메뉴 건너뛰기




Volumn 73, Issue 2, 2016, Pages 240-247

Cryopreservation of lipid bilayers by LEA proteins from Artemia franciscana and trehalose

Author keywords

Artemia franciscana; Freezing; Intrinsically disordered protein; Late embryogenesis abundant protein; Liposome; Mitochondria; Trehalose

Indexed keywords

6 CARBOXYFLUORESCEIN; CYTOCHROME C; LATE EMBRYOGENESIS ABUNDANT PROTEIN; LIPOSOME; MITOCHONDRIAL PROTEIN; TREHALOSE; UNCLASSIFIED DRUG; CRYOPROTECTIVE AGENT; LATE EMBRYOGENESIS ABUNDANT PROTEIN, PLANT; LIPID BILAYER; PLANT PROTEIN;

EID: 84990055147     PISSN: 00112240     EISSN: 10902392     Source Type: Journal    
DOI: 10.1016/j.cryobiol.2016.07.003     Document Type: Article
Times cited : (23)

References (65)
  • 1
    • 84938675673 scopus 로고    scopus 로고
    • Engineered trehalose permeable to mammalian cells
    • [1] Abazari, A., Meimetis, L.G., Budin, G., Bale, S.S., Weissleder, R., Toner, M., Engineered trehalose permeable to mammalian cells. PLoS ONE, 10(6), 2015, e0130323, 10.1371/journal.pone.0130323.
    • (2015) PLoS ONE , vol.10 , Issue.6 , pp. e0130323
    • Abazari, A.1    Meimetis, L.G.2    Budin, G.3    Bale, S.S.4    Weissleder, R.5    Toner, M.6
  • 2
    • 0022931338 scopus 로고
    • The reversible Ca2+-induced permeabilization of rat liver mitochondria
    • [2] Al-Nasser, I., Crompton, M., The reversible Ca2+-induced permeabilization of rat liver mitochondria. Biochem. J. 239 (1986), 19–29.
    • (1986) Biochem. J. , vol.239 , pp. 19-29
    • Al-Nasser, I.1    Crompton, M.2
  • 3
    • 0023394634 scopus 로고
    • Modes of interaction of cryoprotectants with membrane phospholipids during freezing
    • [3] Anchordoguy, T.J., Rudolph, A.S., Carpenter, J.F., Crowe, J.H., Modes of interaction of cryoprotectants with membrane phospholipids during freezing. Cryobiology 24 (1987), 324–331.
    • (1987) Cryobiology , vol.24 , pp. 324-331
    • Anchordoguy, T.J.1    Rudolph, A.S.2    Carpenter, J.F.3    Crowe, J.H.4
  • 4
    • 0029825615 scopus 로고    scopus 로고
    • Constitutive expression of the cold-regulated Arabidopsis thaliana COR15a gene affects both chloroplast and protoplast freezing tolerance
    • [4] Artus, N.N., Uemura, M., Steponkus, P.L., Gilmour, S.J., Lin, C.T., Thomashow, M.F., Constitutive expression of the cold-regulated Arabidopsis thaliana COR15a gene affects both chloroplast and protoplast freezing tolerance. Proc. Natl. Acad. Sci. U. S. A. 93 (1996), 13404–13409.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 13404-13409
    • Artus, N.N.1    Uemura, M.2    Steponkus, P.L.3    Gilmour, S.J.4    Lin, C.T.5    Thomashow, M.F.6
  • 5
    • 57149111077 scopus 로고    scopus 로고
    • The crucial role of plant mitochondria in orchestrating drought tolerance
    • [5] Atkin, O.K., Macherel, D., The crucial role of plant mitochondria in orchestrating drought tolerance. Ann. Bot. 103:4 (2009), 581–597.
    • (2009) Ann. Bot. , vol.103 , Issue.4 , pp. 581-597
    • Atkin, O.K.1    Macherel, D.2
  • 6
    • 0030592172 scopus 로고    scopus 로고
    • The permeability transition pore. Control points of a cyclosporin A-sensitive mitochondrial channel involved in cell death
    • [6] Bernardi, P., The permeability transition pore. Control points of a cyclosporin A-sensitive mitochondrial channel involved in cell death. Biochim. Biophys. Acta 1275 (1996), 5–9.
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 5-9
    • Bernardi, P.1
  • 7
    • 84883776628 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore: a mystery solved?
    • [7] Bernardi, P., The mitochondrial permeability transition pore: a mystery solved?. Front. Physiol., 4, 2013, 95.
    • (2013) Front. Physiol. , vol.4 , pp. 95
    • Bernardi, P.1
  • 8
    • 38449092423 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore
    • [8] Bernardi, P., Forte, M., The mitochondrial permeability transition pore. Novartis Found. Symp. 287 (2007), 157–164.
    • (2007) Novartis Found. Symp. , vol.287 , pp. 157-164
    • Bernardi, P.1    Forte, M.2
  • 10
    • 84899058942 scopus 로고    scopus 로고
    • Quantification of cellular protein expression and molecular features of group 3 LEA proteins from embryos of Artemia franciscana
    • [10] Boswell, L.C., Moore, D.S., Hand, S.C., Quantification of cellular protein expression and molecular features of group 3 LEA proteins from embryos of Artemia franciscana. Cell Stress Chaperon 19 (2014), 329–341.
    • (2014) Cell Stress Chaperon , vol.19 , pp. 329-341
    • Boswell, L.C.1    Moore, D.S.2    Hand, S.C.3
  • 11
    • 2942530843 scopus 로고    scopus 로고
    • Cryopreservation of stem cells using trehalose: evaluation of the method using a human hematopoietic cell line
    • [11] Buchanan, S.S., Gross, S.A., Acker, J.P., Toner, M., Carpenter, J.F., Pyatt, D.W., Cryopreservation of stem cells using trehalose: evaluation of the method using a human hematopoietic cell line. Stem Cells Dev. 13 (2004), 295–305.
    • (2004) Stem Cells Dev. , vol.13 , pp. 295-305
    • Buchanan, S.S.1    Gross, S.A.2    Acker, J.P.3    Toner, M.4    Carpenter, J.F.5    Pyatt, D.W.6
  • 12
    • 0008348285 scopus 로고
    • Arrestment of carbohydrate metabolism during anaerobic dormancy and aerobic acidosis: determination of pH sensitive control points
    • [12] Carpenter, J.H., Hand, S.C., Arrestment of carbohydrate metabolism during anaerobic dormancy and aerobic acidosis: determination of pH sensitive control points. J. Comp. Physiol. B 156:4 (1986), 451–459.
    • (1986) J. Comp. Physiol. B , vol.156 , Issue.4 , pp. 451-459
    • Carpenter, J.H.1    Hand, S.C.2
  • 13
    • 0009002707 scopus 로고
    • Free glycerol in dormant cysts of the brine shrimp Artemia salina, and its disappearance during development
    • [13] Clegg, J.S., Free glycerol in dormant cysts of the brine shrimp Artemia salina, and its disappearance during development. Biol. Bull. Woods Hole 123 (1962), 295–301.
    • (1962) Biol. Bull. Woods Hole , vol.123 , pp. 295-301
    • Clegg, J.S.1
  • 14
    • 0001312707 scopus 로고
    • Origin of trehalose and its significance during formation of encysted dormant embryos of Artemia Salina
    • [14] Clegg, J.S., Origin of trehalose and its significance during formation of encysted dormant embryos of Artemia Salina. Comp. Biochem. Physiol. 14 (1965), 135–143.
    • (1965) Comp. Biochem. Physiol. , vol.14 , pp. 135-143
    • Clegg, J.S.1
  • 15
    • 0017838442 scopus 로고
    • Interrelationships between water and cellular metabolism in Artemia cysts. VIII Sorption isotherms and derived thermodynamic quantities
    • [15] Clegg, J.S., Interrelationships between water and cellular metabolism in Artemia cysts. VIII Sorption isotherms and derived thermodynamic quantities. J. Cell Physiol. 94 (1978), 123–137.
    • (1978) J. Cell Physiol. , vol.94 , pp. 123-137
    • Clegg, J.S.1
  • 16
    • 30744459861 scopus 로고    scopus 로고
    • Desiccation tolerance in encysted embryos of the animal extremophile, Artemia
    • [16] Clegg, J.S., Desiccation tolerance in encysted embryos of the animal extremophile, Artemia. Integr. Comp. Biol. 45 (2005), 715–724.
    • (2005) Integr. Comp. Biol. , vol.45 , pp. 715-724
    • Clegg, J.S.1
  • 17
    • 79957467692 scopus 로고    scopus 로고
    • Stress-related proteins compared in diapause and in activated, anoxic encysted embryos of the animal extremophile, Artemia franciscana
    • [17] Clegg, J.S., Stress-related proteins compared in diapause and in activated, anoxic encysted embryos of the animal extremophile, Artemia franciscana. J. Insect Physiol. 57 (2011), 660–664.
    • (2011) J. Insect Physiol. , vol.57 , pp. 660-664
    • Clegg, J.S.1
  • 18
    • 84881836907 scopus 로고    scopus 로고
    • Water, membranes, and life without water
    • D. Le Bihan H. Hidenao Fukuyama Pan Stanford Publishing Pte. Ltd. Singapore
    • [18] Crowe, J.H., Water, membranes, and life without water. Le Bihan, D., Hidenao Fukuyama, H., (eds.) Water: The Forgotten Molecule, 2011, Pan Stanford Publishing Pte. Ltd., Singapore, 205–232.
    • (2011) Water: The Forgotten Molecule , pp. 205-232
    • Crowe, J.H.1
  • 20
    • 0025160465 scopus 로고
    • Are freezing and dehydration similar stress vectors? A comparison of modes of interaction of stabilizing solutes with biomolecules
    • [20] Crowe, J.H., Carpenter, J.F., Crowe, L.M., Anchordoguy, T.J., Are freezing and dehydration similar stress vectors? A comparison of modes of interaction of stabilizing solutes with biomolecules. Cryobiology 27 (1990), 219–231.
    • (1990) Cryobiology , vol.27 , pp. 219-231
    • Crowe, J.H.1    Carpenter, J.F.2    Crowe, L.M.3    Anchordoguy, T.J.4
  • 22
    • 0348053809 scopus 로고
    • Preservation of membranes in anhydrobiotic organisms: the role of trehalose
    • [22] Crowe, J.H., Crowe, L.M., Chapman, D., Preservation of membranes in anhydrobiotic organisms: the role of trehalose. Science 223 (1984), 701–703.
    • (1984) Science , vol.223 , pp. 701-703
    • Crowe, J.H.1    Crowe, L.M.2    Chapman, D.3
  • 23
    • 0036188792 scopus 로고    scopus 로고
    • The trehalose myth revisited: introduction to a symposium on stabilization of cells in the dry state
    • [23] Crowe, J.H., Crowe, L.M., Oliver, A.E., Tsvetkova, N., Wolkers, W., Tablin, F., The trehalose myth revisited: introduction to a symposium on stabilization of cells in the dry state. Cryobiology 43 (2001), 89–105.
    • (2001) Cryobiology , vol.43 , pp. 89-105
    • Crowe, J.H.1    Crowe, L.M.2    Oliver, A.E.3    Tsvetkova, N.4    Wolkers, W.5    Tablin, F.6
  • 26
    • 0011479137 scopus 로고
    • Preservation of dry liposomes does not require retention of residual water
    • [26] Crowe, J.H., Spargo, B.J., Crowe, L.M., Preservation of dry liposomes does not require retention of residual water. Proc. Natl. Acad. Sci. U. S. A. 84 (1987), 1537–1540.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 1537-1540
    • Crowe, J.H.1    Spargo, B.J.2    Crowe, L.M.3
  • 27
    • 0026437091 scopus 로고
    • Stabilization of dry liposomes by carbohydrates
    • [27] Crowe, L.M., Crowe, J.H., Stabilization of dry liposomes by carbohydrates. Dev. Biol. Stand. 74 (1992), 285–294.
    • (1992) Dev. Biol. Stand. , vol.74 , pp. 285-294
    • Crowe, L.M.1    Crowe, J.H.2
  • 28
    • 0010292777 scopus 로고
    • Observations biochimiques et physiologiques sur le development d'Artemia salina
    • [28] Dutrieu, J., Observations biochimiques et physiologiques sur le development d'Artemia salina. Leach Arch. Zool. Exp. Gen. 99 (1960), 1–133.
    • (1960) Leach Arch. Zool. Exp. Gen. , vol.99 , pp. 1-133
    • Dutrieu, J.1
  • 31
    • 17444426801 scopus 로고    scopus 로고
    • Identification in pea seed mitochondria of a late embryogenesis abundant protein able to protect enzymes from drying
    • [31] Grelet, J., Benamar, A., Teyssier, E., Avelange-Macherel, M.H., Grunwald, D., Macherel, D., Identification in pea seed mitochondria of a late embryogenesis abundant protein able to protect enzymes from drying. Plant Physiol. 137:1 (2005), 157–167.
    • (2005) Plant Physiol. , vol.137 , Issue.1 , pp. 157-167
    • Grelet, J.1    Benamar, A.2    Teyssier, E.3    Avelange-Macherel, M.H.4    Grunwald, D.5    Macherel, D.6
  • 32
    • 47749120750 scopus 로고    scopus 로고
    • New approaches for cell and animal preservation: lessons from aquatic organisms
    • P.J. Walsh S.L. Smith L.E. Fleming H.M. Solo-Gabriele W.H. Gerwick Academic Press San Diego
    • [32] Hand, S.C., Hagedorn, M., New approaches for cell and animal preservation: lessons from aquatic organisms. Walsh, P.J., Smith, S.L., Fleming, L.E., Solo-Gabriele, H.M., Gerwick, W.H., (eds.) Oceans and Human Health: Risks and Remedies from the Seas, 2008, Academic Press, San Diego, 613–631.
    • (2008) Oceans and Human Health: Risks and Remedies from the Seas , pp. 613-631
    • Hand, S.C.1    Hagedorn, M.2
  • 33
    • 0029942396 scopus 로고    scopus 로고
    • Downregulation of cellular metabolism during environmental stress: mechanisms and implications
    • [33] 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
  • 34
    • 33847367791 scopus 로고    scopus 로고
    • Life without water: expression of plant LEA genes by an anhydrobiotic arthropod
    • [34] Hand, S.C., Jones, D., Menze, M.A., Witt, T.L., Life without water: expression of plant LEA genes by an anhydrobiotic arthropod. J. Exp. Zool. A Ecol. Genet. Physiol. 307 (2007), 62–66.
    • (2007) J. Exp. Zool. A Ecol. Genet. Physiol. , vol.307 , pp. 62-66
    • Hand, S.C.1    Jones, D.2    Menze, M.A.3    Witt, T.L.4
  • 35
    • 79951782916 scopus 로고    scopus 로고
    • LEA proteins during water stress: not just for plants anymore
    • [35] Hand, S.C., Menze, M.A., Toner, M., Boswell, L., Moore, D., LEA proteins during water stress: not just for plants anymore. Annu. Rev. Physiol. 73 (2011), 115–134.
    • (2011) Annu. Rev. Physiol. , vol.73 , pp. 115-134
    • Hand, S.C.1    Menze, M.A.2    Toner, M.3    Boswell, L.4    Moore, D.5
  • 36
    • 0000692105 scopus 로고    scopus 로고
    • Trehalose increases freeze-thaw damage in liposomes containing chloroplast glycolipids
    • [36] Hincha, D.K., Crowe, J.H., Trehalose increases freeze-thaw damage in liposomes containing chloroplast glycolipids. Cryobiology 36 (1998), 245–249.
    • (1998) Cryobiology , vol.36 , pp. 245-249
    • Hincha, D.K.1    Crowe, J.H.2
  • 37
    • 0032484571 scopus 로고    scopus 로고
    • The effects of chloroplast lipids on the stability of liposomes during freezing and drying
    • [37] Hincha, D.K., Oliver, A.E., Crowe, J.H., The effects of chloroplast lipids on the stability of liposomes during freezing and drying. Biochim. Biophys. Acta 1368 (1998), 150–160.
    • (1998) Biochim. Biophys. Acta , vol.1368 , pp. 150-160
    • Hincha, D.K.1    Oliver, A.E.2    Crowe, J.H.3
  • 38
    • 27844451441 scopus 로고    scopus 로고
    • Trehalose loading through the mitochondrial permeability transition pore enhances desiccation tolerance in rat liver mitochondria
    • [38] Liu, X.H., Aksan, A., Menze, M.A., Hand, S.C., Toner, M., Trehalose loading through the mitochondrial permeability transition pore enhances desiccation tolerance in rat liver mitochondria. Biochim. Biophys. Acta 1717 (2005), 21–26.
    • (2005) Biochim. Biophys. Acta , vol.1717 , pp. 21-26
    • Liu, X.H.1    Aksan, A.2    Menze, M.A.3    Hand, S.C.4    Toner, M.5
  • 39
    • 84908597142 scopus 로고
    • Anhydrobiosis in nematodes- carbohydrate and lipid-metabolism during dehydration
    • [39] Madin, K.A.C., Crowe, J.H., Anhydrobiosis in nematodes- carbohydrate and lipid-metabolism during dehydration. J. Exp. Zool. 193 (1975), 335–342.
    • (1975) J. Exp. Zool. , vol.193 , pp. 335-342
    • Madin, K.A.C.1    Crowe, J.H.2
  • 40
    • 0026730943 scopus 로고
    • The ‘ins’ and ‘outs’ of mitochondrial membrane channels
    • [40] Mannella, C.A., The ‘ins’ and ‘outs’ of mitochondrial membrane channels. Trends Biochem. Sci. 17 (1992), 315–320.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 315-320
    • Mannella, C.A.1
  • 41
    • 67449106986 scopus 로고    scopus 로고
    • Occurrence of mitochondria-targeted late embryogenesis abundant (LEA) gene in animals increases organelle resistance to water stress
    • [41] Menze, M.A., Boswell, L., Toner, M., Hand, S.C., Occurrence of mitochondria-targeted late embryogenesis abundant (LEA) gene in animals increases organelle resistance to water stress. J. Biol. Chem. 284 (2009), 10714–10719.
    • (2009) J. Biol. Chem. , vol.284 , pp. 10714-10719
    • Menze, M.A.1    Boswell, L.2    Toner, M.3    Hand, S.C.4
  • 42
    • 84946616113 scopus 로고    scopus 로고
    • Liposomes with diverse compositions are protected during desiccation by LEA proteins from Artemia franciscana and trehalose
    • [42] Moore, D.S., Hansen, R., Hand, S.C., Liposomes with diverse compositions are protected during desiccation by LEA proteins from Artemia franciscana and trehalose. Biochim. Biophys. Acta 1858:1 (2016), 104–115.
    • (2016) Biochim. Biophys. Acta , vol.1858 , Issue.1 , pp. 104-115
    • Moore, D.S.1    Hansen, R.2    Hand, S.C.3
  • 43
    • 84872304915 scopus 로고    scopus 로고
    • Metabolic downregulation and inhibition of carbohydrate catabolism during diapause in embryos of Artemia franciscana
    • [43] Patil, Y.N., Marden, B., Brand, M.D., Hand, S.C., Metabolic downregulation and inhibition of carbohydrate catabolism during diapause in embryos of Artemia franciscana. Physiol. Biochem. Zool. 86 (2013), 106–118.
    • (2013) Physiol. Biochem. Zool. , vol.86 , pp. 106-118
    • Patil, Y.N.1    Marden, B.2    Brand, M.D.3    Hand, S.C.4
  • 44
    • 79955802057 scopus 로고    scopus 로고
    • Structural transitions in the intrinsically disordered plant dehydration stress protein LEA7 upon drying are modulated by the presence of membranes
    • [44] Popova, A.V., Hundertmark, M., Seckler, R., Hincha, D.K., Structural transitions in the intrinsically disordered plant dehydration stress protein LEA7 upon drying are modulated by the presence of membranes. Biochim. Biophys. Acta 1808 (2011), 1879–1887.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 1879-1887
    • Popova, A.V.1    Hundertmark, M.2    Seckler, R.3    Hincha, D.K.4
  • 46
    • 0021825079 scopus 로고
    • Membrane stabilization during freezing: the role of two natural cryoprotectants, trehalose and proline
    • [46] Rudolph, A.S., Crowe, J.H., Membrane stabilization during freezing: the role of two natural cryoprotectants, trehalose and proline. Cryobiology 22 (1985), 367–377.
    • (1985) Cryobiology , vol.22 , pp. 367-377
    • Rudolph, A.S.1    Crowe, J.H.2
  • 48
    • 0029913433 scopus 로고    scopus 로고
    • Stability of dry liposomes in sugar glasses
    • [48] Sun, W.Q., Leopold, A.C., Crowe, L.M., Crowe, J.H., Stability of dry liposomes in sugar glasses. Biophys. J. 70 (1996), 1769–1776.
    • (1996) Biophys. J. , vol.70 , pp. 1769-1776
    • Sun, W.Q.1    Leopold, A.C.2    Crowe, L.M.3    Crowe, J.H.4
  • 49
    • 84919624038 scopus 로고    scopus 로고
    • Trehalose is a versatile and long-lived chaperone for desiccation tolerance
    • [49] Tapia, H., Koshland, D.E., Trehalose is a versatile and long-lived chaperone for desiccation tolerance. Curr. Biol. 24 (2014), 2758–2766.
    • (2014) Curr. Biol. , vol.24 , pp. 2758-2766
    • Tapia, H.1    Koshland, D.E.2
  • 50
    • 84907058263 scopus 로고    scopus 로고
    • Disordered Cold Regulated15 proteins protect chloroplast membranes during freezing through binding and folding, but do not stabilize chloroplast enzymes in vivo
    • [50] Thalhammer, A., Bryant, G., Sulpice, R., Hincha, D.K., Disordered Cold Regulated15 proteins protect chloroplast membranes during freezing through binding and folding, but do not stabilize chloroplast enzymes in vivo. Plant Physiol. 166 (2014), 190–201.
    • (2014) Plant Physiol. , vol.166 , pp. 190-201
    • Thalhammer, A.1    Bryant, G.2    Sulpice, R.3    Hincha, D.K.4
  • 51
    • 77954658735 scopus 로고    scopus 로고
    • Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state
    • [51] Thalhammer, A., Hundertmark, M., Popova, A.V., Seckler, R., Hincha, D.K., Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state. Biochim. Biophys. Acta 1798 (2010), 1812–1820.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1812-1820
    • Thalhammer, A.1    Hundertmark, M.2    Popova, A.V.3    Seckler, R.4    Hincha, D.K.5
  • 52
    • 77955652628 scopus 로고    scopus 로고
    • A mitochondrial late embryogenesis abundant protein stabilizes model membranes in the dry state
    • [52] Tolleter, D., Hincha, D.K., Macherel, D., A mitochondrial late embryogenesis abundant protein stabilizes model membranes in the dry state. Biochim. Biophys. Acta 1798 (2010), 1926–1933.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1926-1933
    • Tolleter, D.1    Hincha, D.K.2    Macherel, D.3
  • 54
    • 84939873612 scopus 로고    scopus 로고
    • Group 1 LEA proteins contribute to the desiccation and freeze tolerance of Artemia franciscana embryos during diapause
    • [54] Toxopeus, J., Warner, A.H., MacRae, T.H., Group 1 LEA proteins contribute to the desiccation and freeze tolerance of Artemia franciscana embryos during diapause. Cell Stress Chaperones 19 (2014), 939–948.
    • (2014) Cell Stress Chaperones , vol.19 , pp. 939-948
    • Toxopeus, J.1    Warner, A.H.2    MacRae, T.H.3
  • 55
    • 34548460796 scopus 로고    scopus 로고
    • The continuing conundrum of the LEA proteins
    • [55] Tunnacliffe, A., Wise, M.J., The continuing conundrum of the LEA proteins. Naturwissenschaften 94 (2007), 791–812.
    • (2007) Naturwissenschaften , vol.94 , pp. 791-812
    • Tunnacliffe, A.1    Wise, M.J.2
  • 56
    • 56349137240 scopus 로고    scopus 로고
    • Biogenesis of mitochondrial outer membrane proteins
    • [56] Walther, D.M., Rapaport, D., Biogenesis of mitochondrial outer membrane proteins. Biochim. Biophys. Acta 1793 (2009), 42–51.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 42-51
    • Walther, D.M.1    Rapaport, D.2
  • 58
    • 78049454129 scopus 로고    scopus 로고
    • Evidence for multiple group 1 late embryogenesis abundant proteins in encysted embryos of Artemia and their organelles
    • [58] Warner, A.H., Miroshnychenko, O., Kozarova, A., Vacratsis, P.O., MacRae, T.H., Kim, J., Clegg, J.S., Evidence for multiple group 1 late embryogenesis abundant proteins in encysted embryos of Artemia and their organelles. J. Biochem. 148 (2010), 581–592.
    • (2010) J. Biochem. , vol.148 , pp. 581-592
    • Warner, A.H.1    Miroshnychenko, O.2    Kozarova, A.3    Vacratsis, P.O.4    MacRae, T.H.5    Kim, J.6    Clegg, J.S.7
  • 59
    • 0003690448 scopus 로고
    • Bound Water in Biological Integrity
    • Charles C Thomas Publications Springfield
    • [59] Webb, S.J., Bound Water in Biological Integrity. 1965, Charles C Thomas Publications, Springfield.
    • (1965)
    • Webb, S.J.1
  • 60
    • 0022556107 scopus 로고
    • Carboxyfluorescein leakage assay for lipoprotein-liposome interaction
    • [60] Weinstein, J.N., Blumenthal, R., Klausner, R.D., Carboxyfluorescein leakage assay for lipoprotein-liposome interaction. Methods Enzymol. 128 (1986), 657–668.
    • (1986) Methods Enzymol. , vol.128 , pp. 657-668
    • Weinstein, J.N.1    Blumenthal, R.2    Klausner, R.D.3
  • 61
    • 0035847037 scopus 로고    scopus 로고
    • Isolation and characterization of a D-7 LEA protein from pollen that stabilizes glasses in vitro
    • [61] Wolkers, W.F., McCready, S., Brandt, W.F., Lindsey, G.G., Hoekstra, F.A., Isolation and characterization of a D-7 LEA protein from pollen that stabilizes glasses in vitro. Biochim. Biophys. Acta 1544 (2001), 196–206.
    • (2001) Biochim. Biophys. Acta , vol.1544 , pp. 196-206
    • Wolkers, W.F.1    McCready, S.2    Brandt, W.F.3    Lindsey, G.G.4    Hoekstra, F.A.5
  • 62
    • 0034964582 scopus 로고    scopus 로고
    • Human platelets loaded with trehalose survive freeze-drying
    • [62] Wolkers, W.F., Walker, N.J., Tablin, F., 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
  • 63
    • 33847034701 scopus 로고    scopus 로고
    • Mitochondria frozen with trehalose retain a number of biological functions and preserve outer membrane integrity
    • [63] Yamaguchi, R., Andreyev, A., Murphy, A.N., Perkins, G.A., Ellisman, M.H., Newmeyer, D.D., Mitochondria frozen with trehalose retain a number of biological functions and preserve outer membrane integrity. Cell Death Differ. 14 (2007), 616–624.
    • (2007) Cell Death Differ. , vol.14 , pp. 616-624
    • Yamaguchi, R.1    Andreyev, A.2    Murphy, A.N.3    Perkins, G.A.4    Ellisman, M.H.5    Newmeyer, D.D.6
  • 64
    • 0020336190 scopus 로고
    • Living with water stress: evolution of osmolyte systems
    • [64] Yancey, P.H., Clark, M.E., Hand, S.C., Bowlus, R.D., Somero, G.N., Living with water stress: evolution of osmolyte systems. Science 217 (1982), 1214–1222.
    • (1982) Science , vol.217 , pp. 1214-1222
    • Yancey, P.H.1    Clark, M.E.2    Hand, S.C.3    Bowlus, R.D.4    Somero, G.N.5
  • 65
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • [65] Zoratti, M., Szabo, I., The mitochondrial permeability transition. Biochim. Biophys. Acta 1241 (1995), 139–176.
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabo, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.