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Volumn 18, Issue 1, 2009, Pages 24-36

Effect of trehalose on protein structure

Author keywords

Anhydrobiosis; Carbohydrates; Protein structure; Trehalose

Indexed keywords

TREHALOSE;

EID: 58149477054     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.3     Document Type: Review
Times cited : (708)

References (113)
  • 1
    • 33748588165 scopus 로고    scopus 로고
    • Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant
    • Ignatova Z, Gierasch LM (2006) Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant. Proc Natl Acad Sci USA 103:13357-13361.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13357-13361
    • Ignatova, Z.1    Gierasch, L.M.2
  • 2
    • 35748959041 scopus 로고    scopus 로고
    • Effects of osmolytes on protein folding and aggregation in cells
    • Ignatova Z, Gierasch LM (2007) Effects of osmolytes on protein folding and aggregation in cells. Methods Enzymol 428:355-372.
    • (2007) Methods Enzymol , vol.428 , pp. 355-372
    • Ignatova, Z.1    Gierasch, L.M.2
  • 4
    • 33745479868 scopus 로고    scopus 로고
    • Forced and natural convective drying of trehalose/water thin films: Implication in the desiccation preservation of mammalian cells
    • Chen B, Fowler A, Bhowmick S (2006) Forced and natural convective drying of trehalose/water thin films: implication in the desiccation preservation of mammalian cells. J Biomech Eng 128:335-346.
    • (2006) J Biomech Eng , vol.128 , pp. 335-346
    • Chen, B.1    Fowler, A.2    Bhowmick, S.3
  • 5
    • 33646128944 scopus 로고    scopus 로고
    • Molecular dynamic simulations of trehalose as a 'dynamic reducer' for solvent water molecules in the hydration shell
    • Choi Y, Cho KW, Jeong K, Jung S (2006) Molecular dynamic simulations of trehalose as a 'dynamic reducer' for solvent water molecules in the hydration shell. Carbohydr Res 341:1020-1028.
    • (2006) Carbohydr Res , vol.341 , pp. 1020-1028
    • Choi, Y.1    Cho, K.W.2    Jeong, K.3    Jung, S.4
  • 7
    • 15044350325 scopus 로고    scopus 로고
    • Ramachandran free-energy surfaces for disaccharides: Trehalose, a case study
    • Kuttel MM, Naidoo KJ (2005) Ramachandran free-energy surfaces for disaccharides: trehalose, a case study. Carbohydr Res 340:875-879.
    • (2005) Carbohydr Res , vol.340 , pp. 875-879
    • Kuttel, M.M.1    Naidoo, K.J.2
  • 8
    • 20544474519 scopus 로고    scopus 로고
    • How homogeneous are the trehalose, maltose, and sucrose water solutions? An insight from molecular dynamics simulations
    • Lerbret A, Bordat P, Affouard F, Descamps M, Migliardo F (2005) How homogeneous are the trehalose, maltose, and sucrose water solutions? An insight from molecular dynamics simulations. J Phys Chem B 109:11046-11057.
    • (2005) J Phys Chem B , vol.109 , pp. 11046-11057
    • Lerbret, A.1    Bordat, P.2    Affouard, F.3    Descamps, M.4    Migliardo, F.5
  • 9
    • 15044339135 scopus 로고    scopus 로고
    • Influence of homologous disaccharides on the hydrogen-bond network of water: Complementary Raman scattering experiments and molecular dynamics simulations
    • Lerbret A, Bordat P, Affouard F, Guinet Y, Hedoux A, Paccou L, Prevost D, Descamps M (2005) Influence of homologous disaccharides on the hydrogen-bond network of water: complementary Raman scattering experiments and molecular dynamics simulations. Carbohydr Res 340:881-887.
    • (2005) Carbohydr Res , vol.340 , pp. 881-887
    • Lerbret, A.1    Bordat, P.2    Affouard, F.3    Guinet, Y.4    Hedoux, A.5    Paccou, L.6    Prevost, D.7    Descamps, M.8
  • 10
    • 28444433692 scopus 로고    scopus 로고
    • Correlation between bioprotective effectiveness and dynamic properties of trehalose-water, maltose-water and sucrose-water mixtures
    • Magazú S, Migliardo F, Mondelli C, Vadala M (2005) Correlation between bioprotective effectiveness and dynamic properties of trehalose-water, maltose-water and sucrose-water mixtures. Carbohydr Res 340:2796-2801.
    • (2005) Carbohydr Res , vol.340 , pp. 2796-2801
    • Magazú, S.1    Migliardo, F.2    Mondelli, C.3    Vadala, M.4
  • 12
    • 33644942100 scopus 로고    scopus 로고
    • Metabolic engineering of Corynebacterium glutamicum for trehalose over production: Role of the TreYZ trehalose biosynthetic pathway
    • Carpinelli J, Kraemer R, Agosin E (2006) Metabolic engineering of Corynebacterium glutamicum for trehalose over production: role of the TreYZ trehalose biosynthetic pathway. Appl Environ Microbiol 72:1949-1955.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 1949-1955
    • Carpinelli, J.1    Kraemer, R.2    Agosin, E.3
  • 13
    • 33144481515 scopus 로고    scopus 로고
    • Characterisation of the tre locus and analysis of trehalose cryoprotection in Lactobacillus acidophilus NCFM
    • Duong T, Barrangou R, Russell WM, Klaenhammer TR (2006) Characterisation of the tre locus and analysis of trehalose cryoprotection in Lactobacillus acidophilus NCFM. Appl Environ Microbiol 72:1218-1225.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 1218-1225
    • Duong, T.1    Barrangou, R.2    Russell, W.M.3    Klaenhammer, T.R.4
  • 16
    • 32544442207 scopus 로고    scopus 로고
    • Non-equivalence oFD- anDL-trehalose in stabilizing alkaline phosphatase against freeze-drying and thermal stress. Is chiral recognition involved?
    • Haines AH (2006) Non-equivalence oFD- anDL-trehalose in stabilizing alkaline phosphatase against freeze-drying and thermal stress. Is chiral recognition involved? Org Biomol Chem 4:702-706.
    • (2006) Org Biomol Chem , vol.4 , pp. 702-706
    • Haines, A.H.1
  • 17
    • 33645537217 scopus 로고    scopus 로고
    • The role of a gene cluster for trehalose metabolism in dehydration tolerance of the filamentous cyanobacterium Anabaena sp. PCC 7120
    • Higo A, Katoh H, Ohmori K, Ikeuchi M, Ohmori M (2006) The role of a gene cluster for trehalose metabolism in dehydration tolerance of the filamentous cyanobacterium Anabaena sp. PCC 7120. Microbiology 152:979-987.
    • (2006) Microbiology , vol.152 , pp. 979-987
    • Higo, A.1    Katoh, H.2    Ohmori, K.3    Ikeuchi, M.4    Ohmori, M.5
  • 18
    • 0038376258 scopus 로고    scopus 로고
    • Study oftrehalose addition on aroma retention in dehydrated strawberry puree
    • Komes D, Lovrić T, Ganić KK, Gracin L (2003) Study oftrehalose addition on aroma retention in dehydrated strawberry puree. Food Technol Biotechnol 41:111-120.
    • (2003) Food Technol Biotechnol , vol.41 , pp. 111-120
    • Komes, D.1    Lovrić, T.2    Ganić, K.K.3    Gracin, L.4
  • 20
    • 0036664543 scopus 로고    scopus 로고
    • Novel functions and applications of trehalose
    • Higashiyama T (2002) Novel functions and applications of trehalose. Pure Appl Chem 74:1263-1269.
    • (2002) Pure Appl Chem , vol.74 , pp. 1263-1269
    • Higashiyama, T.1
  • 22
    • 0031719418 scopus 로고    scopus 로고
    • Uptake and synthesis of compatible solutes as microbial stress responses to high-osmolality environments
    • Kempf B, Bremer E (1998) Uptake and synthesis of compatible solutes as microbial stress responses to high-osmolality environments. Arch Microbiol 170:319-330.
    • (1998) Arch Microbiol , vol.170 , pp. 319-330
    • Kempf, B.1    Bremer, E.2
  • 24
    • 0035862420 scopus 로고    scopus 로고
    • Changes in glycogen and trehalose content of Streptomyces brasiliensis during growth in liquid cultures under sporulating and non-sporulating conditions
    • Rueda B, Miguelez EM, Hardisson C, Manzanal MB (2001) Changes in glycogen and trehalose content of Streptomyces brasiliensis during growth in liquid cultures under sporulating and non-sporulating conditions. FEMS Microbiol Lett 194:181-185.
    • (2001) FEMS Microbiol Lett , vol.194 , pp. 181-185
    • Rueda, B.1    Miguelez, E.M.2    Hardisson, C.3    Manzanal, M.B.4
  • 25
    • 0036182386 scopus 로고    scopus 로고
    • Lessons from nature: The role of sugar in anhydrobiosis
    • Crowe LM (2002) Lessons from nature: the role of sugar in anhydrobiosis. Comp Biochem Phys A 131:505-513.
    • (2002) Comp Biochem Phys A , vol.131 , pp. 505-513
    • Crowe, L.M.1
  • 26
    • 33745217856 scopus 로고    scopus 로고
    • Trans-cyclopropanation of mycolic acids on trehalose dimycolate suppresses Mycobacterium tuberculosis-induced inflammation and virulence
    • Rao V, Gao F, Chen B, Jacobs WR, Jr, Glickman MS (2006) Trans-cyclopropanation of mycolic acids on trehalose dimycolate suppresses Mycobacterium tuberculosis-induced inflammation and virulence. J Clin Invest 116:1660-1667.
    • (2006) J Clin Invest , vol.116 , pp. 1660-1667
    • Rao, V.1    Gao, F.2    Chen, B.3    Jacobs Jr, W.R.4    Glickman, M.S.5
  • 27
    • 0036276818 scopus 로고    scopus 로고
    • Sugar sensing and signaling in plants
    • Rolland F, Moore B, Sheen J (2002) Sugar sensing and signaling in plants. Plant Cell 14:s185-s205.
    • (2002) Plant Cell , vol.14
    • Rolland, F.1    Moore, B.2    Sheen, J.3
  • 28
    • 0037243170 scopus 로고    scopus 로고
    • Is trehalose-6-phosphate a regulator of sugar metabolism in plants?
    • Eastmond PJ, Graham IA (2003) Is trehalose-6-phosphate a regulator of sugar metabolism in plants? J Exp Bot 54:533-537.
    • (2003) J Exp Bot , vol.54 , pp. 533-537
    • Eastmond, P.J.1    Graham, I.A.2
  • 29
    • 0035036160 scopus 로고    scopus 로고
    • Trehalose protects corneal epithelial cells from death by drying
    • Matsuo T (2001) Trehalose protects corneal epithelial cells from death by drying. Br J Ophthalmol 85:610-612.
    • (2001) Br J Ophthalmol , vol.85 , pp. 610-612
    • Matsuo, T.1
  • 30
    • 58149461510 scopus 로고    scopus 로고
    • Compositions and methods for wound management. Official Gazette US Pat Trademark
    • Office 1232:424-448
    • Norcia MA (2000) Compositions and methods for wound management. Official Gazette US Pat Trademark Office 1232:424-448.
    • (2000)
    • Norcia, M.A.1
  • 33
    • 48149089155 scopus 로고    scopus 로고
    • Role of trehalose in moisture-induced aggregation of bovine serum albumin
    • Jain NK, Roy I (2008) Role of trehalose in moisture-induced aggregation of bovine serum albumin. Eur J Pharm Biopharm 69:824-834.
    • (2008) Eur J Pharm Biopharm , vol.69 , pp. 824-834
    • Jain, N.K.1    Roy, I.2
  • 34
    • 0028487168 scopus 로고
    • Is vitrification sufficient to preserve liposomes during freeze-drying?
    • Crowe JH, Leslie SM, Crowe LM (1994) Is vitrification sufficient to preserve liposomes during freeze-drying? Cryobiology 31:355-366.
    • (1994) Cryobiology , vol.31 , pp. 355-366
    • Crowe, J.H.1    Leslie, S.M.2    Crowe, L.M.3
  • 35
  • 36
    • 0031195261 scopus 로고    scopus 로고
    • Cytoplasmic vitrification and survival of anhydrobiotic organisms
    • Sun WQ, Leopold AC (1997) Cytoplasmic vitrification and survival of anhydrobiotic organisms. Comp Biochem Physiol 117A:327-333.
    • (1997) Comp Biochem Physiol , vol.117 A , pp. 327-333
    • Sun, W.Q.1    Leopold, A.C.2
  • 38
    • 0036156006 scopus 로고    scopus 로고
    • Beneficial effect of microinjected trehalose on the cryosurvival of human oocytes
    • Eroglu A, Toner M, Toth TL (2002) Beneficial effect of microinjected trehalose on the cryosurvival of human oocytes. Fertil Steril 77:152-158.
    • (2002) Fertil Steril , vol.77 , pp. 152-158
    • Eroglu, A.1    Toner, M.2    Toth, T.L.3
  • 39
    • 0029882614 scopus 로고    scopus 로고
    • Is vitrification involved in depression of the phase transition temperature in dry phospholipids?
    • Crowe JH, Hoekstra FA, Nguyen KHN, Crowe LM (1996) Is vitrification involved in depression of the phase transition temperature in dry phospholipids? Biochim Biophys Acta 1280:187-196.
    • (1996) Biochim Biophys Acta , vol.1280 , pp. 187-196
    • Crowe, J.H.1    Hoekstra, F.A.2    Nguyen, K.H.N.3    Crowe, L.M.4
  • 40
    • 0034747104 scopus 로고    scopus 로고
    • 2 deprivation in drosophila: Novel approaches using genetic models
    • 2 deprivation in drosophila: novel approaches using genetic models. Neuroscientist 7:538-550.
    • (2001) Neuroscientist , vol.7 , pp. 538-550
    • Haddad, G.G.1    Ma, E.2
  • 41
    • 4644236078 scopus 로고    scopus 로고
    • Role of trehalose phosphate synthase and trehalose during hypoxia: From flies to mammals
    • Chen Q, Haddad GG (2004) Role of trehalose phosphate synthase and trehalose during hypoxia: from flies to mammals. J Exp Biol 207:3125-3129.
    • (2004) J Exp Biol , vol.207 , pp. 3125-3129
    • Chen, Q.1    Haddad, G.G.2
  • 43
    • 29644437591 scopus 로고    scopus 로고
    • Wild-type PABPN1 is anti-apoptotic and reduces toxicity of the oculopharyngeal muscular dystrophy mutation
    • Davies JE, Sarkar S, Rubinsztein DC (2006) Wild-type PABPN1 is anti-apoptotic and reduces toxicity of the oculopharyngeal muscular dystrophy mutation. Hum Mol Genet 15:23-31.
    • (2006) Hum Mol Genet , vol.15 , pp. 23-31
    • Davies, J.E.1    Sarkar, S.2    Rubinsztein, D.C.3
  • 45
    • 24044483249 scopus 로고    scopus 로고
    • Trehalose differentially inhibits aggregation and neurotoxicity of beta amyloid 40 and 42
    • Liu R, Barkhordarian H, Emadi S, Park CB, Sierks MR (2005) Trehalose differentially inhibits aggregation and neurotoxicity of beta amyloid 40 and 42. Neurobiol Dis 20:74-81.
    • (2005) Neurobiol Dis , vol.20 , pp. 74-81
    • Liu, R.1    Barkhordarian, H.2    Emadi, S.3    Park, C.B.4    Sierks, M.R.5
  • 47
    • 0033771067 scopus 로고    scopus 로고
    • Physiological roles of trehalose in bacteria and yeasts: A comparative analysis
    • Arguelles JC (2000) Physiological roles of trehalose in bacteria and yeasts: a comparative analysis. Arch Microbiol 174:217-224.
    • (2000) Arch Microbiol , vol.174 , pp. 217-224
    • Arguelles, J.C.1
  • 48
    • 35548957871 scopus 로고    scopus 로고
    • Tardigrades as a potential model organism in space research
    • Jönsson KI (2007) Tardigrades as a potential model organism in space research. Astrobiology 7:757-766.
    • (2007) Astrobiology , vol.7 , pp. 757-766
    • Jönsson, K.I.1
  • 49
    • 0025325884 scopus 로고
    • Brush border enzymes in coeliac disease: Histochemical evaluation
    • Mercer J, Eagles ME, Talbot IC (1990) Brush border enzymes in coeliac disease: histochemical evaluation. J Clin Pathol 43:307-312.
    • (1990) J Clin Pathol , vol.43 , pp. 307-312
    • Mercer, J.1    Eagles, M.E.2    Talbot, I.C.3
  • 50
  • 51
    • 0015061292 scopus 로고
    • Trehalose malabsorption causing intolerance to mushrooms. Report of a probable case
    • Bergoz R (1971) Trehalose malabsorption causing intolerance to mushrooms. Report of a probable case. Gastroenterology 60:909-912.
    • (1971) Gastroenterology , vol.60 , pp. 909-912
    • Bergoz, R.1
  • 52
    • 0038379784 scopus 로고    scopus 로고
    • An investigation into the crystallisation of α,α-trehalose from the amorphous state
    • McGarvey OS, Kett VL, Craig DQM (2003) An investigation into the crystallisation of α,α-trehalose from the amorphous state. J Phys Chem B 107:6614-6620.
    • (2003) J Phys Chem B , vol.107 , pp. 6614-6620
    • McGarvey, O.S.1    Kett, V.L.2    Craig, D.Q.M.3
  • 53
  • 54
    • 0035975159 scopus 로고    scopus 로고
    • Reversible dehydration of trehalose and anhydrobiosis: From solution state to an exotic crystal?
    • Sussich F, Skopec C, Brady J, Cesaro A (2001) Reversible dehydration of trehalose and anhydrobiosis: from solution state to an exotic crystal? Carbohydr Res 334:165-176.
    • (2001) Carbohydr Res , vol.334 , pp. 165-176
    • Sussich, F.1    Skopec, C.2    Brady, J.3    Cesaro, A.4
  • 55
    • 0001478780 scopus 로고
    • The crystal and molecular structure of trehalose dihydrate
    • Taga T, Senma M, Osaki K (1972) The crystal and molecular structure of trehalose dihydrate. Acta Crystallogr B 28:3258-3263.
    • (1972) Acta Crystallogr B , vol.28 , pp. 3258-3263
    • Taga, T.1    Senma, M.2    Osaki, K.3
  • 56
    • 0022434080 scopus 로고
    • The crystal structure of anhydrous alpha,alpha-trehalose at -150 degrees
    • Jeffrey GA, Nanni R (1985) The crystal structure of anhydrous alpha,alpha-trehalose at -150 degrees. Carbohydr Res 137:21-30.
    • (1985) Carbohydr Res , vol.137 , pp. 21-30
    • Jeffrey, G.A.1    Nanni, R.2
  • 57
    • 0242350327 scopus 로고    scopus 로고
    • Influence of dry conditions on dehydration of α,α-trehalose dihydrate
    • Nagase H, Endo T, Ueda H, Nakai T (2003) Influence of dry conditions on dehydration of α,α-trehalose dihydrate. STP Pharm Sci 13:269-275.
    • (2003) STP Pharm Sci , vol.13 , pp. 269-275
    • Nagase, H.1    Endo, T.2    Ueda, H.3    Nakai, T.4
  • 60
    • 33845184276 scopus 로고
    • Phase relations and vitrification in saccharide-water solutions and the trehalose anomaly
    • Green JL, Angell CA (1989) Phase relations and vitrification in saccharide-water solutions and the trehalose anomaly. J Phys Chem 93:2880-2882.
    • (1989) J Phys Chem , vol.93 , pp. 2880-2882
    • Green, J.L.1    Angell, C.A.2
  • 61
    • 0027526185 scopus 로고
    • Melting and glass transitions of low molecular weight carbohydrates
    • Roos Y (1993) Melting and glass transitions of low molecular weight carbohydrates. Carbohydr Res 238:39-48.
    • (1993) Carbohydr Res , vol.238 , pp. 39-48
    • Roos, Y.1
  • 62
    • 0030921176 scopus 로고    scopus 로고
    • Molecular dynamics studies of the hydration of α,α-trehalose
    • Liu Q, Schmidt RK, Teo B, Karplus PA, Bray JW (1997) Molecular dynamics studies of the hydration of α,α-trehalose. J Am Chem Soc 119:7851-7862.
    • (1997) J Am Chem Soc , vol.119 , pp. 7851-7862
    • Liu, Q.1    Schmidt, R.K.2    Teo, B.3    Karplus, P.A.4    Bray, J.W.5
  • 63
    • 0034043093 scopus 로고    scopus 로고
    • Literature review: Supplemented phase diagram of the trehalose-water binary mixture
    • Chen T, Fowler A, Toner M (2000) Literature review: supplemented phase diagram of the trehalose-water binary mixture. Cryobiology 40:277-282.
    • (2000) Cryobiology , vol.40 , pp. 277-282
    • Chen, T.1    Fowler, A.2    Toner, M.3
  • 64
    • 0037162460 scopus 로고    scopus 로고
    • Trehalose synthesis is induced upon exposure of Escherichia coli to cold and is essential for viability at low temperatures
    • Kandror O, DeLeon A, Goldberg AL (2002) Trehalose synthesis is induced upon exposure of Escherichia coli to cold and is essential for viability at low temperatures. Proc Natl Acad Sci USA 99:9727-9732.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9727-9732
    • Kandror, O.1    DeLeon, A.2    Goldberg, A.L.3
  • 65
    • 0022504443 scopus 로고
    • Effects of three stabilizing agents-proline, betaine, and trehaloseon membrane phospholipids
    • Rudolph AS, Crowe JH, Crowe LM (1986) Effects of three stabilizing agents-proline, betaine, and trehaloseon membrane phospholipids. Arch Biochem Biophys 245:134-143.
    • (1986) Arch Biochem Biophys , vol.245 , pp. 134-143
    • Rudolph, A.S.1    Crowe, J.H.2    Crowe, L.M.3
  • 67
    • 0031790908 scopus 로고    scopus 로고
    • Water vapor sorption studies on the physical stability of a series of spray-dried protein/sugar powders for inhalation
    • Forbes RT, Davis KG, Hindle M, Clarke JG, Maas J (1998) Water vapor sorption studies on the physical stability of a series of spray-dried protein/sugar powders for inhalation. J Pharm Sci 87:1316-1321.
    • (1998) J Pharm Sci , vol.87 , pp. 1316-1321
    • Forbes, R.T.1    Davis, K.G.2    Hindle, M.3    Clarke, J.G.4    Maas, J.5
  • 68
    • 11344278664 scopus 로고    scopus 로고
    • Trehalose protects yeast pyrophosphatase against structural and functional damage induced by guanidinium chloride
    • Sola-Penna M, Meyer-Fernandes JR (1996) Trehalose protects yeast pyrophosphatase against structural and functional damage induced by guanidinium chloride. Z Naturforsch Sect C Biosci 51:160-164.
    • (1996) Z Naturforsch Sect C Biosci , vol.51 , pp. 160-164
    • Sola-Penna, M.1    Meyer-Fernandes, J.R.2
  • 70
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • Timasheff SN (1993) The control of protein stability and association by weak interactions with water: how do solvents affect these processes? Annu Rev Biophys Biomol Struct 22:67-97.
    • (1993) Annu Rev Biophys Biomol Struct , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 71
    • 0026941297 scopus 로고
    • Hydration of oligosaccharides: Anomalous hydration ability of trehalose
    • Kawai H, Sakurai M, Inoue Y, Chujo R, Kobayashi S (1992) Hydration of oligosaccharides: anomalous hydration ability of trehalose. Cryobiology 29:599-606.
    • (1992) Cryobiology , vol.29 , pp. 599-606
    • Kawai, H.1    Sakurai, M.2    Inoue, Y.3    Chujo, R.4    Kobayashi, S.5
  • 72
    • 0031098431 scopus 로고    scopus 로고
    • α,α-Trehalose-water solutions. 1. Hydration phenomena and anomalies in the acoustic properties
    • Magazú S, Migliardo P, Musolino AM, Sciortino MT (1997) α,α-Trehalose-water solutions. 1. Hydration phenomena and anomalies in the acoustic properties. J Phys Chem B 101:2348-2351.
    • (1997) J Phys Chem B , vol.101 , pp. 2348-2351
    • Magazú, S.1    Migliardo, P.2    Musolino, A.M.3    Sciortino, M.T.4
  • 73
    • 0004220203 scopus 로고    scopus 로고
    • Trehalose + water fragile system: Properties and glass transition
    • Elias ME, Elias AM (1999) Trehalose + water fragile system: properties and glass transition. J Mol Liq 83:303-310.
    • (1999) J Mol Liq , vol.83 , pp. 303-310
    • Elias, M.E.1    Elias, A.M.2
  • 74
    • 0041327357 scopus 로고    scopus 로고
    • Understanding all of water's anomalies with a nonlocal potential
    • Cho CH, Singh S, Robinson GW (1997) Understanding all of water's anomalies with a nonlocal potential. J Chem Phys 107:7979-7988.
    • (1997) J Chem Phys , vol.107 , pp. 7979-7988
    • Cho, C.H.1    Singh, S.2    Robinson, G.W.3
  • 75
    • 0348053809 scopus 로고
    • Preservation of membranes in anhydrobiotic organisms: The role of trehalose
    • Crowe JH, Crowe LM, Chapman D (1984) Preservation of membranes in anhydrobiotic organisms: the role of trehalose. Science 223:701-703.
    • (1984) Science , vol.223 , pp. 701-703
    • Crowe, J.H.1    Crowe, L.M.2    Chapman, D.3
  • 76
    • 0017785420 scopus 로고    scopus 로고
    • Franks F (1977) Solvation interactions of proteins in solution. Philos Trans R Soc Lond B Life Sci 278:33-57.
    • Franks F (1977) Solvation interactions of proteins in solution. Philos Trans R Soc Lond B Life Sci 278:33-57.
  • 77
    • 0030475396 scopus 로고    scopus 로고
    • Anisotropic solvent structuring in aqueous sugar solutions
    • Liu Q, Brady JW (1996) Anisotropic solvent structuring in aqueous sugar solutions. J Am Chem Soc 118:12276-12286.
    • (1996) J Am Chem Soc , vol.118 , pp. 12276-12286
    • Liu, Q.1    Brady, J.W.2
  • 78
    • 0842281268 scopus 로고    scopus 로고
    • Obtaining higher transesterification rates with subtilisin Carlsberg in nonaqueous media
    • Roy I, Sharma A, Gupta MN (2004) Obtaining higher transesterification rates with subtilisin Carlsberg in nonaqueous media. Bioorg Med Chem Lett 14:887-889.
    • (2004) Bioorg Med Chem Lett , vol.14 , pp. 887-889
    • Roy, I.1    Sharma, A.2    Gupta, M.N.3
  • 79
    • 1942472616 scopus 로고    scopus 로고
    • Freeze-drying of proteins: Some emerging concerns
    • Roy I, Gupta MN (2004) Freeze-drying of proteins: some emerging concerns. Biotechnol Appl Biochem 39:165-177.
    • (2004) Biotechnol Appl Biochem , vol.39 , pp. 165-177
    • Roy, I.1    Gupta, M.N.2
  • 80
    • 0024549238 scopus 로고
    • An infrared spectroscopic study of the interactions of carbohydrates with dried proteins
    • Carpenter JF, Crowe JH (1989) An infrared spectroscopic study of the interactions of carbohydrates with dried proteins. Biochemistry 28:3916-3922.
    • (1989) Biochemistry , vol.28 , pp. 3916-3922
    • Carpenter, J.F.1    Crowe, J.H.2
  • 81
    • 31344451903 scopus 로고    scopus 로고
    • Distinct effects of sucrose and trehalose on protein stability during supercritical fluid drying and freeze-drying
    • Jovanovic N, Bouchard A, Hofland GW, Witkamp GJ, Crommelin DJ, Jiskoot W (2006) Distinct effects of sucrose and trehalose on protein stability during supercritical fluid drying and freeze-drying. Eur J Pharm Sci 27:336-345.
    • (2006) Eur J Pharm Sci , vol.27 , pp. 336-345
    • Jovanovic, N.1    Bouchard, A.2    Hofland, G.W.3    Witkamp, G.J.4    Crommelin, D.J.5    Jiskoot, W.6
  • 82
    • 0023037845 scopus 로고
    • Cryoprotection of phosphofructokinase with organic solutes: Characterization of enhanced protection in the presence of divalent cations
    • Carpenter JF, Hand SC, Crowe LM, Crowe JH (1986) Cryoprotection of phosphofructokinase with organic solutes: characterization of enhanced protection in the presence of divalent cations. Arch Biochem Biophys 250:505-512.
    • (1986) Arch Biochem Biophys , vol.250 , pp. 505-512
    • Carpenter, J.F.1    Hand, S.C.2    Crowe, L.M.3    Crowe, J.H.4
  • 83
    • 0030797432 scopus 로고    scopus 로고
    • Carbohydrate protection of enzyme structure and function against guanidinium chloride treatment depends on the nature of carbohydrate and enzyme
    • Sola-Penna M, Ferreira-Pereira A, Lemos AP, Meyer-Fernandes JR (1997) Carbohydrate protection of enzyme structure and function against guanidinium chloride treatment depends on the nature of carbohydrate and enzyme. Eur J Biochem 248:24-29.
    • (1997) Eur J Biochem , vol.248 , pp. 24-29
    • Sola-Penna, M.1    Ferreira-Pereira, A.2    Lemos, A.P.3    Meyer-Fernandes, J.R.4
  • 84
    • 0019975858 scopus 로고
    • Cellular responses to extreme water loss: The water-replacement hypothesis
    • Clegg JS, Seitz P, Seitz W, Hazlewood CF (1982) Cellular responses to extreme water loss: the water-replacement hypothesis. Cryobiology 19:306-316.
    • (1982) Cryobiology , vol.19 , pp. 306-316
    • Clegg, J.S.1    Seitz, P.2    Seitz, W.3    Hazlewood, C.F.4
  • 85
    • 0031205005 scopus 로고    scopus 로고
    • Stabilization of dry membranes by mixtures of hydroxyethyl starch and glucose: The role of vitrification
    • Crowe JH, Oliver AE, Hoekstra FA, Crowe LM (1997) Stabilization of dry membranes by mixtures of hydroxyethyl starch and glucose: the role of vitrification. Cryobiology 35:20-30.
    • (1997) Cryobiology , vol.35 , pp. 20-30
    • Crowe, J.H.1    Oliver, A.E.2    Hoekstra, F.A.3    Crowe, L.M.4
  • 86
    • 12344290280 scopus 로고    scopus 로고
    • Spray-drying of proteins: Effects of sorbitol and trehalose on aggregation and FT-IR amide I spectrum of an immunoglobulin G
    • Maury M, Murphy K, Kumar S, Mauerer A, Lee G (2005) Spray-drying of proteins: effects of sorbitol and trehalose on aggregation and FT-IR amide I spectrum of an immunoglobulin G. Eur J Pharm Biopharm 59:251-261.
    • (2005) Eur J Pharm Biopharm , vol.59 , pp. 251-261
    • Maury, M.1    Murphy, K.2    Kumar, S.3    Mauerer, A.4    Lee, G.5
  • 87
    • 0030921074 scopus 로고    scopus 로고
    • Trehalose prevents myoglobin collapse and preserves its internal mobility
    • Sastry GH, Agmon N (1997) Trehalose prevents myoglobin collapse and preserves its internal mobility. Biochemistry 36:7097-7108.
    • (1997) Biochemistry , vol.36 , pp. 7097-7108
    • Sastry, G.H.1    Agmon, N.2
  • 88
    • 44049099951 scopus 로고    scopus 로고
    • Heterogeneity in desiccated solutions: Implications for biostabilization
    • Ragoonanan V, Aksan A (2008) Heterogeneity in desiccated solutions: implications for biostabilization. Biophys J 94:2212-2227.
    • (2008) Biophys J , vol.94 , pp. 2212-2227
    • Ragoonanan, V.1    Aksan, A.2
  • 89
    • 57349122408 scopus 로고    scopus 로고
    • Solid state chemistry of proteins: II. The correlation of storage stability of freeze-dried human growth hormone (hGH) with structure and dynamics in the glassy solid
    • Pikal MJ, Rigsbee D, Roy ML, Galreath D, Kovach KJ, Wang BS, Carpenter JF, Cicerone MT. Solid state chemistry of proteins: II. The correlation of storage stability of freeze-dried human growth hormone (hGH) with structure and dynamics in the glassy solid. J Pharm Sci 97:5106-5121.
    • J Pharm Sci , vol.97 , pp. 5106-5121
    • Pikal, M.J.1    Rigsbee, D.2    Roy, M.L.3    Galreath, D.4    Kovach, K.J.5    Wang, B.S.6    Carpenter, J.F.7    Cicerone, M.T.8
  • 90
    • 0029740450 scopus 로고    scopus 로고
    • Stability of trehalose, sucrose and glucose to nonenzymatic browning in model systems
    • O'Brien J (1996) Stability of trehalose, sucrose and glucose to nonenzymatic browning in model systems. J Food Sci 61:679-682.
    • (1996) J Food Sci , vol.61 , pp. 679-682
    • O'Brien, J.1
  • 91
    • 33947488954 scopus 로고
    • Isothermal unfolding of globular proteins in aqueous urea solutions
    • Tanford C (1964) Isothermal unfolding of globular proteins in aqueous urea solutions. J Am Chem Soc 86:2050-2059.
    • (1964) J Am Chem Soc , vol.86 , pp. 2050-2059
    • Tanford, C.1
  • 92
    • 27244437952 scopus 로고    scopus 로고
    • Predicting the energetics of osmolyte-induced protein folding/unfolding
    • Auton M, Bolen DW (2005) Predicting the energetics of osmolyte-induced protein folding/unfolding. Proc Natl Acad Sci USA 102:15065-15068.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15065-15068
    • Auton, M.1    Bolen, D.W.2
  • 93
    • 35748981504 scopus 로고    scopus 로고
    • Application of the transfer model to understand how naturally occurring osmolytes affect protein stability
    • Auton M, Bolen DW (2007) Application of the transfer model to understand how naturally occurring osmolytes affect protein stability. Methods Enzymol 428:397-418.
    • (2007) Methods Enzymol , vol.428 , pp. 397-418
    • Auton, M.1    Bolen, D.W.2
  • 94
    • 57049105810 scopus 로고    scopus 로고
    • Structural thermodynamics of protein preferential solvation: Osmolyte salvation of proteins, aminoacids, and peptides
    • Auton M, Bolen DW, Rösgen J. Structural thermodynamics of protein preferential solvation: osmolyte salvation of proteins, aminoacids, and peptides. Proteins 73:802-813.
    • Proteins , vol.73 , pp. 802-813
    • Auton, M.1    Bolen, D.W.2    Rösgen, J.3
  • 95
    • 0021527182 scopus 로고
    • Linkage graphs: A study in the thermodynamics of macromolecules
    • Wyman J (1984) Linkage graphs: a study in the thermodynamics of macromolecules. Q Rev Biophys 17:453-488.
    • (1984) Q Rev Biophys , vol.17 , pp. 453-488
    • Wyman, J.1
  • 96
    • 22444433527 scopus 로고    scopus 로고
    • Stabilization of the ribosomal protein S6 by trehalose is counterbalanced by the formation of a putative off-pathway species
    • Chen L-Y, Cabrita GJM, Otzen DE, Melo EP (2005) Stabilization of the ribosomal protein S6 by trehalose is counterbalanced by the formation of a putative off-pathway species. J Mol Biol 351:402-416.
    • (2005) J Mol Biol , vol.351 , pp. 402-416
    • Chen, L.-Y.1    Cabrita, G.J.M.2    Otzen, D.E.3    Melo, E.P.4
  • 98
    • 0023668329 scopus 로고
    • Proteins as molecular chaperones
    • Ellis T (1987) Proteins as molecular chaperones. Nature 328:378-379.
    • (1987) Nature , vol.328 , pp. 378-379
    • Ellis, T.1
  • 99
    • 0032039542 scopus 로고    scopus 로고
    • Multiple effects of trehalose on protein folding in vitro and in vivo
    • Singer MA, Lindquist S (1998) Multiple effects of trehalose on protein folding in vitro and in vivo. Mol Cell 1:639-648.
    • (1998) Mol Cell , vol.1 , pp. 639-648
    • Singer, M.A.1    Lindquist, S.2
  • 100
    • 0028054926 scopus 로고
    • The role of trehalose synthesis for the acquisition of thermotolerance in yeast. II. Physiological concentrations of trehalose increase the thermal stability of proteins in vitro
    • Hottiger T, de Virgilio C, Hall MN, Boller T, Wiemken A (1994) The role of trehalose synthesis for the acquisition of thermotolerance in yeast. II. Physiological concentrations of trehalose increase the thermal stability of proteins in vitro. Eur J Biochem 219:187-193.
    • (1994) Eur J Biochem , vol.219 , pp. 187-193
    • Hottiger, T.1    de Virgilio, C.2    Hall, M.N.3    Boller, T.4    Wiemken, A.5
  • 101
    • 0027446935 scopus 로고
    • Disruption of TPS2, the gene encoding the 100-kDa subunit of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae, causes accumulation of trehalose-6-phosphate and loss of trehalose-6-phosphate phosphatase activity
    • de Virgilio C, Buerckert N, Bell W, Jenoe P, Boller T, Wiemken A (1993) Disruption of TPS2, the gene encoding the 100-kDa subunit of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae, causes accumulation of trehalose-6-phosphate and loss of trehalose-6-phosphate phosphatase activity. Eur J Biochem 212:315-323.
    • (1993) Eur J Biochem , vol.212 , pp. 315-323
    • de Virgilio, C.1    Buerckert, N.2    Bell, W.3    Jenoe, P.4    Boller, T.5    Wiemken, A.6
  • 102
    • 0025071981 scopus 로고
    • HSP12, a new small heat shock gene of Saccharomyces cerevisiae: Analysis of structure, regulation and function
    • Praekelt UM, Meacock MP (1990) HSP12, a new small heat shock gene of Saccharomyces cerevisiae: analysis of structure, regulation and function. Mol Gen Genet 223:97-106.
    • (1990) Mol Gen Genet , vol.223 , pp. 97-106
    • Praekelt, U.M.1    Meacock, M.P.2
  • 103
    • 0026322998 scopus 로고
    • Uncoupling thermotolerance from the induction of heat shock proteins
    • Smith BJ, Yaffe MP (1991) Uncoupling thermotolerance from the induction of heat shock proteins. Proc Natl Acad Sci USA 88:11091-11094.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 11091-11094
    • Smith, B.J.1    Yaffe, M.P.2
  • 104
    • 0026330981 scopus 로고
    • Trehalose synthesis genes are controlled by the putative sigma factor encoded by rpoS and are involved in stationary-phase thermotolerance in Escherichia coli
    • Hengge-Aronis R, Klein W, Lange R, Rimmele M, Boos W (1991) Trehalose synthesis genes are controlled by the putative sigma factor encoded by rpoS and are involved in stationary-phase thermotolerance in Escherichia coli. J Bacteriol 173:7918-7924.
    • (1991) J Bacteriol , vol.173 , pp. 7918-7924
    • Hengge-Aronis, R.1    Klein, W.2    Lange, R.3    Rimmele, M.4    Boos, W.5
  • 106
    • 0035968318 scopus 로고    scopus 로고
    • Trehalose accumulation during cellular stress protects cells and cellular proteins from damage by oxygen radicals
    • Benaroudj N, Lee DH, Goldberg AL (2001) Trehalose accumulation during cellular stress protects cells and cellular proteins from damage by oxygen radicals. J Biol Chem 276:24261-24267.
    • (2001) J Biol Chem , vol.276 , pp. 24261-24267
    • Benaroudj, N.1    Lee, D.H.2    Goldberg, A.L.3
  • 108
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • Huntington Collaborative Research Group
    • Huntington Collaborative Research Group (1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72:971-983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 111
    • 34848843707 scopus 로고    scopus 로고
    • Effects of sugar additives on protein stability of recombinant human serum albumin during lyophilization and storage
    • Han Y, Jin BS, Lee SB, Sohn Y, Joung JW, Lee JH (2007) Effects of sugar additives on protein stability of recombinant human serum albumin during lyophilization and storage. Arch Pharm Res 30:1124-1131.
    • (2007) Arch Pharm Res , vol.30 , pp. 1124-1131
    • Han, Y.1    Jin, B.S.2    Lee, S.B.3    Sohn, Y.4    Joung, J.W.5    Lee, J.H.6
  • 112
    • 57349123585 scopus 로고    scopus 로고
    • Effect of pH on stability of recombinant botulinum serotype A vaccine in aqueous solution and during storage of freeze-dried formulations
    • Roy S, Henderson I, Nayar R, Randolph TW, Carpenter JF (2008) Effect of pH on stability of recombinant botulinum serotype A vaccine in aqueous solution and during storage of freeze-dried formulations. J Pharm Sci 97:5132-5146.
    • (2008) J Pharm Sci , vol.97 , pp. 5132-5146
    • Roy, S.1    Henderson, I.2    Nayar, R.3    Randolph, T.W.4    Carpenter, J.F.5


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