메뉴 건너뛰기




Volumn 28, Issue 1, 2008, Pages 57-82

Properties, potentials, and prospects of antifreeze proteins

Author keywords

AFP; HSP; Molecular chaperones; Protein expression; Thermal hysteresis

Indexed keywords

BACTERIA; FREEZING; FUNGI; HYSTERESIS; MEDICAL APPLICATIONS; MOLECULAR BIOLOGY; SPECTROSCOPIC ANALYSIS;

EID: 40349103663     PISSN: 07388551     EISSN: 15497801     Source Type: Journal    
DOI: 10.1080/07388550801891152     Document Type: Review
Times cited : (172)

References (304)
  • 1
    • 4644245307 scopus 로고    scopus 로고
    • Enhanced expression of human cytochrome P450 1A2 by co-expression with human molecular chaperone Hsp70
    • Ahn, T., Yang, S., and Yun, C. H. 2004. Enhanced expression of human cytochrome P450 1A2 by co-expression with human molecular chaperone Hsp70. Toxicol. Lett. 153(2): 267-272.
    • (2004) Toxicol. Lett , vol.153 , Issue.2 , pp. 267-272
    • Ahn, T.1    Yang, S.2    Yun, C.H.3
  • 2
    • 0032485869 scopus 로고    scopus 로고
    • Overexpression of a cytosolic chaperone to improve solubility and secretion of a recombinant IgG protein in insect cells
    • Ailor, E., and Betenbaugh, M. J. 1998. Overexpression of a cytosolic chaperone to improve solubility and secretion of a recombinant IgG protein in insect cells. Biotechnol. Bioeng. 58: 196-203.
    • (1998) Biotechnol. Bioeng , vol.58 , pp. 196-203
    • Ailor, E.1    Betenbaugh, M.J.2
  • 3
    • 0024051679 scopus 로고
    • Freezing avoidance and the distribution of antifreeze glycopeptides in body fluids and tissues of Antarctic fish
    • Alghren, J. A., Cheng, C. H. C., Schrag, J. D., and DeVries, A. L. 1988. Freezing avoidance and the distribution of antifreeze glycopeptides in body fluids and tissues of Antarctic fish. J. Exp. Biol. 137: 549-563.
    • (1988) J. Exp. Biol , vol.137 , pp. 549-563
    • Alghren, J.A.1    Cheng, C.H.C.2    Schrag, J.D.3    DeVries, A.L.4
  • 4
    • 27844523689 scopus 로고    scopus 로고
    • Improved viability and reduced apoptosis in sub-zero 21-hour preservation of transplanted rat hearts using anti-freeze proteins
    • Amir, G., Rubinsky, B., Basheer, S. Y., Horowitz, L., Jonathan, L., Feinberg, M. S., Smolinsky, A. M., and Lavee, J. 2005. Improved viability and reduced apoptosis in sub-zero 21-hour preservation of transplanted rat hearts using anti-freeze proteins. J. Heart Lung Transplant. 24(11): 1915-1929.
    • (2005) J. Heart Lung Transplant , vol.24 , Issue.11 , pp. 1915-1929
    • Amir, G.1    Rubinsky, B.2    Basheer, S.Y.3    Horowitz, L.4    Jonathan, L.5    Feinberg, M.S.6    Smolinsky, A.M.7    Lavee, J.8
  • 5
    • 40349090345 scopus 로고    scopus 로고
    • Improved viability and reduced apoptosis in sub-zero 21 hours preservation of transplanted rat hearts using antifreeze proteins
    • Amir, G., Rubinsky, B., Horovitz, L., Yousif, B. S., Leor, J., Smolinsky, A. K., and Lavee, J. 2004. Improved viability and reduced apoptosis in sub-zero 21 hours preservation of transplanted rat hearts using antifreeze proteins. J. Heart Lung Transplant. 23(2): 171-172.
    • (2004) J. Heart Lung Transplant , vol.23 , Issue.2 , pp. 171-172
    • Amir, G.1    Rubinsky, B.2    Horovitz, L.3    Yousif, B.S.4    Leor, J.5    Smolinsky, A.K.6    Lavee, J.7
  • 6
    • 0041621597 scopus 로고    scopus 로고
    • Preservation of myocyte structure and mitochondrial integrity in sub-zero cryopreservation of mammalian hearts for transplantation using antifreeze proteins - an electron microscopy study
    • Amir, G., Rubinsky, B., Kassif, Y., Horowitz, L., Smolinsky, A. M., and Lavee, J. 2003. Preservation of myocyte structure and mitochondrial integrity in sub-zero cryopreservation of mammalian hearts for transplantation using antifreeze proteins - an electron microscopy study. Eur. J. Cardiothorac. Surg. 24(2): 292-297.
    • (2003) Eur. J. Cardiothorac. Surg , vol.24 , Issue.2 , pp. 292-297
    • Amir, G.1    Rubinsky, B.2    Kassif, Y.3    Horowitz, L.4    Smolinsky, A.M.5    Lavee, J.6
  • 7
    • 0001357768 scopus 로고
    • Antifreeze proteins from the ocean pout, Macrozoarces americanus: Circular dichroism spectral studies on the native and denatured states
    • Ananthanarayanan, V. S., Slaughter, D., and Hew, C. L. 1986. Antifreeze proteins from the ocean pout, Macrozoarces americanus: circular dichroism spectral studies on the native and denatured states. Biochim. Biophys. Acta 870: 154-159.
    • (1986) Biochim. Biophys. Acta , vol.870 , pp. 154-159
    • Ananthanarayanan, V.S.1    Slaughter, D.2    Hew, C.L.3
  • 8
    • 0030586740 scopus 로고    scopus 로고
    • Polymers protect lactate dehydrogenase during freeze-drying by inhibiting dissociation in the frozen state
    • Anchordoquy, T. J., and Carpenter, J. F. 1996. Polymers protect lactate dehydrogenase during freeze-drying by inhibiting dissociation in the frozen state. Arch. Biochem. Biophys. 332: 231-238.
    • (1996) Arch. Biochem. Biophys , vol.332 , pp. 231-238
    • Anchordoquy, T.J.1    Carpenter, J.F.2
  • 9
    • 0034089366 scopus 로고    scopus 로고
    • Isolation and characterization of cDNA clones encoding antifreeze protein of the pyrochorid beetle Dendrodies canadensis
    • Andorfer, C. A., and Duman, J. G. 2000. Isolation and characterization of cDNA clones encoding antifreeze protein of the pyrochorid beetle Dendrodies canadensis. J. Insect. Physiol. 46: 365-372.
    • (2000) J. Insect. Physiol , vol.46 , pp. 365-372
    • Andorfer, C.A.1    Duman, J.G.2
  • 11
    • 0344011029 scopus 로고    scopus 로고
    • Antifreeze proteins in higher plants
    • Atici, O., and Nalbantoglu, B. 2003. Antifreeze proteins in higher plants. Phytochemistry 64: 1187-1196.
    • (2003) Phytochemistry , vol.64 , pp. 1187-1196
    • Atici, O.1    Nalbantoglu, B.2
  • 12
    • 0037137136 scopus 로고    scopus 로고
    • Contribution of hydrophobic residues to ice binding by fish type III antifreeze protein
    • Baardsnes, J., and Davis, P. L. 2002. Contribution of hydrophobic residues to ice binding by fish type III antifreeze protein. Biochim. Biophys. Acta 1601: 49-54.
    • (2002) Biochim. Biophys. Acta , vol.1601 , pp. 49-54
    • Baardsnes, J.1    Davis, P.L.2
  • 13
    • 0036279162 scopus 로고    scopus 로고
    • Sequence analysis and resistance to pepsin hydrolysis as part of an assessment of the potential allergenicity of ice structuring protein type III HPLC 12
    • Baderschneider, B., Crevel, R. W. R., Earl, L. K., Lalljie, A., Sanders, D. J., and Sanders, I. J. 2002. Sequence analysis and resistance to pepsin hydrolysis as part of an assessment of the potential allergenicity of ice structuring protein type III HPLC 12. Food Chem. Toxicol. 40: 965-978.
    • (2002) Food Chem. Toxicol , vol.40 , pp. 965-978
    • Baderschneider, B.1    Crevel, R.W.R.2    Earl, L.K.3    Lalljie, A.4    Sanders, D.J.5    Sanders, I.J.6
  • 14
    • 0031572593 scopus 로고    scopus 로고
    • Hypothermic storage of sheep embryos with antifreeze proteins: Development in vitro and in vivo
    • Baguisi, A., Arav, A., Crosby, T. F., Roche, J. F., and Boland, M. P. 1997. Hypothermic storage of sheep embryos with antifreeze proteins: development in vitro and in vivo. Theriogenology 48: 1017-1024.
    • (1997) Theriogenology , vol.48 , pp. 1017-1024
    • Baguisi, A.1    Arav, A.2    Crosby, T.F.3    Roche, J.F.4    Boland, M.P.5
  • 15
    • 0001855568 scopus 로고    scopus 로고
    • In vivo folding of recombinant proteins in Escherichia coli
    • Davies, J. E, Demain, A. L, Cohen, G, Hershberger, C. L, Forney, L. J, Holland, I. B, Hu, W. S, Wu, J. H. D, Sherman, D. H, and Wilson, R. C, Eds, 2nd ed. pp, American Society for Microbiology, Washington, DC
    • Baneyx, F. 1999. In vivo folding of recombinant proteins in Escherichia coli. In: Davies, J. E., Demain, A. L., Cohen, G., Hershberger, C. L., Forney, L. J., Holland, I. B., Hu, W. S., Wu, J. H. D., Sherman, D. H., and Wilson, R. C. (Eds.), Manual of Industrial Microbiology and Biotechnology. 2nd ed. pp. 551-565. American Society for Microbiology, Washington, DC.
    • (1999) Manual of Industrial Microbiology and Biotechnology , pp. 551-565
    • Baneyx, F.1
  • 16
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx, F., and Mujacic, M. 2004. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotech. 22: 1399-1408.
    • (2004) Nat. Biotech , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 17
    • 33746239110 scopus 로고    scopus 로고
    • Efficient production of a folded and functional, highly disulfide-bonded β-helix antifreeze protein in bacteria
    • Bar, M., Bar-Ziv, R., Scherf, T., and Fass, D. 2006. Efficient production of a folded and functional, highly disulfide-bonded β-helix antifreeze protein in bacteria. Protein Expr. Purif. 48: 243-252.
    • (2006) Protein Expr. Purif , vol.48 , pp. 243-252
    • Bar, M.1    Bar-Ziv, R.2    Scherf, T.3    Fass, D.4
  • 18
    • 0035794246 scopus 로고    scopus 로고
    • Antifreeze glycoproteins - preventing the growth of ice
    • Ben, P. N. 2001. Antifreeze glycoproteins - preventing the growth of ice. Chem. Bio. Chem. 2: 161-166.
    • (2001) Chem. Bio. Chem , vol.2 , pp. 161-166
    • Ben, P.N.1
  • 19
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
    • Bessette, P. H., Aslund, F., Beckwith, J., and Georgiou, G. 1999. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc. Natl. Acad. Sci. USA 96: 13703-13708.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Aslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 21
    • 0023191564 scopus 로고
    • Prospective appraisal of complaints of adverse reactions to foods in children during the first three years of life
    • Bock, S. A. 1987. Prospective appraisal of complaints of adverse reactions to foods in children during the first three years of life. Paediatrics 79: 683-688.
    • (1987) Paediatrics , vol.79 , pp. 683-688
    • Bock, S.A.1
  • 22
    • 0039423955 scopus 로고    scopus 로고
    • The periplasmic Escherichia coli peptidyl prolyl cis, trans-isomerase FkpA
    • Bothmann, H., and Pluckthun, A. 2000. The periplasmic Escherichia coli peptidyl prolyl cis, trans-isomerase FkpA. J. Biol. Chem. 275(22): 17100-17105.
    • (2000) J. Biol. Chem , vol.275 , Issue.22 , pp. 17100-17105
    • Bothmann, H.1    Pluckthun, A.2
  • 23
    • 0028028387 scopus 로고
    • Building bridges disulphide bond formation in the cell
    • Bradwell, J. C. 1994. Building bridges disulphide bond formation in the cell. Mol. Microbiol. 14: 199-205.
    • (1994) Mol. Microbiol , vol.14 , pp. 199-205
    • Bradwell, J.C.1
  • 24
    • 0030051047 scopus 로고    scopus 로고
    • Posttranscriptional regulation of CspA expression in Escherichia coli
    • Brandi, A., Pietroni, P., Gualerzi, C. O., and Pon, C. L. 1996. Posttranscriptional regulation of CspA expression in Escherichia coli. Mol. Microbiol. 19: 231-240.
    • (1996) Mol. Microbiol , vol.19 , pp. 231-240
    • Brandi, A.1    Pietroni, P.2    Gualerzi, C.O.3    Pon, C.L.4
  • 25
    • 0034573551 scopus 로고    scopus 로고
    • Biotechnological applications of plant freezing associated proteins
    • Breton, G., Danyluk, J., Ouellet, F. O., and Sarhan, F. 2000. Biotechnological applications of plant freezing associated proteins. Biotechnol. Ann. Rev. 6: 59-101.
    • (2000) Biotechnol. Ann. Rev , vol.6 , pp. 59-101
    • Breton, G.1    Danyluk, J.2    Ouellet, F.O.3    Sarhan, F.4
  • 26
    • 1842838562 scopus 로고    scopus 로고
    • The structure of fish antifreeze proteins
    • Ewart, K.V, and Hew, C.L, Eds, World Scientific, London
    • Brown, D. J., and Sonnichsen, F. D. 2002. The structure of fish antifreeze proteins. In: Ewart, K.V., and Hew, C.L. (Eds.), Fish Antifreeze Proteins. pp. 109-138. World Scientific, London.
    • (2002) Fish Antifreeze Proteins , pp. 109-138
    • Brown, D.J.1    Sonnichsen, F.D.2
  • 28
    • 0026738944 scopus 로고
    • Antifreeze protein modulates cell survival during cryopreservation: Mediation through influence on ice crystal growth
    • Carpenter, J. F., and Hansen, T. N. 1992. Antifreeze protein modulates cell survival during cryopreservation: mediation through influence on ice crystal growth. Proc. Natl. Acad. Sci. USA 89: 8953-8957.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8953-8957
    • Carpenter, J.F.1    Hansen, T.N.2
  • 29
    • 0028961901 scopus 로고
    • Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
    • Chan, M. K., Mukund, S., Kletzin, A., Adams, M.W., and Rees, D. C. 1995. Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science. 267(5203): 1463-1469.
    • (1995) Science , vol.267 , Issue.5203 , pp. 1463-1469
    • Chan, M.K.1    Mukund, S.2    Kletzin, A.3    Adams, M.W.4    Rees, D.C.5
  • 30
    • 0028859777 scopus 로고
    • Mixing antifreeze protein types changes ice crystal morphology without affecting antifreeze activity
    • Chao, H., DeLuca, C. I., and Davies, P. L. 1995. Mixing antifreeze protein types changes ice crystal morphology without affecting antifreeze activity. FEBS Lett. 357(2): 183-186.
    • (1995) FEBS Lett , vol.357 , Issue.2 , pp. 183-186
    • Chao, H.1    DeLuca, C.I.2    Davies, P.L.3
  • 31
    • 0030249969 scopus 로고    scopus 로고
    • Effects of antifreeze proteins on red blood cell survival during cryopreservation
    • Chao, H. M., Davies, P. L., and Carpenter, J. F. 1996a. Effects of antifreeze proteins on red blood cell survival during cryopreservation. J. Exp. Biol. 199: 2071-2076.
    • (1996) J. Exp. Biol , vol.199 , pp. 2071-2076
    • Chao, H.M.1    Davies, P.L.2    Carpenter, J.F.3
  • 32
    • 0029929966 scopus 로고    scopus 로고
    • A natural variant of type I antifreeze protein with 4 ice-binding repeats is a particularly potent antifreeze
    • Chao, H. M., Hodges, R. S., Kay, C. M., Gauthier, S. Y., and Davies, P. L. 1996b. A natural variant of type I antifreeze protein with 4 ice-binding repeats is a particularly potent antifreeze. Protein Sci. 5(6): 1150-1156.
    • (1996) Protein Sci , vol.5 , Issue.6 , pp. 1150-1156
    • Chao, H.M.1    Hodges, R.S.2    Kay, C.M.3    Gauthier, S.Y.4    Davies, P.L.5
  • 34
    • 0030754209 scopus 로고    scopus 로고
    • Kinetics of antifreeze protein-induced ice growth-inhibition
    • Chapsky, L., and Rubinsky, B. 1997. Kinetics of antifreeze protein-induced ice growth-inhibition. FEBS Lett. 412(1): 241-244.
    • (1997) FEBS Lett , vol.412 , Issue.1 , pp. 241-244
    • Chapsky, L.1    Rubinsky, B.2
  • 35
    • 0032872990 scopus 로고    scopus 로고
    • Ice-binding surface of fish type III antifreeze
    • Chen, G. J., and Jia, Z. C. 1999. Ice-binding surface of fish type III antifreeze. Biophys. J. 77: 1602-1608.
    • (1999) Biophys. J , vol.77 , pp. 1602-1608
    • Chen, G.J.1    Jia, Z.C.2
  • 37
    • 0002037107 scopus 로고
    • The role of antifreeze glycopeptides and peptides in the freezing avoidance of cold-water fish
    • di Prisco, G, Ed, Springer-Verlag, Berlin
    • Cheng C. C., and DeVries A. L. 1991. The role of antifreeze glycopeptides and peptides in the freezing avoidance of cold-water fish. In: di Prisco, G. (Ed.), Life Under Extreme Conditions. pp. 1-14. Springer-Verlag, Berlin.
    • (1991) Life Under Extreme Conditions , pp. 1-14
    • Cheng, C.C.1    DeVries, A.L.2
  • 38
    • 0031771585 scopus 로고    scopus 로고
    • Evolution of the diverse antifreeze proteins
    • Cheng, C. H. C. 1998. Evolution of the diverse antifreeze proteins. Curr. Opin. Genet. Dev. 8: 715-720.
    • (1998) Curr. Opin. Genet. Dev , vol.8 , pp. 715-720
    • Cheng, C.H.C.1
  • 39
    • 0033619225 scopus 로고    scopus 로고
    • Evolution of an antifreeze glycoprotein
    • Cheng, C. H. C., and Chen, L. B. 1999. Evolution of an antifreeze glycoprotein. Nature 401: 443-444.
    • (1999) Nature , vol.401 , pp. 443-444
    • Cheng, C.H.C.1    Chen, L.B.2
  • 40
    • 0027946040 scopus 로고
    • Structure function relationship in the globular type III antifreeze proteins - identification of a cluster of surface residues required for binding to ice
    • Cho, H., Sonnichsen, F. D., DeLuca, C. I., Sykes, B. D., and Davies, P. L. 1994. Structure function relationship in the globular type III antifreeze proteins - identification of a cluster of surface residues required for binding to ice. Protein Sci. 3(10): 1760-1769.
    • (1994) Protein Sci , vol.3 , Issue.10 , pp. 1760-1769
    • Cho, H.1    Sonnichsen, F.D.2    DeLuca, C.I.3    Sykes, B.D.4    Davies, P.L.5
  • 41
    • 0033136533 scopus 로고    scopus 로고
    • Effect of Sec B chaperone on production of periplasmic penicillin acylase in Escherichia coli
    • Chou, C. P., Tseng, J. H., Kuo, B. Y., Lai, K. M., Lin, M. I., and Lin, B. K. 1999. Effect of Sec B chaperone on production of periplasmic penicillin acylase in Escherichia coli. Biotechnol. Prog. 15: 439-445.
    • (1999) Biotechnol. Prog , vol.15 , pp. 439-445
    • Chou, C.P.1    Tseng, J.H.2    Kuo, B.Y.3    Lai, K.M.4    Lin, M.I.5    Lin, B.K.6
  • 42
    • 0035983994 scopus 로고    scopus 로고
    • Ice structuring proteins - a new name for antifreeze proteins
    • Clarke, C. J., Buckley, S. L., and Lindner, N. 2002. Ice structuring proteins - a new name for antifreeze proteins. Cryo Letters 23(2): 89-92.
    • (2002) Cryo Letters , vol.23 , Issue.2 , pp. 89-92
    • Clarke, C.J.1    Buckley, S.L.2    Lindner, N.3
  • 43
    • 0033848415 scopus 로고    scopus 로고
    • Ice crystallization by Pseudomonas syringae
    • Cochet, N., and Widehem, P. 2000. Ice crystallization by Pseudomonas syringae. Appl. Microbiol. Biotechnol. 54: 153-161.
    • (2000) Appl. Microbiol. Biotechnol , vol.54 , pp. 153-161
    • Cochet, N.1    Widehem, P.2
  • 45
    • 65549151592 scopus 로고
    • Molecular characterisation of messenger RNAs for pathogenesis related proteins 1a, 1b, and 1c, induced by TMV infection of tobacco
    • Cornelissen, B. J. C., Van Huijsduijnen, R. A. M. H., Van Loon, L. C., and Bol, J. F. 1986. Molecular characterisation of messenger RNAs for pathogenesis related proteins 1a, 1b, and 1c, induced by TMV infection of tobacco. EMBO J. 5: 37-40.
    • (1986) EMBO J , vol.5 , pp. 37-40
    • Cornelissen, B.J.C.1    Van Huijsduijnen, R.A.M.H.2    Van Loon, L.C.3    Bol, J.F.4
  • 46
    • 0031793406 scopus 로고    scopus 로고
    • Effect of mannitol crystallization on the stability and aerosol performance of a spray dried pharmaceutical protein, recombinant humanized anti-IgE monoclonal antibody
    • Costantino, H. R., and Andya, J. D. 1998. Effect of mannitol crystallization on the stability and aerosol performance of a spray dried pharmaceutical protein, recombinant humanized anti-IgE monoclonal antibody. J. Pharm. Sci. 87: 1406-1411.
    • (1998) J. Pharm. Sci , vol.87 , pp. 1406-1411
    • Costantino, H.R.1    Andya, J.D.2
  • 47
    • 33751335856 scopus 로고    scopus 로고
    • Lack of immunogenicity of ice structuring protein type III HPLC12 preparation administered by the oral route to human volunteers
    • Crevel, R. W. R., Cooper, K. J., Poulsen, L. K., Hummelshoj, L, Bindslev-Jensen, C., Burks, A.W., and Sampson, H. A. 2007. Lack of immunogenicity of ice structuring protein type III HPLC12 preparation administered by the oral route to human volunteers. Food Chem. Toxicol. 45: 79-87.
    • (2007) Food Chem. Toxicol , vol.45 , pp. 79-87
    • Crevel, R.W.R.1    Cooper, K.J.2    Poulsen, L.K.3    Hummelshoj, L.4    Bindslev-Jensen, C.5    Burks, A.W.6    Sampson, H.A.7
  • 48
    • 0036284799 scopus 로고    scopus 로고
    • Antifreeze proteins: Characteristics, occurrence and human exposure
    • Crevel, R.W. R., Fedyk, J. K., and Spurgeon, M. J. 2002. Antifreeze proteins: characteristics, occurrence and human exposure. Food Chem. Toxicol. 40: 899-903.
    • (2002) Food Chem. Toxicol , vol.40 , pp. 899-903
    • Crevel, R.W.R.1    Fedyk, J.K.2    Spurgeon, M.J.3
  • 51
    • 0032428738 scopus 로고    scopus 로고
    • A low temperature induced apoplastic protein isolated from Arachis hypogaea
    • Dave, R. S., and Mitra, R. K. 1998. A low temperature induced apoplastic protein isolated from Arachis hypogaea. Phytochemistry 49: 2207-2213.
    • (1998) Phytochemistry , vol.49 , pp. 2207-2213
    • Dave, R.S.1    Mitra, R.K.2
  • 52
    • 0025325036 scopus 로고
    • Biochemistry of fish antifreeze proteins
    • Davies, P. L., and Hew, C. L. 1990. Biochemistry of fish antifreeze proteins. FASEB J. 4(8): 2460-2468.
    • (1990) FASEB J , vol.4 , Issue.8 , pp. 2460-2468
    • Davies, P.L.1    Hew, C.L.2
  • 54
    • 0020033471 scopus 로고
    • DNAsequence coding for an antifreeze protein precursor from winter flounder
    • Davies, P. L., Roach, A. H., and Hew, C. L. 1982.DNAsequence coding for an antifreeze protein precursor from winter flounder. Proc. Natl. Acad. Sci. USA 79: 335-339.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 335-339
    • Davies, P.L.1    Roach, A.H.2    Hew, C.L.3
  • 55
    • 0000604289 scopus 로고    scopus 로고
    • Freeze resistance strategies based on antifreeze proteins
    • Storey, K. B, Ed, BIOS. Scientific Publishers, Oxford, UK
    • Davies, P. L., Fletcher, G. L., and Hew, C. L. 1999. Freeze resistance strategies based on antifreeze proteins. In: Storey, K. B. (Ed.), Environmental Stress and Gene Regulation. pp. 61-80. BIOS. Scientific Publishers, Oxford, UK.
    • (1999) Environmental Stress and Gene Regulation , pp. 61-80
    • Davies, P.L.1    Fletcher, G.L.2    Hew, C.L.3
  • 56
    • 0029861265 scopus 로고    scopus 로고
    • Effect of type III antifreeze protein dilution and mutation on the growth inhibition of ice
    • DeLuca, C. I., Chao, H., Sonnichsen, F. D., Sykes, B. D., and Davies, P. L. 1996. Effect of type III antifreeze protein dilution and mutation on the growth inhibition of ice. Biophys. J. 71(5): 2346-2355.
    • (1996) Biophys. J , vol.71 , Issue.5 , pp. 2346-2355
    • DeLuca, C.I.1    Chao, H.2    Sonnichsen, F.D.3    Sykes, B.D.4    Davies, P.L.5
  • 57
    • 0031934222 scopus 로고    scopus 로고
    • Antifreeze proteins bind independently to ice
    • DeLuca, C. I., Comley, R., and Davies, P. L. 1998. Antifreeze proteins bind independently to ice. Biophys. J. 74: 1502-1508.
    • (1998) Biophys. J , vol.74 , pp. 1502-1508
    • DeLuca, C.I.1    Comley, R.2    Davies, P.L.3
  • 59
    • 0028181116 scopus 로고
    • Human interferon-beta, expressed in Saccharomyces cerevisiae, is predominantly directed to the vacuoles. Influence of modified co-expression of secretion factors and chaperones
    • Demolder, J., Fiers, W., and Contreras, R. 1994. Human interferon-beta, expressed in Saccharomyces cerevisiae, is predominantly directed to the vacuoles. Influence of modified co-expression of secretion factors and chaperones. J. Biotechnol. 32(2): 179-189.
    • (1994) J. Biotechnol , vol.32 , Issue.2 , pp. 179-189
    • Demolder, J.1    Fiers, W.2    Contreras, R.3
  • 60
    • 0027739665 scopus 로고
    • Mutants that allow disulfide bond formation in the cytoplasm of Escherichia coli
    • Derman, A. I., Prinz, W. A., Belin, D., and Beckwith, J. 1993. Mutants that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science 262: 1744-1747.
    • (1993) Science , vol.262 , pp. 1744-1747
    • Derman, A.I.1    Prinz, W.A.2    Belin, D.3    Beckwith, J.4
  • 61
    • 0015219684 scopus 로고
    • Glycoproteins as biological antifreeze agents in Antarctic fishes
    • DeVries, A. L. 1971. Glycoproteins as biological antifreeze agents in Antarctic fishes. Science 172: 1152-1155.
    • (1971) Science , vol.172 , pp. 1152-1155
    • DeVries, A.L.1
  • 62
    • 0000742353 scopus 로고
    • The role of antifreeze glycopeptides and peptides in the freezing avoidance of Antarctic fishes
    • DeVries, A. L. 1988. The role of antifreeze glycopeptides and peptides in the freezing avoidance of Antarctic fishes. Comp. Biochem. Physiol. 90: 611-621.
    • (1988) Comp. Biochem. Physiol , vol.90 , pp. 611-621
    • DeVries, A.L.1
  • 63
    • 0017730326 scopus 로고
    • Structure of a peptide antifreeze and mechanism of adsorption to ice
    • DeVries, A. L., and Lin, Y. 1977. Structure of a peptide antifreeze and mechanism of adsorption to ice. Biochim. Biophys. Acta 495: 388-392.
    • (1977) Biochim. Biophys. Acta , vol.495 , pp. 388-392
    • DeVries, A.L.1    Lin, Y.2
  • 64
    • 0014939615 scopus 로고
    • Chemical and physical properties of freezing point-depression glycoproteins from Antarctic fishes
    • DeVries, A. L., Komatsu, S. K., and Feeney, R. E. 1970. Chemical and physical properties of freezing point-depression glycoproteins from Antarctic fishes. J. Biol. Chem. 245: 2901-2913.
    • (1970) J. Biol. Chem , vol.245 , pp. 2901-2913
    • DeVries, A.L.1    Komatsu, S.K.2    Feeney, R.E.3
  • 66
    • 0036151155 scopus 로고    scopus 로고
    • A family of expressed antifreeze protein genes from the moth, Choristoneura fumiferana
    • Douchet, D., Tyshenko, M. G., Davies, P. L., and Walker, V. K. 2002. A family of expressed antifreeze protein genes from the moth, Choristoneura fumiferana. Eur. J. Biochem. 269: 38-46.
    • (2002) Eur. J. Biochem , vol.269 , pp. 38-46
    • Douchet, D.1    Tyshenko, M.G.2    Davies, P.L.3    Walker, V.K.4
  • 67
    • 0029009349 scopus 로고
    • Expression and secretion of antifreeze peptides in the yeast Saccharomyces cerevisiae
    • Driedonks, R. A., Toschka, H. Y., Van Almkerk, J.W., Schaffers, I. M., and Verbakel, J. M. A. 1995. Expression and secretion of antifreeze peptides in the yeast Saccharomyces cerevisiae. Yeast 11: 849-864.
    • (1995) Yeast , vol.11 , pp. 849-864
    • Driedonks, R.A.1    Toschka, H.Y.2    Van Almkerk, J.W.3    Schaffers, I.M.4    Verbakel, J.M.A.5
  • 68
    • 0036934412 scopus 로고    scopus 로고
    • The inhibition of ice nucleators by insect antifreeze proteins is enhanced by glycerol and citrate
    • Duman, J. G. 2002. The inhibition of ice nucleators by insect antifreeze proteins is enhanced by glycerol and citrate. J. Comp. Physiol. 172: 163-168.
    • (2002) J. Comp. Physiol , vol.172 , pp. 163-168
    • Duman, J.G.1
  • 69
    • 0000078585 scopus 로고
    • Thermal hysteresis protein activity in bacteria, fungi, and phylogenetically diverse plants
    • Duman, J. G., and Olsen, T. M. 1993. Thermal hysteresis protein activity in bacteria, fungi, and phylogenetically diverse plants. Cryobiology 30: 322-328.
    • (1993) Cryobiology , vol.30 , pp. 322-328
    • Duman, J.G.1    Olsen, T.M.2
  • 70
    • 0036139221 scopus 로고    scopus 로고
    • The role of endogenous antifreeze protein enhancers in the hemolymph thermal hysteresis activity of the beetle Dendroides canadensis
    • Duman, J. G., and Serianni, A. S. 2002. The role of endogenous antifreeze protein enhancers in the hemolymph thermal hysteresis activity of the beetle Dendroides canadensis. J. Insect Physiol. 48: 103-111.
    • (2002) J. Insect Physiol , vol.48 , pp. 103-111
    • Duman, J.G.1    Serianni, A.S.2
  • 73
    • 0003032556 scopus 로고
    • Hemolymph protein involved in insect sub-zero temperature tolerance. Ice nucleators and anti-freeze proteins
    • Lee, R. E, and Deninger, D. L, Eds, Chapman and Hall, New York
    • Duman, J. K., Xu, L., Neven, L. G., Tursman, D., and Wu, D. W. 1991. Hemolymph protein involved in insect sub-zero temperature tolerance. Ice nucleators and anti-freeze proteins. In: Lee, R. E., and Deninger, D. L. (Eds.), Insects at Low Temperature. pp. 94-127. Chapman and Hall, New York.
    • (1991) Insects at Low Temperature , pp. 94-127
    • Duman, J.K.1    Xu, L.2    Neven, L.G.3    Tursman, D.4    Wu, D.W.5
  • 74
    • 0029450070 scopus 로고
    • Antifreeze protein does not confer cold tolerance to transgenic Drosophila melanogaster
    • Duncker, B. P., Chen, C. P., Davies, P. L., and Walker, V. K. 1995. Antifreeze protein does not confer cold tolerance to transgenic Drosophila melanogaster. Cryobiology 32: 521-527.
    • (1995) Cryobiology , vol.32 , pp. 521-527
    • Duncker, B.P.1    Chen, C.P.2    Davies, P.L.3    Walker, V.K.4
  • 75
    • 0029687108 scopus 로고    scopus 로고
    • Expression of cystine-rich fish antifreeze in transgenic Drosophila melanogaster
    • Duncker, B. P., Hermans, J. A., Davies, P. L., and Walker, V. K. 1996. Expression of cystine-rich fish antifreeze in transgenic Drosophila melanogaster. Transgenic Res. 5: 49-55.
    • (1996) Transgenic Res , vol.5 , pp. 49-55
    • Duncker, B.P.1    Hermans, J.A.2    Davies, P.L.3    Walker, V.K.4
  • 76
    • 0025952279 scopus 로고
    • Effect of freezing on aggregation of human growth hormone
    • Eckhardt, B. M., and Oeswein, J. Q. 1991. Effect of freezing on aggregation of human growth hormone. Pharm. Res. 8: 1360-1364.
    • (1991) Pharm. Res , vol.8 , pp. 1360-1364
    • Eckhardt, B.M.1    Oeswein, J.Q.2
  • 77
    • 0028064967 scopus 로고
    • SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
    • Economou, A., and Wickner, W. 1994. SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion. Cell 78: 835-843.
    • (1994) Cell , vol.78 , pp. 835-843
    • Economou, A.1    Wickner, W.2
  • 78
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • Eisenberg, D., and McLachlan, A. D. 1986. Solvation energy in protein folding and binding. Science 319: 199-203.
    • (1986) Science , vol.319 , pp. 199-203
    • Eisenberg, D.1    McLachlan, A.D.2
  • 79
    • 0027723312 scopus 로고
    • Antifreeze glycoproteins increase solution viscosity
    • Eto, T. K., and Rubinsky, B. 1993. Antifreeze glycoproteins increase solution viscosity. Biochem. Biophys. Res. Commun. 197(2): 927-931.
    • (1993) Biochem. Biophys. Res. Commun , vol.197 , Issue.2 , pp. 927-931
    • Eto, T.K.1    Rubinsky, B.2
  • 82
    • 0032982510 scopus 로고    scopus 로고
    • Structure, function and evolution of antifreeze proteins
    • Ewart, K. V., Lin, Q., and Hew, C. L. 1999. Structure, function and evolution of antifreeze proteins. Cell. Mol. Life Sci. 55: 271-83.
    • (1999) Cell. Mol. Life Sci , vol.55 , pp. 271-283
    • Ewart, K.V.1    Lin, Q.2    Hew, C.L.3
  • 83
    • 0026772705 scopus 로고
    • Structural and functional similarity between fish antifreeze proteins and calcium-dependent lectins
    • Ewart, K. V., Rubinsky, B., and Fletcher, G. L. 1992. Structural and functional similarity between fish antifreeze proteins and calcium-dependent lectins. Biochem. Biophys. Res. Commun. 185: 335-345.
    • (1992) Biochem. Biophys. Res. Commun , vol.185 , pp. 335-345
    • Ewart, K.V.1    Rubinsky, B.2    Fletcher, G.L.3
  • 85
    • 0002428654 scopus 로고
    • Antifreeze proteins: Properties, mechanism of action, and possible applications
    • Feeney, R. E., and Yeh, Y. 1993. Antifreeze proteins: properties, mechanism of action, and possible applications. Food Technol. 47: 82-90.
    • (1993) Food Technol , vol.47 , pp. 82-90
    • Feeney, R.E.1    Yeh, Y.2
  • 86
    • 0031811192 scopus 로고    scopus 로고
    • Antifreeze proteins: Current status and possible food uses
    • Feeney, R. F., and Yeh, Y. 1998. Antifreeze proteins: current status and possible food uses. Trends Food Sci. Technol. 9: 1-5.
    • (1998) Trends Food Sci. Technol , vol.9 , pp. 1-5
    • Feeney, R.F.1    Yeh, Y.2
  • 87
    • 4143080300 scopus 로고    scopus 로고
    • Expression of a temperature sensitive esterase in a novel chaperone based Escherichia coli strain
    • Ferrer, M., Chernikova, T. N., Timmis, K. N., and Golyshin, P. N. 2004. Expression of a temperature sensitive esterase in a novel chaperone based Escherichia coli strain. Appl. Environ. Microbiol. 70: 4499-4504.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 4499-4504
    • Ferrer, M.1    Chernikova, T.N.2    Timmis, K.N.3    Golyshin, P.N.4
  • 89
    • 0002128812 scopus 로고    scopus 로고
    • Antifreeze proteins and their genes: From basic research to business opportunity
    • Fletcher, G. L., Goddard, S. V., and Wu, Y. L. 1999. Antifreeze proteins and their genes: From basic research to business opportunity Chemtech. 29: 17-28.
    • (1999) Chemtech , vol.29 , pp. 17-28
    • Fletcher, G.L.1    Goddard, S.V.2    Wu, Y.L.3
  • 90
    • 0000996448 scopus 로고    scopus 로고
    • New insights into fish antifreeze proteins: Physiological significance and molecular regulation
    • Portner H. O, and Playle, R, Eds, Cold Ocean Physiology, Cambridge University Press, Cambridge, UK
    • Fletcher, G. L., Goddard, S.V., Davies, P. L., Gong, Z., Ewart, K.V., and Hew, C. L. 1998. New insights into fish antifreeze proteins: physiological significance and molecular regulation, In: Portner H. O., and Playle, R. (Eds.), Cold Ocean Physiology (Society for Experimental Biology Seminar Series 66). pp. 239-265. Cambridge University Press, Cambridge, UK.
    • (1998) Society for Experimental Biology Seminar Series , vol.66 , pp. 239-265
    • Fletcher, G.L.1    Goddard, S.V.2    Davies, P.L.3    Gong, Z.4    Ewart, K.V.5    Hew, C.L.6
  • 91
  • 92
    • 0009665409 scopus 로고    scopus 로고
    • Antifreeze polypeptide-expressing microorganisms useful in fermentation and freezing of foods
    • U.S. Patent 5676985
    • Fletcher, G. L., Hew, C. L., Joshi, S. B., and Wu, Y. 1997. Antifreeze polypeptide-expressing microorganisms useful in fermentation and freezing of foods. U.S. Patent 5676985.
    • (1997)
    • Fletcher, G.L.1    Hew, C.L.2    Joshi, S.B.3    Wu, Y.4
  • 93
    • 0001350675 scopus 로고
    • Antifreeze peptides confer freezing resistance to fish
    • Fletcher, G. L., Kao, M. H., and Fourney, R. M. 1986. Antifreeze peptides confer freezing resistance to fish. Can. J. Zool. 64: 1897-1901.
    • (1986) Can. J. Zool , vol.64 , pp. 1897-1901
    • Fletcher, G.L.1    Kao, M.H.2    Fourney, R.M.3
  • 94
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman, J. 2001. Folding of newly translated proteins in vivo: the role of molecular chaperones. Ann. Rev. Biochem. 70: 603-649.
    • (2001) Ann. Rev. Biochem , vol.70 , pp. 603-649
    • Frydman, J.1
  • 95
    • 0032209678 scopus 로고    scopus 로고
    • Mechanisms of tissue injury in cryosurgery
    • Gage, A. A., and Baust, J. G. 1998. Mechanisms of tissue injury in cryosurgery. Cryobiology 37: 171-186.
    • (1998) Cryobiology , vol.37 , pp. 171-186
    • Gage, A.A.1    Baust, J.G.2
  • 96
    • 0141449051 scopus 로고    scopus 로고
    • Analysis of thermal hysteresis protein hydration using the random network model
    • Gallagher, K. R., and Sharp, K. A. 2003. Analysis of thermal hysteresis protein hydration using the random network model. Biophys. Chem. 105: 195-209.
    • (2003) Biophys. Chem , vol.105 , pp. 195-209
    • Gallagher, K.R.1    Sharp, K.A.2
  • 97
    • 0032402888 scopus 로고    scopus 로고
    • Disulfide bond mapping and structural characterization of spruce budworm antifreeze protein
    • Gauthier, S. Y., Kay, C. M., Sykes, B. D., Walker, V. K., and Davies, P. L. 1998. Disulfide bond mapping and structural characterization of spruce budworm antifreeze protein. Eur. J. Biochem. 258: 445-453.
    • (1998) Eur. J. Biochem , vol.258 , pp. 445-453
    • Gauthier, S.Y.1    Kay, C.M.2    Sykes, B.D.3    Walker, V.K.4    Davies, P.L.5
  • 98
    • 0003103143 scopus 로고
    • Inoculative freezing and thermal hysteresis in the adult beetles Ips acuminatus and Rhagium inquisitor
    • Gehrken, U. 1992. Inoculative freezing and thermal hysteresis in the adult beetles Ips acuminatus and Rhagium inquisitor. J. Insect Physiol. 38: 519-524.
    • (1992) J. Insect Physiol , vol.38 , pp. 519-524
    • Gehrken, U.1
  • 100
    • 1642473904 scopus 로고    scopus 로고
    • Demonstration of antifreeze protein activity in Antarctic lake bacteria
    • Gilbert, J. A., Hill, P. J., Dodd, C. E. R., and Parry, J. L. 2004. Demonstration of antifreeze protein activity in Antarctic lake bacteria. Microbiology 50: 171-180.
    • (2004) Microbiology , vol.50 , pp. 171-180
    • Gilbert, J.A.1    Hill, P.J.2    Dodd, C.E.R.3    Parry, J.L.4
  • 101
    • 0030669069 scopus 로고    scopus 로고
    • Role of Escherichia coli cspA promoter sequences and adaptation of translational apparatus in the cold shock response
    • Goldenberg, D., Azar, I., Oppenheim, A. B., Brandi, A., Pon, C. L., and Gualerzi, C. O. 1996. Role of Escherichia coli cspA promoter sequences and adaptation of translational apparatus in the cold shock response. Mol. Gen. Genet. 256: 282-290.
    • (1996) Mol. Gen. Genet , vol.256 , pp. 282-290
    • Goldenberg, D.1    Azar, I.2    Oppenheim, A.B.3    Brandi, A.4    Pon, C.L.5    Gualerzi, C.O.6
  • 103
    • 0030049438 scopus 로고    scopus 로고
    • Skin antifreeze protein genes of the winter flounder, Pleuronectes americanus, encode distinct and active polypeptides without the secretory signal and prosequences
    • Gong, Z., Ewart, K. V., Hu, Z., Fletcher, G. L., and Hew, C. L. 1996. Skin antifreeze protein genes of the winter flounder, Pleuronectes americanus, encode distinct and active polypeptides without the secretory signal and prosequences. J. Biol. Chem. 271: 4106-4112.
    • (1996) J. Biol. Chem , vol.271 , pp. 4106-4112
    • Gong, Z.1    Ewart, K.V.2    Hu, Z.3    Fletcher, G.L.4    Hew, C.L.5
  • 104
    • 0344405701 scopus 로고    scopus 로고
    • Spruce budworm antifreeze protein: Changes in structure and dynamics at low temperature
    • Graether, S. P, Gagne, S. M., Spyracopoulos, L., Jai, Z., Davies, P. L., and Sykes. D. B. 2003. Spruce budworm antifreeze protein: changes in structure and dynamics at low temperature. J. Mol. Biol. 327: 1156-1168.
    • (2003) J. Mol. Biol , vol.327 , pp. 1156-1168
    • Graether, S.P.1    Gagne, S.M.2    Spyracopoulos, L.3    Jai, Z.4    Davies, P.L.5    Sykes, D.B.6
  • 105
    • 0033150319 scopus 로고    scopus 로고
    • Crystallization and preliminary x-ray crystallographic analysis of spruce budworm antifreeze protein
    • Graether, S. P., Ye, Q. L., Davies, P. L., and Jia, Z. C. 1999. Crystallization and preliminary x-ray crystallographic analysis of spruce budworm antifreeze protein. J. Struct. Biol. 126: 72-75.
    • (1999) J. Struct. Biol , vol.126 , pp. 72-75
    • Graether, S.P.1    Ye, Q.L.2    Davies, P.L.3    Jia, Z.C.4
  • 106
    • 4344642832 scopus 로고    scopus 로고
    • Cold survival in freeze-intolerant insects. The structure and function of h-helical antifreeze proteins
    • Graether, S. P., and Sykes, B. D. 2004. Cold survival in freeze-intolerant insects. The structure and function of h-helical antifreeze proteins. Eur. J. Biochem. 271: 3285-3296.
    • (2004) Eur. J. Biochem , vol.271 , pp. 3285-3296
    • Graether, S.P.1    Sykes, B.D.2
  • 107
    • 0030760436 scopus 로고    scopus 로고
    • Hyperactive antifreeze protein from beetles
    • Graham, L. A., Liou, Y. C., Walker, V. K., and Davies, P. L. 1997. Hyperactive antifreeze protein from beetles. Nature 388(6644): 727-728.
    • (1997) Nature , vol.388 , Issue.6644 , pp. 727-728
    • Graham, L.A.1    Liou, Y.C.2    Walker, V.K.3    Davies, P.L.4
  • 109
    • 0028835687 scopus 로고
    • Antifreeze proteins and their potential uses in frozen foods
    • Griffith, M., and Ewart, K. V. 1995. Antifreeze proteins and their potential uses in frozen foods. Biotechnol. Adv. 13: 375-402.
    • (1995) Biotechnol. Adv , vol.13 , pp. 375-402
    • Griffith, M.1    Ewart, K.V.2
  • 110
    • 4344568284 scopus 로고    scopus 로고
    • Antifreeze proteins in over wintering plants: A tale of two activities
    • Griffith, M., and Yaish, M. W. F. 2004. Antifreeze proteins in over wintering plants: a tale of two activities. Trends Plant Sci. 9: 399-405.
    • (2004) Trends Plant Sci , vol.9 , pp. 399-405
    • Griffith, M.1    Yaish, M.W.F.2
  • 113
    • 0030463807 scopus 로고    scopus 로고
    • NMR characterization of side-chain flexibility and backbone structure in the type-I antifreeze protein at near freezing temperatures
    • Gronwald, W., Chao, H. M., Reddy, D. V., Davies, P. L., Sykes, B. D., and Sonnichsen, F. D. 1996. NMR characterization of side-chain flexibility and backbone structure in the type-I antifreeze protein at near freezing temperatures. Biochemisty 35: 16698-16704.
    • (1996) Biochemisty , vol.35 , pp. 16698-16704
    • Gronwald, W.1    Chao, H.M.2    Reddy, D.V.3    Davies, P.L.4    Sykes, B.D.5    Sonnichsen, F.D.6
  • 114
    • 0021004977 scopus 로고    scopus 로고
    • Gumpert, J., and Taubeneck, U. 1983. Characteristic properties and biological significance and stable protoplast type L-forms. In: Protoplasts, Lecture. Proceedings of the 6th International Protoplast Symposium, Basel. Exprientia 46: 227-241.
    • Gumpert, J., and Taubeneck, U. 1983. Characteristic properties and biological significance and stable protoplast type L-forms. In: Protoplasts, Lecture. Proceedings of the 6th International Protoplast Symposium, Basel. Exprientia 46: 227-241.
  • 116
    • 0006093370 scopus 로고
    • Serial dilution of Tenebrio molitor haemolymph: Analysis of antifreeze activity by differential scanning calorimetry
    • Hansen, T. N., and Baust, J. G. 1988. Serial dilution of Tenebrio molitor haemolymph: analysis of antifreeze activity by differential scanning calorimetry. Cryo Letters 9: 386-391.
    • (1988) Cryo Letters , vol.9 , pp. 386-391
    • Hansen, T.N.1    Baust, J.G.2
  • 117
    • 0033568338 scopus 로고    scopus 로고
    • Type I 'antifreeze' proteins-structure-activity studies and mechanisms of ice growth inhibition
    • Harding, M. M., Ward, L. G., and Haymet, A. D. J. 1999. Type I 'antifreeze' proteins-structure-activity studies and mechanisms of ice growth inhibition. Eur. J. Biochem. 264: 653-665.
    • (1999) Eur. J. Biochem , vol.264 , pp. 653-665
    • Harding, M.M.1    Ward, L.G.2    Haymet, A.D.J.3
  • 118
    • 0029620311 scopus 로고
    • Protein disulfide isomerase mutant lacking its isomerase activity accelerates protein folding in the cell
    • Hayano, T., Hirose, M., and Kikuchi, M. 1995. Protein disulfide isomerase mutant lacking its isomerase activity accelerates protein folding in the cell. FEBS Lett. 377(3): 505-511.
    • (1995) FEBS Lett , vol.377 , Issue.3 , pp. 505-511
    • Hayano, T.1    Hirose, M.2    Kikuchi, M.3
  • 119
    • 0033540633 scopus 로고    scopus 로고
    • Winter flounder "antifreeze" proteins: Synthesis and ice growth inhibition of analogues that probe the relative importance of hydrophobic and hydrogen-bonding interactions
    • Chem. Soc
    • Haymet, A. D. J., Ward, L. G., and Harding, M. M. 1999. Winter flounder "antifreeze" proteins: synthesis and ice growth inhibition of analogues that probe the relative importance of hydrophobic and hydrogen-bonding interactions. J. Am. Chem. Soc. 121: 941-948.
    • (1999) J. Am , vol.121 , pp. 941-948
    • Haymet, A.D.J.1    Ward, L.G.2    Harding, M.M.3
  • 120
    • 0032479347 scopus 로고    scopus 로고
    • Valine substituted winter flounder antifreeze-preservation of ice growth hysteresis
    • Haymet, A. D. J., Ward, L. G., Harding, M. M., and Knight, C. A. 1998. Valine substituted winter flounder antifreeze-preservation of ice growth hysteresis. FEBS Lett. 430: 301-306.
    • (1998) FEBS Lett , vol.430 , pp. 301-306
    • Haymet, A.D.J.1    Ward, L.G.2    Harding, M.M.3    Knight, C.A.4
  • 121
    • 0029902124 scopus 로고    scopus 로고
    • Antifreeze glycoproteins inhibit leakage from liposomes during thermotropic phase transitions
    • Hays, L. M., Feeney, R. E., Crowe, L. M., Crowe, J. H., and Oliver, A. E. 1996. Antifreeze glycoproteins inhibit leakage from liposomes during thermotropic phase transitions. Proc. Natl. Acad. Sci. USA 93: 6835-6840.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6835-6840
    • Hays, L.M.1    Feeney, R.E.2    Crowe, L.M.3    Crowe, J.H.4    Oliver, A.E.5
  • 122
    • 0028785535 scopus 로고
    • Functional expression of a single chain anti progesterone and body fragment in the cytoplasm of a mutant Escherichia coli
    • He, M., Hamenn, M., Liu, H., Kang, A., and Taussig, M. J. 1995. Functional expression of a single chain anti progesterone and body fragment in the cytoplasm of a mutant Escherichia coli. Nucleic Acids Res. 23: 4009-4010.
    • (1995) Nucleic Acids Res , vol.23 , pp. 4009-4010
    • He, M.1    Hamenn, M.2    Liu, H.3    Kang, A.4    Taussig, M.J.5
  • 123
    • 8344236780 scopus 로고    scopus 로고
    • Cell cultures for the production of recombinant proteins
    • Hellwig, S., Drossard, J., Twyman, R. M., and Fischer, R. 2004. Cell cultures for the production of recombinant proteins. Nat. Biotechnol. 22: 1415-1422.
    • (2004) Nat. Biotechnol , vol.22 , pp. 1415-1422
    • Hellwig, S.1    Drossard, J.2    Twyman, R.M.3    Fischer, R.4
  • 124
    • 0027425585 scopus 로고    scopus 로고
    • Hendrick, J. P., Langer, T., Davis, T. A., Hartal, F. U., and Wiedmann, M. 1993. Control of folding and membrane translocation by binding of the chaperone Dna J to nascent polypeptide. Proc. Natl. Acad. Sci. USA 90: 10216-10220.
    • Hendrick, J. P., Langer, T., Davis, T. A., Hartal, F. U., and Wiedmann, M. 1993. Control of folding and membrane translocation by binding of the chaperone Dna J to nascent polypeptide. Proc. Natl. Acad. Sci. USA 90: 10216-10220.
  • 125
    • 33646077190 scopus 로고    scopus 로고
    • Functional expression of single-chain variable fragment antibody against c-Met in the cytoplasm of Escherichia coli
    • Heo, M. A., Kim, S. H., Kim, S. Y., Kim, Y. J., Chung, J., Oh, M. K., and Lee, S. G. 2006. Functional expression of single-chain variable fragment antibody against c-Met in the cytoplasm of Escherichia coli. Protein Expr. Purif. 47(1): 203-209.
    • (2006) Protein Expr. Purif , vol.47 , Issue.1 , pp. 203-209
    • Heo, M.A.1    Kim, S.H.2    Kim, S.Y.3    Kim, Y.J.4    Chung, J.5    Oh, M.K.6    Lee, S.G.7
  • 126
    • 0026557391 scopus 로고
    • Protein interaction with ice
    • Hew, C. L., and Yang, D. S. C. 1992. Protein interaction with ice. Eur. J. Biochem. 203: 33-42.
    • (1992) Eur. J. Biochem , vol.203 , pp. 33-42
    • Hew, C.L.1    Yang, D.S.C.2
  • 127
    • 0035371799 scopus 로고    scopus 로고
    • The role of aquatic biotechnology in aquaculture
    • Hew, C., and Fletcher, G. 2001. The role of aquatic biotechnology in aquaculture. Aquaculture 197:191-204.
    • (2001) Aquaculture , vol.197 , pp. 191-204
    • Hew, C.1    Fletcher, G.2
  • 129
    • 0035812288 scopus 로고    scopus 로고
    • Targeted expression of a synthetic codon optimized gene, encoding the spruce budworm antifreeze protein, leads to accumulation of antifreeze activity in the apoplasts of transgenic tobacco
    • Holmberg, N., Farrés, J., Bailey, J. E., and Kallio, P. T. 2001. Targeted expression of a synthetic codon optimized gene, encoding the spruce budworm antifreeze protein, leads to accumulation of antifreeze activity in the apoplasts of transgenic tobacco. Gene 275: 115-124.
    • (2001) Gene , vol.275 , pp. 115-124
    • Holmberg, N.1    Farrés, J.2    Bailey, J.E.3    Kallio, P.T.4
  • 132
    • 0033148013 scopus 로고    scopus 로고
    • Physiological and biochemical significance of antifreeze substances in plants
    • Hoshino, T., Odaira, M., Yoshida, M., and Tsuda, S. 1999. Physiological and biochemical significance of antifreeze substances in plants. J. Plant Res. 112: 255-261.
    • (1999) J. Plant Res , vol.112 , pp. 255-261
    • Hoshino, T.1    Odaira, M.2    Yoshida, M.3    Tsuda, S.4
  • 133
    • 0036790314 scopus 로고    scopus 로고
    • Expression of an insect (Dendroides canadensis) antifreeze protein in Arabidopsis thaliana results in a decrease in plant freezing temperature
    • Huang, T., Nicodemus, J., and Zarka, D. G., Thomashow, M. F., Wisniewski, M., and Duman, J. G. 2002. Expression of an insect (Dendroides canadensis) antifreeze protein in Arabidopsis thaliana results in a decrease in plant freezing temperature. Plant Mol. Biol. 50: 333-344.
    • (2002) Plant Mol. Biol , vol.50 , pp. 333-344
    • Huang, T.1    Nicodemus, J.2    Zarka, D.G.3    Thomashow, M.F.4    Wisniewski, M.5    Duman, J.G.6
  • 134
    • 0032878235 scopus 로고    scopus 로고
    • High level expression of Thermococcus litoralis 4-α-glucanotransferase in a soluble form in Escherichia coli with a novel expression system involving minor arginine tRNAs and GroELS
    • Imamura, H., Jeon, B. S., Wakagi, T., and Matsuzawa, H. 1999. High level expression of Thermococcus litoralis 4-α-glucanotransferase in a soluble form in Escherichia coli with a novel expression system involving minor arginine tRNAs and GroELS. FEBS Lett. 457:393-396.
    • (1999) FEBS Lett , vol.457 , pp. 393-396
    • Imamura, H.1    Jeon, B.S.2    Wakagi, T.3    Matsuzawa, H.4
  • 135
    • 33745341890 scopus 로고    scopus 로고
    • Diffusion NMR studies on fish antifreeze proteins and synthetic analogues
    • Inglis, S. R., McGann, M. J., Price, W. S., and Harding, M. M. 2006. Diffusion NMR studies on fish antifreeze proteins and synthetic analogues. FEBS Letters. 580: 3911-3915.
    • (2006) FEBS Letters , vol.580 , pp. 3911-3915
    • Inglis, S.R.1    McGann, M.J.2    Price, W.S.3    Harding, M.M.4
  • 136
    • 0032108477 scopus 로고    scopus 로고
    • Influence of fish antifreeze proteins on the freezing of cell suspensions with cryoprotectant penetrating cells
    • Ishiguo, H., and Rubinsky, B. 1998. Influence of fish antifreeze proteins on the freezing of cell suspensions with cryoprotectant penetrating cells. Int. J. Heat. Mass Trans. 41(13): 1907-1915.
    • (1998) Int. J. Heat. Mass Trans , vol.41 , Issue.13 , pp. 1907-1915
    • Ishiguo, H.1    Rubinsky, B.2
  • 138
    • 0037137136 scopus 로고    scopus 로고
    • Contribution of hydrophobic residues to ice binding by fish type III antifreeze protein
    • Jason, B., and Davies, P. L. 2002. Contribution of hydrophobic residues to ice binding by fish type III antifreeze protein. Biochim. Biophys. Acta 1601: 49-54.
    • (2002) Biochim. Biophys. Acta , vol.1601 , pp. 49-54
    • Jason, B.1    Davies, P.L.2
  • 139
    • 0029856558 scopus 로고    scopus 로고
    • Structural basis for the binding of a globular antifreeze protein to ice
    • Jia, Z., DeLuca C. I., Chao, H., and Davies, P. L. 1996. Structural basis for the binding of a globular antifreeze protein to ice. Nature 384: 285-288.
    • (1996) Nature , vol.384 , pp. 285-288
    • Jia, Z.1    DeLuca, C.I.2    Chao, H.3    Davies, P.L.4
  • 140
    • 0032539933 scopus 로고    scopus 로고
    • Overexpression of Escherichia coli periplasmic oxidoreductases increases recombinant insulin-like growth factor-I accumulation
    • Joly, J. C., Leung, W. S., and Swartz, J. R. 1998. Overexpression of Escherichia coli periplasmic oxidoreductases increases recombinant insulin-like growth factor-I accumulation. Proc. Natl. Acad. Sci. USA 95: 2773-2777.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2773-2777
    • Joly, J.C.1    Leung, W.S.2    Swartz, J.R.3
  • 141
    • 0347803667 scopus 로고    scopus 로고
    • Effect of antifreeze protein glycoprotein on quality of cryo conserved carp sperm
    • Karanova, M. V., Zsvetkova, L. T., and Peterpavlov, N. N. 1997. Effect of antifreeze protein glycoprotein on quality of cryo conserved carp sperm. Biofizika 42(3): 725-728.
    • (1997) Biofizika , vol.42 , Issue.3 , pp. 725-728
    • Karanova, M.V.1    Zsvetkova, L.T.2    Peterpavlov, N.N.3
  • 142
    • 0036968804 scopus 로고    scopus 로고
    • The structures and functions of ice crystal-controlling proteins from bacteria
    • Kawahara, H. 2002. The structures and functions of ice crystal-controlling proteins from bacteria. J. Biosci. Bioeng. 94(6): 492-496.
    • (2002) J. Biosci. Bioeng , vol.94 , Issue.6 , pp. 492-496
    • Kawahara, H.1
  • 143
    • 6944228892 scopus 로고    scopus 로고
    • Production of two types of ice crystal-controlling proteins in Antarctic bacterium
    • Kawahara, H., Nakano, Y., Omiya, K., Muryoi, O., Nishikawa, J., and Obata, H. 2004. Production of two types of ice crystal-controlling proteins in Antarctic bacterium. J. BioSci. Bioeng. 98(3): 220-223.
    • (2004) J. BioSci. Bioeng , vol.98 , Issue.3 , pp. 220-223
    • Kawahara, H.1    Nakano, Y.2    Omiya, K.3    Muryoi, O.4    Nishikawa, J.5    Obata, H.6
  • 144
    • 0027674917 scopus 로고
    • Accumulation of type I fish antifreeze protein in transgenic tobacco in cold specific
    • Kenward, K. D., Altschuler, M., Hilderbrand, D., and Davies, P. L. 1993. Accumulation of type I fish antifreeze protein in transgenic tobacco in cold specific. Plant Mol. Biol. 23: 377-385.
    • (1993) Plant Mol. Biol , vol.23 , pp. 377-385
    • Kenward, K.D.1    Altschuler, M.2    Hilderbrand, D.3    Davies, P.L.4
  • 145
    • 18144376288 scopus 로고    scopus 로고
    • Coexpression of folding accessory proteins for production of active cyclodextrin glycosyltransferase of Bacillus macerans in recombinant Escherichia coli
    • Kim, S. G., Kweon, D. H., Lee, D. H., Park, Y. C., and Seo, J. H. 2005. Coexpression of folding accessory proteins for production of active cyclodextrin glycosyltransferase of Bacillus macerans in recombinant Escherichia coli. Protein Expr. Purif. 41(2): 426-432.
    • (2005) Protein Expr. Purif , vol.41 , Issue.2 , pp. 426-432
    • Kim, S.G.1    Kweon, D.H.2    Lee, D.H.3    Park, Y.C.4    Seo, J.H.5
  • 146
    • 0027956170 scopus 로고
    • SecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state
    • Kim, Y. J., Rajapandi, T., and Oliver, D. 1994. SecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state. Cell 78: 845-853.
    • (1994) Cell , vol.78 , pp. 845-853
    • Kim, Y.J.1    Rajapandi, T.2    Oliver, D.3
  • 147
    • 0025959821 scopus 로고
    • Adsorption of alpha-helical antifreeze peptides on specific ice crystal surface planes
    • Knight, C. A., Cheng, C. C., and DeVries, A. L. 1991. Adsorption of alpha-helical antifreeze peptides on specific ice crystal surface planes. Biophys. J. 59: 409-18.
    • (1991) Biophys. J , vol.59 , pp. 409-418
    • Knight, C.A.1    Cheng, C.C.2    DeVries, A.L.3
  • 148
    • 0021236688 scopus 로고
    • Fish antifreeze protein and the freezing and recrystallization of ice
    • Knight, C. A., DeVries, A. L., and Oolman, L. D. 1984. Fish antifreeze protein and the freezing and recrystallization of ice. Nature 308: 295-296.
    • (1984) Nature , vol.308 , pp. 295-296
    • Knight, C.A.1    DeVries, A.L.2    Oolman, L.D.3
  • 149
    • 0027396926 scopus 로고
    • Adsorption to ice of fish antifreeze glycopeptides 7 and 8
    • Knight, C. A., Driggers, E., and DeVries, A. L. 1993. Adsorption to ice of fish antifreeze glycopeptides 7 and 8. Biophys. J. 64: 252-259.
    • (1993) Biophys. J , vol.64 , pp. 252-259
    • Knight, C.A.1    Driggers, E.2    DeVries, A.L.3
  • 150
    • 0023840588 scopus 로고
    • Solute effects on ice recrystallization: An assessment technique
    • Knight, C. A., Hallett, J., and DeVries, A. L. 1988. Solute effects on ice recrystallization: an assessment technique. Cryobiology 25: 55-60.
    • (1988) Cryobiology , vol.25 , pp. 55-60
    • Knight, C.A.1    Hallett, J.2    DeVries, A.L.3
  • 151
    • 0029248188 scopus 로고
    • Nonequilibrium antifreeze proteins and the recrystallization of ice
    • Knight, C. A., Wen, D., and Laursen, R. A. 1995. Nonequilibrium antifreeze proteins and the recrystallization of ice. Cryobiology 32: 23-34.
    • (1995) Cryobiology , vol.32 , pp. 23-34
    • Knight, C.A.1    Wen, D.2    Laursen, R.A.3
  • 153
    • 0034515175 scopus 로고    scopus 로고
    • Improvement of productivity of active horseradish peroxidase in Escherichia coli by coexpression of Dsb proteins
    • Kondo, A., Kohda, J., Endo, Y., Shiromizu, T., Kurokawa, Y., Nishihara, K., Yanagi, H., Yura, T., and Fukuda, H. 2000. Improvement of productivity of active horseradish peroxidase in Escherichia coli by coexpression of Dsb proteins. J. Biosci. Bioeng. 90(6): 600-606.
    • (2000) J. Biosci. Bioeng , vol.90 , Issue.6 , pp. 600-606
    • Kondo, A.1    Kohda, J.2    Endo, Y.3    Shiromizu, T.4    Kurokawa, Y.5    Nishihara, K.6    Yanagi, H.7    Yura, T.8    Fukuda, H.9
  • 154
    • 33847736199 scopus 로고    scopus 로고
    • Isolation and characterization of ice structuring proteins from cold-acclimated winter wheat grass extract for recrystallization inhibition in frozen foods
    • Kontogiorgos, V., Regand, A., Yada, R. Y., and Goff, H. D. 2007. Isolation and characterization of ice structuring proteins from cold-acclimated winter wheat grass extract for recrystallization inhibition in frozen foods. J. Food Biochem. 31: 139-160.
    • (2007) J. Food Biochem , vol.31 , pp. 139-160
    • Kontogiorgos, V.1    Regand, A.2    Yada, R.Y.3    Goff, H.D.4
  • 155
    • 0030615223 scopus 로고    scopus 로고
    • Effect of antifreeze proteins on frozen primary prostatic adenocarcinoma cells
    • Koushafar, H., and Rubinsky, B. 1997. Effect of antifreeze proteins on frozen primary prostatic adenocarcinoma cells. Urology 49: 421-425.
    • (1997) Urology , vol.49 , pp. 421-425
    • Koushafar, H.1    Rubinsky, B.2
  • 156
    • 0030734067 scopus 로고    scopus 로고
    • Chemical adjuvant cryosurgery with antifreeze proteins
    • Koushafar, H., Pham, L., Lee, C., and Rubinsky, B. 1997. Chemical adjuvant cryosurgery with antifreeze proteins. J. Surg. Oncol. 66: 114-121.
    • (1997) J. Surg. Oncol , vol.66 , pp. 114-121
    • Koushafar, H.1    Pham, L.2    Lee, C.3    Rubinsky, B.4
  • 158
    • 28744456989 scopus 로고    scopus 로고
    • The mechanism by which fish antifreeze proteins cause thermal hysteresis
    • Kristiansen, E., and Zachariassen, K. E. 2005. The mechanism by which fish antifreeze proteins cause thermal hysteresis. Cryobiology 51: 262-280.
    • (2005) Cryobiology , vol.51 , pp. 262-280
    • Kristiansen, E.1    Zachariassen, K.E.2
  • 159
    • 0033827610 scopus 로고    scopus 로고
    • Overexpression of protein disulfide isomerase DsbC stabilizes multiple disulfide-bonded recombinant protein produced and transported to the periplasm in Escherichia coli
    • Kurokawa, Y., Yanagi, H., and Yura, T. 2000. Overexpression of protein disulfide isomerase DsbC stabilizes multiple disulfide-bonded recombinant protein produced and transported to the periplasm in Escherichia coli. Appl. Environ. Microbiol. 66(9): 3960-3965.
    • (2000) Appl. Environ. Microbiol , vol.66 , Issue.9 , pp. 3960-3965
    • Kurokawa, Y.1    Yanagi, H.2    Yura, T.3
  • 160
    • 0035957961 scopus 로고    scopus 로고
    • Overproduction of bacterial protein disulfide isomerase (DsbC) and its modulator (DsbD) markedly enhances periplasmic production of human nerve growth factor in Escherichia coli
    • Kurokawa, Y., Yanagi, H., and Yura, T. 2001. Overproduction of bacterial protein disulfide isomerase (DsbC) and its modulator (DsbD) markedly enhances periplasmic production of human nerve growth factor in Escherichia coli. J. Biol. Chem. 276: 14393-14399.
    • (2001) J. Biol. Chem , vol.276 , pp. 14393-14399
    • Kurokawa, Y.1    Yanagi, H.2    Yura, T.3
  • 161
    • 0031555505 scopus 로고    scopus 로고
    • Production of recombinant proteins in transgenic plants: Practical considerations
    • Kusnadi, A. R., Nikolov, Z. L., and Howard, J. A. 1997. Production of recombinant proteins in transgenic plants: practical considerations. Biotechnol. Bioeng. 56: 473-484.
    • (1997) Biotechnol. Bioeng , vol.56 , pp. 473-484
    • Kusnadi, A.R.1    Nikolov, Z.L.2    Howard, J.A.3
  • 162
    • 0001844730 scopus 로고
    • Hypothermic preservation of whole mammalian organs with antifreeze proteins
    • Lee, C. Y., Rubinsky, B., and Fletcher, G. L. 1992. Hypothermic preservation of whole mammalian organs with antifreeze proteins. Cryo Letters 13: 59-66.
    • (1992) Cryo Letters , vol.13 , pp. 59-66
    • Lee, C.Y.1    Rubinsky, B.2    Fletcher, G.L.3
  • 163
    • 0037031949 scopus 로고    scopus 로고
    • α-Helical antifreeze protein isoform with increased activity-structural and functional insights
    • Leinala, E. K., Davies, P. L., Doucet, D., Tyshenko, M. G., Walker, V. K., and Jia, Z. 2002. α-Helical antifreeze protein isoform with increased activity-structural and functional insights. J. Biol. Chem. 277(36): 33349-33352.
    • (2002) J. Biol. Chem , vol.277 , Issue.36 , pp. 33349-33352
    • Leinala, E.K.1    Davies, P.L.2    Doucet, D.3    Tyshenko, M.G.4    Walker, V.K.5    Jia, Z.6
  • 164
    • 0034756555 scopus 로고    scopus 로고
    • Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones
    • Levy, R., Weiss, R., Chen, G., Iverson, B. L., and Georgiou, G. 2001. Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones. Protein Expr. Purif. 23: 338-347.
    • (2001) Protein Expr. Purif , vol.23 , pp. 338-347
    • Levy, R.1    Weiss, R.2    Chen, G.3    Iverson, B.L.4    Georgiou, G.5
  • 165
    • 0032407543 scopus 로고    scopus 로고
    • Secondary structure of antifreeze proteins from overwintering larvae of the beetle Dendroides canadensis
    • Li, N., Kendrick, B. S., Manning, M. C., Carpenter, J. F., and Duman, J. G. 1998. Secondary structure of antifreeze proteins from overwintering larvae of the beetle Dendroides canadensis. Arch. Biochem. Biophys. 360: 25-32.
    • (1998) Arch. Biochem. Biophys , vol.360 , pp. 25-32
    • Li, N.1    Kendrick, B.S.2    Manning, M.C.3    Carpenter, J.F.4    Duman, J.G.5
  • 166
    • 0026331527 scopus 로고    scopus 로고
    • Li, X., and Hew, C. L. 1991. Expression and characterization of an active and thermally more stable recombinant antifreeze polypeptide from ocean pout, Macrozoarces americanus, in Escherichia coli: improved expression by modifying the secondary structure of the mRNA. Protein Eng. 4: 996-1002.
    • Li, X., and Hew, C. L. 1991. Expression and characterization of an active and thermally more stable recombinant antifreeze polypeptide from ocean pout, Macrozoarces americanus, in Escherichia coli: improved expression by modifying the secondary structure of the mRNA. Protein Eng. 4: 996-1002.
  • 167
    • 0035715001 scopus 로고    scopus 로고
    • Low-temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris
    • Li, Z., Xiong, F., Lin, Q., d'Anjou, M., Daugulis, A. J., Yang, D. S. C., and Hew, C. L. 2001a. Low-temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris. Protein Expr. Purif. 21: 438-445.
    • (2001) Protein Expr. Purif , vol.21 , pp. 438-445
    • Li, Z.1    Xiong, F.2    Lin, Q.3    d'Anjou, M.4    Daugulis, A.J.5    Yang, D.S.C.6    Hew, C.L.7
  • 168
    • 0035812938 scopus 로고    scopus 로고
    • The chaperone activity of trigger factor is distinct from its isomerase activity during co-expression with adenylate kinase in Escherichia coli
    • Li, Z. Y., Liu, C. P., Zhu, L. Q., Jing, G. Z., and Zhou, J. M. 2001b. The chaperone activity of trigger factor is distinct from its isomerase activity during co-expression with adenylate kinase in Escherichia coli. FEBS Lett. 506(2): 108-112.
    • (2001) FEBS Lett , vol.506 , Issue.2 , pp. 108-112
    • Li, Z.Y.1    Liu, C.P.2    Zhu, L.Q.3    Jing, G.Z.4    Zhou, J.M.5
  • 169
    • 0028602825 scopus 로고
    • Antifreeze proteins
    • Lillford, P. J., and Holt, C. B. 1994. Antifreeze proteins. J. Food Eng. 22: 475-482.
    • (1994) J. Food Eng , vol.22 , pp. 475-482
    • Lillford, P.J.1    Holt, C.B.2
  • 170
    • 0034084576 scopus 로고    scopus 로고
    • Folding and structural characterization of highly disulfide-bonded beetle antifreeze protein produced in bacteria
    • Liou, Y. C., Margaret, E., Daley, Graham, L. A., Kay, C. M., Walker, V. K., Sykes, B. D., and Davies, P. L. 2000a. Folding and structural characterization of highly disulfide-bonded beetle antifreeze protein produced in bacteria. Protein Expr. Purif. 19: 148-157.
    • (2000) Protein Expr. Purif , vol.19 , pp. 148-157
    • Liou, Y.1    Margaret, C.2    Daley, E.3    Graham, L.A.4    Kay, C.M.5    Walker, V.K.6    Sykes, B.D.7    Davies, P.L.8
  • 171
    • 0034691568 scopus 로고    scopus 로고
    • Mimicry of ice structure by surface hydroxyls and water of a beta-helix antifreeze protein
    • Liou, Y. C., Tocilj, A., Davies, P. L., and Jia, Z. 2000b. Mimicry of ice structure by surface hydroxyls and water of a beta-helix antifreeze protein. Nature 406: 322-324.
    • (2000) Nature , vol.406 , pp. 322-324
    • Liou, Y.C.1    Tocilj, A.2    Davies, P.L.3    Jia, Z.4
  • 172
    • 0033621028 scopus 로고    scopus 로고
    • A complex family of highly heterogeneous and internally repetitive hyperactive antifreeze proteins from the beetle Tenebrio molitor
    • Liou, Y. C., Thibault, P., Walker, V. K., Davies, P. L., and Graham, L. A. 1999. A complex family of highly heterogeneous and internally repetitive hyperactive antifreeze proteins from the beetle Tenebrio molitor, Biochemisty 38: 11415-11424.
    • (1999) Biochemisty , vol.38 , pp. 11415-11424
    • Liou, Y.C.1    Thibault, P.2    Walker, V.K.3    Davies, P.L.4    Graham, L.A.5
  • 173
    • 33646049352 scopus 로고    scopus 로고
    • Theoretical model of antifreeze protein-ice adsorption: Binding of large ligands to a two-dimensional homogeneous lattice
    • Liu, J., and Li, Q. 2006. Theoretical model of antifreeze protein-ice adsorption: binding of large ligands to a two-dimensional homogeneous lattice. Chem. Phys. Lett. 422: 67-71.
    • (2006) Chem. Phys. Lett , vol.422 , pp. 67-71
    • Liu, J.1    Li, Q.2
  • 175
    • 0032559044 scopus 로고    scopus 로고
    • The ice-binding site of sea raven antifreeze protein is distinct from the carbohydrate-binding site of the homologous Ctype lectin
    • Loewen, M. C., Gronwald, W., Sonnichsen, F. D., Sykes, B. D., and Davies, P. L. 1998. The ice-binding site of sea raven antifreeze protein is distinct from the carbohydrate-binding site of the homologous Ctype lectin. Biochemistry 37: 17745-17753.
    • (1998) Biochemistry , vol.37 , pp. 17745-17753
    • Loewen, M.C.1    Gronwald, W.2    Sonnichsen, F.D.3    Sykes, B.D.4    Davies, P.L.5
  • 176
    • 21944456915 scopus 로고    scopus 로고
    • Secretory antifreeze proteins produced in suspension culture cells of Rhodiola algida var. tangutica during cold acclimation
    • Lu, C. F., Jian, L. C., and Kuang, T. Y. 2000. Secretory antifreeze proteins produced in suspension culture cells of Rhodiola algida var. tangutica during cold acclimation. Prog. Biochem. Biophys. 27: 555-559.
    • (2000) Prog. Biochem. Biophys , vol.27 , pp. 555-559
    • Lu, C.F.1    Jian, L.C.2    Kuang, T.Y.3
  • 178
    • 0344234368 scopus 로고    scopus 로고
    • Safety evaluation of ice-structuring protein (ISP) type III HPLC 12 preparation. Lack of genotoxicity and subchronic toxicity
    • Manning, T. H., Spurgeon, M., Wolfreys, A. M., and Baldrick, A. P. 2004. Safety evaluation of ice-structuring protein (ISP) type III HPLC 12 preparation. Lack of genotoxicity and subchronic toxicity. Food and Chemical Toxicology. 42: 321-333.
    • (2004) Food and Chemical Toxicology , vol.42 , pp. 321-333
    • Manning, T.H.1    Spurgeon, M.2    Wolfreys, A.M.3    Baldrick, A.P.4
  • 179
    • 0033810061 scopus 로고    scopus 로고
    • Recombinant maize protoporpyrinogen IX oxidase expressed in Escherichia coli forms complexes with GroEL and DnaK chaperones
    • Marco, A., Volrath, S., Bruyere, T., Law, M., and Pfister, R. F. 2000. Recombinant maize protoporpyrinogen IX oxidase expressed in Escherichia coli forms complexes with GroEL and DnaK chaperones. Protein Expr. Purif. 20: 81-86.
    • (2000) Protein Expr. Purif , vol.20 , pp. 81-86
    • Marco, A.1    Volrath, S.2    Bruyere, T.3    Law, M.4    Pfister, R.F.5
  • 180
    • 2442688072 scopus 로고    scopus 로고
    • Hyperactive antifreeze protein in a fish
    • Marshall, C. B., Fletcher, G. L., and Davies, P. L. 2004. Hyperactive antifreeze protein in a fish. Nature 29(6988): 153.
    • (2004) Nature , vol.29 , Issue.6988 , pp. 153
    • Marshall, C.B.1    Fletcher, G.L.2    Davies, P.L.3
  • 181
    • 0037229810 scopus 로고    scopus 로고
    • DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo
    • Maskos, K., Huber-Wunderlich, M., and Glockshuber, R. 2003. DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo. J. Mol. Biol. 325(3): 495-513.
    • (2003) J. Mol. Biol , vol.325 , Issue.3 , pp. 495-513
    • Maskos, K.1    Huber-Wunderlich, M.2    Glockshuber, R.3
  • 182
    • 0034932595 scopus 로고    scopus 로고
    • Genes encoding chitinase antifreeze proteins are regulated by cold and expressed by all cell types in winter rye shoots
    • Maunsbach, P. K., Moffatt, B., Testillano, P., Risueno, M., Yeh, S., Griffith, M., and Maunsbach, A. B. 2001. Genes encoding chitinase antifreeze proteins are regulated by cold and expressed by all cell types in winter rye shoots. Physiol. Plantarum 112(3): 359-371.
    • (2001) Physiol. Plantarum , vol.112 , Issue.3 , pp. 359-371
    • Maunsbach, P.K.1    Moffatt, B.2    Testillano, P.3    Risueno, M.4    Yeh, S.5    Griffith, M.6    Maunsbach, A.B.7
  • 185
    • 0029187610 scopus 로고
    • Expression of foreign proteins in Trichoplusia ni larvae
    • Medin, J. A., Gathy, K., Coleman, M. S. 1995. Expression of foreign proteins in Trichoplusia ni larvae. Methods Mol Biol. 39: 265-275.
    • (1995) Methods Mol Biol , vol.39 , pp. 265-275
    • Medin, J.A.1    Gathy, K.2    Coleman, M.S.3
  • 186
    • 0025349629 scopus 로고
    • Efficient, low-cost protein factories: Expression of human adenosine deaminase in baculovirus-infected insect larvae
    • Medin, J. A., Hunt, L., Gathy, K., Evans, R. K., and Coleman, M. S. 1990. Efficient, low-cost protein factories: expression of human adenosine deaminase in baculovirus-infected insect larvae. Proc Natl Acad Sci USA. 87(7): 2760-2764.
    • (1990) Proc Natl Acad Sci USA , vol.87 , Issue.7 , pp. 2760-2764
    • Medin, J.A.1    Hunt, L.2    Gathy, K.3    Evans, R.K.4    Coleman, M.S.5
  • 188
    • 0032973262 scopus 로고    scopus 로고
    • A leucine-rich repeat protein of carrot that exhibits antifreeze activity
    • Meyer, K., Keil, M., and Naldrett, M. J. 1999. A leucine-rich repeat protein of carrot that exhibits antifreeze activity. FEBS Lett. 447: 171-178.
    • (1999) FEBS Lett , vol.447 , pp. 171-178
    • Meyer, K.1    Keil, M.2    Naldrett, M.J.3
  • 189
    • 40349102552 scopus 로고    scopus 로고
    • Anti-freeze proteins: Prospects and perspectives in food sector
    • Mishra, V., and Pattnaik, P. 1999. Anti-freeze proteins: prospects and perspectives in food sector. Ind. Food Industry 18(4): 238-244.
    • (1999) Ind. Food Industry , vol.18 , Issue.4 , pp. 238-244
    • Mishra, V.1    Pattnaik, P.2
  • 190
    • 0032519332 scopus 로고    scopus 로고
    • Production of soluble single chain T cell receptor fragments in E. coli trxB mutants
    • Molloy, P. E., Harris, W. J., Strachan, G., Watts, C., and Cunningham, C. 1998. Production of soluble single chain T cell receptor fragments in E. coli trxB mutants. Mol. Immunol. 35: 73-81.
    • (1998) Mol. Immunol , vol.35 , pp. 73-81
    • Molloy, P.E.1    Harris, W.J.2    Strachan, G.3    Watts, C.4    Cunningham, C.5
  • 191
    • 0039700271 scopus 로고    scopus 로고
    • Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from Escherichia coli
    • Mossner, E., Wunderlich, M. H., Rietsch, A., Beckwith, J., Gluckshuber, R., and Aslund, F. 1999. Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from Escherichia coli. J. Biol. Chem. 274: 25254-25259.
    • (1999) J. Biol. Chem , vol.274 , pp. 25254-25259
    • Mossner, E.1    Wunderlich, M.H.2    Rietsch, A.3    Beckwith, J.4    Gluckshuber, R.5    Aslund, F.6
  • 192
    • 0025807690 scopus 로고
    • Inhibition of recrystallization in ice by chimeric proteins containing antifreeze domains
    • Mueller, G. M., McKown, R. L., Corotto, L. V., Hague, C., and Warren, G. J. 1991. Inhibition of recrystallization in ice by chimeric proteins containing antifreeze domains. J. Biol. Chem. 266: 7339-7344.
    • (1991) J. Biol. Chem , vol.266 , pp. 7339-7344
    • Mueller, G.M.1    McKown, R.L.2    Corotto, L.V.3    Hague, C.4    Warren, G.J.5
  • 193
    • 0032883737 scopus 로고    scopus 로고
    • Cold-inducible cloning vectors for low temperature protein expression in Escherichia coli: Application to the production of a toxic and proteolytically sensitive fusion protein
    • Mujacic, M., Cooper, K. W., and Baneyx, F. 1999. Cold-inducible cloning vectors for low temperature protein expression in Escherichia coli: application to the production of a toxic and proteolytically sensitive fusion protein. Gene 238: 325-332.
    • (1999) Gene , vol.238 , pp. 325-332
    • Mujacic, M.1    Cooper, K.W.2    Baneyx, F.3
  • 195
    • 0031448840 scopus 로고    scopus 로고
    • Cryopreservative of Crassostrea gigas oocytes embryo and larvae using antioxidants echinochromes A and antifreeze protein AFP-I
    • Naidenko, T. 1997. Cryopreservative of Crassostrea gigas oocytes embryo and larvae using antioxidants echinochromes A and antifreeze protein AFP-I. Cryo Letters 18: 375-382.
    • (1997) Cryo Letters , vol.18 , pp. 375-382
    • Naidenko, T.1
  • 197
    • 33746316803 scopus 로고    scopus 로고
    • Expression of beetle, Dendroides canadenis antifreeze protein in Drosophila melanogaster
    • Nicodemus, J., Otousa, J. E., and Duman, J. G. 2006. Expression of beetle, Dendroides canadenis antifreeze protein in Drosophila melanogaster. J. Insect. Physiol. 52: 888-896.
    • (2006) J. Insect. Physiol , vol.52 , pp. 888-896
    • Nicodemus, J.1    Otousa, J.E.2    Duman, J.G.3
  • 198
    • 0031860811 scopus 로고    scopus 로고
    • Chaperone co-expression plasmids differential and synergistic roles in DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2 in Escherichia coli
    • Nishihara, K., Kanemori, M., Kitagawa, M., Yanagi, H., and Yura, T. 1998. Chaperone co-expression plasmids differential and synergistic roles in DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2 in Escherichia coli. Appl. Environ. Microbiol. 64(5): 1694-1699.
    • (1998) Appl. Environ. Microbiol , vol.64 , Issue.5 , pp. 1694-1699
    • Nishihara, K.1    Kanemori, M.2    Kitagawa, M.3    Yanagi, H.4    Yura, T.5
  • 199
    • 0034050548 scopus 로고    scopus 로고
    • Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli
    • Nishihara, K., Kanemori, M., Yanagi, H., and Yura, T. 2000. Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli. Appl. Environ. Microbiol. 66(3): 884-889.
    • (2000) Appl. Environ. Microbiol , vol.66 , Issue.3 , pp. 884-889
    • Nishihara, K.1    Kanemori, M.2    Yanagi, H.3    Yura, T.4
  • 200
    • 0007568005 scopus 로고    scopus 로고
    • Antifreeze glycoproteins can protect human platelets from cold-induced activation and prevent lateral-phase separation in membranes below the phase-transition temperature
    • Oliver, A. E., Tablin, F., Crowe, J. H., Tsvetkova, N. M., Fisk, E. L., Walker, N. J., Hays, L. M., Crowe, L. M., and Feeney, R. E. 1997. Antifreeze glycoproteins can protect human platelets from cold-induced activation and prevent lateral-phase separation in membranes below the phase-transition temperature. Cryobiology 35:333-334.
    • (1997) Cryobiology , vol.35 , pp. 333-334
    • Oliver, A.E.1    Tablin, F.2    Crowe, J.H.3    Tsvetkova, N.M.4    Fisk, E.L.5    Walker, N.J.6    Hays, L.M.7    Crowe, L.M.8    Feeney, R.E.9
  • 201
    • 0030933727 scopus 로고    scopus 로고
    • Maintenance of the supercooled state in overwintering pyrochroid beetle larvae Dendroides canadensis: Role of hemolymph ice nucleators and antifreeze proteins
    • Olsen, T. M., and Duman, J. G. 1997. Maintenance of the supercooled state in overwintering pyrochroid beetle larvae Dendroides canadensis: role of hemolymph ice nucleators and antifreeze proteins. J. Comp. Physiol. 167: 105-113.
    • (1997) J. Comp. Physiol , vol.167 , pp. 105-113
    • Olsen, T.M.1    Duman, J.G.2
  • 202
    • 0031874946 scopus 로고    scopus 로고
    • Factors contributing to seasonal increases in inoculative freezing resistance in overwintering fire-colored beetle larvae Dendroides canadensis (Pyrochroidae)
    • Olsen, T. M., and Duman, J. G. 1998. Factors contributing to seasonal increases in inoculative freezing resistance in overwintering fire-colored beetle larvae Dendroides canadensis (Pyrochroidae). J. Exp. Biol. 201: 1585-1594.
    • (1998) J. Exp. Biol , vol.201 , pp. 1585-1594
    • Olsen, T.M.1    Duman, J.G.2
  • 203
    • 15844371986 scopus 로고    scopus 로고
    • Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases in the yield of a heterologous secreted protein with disulfide bonds
    • Ostermeier, M., De Sutter, K., and Georgiou, G. 1996. Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases in the yield of a heterologous secreted protein with disulfide bonds. J. Biol. Chem. 271: 10616-10622.
    • (1996) J. Biol. Chem , vol.271 , pp. 10616-10622
    • Ostermeier, M.1    De Sutter, K.2    Georgiou, G.3
  • 204
    • 0029710025 scopus 로고    scopus 로고
    • Cryopreservation of mammalian embryos and oocytes
    • Palasz, A. T., and Mapletoft, R. J. 1996. Cryopreservation of mammalian embryos and oocytes. Recent Adv. Biotechnol. Adv. 14(2): 127-149.
    • (1996) Recent Adv. Biotechnol. Adv , vol.14 , Issue.2 , pp. 127-149
    • Palasz, A.T.1    Mapletoft, R.J.2
  • 206
    • 0026477999 scopus 로고
    • Fish allergy: Evaluation of the importance of cross-reactivity
    • Pascual, C., Martin, M., Esteban, M., and Crespo, J. F. 1992. Fish allergy: evaluation of the importance of cross-reactivity. Journal of Paediatrics'. 121: 29-34.
    • (1992) Journal of Paediatrics , vol.121 , pp. 29-34
    • Pascual, C.1    Martin, M.2    Esteban, M.3    Crespo, J.F.4
  • 207
    • 21844481638 scopus 로고
    • Effects of pre-slaughter administration of antifreeze proteins on frozen meat quality
    • Payne, S. R., and Young, O. A. 1995. Effects of pre-slaughter administration of antifreeze proteins on frozen meat quality. Meat Sci. 41: 147-155.
    • (1995) Meat Sci , vol.41 , pp. 147-155
    • Payne, S.R.1    Young, O.A.2
  • 208
    • 21344488051 scopus 로고
    • The effects of antifreeze proteins on chilled and frozen meats
    • Payne, S. R., Sandford, D., Harris, A., and Young, O. A. 1994. The effects of antifreeze proteins on chilled and frozen meats. Meat Sci. 37: 429-438.
    • (1994) Meat Sci , vol.37 , pp. 429-438
    • Payne, S.R.1    Sandford, D.2    Harris, A.3    Young, O.A.4
  • 209
    • 14744301100 scopus 로고
    • Increasing the efficiency of protein export in Escherichia coli
    • Perez-Perez, J., Marquez, G., Barbero, J. L., and Gutierrez, J. 1994. Increasing the efficiency of protein export in Escherichia coli. Biotechnology 12:178-180.
    • (1994) Biotechnology , vol.12 , pp. 178-180
    • Perez-Perez, J.1    Marquez, G.2    Barbero, J.L.3    Gutierrez, J.4
  • 210
    • 0024828809 scopus 로고
    • Biosynthesis of winter flounder antifreeze proprotein in E. coli
    • Peters, I. D., Hew C. L., and Davies, P. L. 1989. Biosynthesis of winter flounder antifreeze proprotein in E. coli. Protein Eng. 3: 145-151.
    • (1989) Protein Eng , vol.3 , pp. 145-151
    • Peters, I.D.1    Hew, C.L.2    Davies, P.L.3
  • 211
    • 0032792524 scopus 로고    scopus 로고
    • An in vivo study of antifreeze protein adjuvant cryosurgery
    • Pham, L., Dahiya, R., and Rubinsky, B. 1999. An in vivo study of antifreeze protein adjuvant cryosurgery. Cryobiology 38: 169-175.
    • (1999) Cryobiology , vol.38 , pp. 169-175
    • Pham, L.1    Dahiya, R.2    Rubinsky, B.3
  • 212
    • 0003220389 scopus 로고
    • Freeze-drying of proteins: Process, formulation, and stability
    • Cleland, J. L, and Langer, R, Eds, American Chemical Society, Washington, DC
    • Pikal, M. J. 1994. Freeze-drying of proteins: process, formulation, and stability. In: Cleland, J. L., and Langer, R. (Eds.), Formulation and Delivery of Protein and Peptides. pp. 120-133. American Chemical Society, Washington, DC.
    • (1994) Formulation and Delivery of Protein and Peptides , pp. 120-133
    • Pikal, M.J.1
  • 213
    • 0026493276 scopus 로고
    • Formulation and stability of freeze-dried proteins. Effect of moisture and oxygen on the stability of freeze-dried formulations of human growth hormone
    • Pikal, M. J., Dellerman, K., and Roy, M. L. 1990. Formulation and stability of freeze-dried proteins. Effect of moisture and oxygen on the stability of freeze-dried formulations of human growth hormone. Dev. Biol. Stand. 74: 21-37.
    • (1990) Dev. Biol. Stand , vol.74 , pp. 21-37
    • Pikal, M.J.1    Dellerman, K.2    Roy, M.L.3
  • 214
    • 0034671999 scopus 로고    scopus 로고
    • Protein denaturation during freezing and thawing in phosphate buffer systems: Monomeric and tetrameric β-galactosidase
    • Pikal-Cleland, K. A., Rodriguez-Hornedo, N., Amidon, G. L., and Carpenter, J. F. 2000. Protein denaturation during freezing and thawing in phosphate buffer systems: monomeric and tetrameric β-galactosidase. Arch. Biochem. Biophys. 384(2): 398-406.
    • (2000) Arch. Biochem. Biophys , vol.384 , Issue.2 , pp. 398-406
    • Pikal-Cleland, K.A.1    Rodriguez-Hornedo, N.2    Amidon, G.L.3    Carpenter, J.F.4
  • 216
    • 33749236097 scopus 로고    scopus 로고
    • Impact of antifreeze proteins and antifreeze glycoproteins on bovine sperm during freeze-thaw
    • Prathalingam, N. S., Holt, W. V., Revell, S.G., Mirczuk, S., Fleck, R. A., and Watson, P. F. 2006. Impact of antifreeze proteins and antifreeze glycoproteins on bovine sperm during freeze-thaw.Theriogenology 66(8): 1894-1900.
    • (2006) Theriogenology , vol.66 , Issue.8 , pp. 1894-1900
    • Prathalingam, N.S.1    Holt, W.V.2    Revell, S.G.3    Mirczuk, S.4    Fleck, R.A.5    Watson, P.F.6
  • 217
    • 0024516350 scopus 로고
    • Complementation of recombinant baculovirus by co-infection with wild-type virus facilitates production in insect larvae of antigen proteins of hepatitis B virus and influenza virus
    • Price, P. M., Reichelderfer, C. F., Johanssor, B. E., Kilebourne, E. D., and Acs, G. 1989. Complementation of recombinant baculovirus by co-infection with wild-type virus facilitates production in insect larvae of antigen proteins of hepatitis B virus and influenza virus. Proc. Natl. Acad. Sci. USA 86: 1453-1456.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1453-1456
    • Price, P.M.1    Reichelderfer, C.F.2    Johanssor, B.E.3    Kilebourne, E.D.4    Acs, G.5
  • 218
    • 0029068068 scopus 로고
    • Functional antibody single chain fragments form the cytoplasm of Escherichia coli: Influence of thioredoxin reductase (TrxB)
    • Proba, K., Ge, L., and Pluckthun, A. 1995. Functional antibody single chain fragments form the cytoplasm of Escherichia coli: influence of thioredoxin reductase (TrxB). Gene 159: 203-207.
    • (1995) Gene , vol.159 , pp. 203-207
    • Proba, K.1    Ge, L.2    Pluckthun, A.3
  • 219
    • 0003067815 scopus 로고
    • Supercooling points and water content in Acari
    • Pugh, P. J. A. 1994. Supercooling points and water content in Acari. Acta Ecol. 15: 71-77.
    • (1994) Acta Ecol , vol.15 , pp. 71-77
    • Pugh, P.J.A.1
  • 221
    • 0042183228 scopus 로고
    • Adsorption inhibition as a mechanism of freezing resistance in polar fishes
    • Raymond, J. A., and DeVries, A. L. 1977. Adsorption inhibition as a mechanism of freezing resistance in polar fishes. Proc. Natl. Acad. Sci. USA 74: 2589-2593.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 2589-2593
    • Raymond, J.A.1    DeVries, A.L.2
  • 222
    • 0036171347 scopus 로고    scopus 로고
    • Semipurification and ice recrystallization inhibition activity of ice-active substances associated with Antarctic photosynthetic organisms
    • Raymond, J. A., and Fritsen, C. H. 2001. Semipurification and ice recrystallization inhibition activity of ice-active substances associated with Antarctic photosynthetic organisms. Cryobiology 43: 63-70.
    • (2001) Cryobiology , vol.43 , pp. 63-70
    • Raymond, J.A.1    Fritsen, C.H.2
  • 223
    • 0031766998 scopus 로고    scopus 로고
    • Procaryotic expression of single chain variable-fragment (scFv) antibodies: Secretion in L-form cells of Proteus mirabilis leads to active product and overcomes the limitations of periplasmic expression in Escherichia coli
    • Rippmann, J. F., Klein, M., Hoischen, C., Brocks, B., Rettig, W. J., Gumpert, J., Pfizenmaier, K., Mattes, R., and Moosmayer, D. 1998. Procaryotic expression of single chain variable-fragment (scFv) antibodies: secretion in L-form cells of Proteus mirabilis leads to active product and overcomes the limitations of periplasmic expression in Escherichia coli. Appl. Environ. Microbiol. 64: 4862-4869.
    • (1998) Appl. Environ. Microbiol , vol.64 , pp. 4862-4869
    • Rippmann, J.F.1    Klein, M.2    Hoischen, C.3    Brocks, B.4    Rettig, W.J.5    Gumpert, J.6    Pfizenmaier, K.7    Mattes, R.8    Moosmayer, D.9
  • 224
    • 33751335035 scopus 로고    scopus 로고
    • Microinjection of the antifreeze protein type III (AFPIII) in turbot (Scophthalmus maximus) embryos: Toxicity and protein distribution
    • Robles, V., Cabrita, E., Anelb, L., and Herraez, M. P. 2006. Microinjection of the antifreeze protein type III (AFPIII) in turbot (Scophthalmus maximus) embryos: toxicity and protein distribution. Aquaculture 261: 1299-1306.
    • (2006) Aquaculture , vol.261 , pp. 1299-1306
    • Robles, V.1    Cabrita, E.2    Anelb, L.3    Herraez, M.P.4
  • 225
    • 0025721843 scopus 로고
    • Hypothermic protection - a fundamental property of "antifreeze" proteins
    • Rubinsky, B., Arav, A., and Fletcher, G. L. 1991. Hypothermic protection - a fundamental property of "antifreeze" proteins. Biochem. Biophys. Res. Comm. 180: 566-571.
    • (1991) Biochem. Biophys. Res. Comm , vol.180 , pp. 566-571
    • Rubinsky, B.1    Arav, A.2    Fletcher, G.L.3
  • 226
    • 0028213138 scopus 로고
    • Freezing of mammalian livers with glycerol and antifreeze proteins
    • Rubinsky, B., Arav, A., Hong, J. S., and Lee, C. Y. 1994a. Freezing of mammalian livers with glycerol and antifreeze proteins. Biochem. Biophys. Res. Commun. 200: 732-741.
    • (1994) Biochem. Biophys. Res. Commun , vol.200 , pp. 732-741
    • Rubinsky, B.1    Arav, A.2    Hong, J.S.3    Lee, C.Y.4
  • 227
    • 0009660481 scopus 로고
    • Interaction of thermal hysteresis protein with cells and cell membranes and associated
    • applications. U.S. Patent 5358931
    • Rubinsky, B., Devries, A., and Arav, A. 1994b. Interaction of thermal hysteresis protein with cells and cell membranes and associated applications. U.S. Patent 5358931.
    • (1994)
    • Rubinsky, B.1    Devries, A.2    Arav, A.3
  • 230
    • 0032703669 scopus 로고    scopus 로고
    • Effects of buffer composition and processing conditions on aggregation of bovine IgG during freeze-drying
    • Sarciaux, J. M., Mansour, S., Hageman, M. J., and Nail, S. L. 1999. Effects of buffer composition and processing conditions on aggregation of bovine IgG during freeze-drying. J. Pharm. Sci. 88: 1354-1361.
    • (1999) J. Pharm. Sci , vol.88 , pp. 1354-1361
    • Sarciaux, J.M.1    Mansour, S.2    Hageman, M.J.3    Nail, S.L.4
  • 232
    • 0037071907 scopus 로고    scopus 로고
    • Prevention and reversion of protein aggregation by molecular chaperones in Escherichia coli cytosol implications for their applicability in biotechnology
    • Schlieker, C., Bukau, B., and Mogk, A. 2002. Prevention and reversion of protein aggregation by molecular chaperones in Escherichia coli cytosol implications for their applicability in biotechnology. J. Biotechnol. 96: 13-21.
    • (2002) J. Biotechnol , vol.96 , pp. 13-21
    • Schlieker, C.1    Bukau, B.2    Mogk, A.3
  • 233
    • 4644348208 scopus 로고    scopus 로고
    • Recombinant expression system in the pharmaceutical industry
    • Schmidt, F. R. 2004. Recombinant expression system in the pharmaceutical industry. Appl. Microbiol. Biotechnol. 65: 363-372.
    • (2004) Appl. Microbiol. Biotechnol , vol.65 , pp. 363-372
    • Schmidt, F.R.1
  • 234
    • 0030978089 scopus 로고    scopus 로고
    • Manipulating the aggregation and oxidation of human SPARC in the cytoplasm of Escherichia coli
    • Schneider, E. L., Thomas, J. G., Bassuk, J. A., Sage, E. H., and Baneyx, F. 1997. Manipulating the aggregation and oxidation of human SPARC in the cytoplasm of Escherichia coli. Nat. Biotechnol. 15: 581-585.
    • (1997) Nat. Biotechnol , vol.15 , pp. 581-585
    • Schneider, E.L.1    Thomas, J.G.2    Bassuk, J.A.3    Sage, E.H.4    Baneyx, F.5
  • 235
    • 0001206914 scopus 로고
    • Freezing-point depressing peptides and glycoproteins from Arctic-boreal and Antarctic fishes
    • Schneppenheim, R., and Theede, H. 1982. Freezing-point depressing peptides and glycoproteins from Arctic-boreal and Antarctic fishes. Polar Biol. 1: 115-123.
    • (1982) Polar Biol , vol.1 , pp. 115-123
    • Schneppenheim, R.1    Theede, H.2
  • 236
    • 0023686487 scopus 로고
    • Wolffish antifreeze protein genes are primarily organized as tandem repeats that contain two genes in inverted orientation
    • Schrag, J. D., Hayes, P. H., Fletcher, G. L., and Davies, P. L. 1988. Wolffish antifreeze protein genes are primarily organized as tandem repeats that contain two genes in inverted orientation. Mol. Cell. Biol. 8: 3670-3675.
    • (1988) Mol. Cell. Biol , vol.8 , pp. 3670-3675
    • Schrag, J.D.1    Hayes, P.H.2    Fletcher, G.L.3    Davies, P.L.4
  • 237
    • 33646561904 scopus 로고    scopus 로고
    • Expression and purification of sea raven type II antifreeze protein from Drosophila melanogaster S2 cells
    • Scotter, A. J., Kuntz, D. A., Saul, M., Graham, L. A., Davies, P. L., and Rose, D.R. 2006. Expression and purification of sea raven type II antifreeze protein from Drosophila melanogaster S2 cells. Protein Expr. Purif. 47: 374-383.
    • (2006) Protein Expr. Purif , vol.47 , pp. 374-383
    • Scotter, A.J.1    Kuntz, D.A.2    Saul, M.3    Graham, L.A.4    Davies, P.L.5    Rose, D.R.6
  • 238
    • 0009738539 scopus 로고
    • Survival of mouse blastocysts slow cooled in propanediol or ethylene glycol is influenced by the thawing procedure, sucrose and antifreeze proteins
    • Shaw, J. M., Ward, C., and Trounson, A. O. 1995. Survival of mouse blastocysts slow cooled in propanediol or ethylene glycol is influenced by the thawing procedure, sucrose and antifreeze proteins. Theriogenology 43: 1289-1300.
    • (1995) Theriogenology , vol.43 , pp. 1289-1300
    • Shaw, J.M.1    Ward, C.2    Trounson, A.O.3
  • 239
    • 0028224526 scopus 로고
    • Expression of recombinant human casein kinase II and recombinant heat shock protein 90 in Escherichia coli and characterization of their interactions
    • Shi, Y., Brown, E. D., and Walsh C. T. 1994. Expression of recombinant human casein kinase II and recombinant heat shock protein 90 in Escherichia coli and characterization of their interactions. Proc. Natl. Acad. Sci. USA 91(7): 2767-2771.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , Issue.7 , pp. 2767-2771
    • Shi, Y.1    Brown, E.D.2    Walsh, C.T.3
  • 240
    • 0029013417 scopus 로고
    • Ice-binding structure and mechanism of an antifreeze protein winter flounder
    • Sicheri, F., and Yang, D. S. C. 1995. Ice-binding structure and mechanism of an antifreeze protein winter flounder. Nature 375: 427-431.
    • (1995) Nature , vol.375 , pp. 427-431
    • Sicheri, F.1    Yang, D.S.C.2
  • 242
    • 0033864194 scopus 로고    scopus 로고
    • Seasonal changes in tolerance to cold and desiccation in Phauloppia sp. (Acari, Oribatida) from Finse, Norway
    • Sjursen, H., and Somme, L. 2000. Seasonal changes in tolerance to cold and desiccation in Phauloppia sp. (Acari, Oribatida) from Finse, Norway. J. Insect Physiol. 46: 1387-1396.
    • (2000) J. Insect Physiol , vol.46 , pp. 1387-1396
    • Sjursen, H.1    Somme, L.2
  • 244
    • 0033152671 scopus 로고    scopus 로고
    • Stable, high-level expression of a type I antifreeze protein in Escherichia coli
    • Solomon, R. G., and Appels, R. 1999. Stable, high-level expression of a type I antifreeze protein in Escherichia coli. Protein Expr. Purif. 16: 53-62.
    • (1999) Protein Expr. Purif , vol.16 , pp. 53-62
    • Solomon, R.G.1    Appels, R.2
  • 245
    • 0035746731 scopus 로고    scopus 로고
    • Successful nonfreezing, sub-zero preservation of rat liver with 2, 3-butanediol and type I antifreeze protein
    • Soltys, K. A., Batta, A. K., and Koneru, B. 2001. Successful nonfreezing, sub-zero preservation of rat liver with 2, 3-butanediol and type I antifreeze protein. J. Surg. Res. 96(1): 30-34.
    • (2001) J. Surg. Res , vol.96 , Issue.1 , pp. 30-34
    • Soltys, K.A.1    Batta, A.K.2    Koneru, B.3
  • 246
    • 0030929723 scopus 로고    scopus 로고
    • Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds
    • Sone, M., Akiyama, Y., and Ito, K. 1997. Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds. J. Biol. Chem. 272:10349-10352.
    • (1997) J. Biol. Chem , vol.272 , pp. 10349-10352
    • Sone, M.1    Akiyama, Y.2    Ito, K.3
  • 247
    • 0030589054 scopus 로고    scopus 로고
    • Refined, solution structure of type III antifreeze protein: Hydrophobic group may be involved in the energetics of the protein-ice interaction
    • Sonnichsen, F. D., DeLuca, C. I., Davies, P. L., and Sykes, B. D. 1996. Refined, solution structure of type III antifreeze protein: hydrophobic group may be involved in the energetics of the protein-ice interaction. Structure 4: 1325-1337.
    • (1996) Structure , vol.4 , pp. 1325-1337
    • Sonnichsen, F.D.1    DeLuca, C.I.2    Davies, P.L.3    Sykes, B.D.4
  • 248
    • 0027536918 scopus 로고
    • The nonhelical structure of antifreeze protein type III
    • Sonnichsen, F. D., Sykes, B. D., Chao, H., and Davies, P. L. 1993. The nonhelical structure of antifreeze protein type III. Science 259: 1154-1157.
    • (1993) Science , vol.259 , pp. 1154-1157
    • Sonnichsen, F.D.1    Sykes, B.D.2    Chao, H.3    Davies, P.L.4
  • 249
    • 0028905125 scopus 로고
    • Comparative modeling of the three-dimensional structure of type II antifreeze protein
    • Sonnichsen, F. D., Sykes, B. D., and Davies, P. L. 1995. Comparative modeling of the three-dimensional structure of type II antifreeze protein. Protein Sci. 4: 460-471.
    • (1995) Protein Sci , vol.4 , pp. 460-471
    • Sonnichsen, F.D.1    Sykes, B.D.2    Davies, P.L.3
  • 250
    • 0028807747 scopus 로고
    • Low temperature growth, freezing survival, and production of antifreeze protein by the plant growth promoting rhizobacterium Pseudomonas putida GR12-2
    • Sun, X., Griffith, M., Pastemak, J. J., and Glick, B. R. 1995. Low temperature growth, freezing survival, and production of antifreeze protein by the plant growth promoting rhizobacterium Pseudomonas putida GR12-2. Can. J. Microbiol. 41: 776-784.
    • (1995) Can. J. Microbiol , vol.41 , pp. 776-784
    • Sun, X.1    Griffith, M.2    Pastemak, J.J.3    Glick, B.R.4
  • 251
    • 8844277667 scopus 로고    scopus 로고
    • Key players involved in bacterial disulfide-bond formation
    • Tan, J. T., and Bardwell, J. C. A. 2004. Key players involved in bacterial disulfide-bond formation. ChemBioChem. 5: 1479-1487.
    • (2004) ChemBioChem , vol.5 , pp. 1479-1487
    • Tan, J.T.1    Bardwell, J.C.A.2
  • 252
    • 0025806533 scopus 로고
    • Evidence for intramolecular disulfide bond shuffling in the folding of mutant human lysozyme
    • Taniyama, Y., Kuroki, R., Omura, F., Seko, C., and Kikuchi, M. 1991. Evidence for intramolecular disulfide bond shuffling in the folding of mutant human lysozyme. J. Biol. Chem. 266: 6456-6461.
    • (1991) J. Biol. Chem , vol.266 , pp. 6456-6461
    • Taniyama, Y.1    Kuroki, R.2    Omura, F.3    Seko, C.4    Kikuchi, M.5
  • 253
    • 0033580920 scopus 로고    scopus 로고
    • Molecular chaperones stimulate the functional expression of the cocaine sensitive serotonin transporter
    • Tate, C. G., Whiteley, E., and Betenbaugh, J. M. 1999. Molecular chaperones stimulate the functional expression of the cocaine sensitive serotonin transporter. J. Biol. Chem. 274 (25): 17551-17558.
    • (1999) J. Biol. Chem , vol.274 , Issue.25 , pp. 17551-17558
    • Tate, C.G.1    Whiteley, E.2    Betenbaugh, J.M.3
  • 254
    • 0033933125 scopus 로고    scopus 로고
    • ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells
    • Thomas, J. G., and Baneyx, F. 2000. ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells. Mol. Microbiol. 36(6): 1360-1370.
    • (2000) Mol. Microbiol , vol.36 , Issue.6 , pp. 1360-1370
    • Thomas, J.G.1    Baneyx, F.2
  • 256
    • 0242521447 scopus 로고    scopus 로고
    • A facile method for determining ice recrystallization inhibition by antifreeze proteins
    • Tomczak, M. M., Marshall, C. B., Gilbert, J. A., and Davies, P. L. 2003. A facile method for determining ice recrystallization inhibition by antifreeze proteins. Biochem. Biophys. Res. Commun. 311: 1041-1046.
    • (2003) Biochem. Biophys. Res. Commun , vol.311 , pp. 1041-1046
    • Tomczak, M.M.1    Marshall, C.B.2    Gilbert, J.A.3    Davies, P.L.4
  • 257
    • 0034065261 scopus 로고    scopus 로고
    • Extracellular expression, purification, and characterrization of a winter flounder antifreeze polypeptide from Escherichia coli
    • Tong, L., Lin, Q., Wong, W. K. R., Ali, A., Lim, D., Sung, W. L., Hew, C. L., and Yang, D. S. C. 2000. Extracellular expression, purification, and characterrization of a winter flounder antifreeze polypeptide from Escherichia coli. Protein Expr. Purif. 18: 175-181.
    • (2000) Protein Expr. Purif , vol.18 , pp. 175-181
    • Tong, L.1    Lin, Q.2    Wong, W.K.R.3    Ali, A.4    Lim, D.5    Sung, W.L.6    Hew, C.L.7    Yang, D.S.C.8
  • 258
    • 0036252440 scopus 로고    scopus 로고
    • The hydrophobic effect: A new insight from cold denaturation and a two state water structure
    • Tsai, C. J., Maizel, J. V., Jr., and Nusionov, R. 2002. The hydrophobic effect: A new insight from cold denaturation and a two state water structure. Crit. Rev. Biochem. Mol. Biol. 37(2): 55-69.
    • (2002) Crit. Rev. Biochem. Mol. Biol , vol.37 , Issue.2 , pp. 55-69
    • Tsai, C.J.1    Maizel Jr., J.V.2    Nusionov, R.3
  • 259
    • 84985095025 scopus 로고
    • Cryoprotective effects of thermal hysteresis protein on survivorship of frozen gut cells in the freeze-tolerant centipede Lithobius forficatus
    • Tursman, D., and Duman, J. G. 1995. Cryoprotective effects of thermal hysteresis protein on survivorship of frozen gut cells in the freeze-tolerant centipede Lithobius forficatus. J. Exp. Zool. 274: 249-257.
    • (1995) J. Exp. Zool , vol.274 , pp. 249-257
    • Tursman, D.1    Duman, J.G.2
  • 260
    • 3242661672 scopus 로고    scopus 로고
    • Hyperactive spruce budworm antifreeze protein expression in transgenic Drosophila does not confer cold shock tolerance
    • Tyshenko, M. G., and Walker, V. K. 2004. Hyperactive spruce budworm antifreeze protein expression in transgenic Drosophila does not confer cold shock tolerance. Cryobiology 49: 28-36.
    • (2004) Cryobiology , vol.49 , pp. 28-36
    • Tyshenko, M.G.1    Walker, V.K.2
  • 261
    • 33646104418 scopus 로고    scopus 로고
    • Challenges in the expression of disulphide bonded, threonine-rich antifreeze protein in bacteria and yeast
    • Tyshenko, M. G., Anjoy, M. D., Davies, P. L., Daugulis, A. J., and Walker, V. K. 2006. Challenges in the expression of disulphide bonded, threonine-rich antifreeze protein in bacteria and yeast. Protein Expr. Purif. 47(1): 152-161.
    • (2006) Protein Expr. Purif , vol.47 , Issue.1 , pp. 152-161
    • Tyshenko, M.G.1    Anjoy, M.D.2    Davies, P.L.3    Daugulis, A.J.4    Walker, V.K.5
  • 262
    • 0030828487 scopus 로고    scopus 로고
    • The antifreeze potential of the spruce budworm thermal hysteresis protein
    • Tyshenko, M. G., Doucet, D., Davies, P. L., and Walker, V. K. 1997. The antifreeze potential of the spruce budworm thermal hysteresis protein. Nat. Biotechnol. 15: 887-890.
    • (1997) Nat. Biotechnol , vol.15 , pp. 887-890
    • Tyshenko, M.G.1    Doucet, D.2    Davies, P.L.3    Walker, V.K.4
  • 264
    • 13544253581 scopus 로고    scopus 로고
    • Gabrielsen OS. Engineering of a Pichia pastoris expression system for secretion of high amounts of intact human parathyroid hormone
    • Vad, R., Nafstad, E., and Dahl, L. A. 2005. Gabrielsen OS. Engineering of a Pichia pastoris expression system for secretion of high amounts of intact human parathyroid hormone. J. Biotechnol. 116(3): 251-260.
    • (2005) J. Biotechnol , vol.116 , Issue.3 , pp. 251-260
    • Vad, R.1    Nafstad, E.2    Dahl, L.A.3
  • 265
    • 0027047408 scopus 로고
    • Survival of Northern Atlantic cod (Gadus morhua) eggs and larvae when exposed to ice and low temperature
    • Valerio, P. F., Goddard, S. V., Kao, M. H., and Fletcher, G. L. 1992. Survival of Northern Atlantic cod (Gadus morhua) eggs and larvae when exposed to ice and low temperature. Can. J. Fish. Aquat. Sci. 49:1-8.
    • (1992) Can. J. Fish. Aquat. Sci , vol.49 , pp. 1-8
    • Valerio, P.F.1    Goddard, S.V.2    Kao, M.H.3    Fletcher, G.L.4
  • 267
    • 0031105876 scopus 로고    scopus 로고
    • Expression of aggregation-prone recombinant proteins at slow temperatures: A comparative study of the Escherichia coli cspA and tac promoter systems
    • Vasina, J. A., and Baneyx, F. 1997. Expression of aggregation-prone recombinant proteins at slow temperatures: a comparative study of the Escherichia coli cspA and tac promoter systems. Protein Expr. Purif. 9: 211-218.
    • (1997) Protein Expr. Purif , vol.9 , pp. 211-218
    • Vasina, J.A.1    Baneyx, F.2
  • 268
    • 0032171082 scopus 로고    scopus 로고
    • Scale-up and optimization of the low temperature inducible cspA promoter system
    • Vasina, J. A., Peterson, M. S., and Baneyx, F. 1998. Scale-up and optimization of the low temperature inducible cspA promoter system. Biotechnol. Prog. 14: 714-721.
    • (1998) Biotechnol. Prog , vol.14 , pp. 714-721
    • Vasina, J.A.1    Peterson, M.S.2    Baneyx, F.3
  • 269
    • 0009660482 scopus 로고
    • The transfer of fish antifreeze genes to Drosophila: A model for the generation of transgenic beneficial insects
    • Walker, V. K., Rancourt, D. E., and Duncker, B. P. 1995. The transfer of fish antifreeze genes to Drosophila: a model for the generation of transgenic beneficial insects. Proc. Entomol. Soc. Ont. 126: 3-13.
    • (1995) Proc. Entomol. Soc. Ont , vol.126 , pp. 3-13
    • Walker, V.K.1    Rancourt, D.E.2    Duncker, B.P.3
  • 270
    • 0031260422 scopus 로고    scopus 로고
    • Expression of a synthetic antifreeze protein in potato reduces electrolyte release at freezing temperatures
    • Wallis, J. G., Wang, H. Y., and Guerra, D. J. 1997. Expression of a synthetic antifreeze protein in potato reduces electrolyte release at freezing temperatures. Plant Mol. Biol. 35(3): 323-330.
    • (1997) Plant Mol. Biol , vol.35 , Issue.3 , pp. 323-330
    • Wallis, J.G.1    Wang, H.Y.2    Guerra, D.J.3
  • 271
    • 0033775327 scopus 로고    scopus 로고
    • A comprehensive evaluation of the effects and mechanisms of antifreeze proteins during low-temperature preservation
    • Wang, J. H. 2000. A comprehensive evaluation of the effects and mechanisms of antifreeze proteins during low-temperature preservation. Cryobiology 41: 1-9.
    • (2000) Cryobiology , vol.41 , pp. 1-9
    • Wang, J.H.1
  • 272
    • 0000189660 scopus 로고    scopus 로고
    • Studies on the application of antifreeze proteins in cryopreservation of rice embryogenic suspension cells
    • Wang, J. H., Bian, H. W., Huang, C. N., and Ge, J. G. 1999. Studies on the application of antifreeze proteins in cryopreservation of rice embryogenic suspension cells. Acta Biol. Exp. Sinica. 32:271-276.
    • (1999) Acta Biol. Exp. Sinica , vol.32 , pp. 271-276
    • Wang, J.H.1    Bian, H.W.2    Huang, C.N.3    Ge, J.G.4
  • 273
    • 40349092028 scopus 로고    scopus 로고
    • Wang, J.H., and Huang, C.N. 1996. Antifreeze proteins: In hypothermic and cryogenic preservation. Chinese J. Cell Biol. 18: 107-111.
    • Wang, J.H., and Huang, C.N. 1996. Antifreeze proteins: In hypothermic and cryogenic preservation. Chinese J. Cell Biol. 18: 107-111.
  • 274
    • 0029257418 scopus 로고
    • Expression of the antifreeze protein gene in transgenic goldfish (Carassius auratus) and its implication in cold adaptation
    • Wang, R., Zhang, P., Gong, Z., and Hew, C. L. 1995. Expression of the antifreeze protein gene in transgenic goldfish (Carassius auratus) and its implication in cold adaptation. Mol. Mar. Biol. Biotechnol. 4(1): 20-26.
    • (1995) Mol. Mar. Biol. Biotechnol , vol.4 , Issue.1 , pp. 20-26
    • Wang, R.1    Zhang, P.2    Gong, Z.3    Hew, C.L.4
  • 275
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • Wang, W. 2005. Protein aggregation and its inhibition in biopharmaceutics. Int. J. Pharm. 289: 1-30.
    • (2005) Int. J. Pharm , vol.289 , pp. 1-30
    • Wang, W.1
  • 276
  • 277
    • 0003832598 scopus 로고
    • Ice crystal growth suppression polypeptides and method of making
    • U.S. Patent 5118792
    • Warren, G. J., Mueller, G. M., and McKown, R. L. 1992. Ice crystal growth suppression polypeptides and method of making. U.S. Patent 5118792.
    • (1992)
    • Warren, G.J.1    Mueller, G.M.2    McKown, R.L.3
  • 278
    • 0037460192 scopus 로고    scopus 로고
    • A new model for simulating 3-D crystal growth and its application to the study of antifreeze proteins
    • Wathen, B., Kuiper, M., Walker, V., and Jia, Z. 2003. A new model for simulating 3-D crystal growth and its application to the study of antifreeze proteins. J. Am. Chem. Soc. 125: 729-737.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 729-737
    • Wathen, B.1    Kuiper, M.2    Walker, V.3    Jia, Z.4
  • 279
    • 0027459477 scopus 로고
    • A D-antifreeze polypeptide displays the same activity as its natural L-enantiomer
    • Wen, D., and Laursen, R. A. 1993. A D-antifreeze polypeptide displays the same activity as its natural L-enantiomer. FEBS Lett. 317: 31-34.
    • (1993) FEBS Lett , vol.317 , pp. 31-34
    • Wen, D.1    Laursen, R.A.2
  • 280
    • 34548647991 scopus 로고    scopus 로고
    • Antifreeze proteins at the ice/water interface: Three calculated discriminating properties for orientation of type I proteins
    • Wierzbicki, A., Dalal, P., Cheatham, T. E., Knickelbein, J. E., Haymet, A. D. J., and Madura, J. D., 2007. Antifreeze proteins at the ice/water interface: three calculated discriminating properties for orientation of type I proteins. Biophys. J. 93: 1442-1451.
    • (2007) Biophys. J , vol.93 , pp. 1442-1451
    • Wierzbicki, A.1    Dalal, P.2    Cheatham, T.E.3    Knickelbein, J.E.4    Haymet, A.D.J.5    Madura, J.D.6
  • 281
    • 0027163901 scopus 로고
    • Antifreeze glycopeptide adsorption on single crystal ice surfaces using ellipsometry
    • Wilson, P. W., Beaglehole, D., and DeVries, A. L. 1993. Antifreeze glycopeptide adsorption on single crystal ice surfaces using ellipsometry. Biophys. J. 64: 1878-1884.
    • (1993) Biophys. J , vol.64 , pp. 1878-1884
    • Wilson, P.W.1    Beaglehole, D.2    DeVries, A.L.3
  • 282
    • 0036628396 scopus 로고    scopus 로고
    • Hexagonal shaped ice spicules in frozen antifreeze protein solutions
    • Wilson, P., Gould, M., and DeVries, A. 2002. Hexagonal shaped ice spicules in frozen antifreeze protein solutions. Cryobiology 44: 240-250.
    • (2002) Cryobiology , vol.44 , pp. 240-250
    • Wilson, P.1    Gould, M.2    DeVries, A.3
  • 283
    • 34247563714 scopus 로고    scopus 로고
    • Safety Aspects of Genetically Modified Foods of Plant Origin
    • World Health Organization WHO, World Health Organization, Geneva
    • World Health Organization (WHO). 2000. Safety Aspects of Genetically Modified Foods of Plant Origin. Report of a Joint FAO/WHO Expert Consultation, World Health Organization, Geneva.
    • (2000) Report of a Joint FAO/WHO Expert Consultation
  • 286
    • 18144417823 scopus 로고    scopus 로고
    • Expression of soluble, biologically active recombinant human endostatin in Escherichia coli
    • Xu, H. M., Zhang, G. Y., Ji, X. D., Cao, L., Shu, L., and Hua, Z. C. 2005a. Expression of soluble, biologically active recombinant human endostatin in Escherichia coli. Protein Expr. Purif. 41(2): 252-258.
    • (2005) Protein Expr. Purif , vol.41 , Issue.2 , pp. 252-258
    • Xu, H.M.1    Zhang, G.Y.2    Ji, X.D.3    Cao, L.4    Shu, L.5    Hua, Z.C.6
  • 287
    • 26844560708 scopus 로고    scopus 로고
    • Chaperone-mediated folding and maturation of the penicillin acylase precursor in the cytoplasm of Escherichia coli
    • Xu, Y., Weng, C. L., Narayanan, N., Hsieh, M. Y., Anderson, W. A., Scharer, J. M., Moo-Young, M., and Chou, C. P. 2005b. Chaperone-mediated folding and maturation of the penicillin acylase precursor in the cytoplasm of Escherichia coli. Appl. Environ. Microbiol. 71(10): 6247-6253.
    • (2005) Appl. Environ. Microbiol , vol.71 , Issue.10 , pp. 6247-6253
    • Xu, Y.1    Weng, C.L.2    Narayanan, N.3    Hsieh, M.Y.4    Anderson, W.A.5    Scharer, J.M.6    Moo-Young, M.7    Chou, C.P.8
  • 289
    • 1642587769 scopus 로고    scopus 로고
    • The mechanism of the type III antifreeze protein action: A computational study
    • Yang, C., and Sharp, K. A. 2004. The mechanism of the type III antifreeze protein action: a computational study. Biophysical Chemistry. 109: 137-148.
    • (2004) Biophysical Chemistry , vol.109 , pp. 137-148
    • Yang, C.1    Sharp, K.A.2
  • 290
    • 0024291721 scopus 로고    scopus 로고
    • Crystal structure of an antifreeze polypeptide and its mechanistic implications
    • Yang, D. S. C., Sax, M., Chakrabartty, A., and Hew, C. L. 1998. Crystal structure of an antifreeze polypeptide and its mechanistic implications. Nature 333: 232-237.
    • (1998) Nature , vol.333 , pp. 232-237
    • Yang, D.S.C.1    Sax, M.2    Chakrabartty, A.3    Hew, C.L.4
  • 291
    • 0030890964 scopus 로고    scopus 로고
    • The presence of complete but masked freezing nuclei in various artificially constructed ice nucleation-active Proteobacteria
    • Yankofsky, S. A., Nadler, T., and Kaplan, H. 1997. The presence of complete but masked freezing nuclei in various artificially constructed ice nucleation-active Proteobacteria. Curr. Microbiol. 34: 318-325.
    • (1997) Curr. Microbiol , vol.34 , pp. 318-325
    • Yankofsky, S.A.1    Nadler, T.2    Kaplan, H.3
  • 292
    • 0032128158 scopus 로고    scopus 로고
    • Structure of type III antifreeze protein at 277 K
    • Ye, Q., Leinala, E., and Jia, Z. 1998. Structure of type III antifreeze protein at 277 K. Acta Cryst. 54: 700-702.
    • (1998) Acta Cryst , vol.54 , pp. 700-702
    • Ye, Q.1    Leinala, E.2    Jia, Z.3
  • 294
    • 9144257407 scopus 로고    scopus 로고
    • Antifreeze proteins: Structures and mechanisms of function
    • Yeh, Y., and Feeney, R. E. 1996. Antifreeze proteins: structures and mechanisms of function. Chem. Rev. 96: 601-617.
    • (1996) Chem. Rev , vol.96 , pp. 601-617
    • Yeh, Y.1    Feeney, R.E.2
  • 295
    • 0028090114 scopus 로고
    • Measurement of grain growth in the recrystallization of rapidly frozen solutions of antifreeze glycoproteins
    • Yeh, Y., Feeney, R. E., McKown, R. L., and Warren, G. J. 1994. Measurement of grain growth in the recrystallization of rapidly frozen solutions of antifreeze glycoproteins. Biopolymers. 84: 1495-1504.
    • (1994) Biopolymers , vol.84 , pp. 1495-1504
    • Yeh, Y.1    Feeney, R.E.2    McKown, R.L.3    Warren, G.J.4
  • 296
    • 0032086125 scopus 로고    scopus 로고
    • Overproduction of DnaJ in Escherichia coli improves in vivo solubility of recombinant fish-derived transglutaminase
    • Yokoyama, K., Kikuchi, Y., and Yasueda, H. 1998. Overproduction of DnaJ in Escherichia coli improves in vivo solubility of recombinant fish-derived transglutaminase. Biosci. Biotechnol. Biochem. 62(6): 1205-1210.
    • (1998) Biosci. Biotechnol. Biochem , vol.62 , Issue.6 , pp. 1205-1210
    • Yokoyama, K.1    Kikuchi, Y.2    Yasueda, H.3
  • 297
    • 5044239107 scopus 로고    scopus 로고
    • Pathways of chaperone mediated protein folding in the cytosol
    • Young, J. C., Agashe, V. R., Siegers, K., and Hartl, F. U. 2004. Pathways of chaperone mediated protein folding in the cytosol. Nat. Mol. Cell Biol. 5: 781-791.
    • (2004) Nat. Mol. Cell Biol , vol.5 , pp. 781-791
    • Young, J.C.1    Agashe, V.R.2    Siegers, K.3    Hartl, F.U.4
  • 298
    • 0035035047 scopus 로고    scopus 로고
    • Winter rye antifreeze activity increases in response to cold and drought, but not abscisic acid
    • Yu, X. M., and Griffith, M. 2001. Winter rye antifreeze activity increases in response to cold and drought, but not abscisic acid. Physiol. Plantarum 112: 78-86.
    • (2001) Physiol. Plantarum , vol.112 , pp. 78-86
    • Yu, X.M.1    Griffith, M.2
  • 299
    • 0034948272 scopus 로고    scopus 로고
    • Ethylene induces antifreeze activity in winter rye leaves
    • Yu, X. M., Griffith, M., and Wiseman, S. B. 2001. Ethylene induces antifreeze activity in winter rye leaves. Plant Physiol. 126: 1232-1240.
    • (2001) Plant Physiol , vol.126 , pp. 1232-1240
    • Yu, X.M.1    Griffith, M.2    Wiseman, S.B.3
  • 300
    • 0034480912 scopus 로고    scopus 로고
    • Ice nucleation and antinucleation in nature
    • Zachariassen, K. E., and Kristiansen, E. 2000. Ice nucleation and antinucleation in nature. Cryobiology 41: 257-279.
    • (2000) Cryobiology , vol.41 , pp. 257-279
    • Zachariassen, K.E.1    Kristiansen, E.2
  • 302
    • 2642520558 scopus 로고    scopus 로고
    • Expression, purification, and antifreeze activity of carrot antifreeze protein and its mutants
    • Zhang, D. Q., Liu, B., Feng, D., He, M., and Wang, J. 2004. Expression, purification, and antifreeze activity of carrot antifreeze protein and its mutants. Protein Expr. Purif. 35: 257-263.
    • (2004) Protein Expr. Purif , vol.35 , pp. 257-263
    • Zhang, D.Q.1    Liu, B.2    Feng, D.3    He, M.4    Wang, J.5
  • 303
    • 0032774995 scopus 로고    scopus 로고
    • Artificial antifreeze polypeptides: K-helical peptides with KAAK motifs have antifreeze and ice crystal morphology modifying properties
    • Zhang, W., and Laursen R. A. 1999. Artificial antifreeze polypeptides: K-helical peptides with KAAK motifs have antifreeze and ice crystal morphology modifying properties. FEBS Lett. 455: 372-376.
    • (1999) FEBS Lett , vol.455 , pp. 372-376
    • Zhang, W.1    Laursen, R.A.2
  • 304
    • 0032567416 scopus 로고    scopus 로고
    • Structure-function relationships in a type I antifreeze polypeptide. The role of threonine methyl and hydroxyl groups in antifreeze activity
    • Zhang, W., and Laursen, R. A. 1998. Structure-function relationships in a type I antifreeze polypeptide. The role of threonine methyl and hydroxyl groups in antifreeze activity. J. Biol. Chem. 273: 34806-34812.
    • (1998) J. Biol. Chem , vol.273 , pp. 34806-34812
    • Zhang, W.1    Laursen, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.