메뉴 건너뛰기




Volumn 22, Issue C, 2005, Pages 155-201

Antifreeze Proteins and Organismal Freezing Avoidance in Polar Fishes

Author keywords

[No Author keywords available]

Indexed keywords

PISCES;

EID: 77956743709     PISSN: 15465098     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1546-5098(04)22004-0     Document Type: Review
Times cited : (118)

References (163)
  • 1
    • 0024051679 scopus 로고
    • Freezing avoidance and the distribution of antifreeze glycopeptides in body fluids and tissues of antarctic fish
    • Ahlgren J.A., Cheng C.-H.C., Schrag J.D., and DeVries A.L. Freezing avoidance and the distribution of antifreeze glycopeptides in body fluids and tissues of antarctic fish. J. Exp. Biol. 137 (1988) 549-563
    • (1988) J. Exp. Biol. , vol.137 , pp. 549-563
    • Ahlgren, J.A.1    Cheng, C.-H.C.2    Schrag, J.D.3    DeVries, A.L.4
  • 2
    • 0006241923 scopus 로고
    • Comparison of antifreeze glycoproteins from several Antarctic fishes
    • Ahlgren J.A., and DeVries A.L. Comparison of antifreeze glycoproteins from several Antarctic fishes. Polar Biol. 3 (1984) 93-97
    • (1984) Polar Biol. , vol.3 , pp. 93-97
    • Ahlgren, J.A.1    DeVries, A.L.2
  • 3
    • 0000163856 scopus 로고
    • Supercooled water
    • Franks F. (Ed), Plenum Press, New York
    • Angell C.A. Supercooled water. In: Franks F. (Ed). "Water: A Comprehensive Treatise" Vol. 7 (1982), Plenum Press, New York 1-81
    • (1982) "Water: A Comprehensive Treatise" , vol.7 , pp. 1-81
    • Angell, C.A.1
  • 4
    • 0035425519 scopus 로고    scopus 로고
    • Sialic acid synthase: The origin of fish type III antifreeze protein?
    • Baardsnes J., and Davies P.L. Sialic acid synthase: The origin of fish type III antifreeze protein?. TIBS 24 (2001) 468-469
    • (2001) TIBS , vol.24 , pp. 468-469
    • Baardsnes, J.1    Davies, P.L.2
  • 7
    • 0039692092 scopus 로고
    • Some aspects of the physiology of fish
    • Black V.S. Some aspects of the physiology of fish. Univ. Toronto Stud. Biol. Ser. 71 (1951) 53-89
    • (1951) Univ. Toronto Stud. Biol. Ser. , vol.71 , pp. 53-89
    • Black, V.S.1
  • 8
    • 0021077663 scopus 로고
    • The seasonal distribution of anionic binding sites in the basement membrane of the kidney glomerulus of the winter flounder Pseudopleuronectes americanus
    • Boyd R.B., and DeVries A.L. The seasonal distribution of anionic binding sites in the basement membrane of the kidney glomerulus of the winter flounder Pseudopleuronectes americanus. Cell Tissue Res. 234 (1983) 271-277
    • (1983) Cell Tissue Res. , vol.234 , pp. 271-277
    • Boyd, R.B.1    DeVries, A.L.2
  • 9
    • 1842838562 scopus 로고    scopus 로고
    • The structure of fish antifreeze proteins
    • Ewart K.V., and Hew C.L. (Eds), World Scientific, Singapore
    • Brown J.D., and Sonnichsen F.D. The structure of fish antifreeze proteins. In: Ewart K.V., and Hew C.L. (Eds). "Fish Antifreeze Proteins" (2002), World Scientific, Singapore 109-138
    • (2002) "Fish Antifreeze Proteins" , pp. 109-138
    • Brown, J.D.1    Sonnichsen, F.D.2
  • 10
    • 0022800346 scopus 로고
    • Conformation of the glycotripeptide repeating unit of antifreeze glycoprotein of polar fish as determined from the fully assigned proton N.M.R. spectrum
    • Bush C.A., and Feeney R.E. Conformation of the glycotripeptide repeating unit of antifreeze glycoprotein of polar fish as determined from the fully assigned proton N.M.R. spectrum. Int. J. Pept. Protein Res. 28 (1986) 386-397
    • (1986) Int. J. Pept. Protein Res. , vol.28 , pp. 386-397
    • Bush, C.A.1    Feeney, R.E.2
  • 11
    • 0024962189 scopus 로고
    • Structure-function relationship in a winter flounder antifreeze polypeptide: II. Alteration of the component growth rates of ice by synthetic antifreeze polypeptides
    • Chakrabartty A., Yang D.S., and Hew C.L. Structure-function relationship in a winter flounder antifreeze polypeptide: II. Alteration of the component growth rates of ice by synthetic antifreeze polypeptides. J. Biol. Chem. 264 (1989) 11313-11316
    • (1989) J. Biol. Chem. , vol.264 , pp. 11313-11316
    • Chakrabartty, A.1    Yang, D.S.2    Hew, C.L.3
  • 12
    • 0028859777 scopus 로고
    • Mixing antifreeze protein types changes ice crystal morphology without affecting antifreeze activity
    • Chao H.M., Deluca C.I., and Davies P.L. Mixing antifreeze protein types changes ice crystal morphology without affecting antifreeze activity. FEBS Lett. 357 (1995) 183-186
    • (1995) FEBS Lett. , vol.357 , pp. 183-186
    • Chao, H.M.1    Deluca, C.I.2    Davies, P.L.3
  • 14
    • 0030970280 scopus 로고    scopus 로고
    • Evolution of antifreeze glycoprotein gene from a trypsinogen gene in Antarctic notothenioid fish
    • Chen L., DeVries A.L., and Cheng C.C.-H. Evolution of antifreeze glycoprotein gene from a trypsinogen gene in Antarctic notothenioid fish. Proc. Natl. Acad. Sci. USA 94 (1997) 3811-3816
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3811-3816
    • Chen, L.1    DeVries, A.L.2    Cheng, C.C.-H.3
  • 15
    • 0030890706 scopus 로고    scopus 로고
    • Convergent evolution of antifreeze glycoproteins in Antarctic notothenioid fish and Arctic cod
    • Chen L., DeVries A.L., and Cheng C.C.-H. Convergent evolution of antifreeze glycoproteins in Antarctic notothenioid fish and Arctic cod. Proc. Natl. Acad. Sci. USA 94 (1997) 3817-3822
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3817-3822
    • Chen, L.1    DeVries, A.L.2    Cheng, C.C.-H.3
  • 16
    • 0033619225 scopus 로고    scopus 로고
    • Evolution of an antifreeze glycoprotein
    • Cheng C.-H., and Chen L. Evolution of an antifreeze glycoprotein. Nature 40 (1999) 443-444
    • (1999) Nature , vol.40 , pp. 443-444
    • Cheng, C.-H.1    Chen, L.2
  • 17
    • 0242394504 scopus 로고    scopus 로고
    • Genomic basis for antifreeze glycopeptide heterogeneity and abundance in Antarctic notothenioid fishes
    • "Gene Expression and Manipulation in Aquatic Organisms". Ennion S.J., and Goldspink G. (Eds), Cambridge University Press, Cambridge
    • Cheng C.-H.C. Genomic basis for antifreeze glycopeptide heterogeneity and abundance in Antarctic notothenioid fishes. In: Ennion S.J., and Goldspink G. (Eds). "Gene Expression and Manipulation in Aquatic Organisms". Soc. of Expt. Biol. Seminar Series 58 (1996), Cambridge University Press, Cambridge 1-20
    • (1996) Soc. of Expt. Biol. Seminar Series , vol.58 , pp. 1-20
    • Cheng, C.-H.C.1
  • 18
    • 0031771585 scopus 로고    scopus 로고
    • Evolution of the diverse antifreeze proteins
    • Cheng C.-H.C. Evolution of the diverse antifreeze proteins. Curr. Opin. Genet. Dev. 8 (1998) 715-720
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 715-720
    • Cheng, C.-H.C.1
  • 19
    • 0024979559 scopus 로고
    • Structures of antifreeze peptides from the antarctic eel pout, Austrolycichthys brachycephalus
    • Cheng C.-H.C., and DeVries A.L. Structures of antifreeze peptides from the antarctic eel pout, Austrolycichthys brachycephalus. Biochim. Biophys. Acta 997 (1989) 55-64
    • (1989) Biochim. Biophys. Acta , vol.997 , pp. 55-64
    • Cheng, C.-H.C.1    DeVries, A.L.2
  • 20
    • 77956723228 scopus 로고    scopus 로고
    • Prevention of intestinal freezing by pancreatic expression of antifreeze proteins: A common mechanism in all antifreeze-bearing fish
    • (manuscript submitted).
    • Cheng C.-H.C., Logue J., Cziko P., and Chen L. Prevention of intestinal freezing by pancreatic expression of antifreeze proteins: A common mechanism in all antifreeze-bearing fish. J. Biol. Chem. (2005) (manuscript submitted).
    • (2005) J. Biol. Chem.
    • Cheng, C.-H.C.1    Logue, J.2    Cziko, P.3    Chen, L.4
  • 21
    • 0036789530 scopus 로고    scopus 로고
    • Analysis of ice-binding sites in fish type II antifreeze protein by quantum mechanics
    • Cheng Y., Yang Z., Tan H., Liu R., Chen G., and Jia Z. Analysis of ice-binding sites in fish type II antifreeze protein by quantum mechanics. Biophys. J. 83 (2002) 2202-2210
    • (2002) Biophys. J. , vol.83 , pp. 2202-2210
    • Cheng, Y.1    Yang, Z.2    Tan, H.3    Liu, R.4    Chen, G.5    Jia, Z.6
  • 22
    • 0000025470 scopus 로고
    • An Arctic teleost fish with a noticeably high body fluid osmolality: A note on the navaga, Eleginus navaga (Pallas 1811), from the White Sea
    • Christiansen J.S., Chernitsky A.G., and Karamushko O.V. An Arctic teleost fish with a noticeably high body fluid osmolality: A note on the navaga, Eleginus navaga (Pallas 1811), from the White Sea. Polar Biol. 15 (1995) 303-306
    • (1995) Polar Biol. , vol.15 , pp. 303-306
    • Christiansen, J.S.1    Chernitsky, A.G.2    Karamushko, O.V.3
  • 23
    • 33746025007 scopus 로고
    • Seasonality in the Antarctic marine environment
    • Clarke A. Seasonality in the Antarctic marine environment. Comp. Biochem. Physiol. 90 (1987) 461-473
    • (1987) Comp. Biochem. Physiol. , vol.90 , pp. 461-473
    • Clarke, A.1
  • 25
    • 0030957967 scopus 로고    scopus 로고
    • Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder
    • Cole A.M., Peddrick W., and Diamond G. Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder. J. Biol. Chem. 272 (1997) 12008-12013
    • (1997) J. Biol. Chem. , vol.272 , pp. 12008-12013
    • Cole, A.M.1    Peddrick, W.2    Diamond, G.3
  • 26
    • 2042437650 scopus 로고    scopus 로고
    • Initial sequencing and analysis of the human genome
    • Consortium I.H.G.S. Initial sequencing and analysis of the human genome. Nature 409 (2001) 860-921
    • (2001) Nature , vol.409 , pp. 860-921
    • Consortium, I.H.G.S.1
  • 31
    • 0021325192 scopus 로고
    • Ion and water transport by the flounder urinary bladder: Salinity dependence
    • Demarest J.R. Ion and water transport by the flounder urinary bladder: Salinity dependence. J. Physiol. 246 (1984) F395
    • (1984) J. Physiol. , vol.246
    • Demarest, J.R.1
  • 32
    • 0000243371 scopus 로고
    • Spatial and temporal aspects of the ocean migration of anadromous Arctic char
    • Dempson J.B., and Krístofferson A.H. Spatial and temporal aspects of the ocean migration of anadromous Arctic char. Am. Fish. Soc. Symp. 1 (1987) 340-357
    • (1987) Am. Fish. Soc. Symp. , vol.1 , pp. 340-357
    • Dempson, J.B.1    Krístofferson, A.H.2
  • 33
    • 0031026370 scopus 로고    scopus 로고
    • Amino acid sequence of a new type of antifreeze protein from the long horn sculpin Myoxocephalus octodecimspinosis
    • Deng G., Andrews D.W., and Laursen R.A. Amino acid sequence of a new type of antifreeze protein from the long horn sculpin Myoxocephalus octodecimspinosis. FEBS Lett. 402 (1997) 17-20
    • (1997) FEBS Lett. , vol.402 , pp. 17-20
    • Deng, G.1    Andrews, D.W.2    Laursen, R.A.3
  • 34
    • 0032506091 scopus 로고    scopus 로고
    • Isolation and characterization of an antifreeze protein from the longhorn sculpin, Myoxocephalus octodecimspinosis
    • Deng G., and Laursen R.A. Isolation and characterization of an antifreeze protein from the longhorn sculpin, Myoxocephalus octodecimspinosis. Biochim. Biophys. Acta 1388 (1998) 305-314
    • (1998) Biochim. Biophys. Acta , vol.1388 , pp. 305-314
    • Deng, G.1    Laursen, R.A.2
  • 36
    • 33746353872 scopus 로고
    • Freezing resistance in antarctic fishes
    • Holdgate M.W. (Ed), Academic Press, New York
    • DeVries A.L. Freezing resistance in antarctic fishes. In: Holdgate M.W. (Ed). "Antarctic Ecology." (1970), Academic Press, New York 320-328
    • (1970) "Antarctic Ecology." , pp. 320-328
    • DeVries, A.L.1
  • 37
    • 0015219684 scopus 로고
    • Glycoproteins as biological antifreeze agents in Antarctic fishes
    • DeVries A.L. Glycoproteins as biological antifreeze agents in Antarctic fishes. Science 172 (1971) 1152-1155
    • (1971) Science , vol.172 , pp. 1152-1155
    • DeVries, A.L.1
  • 38
    • 0001222759 scopus 로고
    • Biological antifreeze agents in cold water fishes
    • DeVries A.L. Biological antifreeze agents in cold water fishes. Comp. Biochem. Physiol. 73A (1982) 627-640
    • (1982) Comp. Biochem. Physiol. , vol.73 A , pp. 627-640
    • DeVries, A.L.1
  • 39
    • 0000555628 scopus 로고
    • Role of glycopeptides and peptides in inhibition of crystallization of water in polar fishes
    • DeVries A.L. Role of glycopeptides and peptides in inhibition of crystallization of water in polar fishes. Trans. Roy. Soc. Lond. B 304 (1984) 575-588
    • (1984) Trans. Roy. Soc. Lond. B , vol.304 , pp. 575-588
    • DeVries, A.L.1
  • 40
    • 0022523733 scopus 로고
    • Glycopeptide and peptide antifreeze-Interaction with ice
    • Colowick S.P., and Kaplan N.O. (Eds), Academic Press, New York
    • DeVries A.L. Glycopeptide and peptide antifreeze-Interaction with ice. In: Colowick S.P., and Kaplan N.O. (Eds). "Methods in Enzymology" Vol. 127 (1986), Academic Press, New York 293-303
    • (1986) "Methods in Enzymology" , vol.127 , pp. 293-303
    • DeVries, A.L.1
  • 41
    • 0000742353 scopus 로고
    • The role of antifreeze glycopeptides and peptides in the freezing avoidance of Antarctic fishes
    • DeVries A.L. The role of antifreeze glycopeptides and peptides in the freezing avoidance of Antarctic fishes. Comp. Biochem. Physiol. 90B (1988) 611-621
    • (1988) Comp. Biochem. Physiol. , vol.90 B , pp. 611-621
    • DeVries, A.L.1
  • 43
    • 0014939615 scopus 로고
    • Chemical and physical properties of freezing point depressing glycoproteins from Antarctic fishes
    • DeVries A.L., Komatsu S.K., and Feeney R.E. Chemical and physical properties of freezing point depressing glycoproteins from Antarctic fishes. J. Biol. Chem. 245 (1970) 2901-2908
    • (1970) J. Biol. Chem. , vol.245 , pp. 2901-2908
    • DeVries, A.L.1    Komatsu, S.K.2    Feeney, R.E.3
  • 44
    • 0017730326 scopus 로고
    • Structure of a peptide antifreeze and mechanism of adsorption to ice
    • DeVries A.L., and Lin Y. Structure of a peptide antifreeze and mechanism of adsorption to ice. Biochim. Biophys. Acta 495 (1977) 388-392
    • (1977) Biochim. Biophys. Acta , vol.495 , pp. 388-392
    • DeVries, A.L.1    Lin, Y.2
  • 45
    • 0015239007 scopus 로고
    • Primary structure of freezing point-depressing glycoproteins
    • DeVries A.L., Vandenheede J., and Feeney R.E. Primary structure of freezing point-depressing glycoproteins. J. Biol. Chem. 246 (1971) 305-308
    • (1971) J. Biol. Chem. , vol.246 , pp. 305-308
    • DeVries, A.L.1    Vandenheede, J.2    Feeney, R.E.3
  • 46
    • 0014666651 scopus 로고
    • Freezing resistance in some Antarctic fishes
    • DeVries A.L., and Wohlschlag D.E. Freezing resistance in some Antarctic fishes. Science 163 (1969) 1073-1075
    • (1969) Science , vol.163 , pp. 1073-1075
    • DeVries, A.L.1    Wohlschlag, D.E.2
  • 47
    • 0022916906 scopus 로고
    • The occurrence of ice platelets at 250m depth near the Filchner Ice Shelf and its significance for sea ice biology
    • Dieckmann G., Rohardt G., Hellmer H., and Kipfstuhl J. The occurrence of ice platelets at 250m depth near the Filchner Ice Shelf and its significance for sea ice biology. Deep-Sea Res. 33 (1986) 141-148
    • (1986) Deep-Sea Res. , vol.33 , pp. 141-148
    • Dieckmann, G.1    Rohardt, G.2    Hellmer, H.3    Kipfstuhl, J.4
  • 48
    • 0003009085 scopus 로고
    • Renal function in Antarctic teleost fishes: Serum and urine composition
    • Dobbs G.H., and DeVries A.L. Renal function in Antarctic teleost fishes: Serum and urine composition. Mar. Biol. 29 (1975) 59-70
    • (1975) Mar. Biol. , vol.29 , pp. 59-70
    • Dobbs, G.H.1    DeVries, A.L.2
  • 49
    • 0016405177 scopus 로고
    • Aglomerularism in Antarctic fish
    • Dobbs G.H., Lin Y.L., and DeVries A.L. Aglomerularism in Antarctic fish. Science 185 (1974) 793-794
    • (1974) Science , vol.185 , pp. 793-794
    • Dobbs, G.H.1    Lin, Y.L.2    DeVries, A.L.3
  • 50
    • 0000641685 scopus 로고
    • Freezing resistance in winter flounder, Pseudopleuronectes americanus
    • Duman J.G., and DeVries A.L. Freezing resistance in winter flounder, Pseudopleuronectes americanus. Nature 247 (1974) 237-238
    • (1974) Nature , vol.247 , pp. 237-238
    • Duman, J.G.1    DeVries, A.L.2
  • 51
    • 0016826326 scopus 로고
    • The role of macromolecular antifreezes in cold water fishes
    • Duman J.G., and DeVries A.L. The role of macromolecular antifreezes in cold water fishes. Comp. Biochem. Physiol. 52A (1975) 193-199
    • (1975) Comp. Biochem. Physiol. , vol.52 A , pp. 193-199
    • Duman, J.G.1    DeVries, A.L.2
  • 52
    • 0017118163 scopus 로고
    • Isolation, characterization, and physical properties of protein antifreezes from the winter flounder, Pseudopleuronectes americanus
    • Duman J.G., and DeVries A.L. Isolation, characterization, and physical properties of protein antifreezes from the winter flounder, Pseudopleuronectes americanus. Comp. Biochem. Physiol. 53B (1976) 375-380
    • (1976) Comp. Biochem. Physiol. , vol.53 B , pp. 375-380
    • Duman, J.G.1    DeVries, A.L.2
  • 53
    • 0006657942 scopus 로고
    • Renal corpuscle development in boreal fishes with and without antifreezes
    • Eastman J.T., Boyd R.B., and DeVries A.L. Renal corpuscle development in boreal fishes with and without antifreezes. Fish Physiol. Biochem. 4 (1987) 89-100
    • (1987) Fish Physiol. Biochem. , vol.4 , pp. 89-100
    • Eastman, J.T.1    Boyd, R.B.2    DeVries, A.L.3
  • 54
    • 84985161024 scopus 로고
    • Renal glomerular evolution in Antarctic notothenioid fishes
    • Eastman J.T., and DeVries A.L. Renal glomerular evolution in Antarctic notothenioid fishes. J. Fish Biol. 29 (1986) 649-662
    • (1986) J. Fish Biol. , vol.29 , pp. 649-662
    • Eastman, J.T.1    DeVries, A.L.2
  • 55
    • 0031022097 scopus 로고    scopus 로고
    • Morphology of the digestive system of Antarctic nototheniid fishes
    • Eastman J.T., and DeVries A.L. Morphology of the digestive system of Antarctic nototheniid fishes. Polar Biol. 17 (1997) 1-13
    • (1997) Polar Biol. , vol.17 , pp. 1-13
    • Eastman, J.T.1    DeVries, A.L.2
  • 56
    • 0018645127 scopus 로고
    • Renal conservation of antifreeze peptide in Antarctic eelpout, Rhigophila dearborni
    • Eastman J.T., DeVries A.L., Coalson R.E., Nordquist R.E., and Boyd R.B. Renal conservation of antifreeze peptide in Antarctic eelpout, Rhigophila dearborni. Nature 282 (1979) 217-218
    • (1979) Nature , vol.282 , pp. 217-218
    • Eastman, J.T.1    DeVries, A.L.2    Coalson, R.E.3    Nordquist, R.E.4    Boyd, R.B.5
  • 57
    • 0038199673 scopus 로고    scopus 로고
    • Does fish from the Disko Bay area of Greenland possess antifreeze proteins during the summer?
    • Enevoldsen L.T., Heiner I., DeVries A.L., and Steffensen J.F. Does fish from the Disko Bay area of Greenland possess antifreeze proteins during the summer?. Polar Biol. 26 (2003) 365-370
    • (2003) Polar Biol. , vol.26 , pp. 365-370
    • Enevoldsen, L.T.1    Heiner, I.2    DeVries, A.L.3    Steffensen, J.F.4
  • 58
    • 0035844710 scopus 로고    scopus 로고
    • Isolation and characterization of type I antifreeze proteins from Atlantic snailfish (Liparis atlanticus) and dusky snailfish (Liparis gibbus)
    • Evan R.P., and Fletcher G.L. Isolation and characterization of type I antifreeze proteins from Atlantic snailfish (Liparis atlanticus) and dusky snailfish (Liparis gibbus). Biochim. Biophys. Acta 1547 (2001) 235-244
    • (2001) Biochim. Biophys. Acta , vol.1547 , pp. 235-244
    • Evan, R.P.1    Fletcher, G.L.2
  • 59
    • 0002410699 scopus 로고
    • Osmotic and ionic regulation
    • Evans D.H. (Ed), CRC Press, Boca Raton
    • Evans D.H. Osmotic and ionic regulation. In: Evans D.H. (Ed). "The Physiology of Fishes" (1993), CRC Press, Boca Raton
    • (1993) "The Physiology of Fishes"
    • Evans, D.H.1
  • 60
    • 0001446789 scopus 로고
    • Isolation and characterization of antifreeze proteins from smelt (Osmerus mordax) and Atlantic herring (Culpea harengus harengus)
    • Ewart K.V., and Fletcher G.L. Isolation and characterization of antifreeze proteins from smelt (Osmerus mordax) and Atlantic herring (Culpea harengus harengus). Can. J. Zool. 68 (1990) 1652-1658
    • (1990) Can. J. Zool. , vol.68 , pp. 1652-1658
    • Ewart, K.V.1    Fletcher, G.L.2
  • 61
    • 0027551726 scopus 로고
    • Herring antifreeze protein: Primary structure and evidence for a C-type lectin evolutionary origin
    • Ewart K.V., and Fletcher G.L. Herring antifreeze protein: Primary structure and evidence for a C-type lectin evolutionary origin. Mol. Mar. Biol. Biotech. 2 (1993) 20-27
    • (1993) Mol. Mar. Biol. Biotech. , vol.2 , pp. 20-27
    • Ewart, K.V.1    Fletcher, G.L.2
  • 62
    • 0001044156 scopus 로고    scopus 로고
    • The ice-binding site of Atlantic herring antifreeze protein corresponds to the carbohydrate-binding site of C-type lectins
    • Ewart K.V., Li Z., Yang D.S.C., Fletcher G.L., and Hew C.L. The ice-binding site of Atlantic herring antifreeze protein corresponds to the carbohydrate-binding site of C-type lectins. Biochem. 37 (1998) 4080-4085
    • (1998) Biochem. , vol.37 , pp. 4080-4085
    • Ewart, K.V.1    Li, Z.2    Yang, D.S.C.3    Fletcher, G.L.4    Hew, C.L.5
  • 63
    • 0026772705 scopus 로고
    • Structural and functional similarity between fish antifreeze proteins and calcium-dependent lectins
    • Ewart K.V., Rubinsky B., and Fletcher G.L. Structural and functional similarity between fish antifreeze proteins and calcium-dependent lectins. Biochim. Biophys. Res. Commun. 185 (1992) 335-340
    • (1992) Biochim. Biophys. Res. Commun. , vol.185 , pp. 335-340
    • Ewart, K.V.1    Rubinsky, B.2    Fletcher, G.L.3
  • 64
    • 0022005282 scopus 로고
    • The fish spleen: Structure and function
    • Fänge R., and Nilsson S. The fish spleen: Structure and function. Experientia 41 (1985) 152-158
    • (1985) Experientia , vol.41 , pp. 152-158
    • Fänge, R.1    Nilsson, S.2
  • 65
    • 0033538414 scopus 로고    scopus 로고
    • RAPD and scnDNA analyses of polar cod, Boreogadus saida (Pisces, Gadidae) in the north Atlantic
    • Fevolden S.E., Martinez I., and Christiansen J.S. RAPD and scnDNA analyses of polar cod, Boreogadus saida (Pisces, Gadidae) in the north Atlantic. SARSIA 84 (1999) 99-103
    • (1999) SARSIA , vol.84 , pp. 99-103
    • Fevolden, S.E.1    Martinez, I.2    Christiansen, J.S.3
  • 66
    • 0000447121 scopus 로고
    • Antifreeze proteins in the Arctic shorthorn sculpin (Myoxocephalus scorpius)
    • Fletcher G.L., Addison R.F., Hew C.L., and Slaughter D. Antifreeze proteins in the Arctic shorthorn sculpin (Myoxocephalus scorpius). Arctic 35 (1982) 302-306
    • (1982) Arctic , vol.35 , pp. 302-306
    • Fletcher, G.L.1    Addison, R.F.2    Hew, C.L.3    Slaughter, D.4
  • 67
    • 0000256338 scopus 로고
    • Annual antifreeze cycles in Newfoundland, New Brunswick and Long Island winter flounder Pseudopleuronectes americanus
    • Fletcher G.L., Haya K., King M.J., and Reisman H.M. Annual antifreeze cycles in Newfoundland, New Brunswick and Long Island winter flounder Pseudopleuronectes americanus. Mar. Ecol Prog. Ser. 21 (1985) 205-212
    • (1985) Mar. Ecol Prog. Ser. , vol.21 , pp. 205-212
    • Fletcher, G.L.1    Haya, K.2    King, M.J.3    Reisman, H.M.4
  • 69
    • 0000423097 scopus 로고
    • Isolation and characterization of antifreeze glycoproteins from the frost fish, Microgadus tomcod
    • Fletcher G.L., Hew C.H., and Joshi S.B. Isolation and characterization of antifreeze glycoproteins from the frost fish, Microgadus tomcod. Can. J. Zool. 60 (1981) 348-355
    • (1981) Can. J. Zool. , vol.60 , pp. 348-355
    • Fletcher, G.L.1    Hew, C.H.2    Joshi, S.B.3
  • 70
    • 0000129524 scopus 로고
    • Year-round presence of high levels of plasma antifreeze peptides in a temperate fish, ocean pout (Macrozoarces americanus)
    • Fletcher G.L., Hew C.L., Li X., Haya K., and Kao M.H. Year-round presence of high levels of plasma antifreeze peptides in a temperate fish, ocean pout (Macrozoarces americanus). Can. J. Zool. 63 (1985) 488-493
    • (1985) Can. J. Zool. , vol.63 , pp. 488-493
    • Fletcher, G.L.1    Hew, C.L.2    Li, X.3    Haya, K.4    Kao, M.H.5
  • 73
    • 0016036394 scopus 로고
    • Conditional instability of sea water at the freezing point
    • Foldvik A., and Kvinge T. Conditional instability of sea water at the freezing point. Deep-Sea Res. 21 (1974) 169-174
    • (1974) Deep-Sea Res. , vol.21 , pp. 169-174
    • Foldvik, A.1    Kvinge, T.2
  • 74
    • 0021536657 scopus 로고
    • The marine environment
    • Laws R.M. (Ed), Academic Press, London
    • Foster T.D. The marine environment. In: Laws R.M. (Ed). "Antarctic Ecology" Vol. 2 (1984), Academic Press, London 345-371
    • (1984) "Antarctic Ecology" , vol.2 , pp. 345-371
    • Foster, T.D.1
  • 75
    • 0001127637 scopus 로고
    • The role of the spleen during exercise in Antarctic teleost, Pagothenia borchgrevinki
    • Franklin C.E., Davison W., and McKenzie J.C. The role of the spleen during exercise in Antarctic teleost, Pagothenia borchgrevinki. J. Exp. Biol. 174 (1993) 381-386
    • (1993) J. Exp. Biol. , vol.174 , pp. 381-386
    • Franklin, C.E.1    Davison, W.2    McKenzie, J.C.3
  • 76
    • 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 pro-sequences
    • Gong Z., Ewart K.V., Hu Z., Fletcher G.L., and Hew C.L. Skin antifreeze protein genes of the winter flounder, Pleuronectes americanus, encode distinct and active polypeptides without the secretory signal and pro-sequences. J. Biol. Chem. 271 (1996) 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
  • 78
    • 0033568338 scopus 로고    scopus 로고
    • Type I antifreeze proteins: Structure-activity studies and mechanism of ice growth inhibition
    • Harding M.M., Ward L.G., and Haymet A.D.J. Type I antifreeze proteins: Structure-activity studies and mechanism of ice growth inhibition. Eur. J. Biochem. 264 (1999) 653-665
    • (1999) Eur. J. Biochem. , vol.264 , pp. 653-665
    • Harding, M.M.1    Ward, L.G.2    Haymet, A.D.J.3
  • 79
    • 1842392830 scopus 로고
    • Antifreeze glycoprotein synthesis in the Antarctic fish Trematomus hansoni by constant infusion in vivo
    • Haschemeyer A.E.V., and Mathews R.W. Antifreeze glycoprotein synthesis in the Antarctic fish Trematomus hansoni by constant infusion in vivo. Physiol. Zool. 53 (1980) 383-393
    • (1980) Physiol. Zool. , vol.53 , pp. 383-393
    • Haschemeyer, A.E.V.1    Mathews, R.W.2
  • 80
    • 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
    • Haymet A.D.J., Ward L.G., and Harding M.M. 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 (1999) 941-948
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 941-948
    • Haymet, A.D.J.1    Ward, L.G.2    Harding, M.M.3
  • 82
    • 0001439639 scopus 로고
    • Antifreeze glycoproteins in the plasma of Newfoundland Atlantic cod (Gadus morhua)
    • Hew C.L., Slaughter D., Fletcher G.L., and Joshi S. Antifreeze glycoproteins in the plasma of Newfoundland Atlantic cod (Gadus morhua). Can. J. Zool. 59 (1981) 2186-2192
    • (1981) Can. J. Zool. , vol.59 , pp. 2186-2192
    • Hew, C.L.1    Slaughter, D.2    Fletcher, G.L.3    Joshi, S.4
  • 83
    • 0003101944 scopus 로고
    • Antifreeze polypeptides from the Newfoundland ocean pout, Macrozoarces americanus: Presence of multiple and compositionally diverse components
    • Hew C.L., Slaughter D., Joshi S., Fletcher G.L., and Ananthanarayanan V.S. Antifreeze polypeptides from the Newfoundland ocean pout, Macrozoarces americanus: Presence of multiple and compositionally diverse components. J. Comp. Physiol. B155 (1984) 81-88
    • (1984) J. Comp. Physiol. , vol.B155 , pp. 81-88
    • Hew, C.L.1    Slaughter, D.2    Joshi, S.3    Fletcher, G.L.4    Ananthanarayanan, V.S.5
  • 84
    • 0023682265 scopus 로고
    • Multiple genes provide the basis for antifreeze protein diversity and dosage in the ocean pout, Macrozoarces americanus
    • Hew C.L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K., Hayes P.H., Buettner B., and Davies P.L. Multiple genes provide the basis for antifreeze protein diversity and dosage in the ocean pout, Macrozoarces americanus. J. Biol. Chem. 263 (1988) 12049-12055
    • (1988) J. Biol. Chem. , vol.263 , pp. 12049-12055
    • Hew, C.L.1    Wang, N.-C.2    Joshi, S.3    Fletcher, G.L.4    Scott, G.K.5    Hayes, P.H.6    Buettner, B.7    Davies, P.L.8
  • 85
    • 0017126510 scopus 로고
    • The synthesis of freezing-point depression protein of the winter flounder Pseudopleuronectes americanus in Xenopus laevis oocytes
    • Hew C.L., and Yip C. The synthesis of freezing-point depression protein of the winter flounder Pseudopleuronectes americanus in Xenopus laevis oocytes. Biochim. Biophys. Res. Commun. 71 (1976) 845-850
    • (1976) Biochim. Biophys. Res. Commun. , vol.71 , pp. 845-850
    • Hew, C.L.1    Yip, C.2
  • 86
    • 0005294294 scopus 로고
    • Morphology and enzyme histochemistry in liver of largemouth bass (Micropterus salmoides)
    • Hinton D.E., Snipes R.L., and Kendall M.W. Morphology and enzyme histochemistry in liver of largemouth bass (Micropterus salmoides). J. Fish Res. Board Can. 29 (1972) 531-534
    • (1972) J. Fish Res. Board Can. , vol.29 , pp. 531-534
    • Hinton, D.E.1    Snipes, R.L.2    Kendall, M.W.3
  • 88
    • 0026271147 scopus 로고
    • Biogeography of gadoid fishes
    • Howe G.J. Biogeography of gadoid fishes. J. Biogeogr. 18 (1991) 595-622
    • (1991) J. Biogeogr. , vol.18 , pp. 595-622
    • Howe, G.J.1
  • 90
    • 0141458030 scopus 로고    scopus 로고
    • Annual warming episodes in seawater temperatures in McMurdo Sound in relationship to endogenous ice in notothenioid fish
    • Hunt B.M., Hoefling K., and Cheng C.-H.C. Annual warming episodes in seawater temperatures in McMurdo Sound in relationship to endogenous ice in notothenioid fish. Antarct. Sci. 15 (2003) 333-338
    • (2003) Antarct. Sci. , vol.15 , pp. 333-338
    • Hunt, B.M.1    Hoefling, K.2    Cheng, C.-H.C.3
  • 91
    • 0001860052 scopus 로고    scopus 로고
    • Ontogeny of feeding and respiration in larval Atlantic cod Gadus morhua (Teleostei, Gadiformes). I. Morphology
    • Hunt von Herbing I., Miyake T., Hall B.K., and Boutilier R.G. Ontogeny of feeding and respiration in larval Atlantic cod Gadus morhua (Teleostei, Gadiformes). I. Morphology. J. Morphol. 227 (1996) 15-35
    • (1996) J. Morphol. , vol.227 , pp. 15-35
    • Hunt von Herbing, I.1    Miyake, T.2    Hall, B.K.3    Boutilier, R.G.4
  • 92
    • 0002783722 scopus 로고    scopus 로고
    • Ontogeny of feeding and respiration in larval Atlantic cod Gadus morhua (Teleostei, Gadiformes). II. Function
    • Hunt von Herbing I., Miyake T., Hall B.K., and Boutilier R.G. Ontogeny of feeding and respiration in larval Atlantic cod Gadus morhua (Teleostei, Gadiformes). II. Function. J. Morphol. 227 (1996) 37-50
    • (1996) J. Morphol. , vol.227 , pp. 37-50
    • Hunt von Herbing, I.1    Miyake, T.2    Hall, B.K.3    Boutilier, R.G.4
  • 93
    • 0029856558 scopus 로고    scopus 로고
    • Structural basis for the binding of a globular antifreeze protein to ice
    • Jia Z.C., Deluca C.I., Chao H.M., and Davies P.L. Structural basis for the binding of a globular antifreeze protein to ice. Nature 384 (1996) 285-288
    • (1996) Nature , vol.384 , pp. 285-288
    • Jia, Z.C.1    Deluca, C.I.2    Chao, H.M.3    Davies, P.L.4
  • 95
    • 0035206618 scopus 로고    scopus 로고
    • Oxygen consumption of East Siberian cod: No support for the metabolic cold adaptation theory
    • Jordan A.D., Jurngersen M., and Steffensen J.F. Oxygen consumption of East Siberian cod: No support for the metabolic cold adaptation theory. J. Fish Biol. 59 (2001) 818-823
    • (2001) J. Fish Biol. , vol.59 , pp. 818-823
    • Jordan, A.D.1    Jurngersen, M.2    Steffensen, J.F.3
  • 96
    • 0039692087 scopus 로고
    • Protein content and freezing avoidance properties of the subdermal extracellular matrix and serum of the Antarctic snailfish, Paraliparis devriesi
    • Jung A., Johnson P., Eastman J.T., and DeVries A.L. Protein content and freezing avoidance properties of the subdermal extracellular matrix and serum of the Antarctic snailfish, Paraliparis devriesi. Fish Physiol. Biochem. 14 (1995) 71-80
    • (1995) Fish Physiol. Biochem. , vol.14 , pp. 71-80
    • Jung, A.1    Johnson, P.2    Eastman, J.T.3    DeVries, A.L.4
  • 97
    • 0001427778 scopus 로고
    • The relationship between molecular weight and antifreeze polypeptide activity in marine fish
    • Kao M.H., Fletcher G.L., Wang N.C., and Hew C.H. The relationship between molecular weight and antifreeze polypeptide activity in marine fish. Can. J. Zool. 64 (1985) 578-582
    • (1985) Can. J. Zool. , vol.64 , pp. 578-582
    • Kao, M.H.1    Fletcher, G.L.2    Wang, N.C.3    Hew, C.H.4
  • 98
    • 0000523437 scopus 로고
    • Cenozoic evolution of Antarctic glaciation, the circum-Antarctic Ocean, and their impact on global paleoceanography
    • Kennett J.P. Cenozoic evolution of Antarctic glaciation, the circum-Antarctic Ocean, and their impact on global paleoceanography. J. Geophys. Res. 82 (1977) 3843-3860
    • (1977) J. Geophys. Res. , vol.82 , pp. 3843-3860
    • Kennett, J.P.1
  • 100
    • 0025959821 scopus 로고
    • Adsorption of helical antifreeze peptides on specific ice crystal surface planes
    • Knight C.A., Cheng C.-H.C., and DeVries A.L. Adsorption of helical antifreeze peptides on specific ice crystal surface planes. Biophys. J. 59 (1991) 409-418
    • (1991) Biophys. J. , vol.59 , pp. 409-418
    • Knight, C.A.1    Cheng, C.-H.C.2    DeVries, A.L.3
  • 101
    • 0028761625 scopus 로고
    • Effects of a polymeric, non-equilibrium "antifreeze" upon ice growth from water
    • Knight C.A., and DeVries A.L. Effects of a polymeric, non-equilibrium "antifreeze" upon ice growth from water. J. Crystal Growth 143 (1994) 301-310
    • (1994) J. Crystal Growth , vol.143 , pp. 301-310
    • Knight, C.A.1    DeVries, A.L.2
  • 102
    • 0021236688 scopus 로고
    • Fish antifreeze protein and the freezing and recrystallization of ice
    • Knight C.A., DeVries A.L., and Oolman L.D. Fish antifreeze protein and the freezing and recrystallization of ice. Nature 308 (1984) 295-296
    • (1984) Nature , vol.308 , pp. 295-296
    • Knight, C.A.1    DeVries, A.L.2    Oolman, L.D.3
  • 103
    • 0027396926 scopus 로고
    • Adsorption of fish antifreeze glycopeptides to ice, and effects on ice crystal growth
    • Knight C.A., Driggers E., and DeVries A.L. Adsorption of fish antifreeze glycopeptides to ice, and effects on ice crystal growth. Biophys. J. 64 (1993) 252-259
    • (1993) Biophys. J. , vol.64 , pp. 252-259
    • Knight, C.A.1    Driggers, E.2    DeVries, A.L.3
  • 104
    • 0037306916 scopus 로고    scopus 로고
    • The refined crystal structure of an eel pout Type III antifreeze protein RD1 at 0.62A resolution reveals structural microheterogeneity of protein and solvation
    • Ko T.P., Robinson H., Gao Y.-G., Cheng C.-H.C., DeVries A.L., and Wang A.H.-J. The refined crystal structure of an eel pout Type III antifreeze protein RD1 at 0.62A resolution reveals structural microheterogeneity of protein and solvation. Biophys. J. 84 (2003) 1228-1237
    • (2003) Biophys. J. , vol.84 , pp. 1228-1237
    • Ko, T.P.1    Robinson, H.2    Gao, Y.-G.3    Cheng, C.-H.C.4    DeVries, A.L.5    Wang, A.H.-J.6
  • 106
    • 0029108415 scopus 로고
    • Structure of the exocrine pancreas of flounder (Paralichthys olivaceus): Immunological localization of zymogen granules in the digestive tract using anti-trypsinogen antibody
    • Kurokawa T., and Suzuki T. Structure of the exocrine pancreas of flounder (Paralichthys olivaceus): Immunological localization of zymogen granules in the digestive tract using anti-trypsinogen antibody. J. Fish Biol. 46 (1995) 292-301
    • (1995) J. Fish Biol. , vol.46 , pp. 292-301
    • Kurokawa, T.1    Suzuki, T.2
  • 108
    • 0018800324 scopus 로고
    • Environmental regulation of gene expression
    • Lin Y. Environmental regulation of gene expression. J. Biol. Chem. 254 (1979) 1422-1426
    • (1979) J. Biol. Chem. , vol.254 , pp. 1422-1426
    • Lin, Y.1
  • 109
    • 0019327874 scopus 로고
    • Purification and characterization of winter flounder antifreeze peptide messenger ribonucleic acid
    • Lin Y., and Long D.J. Purification and characterization of winter flounder antifreeze peptide messenger ribonucleic acid. Biochemistry 19 (1980) 1111-1116
    • (1980) Biochemistry , vol.19 , pp. 1111-1116
    • Lin, Y.1    Long, D.J.2
  • 110
    • 0002435281 scopus 로고
    • Oceanographic investigations in McMurdo Sound, Antarctica
    • Llano G.A. (Ed), American Geophysical Union, Washington, DC
    • Littlepage J.L. Oceanographic investigations in McMurdo Sound, Antarctica. In: Llano G.A. (Ed). "Biology of the Antarctic Seas II" Vol. 5 (1965), American Geophysical Union, Washington, DC 1-37
    • (1965) "Biology of the Antarctic Seas II" , vol.5 , pp. 1-37
    • Littlepage, J.L.1
  • 111
    • 0035853750 scopus 로고    scopus 로고
    • Isolation and characterization of skin-type, type I antifreeze polypeptides from the longhorn sculpin, Myoxocephalus octodecemspinosus
    • Low W.K., Lin Q., Stathakis C., Miao M., Fletcher G.L., and Hew C.L. Isolation and characterization of skin-type, type I antifreeze polypeptides from the longhorn sculpin, Myoxocephalus octodecemspinosus. J. Biol. Chem. 276 (2001) 11582-11589
    • (2001) J. Biol. Chem. , vol.276 , pp. 11582-11589
    • Low, W.K.1    Lin, Q.2    Stathakis, C.3    Miao, M.4    Fletcher, G.L.5    Hew, C.L.6
  • 112
    • 0032483453 scopus 로고    scopus 로고
    • Skin-type antifreeze protein from the shorthorn sculpin, Myoxocephalus scorpius: Expression and characterization of Mr 9700 recombinant protein
    • Low W.K., Miao M., Ewart K.V., Yang D.S., Fletcher G.L., and Hew C.L. Skin-type antifreeze protein from the shorthorn sculpin, Myoxocephalus scorpius: Expression and characterization of Mr 9700 recombinant protein. J. Biol. Chem. 273 (1998) 23098-23103
    • (1998) J. Biol. Chem. , vol.273 , pp. 23098-23103
    • Low, W.K.1    Miao, M.2    Ewart, K.V.3    Yang, D.S.4    Fletcher, G.L.5    Hew, C.L.6
  • 113
    • 2442688072 scopus 로고    scopus 로고
    • Hyperactive antifreeze protein in a fish
    • Marshall C.B., and Davies P.L. Hyperactive antifreeze protein in a fish. Nature 429 (2004) 153
    • (2004) Nature , vol.429 , pp. 153
    • Marshall, C.B.1    Davies, P.L.2
  • 114
    • 0002225921 scopus 로고
    • Physical and chemical basis of injury in single-celled miro-organisms subjected to freezing and thawing
    • Meryman H.T. (Ed), Academic Press, London
    • Mazur P. Physical and chemical basis of injury in single-celled miro-organisms subjected to freezing and thawing. In: Meryman H.T. (Ed). "Cryobiology" (1966), Academic Press, London 214-310
    • (1966) "Cryobiology" , pp. 214-310
    • Mazur, P.1
  • 115
    • 0003289808 scopus 로고
    • Freezing point of seawater-Eighth report of the joint panel of oceanographic tables and standards
    • UNESCO, Paris
    • Millero F.J. Freezing point of seawater-Eighth report of the joint panel of oceanographic tables and standards. UNESCO Technical Papers in Marine Science 28 (1978), UNESCO, Paris 29-31
    • (1978) UNESCO Technical Papers in Marine Science 28 , pp. 29-31
    • Millero, F.J.1
  • 116
    • 0038084267 scopus 로고    scopus 로고
    • Spatial expression patterns of skin-type antifreeze protein in winter flounder (Pseudopleuronectes americanus) epidermis following metamorphosis
    • Murray H.M., Hew C.H., and Fletcher G.L. Spatial expression patterns of skin-type antifreeze protein in winter flounder (Pseudopleuronectes americanus) epidermis following metamorphosis. J. Morphol. 257 (2003) 78-86
    • (2003) J. Morphol. , vol.257 , pp. 78-86
    • Murray, H.M.1    Hew, C.H.2    Fletcher, G.L.3
  • 117
    • 0001051857 scopus 로고
    • Marine climate off Newfoundland and its influence on salmon (Salmo salar) and capelin (Mallotus villosus)
    • Beamish R.J. (Ed), Can. Spec. Publ. Fish. Aquat. Sci., Ottawa
    • Narayanan S., Carscadden J., Dempson J.B., O'Connell M.F., Prinsenberg S., Reddin D.G., and Shackell N. Marine climate off Newfoundland and its influence on salmon (Salmo salar) and capelin (Mallotus villosus). In: Beamish R.J. (Ed). "Climate Change and Northern Fish Populations" Vol. 121 (1995), Can. Spec. Publ. Fish. Aquat. Sci., Ottawa 461-474
    • (1995) "Climate Change and Northern Fish Populations" , vol.121 , pp. 461-474
    • Narayanan, S.1    Carscadden, J.2    Dempson, J.B.3    O'Connell, M.F.4    Prinsenberg, S.5    Reddin, D.G.6    Shackell, N.7
  • 118
    • 0026761365 scopus 로고
    • Structure of an antifreeze polypeptide from the sea raven: Disulfide bonds and similarity to lectin binding proteins
    • Ng N.F.L., and Hew C.L. Structure of an antifreeze polypeptide from the sea raven: Disulfide bonds and similarity to lectin binding proteins. J. Biol. Chem. 267 (1992) 16069-16075
    • (1992) J. Biol. Chem. , vol.267 , pp. 16069-16075
    • Ng, N.F.L.1    Hew, C.L.2
  • 119
    • 0001762685 scopus 로고    scopus 로고
    • Ocean circulation beneath the western Ronne Ice Shelf, as derived from in situ measurements of water currents and properties
    • "Ocean, Ice and Atmosphere: Interactions at the Antarctic continental margin.". Jacobs S.S., and Weiss R.F. (Eds), American Geophysical Union, Washington DC
    • Nicholls K.W., and Makinson K. Ocean circulation beneath the western Ronne Ice Shelf, as derived from in situ measurements of water currents and properties. In: Jacobs S.S., and Weiss R.F. (Eds). "Ocean, Ice and Atmosphere: Interactions at the Antarctic continental margin.". Antarctic Research Series Vol. 75 (1998), American Geophysical Union, Washington DC 301-318
    • (1998) Antarctic Research Series , vol.75 , pp. 301-318
    • Nicholls, K.W.1    Makinson, K.2
  • 120
    • 0020478817 scopus 로고
    • Characterization of glycoprotein antifreeze biosynthesis in isolated hepatocytes from Pagothenia borchgrevinki
    • O'Grady S.M., Clarke A., and DeVries A.L. Characterization of glycoprotein antifreeze biosynthesis in isolated hepatocytes from Pagothenia borchgrevinki. J. Exp. Zool. 220 (1982) 179-189
    • (1982) J. Exp. Zool. , vol.220 , pp. 179-189
    • O'Grady, S.M.1    Clarke, A.2    DeVries, A.L.3
  • 121
    • 0020149633 scopus 로고
    • Protein and glycoprotein antifreezes in intestinal fluid of polar fishes
    • O'Grady S.M., Ellory J.C., and DeVries A.L. Protein and glycoprotein antifreezes in intestinal fluid of polar fishes. J. Exp. Biol. 98 (1982) 429-438
    • (1982) J. Exp. Biol. , vol.98 , pp. 429-438
    • O'Grady, S.M.1    Ellory, J.C.2    DeVries, A.L.3
  • 122
    • 0012354274 scopus 로고
    • The role of low molecular weight antifreeze glycopeptides in the bile and intestinal fluid of Antarctic fishes
    • O'Grady S.M., Ellory J.C., and DeVries A.L. The role of low molecular weight antifreeze glycopeptides in the bile and intestinal fluid of Antarctic fishes. J. Exp. Biol. 104 (1983) 149-162
    • (1983) J. Exp. Biol. , vol.104 , pp. 149-162
    • O'Grady, S.M.1    Ellory, J.C.2    DeVries, A.L.3
  • 123
    • 0000286513 scopus 로고
    • Comparison of antifreeze glycopeptides from Arctic and Antarctic fishes
    • O'Grady S.M., Schrag J.D., Raymond J.A., and DeVries A.L. Comparison of antifreeze glycopeptides from Arctic and Antarctic fishes. J. Exp. Zool. 224 (1982) 177-185
    • (1982) J. Exp. Zool. , vol.224 , pp. 177-185
    • O'Grady, S.M.1    Schrag, J.D.2    Raymond, J.A.3    DeVries, A.L.4
  • 124
    • 0000923342 scopus 로고
    • Activity, movements, and feeding behavior of the cunner, Tautogolabrus adspersus, and comparison of food habits with young tautog, Tautoga onitus, off Long Island, New York
    • Olla B.L., Bejda A.J., and Martin D. Activity, movements, and feeding behavior of the cunner, Tautogolabrus adspersus, and comparison of food habits with young tautog, Tautoga onitus, off Long Island, New York. Fishery Bull. Ill. 733 (1975) 895-900
    • (1975) Fishery Bull. Ill. , vol.733 , pp. 895-900
    • Olla, B.L.1    Bejda, A.J.2    Martin, D.3
  • 125
    • 0017895427 scopus 로고
    • Antifreeze glycoproteins from Arctic fish
    • Osuga D.T., and Feeney R.E. Antifreeze glycoproteins from Arctic fish. J. Biol. Chem. 253 (1978) 5338-5343
    • (1978) J. Biol. Chem. , vol.253 , pp. 5338-5343
    • Osuga, D.T.1    Feeney, R.E.2
  • 126
    • 0002400688 scopus 로고
    • Seasonal changes in osmotic pressure in flounder sera
    • Pearcy W.G. Seasonal changes in osmotic pressure in flounder sera. Science 134 (1961) 193-194
    • (1961) Science , vol.134 , pp. 193-194
    • Pearcy, W.G.1
  • 128
  • 129
    • 84987493121 scopus 로고
    • Seasonal variation of antifreeze peptide in the winter flounder, Pseudopleuronectes americanus
    • Petzel D.H., Reisman H.M., and DeVries A.L. Seasonal variation of antifreeze peptide in the winter flounder, Pseudopleuronectes americanus. J. Exp. Zool. 211 (1980) 63-69
    • (1980) J. Exp. Zool. , vol.211 , pp. 63-69
    • Petzel, D.H.1    Reisman, H.M.2    DeVries, A.L.3
  • 130
    • 0001514211 scopus 로고
    • Glycerol is a colligative antifreeze in some northern fishes
    • Raymond J.A. Glycerol is a colligative antifreeze in some northern fishes. J. Exp. Zool. 262 (1992) 347-352
    • (1992) J. Exp. Zool. , vol.262 , pp. 347-352
    • Raymond, J.A.1
  • 131
    • 0015451003 scopus 로고
    • Freezing behavior of fish blood glycoproteins with antifreeze properties
    • Raymond J.A., and DeVries A.L. Freezing behavior of fish blood glycoproteins with antifreeze properties. Cryobiology 9 (1972) 541-547
    • (1972) Cryobiology , vol.9 , pp. 541-547
    • Raymond, J.A.1    DeVries, A.L.2
  • 132
    • 0042183228 scopus 로고
    • Adsorption-inhibition as a mechanism of freezing resistance in polar fishes
    • Raymond J.A., and DeVries A.L. Adsorption-inhibition as a mechanism of freezing resistance in polar fishes. Proc. Natl. Acad. Sci. USA 74 (1977) 2589-2593
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 2589-2593
    • Raymond, J.A.1    DeVries, A.L.2
  • 133
    • 0016760582 scopus 로고
    • Glycoprotein and protein antifreezes in two Alaskan fishes
    • Raymond J.A., Lin Y., and DeVries A.L. Glycoprotein and protein antifreezes in two Alaskan fishes. J. Exp. Zool. 193 (1975) 125-130
    • (1975) J. Exp. Zool. , vol.193 , pp. 125-130
    • Raymond, J.A.1    Lin, Y.2    DeVries, A.L.3
  • 134
    • 0017751787 scopus 로고
    • Circular dichroism of protein and glycoprotein fish antifreeze
    • Raymond J.A., Radding W., and DeVries A.L. Circular dichroism of protein and glycoprotein fish antifreeze. Biopolymers 16 (1977) 2575-2578
    • (1977) Biopolymers , vol.16 , pp. 2575-2578
    • Raymond, J.A.1    Radding, W.2    DeVries, A.L.3
  • 135
    • 0024616108 scopus 로고
    • Inhibition of growth of non-basal planes in ice by fish antifreeze
    • Raymond J.A., Wilson P.W., and DeVries A.L. Inhibition of growth of non-basal planes in ice by fish antifreeze. Proc. Natl. Acad. Sci. USA 86 (1989) 881-885
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 881-885
    • Raymond, J.A.1    Wilson, P.W.2    DeVries, A.L.3
  • 136
    • 51249173699 scopus 로고
    • Antifreeze proteins in the grubby sculpin, Myoxocephalus aenaeus and the tomcod, Microgadus tomcod: Comparisons of seasonal cycles
    • Reisman H.M., Fletcher G.L., Kao M.H., and Shears M.A. Antifreeze proteins in the grubby sculpin, Myoxocephalus aenaeus and the tomcod, Microgadus tomcod: Comparisons of seasonal cycles. Env. Biol. Fishes 18 (1987) 295-301
    • (1987) Env. Biol. Fishes , vol.18 , pp. 295-301
    • Reisman, H.M.1    Fletcher, G.L.2    Kao, M.H.3    Shears, M.A.4
  • 137
    • 33745278140 scopus 로고
    • Antifreeze glycoprotein in a southern population of Atlantic tomcod, Microgadus tomcod
    • Reisman H.M., Kao M.H., and Fletcher G.L. Antifreeze glycoprotein in a southern population of Atlantic tomcod, Microgadus tomcod. Comp. Biochem. Physiol. 78A (1984) 445-447
    • (1984) Comp. Biochem. Physiol. , vol.78 A , pp. 445-447
    • Reisman, H.M.1    Kao, M.H.2    Fletcher, G.L.3
  • 139
    • 0023656535 scopus 로고
    • Primary and secondary structure of antifreeze peptides from arctic and antarctic zoarcid fishes
    • Schrag J.D., Cheng C.-H.C., Panico M., Morris H.R., and DeVries A.L. Primary and secondary structure of antifreeze peptides from arctic and antarctic zoarcid fishes. Biochim. Biophys. Acta 915 (1987) 357-370
    • (1987) Biochim. Biophys. Acta , vol.915 , pp. 357-370
    • Schrag, J.D.1    Cheng, C.-H.C.2    Panico, M.3    Morris, H.R.4    DeVries, A.L.5
  • 140
    • 0345039273 scopus 로고
    • The effects of freezing rate on the cooperativity of antifreeze glycopeptides
    • Schrag J.D., and DeVries A.L. The effects of freezing rate on the cooperativity of antifreeze glycopeptides. Comp. Biochem. Physiol. 74A (1982) 381-385
    • (1982) Comp. Biochem. Physiol. , vol.74 A , pp. 381-385
    • Schrag, J.D.1    DeVries, A.L.2
  • 141
    • 0020476213 scopus 로고
    • Relationship of amino acid composition and molecular weight of antifreeze glycopeptides to non-colligative freezing point depression
    • Schrag J.D., O'Grady S.M., and DeVries A.L. Relationship of amino acid composition and molecular weight of antifreeze glycopeptides to non-colligative freezing point depression. Biochim. Biophys. Acta 717 (1982) 322-326
    • (1982) Biochim. Biophys. Acta , vol.717 , pp. 322-326
    • Schrag, J.D.1    O'Grady, S.M.2    DeVries, A.L.3
  • 142
    • 0023686487 scopus 로고
    • Wolffish antifreeze protein genes are primarily organized as tandem repeats that each contain two genes in inverted orientation
    • Scott G.K., Hayes P.H., Fletcher G.L., and Davies P.L. Wolffish antifreeze protein genes are primarily organized as tandem repeats that each contain two genes in inverted orientation. Mol. Cell. Biol. 8 (1988) 3670-3675
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3670-3675
    • Scott, G.K.1    Hayes, P.H.2    Fletcher, G.L.3    Davies, P.L.4
  • 143
    • 0016698744 scopus 로고
    • Carbohydrate of antifreeze glycoproteins from an Antarctic fish
    • Shier W.T., and DeVries A.L. Carbohydrate of antifreeze glycoproteins from an Antarctic fish. FEBS Lett. 54 (1975) 135
    • (1975) FEBS Lett. , vol.54 , pp. 135
    • Shier, W.T.1    DeVries, A.L.2
  • 144
    • 0015508290 scopus 로고
    • Structure and mode of action of glycoproteins from Antarctic fishes
    • Shier W.T., Lin Y., and DeVries A.L. Structure and mode of action of glycoproteins from Antarctic fishes. Biochim. Biophys. Acta 263 (1972) 406-413
    • (1972) Biochim. Biophys. Acta , vol.263 , pp. 406-413
    • Shier, W.T.1    Lin, Y.2    DeVries, A.L.3
  • 147
    • 0030589054 scopus 로고    scopus 로고
    • Refined solution structure of type III antifreeze protein: Hydrophobic groups may be involved in the energetics of the protein-ice interaction
    • Sonnichsen F.D., Deluca C.I., Davies P.L., and Sykes B.D. Refined solution structure of type III antifreeze protein: Hydrophobic groups may be involved in the energetics of the protein-ice interaction. Structure 4 (1996) 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
  • 148
    • 0034903041 scopus 로고    scopus 로고
    • Variations in antifreeze activity and serum inorganic ions in the eelpout Zoarces viviparus: Antifreeze activity in the embryonic state
    • Sørensen T.F., and Ramløv H. Variations in antifreeze activity and serum inorganic ions in the eelpout Zoarces viviparus: Antifreeze activity in the embryonic state. Comp. Biochem. Physiol. 130A (2001) 123-132
    • (2001) Comp. Biochem. Physiol. , vol.130 A , pp. 123-132
    • Sørensen, T.F.1    Ramløv, H.2
  • 149
    • 4243345054 scopus 로고    scopus 로고
    • Maternal-fetal relations in antifreeze production in the eelpout Zoarces viviparus
    • Sørensen T.F., and Ramløv H. Maternal-fetal relations in antifreeze production in the eelpout Zoarces viviparus. Cryo-Lett. 23 (2002) 183-190
    • (2002) Cryo-Lett. , vol.23 , pp. 183-190
    • Sørensen, T.F.1    Ramløv, H.2
  • 151
    • 0022295587 scopus 로고
    • Ocular freezing avoidance in antarctic fishes
    • Turner J.D., Schrag J.D., and DeVries A.L. Ocular freezing avoidance in antarctic fishes. J. Exp. Biol. 118 (1985) 121-132
    • (1985) J. Exp. Biol. , vol.118 , pp. 121-132
    • Turner, J.D.1    Schrag, J.D.2    DeVries, A.L.3
  • 152
    • 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. Survival of northern Atlantic cod (Gadus morhua) eggs and larvae when exposed to ice and low temperature. Can. J. Fish. Aquat. Sci. 49 (1992) 2588-2595
    • (1992) Can. J. Fish. Aquat. Sci. , vol.49 , pp. 2588-2595
    • Valerio, P.F.1    Goddard, S.V.2    Kao, M.H.3    Fletcher, G.L.4
  • 153
    • 0000459479 scopus 로고
    • Thermal hysteresis activity in the skin of the cunner, Tautogolabrus adspersus
    • Valerio P.F., Kao M.H., and Fletcher G.L. Thermal hysteresis activity in the skin of the cunner, Tautogolabrus adspersus. Can. J. Zool. 68 (1990)
    • (1990) Can. J. Zool. , vol.68
    • Valerio, P.F.1    Kao, M.H.2    Fletcher, G.L.3
  • 154
    • 0001274452 scopus 로고
    • Fish skin: An effective barrier to ice crystal propagation
    • Valerio P.F., Kao M.H., and Fletcher G.L. Fish skin: An effective barrier to ice crystal propagation. J. Exp. Biol. 164 (1992) 135-151
    • (1992) J. Exp. Biol. , vol.164 , pp. 135-151
    • Valerio, P.F.1    Kao, M.H.2    Fletcher, G.L.3
  • 155
    • 0000239233 scopus 로고
    • Glycoproteins as biological antifreeze agents in the cod Gadus ogac (Richardson)
    • Van Voorhies W.V., Raymond J.A., and DeVries A.L. Glycoproteins as biological antifreeze agents in the cod Gadus ogac (Richardson). Physiol. Zool. 51 (1978) 347-353
    • (1978) Physiol. Zool. , vol.51 , pp. 347-353
    • Van Voorhies, W.V.1    Raymond, J.A.2    DeVries, A.L.3
  • 156
    • 0029310565 scopus 로고
    • Genomic basis for antifreeze peptide heterogeneity and abundance in an Antarctic eel pout: Gene structures and organization
    • Wang X., DeVries A.L., and Cheng C.-H.C. Genomic basis for antifreeze peptide heterogeneity and abundance in an Antarctic eel pout: Gene structures and organization. Mol. Mar. Biol. Biotech. 4 (1995) 135-147
    • (1995) Mol. Mar. Biol. Biotech. , vol.4 , pp. 135-147
    • Wang, X.1    DeVries, A.L.2    Cheng, C.-H.C.3
  • 157
    • 0028908422 scopus 로고
    • Antifreeze peptide heterogeneity in an Antarctic eel pout includes an unusually large major variant comprised of two 7 kDa type III AFPs linked in tandem
    • Wang X., DeVries A.L., and Cheng C.-H.C. Antifreeze peptide heterogeneity in an Antarctic eel pout includes an unusually large major variant comprised of two 7 kDa type III AFPs linked in tandem. Biochim. Biophys. Acta 1247 (1995) 163-172
    • (1995) Biochim. Biophys. Acta , vol.1247 , pp. 163-172
    • Wang, X.1    DeVries, A.L.2    Cheng, C.-H.C.3
  • 159
    • 0027163901 scopus 로고
    • Ellipsometry determination of glycopeptide antifreeze adsorption to ice
    • Wilson P.W., Beaglehole D., and DeVries A.L. Ellipsometry determination of glycopeptide antifreeze adsorption to ice. Biophys. J. 64 (1993) 1878-1884
    • (1993) Biophys. J. , vol.64 , pp. 1878-1884
    • Wilson, P.W.1    Beaglehole, D.2    DeVries, A.L.3
  • 160
    • 0036628396 scopus 로고    scopus 로고
    • Hexagonal shaped spicules in frozen fish antifreeze solutions
    • Wilson P.W., Gould M., and DeVries A.L. Hexagonal shaped spicules in frozen fish antifreeze solutions. Cryobiology 44 (2002) 240-250
    • (2002) Cryobiology , vol.44 , pp. 240-250
    • Wilson, P.W.1    Gould, M.2    DeVries, A.L.3
  • 161
    • 0031968333 scopus 로고    scopus 로고
    • Identification of the ice-binding surface on a type III antifreeze protein with a "flatness function" algorithm
    • Yang D.S., Hon W., Bubanko S., Xue Y., Seetharaman J., Hew C.L., and Sicheri F. Identification of the ice-binding surface on a type III antifreeze protein with a "flatness function" algorithm. Biophys. J. 74 (1998) 2142-2151
    • (1998) Biophys. J. , vol.74 , pp. 2142-2151
    • Yang, D.S.1    Hon, W.2    Bubanko, S.3    Xue, Y.4    Seetharaman, J.5    Hew, C.L.6    Sicheri, F.7
  • 162
    • 0007789769 scopus 로고    scopus 로고
    • Diversity of Digenea, parasites of fishes in various areas of the Antarctic
    • di Prisco G., Pisano E., and Clarke A. (Eds), Springer-Verlag, Milano
    • Zdzitowiecki K. Diversity of Digenea, parasites of fishes in various areas of the Antarctic. In: di Prisco G., Pisano E., and Clarke A. (Eds). "Fishes of Antarctica, a Biological Overview" (1998), Springer-Verlag, Milano 87-94
    • (1998) "Fishes of Antarctica, a Biological Overview" , pp. 87-94
    • Zdzitowiecki, K.1
  • 163
    • 0032539653 scopus 로고    scopus 로고
    • Cloning and sequencing of cDNA encoding the LS-12 antifreeze protein in the longhorn sculpin, Myoxocephalus octodecimspinosis
    • Zhao Z., Deng G., Lui Q., and Laursen R.A. Cloning and sequencing of cDNA encoding the LS-12 antifreeze protein in the longhorn sculpin, Myoxocephalus octodecimspinosis. Biochim. Biophys. Acta 1382 (1998) 177-180
    • (1998) Biochim. Biophys. Acta , vol.1382 , pp. 177-180
    • Zhao, Z.1    Deng, G.2    Lui, Q.3    Laursen, R.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.