hirano A., and Gundersen C.B. Interaction between constitutively expressed heat shock protein, Hsc70, and cysteine string protein is important for cortical granule exocytosis in Xenopus oocytes. J. Biol. Chem. 280 (2005) 32669-32675
    • (2005) J. Biol. Chem. , vol.280 , pp. 32669-32675
    • Smith, G.B.1    Umbach, J.A.2    Hirano, A.3    Gundersen, C.B.4
  • 165
    • 0029100782 scopus 로고
    • The cDNA encoding Xenopus laevis heat-shock factor 1 (XHSF1): nucleotide and deduced amino-acid sequences, and properties of the encoded protein
    • Stumpf D.G., Landsberger N., and Wolffe A.P. The cDNA encoding Xenopus laevis heat-shock factor 1 (XHSF1): nucleotide and deduced amino-acid sequences, and properties of the encoded protein. Gene 160 (1995) 207-211
    • (1995) Gene , vol.160 , pp. 207-211
    • Stumpf, D.G.1    Landsberger, N.2    Wolffe, A.P.3
  • 166
    • 0029558353 scopus 로고
    • Identification of members of the hsp30 small heat shock protein family and characterization of their developmental regulation in heat-shocked Xenopus laevis embryos
    • Tam Y., and Heikkila J.J. Identification of members of the hsp30 small heat shock protein family and characterization of their developmental regulation in heat-shocked Xenopus laevis embryos. Dev. Genet. 17 (1995) 331-339
    • (1995) Dev. Genet. , vol.17 , pp. 331-339
    • Tam, Y.1    Heikkila, J.J.2
  • 167
    • 84993865989 scopus 로고
    • Limb amputation and heat shock induce changes in protein expression in the newt, Notophthalmus viridescens
    • Tam Y., Vethamany-Globus S., and Globus M. Limb amputation and heat shock induce changes in protein expression in the newt, Notophthalmus viridescens. J. Exp. Zool. 264 (1992) 64-74
    • (1992) J. Exp. Zool. , vol.264 , pp. 64-74
    • Tam, Y.1    Vethamany-Globus, S.2    Globus, M.3
  • 168
    • 0021094229 scopus 로고
    • The absence of the long 3′-non-translated region in mRNA coding for eye lens αA2-crystallin of the frog (Rana temporaria)
    • Tomarev S.I., Zinovieva R.D., Dolgilevich S.M., Krayev A.S., Skryabin K.G., and Gause Jr. G.G. The absence of the long 3′-non-translated region in mRNA coding for eye lens αA2-crystallin of the frog (Rana temporaria). FEBS Letts. 162 (1983) 47-51
    • (1983) FEBS Letts. , vol.162 , pp. 47-51
    • Tomarev, S.I.1    Zinovieva, R.D.2    Dolgilevich, S.M.3    Krayev, A.S.4    Skryabin, K.G.5    Gause Jr., G.G.6
  • 169
    • 23344436560 scopus 로고    scopus 로고
    • Regulation of heat shock gene transcription in neuronal cells
    • Tonkiss J., and Calderwood S.K. Regulation of heat shock gene transcription in neuronal cells. Int. J. Hyperthermia 21 (2005) 433-444
    • (2005) Int. J. Hyperthermia , vol.21 , pp. 433-444
    • Tonkiss, J.1    Calderwood, S.K.2
  • 170
    • 77950857536 scopus 로고    scopus 로고
    • Hsp27 is persistently expressed in zebrafish skeletal and cardiac muscle tissues but dispensable for their morphogenesis
    • Tucker N.R., Ustyugov A., Bryantsev A.L., Konkel M.E., and Shelden E.A. Hsp27 is persistently expressed in zebrafish skeletal and cardiac muscle tissues but dispensable for their morphogenesis. Cell Stress Chaperones 14 (2009) 521-533
    • (2009) Cell Stress Chaperones , vol.14 , pp. 521-533
    • Tucker, N.R.1    Ustyugov, A.2    Bryantsev, A.L.3    Konkel, M.E.4    Shelden, E.A.5
  • 171
    • 33947508130 scopus 로고    scopus 로고
    • Analysis of the small heat shock protein gene, hsp27, in Xenopus laevis embryos
    • Tuttle A.M., Gauley J., Chan N., and Heikkila J.J. Analysis of the small heat shock protein gene, hsp27, in Xenopus laevis embryos. Comp. Biochem. Physiol. Part A 147 (2007) 112-121
    • (2007) Comp. Biochem. Physiol. Part A , vol.147 , pp. 112-121
    • Tuttle, A.M.1    Gauley, J.2    Chan, N.3    Heikkila, J.J.4
  • 172
    • 0028841776 scopus 로고
    • Identification of a complex between heat shock proteins in CSF-arrested Xenopus oocytes and dissociation of the complex following oocyte activation
    • Uzawa M., Grams J., Madden B., Toft D., and Salisbury J.L. Identification of a complex between heat shock proteins in CSF-arrested Xenopus oocytes and dissociation of the complex following oocyte activation. Dev. Biol. 171 (1995) 51-59
    • (1995) Dev. Biol. , vol.171 , pp. 51-59
    • Uzawa, M.1    Grams, J.2    Madden, B.3    Toft, D.4    Salisbury, J.L.5
  • 173
    • 0035718677 scopus 로고    scopus 로고
    • Structure and function of the small heat shock protein/α-crystallin family of molecular chaperones
    • Van Montfort R., Slingsby C., and Vierling E. Structure and function of the small heat shock protein/α-crystallin family of molecular chaperones. Adv. Protein Chem. 59 (2002) 105-156
    • (2002) Adv. Protein Chem. , vol.59 , pp. 105-156
    • Van Montfort, R.1    Slingsby, C.2    Vierling, E.3
  • 174
    • 0027934182 scopus 로고
    • Constitutive expression of a microinjected glucose-regulated protein (grp78) fusion gene during early Xenopus laevis development
    • Vezina C., Wooden S.K., Lee A.S., and Heikkila J.J. Constitutive expression of a microinjected glucose-regulated protein (grp78) fusion gene during early Xenopus laevis development. Differentiation 57 (1994) 171-177
    • (1994) Differentiation , vol.57 , pp. 171-177
    • Vezina, C.1    Wooden, S.K.2    Lee, A.S.3    Heikkila, J.J.4
  • 175
    • 3542991477 scopus 로고    scopus 로고
    • On mechanisms that control heat shock transcription factor activity in metazoan cells
    • Voellmy R. On mechanisms that control heat shock transcription factor activity in metazoan cells. Cell Stress Chaperones 9 (2004) 122-133
    • (2004) Cell Stress Chaperones , vol.9 , pp. 122-133
    • Voellmy, R.1
  • 176
    • 0019944776 scopus 로고
    • Transcription of a Drosophila heat shock gene is heat-induced in Xenopus oocytes
    • Voellmy R., and Rungger D. Transcription of a Drosophila heat shock gene is heat-induced in Xenopus oocytes. Proc. Natl. Acad. Sci. U. S. A. 79 (1982) 1776-1780
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 1776-1780
    • Voellmy, R.1    Rungger, D.2
  • 177
    • 46849116411 scopus 로고    scopus 로고
    • Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families
    • Vos M.J., Hageman J., Carra S., and Kampinga H.H. Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families. Biochemistry 47 (2008) 7001-7011
    • (2008) Biochemistry , vol.47 , pp. 7001-7011
    • Vos, M.J.1    Hageman, J.2    Carra, S.3    Kampinga, H.H.4
  • 178
    • 49549105093 scopus 로고    scopus 로고
    • Comparison of the effect of heat shock factor inhibitor, KNK437, on heat shock- and chemical stress-induced hsp30 gene expression in Xenopus laevis A6 cells
    • Voyer J., and Heikkila J.J. Comparison of the effect of heat shock factor inhibitor, KNK437, on heat shock- and chemical stress-induced hsp30 gene expression in Xenopus laevis A6 cells. Comp. Biochem. Physiol. 151 (2008) 253-261
    • (2008) Comp. Biochem. Physiol. , vol.151 , pp. 253-261
    • Voyer, J.1    Heikkila, J.J.2
  • 179
    • 0142219722 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of cadmium carcinogenesis
    • Waisberg M., Pius J., Hale B., and Beyersmann D. Molecular and cellular mechanisms of cadmium carcinogenesis. Toxicology 192 (2003) 95-117
    • (2003) Toxicology , vol.192 , pp. 95-117
    • Waisberg, M.1    Pius, J.2    Hale, B.3    Beyersmann, D.4
  • 180
    • 0034644108 scopus 로고    scopus 로고
    • Inducible gene expression in transgenic Xenopus embryos
    • Wheeler G.N., Hamilton F.S., and Hoppler S. Inducible gene expression in transgenic Xenopus embryos. Curr. Biol. 10 (2000) 849-852
    • (2000) Curr. Biol. , vol.10 , pp. 849-852
    • Wheeler, G.N.1    Hamilton, F.S.2    Hoppler, S.3
  • 181
    • 0024369102 scopus 로고
    • Induction of glucose-regulated proteins in Xenopus laevis A6 cells
    • Winning R.S., Heikkila J.J., and Bols N.C. Induction of glucose-regulated proteins in Xenopus laevis A6 cells. J. Cell. Physiol. 140 (1989) 239-245
    • (1989) J. Cell. Physiol. , vol.140 , pp. 239-245
    • Winning, R.S.1    Heikkila, J.J.2    Bols, N.C.3
  • 182
    • 0025735221 scopus 로고
    • Tunicamycin-inducible polypeptide synthesis during Xenopus laevis embryogenesis
    • Winning R.S., Bols N.C., and Heikkila J.J. Tunicamycin-inducible polypeptide synthesis during Xenopus laevis embryogenesis. Differentiation 46 (1991) 167-172
    • (1991) Differentiation , vol.46 , pp. 167-172
    • Winning, R.S.1    Bols, N.C.2    Heikkila, J.J.3
  • 183
    • 0026516045 scopus 로고
    • Analysis of the expression of a glucose-regulated protein (GRP78) promoter/CAT fusion gene during early Xenopus laevis development
    • Winning R.S., Bols N.C., Wooden S.K., Lee A.S., and Heikkila J.J. Analysis of the expression of a glucose-regulated protein (GRP78) promoter/CAT fusion gene during early Xenopus laevis development. Differentiation 49 (1992) 1-6
    • (1992) Differentiation , vol.49 , pp. 1-6
    • Winning, R.S.1    Bols, N.C.2    Wooden, S.K.3    Lee, A.S.4    Heikkila, J.J.5
  • 184
    • 0021133350 scopus 로고
    • Culture shock: synthesis of heat-shock-like proteins in fresh primary cell cultures
    • Wolffe A.P., Glover J.F., and Tata J.R. Culture shock: synthesis of heat-shock-like proteins in fresh primary cell cultures. Exp. Cell Res. 154 (1984) 581-590
    • (1984) Exp. Cell Res. , vol.154 , pp. 581-590
    • Wolffe, A.P.1    Glover, J.F.2    Tata, J.R.3
  • 185
    • 56649105146 scopus 로고    scopus 로고
    • Examination of cadmium-induced expression of the small heat shock protein gene, hsp30, in Xenopus laevis A6 kidney epithelial cells
    • Woolfson J.P., and Heikkila J.J. Examination of cadmium-induced expression of the small heat shock protein gene, hsp30, in Xenopus laevis A6 kidney epithelial cells. Comp. Biochem. Physiol. Part A 152 (2009) 91-99
    • (2009) Comp. Biochem. Physiol. Part A , vol.152 , pp. 91-99
    • Woolfson, J.P.1    Heikkila, J.J.2
  • 186
    • 0023666534 scopus 로고
    • Purification and properties of Drosophila heat shock activator protein
    • Wu C., Wilson S., Walker B., Dawid I., Paisley T., Zimarino V., and Ueda H. Purification and properties of Drosophila heat shock activator protein. Science 238 (1987) 1247-1253
    • (1987) Science , vol.238 , pp. 1247-1253
    • Wu, C.1    Wilson, S.2    Walker, B.3    Dawid, I.4    Paisley, T.5    Zimarino, V.6    Ueda, H.7
  • 187
    • 0034666164 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3b negatively regulates both DNA-binding and transcriptional activities of heat shock factor 1
    • Xavier I.J., Mercier P.A., McLoughlin C.M., Ali A., Woodgett J.R., and Ovsenek N. Glycogen synthase kinase 3b negatively regulates both DNA-binding and transcriptional activities of heat shock factor 1. J. Biol. Chem. 275 (2000) 29147-29152
    • (2000) J. Biol. Chem. , vol.275 , pp. 29147-29152
    • Xavier, I.J.1    Mercier, P.A.2    McLoughlin, C.M.3    Ali, A.4    Woodgett, J.R.5    Ovsenek, N.6
  • 188
    • 0346037326 scopus 로고    scopus 로고
    • The Kruppel-like factor Zf9 and proteins in the Sp1 family regulate the expression of HSP47, a collagen-specific molecular chaperone
    • Yasuda K., Hirayoshi K., Hirata H., Kubota H., Hosokawa N., and Nagata K. The Kruppel-like factor Zf9 and proteins in the Sp1 family regulate the expression of HSP47, a collagen-specific molecular chaperone. J. Biol. Chem. 277 (2002) 44613-44622
    • (2002) J. Biol. Chem. , vol.277 , pp. 44613-44622
    • Yasuda, K.1    Hirayoshi, K.2    Hirata, H.3    Kubota, H.4    Hosokawa, N.5    Nagata, K.6
  • 189
    • 34249292278 scopus 로고    scopus 로고
    • Wint-β-catenin signaling has an essential role in the initiation of limb regeneration
    • Yokoyama H., Ogino H., Stoick-Cooper C.L., Grainger R.M., and Moon R.T. Wint-β-catenin signaling has an essential role in the initiation of limb regeneration. Dev. Biol. 306 (2007) 170-178
    • (2007) Dev. Biol. , vol.306 , pp. 170-178
    • Yokoyama, H.1    Ogino, H.2    Stoick-Cooper, C.L.3    Grainger, R.M.4    Moon, R.T.5
  • 190
    • 77951257992 scopus 로고    scopus 로고
    • Proteasome inhibition induces hsp30 and hsp70 gene expression as well as the acquisition of thermotolerance in Xenopus laevis A6 cells
    • in press, doi:10.1007/s12192-009-0147-4
    • Young, J.T.F., Heikkila, J.J. in press. Proteasome inhibition induces hsp30 and hsp70 gene expression as well as the acquisition of thermotolerance in Xenopus laevis A6 cells. Cell Stress Chaperones. doi:10.1007/s12192-009-0147-4.
    • Cell Stress Chaperones
    • Young, J.T.F.1    Heikkila, J.J.2
  • 191
    • 65649117011 scopus 로고    scopus 로고
    • Simultaneous exposure of Xenopus A6 kidney epithelial cells to concurrent mild sodium arsenite and heat stress results in enhanced hsp30 and hsp70 gene expression and the acquisition of thermotolerance
    • Young J.T.F., Gauley J., and Heikkila J.J. Simultaneous exposure of Xenopus A6 kidney epithelial cells to concurrent mild sodium arsenite and heat stress results in enhanced hsp30 and hsp70 gene expression and the acquisition of thermotolerance. Comp. Biochem. Physiol. Part A 153 (2009) 417-424
    • (2009) Comp. Biochem. Physiol. Part A , vol.153 , pp. 417-424
    • Young, J.T.F.1    Gauley, J.2    Heikkila, J.J.3
  • 192
    • 0001874380 scopus 로고
    • Monoclonal antibody ELISA test indicates that large amounts of constitutive hsp-70 are present in salamanders, turtle and fish
    • Yu Z., Magee W.E., and Spotila J.R. Monoclonal antibody ELISA test indicates that large amounts of constitutive hsp-70 are present in salamanders, turtle and fish. J. Therm. Biol. 19 (1994) 41-53
    • (1994) J. Therm. Biol. , vol.19 , pp. 41-53
    • Yu, Z.1    Magee, W.E.2    Spotila, J.R.3


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