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Volumn 294, Issue 6, 2008, Pages

Rapid cold-hardening in larvae of the Antarctic midge Belgica antarctica: Cellular cold-sensing and a role for calcium

Author keywords

Calcium signaling; Freezetolerant insects; Insect cold hardening; Rapid acclimation

Indexed keywords

CALCIUM; ETHYLENE GLYCOL 1,2 BIS(2 AMINOPHENYL) ETHER N,N,N',N' TETRAACETIC ACID; N (6 AMINOHEXYL) 5 CHLORO 1 NAPHTHALENESULFONAMIDE; 1,2 BIS(2 AMINOPHENOXY)ETHANE N,N,N',N' TETRAACETIC ACID ACETOXYMETHYL ESTER; 1,2-BIS(2-AMINOPHENOXY)ETHANE N,N,N',N'-TETRAACETIC ACID ACETOXYMETHYL ESTER; CALMODULIN; CHELATING AGENT; DRUG DERIVATIVE; EGTAZIC ACID; SULFONAMIDE;

EID: 47549103727     PISSN: 03636119     EISSN: 15221490     Source Type: Journal    
DOI: 10.1152/ajpregu.00459.2007     Document Type: Article
Times cited : (56)

References (70)
  • 1
    • 0029789334 scopus 로고    scopus 로고
    • Yeast respond to hypotonic shock with a calcium pulse
    • Batiza AF, Schulz T, Masson PH. Yeast respond to hypotonic shock with a calcium pulse. J Biol Chem 271: 23357-23362, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 23357-23362
    • Batiza, A.F.1    Schulz, T.2    Masson, P.H.3
  • 2
    • 0001905066 scopus 로고
    • Low temperature tolerance in an Antarctic insect: A relict adaptation?
    • Baust JG. Low temperature tolerance in an Antarctic insect: a relict adaptation? Cryo Lett 1: 360-371, 1980.
    • (1980) Cryo Lett , vol.1 , pp. 360-371
    • Baust, J.G.1
  • 3
    • 0031033087 scopus 로고    scopus 로고
    • Modeling seasonal changes in intracellular freeze-tolerance of fat body cells of the gall fly Eurosta solidaginis (Diptera, Tephritidae)
    • Bennett VA, Lee RE. Modeling seasonal changes in intracellular freeze-tolerance of fat body cells of the gall fly Eurosta solidaginis (Diptera, Tephritidae). J Exp Biol 200: 185-192, 1997.
    • (1997) J Exp Biol , vol.200 , pp. 185-192
    • Bennett, V.A.1    Lee, R.E.2
  • 4
    • 0030803832 scopus 로고    scopus 로고
    • Reversible protein phosphorylation regulates the activity of the slow-vacuolar ion channel
    • Bethke PC, Jones RL. Reversible protein phosphorylation regulates the activity of the slow-vacuolar ion channel. Plant J 11: 1227-1235, 1997.
    • (1997) Plant J , vol.11 , pp. 1227-1235
    • Bethke, P.C.1    Jones, R.L.2
  • 5
    • 0000111069 scopus 로고
    • Low temperature adaptations in beetles from the Sub-Antarctic island of South Georgia
    • Block W, Somme L. Low temperature adaptations in beetles from the Sub-Antarctic island of South Georgia. Polar Biol 2: 109-114, 1983.
    • (1983) Polar Biol , vol.2 , pp. 109-114
    • Block, W.1    Somme, L.2
  • 6
    • 0035746173 scopus 로고    scopus 로고
    • Characterization of transepithelial potential oscillations in the Drosophila Malpighian tubule
    • Blumenthal EM. Characterization of transepithelial potential oscillations in the Drosophila Malpighian tubule. J Exp Biol 204: 3075-3084, 2001.
    • (2001) J Exp Biol , vol.204 , pp. 3075-3084
    • Blumenthal, E.M.1
  • 7
    • 0015798850 scopus 로고
    • Unimpaired infectivity of the nematode Haemonchus contortus after freezing for 44 weeks in the presence of liquid nitrogen
    • Campbell WC, Blair LS, Egerton JR. Unimpaired infectivity of the nematode Haemonchus contortus after freezing for 44 weeks in the presence of liquid nitrogen. J Parasitol 59: 425-427, 1973.
    • (1973) J Parasitol , vol.59 , pp. 425-427
    • Campbell, W.C.1    Blair, L.S.2    Egerton, J.R.3
  • 8
    • 0000146539 scopus 로고
    • Cold-shock injury and rapid cold-hardening in the flesh fly Sarcophaga crassipalpis
    • Chen CP, Denlinger DL, Lee RE. Cold-shock injury and rapid cold-hardening in the flesh fly Sarcophaga crassipalpis. Physiol Zool 60: 297-304, 1987.
    • (1987) Physiol Zool , vol.60 , pp. 297-304
    • Chen, C.P.1    Denlinger, D.L.2    Lee, R.E.3
  • 10
    • 0001503389 scopus 로고
    • Fluid secretion by single isolated Malpighian tubules of the house cricket, Acheta domesticus, and their response to diuretic hormone
    • Coast GM, Krasnoff SB. Fluid secretion by single isolated Malpighian tubules of the house cricket, Acheta domesticus, and their response to diuretic hormone. Physiol Entomol 13: 381-391, 1988.
    • (1988) Physiol Entomol , vol.13 , pp. 381-391
    • Coast, G.M.1    Krasnoff, S.B.2
  • 11
    • 0031432578 scopus 로고    scopus 로고
    • How are the life history strategies of Antarctic terrestrial invertebrates influenced by extreme environmental conditions?
    • Convey P. How are the life history strategies of Antarctic terrestrial invertebrates influenced by extreme environmental conditions? J Therm Biol 22: 429-440, 1997.
    • (1997) J Therm Biol , vol.22 , pp. 429-440
    • Convey, P.1
  • 12
    • 0037033784 scopus 로고    scopus 로고
    • 2+ release in yeast is triggered by hypertonic shock and mediated by a TRP channel homologue
    • 2+ release in yeast is triggered by hypertonic shock and mediated by a TRP channel homologue. J Cell Biol 156: 29-34, 2002.
    • (2002) J Cell Biol , vol.156 , pp. 29-34
    • Denis, V.1    Cyert, M.S.2
  • 13
    • 0029768088 scopus 로고    scopus 로고
    • Regulation of mitogen-activated protein kinases by a calcium/calmodulin- dependent protein kinase cascade
    • Enslen H, Tokumitsu H, Stork PJS, Davis RJ, Soderling TR. Regulation of mitogen-activated protein kinases by a calcium/calmodulin- dependent protein kinase cascade. Proc Natl Acad Sci USA 93: 10803-10808, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10803-10808
    • Enslen, H.1    Tokumitsu, H.2    Stork, P.J.S.3    Davis, R.J.4    Soderling, T.R.5
  • 14
    • 0036182380 scopus 로고    scopus 로고
    • Calcium and oxidative stress: From cell signaling to cell death
    • Ermak G, Davies KJA. Calcium and oxidative stress: from cell signaling to cell death. Mol Immunol 38: 713-721, 2001.
    • (2001) Mol Immunol , vol.38 , pp. 713-721
    • Ermak, G.1    Davies, K.J.A.2
  • 15
    • 35648946797 scopus 로고    scopus 로고
    • p38 MAP kinase is a likely component of the signal transduction pathway triggering rapid cold hardening in the flesh fly, Sarcophaga crassipalpis
    • Fujiwara Y, Denlinger DL. p38 MAP kinase is a likely component of the signal transduction pathway triggering rapid cold hardening in the flesh fly, Sarcophaga crassipalpis. J Exp Biol 210: 3295-3300, 2007.
    • (2007) J Exp Biol , vol.210 , pp. 3295-3300
    • Fujiwara, Y.1    Denlinger, D.L.2
  • 19
    • 0022590628 scopus 로고
    • Defense strategies against hypoxia and hypothermia
    • Hochachka PW. Defense strategies against hypoxia and hypothermia. Science 231: 234-241, 1986.
    • (1986) Science , vol.231 , pp. 234-241
    • Hochachka, P.W.1
  • 20
    • 0030032040 scopus 로고    scopus 로고
    • Calcium binding and conformational response in EF-hand proteins
    • Ikura M. Calcium binding and conformational response in EF-hand proteins. Trends Biochem Sci 21: 14-17, 1996.
    • (1996) Trends Biochem Sci , vol.21 , pp. 14-17
    • Ikura, M.1
  • 21
    • 0035996798 scopus 로고    scopus 로고
    • The role of calcium-binding proteins in the control of transcription: Structure to function
    • Ikura M, Osawa M, Ames JB. The role of calcium-binding proteins in the control of transcription: structure to function. Bioessays 24: 625-636, 2002.
    • (2002) Bioessays , vol.24 , pp. 625-636
    • Ikura, M.1    Osawa, M.2    Ames, J.B.3
  • 22
    • 0029787520 scopus 로고    scopus 로고
    • Oxidative stress and antioxidants in overwintering larvae of cold-hardy goldenrod gall insects
    • Joanisse DR, Storey KB. Oxidative stress and antioxidants in overwintering larvae of cold-hardy goldenrod gall insects. J Exp Biol 199: 1483-1491, 1996.
    • (1996) J Exp Biol , vol.199 , pp. 1483-1491
    • Joanisse, D.R.1    Storey, K.B.2
  • 23
    • 0016054295 scopus 로고
    • Survival of Nippostrongylus brasiliensis larvae after freezing over liquid nitrogen
    • Kelly JD, Campbell WC. Survival of Nippostrongylus brasiliensis larvae after freezing over liquid nitrogen. Int J Parasitol 4: 173-176, 1974.
    • (1974) Int J Parasitol , vol.4 , pp. 173-176
    • Kelly, J.D.1    Campbell, W.C.2
  • 24
    • 0032769860 scopus 로고    scopus 로고
    • Induction of rapid cold hardening by cooling at ecologically relevant rates in Drosophila melanogaster
    • Kelty JD, Lee RE. Induction of rapid cold hardening by cooling at ecologically relevant rates in Drosophila melanogaster. J Insect Physiol 45: 719-726, 1999.
    • (1999) J Insect Physiol , vol.45 , pp. 719-726
    • Kelty, J.D.1    Lee, R.E.2
  • 25
    • 0035745506 scopus 로고    scopus 로고
    • Rapid cold-hardening of Drosophila melanogaster (Diptera: Drosophilidae) during ecologically based thermoperiodic cycles
    • Kelty JD, Lee RE. Rapid cold-hardening of Drosophila melanogaster (Diptera: Drosophilidae) during ecologically based thermoperiodic cycles. J Exp Biol 204: 1659-1666, 2001.
    • (2001) J Exp Biol , vol.204 , pp. 1659-1666
    • Kelty, J.D.1    Lee, R.E.2
  • 27
    • 0030096580 scopus 로고    scopus 로고
    • Cold calcium signaling in Arabidopsis involves two cellular pools and a change in calcium signature after acclimation
    • Knight H, Trewavas AJ, Knight MR. Cold calcium signaling in Arabidopsis involves two cellular pools and a change in calcium signature after acclimation. Plant Cell 8: 489-503, 1996.
    • (1996) Plant Cell , vol.8 , pp. 489-503
    • Knight, H.1    Trewavas, A.J.2    Knight, M.R.3
  • 28
    • 2342584216 scopus 로고    scopus 로고
    • On the nature of pre-freeze mortality in insects: Water balance, ion homeostasis and energy charge in the adults of Pyrrhocoris apterus
    • Kostal V, Vambera J, Bastl J. On the nature of pre-freeze mortality in insects: water balance, ion homeostasis and energy charge in the adults of Pyrrhocoris apterus. J Exp Biol 207: 1509-1521, 2004.
    • (2004) J Exp Biol , vol.207 , pp. 1509-1521
    • Kostal, V.1    Vambera, J.2    Bastl, J.3
  • 29
    • 0023490966 scopus 로고
    • A rapid cold-hardening process in insects
    • Lee RE, Chen CP, Denlinger DL. A rapid cold-hardening process in insects. Science 238: 1415-1417, 1987.
    • (1987) Science , vol.238 , pp. 1415-1417
    • Lee, R.E.1    Chen, C.P.2    Denlinger, D.L.3
  • 30
    • 33749055993 scopus 로고    scopus 로고
    • Rapid cold-hardening increases membrane fluidity and cold tolerance of insect cells
    • Lee RE, Damodaran K, Yi SX, Lorigan GA. Rapid cold-hardening increases membrane fluidity and cold tolerance of insect cells. Cryobiology 52: 459-463, 2006.
    • (2006) Cryobiology , vol.52 , pp. 459-463
    • Lee, R.E.1    Damodaran, K.2    Yi, S.X.3    Lorigan, G.A.4
  • 32
    • 0000006508 scopus 로고
    • Survival of intracellular freezing, lipid coalescence and osmotic fragility in fat body cells of the freeze-tolerant gall fly Eurosta solidaginis
    • Lee RE, Mcgrath JJ, Morason RT, Taddeo RM. Survival of intracellular freezing, lipid coalescence and osmotic fragility in fat body cells of the freeze-tolerant gall fly Eurosta solidaginis. J Insect Physiol 39: 445-450, 1993.
    • (1993) J Insect Physiol , vol.39 , pp. 445-450
    • Lee, R.E.1    Mcgrath, J.J.2    Morason, R.T.3    Taddeo, R.M.4
  • 33
    • 0032030547 scopus 로고    scopus 로고
    • +-ATPase from beet root is inhibited by a calcium-dependent phosphorylation
    • +-ATPase from beet root is inhibited by a calcium-dependent phosphorylation. Planta 204: 352-359, 1998.
    • (1998) Planta , vol.204 , pp. 352-359
    • Lino, B.1    Baizabal-Aguirre, V.M.2    de la Vara, L.E.G.3
  • 34
    • 28444441250 scopus 로고    scopus 로고
    • Cold, salinity and drought stresses: An overview
    • Mahajan S, Tuteja N. Cold, salinity and drought stresses: an overview. Arch Biochem Biophys 444: 139-158, 2005.
    • (2005) Arch Biochem Biophys , vol.444 , pp. 139-158
    • Mahajan, S.1    Tuteja, N.2
  • 35
    • 33748440409 scopus 로고    scopus 로고
    • Molecular modalities of insect cold survival: Current understanding and future trends
    • Michaud MR, Denlinger DL. Molecular modalities of insect cold survival: current understanding and future trends. Intl Congr Ser 1275: 32-46, 2004.
    • (2004) Intl Congr Ser , vol.1275 , pp. 32-46
    • Michaud, M.R.1    Denlinger, D.L.2
  • 36
    • 33750318810 scopus 로고    scopus 로고
    • Oleic acid is elevated in cell membranes during rapid cold-hardening and pupal diapause in the flesh fly, Sarcophaga crassipalpis
    • Michaud MR, Denlinger DL. Oleic acid is elevated in cell membranes during rapid cold-hardening and pupal diapause in the flesh fly, Sarcophaga crassipalpis. J Insect Physiol 52: 1073-1082, 2006.
    • (2006) J Insect Physiol , vol.52 , pp. 1073-1082
    • Michaud, M.R.1    Denlinger, D.L.2
  • 37
    • 0035102762 scopus 로고    scopus 로고
    • Cold tolerance and proline metabolic gene expression in Drosophila melanogaster
    • Misener SR, Chen CP, Walker VK. Cold tolerance and proline metabolic gene expression in Drosophila melanogaster. J Insect Physiol 47: 393-400, 2001.
    • (2001) J Insect Physiol , vol.47 , pp. 393-400
    • Misener, S.R.1    Chen, C.P.2    Walker, V.K.3
  • 38
    • 0029257293 scopus 로고
    • Low-temperature signal transduction: Induction of cold acclimation-specific genes of alfalfa by calcium at 25 degrees C
    • Monroy AF, Dhindsa RS. Low-temperature signal transduction: induction of cold acclimation-specific genes of alfalfa by calcium at 25 degrees C. Plant Cell 7: 321-331, 1995.
    • (1995) Plant Cell , vol.7 , pp. 321-331
    • Monroy, A.F.1    Dhindsa, R.S.2
  • 39
    • 12044259918 scopus 로고
    • Cold-induced changes in freezing tolerance, protein phosphorylation, and gene expression (evidence for a role of calcium)
    • Monroy AF, Sarhan F, Dhindsa RS. Cold-induced changes in freezing tolerance, protein phosphorylation, and gene expression (evidence for a role of calcium). Plant Physiol 102: 1227-1235, 1993.
    • (1993) Plant Physiol , vol.102 , pp. 1227-1235
    • Monroy, A.F.1    Sarhan, F.2    Dhindsa, R.S.3
  • 40
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 65: 55-63, 1983.
    • (1983) J Immunol Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 41
    • 0023916588 scopus 로고
    • Cryopreservation of first-stage and infective third-stage larvae of Strongyloides stercoralis
    • Nolan TJ, Aikens LM, Schad GA. Cryopreservation of first-stage and infective third-stage larvae of Strongyloides stercoralis. J Parasitol 74: 387-391, 1988.
    • (1988) J Parasitol , vol.74 , pp. 387-391
    • Nolan, T.J.1    Aikens, L.M.2    Schad, G.A.3
  • 43
    • 0033801589 scopus 로고    scopus 로고
    • Early steps in cold sensing by plant cells: The role of actin cytoskeleton and membrane fluidity
    • Orvar BL, Sangwan V, Omann F, Dhindsa RS. Early steps in cold sensing by plant cells: the role of actin cytoskeleton and membrane fluidity. Plant J 23: 785-794, 2000.
    • (2000) Plant J , vol.23 , pp. 785-794
    • Orvar, B.L.1    Sangwan, V.2    Omann, F.3    Dhindsa, R.S.4
  • 45
    • 27644459878 scopus 로고    scopus 로고
    • Changes in membrane lipid composition following rapid cold hardening in Drosophila melanogaster
    • Overgaard J, Sorensen JG, Petersen SO, Loeschcke V, Holmstrup M. Changes in membrane lipid composition following rapid cold hardening in Drosophila melanogaster. J Insect Physiol 51: 1173-1182, 2005.
    • (2005) J Insect Physiol , vol.51 , pp. 1173-1182
    • Overgaard, J.1    Sorensen, J.G.2    Petersen, S.O.3    Loeschcke, V.4    Holmstrup, M.5
  • 46
    • 29144501474 scopus 로고    scopus 로고
    • Insect freeze tolerance: Roles of protein phosphatases and protein kinase A
    • Pfister TD, Storey KB. Insect freeze tolerance: roles of protein phosphatases and protein kinase A. Insect Biochem Mol Biol 36: 18-24, 2006.
    • (2006) Insect Biochem Mol Biol , vol.36 , pp. 18-24
    • Pfister, T.D.1    Storey, K.B.2
  • 47
    • 43049090897 scopus 로고    scopus 로고
    • Aquaporins play a role in desiccation and freeze tolerance in larvae of the goldenrod gall fly, Eurosta solidaginis
    • Philip BN, Yi SX, Elnitsky MA, Lee RE. Aquaporins play a role in desiccation and freeze tolerance in larvae of the goldenrod gall fly, Eurosta solidaginis. J Exp Biol 211: 1114-1119, 2008.
    • (2008) J Exp Biol , vol.211 , pp. 1114-1119
    • Philip, B.N.1    Yi, S.X.2    Elnitsky, M.A.3    Lee, R.E.4
  • 49
    • 33845899087 scopus 로고    scopus 로고
    • Stress-induced activation of the AMP-activated protein kinase in the freeze-tolerant frog Rana sylvatica
    • Rider MH, Hussain N, Horman S, Dilworth SM, Storey KB. Stress-induced activation of the AMP-activated protein kinase in the freeze-tolerant frog Rana sylvatica. Cryobiology 53: 297-309, 2006.
    • (2006) Cryobiology , vol.53 , pp. 297-309
    • Rider, M.H.1    Hussain, N.2    Horman, S.3    Dilworth, S.M.4    Storey, K.B.5
  • 50
    • 0034521421 scopus 로고    scopus 로고
    • Thermotolerance and rapid cold-hardening ameliorate the negative effects of brief exposures to high or low temperatures on fecundity in the flesh fly, Sarcophaga crassipalpis
    • Rinehart JP, Yocum GD, Denlinger DL. Thermotolerance and rapid cold-hardening ameliorate the negative effects of brief exposures to high or low temperatures on fecundity in the flesh fly, Sarcophaga crassipalpis. Physiol Entomol 25: 330-336, 2000.
    • (2000) Physiol Entomol , vol.25 , pp. 330-336
    • Rinehart, J.P.1    Yocum, G.D.2    Denlinger, D.L.3
  • 52
    • 3042553383 scopus 로고    scopus 로고
    • The preservation of reproductive behaviors during modest cooling: Rapid cold-hardening fine-tunes organismal response
    • Shreve SM, Kelty JD, Lee RE. The preservation of reproductive behaviors during modest cooling: rapid cold-hardening fine-tunes organismal response. J Exp Biol 207: 1797-1802, 2004.
    • (2004) J Exp Biol , vol.207 , pp. 1797-1802
    • Shreve, S.M.1    Kelty, J.D.2    Lee, R.E.3
  • 54
    • 0037280893 scopus 로고    scopus 로고
    • Rapid responses to high temperature and desiccation but not to low temperature in the freeze tolerant sub-Antarctic caterpillar Pringleophaga marioni (Lepidoptera, Tineidae)
    • Sinclair BJ, Chown SL. Rapid responses to high temperature and desiccation but not to low temperature in the freeze tolerant sub-Antarctic caterpillar Pringleophaga marioni (Lepidoptera, Tineidae). J Insect Physiol 49: 45-52, 2003.
    • (2003) J Insect Physiol , vol.49 , pp. 45-52
    • Sinclair, B.J.1    Chown, S.L.2
  • 55
    • 0242350252 scopus 로고    scopus 로고
    • Diurnal variation in supercooling points of three species of Collembola from Cape Hallett, Antarctica
    • Sinclair BJ, Klok CJ, Scott MB, Terblanche JS, Chown SL. Diurnal variation in supercooling points of three species of Collembola from Cape Hallett, Antarctica. J Insect Physiol 49: 1049-1061, 2003.
    • (2003) J Insect Physiol , vol.49 , pp. 1049-1061
    • Sinclair, B.J.1    Klok, C.J.2    Scott, M.B.3    Terblanche, J.S.4    Chown, S.L.5
  • 56
    • 0001281780 scopus 로고    scopus 로고
    • Anhydrobiosis and cold tolerance in tardigrades
    • Somme L. Anhydrobiosis and cold tolerance in tardigrades. Eur J Entomol 93: 349-357, 1996.
    • (1996) Eur J Entomol , vol.93 , pp. 349-357
    • Somme, L.1
  • 57
    • 0001155359 scopus 로고
    • Role of the plasma membrane in freezing injury and cold acclimation
    • Steponkus PL. Role of the plasma membrane in freezing injury and cold acclimation. Annu Rev Plant Physiol 35: 543-584, 1984.
    • (1984) Annu Rev Plant Physiol , vol.35 , pp. 543-584
    • Steponkus, P.L.1
  • 58
    • 0035951789 scopus 로고    scopus 로고
    • 2+-dependent cell signaling through calmodulin-activated protein phosphatase and protein kinases
    • 2+-dependent cell signaling through calmodulin-activated protein phosphatase and protein kinases. J Biol Chem 276: 2311-2312, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 2311-2312
    • Stull, J.T.1
  • 59
    • 0017528802 scopus 로고
    • Cryopreservation of the infective larvae of the common nematodes of ruminants
    • Van Wyk JA, Gerber HM, Van Aardt WP. Cryopreservation of the infective larvae of the common nematodes of ruminants. Onderstepoort J Vet Res 44: 173-194, 1977.
    • (1977) Onderstepoort J Vet Res , vol.44 , pp. 173-194
    • Van Wyk, J.A.1    Gerber, H.M.2    Van Aardt, W.P.3
  • 60
    • 0036749175 scopus 로고    scopus 로고
    • Mechanism allowing an insect to survive complete dehydration and extreme temperatures
    • Watanabe M, Kikawada T, Minagawa N, Yukuhiro F, Okuda T. Mechanism allowing an insect to survive complete dehydration and extreme temperatures. J Exp Biol 205: 2799-2802, 2002.
    • (2002) J Exp Biol , vol.205 , pp. 2799-2802
    • Watanabe, M.1    Kikawada, T.2    Minagawa, N.3    Yukuhiro, F.4    Okuda, T.5
  • 61
    • 0034119594 scopus 로고    scopus 로고
    • Survival of Heleomyza borealis (Diptera, Heleomyzidae) larvae down to -60° C
    • Worland MR, Block W, Grubor-Lajsic G. Survival of Heleomyza borealis (Diptera, Heleomyzidae) larvae down to -60° C. Physiol Entomol 25: 1-5, 2000.
    • (2000) Physiol Entomol , vol.25 , pp. 1-5
    • Worland, M.R.1    Block, W.2    Grubor-Lajsic, G.3
  • 62
    • 0034864667 scopus 로고    scopus 로고
    • Rapid cold hardening in Antarctic microarthropods
    • Worland MR, Convey P. Rapid cold hardening in Antarctic microarthropods. Funct Ecol 15: 515-524, 2001.
    • (2001) Funct Ecol , vol.15 , pp. 515-524
    • Worland, M.R.1    Convey, P.2
  • 63
    • 0027071310 scopus 로고
    • Survival of sub-zero temperatures by two South Georgian beetles (Coleoptera, Perimylopidae)
    • Worland R, Block W, Rothery P. Survival of sub-zero temperatures by two South Georgian beetles (Coleoptera, Perimylopidae). Polar Biol 11: 607-613, 1992.
    • (1992) Polar Biol , vol.11 , pp. 607-613
    • Worland, R.1    Block, W.2    Rothery, P.3
  • 65
    • 0032506514 scopus 로고    scopus 로고
    • Calcium promotes cell survival through CaM-K kinase activation of the protein kinase-B pathway
    • Yano S, Tokumitsu H, Sodeling TR. Calcium promotes cell survival through CaM-K kinase activation of the protein kinase-B pathway. Nature 396: 584-587, 1998.
    • (1998) Nature , vol.396 , pp. 584-587
    • Yano, S.1    Tokumitsu, H.2    Sodeling, T.R.3
  • 66
    • 0242350281 scopus 로고    scopus 로고
    • Detecting freeze injury and seasonal cold-hardening of cells and tissues in the gall fly larvae, Eurosta solidaginis (Diptera: Tephritidae) using fluorescent vital dyes
    • Yi SX, Lee RE. Detecting freeze injury and seasonal cold-hardening of cells and tissues in the gall fly larvae, Eurosta solidaginis (Diptera: Tephritidae) using fluorescent vital dyes. J Insect Physiol 49: 999-1004, 2003.
    • (2003) J Insect Physiol , vol.49 , pp. 999-1004
    • Yi, S.X.1    Lee, R.E.2
  • 67
    • 11144245310 scopus 로고    scopus 로고
    • In vivo and in vitro rapid cold-hardening protects cells from cold-shock injury in the flesh fly
    • Yi SX, Lee RE. In vivo and in vitro rapid cold-hardening protects cells from cold-shock injury in the flesh fly. J Comp Physiol B 174: 611-615, 2004.
    • (2004) J Comp Physiol B , vol.174 , pp. 611-615
    • Yi, S.X.1    Lee, R.E.2
  • 68
    • 34249993205 scopus 로고    scopus 로고
    • Rapid cold-hardening protects Drosophila melanogaster from cold-induced apoptosis
    • Yi SX, Moore CW, Lee RE. Rapid cold-hardening protects Drosophila melanogaster from cold-induced apoptosis. Apoptosis 12: 1183-1193, 2007.
    • (2007) Apoptosis , vol.12 , pp. 1183-1193
    • Yi, S.X.1    Moore, C.W.2    Lee, R.E.3
  • 69
    • 38249036413 scopus 로고
    • The in vitro biosynthesis and secretion of glycerol by larval fat bodies of chilled Ostrinia nubialis
    • Yi SX, Yin CM, Nordin JH. The in vitro biosynthesis and secretion of glycerol by larval fat bodies of chilled Ostrinia nubialis. J Insect Physiol 33: 523-528, 1987.
    • (1987) J Insect Physiol , vol.33 , pp. 523-528
    • Yi, S.X.1    Yin, C.M.2    Nordin, J.H.3
  • 70
    • 0036999615 scopus 로고    scopus 로고
    • Salt and drought stress signal transduction in plants
    • Zhu JK. Salt and drought stress signal transduction in plants. Annu Rev Plant Biol 53: 247-273, 2002.
    • (2002) Annu Rev Plant Biol , vol.53 , pp. 247-273
    • Zhu, J.K.1


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