메뉴 건너뛰기




Volumn 14, Issue 5, 2003, Pages 251-258

Molecular chaperones, stress resistance and development in Artemia franciscana

Author keywords

Artemia franciscana; Diapause; Embryo development; Molecular chaperone; Small heat shock crystallin proteins

Indexed keywords

ALPHA CRYSTALLIN; ARTEMIN; CHAPERONE; DISACCHARIDE; FERRITIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; PROTEIN P26; TREHALOSE; UNCLASSIFIED DRUG;

EID: 0742322606     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.semcdb.2003.09.019     Document Type: Article
Times cited : (102)

References (65)
  • 1
    • 0031857075 scopus 로고    scopus 로고
    • Review of the biogeography of the genus Artemia (Crustacea, Anostraca)
    • Triantaphyllidis G.V., Abatzopoulos T.J., Sorgeloos P. Review of the biogeography of the genus Artemia (Crustacea, Anostraca). J. Biogeogr. 25:1998;213-226.
    • (1998) J. Biogeogr. , vol.25 , pp. 213-226
    • Triantaphyllidis, G.V.1    Abatzopoulos, T.J.2    Sorgeloos, P.3
  • 2
  • 3
    • 0014839134 scopus 로고
    • The origin and structure of the tertiary envelope in thick-shelled eggs of the brine shrimp, Artemia
    • Anderson E., Lochhead J.H., Lochhead M.S., Huebner E. The origin and structure of the tertiary envelope in thick-shelled eggs of the brine shrimp, Artemia. J. Ultrastruct. Res. 32:1970;497-525.
    • (1970) J. Ultrastruct. Res. , vol.32 , pp. 497-525
    • Anderson, E.1    Lochhead, J.H.2    Lochhead, M.S.3    Huebner, E.4
  • 5
    • 85029463032 scopus 로고    scopus 로고
    • Storey KB, editor. Molecular mechanisms of metabolic arrest: life in limbo. Oxford: BIOS Scientific Publishing
    • MacRae TH. Do stress proteins protect embryos during metabolic arrest and diapause? In: Storey KB, editor. Molecular mechanisms of metabolic arrest: life in limbo. Oxford: BIOS Scientific Publishing; 2001. p. 169-86.
    • (2001) Do Stress Proteins Protect Embryos during Metabolic Arrest and Diapause? , pp. 169-186
    • MacRae, T.H.1
  • 7
    • 0023154238 scopus 로고
    • Regulation of embryonic diapause in Artemia: Environmental and physiological signals
    • Drinkwater L.E., Crowe J.H. Regulation of embryonic diapause in Artemia: environmental and physiological signals. J. Exp. Zool. 241:1987;297-307.
    • (1987) J. Exp. Zool. , vol.241 , pp. 297-307
    • Drinkwater, L.E.1    Crowe, J.H.2
  • 8
    • 85051493040 scopus 로고
    • Browne RA, Sorgeloos P, Trotman CNA, editors. Artemia biology. Boca Raton, FL: CRC Press
    • Drinkwater LE, Clegg JS. Experimental biology of cyst diapause. In: Browne RA, Sorgeloos P, Trotman CNA, editors. Artemia biology. Boca Raton, FL: CRC Press; 1991. p. 93-117.
    • (1991) Experimental Biology of Cyst Diapause , pp. 93-117
    • Le, D.1    Clegg, J.S.2
  • 9
    • 0033559203 scopus 로고    scopus 로고
    • The synthesis of a small heat shock/α-crystallin protein in Artemia and its relationship to stress tolerance during development
    • Liang P., MacRae T.H. The synthesis of a small heat shock/α- crystallin protein in Artemia and its relationship to stress tolerance during development. Dev. Biol. 207:1999;445-456.
    • (1999) Dev. Biol. , vol.207 , pp. 445-456
    • Liang, P.1    MacRae, T.H.2
  • 10
    • 22844453994 scopus 로고    scopus 로고
    • Adaptive significance of a small heat shock/α-crystallin protein (p26) in encysted embryos of the brine shrimp Artemia franciscana
    • Clegg J.S., Willsie J.K., Jackson S.A. Adaptive significance of a small heat shock/α-crystallin protein (p26) in encysted embryos of the brine shrimp Artemia franciscana. Am. Zool. 39:1999;836-847.
    • (1999) Am. Zool. , vol.39 , pp. 836-847
    • Clegg, J.S.1    Willsie, J.K.2    Jackson, S.A.3
  • 11
    • 0001299081 scopus 로고
    • Hydration, its reversibility, and the beginning of development in the brine shrimp, Artemia salina
    • Morris J.E. Hydration, its reversibility, and the beginning of development in the brine shrimp, Artemia salina. Comp. Biochem. Physiol. 39:1971;843-857.
    • (1971) Comp. Biochem. Physiol. , vol.39 , pp. 843-857
    • Morris, J.E.1
  • 12
    • 0027397807 scopus 로고
    • Extension of enzyme half-life during quiescence in Artemia embryos
    • Anchordoguy T.J., Hofmann G.E., Hand S.C. Extension of enzyme half-life during quiescence in Artemia embryos. Am. J. Physiol. 264:1993;R85-R89.
    • (1993) Am. J. Physiol. , vol.264
    • Anchordoguy, T.J.1    Hofmann, G.E.2    Hand, S.C.3
  • 13
    • 0028035896 scopus 로고
    • Unusual response of Artemia franciscana embryos to prolonged anoxia
    • Clegg J.S. Unusual response of Artemia franciscana embryos to prolonged anoxia. J. Exp. Zool. 270:1994;332-334.
    • (1994) J. Exp. Zool. , vol.270 , pp. 332-334
    • Clegg, J.S.1
  • 14
    • 0030830201 scopus 로고    scopus 로고
    • Embryos of Artemia franciscana survive four years of continuous anoxia: The case for complete metabolic rate depression
    • Clegg J.S. Embryos of Artemia franciscana survive four years of continuous anoxia: the case for complete metabolic rate depression. J. Exp. Biol. 200:1997;467-475.
    • (1997) J. Exp. Biol. , vol.200 , pp. 467-475
    • Clegg, J.S.1
  • 15
    • 0000829345 scopus 로고    scopus 로고
    • The metabolic status of quiescent and diapause embryos of Artemia franciscana (Kellogg)
    • Clegg J.S., Jackson S.A. The metabolic status of quiescent and diapause embryos of Artemia franciscana (Kellogg). Arch. Hydrobiol. Spec. Issues Adv. Limnol. 52:1998;425-439.
    • (1998) Arch. Hydrobiol. Spec. Issues Adv. Limnol. , vol.52 , pp. 425-439
    • Clegg, J.S.1    Jackson, S.A.2
  • 16
    • 0030018997 scopus 로고    scopus 로고
    • The metabolic status of diapause embryos of Artemia franciscana (SFB)
    • Clegg J.S., Drinkwater L.E., Sorgeloos P. The metabolic status of diapause embryos of Artemia franciscana (SFB). Physiol. Zool. 69:1996;49-66.
    • (1996) Physiol. Zool. , vol.69 , pp. 49-66
    • Clegg, J.S.1    Drinkwater, L.E.2    Sorgeloos, P.3
  • 17
    • 0033845794 scopus 로고    scopus 로고
    • Long-term anoxia in encysted embryos of the crustacean, Artemia franciscana: Viability, ultrastructure, and stress proteins
    • Clegg J.S., Jackson S.A., Popov V.I. Long-term anoxia in encysted embryos of the crustacean, Artemia franciscana: viability, ultrastructure, and stress proteins. Cell Tissues Res. 301:2000;433-446.
    • (2000) Cell Tissues Res. , vol.301 , pp. 433-446
    • Clegg, J.S.1    Jackson, S.A.2    Popov, V.I.3
  • 18
    • 0034826341 scopus 로고    scopus 로고
    • Diguanosine nucleotide metabolism and the survival of Artemia embryos during years of continuous anoxia
    • Warner A.H., Clegg J.S. Diguanosine nucleotide metabolism and the survival of Artemia embryos during years of continuous anoxia. Eur. J. Biochem. 268:2001;1568-1576.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1568-1576
    • Warner, A.H.1    Clegg, J.S.2
  • 19
    • 0037323025 scopus 로고    scopus 로고
    • Transcriptional initiation under conditions of anoxia-induced quiescence in mitochondria from Artemia franciscana embryos
    • Eads B.D., Hand S.C. Transcriptional initiation under conditions of anoxia-induced quiescence in mitochondria from Artemia franciscana embryos. J. Exp. Biol. 206:2003;577-589.
    • (2003) J. Exp. Biol. , vol.206 , pp. 577-589
    • Eads, B.D.1    Hand, S.C.2
  • 22
    • 0038692918 scopus 로고    scopus 로고
    • Effect of histone deacetylase inhibitors on heat shock protein gene expression during Xenopus development
    • Ovakim D.H., 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
  • 23
    • 0029952344 scopus 로고    scopus 로고
    • Ontogeny of low molecular weight stress protein p26 during early development of the brine shrimp, Artemia franciscana
    • Jackson S.A., Clegg J.S. Ontogeny of low molecular weight stress protein p26 during early development of the brine shrimp, Artemia franciscana. Dev. Growth Differ. 38:1996;153-160.
    • (1996) Dev. Growth Differ. , vol.38 , pp. 153-160
    • Jackson, S.A.1    Clegg, J.S.2
  • 24
    • 0000038312 scopus 로고
    • The heat shock response of the cryptobiotic brine shrimp Artemia-1. A comparison of the thermotolerance of cysts and larvae
    • Miller D., McLennan A.G. The heat shock response of the cryptobiotic brine shrimp Artemia-1. A comparison of the thermotolerance of cysts and larvae. J. Therm. Biol. 13:1988;119-123.
    • (1988) J. Therm. Biol. , vol.13 , pp. 119-123
    • Miller, D.1    McLennan, A.G.2
  • 25
    • 0000107501 scopus 로고
    • The heat shock response of the cryptobiotic brine shrimp Artemia-II. Heat shock proteins
    • Miller D., McLennan A.G. The heat shock response of the cryptobiotic brine shrimp Artemia-II. Heat shock proteins. J. Therm. Biol. 13:1988;125-134.
    • (1988) J. Therm. Biol. , vol.13 , pp. 125-134
    • Miller, D.1    McLennan, A.G.2
  • 26
    • 0025097023 scopus 로고
    • A biological role for the heat shock response in crustaceans
    • McLennan A.G., Miller D. A biological role for the heat shock response in crustaceans. J. Therm. Biol. 15:1990;61-66.
    • (1990) J. Therm. Biol. , vol.15 , pp. 61-66
    • McLennan, A.G.1    Miller, D.2
  • 27
    • 0037219976 scopus 로고    scopus 로고
    • Molecular characterization of artemin and ferritin from Artemia franciscana
    • Chen T., Amons R., Clegg J.S., Warner A.H., MacRae T.H. Molecular characterization of artemin and ferritin from Artemia franciscana. Eur. J. Biochem. 270:2003;137-145.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 137-145
    • Chen, T.1    Amons, R.2    Clegg, J.S.3    Warner, A.H.4    MacRae, T.H.5
  • 28
  • 29
    • 0030973550 scopus 로고    scopus 로고
    • Unique structural features of a novel class of small heat shock proteins
    • Leroux M.R., Ma B.J., Batelier G., Melki R., Candido E.P.M. Unique structural features of a novel class of small heat shock proteins. J. Biol. Chem. 272:1997;12847-12853.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12847-12853
    • Leroux, M.R.1    Ma, B.J.2    Batelier, G.3    Melki, R.4    Candido, E.P.M.5
  • 30
    • 0030829559 scopus 로고    scopus 로고
    • A plant small heat shock protein gene expressed during zygotic embryogenesis but noninducible by heat stress
    • Carranco R., Almoguera C., Jordano J. A plant small heat shock protein gene expressed during zygotic embryogenesis but noninducible by heat stress. J. Biol. Chem. 272:1997;27470-27475.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27470-27475
    • Carranco, R.1    Almoguera, C.2    Jordano, J.3
  • 31
    • 0026605621 scopus 로고
    • Aerobic heat shock activates trehalose synthesis in embryos of Artemia franciscana
    • Clegg J.S., Jackson S.A. Aerobic heat shock activates trehalose synthesis in embryos of Artemia franciscana. FEBS Lett. 303:1992;45-47.
    • (1992) FEBS Lett. , vol.303 , pp. 45-47
    • Clegg, J.S.1    Jackson, S.A.2
  • 34
    • 0030154323 scopus 로고    scopus 로고
    • Influence of molecular and chemical chaperones on protein folding
    • Welsh W.J., Brown C.R. Influence of molecular and chemical chaperones on protein folding. Cell Stress Chaperones. 1:1996;109-115.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 109-115
    • Welsh, W.J.1    Brown, C.R.2
  • 35
    • 0034992527 scopus 로고    scopus 로고
    • Influence of trehalose on the molecular chaperone activity of p26 a small heat shock/α-crystallin protein
    • Viner R.I., Clegg J.S. Influence of trehalose on the molecular chaperone activity of p26 a small heat shock/α-crystallin protein. Cell Stress Chaperones. 6:2001;126-135.
    • (2001) Cell Stress Chaperones , vol.6 , pp. 126-135
    • Viner, R.I.1    Clegg, J.S.2
  • 36
    • 0031020927 scopus 로고    scopus 로고
    • Purification, structure and in vitro molecular-chaperone activity of Artemia p26, a small-heat shock/α-crystallin protein
    • Liang P., Amons R., MacRae T.H., Clegg J.S. Purification, structure and in vitro molecular-chaperone activity of Artemia p26, a small-heat shock/α-crystallin protein. Eur. J. Biochem. 243:1997;225-232.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 225-232
    • Liang, P.1    Amons, R.2    MacRae, T.H.3    Clegg, J.S.4
  • 37
    • 0030755398 scopus 로고    scopus 로고
    • Molecular characterization of a small heat shock/α-crystallin protein in encysted Artemia embryos
    • Liang P., Amons R., Clegg J.S., MacRae T.H. Molecular characterization of a small heat shock/α-crystallin protein in encysted Artemia embryos. J. Biol. Chem. 272:1997;19051-19058.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19051-19058
    • Liang, P.1    Amons, R.2    Clegg, J.S.3    MacRae, T.H.4
  • 38
    • 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
  • 39
    • 0036195722 scopus 로고    scopus 로고
    • α-Crystallin-type heat shock proteins: Socializing minichaperones in the context of a multichaperone network
    • Narberhaus F. α-Crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network. Microbiol. Mol. Biol. Rev. 66:2002;64-93.
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 64-93
    • Narberhaus, F.1
  • 40
    • 0041525250 scopus 로고    scopus 로고
    • A small heat shock/(-crystallin protein from encysted Artemia embryos suppresses tubulin denaturation
    • Day R.M., Gupta J.S., MacRae T.H. A small heat shock/(-crystallin protein from encysted Artemia embryos suppresses tubulin denaturation. Cell Stress Chaperones. 8:2003;183-193.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 183-193
    • Day, R.M.1    Gupta, J.S.2    MacRae, T.H.3
  • 42
    • 0035667159 scopus 로고    scopus 로고
    • ATP causes small heat shock proteins to release denatured protein
    • Wang K., Spector A. ATP causes small heat shock proteins to release denatured protein. Eur. J. Biochem. 268:2001;6335-6345.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6335-6345
    • Wang, K.1    Spector, A.2
  • 43
    • 0036186814 scopus 로고    scopus 로고
    • Functional analysis of a small heat shock/α-crystallin protein from Artemia franciscana. Oligomerization and thermotolerance
    • Crack J.A., Mansour M., Sun Y., MacRae T.H. Functional analysis of a small heat shock/α-crystallin protein from Artemia franciscana. Oligomerization and thermotolerance. Eur. J. Biochem. 269:2002;933-942.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 933-942
    • Crack, J.A.1    Mansour, M.2    Sun, Y.3    MacRae, T.H.4
  • 44
    • 0037415685 scopus 로고    scopus 로고
    • Nitric oxide-induced suspended animation promotes survival during hypoxia
    • Teodoro R.O., O'Farrell P.H. Nitric oxide-induced suspended animation promotes survival during hypoxia. EMBO J. 22:2003;580-587.
    • (2003) EMBO J. , vol.22 , pp. 580-587
    • Teodoro, R.O.1    O'Farrell, P.H.2
  • 45
    • 0038789632 scopus 로고
    • Intracellular pH regulates transitions between dormancy and development of brine shrimp (Artemia salina) embryos
    • Busa W.B., Crowe J.H. Intracellular pH regulates transitions between dormancy and development of brine shrimp (Artemia salina) embryos. Science. 221:1983;366-368.
    • (1983) Science , vol.221 , pp. 366-368
    • Busa, W.B.1    Crowe, J.H.2
  • 46
    • 0000420251 scopus 로고
    • Cytological studies of Artemia salina. I. Embryonic development without cell multiplication after the blastula stage in encysted dry eggs
    • Nakanishi Y.H., Iwasaki T., Okigaki T., Kato H. Cytological studies of Artemia salina. I. Embryonic development without cell multiplication after the blastula stage in encysted dry eggs. Annot. Zool. Jpn. 35:1962;223-228.
    • (1962) Annot. Zool. Jpn. , vol.35 , pp. 223-228
    • Nakanishi, Y.H.1    Iwasaki, T.2    Okigaki, T.3    Kato, H.4
  • 48
    • 0038059318 scopus 로고    scopus 로고
    • Regulation of promoter occupancy during activation of cryptobiotic embryos from the crustacean Artemia franciscana
    • Martinez-Lamparero A., Casero M.-C., Ortiz-Caro J., Sastre L. Regulation of promoter occupancy during activation of cryptobiotic embryos from the crustacean Artemia franciscana. J. Exp. Biol. 206:2003;1565-1573.
    • (2003) J. Exp. Biol. , vol.206 , pp. 1565-1573
    • Martinez-Lamparero, A.1    Casero, M.-C.2    Ortiz-Caro, J.3    Sastre, L.4
  • 49
    • 0037246247 scopus 로고    scopus 로고
    • On the role of Hsp27 in regulating apoptosis
    • Concannon C.G., Gorman A.M., Samali A. On the role of Hsp27 in regulating apoptosis. Apoptosis. 8:2003;61-70.
    • (2003) Apoptosis , vol.8 , pp. 61-70
    • Concannon, C.G.1    Gorman, A.M.2    Samali, A.3
  • 50
    • 0037064065 scopus 로고    scopus 로고
    • The small heat shock protein αb-crystallin negatively regulates apoptosis during myogenic differentiation by inhibiting caspase-3 activation
    • Kamradt M.C., Chen F., Sam S., Cryns V.L. The small heat shock protein αB-crystallin negatively regulates apoptosis during myogenic differentiation by inhibiting caspase-3 activation. J. Biol. Chem. 277:2002;38731-38736.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38731-38736
    • Kamradt, M.C.1    Chen, F.2    Sam, S.3    Cryns, V.L.4
  • 51
    • 0035745767 scopus 로고    scopus 로고
    • Nuclear p26, a small heat shock/α-crystallin protein, and its relationship to stress resistance in Artemia franciscana embryos
    • Willsie J.K., Clegg J.S. Nuclear p26, a small heat shock/α- crystallin protein, and its relationship to stress resistance in Artemia franciscana embryos. J. Exp. Biol. 204:2001;2339-2350.
    • (2001) J. Exp. Biol. , vol.204 , pp. 2339-2350
    • Willsie, J.K.1    Clegg, J.S.2
  • 52
    • 0001783478 scopus 로고
    • Structure and function of the crustacean larval salt gland
    • Conte F.P. Structure and function of the crustacean larval salt gland. Int. Rev. Cytol. 91:1984;45-106.
    • (1984) Int. Rev. Cytol. , vol.91 , pp. 45-106
    • Conte, F.P.1
  • 53
    • 0036745281 scopus 로고    scopus 로고
    • Expression of the Artemia trachealess gene in the salt gland and epipod
    • Mitchell B., Crews S.T. Expression of the Artemia trachealess gene in the salt gland and epipod. Evol. Dev. 4:2002;344-353.
    • (2002) Evol. Dev. , vol.4 , pp. 344-353
    • Mitchell, B.1    Crews, S.T.2
  • 54
    • 0028365340 scopus 로고
    • Extensive intracellular translocations of a major protein accompany anoxia in embryos of Artemia franciscana
    • Clegg J.S., Jackson S.A., Warner A.H. Extensive intracellular translocations of a major protein accompany anoxia in embryos of Artemia franciscana. Exp. Cell Res. 212:1994;77-83.
    • (1994) Exp. Cell Res. , vol.212 , pp. 77-83
    • Clegg, J.S.1    Jackson, S.A.2    Warner, A.H.3
  • 55
    • 0029115241 scopus 로고
    • Nuclear-cytoplasmic translocations of protein p26 during aerobic-anoxic transitions in embryos of Artemia franciscana
    • Clegg J.S., Jackson S.A., Liang P., MacRae T.H. Nuclear-cytoplasmic translocations of protein p26 during aerobic-anoxic transitions in embryos of Artemia franciscana. Exp. Cell Res. 219:1995;1-7.
    • (1995) Exp. Cell Res. , vol.219 , pp. 1-7
    • Clegg, J.S.1    Jackson, S.A.2    Liang, P.3    MacRae, T.H.4
  • 56
    • 0035698491 scopus 로고    scopus 로고
    • Small heat shock protein p26 associates with nuclear lamins and HSP70 in nuclei and nuclear matrix fractions from stressed cells
    • Willsie J.K., Clegg J.S. Small heat shock protein p26 associates with nuclear lamins and HSP70 in nuclei and nuclear matrix fractions from stressed cells. J. Cell Biochem. 84:2002;601-614.
    • (2002) J. Cell Biochem. , vol.84 , pp. 601-614
    • Willsie, J.K.1    Clegg, J.S.2
  • 57
    • 0008348285 scopus 로고
    • Arrestment of carbohydrate metabolism during anaerobic dormancy and aerobic acidosis in Artemia embryos: Determination of pH-sensitive control points
    • Carpenter J.F., Hand S.C. Arrestment of carbohydrate metabolism during anaerobic dormancy and aerobic acidosis in Artemia embryos: determination of pH-sensitive control points. J. Comp. Physiol. B. 156:1986;451-459.
    • (1986) J. Comp. Physiol. B , vol.156 , pp. 451-459
    • Carpenter, J.F.1    Hand, S.C.2
  • 58
    • 0034058749 scopus 로고    scopus 로고
    • Depression of nuclear transcription and extension of mRNA half-life under anoxia in Artemia franciscana embryos
    • van Breukelen F., Maier R., Hand S.C. Depression of nuclear transcription and extension of mRNA half-life under anoxia in Artemia franciscana embryos. J. Exp. Biol. 203:2000;1123-1130.
    • (2000) J. Exp. Biol. , vol.203 , pp. 1123-1130
    • Van Breukelen, F.1    Maier, R.2    Hand, S.C.3
  • 59
    • 0029942396 scopus 로고    scopus 로고
    • Downregulation of cellular metabolism during environmental stress: Mechanisms and implications
    • Hand S.C., Hardewig I. Downregulation of cellular metabolism during environmental stress: mechanisms and implications. Annu. Rev. Physiol. 58:1996;539-563.
    • (1996) Annu. Rev. Physiol. , vol.58 , pp. 539-563
    • Hand, S.C.1    Hardewig, I.2
  • 60
    • 0141789674 scopus 로고    scopus 로고
    • Expressed sequence tag (EST)-based characterization of gene regulation in Artemia larvae
    • Chen T., Reith M.E., Ross N.W., MacRae T.H. Expressed sequence tag (EST)-based characterization of gene regulation in Artemia larvae. Invert. Reprod. Dev. 44:2003;33-44.
    • (2003) Invert. Reprod. Dev. , vol.44 , pp. 33-44
    • Chen, T.1    Reith, M.E.2    Ross, N.W.3    MacRae, T.H.4
  • 61
    • 0037070101 scopus 로고    scopus 로고
    • Upregulation by retinoic acid of transforming growth factor-β- stimulated heat shock protein 27 induction in osteoblasts: Involvement of mitogen-activated protein kinases
    • Hatakeyama D., Kozawa O., Niwa M., Matsuno H., Ito H., Kato K.et al. Upregulation by retinoic acid of transforming growth factor-β-stimulated heat shock protein 27 induction in osteoblasts: involvement of mitogen-activated protein kinases. Biochim. Biophys. Acta. 1589:2002;15-30.
    • (2002) Biochim. Biophys. Acta , vol.1589 , pp. 15-30
    • Hatakeyama, D.1    Kozawa, O.2    Niwa, M.3    Matsuno, H.4    Ito, H.5    Kato, K.6
  • 62
    • 0036696889 scopus 로고    scopus 로고
    • Aeging is reversed, and metabolism is reset to young levels in recovering dauer larvae of C. elegans
    • Houthoofd K., Braeckman B.P., Lenaerts I., Brys K., De Vreese A., Van Eygen S.et al. Aeging is reversed, and metabolism is reset to young levels in recovering dauer larvae of C. elegans. Exp. Gerontol. 37:2002;1015-1021.
    • (2002) Exp. Gerontol. , vol.37 , pp. 1015-1021
    • Houthoofd, K.1    Braeckman, B.P.2    Lenaerts, I.3    Brys, K.4    De Vreese, A.5    Van Eygen, S.6
  • 63
    • 0037174629 scopus 로고    scopus 로고
    • Timing requirements for insulin/IGF-1 signaling in C. elegans
    • Dillin A., Crawford D.K., Kenyon C. Timing requirements for insulin/ IGF-1 signaling in C. elegans. Science. 298:2002;830-834.
    • (2002) Science , vol.298 , pp. 830-834
    • Dillin, A.1    Crawford, D.K.2    Kenyon, C.3
  • 64
    • 0034647439 scopus 로고    scopus 로고
    • Diverse Caenorhabditis elegans genes that are upregulated in dauer larvae also show elevated transcript levels in long-lived, aged, or starved adults
    • Cherkasova V., Ayyadevara S., Egilmez N., Reis R.S. Diverse Caenorhabditis elegans genes that are upregulated in dauer larvae also show elevated transcript levels in long-lived, aged, or starved adults. J. Mol. Biol. 300:2000;433-448.
    • (2000) J. Mol. Biol. , vol.300 , pp. 433-448
    • Cherkasova, V.1    Ayyadevara, S.2    Egilmez, N.3    Reis, R.S.4
  • 65
    • 0037124024 scopus 로고    scopus 로고
    • A role for p53 in maintaining and establishing the quiescence growth arrest in human cells
    • Itahana K., Dimri G.P., Hara E., Itahana Y., Zou Y., Desprez P.-Y.et al. A role for p53 in maintaining and establishing the quiescence growth arrest in human cells. J. Biol. Chem. 277:2002;18206-18214.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18206-18214
    • Itahana, K.1    Dimri, G.P.2    Hara, E.3    Itahana, Y.4    Zou, Y.5    Desprez, P.-Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.