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Volumn 27, Issue 4, 2009, Pages 348-352

Molecular mechanisms of tolerance in tardigrades: New perspectives for preservation and stabilization of biological material

Author keywords

Anhydrobiosis; Biostabilization; Cryobanking; Cryopreservation; Cryoprotectant; Cryptobiosis

Indexed keywords

ANHYDROBIOSIS; BIOSTABILIZATION; CRYOBANKING; CRYOPRESERVATION; CRYOPROTECTANT; CRYPTOBIOSIS;

EID: 67349124386     PISSN: 07349750     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biotechadv.2009.01.011     Document Type: Review
Times cited : (56)

References (100)
  • 1
    • 30744473948 scopus 로고    scopus 로고
    • The limits and frontiers of desiccation-tolerant life
    • Alpert P. The limits and frontiers of desiccation-tolerant life. Integr Comp Biol 45 (2005) 685-695
    • (2005) Integr Comp Biol , vol.45 , pp. 685-695
    • Alpert, P.1
  • 2
    • 33744792923 scopus 로고    scopus 로고
    • Constraints of tolerance: why are desiccation-tolerant organisms so small or rare?
    • Alpert P. Constraints of tolerance: why are desiccation-tolerant organisms so small or rare?. J Exp Biol 209 (2006) 1575-1584
    • (2006) J Exp Biol , vol.209 , pp. 1575-1584
    • Alpert, P.1
  • 3
    • 0001179757 scopus 로고
    • Die Anabiose der Tardigraden
    • Baumann H. Die Anabiose der Tardigraden. Zool Jahrb (1922) 501-556
    • (1922) Zool Jahrb , pp. 501-556
    • Baumann, H.1
  • 5
    • 0027140360 scopus 로고
    • Molecular responses to water deficit
    • Bray E.A. Molecular responses to water deficit. Plant Physiol 103 (1993) 1035-1040
    • (1993) Plant Physiol , vol.103 , pp. 1035-1040
    • Bray, E.A.1
  • 6
    • 0000881487 scopus 로고
    • A limnological study of certain fresh-water polyzoa with special reference to their statoblasts
    • Brown C.J.D. A limnological study of certain fresh-water polyzoa with special reference to their statoblasts. Trans Am Microsc Soc 52 (1933) 271-316
    • (1933) Trans Am Microsc Soc , vol.52 , pp. 271-316
    • Brown, C.J.D.1
  • 7
    • 0037034885 scopus 로고    scopus 로고
    • Anhydrobiosis - plant desiccation gene found in a nematode
    • Browne J., Tunnacliffe A., and Burnell A. Anhydrobiosis - plant desiccation gene found in a nematode. Nature 416 (2002) 38
    • (2002) Nature , vol.416 , pp. 38
    • Browne, J.1    Tunnacliffe, A.2    Burnell, A.3
  • 8
    • 4143088129 scopus 로고    scopus 로고
    • Dehydration-specific induction of hydrophilic protein genes in the anhydrobiotic nematode aphelenchus avenae
    • Browne J.A., Dolan K.M., Tyson T., Goyal K., Tunnacliffe A., and Burnell A.M. Dehydration-specific induction of hydrophilic protein genes in the anhydrobiotic nematode aphelenchus avenae. Eukaryot Cell 3 (2004) 966-975
    • (2004) Eukaryot Cell , vol.3 , pp. 966-975
    • Browne, J.A.1    Dolan, K.M.2    Tyson, T.3    Goyal, K.4    Tunnacliffe, A.5    Burnell, A.M.6
  • 11
    • 0037219976 scopus 로고    scopus 로고
    • Molecular characterization of artemin and ferritin from Artemia franciscana
    • Chen T., Amons R., Clegg J.S., Warner A.H., and 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
  • 12
    • 33846821809 scopus 로고    scopus 로고
    • Functional characterization of artemin, a ferritin homolog synthesized in Artemia embryos during encystment and diapause
    • Chen T., Villeneuve T.S., Garant K.A., Amons R., and MacRae T.H. Functional characterization of artemin, a ferritin homolog synthesized in Artemia embryos during encystment and diapause. FEBS J 274 (2007) 1093-1101
    • (2007) FEBS J , vol.274 , pp. 1093-1101
    • Chen, T.1    Villeneuve, T.S.2    Garant, K.A.3    Amons, R.4    MacRae, T.H.5
  • 13
    • 39649088018 scopus 로고    scopus 로고
    • Surviving extreme polar winters by desiccation: clues from Arctic springtail (Onychiurus arcticus) EST libraries
    • Clark M.S., Thorne M.A., Purac J., Grubor-Lajsic G., Kube M., Reinhardt R., et al. Surviving extreme polar winters by desiccation: clues from Arctic springtail (Onychiurus arcticus) EST libraries. BMC Genomics 8 (2007) 475
    • (2007) BMC Genomics , vol.8 , pp. 475
    • Clark, M.S.1    Thorne, M.A.2    Purac, J.3    Grubor-Lajsic, G.4    Kube, M.5    Reinhardt, R.6
  • 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
    • 0035060319 scopus 로고    scopus 로고
    • Cryptobiosis - a peculiar state of biological organization
    • Clegg J.S. Cryptobiosis - a peculiar state of biological organization. Comp Biochem Physiol Part B Biochem Mol Biol 128 (2001) 613-624
    • (2001) Comp Biochem Physiol Part B Biochem Mol Biol , vol.128 , pp. 613-624
    • Clegg, J.S.1
  • 16
    • 0026605621 scopus 로고    scopus 로고
    • Aerobic heat shock activates trehalose synthesis in embryos of artemia franciscana
    • Clegg J.S., and Jackson S.A. Aerobic heat shock activates trehalose synthesis in embryos of artemia franciscana. FEBS 303 (2004) 45-47
    • (2004) FEBS , vol.303 , pp. 45-47
    • Clegg, J.S.1    Jackson, S.A.2
  • 17
    • 22844453994 scopus 로고    scopus 로고
    • Adaptive significance of a small heat shock/alpha-crystallin protein (p26) in encysted embryos of the brine shrimp, Artemia franciscana
    • Clegg J.S., Willsie J.K., and Jackson S.A. Adaptive significance of a small heat shock/alpha-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
  • 18
    • 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., and Popov V.I. Long-term anoxia in encysted embryos of the crustacean, artemia franciscana: viability, ultrastructure, and stress proteins. Cell Tissue Res 301 (2000) 433-446
    • (2000) Cell Tissue Res , vol.301 , pp. 433-446
    • Clegg, J.S.1    Jackson, S.A.2    Popov, V.I.3
  • 20
    • 0031040618 scopus 로고    scopus 로고
    • Water deficit rapidly stimulates the activity of a protein kinase in the elongation zone of the maize primary root
    • Conley T.R., Sharp R.E., and Walker J.C. Water deficit rapidly stimulates the activity of a protein kinase in the elongation zone of the maize primary root. Plant Physiol 113 (1997) 219-226
    • (1997) Plant Physiol , vol.113 , pp. 219-226
    • Conley, T.R.1    Sharp, R.E.2    Walker, J.C.3
  • 21
    • 0345094935 scopus 로고    scopus 로고
    • Eukaryotic chaperonins: lubricating the folding of WD-repeat proteins
    • Craig E.A. Eukaryotic chaperonins: lubricating the folding of WD-repeat proteins. Curr Biol 13 (2003) R904-905
    • (2003) Curr Biol , vol.13
    • Craig, E.A.1
  • 22
    • 84934441777 scopus 로고    scopus 로고
    • Springer-Verlag, Berlin
    • Crowe J.H. Trehalose as a "chemical chaperone": fact and fantasy. Adv Exp Med Biolf Csermely and L. Vigh vol. 16 (2007), Springer-Verlag, Berlin 143-158
    • (2007) Adv Exp Med Biolf Csermely and L. Vigh , vol.16 , pp. 143-158
    • Crowe, J.H.1
  • 23
    • 0023653939 scopus 로고
    • Stabilization of dry phospholipid-bilayers and proteins by sugars
    • Crowe J.H., Crowe L.M., Carpenter J.F., and Wistrom C.A. Stabilization of dry phospholipid-bilayers and proteins by sugars. Biochem J 242 (1987) 1-10
    • (1987) Biochem J , vol.242 , pp. 1-10
    • Crowe, J.H.1    Crowe, L.M.2    Carpenter, J.F.3    Wistrom, C.A.4
  • 26
    • 0036182386 scopus 로고    scopus 로고
    • Lessons from nature: the role of sugars in anhydrobiosis
    • Crowe L.M. Lessons from nature: the role of sugars in anhydrobiosis. Comp Biochem Physiol Part A Mol Integr Physiol 131 (2002) 505-513
    • (2002) Comp Biochem Physiol Part A Mol Integr Physiol , vol.131 , pp. 505-513
    • Crowe, L.M.1
  • 27
    • 0029820371 scopus 로고    scopus 로고
    • Is trehalose special for preserving dry biomaterials?
    • Crowe L.M., Reid D.S., and Crowe J.H. Is trehalose special for preserving dry biomaterials?. Biophys J 71 (1996) 2087-2093
    • (1996) Biophys J , vol.71 , pp. 2087-2093
    • Crowe, L.M.1    Reid, D.S.2    Crowe, J.H.3
  • 29
    • 0027564435 scopus 로고
    • A repeating 11-mer amino acid motif and plant desiccation
    • Dure III L. A repeating 11-mer amino acid motif and plant desiccation. Plant J 3 (1993) 363-369
    • (1993) Plant J , vol.3 , pp. 363-369
    • Dure III, L.1
  • 31
    • 0035022351 scopus 로고    scopus 로고
    • Occurrence of a repeating 11-mer amino acid sequence motif in diverse organisms
    • Dure III L. Occurrence of a repeating 11-mer amino acid sequence motif in diverse organisms. Protein Pept Lett 8 (2001) 115-122
    • (2001) Protein Pept Lett , vol.8 , pp. 115-122
    • Dure III, L.1
  • 32
    • 0033951109 scopus 로고    scopus 로고
    • Intracellular trehalose improves the survival of cryopreserved mammalian cells
    • Eroglu A., Russo M.J., Bieganski R., Fowler A., Cheley S., Bayley H., et al. Intracellular trehalose improves the survival of cryopreserved mammalian cells. Nat Biotechnol 18 (2000) 163-167
    • (2000) Nat Biotechnol , vol.18 , pp. 163-167
    • Eroglu, A.1    Russo, M.J.2    Bieganski, R.3    Fowler, A.4    Cheley, S.5    Bayley, H.6
  • 33
    • 0036156006 scopus 로고    scopus 로고
    • Beneficial effect of microinjected trehalose on the cryosurvival of human oocytes
    • Eroglu A., Toner M., and Toth T.L. Beneficial effect of microinjected trehalose on the cryosurvival of human oocytes. Fertil Steril 77 (2002) 152-158
    • (2002) Fertil Steril , vol.77 , pp. 152-158
    • Eroglu, A.1    Toner, M.2    Toth, T.L.3
  • 34
    • 0013550233 scopus 로고
    • Survival of the gemmules of Anheteromeyenia ryderi (Potts) following aerial exposure during winter in New-England
    • Fell P.E., and Bazer L.J. Survival of the gemmules of Anheteromeyenia ryderi (Potts) following aerial exposure during winter in New-England. Hydrobiologia 190 (1990) 241-246
    • (1990) Hydrobiologia , vol.190 , pp. 241-246
    • Fell, P.E.1    Bazer, L.J.2
  • 35
    • 6344219787 scopus 로고    scopus 로고
    • Influence of gut morphology on passive transport of freshwater bryozoans by waterfowl in Donana (southwestern Spain)
    • Figuerola J., Green A.J., Black K., and Okamura B. Influence of gut morphology on passive transport of freshwater bryozoans by waterfowl in Donana (southwestern Spain). Can J Zool 82 (2004) 835-840
    • (2004) Can J Zool , vol.82 , pp. 835-840
    • Figuerola, J.1    Green, A.J.2    Black, K.3    Okamura, B.4
  • 38
    • 33646591460 scopus 로고    scopus 로고
    • Tardigrade taxonomy: an updated check list of the taxa and a list of characters for their identification
    • Guidetti R., and Bertolani R. Tardigrade taxonomy: an updated check list of the taxa and a list of characters for their identification. Zootaxa 845 (2005) 1-46
    • (2005) Zootaxa , vol.845 , pp. 1-46
    • Guidetti, R.1    Bertolani, R.2
  • 39
    • 0033950708 scopus 로고    scopus 로고
    • Trehalose expression confers desiccation tolerance on human cells
    • Guo N., Puhlev I., Brown D.R., Mansbridge J., and Levine F. Trehalose expression confers desiccation tolerance on human cells. Nat Biotechnol 18 (2000) 168-171
    • (2000) Nat Biotechnol , vol.18 , pp. 168-171
    • Guo, N.1    Puhlev, I.2    Brown, D.R.3    Mansbridge, J.4    Levine, F.5
  • 40
    • 33847367791 scopus 로고    scopus 로고
    • Life without water: expression of plant LEA genes by an anhydrobiotic arthropod
    • Hand S.C., Jones D., Menze M.A., and Witt T.L. Life without water: expression of plant LEA genes by an anhydrobiotic arthropod. J Exp Zool 307A (2007) 62-66
    • (2007) J Exp Zool , vol.307 A , pp. 62-66
    • Hand, S.C.1    Jones, D.2    Menze, M.A.3    Witt, T.L.4
  • 42
    • 47349133713 scopus 로고    scopus 로고
    • Anhydrobiosis in tardigrades and its effects on longevity traits
    • Hengherr S., Brümmer F., and Schill R.O. Anhydrobiosis in tardigrades and its effects on longevity traits. J Zool (Lond) 275 (2008) 216-220
    • (2008) J Zool (Lond) , vol.275 , pp. 216-220
    • Hengherr, S.1    Brümmer, F.2    Schill, R.O.3
  • 43
    • 37849009975 scopus 로고    scopus 로고
    • Trehalose and anhydrobiosis in tardigrades - evidence for divergence in responses to dehydration
    • Hengherr S., Heyer A.G., Köhler H.R., and Schill R.O. Trehalose and anhydrobiosis in tardigrades - evidence for divergence in responses to dehydration. FEBS J 275 (2008) 281-288
    • (2008) FEBS J , vol.275 , pp. 281-288
    • Hengherr, S.1    Heyer, A.G.2    Köhler, H.R.3    Schill, R.O.4
  • 45
    • 4043084803 scopus 로고    scopus 로고
    • Response of human cells to desiccation: comparison with hyperosmotic stress response
    • Huang Z., and Tunnacliffe A. Response of human cells to desiccation: comparison with hyperosmotic stress response. J Physiol 558 (2004) 181-191
    • (2004) J Physiol , vol.558 , pp. 181-191
    • Huang, Z.1    Tunnacliffe, A.2
  • 46
    • 24144463791 scopus 로고    scopus 로고
    • Gene induction by desiccation stress in human cell cultures
    • Huang Z., and Tunnacliffe A. Gene induction by desiccation stress in human cell cultures. FEBS Lett 579 (2005) 4973-4977
    • (2005) FEBS Lett , vol.579 , pp. 4973-4977
    • Huang, Z.1    Tunnacliffe, A.2
  • 47
  • 48
    • 33847312694 scopus 로고    scopus 로고
    • Induction of Hsp70 by desiccation, ionising radiation and heat-shock in the eutardigrade Richtersius coronifer
    • Jönsson K.I., and Schill R.O. Induction of Hsp70 by desiccation, ionising radiation and heat-shock in the eutardigrade Richtersius coronifer. Comp Biochem Physiol B Comp Physiol 146 (2007) 456-460
    • (2007) Comp Biochem Physiol B Comp Physiol , vol.146 , pp. 456-460
    • Jönsson, K.I.1    Schill, R.O.2
  • 50
    • 0142200333 scopus 로고    scopus 로고
    • Anhydrobiosis without trehalose in bdelloid rotifers
    • Lapinski J., and Tunnacliffe A. Anhydrobiosis without trehalose in bdelloid rotifers. FEBS Lett 553 (2003) 387-390
    • (2003) FEBS Lett , vol.553 , pp. 387-390
    • Lapinski, J.1    Tunnacliffe, A.2
  • 51
    • 0033559203 scopus 로고    scopus 로고
    • The synthesis of a small heat shock/alpha-crystallin protein in artemia and its relationship to stress tolerance during development
    • Liang P., and MacRae T.H. The synthesis of a small heat shock/alpha-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
  • 52
    • 0030755398 scopus 로고    scopus 로고
    • Molecular characterization of a small heat shock alpha-crystallin protein in encysted artemia embryos
    • Liang P., Amons R., Clegg J.S., and MacRae T.H. Molecular characterization of a small heat shock alpha-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
  • 53
    • 0031020927 scopus 로고    scopus 로고
    • Purification, structure and in vitro molecular-chaperone activity of Artemia p26, a small heat-shock/alpha-crystallin protein
    • Liang P., Amons R., Macrae T.H., and Clegg J.S. Purification, structure and in vitro molecular-chaperone activity of Artemia p26, a small heat-shock/alpha-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
  • 54
    • 0030462264 scopus 로고    scopus 로고
    • Metabolism of gemmules from the freshwater sponge Eunapius fragilis during diapause and post-diapause states
    • Loomis S.H., Hand S.C., and Fell P.E. Metabolism of gemmules from the freshwater sponge Eunapius fragilis during diapause and post-diapause states. Biolo Bull 191 (1996) 385-392
    • (1996) Biolo Bull , vol.191 , pp. 385-392
    • Loomis, S.H.1    Hand, S.C.2    Fell, P.E.3
  • 55
    • 23444443329 scopus 로고    scopus 로고
    • A small stress protein acts synergistically with trehalose to confer desiccation tolerance on mammalian cells
    • Ma X., Jamil K., Macrae T.H., Clegg J.S., Russell J.M., Villeneuve T.S., et al. A small stress protein acts synergistically with trehalose to confer desiccation tolerance on mammalian cells. Cryobiology 51 (2005) 15-28
    • (2005) Cryobiology , vol.51 , pp. 15-28
    • Ma, X.1    Jamil, K.2    Macrae, T.H.3    Clegg, J.S.4    Russell, J.M.5    Villeneuve, T.S.6
  • 56
    • 0742322606 scopus 로고    scopus 로고
    • Molecular chaperones, stress resistance and development in Artemia franciscana
    • MacRae T.H. Molecular chaperones, stress resistance and development in Artemia franciscana. Semin Cell Dev Biol 14 (2003) 251-258
    • (2003) Semin Cell Dev Biol , vol.14 , pp. 251-258
    • MacRae, T.H.1
  • 57
    • 0344025281 scopus 로고
    • Freezing of living cells: mechanisms and implications
    • Mazur P. Freezing of living cells: mechanisms and implications. Am J Physiol 247 (1984) C125-142
    • (1984) Am J Physiol , vol.247
    • Mazur, P.1
  • 58
    • 0033983233 scopus 로고    scopus 로고
    • Osmotic stress induces rapid activation of a salicylic acid-induced protein kinase and a homolog of protein kinase ASK1 in tobacco cells
    • Mikolajczyk M., Awotunde O.S., Muszynska G., Klessig D.F., and Dobrowolska G. Osmotic stress induces rapid activation of a salicylic acid-induced protein kinase and a homolog of protein kinase ASK1 in tobacco cells. Plant Cell 12 (2000) 165-178
    • (2000) Plant Cell , vol.12 , pp. 165-178
    • Mikolajczyk, M.1    Awotunde, O.S.2    Muszynska, G.3    Klessig, D.F.4    Dobrowolska, G.5
  • 59
    • 0030052839 scopus 로고    scopus 로고
    • A gene encoding a mitogen-activated protein kinase kinase kinase is induced simultaneously with genes for a mitogen-activated protein kinase and an S6 ribosomal protein kinase by touch, cold, and water stress in Arabidopsis thaliana
    • Mizoguchi T., Irie K., Hirayama T., Hayashida N., Yamaguchi-Shinozaki K., Matsumoto K., et al. A gene encoding a mitogen-activated protein kinase kinase kinase is induced simultaneously with genes for a mitogen-activated protein kinase and an S6 ribosomal protein kinase by touch, cold, and water stress in Arabidopsis thaliana. Proc Natl Acad Sci U S A 93 (1996) 765-769
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 765-769
    • Mizoguchi, T.1    Irie, K.2    Hirayama, T.3    Hayashida, N.4    Yamaguchi-Shinozaki, K.5    Matsumoto, K.6
  • 60
    • 1142302227 scopus 로고    scopus 로고
    • Molecular chaperones: structure of a protein disaggregase
    • Mogk A., and Bukau B. Molecular chaperones: structure of a protein disaggregase. Curr Biol 14 (2004) R78-80
    • (2004) Curr Biol , vol.14
    • Mogk, A.1    Bukau, B.2
  • 61
    • 0036625891 scopus 로고    scopus 로고
    • Current status of the tardigrada: evolution and ecology
    • Nelson D.R. Current status of the tardigrada: evolution and ecology. Integr Comp Biol 42 (2002) 652-659
    • (2002) Integr Comp Biol , vol.42 , pp. 652-659
    • Nelson, D.R.1
  • 63
    • 0036181843 scopus 로고    scopus 로고
    • Looking beyond sugars: the role of amphiphilic solutes in preventing adventitious reactions in anhydrobiotes at low water contents
    • Oliver A.E., Hincha D.K., and Crowe J.H. Looking beyond sugars: the role of amphiphilic solutes in preventing adventitious reactions in anhydrobiotes at low water contents. Comp Biochem Physiol Part A Mol Integr Physiol 131 (2002) 515-525
    • (2002) Comp Biochem Physiol Part A Mol Integr Physiol , vol.131 , pp. 515-525
    • Oliver, A.E.1    Hincha, D.K.2    Crowe, J.H.3
  • 64
    • 0347360092 scopus 로고    scopus 로고
    • Loading human mesenchymal stem cells with trehalose by fluid-phase endocytosis
    • Oliver A.E., Kamran J., Crowe J.H., and Tablin F. Loading human mesenchymal stem cells with trehalose by fluid-phase endocytosis. Cell Preservation Technol 2 (2004) 35-49
    • (2004) Cell Preservation Technol , vol.2 , pp. 35-49
    • Oliver, A.E.1    Kamran, J.2    Crowe, J.H.3    Tablin, F.4
  • 65
    • 30744466639 scopus 로고    scopus 로고
    • Desiccation tolerance in bryophytes: a reflection of the primitive strategy for plant survival in dehydrating habitats?
    • Oliver M.J., Velten J., and Mishler B.D. Desiccation tolerance in bryophytes: a reflection of the primitive strategy for plant survival in dehydrating habitats?. Integr Comp Biol 45 (2005) 788-799
    • (2005) Integr Comp Biol , vol.45 , pp. 788-799
    • Oliver, M.J.1    Velten, J.2    Mishler, B.D.3
  • 66
    • 0033282707 scopus 로고    scopus 로고
    • Desiccation survival of parasitic nematodes
    • Perry R.N. Desiccation survival of parasitic nematodes. Parasitology 119 (1999) S19-S30
    • (1999) Parasitology , vol.119
    • Perry, R.N.1
  • 68
    • 0035520398 scopus 로고    scopus 로고
    • Desiccation tolerance: a simple process?
    • Potts M. Desiccation tolerance: a simple process?. Trends Microbiol 9 (2001) 553-559
    • (2001) Trends Microbiol , vol.9 , pp. 553-559
    • Potts, M.1
  • 69
    • 0000193175 scopus 로고
    • Survival of the cryptobiotic eutardigrade Adorybiotus coronifer during cooling to - 196 °C: effect of cooling rate, trehalose level, and short-term acclimation
    • Ramlov H., and Westh P. Survival of the cryptobiotic eutardigrade Adorybiotus coronifer during cooling to - 196 °C: effect of cooling rate, trehalose level, and short-term acclimation. Cryobiology 29 (1992) 125-130
    • (1992) Cryobiology , vol.29 , pp. 125-130
    • Ramlov, H.1    Westh, P.2
  • 70
    • 0035709916 scopus 로고    scopus 로고
    • Cryptobiosis in the eutardigrade Adorybiotus coronifer: tolerance to alcohols, temperature and de novo protein synthesis
    • Ramløv H., and Westh P. Cryptobiosis in the eutardigrade Adorybiotus coronifer: tolerance to alcohols, temperature and de novo protein synthesis. Zool Anz 240 (2001) 517-523
    • (2001) Zool Anz , vol.240 , pp. 517-523
    • Ramløv, H.1    Westh, P.2
  • 71
    • 0028816030 scopus 로고
    • Preservation of hemostatic and structural properties of rehydrated lyophilized platelets: potential for long-term storage of dried platelets for transfusion
    • Read M.S., Reddick R.L., Bode A.P., Bellinger D.A., Nichols T.C., Taylor K., et al. Preservation of hemostatic and structural properties of rehydrated lyophilized platelets: potential for long-term storage of dried platelets for transfusion. Proc Natl Acad Sci U S A 92 (1995) 397-401
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 397-401
    • Read, M.S.1    Reddick, R.L.2    Bode, A.P.3    Bellinger, D.A.4    Nichols, T.C.5    Taylor, K.6
  • 72
    • 34547617765 scopus 로고
    • Studies on fresh-water bryozoa. VII. On the viability of dried statoblasts of Lophopodella carteri var. typica
    • Rogick M.D. Studies on fresh-water bryozoa. VII. On the viability of dried statoblasts of Lophopodella carteri var. typica. Trans Am Microsc Soc 57 (1938) 178-199
    • (1938) Trans Am Microsc Soc , vol.57 , pp. 178-199
    • Rogick, M.D.1
  • 73
    • 67349186388 scopus 로고
    • Desiccation tolerance in embryonic stages of the tardigrade Milnesium tardigradum
    • Schill R.O., and Fritz G.B. Desiccation tolerance in embryonic stages of the tardigrade Milnesium tardigradum. J Zool (Lond) 276 (1938) 103-107
    • (1938) J Zool (Lond) , vol.276 , pp. 103-107
    • Schill, R.O.1    Fritz, G.B.2
  • 74
    • 2442540307 scopus 로고    scopus 로고
    • Stress gene (hsp70) sequences and quantitative expression in Milnesium tardigradum (Tardigrada) during active and cryptobiotic stages
    • Schill R.O., Steinbruck G.H., and Kohler H.R. Stress gene (hsp70) sequences and quantitative expression in Milnesium tardigradum (Tardigrada) during active and cryptobiotic stages. J Exp Biol 207 (2004) 1607-1613
    • (2004) J Exp Biol , vol.207 , pp. 1607-1613
    • Schill, R.O.1    Steinbruck, G.H.2    Kohler, H.R.3
  • 75
    • 33646500354 scopus 로고    scopus 로고
    • Quiescent gemmules of the freshwater sponge, Spongilla lacustris (Linnaeus, 1759), contain remarkably high levels of Hsp70 stress protein and hsp70 stress gene mRNA
    • Schill R.O., Pfannkuchen M., Fritz G., Köhler H.-R., and Brümmer F. Quiescent gemmules of the freshwater sponge, Spongilla lacustris (Linnaeus, 1759), contain remarkably high levels of Hsp70 stress protein and hsp70 stress gene mRNA. J Exp Zoolog A Comp Exp Biol 305A (2006) 449-457
    • (2006) J Exp Zoolog A Comp Exp Biol , vol.305 A , pp. 449-457
    • Schill, R.O.1    Pfannkuchen, M.2    Fritz, G.3    Köhler, H.-R.4    Brümmer, F.5
  • 76
    • 0033822325 scopus 로고    scopus 로고
    • Resurrection plants and the secrets of eternal leaf
    • Scott P. Resurrection plants and the secrets of eternal leaf. Ann Bot (Lond) 85 (2000) 159-166
    • (2000) Ann Bot (Lond) , vol.85 , pp. 159-166
    • Scott, P.1
  • 77
    • 0032578825 scopus 로고    scopus 로고
    • Preserving tardigrades under pressure
    • Seki K., and Toyoshima M. Preserving tardigrades under pressure. Nature 395 (1998) 853-854
    • (1998) Nature , vol.395 , pp. 853-854
    • Seki, K.1    Toyoshima, M.2
  • 78
    • 0035107803 scopus 로고    scopus 로고
    • Monitoring the expression pattern of 1300 Arabidopsis genes under drought and cold stresses by using a full-length cDNA microarray
    • Seki M., Narusaka M., Abe H., Kasuga M., Yamaguchi-Shinozaki K., Carninci P., et al. Monitoring the expression pattern of 1300 Arabidopsis genes under drought and cold stresses by using a full-length cDNA microarray. Plant Cell 13 (2001) 61-72
    • (2001) Plant Cell , vol.13 , pp. 61-72
    • Seki, M.1    Narusaka, M.2    Abe, H.3    Kasuga, M.4    Yamaguchi-Shinozaki, K.5    Carninci, P.6
  • 79
    • 0001281780 scopus 로고    scopus 로고
    • Anhydrobiosis and cold tolerance in tardigrades
    • Somme L. Anhydrobiosis and cold tolerance in tardigrades. Eur J Entomol 93 (1996) 349-357
    • (1996) Eur J Entomol , vol.93 , pp. 349-357
    • Somme, L.1
  • 80
    • 20444478694 scopus 로고    scopus 로고
    • The small heat shock proteins and their role in human disease
    • Sun Y., and MacRae T.H. The small heat shock proteins and their role in human disease. FEBS J 272 (2005) 2613-2627
    • (2005) FEBS J , vol.272 , pp. 2613-2627
    • Sun, Y.1    MacRae, T.H.2
  • 81
    • 29144527460 scopus 로고    scopus 로고
    • Small heat shock proteins: molecular structure and chaperone function
    • Sun Y., and MacRae T.H. Small heat shock proteins: molecular structure and chaperone function. Cell Mol Life Sci 62 (2005) 2460-2476
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2460-2476
    • Sun, Y.1    MacRae, T.H.2
  • 82
    • 4544356426 scopus 로고    scopus 로고
    • Oligomerization, chaperone activity, and nuclear localization of p26, a small heat shock protein from Artemia franciscana
    • Sun Y., Mansour M., Crack J.A., Gass G.L., and MacRae T.H. Oligomerization, chaperone activity, and nuclear localization of p26, a small heat shock protein from Artemia franciscana. J Biol Chem 279 (2004) 39999-40006
    • (2004) J Biol Chem , vol.279 , pp. 39999-40006
    • Sun, Y.1    Mansour, M.2    Crack, J.A.3    Gass, G.L.4    MacRae, T.H.5
  • 83
    • 33644933681 scopus 로고    scopus 로고
    • Structural and functional roles for beta-strand 7 in the alpha-crystallin domain of p26, a polydisperse small heat shock protein from Artemia franciscana
    • Sun Y., Bojikova-Fournier S., and MacRae T.H. Structural and functional roles for beta-strand 7 in the alpha-crystallin domain of p26, a polydisperse small heat shock protein from Artemia franciscana. FEBS J 273 (2006) 1020-1034
    • (2006) FEBS J , vol.273 , pp. 1020-1034
    • Sun, Y.1    Bojikova-Fournier, S.2    MacRae, T.H.3
  • 84
    • 0142216204 scopus 로고    scopus 로고
    • Resurrecting Van Leeuwenhoek s rotifers: a reappraisal of the role of disaccharides in anhydrobiosis
    • Tunnacliffe A., and Lapinski J. Resurrecting Van Leeuwenhoek s rotifers: a reappraisal of the role of disaccharides in anhydrobiosis. Philos Trans R Soc Lond B Biol Sci 358 (2003) 1755-1771
    • (2003) Philos Trans R Soc Lond B Biol Sci , vol.358 , pp. 1755-1771
    • Tunnacliffe, A.1    Lapinski, J.2
  • 85
    • 0036188985 scopus 로고    scopus 로고
    • Anhydrobiotic engineering of bacterial and mammalian cells: is intracellular trehalose sufficient?
    • Tunnacliffe A., de Castro A.G., and Manzanera M. Anhydrobiotic engineering of bacterial and mammalian cells: is intracellular trehalose sufficient?. Cryobiology 43 (2001) 124-132
    • (2001) Cryobiology , vol.43 , pp. 124-132
    • Tunnacliffe, A.1    de Castro, A.G.2    Manzanera, M.3
  • 86
    • 0015951878 scopus 로고
    • A simple method for freezing human platelets using 6 per cent dimethylsulfoxide and storage at - 80 degrees C
    • Valeri C.R., Feingold H., and Marchionni L.D. A simple method for freezing human platelets using 6 per cent dimethylsulfoxide and storage at - 80 degrees C. Blood 43 (1974) 131-136
    • (1974) Blood , vol.43 , pp. 131-136
    • Valeri, C.R.1    Feingold, H.2    Marchionni, L.D.3
  • 87
    • 33644836723 scopus 로고    scopus 로고
    • Inhibition of apoptosis by p26: implications for small heat shock protein function during Artemia development
    • Villeneuve T.S., Ma X., Sun Y., Oulton M.M., Oliver A.E., and MacRae T.H. Inhibition of apoptosis by p26: implications for small heat shock protein function during Artemia development. Cell Stress Chaperones 11 (2006) 71-80
    • (2006) Cell Stress Chaperones , vol.11 , pp. 71-80
    • Villeneuve, T.S.1    Ma, X.2    Sun, Y.3    Oulton, M.M.4    Oliver, A.E.5    MacRae, T.H.6
  • 88
    • 0034992527 scopus 로고    scopus 로고
    • Influence of trehalose on the molecular chaperone activity of p26, a small heat shock/alpha-crystallin protein
    • Viner R.I., and Clegg J.S. Influence of trehalose on the molecular chaperone activity of p26, a small heat shock/alpha-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
  • 89
    • 37049050308 scopus 로고
    • Bound water, metabolites and genetic continuity
    • Webb S.J. Bound water, metabolites and genetic continuity. Nature 203 (1964) 374-377
    • (1964) Nature , vol.203 , pp. 374-377
    • Webb, S.J.1
  • 90
    • 0342719995 scopus 로고
    • Bound water, inositol, and the biosynthesis of temperate and virulent bacteriophages by air-dried Escherichia coli
    • Webb S.J., Dumasia M.D., and Bhorjee J.S. Bound water, inositol, and the biosynthesis of temperate and virulent bacteriophages by air-dried Escherichia coli. Can J Microbiol 11 (1965) 141-150
    • (1965) Can J Microbiol , vol.11 , pp. 141-150
    • Webb, S.J.1    Dumasia, M.D.2    Bhorjee, J.S.3
  • 91
    • 46749120245 scopus 로고    scopus 로고
    • Glucose, sucrose and trehalose are partially excluded from the interface of hydrated DMPC bilayers
    • Westh P. Glucose, sucrose and trehalose are partially excluded from the interface of hydrated DMPC bilayers. Phys Chem Chem Phys 10 (2008) 4110-4112
    • (2008) Phys Chem Chem Phys , vol.10 , pp. 4110-4112
    • Westh, P.1
  • 92
    • 0008358772 scopus 로고
    • Freeze tolerance in the tardigrade Adorybiotus coronifer ice content and evidence of ice-nucleating agents
    • Westh P., and Hvidt A. Freeze tolerance in the tardigrade Adorybiotus coronifer ice content and evidence of ice-nucleating agents. Cryobiology 27 (1990) 679
    • (1990) Cryobiology , vol.27 , pp. 679
    • Westh, P.1    Hvidt, A.2
  • 93
    • 84989625587 scopus 로고
    • Trehalose accumulation in the tardigrade Adorybiotus coronifer during anhydrobiosis
    • Westh P., and Ramlov H. Trehalose accumulation in the tardigrade Adorybiotus coronifer during anhydrobiosis. J Exp Zool 258 (1991) 303-311
    • (1991) J Exp Zool , vol.258 , pp. 303-311
    • Westh, P.1    Ramlov, H.2
  • 94
    • 0025859022 scopus 로고
    • Ice-nucleating activity in the freeze-tolerant tardigrade Adorybiotus coronifer
    • Westh P., Kristiansen J., and Hvidt A. Ice-nucleating activity in the freeze-tolerant tardigrade Adorybiotus coronifer. Comp Biochem Physiol A Comp Physiol 99 (1991) 401-404
    • (1991) Comp Biochem Physiol A Comp Physiol , vol.99 , pp. 401-404
    • Westh, P.1    Kristiansen, J.2    Hvidt, A.3
  • 95
    • 0034964582 scopus 로고    scopus 로고
    • Human platelets loaded with trehalose survive freeze-drying
    • Wolkers W.F., Walker N.J., Tablin F., and Crowe J.H. Human platelets loaded with trehalose survive freeze-drying. Cryobiology 42 (2001) 79-87
    • (2001) Cryobiology , vol.42 , pp. 79-87
    • Wolkers, W.F.1    Walker, N.J.2    Tablin, F.3    Crowe, J.H.4
  • 97
    • 0035709607 scopus 로고    scopus 로고
    • Cryptobiosis 300 years on from van Leeuwenhoek: what have we learned about tardigrades?
    • Wright J.C. Cryptobiosis 300 years on from van Leeuwenhoek: what have we learned about tardigrades?. Zool Anz 240 (2001) 563-582
    • (2001) Zool Anz , vol.240 , pp. 563-582
    • Wright, J.C.1
  • 98
    • 3142590478 scopus 로고    scopus 로고
    • Scaffold proteins in mammalian MAP kinase cascades
    • Yoshioka K. Scaffold proteins in mammalian MAP kinase cascades. J Biochem 135 (2004) 657-661
    • (2004) J Biochem , vol.135 , pp. 657-661
    • Yoshioka, K.1
  • 99
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: a specialized but essential protein-folding tool
    • Young J.C., Moarefi I., and Hartl F.U. Hsp90: a specialized but essential protein-folding tool. J Cell Biochem 154 (2001) 267-273
    • (2001) J Cell Biochem , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3
  • 100
    • 0033738988 scopus 로고    scopus 로고
    • Genetic analysis of plant salt tolerance using Arabidopsis
    • Zhu J.K. Genetic analysis of plant salt tolerance using Arabidopsis. Plant Physiol 124 (2000) 941-948
    • (2000) Plant Physiol , vol.124 , pp. 941-948
    • Zhu, J.K.1


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