메뉴 건너뛰기




Volumn 11, Issue 95, 2014, Pages

Localization of trehalose in partially hydrated DOPC bilayers: Insights into cryoprotective mechanisms

Author keywords

Anhydrobiology; Cryobiology; Cryoprotection; Lipid membrane; Membrane diffraction

Indexed keywords

CYTOLOGY; DEHYDRATION; DIFFRACTION;

EID: 84901456943     PISSN: 17425689     EISSN: 17425662     Source Type: Journal    
DOI: 10.1098/rsif.2014.0069     Document Type: Article
Times cited : (41)

References (52)
  • 1
    • 0342493327 scopus 로고    scopus 로고
    • Effects of vitrified and nonvitrified sugars on phosphatidylcholine fluid-to-gel phase transitions
    • doi:10.1016/S0006-3495(00)76741-5
    • Koster KL, Lei YP, Anderson M, Martin S, Bryant G. Effects of vitrified and nonvitrified sugars on phosphatidylcholine fluid-to-gel phase transitions. Biophys. J. 78, 1932-1946. (doi:10.1016/S0006-3495(00)76741-5)
    • Biophys. J. , vol.78 , pp. 1932-1946
    • Koster, K.L.1    Lei, Y.P.2    Anderson, M.3    Martin, S.4    Bryant, G.5
  • 2
    • 85032068559 scopus 로고
    • Sugars and desiccation tolerance in seeds
    • doi:10.1104/pp.88.3.829
    • Koster KL, Leopold AC. 1988 Sugars and desiccation tolerance in seeds. Plant Physiol. 88, 829-832. (doi:10.1104/pp.88.3.829)
    • (1988) Plant Physiol. , vol.88 , pp. 829-832
    • Koster, K.L.1    Leopold, A.C.2
  • 3
    • 0028048734 scopus 로고    scopus 로고
    • Interactions between soluble sugars and POPC (1-palmitoyl-2- oleoylphosphatidylcholine) during dehydration: Vitrification of sugars alters the phase behavior of the phospholipid. Biochim
    • doi:10.1016/0005-2736(94) 90343-3
    • Koster KL, Webb MS, Bryant G, Lynch DV. Interactions between soluble sugars and POPC (1-palmitoyl-2-oleoylphosphatidylcholine) during dehydration: vitrification of sugars alters the phase behavior of the phospholipid. Biochim. Biophys. Acta Biomembr. 1193, 143-150. (doi:10.1016/0005-2736(94) 90343-3)
    • Biophys. Acta Biomembr. , vol.1193 , pp. 143-150
    • Koster, K.L.1    Webb, M.S.2    Bryant, G.3    Lynch, D.V.4
  • 4
    • 0348053809 scopus 로고
    • Preservation of membranes in anhydrobiotic organisms: The role of trehalose
    • doi:10.1126/science.223.4637.701
    • Crowe JH, Crowe LM, Chapman D. 1984 Preservation of membranes in anhydrobiotic organisms: the role of trehalose. Science 223, 701-703. (doi:10.1126/science.223.4637.701)
    • (1984) Science , vol.223 , pp. 701-703
    • Crowe, J.H.1    Crowe, L.M.2    Chapman, D.3
  • 5
    • 0022365706 scopus 로고
    • Preservation of freeze-dried liposomes by trehalose
    • doi:10.1016/0003-9861(85)90498-9
    • Crowe LM, Crowe JH, Rudolph A, Womersley C, Appel L. 1985 Preservation of freeze-dried liposomes by trehalose. Arch. Biochem. Biophys. 242, 240-247. (doi:10.1016/0003-9861(85)90498-9)
    • (1985) Arch. Biochem. Biophys. , vol.242 , pp. 240-247
    • Crowe, L.M.1    Crowe, J.H.2    Rudolph, A.3    Womersley, C.4    Appel, L.5
  • 6
    • 0019975858 scopus 로고
    • Cellular responses to extreme water loss: The water-replacement hypothesis
    • doi:10.1016/0011-2240(82)90159-6
    • Clegg JS, Seitz P, Seitz W, Hazlewood CF. 1982 Cellular responses to extreme water loss: the water-replacement hypothesis. Cryobiology 19, 306-316. (doi:10.1016/0011-2240(82)90159-6)
    • (1982) Cryobiology , vol.19 , pp. 306-316
    • Clegg, J.S.1    Seitz, P.2    Seitz, W.3    Hazlewood, C.F.4
  • 7
    • 0026562056 scopus 로고
    • Anhydrobiosis
    • doi:10.1146/annurev.ph.54.030192.003051
    • Crowe JH, Hoekstra FA, Crowe LM. 1992 Anhydrobiosis. Annu. Rev. Physiol. 54, 579-599. (doi:10.1146/annurev.ph.54.030192.003051)
    • (1992) Annu. Rev. Physiol. , vol.54 , pp. 579-599
    • Crowe, J.H.1    Hoekstra, F.A.2    Crowe, L.M.3
  • 8
    • 0029913433 scopus 로고    scopus 로고
    • Stability of dry liposomes in sugar glasses
    • doi:10.1016/S0006-3495(96)79740-0
    • Sun WQ, Leopold AC, Crowe LM, Crowe JH. 1996 Stability of dry liposomes in sugar glasses. Biophys. J. 70, 1769-1776. (doi:10.1016/S0006-3495(96)79740-0)
    • (1996) Biophys. J. , vol.70 , pp. 1769-1776
    • Sun, W.Q.1    Leopold, A.C.2    Crowe, L.M.3    Crowe, J.H.4
  • 9
    • 0036188792 scopus 로고    scopus 로고
    • The trehalose myth revisited: Introduction to a symposium on stabilization of cells in the dry state
    • doi:10.1006/cryo.2001.2353
    • Crowe JH, Crowe LM, Oliver AE, Tsvetkova N, Wolkers W, Tablin F. 2001 The trehalose myth revisited: introduction to a symposium on stabilization of cells in the dry state. Cryobiology 43, 89-105. (doi:10.1006/cryo.2001.2353)
    • (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
  • 10
    • 0029882614 scopus 로고    scopus 로고
    • Is vitrification involved in depression of the phase transition temperature in dry phospholipids?
    • doi:10.1016/0005-2736(95)00287-1
    • Crowe JH, Hoekstra FA, Nguyen KHN, Crowe LM. Is vitrification involved in depression of the phase transition temperature in dry phospholipids? Biochim. Biophys. Acta Biomembr. 1280, 187-196. (doi:10.1016/0005-2736(95)00287-1)
    • Biochim. Biophys. Acta Biomembr. , vol.1280 , pp. 187-196
    • Crowe, J.H.1    Hoekstra, F.A.2    Nguyen, K.H.N.3    Crowe, L.M.4
  • 11
    • 0033690044 scopus 로고    scopus 로고
    • Trehalose interacts with phospholipid polar heads in Langmuir monolayers
    • doi:10.1021/la991641e
    • Lambruschini C, Relini A, Ridi A, Cordone L, Gliozzi A. 2000 Trehalose interacts with phospholipid polar heads in Langmuir monolayers. Langmuir 16, 5467-5470. (doi:10.1021/la991641e)
    • (2000) Langmuir , vol.16 , pp. 5467-5470
    • Lambruschini, C.1    Relini, A.2    Ridi, A.3    Cordone, L.4    Gliozzi, A.5
  • 12
    • 1542360627 scopus 로고    scopus 로고
    • Preservation of dried liposomes in the presence of sugar and phosphate
    • doi:10.1016/j.bbamem.2003.12.006
    • Wolkers WF, Oldenhof H, Tablin F, Crowe JH. 2004 Preservation of dried liposomes in the presence of sugar and phosphate. Biochim. Biophys. Acta Biomembr. 1661, 125-134. (doi:10.1016/j.bbamem.2003.12.006)
    • (2004) Biochim. Biophys. Acta Biomembr. , vol.1661 , pp. 125-134
    • Wolkers, W.F.1    Oldenhof, H.2    Tablin, F.3    Crowe, J.H.4
  • 13
    • 33748282775 scopus 로고    scopus 로고
    • Interaction of the sugars trehalose, maltose and glucose with a phospholipid bilayer: A comparative molecular dynamics study
    • doi:10.1021/jp0607891
    • Pereira CS, Huenenberger PH. 2006 Interaction of the sugars trehalose, maltose and glucose with a phospholipid bilayer: a comparative molecular dynamics study. J. Phys. Chem. B 110, 15 572-15 581. (doi:10.1021/jp0607891)
    • (2006) J. Phys. Chem. B , vol.110 , pp. 15572-15581
    • Pereira, C.S.1    Huenenberger, P.H.2
  • 14
    • 56049125731 scopus 로고    scopus 로고
    • Effect of trehalose on a phospholipid membrane under mechanical stress
    • doi:10.1529/biophysj.108.131656
    • Pereira CS, Hünenberger PH. 2008 Effect of trehalose on a phospholipid membrane under mechanical stress. Biophys. J. 95, 3525-3534. (doi:10.1529/biophysj.108.131656)
    • (2008) Biophys. J. , vol.95 , pp. 3525-3534
    • Pereira, C.S.1    Hünenberger, P.H.2
  • 15
    • 0032697367 scopus 로고    scopus 로고
    • Freezing, drying, and/or vitrification of membrane-solute-water systems
    • doi:10.1006/cryo.1999.2195
    • Wolfe J, Bryant G. 1999 Freezing, drying, and/or vitrification of membrane-solute-water systems. Cryobiology 39, 103-129. (doi:10.1006/cryo.1999. 2195)
    • (1999) Cryobiology , vol.39 , pp. 103-129
    • Wolfe, J.1    Bryant, G.2
  • 16
    • 0034914256 scopus 로고    scopus 로고
    • Membrane behaviour in seeds and other systems at low water content: The various effects of solutes
    • doi:10.1079/SSR200056
    • Bryant G, Koster KL, Wolfe J. 2001 Membrane behaviour in seeds and other systems at low water content: the various effects of solutes. Seed Sci. Res. 11, 17-25. (doi:10.1079/SSR200056)
    • (2001) Seed Sci. Res. , vol.11 , pp. 17-25
    • Bryant, G.1    Koster, K.L.2    Wolfe, J.3
  • 17
    • 33751207114 scopus 로고    scopus 로고
    • Location of sugars in multilamellar membranes at low hydration
    • doi:10.1016/j.physb.2006.05.127
    • Lenné T, Bryant G, Garvey CJ, Keiderling U, Koster KL. 2006 Location of sugars in multilamellar membranes at low hydration. Physica B. Condens. Matter 385-386, 862-864. (doi:10.1016/j.physb.2006.05.127)
    • (2006) Physica B. Condens. Matter , vol.385-386 , pp. 862-864
    • Lenné, T.1    Bryant, G.2    Garvey, C.J.3    Keiderling, U.4    Koster, K.L.5
  • 18
    • 34047253359 scopus 로고
    • 2007 How much solute is needed to inhibit the fluid to gel membrane phase transition at low hydration?
    • doi:10.1016/j.bbamem.2007.01.008
    • Lenné T, Bryant G, Holcomb R, Koster KL. 2007 How much solute is needed to inhibit the fluid to gel membrane phase transition at low hydration? Biochim. Biophys. Acta Biomembr. 1768, 1019-1022. (doi:10.1016/j.bbamem.2007.01. 008)
    • (1768) Biochim. Biophys. Acta Biomembr. , pp. 1019-1022
    • Lenné, T.1    Bryant, G.2    Holcomb, R.3    Koster, K.L.4
  • 19
    • 65249160261 scopus 로고    scopus 로고
    • Effects of sugars on lipid bilayers during dehydration: SAXS/WAXS measurements and quantitative model
    • doi:10.1021/jp808670t
    • Lenné T, Garvey CJ, Koster KL, Bryant G. 2009 Effects of sugars on lipid bilayers during dehydration: SAXS/WAXS measurements and quantitative model. J. Phys. Chem. B 113, 2486-2491. (doi:10.1021/jp808670t)
    • (2009) J. Phys. Chem. B , vol.113 , pp. 2486-2491
    • Lenné, T.1    Garvey, C.J.2    Koster, K.L.3    Bryant, G.4
  • 20
    • 79951634900 scopus 로고    scopus 로고
    • Measurement of glucose exclusion from the fully hydrated DOPE inverse hexagonal phase
    • doi:10.1039/b919086d
    • Kent B, Garvey CJ, Lenne T, Porcar L, Garamus VM, Bryant G. 2010 Measurement of glucose exclusion from the fully hydrated DOPE inverse hexagonal phase. Soft Matter 6, 1197-1202. (doi:10.1039/b919086d)
    • (2010) Soft Matter , vol.6 , pp. 1197-1202
    • Kent, B.1    Garvey, C.J.2    Lenne, T.3    Porcar, L.4    Garamus, V.M.5    Bryant, G.6
  • 21
    • 0028702887 scopus 로고
    • Do trehalose and dimethyl sulfoxide affect intermembrane forces?
    • doi:10.1006/cryo.1994.1064
    • Pincet F, Perez E, Wolfe J. 1994 Do trehalose and dimethyl sulfoxide affect intermembrane forces? Cryobiology 31, 531-539. (doi:10.1006/cryo.1994. 1064)
    • (1994) Cryobiology , vol.31 , pp. 531-539
    • Pincet, F.1    Perez, E.2    Wolfe, J.3
  • 22
    • 0001272229 scopus 로고    scopus 로고
    • The effects of solutes on the freezing properties of and hydration forces in lipid lamellar phases
    • doi:10.1016/S0006-3495(98)77903-2
    • Yoon YH, Pope JM, Wolfe J. 1998 The effects of solutes on the freezing properties of and hydration forces in lipid lamellar phases. Biophys. J. 74, 1949-1965. (doi:10.1016/S0006-3495(98)77903-2)
    • (1998) Biophys. J. , vol.74 , pp. 1949-1965
    • Yoon, Y.H.1    Pope, J.M.2    Wolfe, J.3
  • 23
    • 57249096972 scopus 로고    scopus 로고
    • The inverse hexagonal-inverse ribbon-lamellar gel phase transition sequence in low hydration DOPC:DOPE phospholipid mixtures
    • doi:10.1016/j.chemphyslip.2008.10.003
    • Kent B, Garvey CJ, Cookson D, Bryant G. 2009 The inverse hexagonal-inverse ribbon-lamellar gel phase transition sequence in low hydration DOPC:DOPE phospholipid mixtures. Chem. Phys. Lipids 157, 56-60. (doi:10.1016/j.chemphyslip.2008.10.003)
    • (2009) Chem. Phys. Lipids , vol.157 , pp. 56-60
    • Kent, B.1    Garvey, C.J.2    Cookson, D.3    Bryant, G.4
  • 24
    • 74149087442 scopus 로고    scopus 로고
    • Kinetics of the lamellar gel-fluid transition in phosphatidylcholine membranes in the presence of sugars
    • doi:10.1016/j.chemphyslip.2009.12.001
    • Lenné T, Garvey CJ, Koster KL, Bryant G. 2010 Kinetics of the lamellar gel-fluid transition in phosphatidylcholine membranes in the presence of sugars. Chem. Phys. Lipids 163, 236-242. (doi:10.1016/j.chemphyslip.2009.12. 001)
    • (2010) Chem. Phys. Lipids , vol.163 , pp. 236-242
    • Lenné, T.1    Garvey, C.J.2    Koster, K.L.3    Bryant, G.4
  • 25
    • 79952167898 scopus 로고    scopus 로고
    • Reconciliation of opposing views on membrane-sugar interactions
    • doi:10.1073/pnas.1012516108
    • Andersen HD, Wang C, Arleth L, Peters GH, Westh P. Reconciliation of opposing views on membrane-sugar interactions. Proc. Natl Acad. Sci. USA 108, 1874-1878. (doi:10.1073/pnas.1012516108)
    • Proc. Natl Acad. Sci. USA , vol.108 , pp. 1874-1878
    • Andersen, H.D.1    Wang, C.2    Arleth, L.3    Peters, G.H.4    Westh, P.5
  • 26
    • 0018792901 scopus 로고
    • Neutron diffraction studies on phosphatidylcholine model membranes. I. Head group conformation
    • doi:10.1016/0022-2836(79)90479-0
    • Buldt G, Gally HU, Seelig J, Zaccai G. 1979 Neutron diffraction studies on phosphatidylcholine model membranes. I. Head group conformation. J. Mol. Biol. 134, 673-691. (doi:10.1016/0022-2836(79)90479-0)
    • (1979) J. Mol. Biol. , vol.134 , pp. 673-691
    • Buldt, G.1    Gally, H.U.2    Seelig, J.3    Zaccai, G.4
  • 27
    • 77954214722 scopus 로고    scopus 로고
    • Applications of neutron and X-ray scattering to the study of biologically relevant model membranes
    • doi:10.1016/j.chemphyslip.2010.03.010
    • Pabst G, Kucerka N, Nieh MP, Rheinstädter MC, Katsaras J. 2010 Applications of neutron and X-ray scattering to the study of biologically relevant model membranes. Chem. Phys. Lipids 163, 460-479. (doi:10.1016/j. chemphyslip.2010.03.010)
    • (2010) Chem. Phys. Lipids , vol.163 , pp. 460-479
    • Pabst, G.1    Kucerka, N.2    Nieh, M.P.3    Rheinstädter, M.C.4    Katsaras, J.5
  • 28
    • 0026729232 scopus 로고
    • Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of X-ray and neutron-diffraction data. III. Complete structure
    • doi:10.1016/S0006-3495(92)81849-0
    • Wiener MC, White SH. 1992 Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of X-ray and neutron-diffraction data. III. Complete structure. Biophys. J. 61, 434-447. (doi:10.1016/S0006-3495(92)81849-0)
    • (1992) Biophys. J. , vol.61 , pp. 434-447
    • Wiener, M.C.1    White, S.H.2
  • 29
    • 0017232478 scopus 로고
    • Structural analysis of hydrated egg lecithin and cholesterol bilayers. II. Neutron diffraction
    • doi:10.1016/S0022-2836(76)80068-X
    • Worcester DL, Franks NP. 1976 Structural analysis of hydrated egg lecithin and cholesterol bilayers. II. Neutron diffraction. J. Mol. Biol. 100, 359-378. (doi:10.1016/S0022-2836(76)80068-X)
    • (1976) J. Mol. Biol. , vol.100 , pp. 359-378
    • Worcester, D.L.1    Franks, N.P.2
  • 30
    • 0018597218 scopus 로고
    • The structure of lipid bilayers and the effects of general anaesthetics: An X-ray and neutron diffraction study
    • doi:10.1016/0022-2836(79)90403-0
    • Franks NP, Lieb WR. 1979 The structure of lipid bilayers and the effects of general anaesthetics: an X-ray and neutron diffraction study. J. Mol. Biol. 133, 469-500. (doi:10.1016/0022-2836(79)90403-0)
    • (1979) J. Mol. Biol. , vol.133 , pp. 469-500
    • Franks, N.P.1    Lieb, W.R.2
  • 31
    • 77956302956 scopus 로고    scopus 로고
    • Structure from substrate supported lipid bilayers
    • (review). doi:10.1116/1.2992133
    • Katsaras J, Kucerka N, Nieh MP. 2008 Structure from substrate supported lipid bilayers (review). Biointerphases 3, FB55-FB63. (doi:10.1116/1.2992133)
    • (2008) Biointerphases , vol.3
    • Katsaras, J.1    Kucerka, N.2    Nieh, M.P.3
  • 32
    • 51649129838 scopus 로고    scopus 로고
    • Lipid bilayer structure determined by the simultaneous analysis of neutron and X-ray scattering data
    • doi:10.1529/biophysj.108.132662
    • Kucerka N, Nagle JF, Sachs JN, Feller SE, Pencer J, Jackson A, Katsaras J. 2008 Lipid bilayer structure determined by the simultaneous analysis of neutron and X-ray scattering data. Biophys. J. 95, 2356-2367. (doi:10.1529/biophysj.108.132662)
    • (2008) Biophys. J. , vol.95 , pp. 2356-2367
    • Kucerka, N.1    Nagle, J.F.2    Sachs, J.N.3    Feller, S.E.4    Pencer, J.5    Jackson, A.6    Katsaras, J.7
  • 34
    • 0036842021 scopus 로고    scopus 로고
    • Beta-amyloid 25 to 35 is intercalated in anionic and zwitterionic lipid membranes to different extents
    • doi:10.1016/S0006-3495(02)75271-5
    • Dante S, Hauss T, Dencher NA. 2002 Beta-amyloid 25 to 35 is intercalated in anionic and zwitterionic lipid membranes to different extents. Biophys. J. 83, 2610-2616. (doi:10.1016/S0006-3495(02)75271-5)
    • (2002) Biophys. J. , vol.83 , pp. 2610-2616
    • Dante, S.1    Hauss, T.2    Dencher, N.A.3
  • 35
    • 27644585264 scopus 로고    scopus 로고
    • Localization of coenzyme Q(10) in the center of a deuterated lipid membrane by neutron diffraction
    • doi:10.1016/j.bbabio.2005.08.007
    • Hauss T, Dante S, Haines TH, Dencher NA. 2005 Localization of coenzyme Q(10) in the center of a deuterated lipid membrane by neutron diffraction. Biochim. Biophys. Acta Bioenerg. 1710, 57-62. (doi:10.1016/j.bbabio.2005.08.007)
    • (2005) Biochim. Biophys. Acta Bioenerg. , vol.1710 , pp. 57-62
    • Hauss, T.1    Dante, S.2    Haines, T.H.3    Dencher, N.A.4
  • 36
    • 0035144532 scopus 로고    scopus 로고
    • Structure, location, and lipid perturbations of melittin at the membrane interface
    • doi:10.1016/S0006-3495(01)76059-6
    • Hristova K, Dempsey C, White S. 2001 Structure, location, and lipid perturbations of melittin at the membrane interface. Biophys. J. 80, 801-811. (doi:10.1016/S0006-3495(01)76059-6)
    • (2001) Biophys. J. , vol.80 , pp. 801-811
    • Hristova, K.1    Dempsey, C.2    White, S.3
  • 37
    • 0029594533 scopus 로고
    • Membrane thinning caused by magainin 2
    • doi:10.1021/bi00051a026
    • Ludtke S, He K, Huang H. 1995 Membrane thinning caused by magainin 2. Biochemistry 34, 16 764- 16 769. (doi:10.1021/bi00051a026)
    • (1995) Biochemistry , vol.34 , pp. 16764-16769
    • Ludtke, S.1    He, K.2    Huang, H.3
  • 38
    • 84868271598 scopus 로고    scopus 로고
    • Neutron diffraction studies of the interaction between amphotericin B and lipid-sterol model membranes
    • doi:10.1038/srep00778
    • Foglia F, Lawrence MJ, Deme? B, Fragneto G, Barlow D. 2012 Neutron diffraction studies of the interaction between amphotericin B and lipid-sterol model membranes. Sci. Rep. 2, 778. (doi:10.1038/srep00778)
    • (2012) Sci. Rep. , vol.2 , pp. 778
    • Foglia, F.1    Lawrence, M.J.2    Deme, B.3    Fragneto, G.4    Barlow, D.5
  • 39
    • 4243221672 scopus 로고
    • A novel method for specific labelling of carbohydrates with deuterium by catalytic exchange
    • doi:10.1016/S0008-6215(00)83319-4
    • Koch HJ, Stuart RS. 1977 A novel method for specific labelling of carbohydrates with deuterium by catalytic exchange. Carbohydr. Res. 59, C1-C6. (doi:10.1016/S0008-6215(00)83319-4)
    • (1977) Carbohydr. Res. , vol.59
    • Koch, H.J.1    Stuart, R.S.2
  • 40
    • 0006474399 scopus 로고
    • The catalytic C-deuteration of some carbohydrate derivatives
    • doi:10.1016/S0008-6215(00)84123-3
    • Koch HJ, Stuart RS. 1978 The catalytic C-deuteration of some carbohydrate derivatives. Carbohydr. Res. 67, 341-348. (doi:10.1016/S0008-6215(00)84123-3)
    • (1978) Carbohydr. Res. , vol.67 , pp. 341-348
    • Koch, H.J.1    Stuart, R.S.2
  • 41
    • 33751206213 scopus 로고    scopus 로고
    • Neutron diffraction studies of fluid bilayers with transmembrane proteins: Structural consequences of the achondroplasia mutation
    • doi:10.1529/biophysj.106.092247
    • Han X, Mihailescu M, Hristova K. 2006 Neutron diffraction studies of fluid bilayers with transmembrane proteins: structural consequences of the achondroplasia mutation. Biophys. J. 91, 3736-3747. (doi:10.1529/biophysj.106. 092247)
    • (2006) Biophys. J. , vol.91 , pp. 3736-3747
    • Han, X.1    Mihailescu, M.2    Hristova, K.3
  • 42
    • 0038575707 scopus 로고    scopus 로고
    • Exclusion of maltodextrins from phosphatidylcholine multilayers during dehydration: Effects on membrane phase behaviour
    • Koster KL, Maddocks KJ, Bryant G. 2003 Exclusion of maltodextrins from phosphatidylcholine multilayers during dehydration: effects on membrane phase behaviour. Eur. Biophys. J. Biophys. Lett. 32, 96-105. (Pubitemid 36749527)
    • (2003) European Biophysics Journal , vol.32 , Issue.2 , pp. 96-105
    • Koster, K.L.1    Maddocks, K.J.2    Bryant, G.3
  • 43
    • 0034496684 scopus 로고    scopus 로고
    • Measurement of sugar depletion from uncharged lamellar phases by SANS contrast variation
    • doi:10.1107/S0021889899013680
    • Deme B, Zemb T. 2000 Measurement of sugar depletion from uncharged lamellar phases by SANS contrast variation. J. Appl. Crystallogr. 33, 569-573. (doi:10.1107/S0021889899013680)
    • (2000) J. Appl. Crystallogr. , vol.33 , pp. 569-573
    • Deme, B.1    Zemb, T.2
  • 44
    • 0020477017 scopus 로고
    • Stabilization of protein-structure by sugars
    • doi:10.1021/bi00268a033
    • Arakawa T, Timasheff SN. 1982 Stabilization of protein-structure by sugars. Biochemistry 21, 6536-6544. (doi:10.1021/bi00268a033)
    • (1982) Biochemistry , vol.21 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 45
    • 0034035899 scopus 로고    scopus 로고
    • Probing protein-sugar interactions
    • doi:10.1016/S0006-3495(00)76601-X
    • Ebel C, Eisenberg H, Ghirlando R. 2000 Probing protein-sugar interactions. Biophys. J. 78, 385-393. (doi:10.1016/S0006-3495(00)76601-X)
    • (2000) Biophys. J. , vol.78 , pp. 385-393
    • Ebel, C.1    Eisenberg, H.2    Ghirlando, R.3
  • 46
    • 0025356674 scopus 로고
    • The role of trehalose as a substitute for nitrogen-containing compatible solutes (ectothiorhodospira-halochloris)
    • doi:10.1007/BF00245273
    • Galinski EA, Herzog RM. 1990 The role of trehalose as a substitute for nitrogen-containing compatible solutes (ectothiorhodospira-halochloris). Arch. Microbiol. 153, 607-613. (doi:10.1007/BF00245273)
    • (1990) Arch. Microbiol. , vol.153 , pp. 607-613
    • Galinski, E.A.1    Herzog, R.M.2
  • 47
    • 0019872622 scopus 로고
    • Mechanism of protein stabilization by glycerol - Preferential hydration in glycerol-water mixtures
    • doi:10.1021/bi00519a023
    • Gekko K, Timasheff SN. 1981 Mechanism of protein stabilization by glycerol - preferential hydration in glycerol-water mixtures. Biochemistry 20, 4667-4676. (doi:10.1021/bi00519a023)
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2
  • 48
    • 0021769831 scopus 로고
    • Neutron small-angle scattering studies of ribonuclease in mixed aqueous solutions and determination of the preferentially bound water
    • doi:10.1021/bi00304a008
    • Lehmann MS, Zaccai G. 1984 Neutron small-angle scattering studies of ribonuclease in mixed aqueous solutions and determination of the preferentially bound water. Biochemistry 23, 1939-1942. (doi:10.1021/bi00304a008)
    • (1984) Biochemistry , vol.23 , pp. 1939-1942
    • Lehmann, M.S.1    Zaccai, G.2
  • 49
    • 0142216204 scopus 로고    scopus 로고
    • Resurrecting Van Leeuwenhoek's rotifers: A reappraisal of the role of disaccharides in anhydrobiosis
    • doi:10.1098/rstb.2002.1214
    • Tunnacliffe A, Lapinski J. 2003 Resurrecting Van Leeuwenhoek's rotifers: a reappraisal of the role of disaccharides in anhydrobiosis. Phil. Trans. R. Soc. Lond. B 358, 1755-1771. (doi:10.1098/rstb.2002.1214)
    • (2003) Phil. Trans. R. Soc. Lond. B , vol.358 , pp. 1755-1771
    • Tunnacliffe, A.1    Lapinski, J.2
  • 50
    • 0001198203 scopus 로고
    • The role of trehalose in dehydration resistance of Saccharomyces cerevisiae
    • doi:10.1111/j.1574-6968.1987.tb02551.x
    • Gadd GM, Chalmers K, Reed RH. 1987 The role of trehalose in dehydration resistance of Saccharomyces cerevisiae. FEMS Microbiol. Lett. 48, 249-254. (doi:10.1111/j.1574-6968.1987.tb02551.x)
    • (1987) FEMS Microbiol. Lett. , vol.48 , pp. 249-254
    • Gadd, G.M.1    Chalmers, K.2    Reed, R.H.3
  • 51
    • 0242385390 scopus 로고    scopus 로고
    • Molecular simulation study of phospholipid bilayers and insights of the interactions with disaccharides
    • doi:10.1016/S0006- 3495(03)74706-7
    • Sum AK, Faller R, Pablo JJd. 2003 Molecular simulation study of phospholipid bilayers and insights of the interactions with disaccharides. Biophys. J. 85, 2830-2844. (doi:10.1016/S0006- 3495(03)74706-7)
    • (2003) Biophys. J. , vol.85 , pp. 2830-2844
    • Sum, A.K.1    Faller, R.2    Pablo, J.3
  • 52
    • 84873386975 scopus 로고    scopus 로고
    • Taste of sugar at the membrane: Thermodynamics and kinetics of the interaction of a disaccharide with lipid bilayers
    • doi:10.1016/j.bpj.2012.12.011
    • Tian J, Sethi A, Swanson BI, Goldstein B, Gnanakaran S. Taste of sugar at the membrane: thermodynamics and kinetics of the interaction of a disaccharide with lipid bilayers. Biophys. J. 104, 622-632. (doi:10.1016/j.bpj.2012.12.011)
    • Biophys. J. , vol.104 , pp. 622-632
    • Tian, J.1    Sethi, A.2    Swanson, B.I.3    Goldstein, B.4    Gnanakaran, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.