메뉴 건너뛰기




Volumn 278, Issue 19, 2011, Pages 3699-3710

Isolation and characterization of type i antifreeze proteins from cunner, Tautogolabrus adspersus, order Perciformes

Author keywords

amino acid sequence; cDNA sequence; convergent evolution; seasonal cycle; thermal hysteresis

Indexed keywords

ALANINE; ANTIFREEZE PROTEIN; COMPLEMENTARY DNA; MESSENGER RNA; THREONINE;

EID: 80052963229     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08288.x     Document Type: Article
Times cited : (20)

References (68)
  • 1
    • 0001350675 scopus 로고
    • Antifreeze proteins confer freezing resistance to fish
    • Fletcher GL, Kao MH, &, Fourney RM, (1986) Antifreeze proteins 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
  • 2
    • 56449100146 scopus 로고    scopus 로고
    • A re-evaluation of the role of type IV antifreeze protein
    • DOI 10.1016/j.cryobiol.2008.10.122, PII S0011224008002666
    • Gauthier SY, Scotter AJ, Lin FH, Baardsnes J, Fletcher GL, &, Davies PL, (2008) A re-evaluation of the role of type IV antifreeze protein. Cryobiology 57, 292-296. (Pubitemid 50324670)
    • (2008) Cryobiology , vol.57 , Issue.3 , pp. 292-296
    • Gauthier, S.Y.1    Scotter, A.J.2    Lin, F.-H.3    Baardsnes, J.4    Fletcher, G.L.5    Davies, P.L.6
  • 4
  • 5
    • 0033568338 scopus 로고    scopus 로고
    • Type I 'antifreeze' proteins. Structure-activity studies and mechanisms of ice growth inhibition
    • DOI 10.1046/j.1432-1327.1999.00617.x
    • Harding MM, Ward LG, &, Haymet AD, (1999) Type I 'antifreeze' proteins. Structure-activity studies and mechanisms of ice growth inhibition. Eur J Biochem 264, 653-665. (Pubitemid 29437194)
    • (1999) European Journal of Biochemistry , vol.264 , Issue.3 , pp. 653-665
    • Harding, M.M.1    Ward, L.G.2    Haymet, A.D.J.3
  • 6
    • 0032982510 scopus 로고    scopus 로고
    • Structure, function and evolution of antifreeze proteins
    • DOI 10.1007/s000180050289
    • Ewart KV, Lin Q, &, Hew CL, (1999) Structure, function and evolution of antifreeze proteins. Cell Mol Life Sci 55, 271-283. (Pubitemid 29118893)
    • (1999) Cellular and Molecular Life Sciences , vol.55 , Issue.2 , pp. 271-283
    • Ewart, K.V.1    Lin, Q.2    Hew, C.L.3
  • 8
    • 0000641685 scopus 로고
    • Freezing resistance in winter flounder, Pseudopleuronectes americanus
    • Duman JG, &, DeVries AL, (1974) Freezing resistance in winter flounder, Pseudopleuronectes americanus. Nature 247, 237-238.
    • (1974) Nature , vol.247 , pp. 237-238
    • Duman, J.G.1    Devries, A.L.2
  • 9
    • 0029013417 scopus 로고
    • Ice-binding structure and mechanism of an antifreeze protein from winter flounder
    • Sicheri F, &, Yang DS, (1995) Ice-binding structure and mechanism of an antifreeze protein from winter flounder. Nature 375, 427-431.
    • (1995) Nature , vol.375 , pp. 427-431
    • Sicheri, F.1    Yang, D.S.2
  • 10
    • 0035853750 scopus 로고    scopus 로고
    • Isolation and characterization of skin-type, type i antifreeze polypeptides from the longhorn sculpin, Myoxocephalus octodecemspinosus
    • Low WK, Lin Q, Stathakis C, Miao M, Fletcher GL, &, Hew CL, (2001) Isolation and characterization of skin-type, type I antifreeze polypeptides from the longhorn sculpin, Myoxocephalus octodecemspinosus. J Biol Chem 276, 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
  • 11
    • 0023642613 scopus 로고
    • Structural variations in the alanine-rich antifreeze proteins of the Pleuronectinae
    • Scott GK, Davies PL, Shears MA, &, Fletcher GL, (1987) Structural variations in the alanine-rich antifreeze proteins of the Pleuronectinae. Eur J Biochem 168, 629-633.
    • (1987) Eur J Biochem , vol.168 , pp. 629-633
    • Scott, G.K.1    Davies, P.L.2    Shears, M.A.3    Fletcher, G.L.4
  • 12
    • 0023688606 scopus 로고
    • Differential amplification of antifreeze protein genes in the Pleuronectinae
    • Scott GK, Davies PL, Kao MH, &, Fletcher GL, (1988) Differential amplification of antifreeze protein genes in the Pleuronectinae. J Mol Evol 27, 29-35.
    • (1988) J Mol Evol , vol.27 , pp. 29-35
    • Scott, G.K.1    Davies, P.L.2    Kao, M.H.3    Fletcher, G.L.4
  • 13
    • 0025959821 scopus 로고
    • Adsorption of alpha-helical antifreeze peptides on specific ice crystal surface planes
    • Knight CA, Cheng CC, &, DeVries AL, (1991) Adsorption of alpha-helical antifreeze peptides on specific ice crystal surface planes. Biophys J 59, 409-418.
    • (1991) Biophys J , vol.59 , pp. 409-418
    • Knight, C.A.1    Cheng, C.C.2    Devries, A.L.3
  • 14
    • 24644497249 scopus 로고    scopus 로고
    • Hyperactive antifreeze protein in flounder species: The sole freeze protectant in American plaice
    • DOI 10.1111/j.1742-4658.2005.04859.x
    • Gauthier SY, Marshall CB, Fletcher GL, &, Davies PL, (2005) Hyperactive antifreeze protein in flounder species. The sole freeze protectant in American plaice. FEBS J 272, 4439-4449. (Pubitemid 41284417)
    • (2005) FEBS Journal , vol.272 , Issue.17 , pp. 4439-4449
    • Gauthier, S.Y.1    Marshall, C.B.2    Fletcher, G.L.3    Davies, P.L.4
  • 17
    • 0001660887 scopus 로고
    • Primary structure of the alanine-rich antifreeze polypeptides from the grubby sculpin, Myoxocephalus aenaeus
    • Chakrabartty A, Hew C, Shears M, &, Fletcher G, (1988) Primary structure of the alanine-rich antifreeze polypeptides from the grubby sculpin, Myoxocephalus aenaeus. Can J Zool 66, 403-408.
    • (1988) Can J Zool , vol.66 , pp. 403-408
    • Chakrabartty, A.1    Hew, C.2    Shears, M.3    Fletcher, G.4
  • 18
    • 0024291721 scopus 로고
    • Crystal structure of an antifreeze polypeptide and its mechanistic implications
    • Yang DS, Sax M, Chakrabartty A, &, Hew CL, (1988) Crystal structure of an antifreeze polypeptide and its mechanistic implications. Nature 333, 232-237.
    • (1988) Nature , vol.333 , pp. 232-237
    • Yang, D.S.1    Sax, M.2    Chakrabartty, A.3    Hew, C.L.4
  • 19
    • 0035844710 scopus 로고    scopus 로고
    • Isolation and characterization of type I antifreeze proteins from Atlantic snailfish (Liparis atlanticus) and dusky snailfish (Liparis gibbus)
    • DOI 10.1016/S0167-4838(01)00190-X, PII S016748380100190X
    • Evans RP, &, Fletcher GL, (2001) Isolation and characterization of type I antifreeze proteins from Atlantic snailfish (Liparis atlanticus) and dusky snailfish (Liparis gibbus). Biochim Biophys Acta 1547, 235-244. (Pubitemid 32532141)
    • (2001) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1547 , Issue.2 , pp. 235-244
    • Evans, R.P.1    Fletcher, G.L.2
  • 21
    • 0000459479 scopus 로고
    • Thermal hysteresis activity in the skin of cunner, Tautogolabrus adspersus
    • Valerio PF, Kao MH, Fletcher GL, &, Hew CL, (1990) Thermal hysteresis activity in the skin of cunner, Tautogolabrus adspersus. Can J Zool 68, 1065-1067.
    • (1990) Can J Zool , vol.68 , pp. 1065-1067
    • Valerio, P.F.1    Kao, M.H.2    Fletcher, G.L.3    Hew, C.L.4
  • 22
    • 0001274452 scopus 로고
    • Fish skin: An effective barrier to ice crystal propagation
    • Valerio PF, Kao MH, &, Fletcher GL, (1992) Fish skin: an effective barrier to ice crystal propagation. J Exp Biol 164, 135-151.
    • (1992) J Exp Biol , vol.164 , pp. 135-151
    • Valerio, P.F.1    Kao, M.H.2    Fletcher, G.L.3
  • 23
    • 3242733074 scopus 로고    scopus 로고
    • Isolation and purification of antifreeze proteins from skin tissues of snailfish, cunner and sea raven
    • DOI 10.1016/j.bbapap.2004.05.006, PII S157096390400144X
    • Evans RP, &, Fletcher GL, (2004) Isolation and purification of antifreeze proteins from skin tissues of snailfish, cunner and sea raven. Biochim Biophys Acta 1700, 209-217. (Pubitemid 38950706)
    • (2004) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1700 , Issue.2 , pp. 209-217
    • Evans, R.P.1    Fletcher, G.L.2
  • 24
    • 0002416786 scopus 로고
    • Heterogeneity of antifreeze polypeptides from Newfoundland winter flounder, Pseudopleuronectes americanus
    • Fourney RM, Shashikant JB, Kao MH, &, Hew CL, (1983) Heterogeneity of antifreeze polypeptides from Newfoundland winter flounder, Pseudopleuronectes americanus. Can J Zool 62, 28-33.
    • (1983) Can J Zool , vol.62 , pp. 28-33
    • Fourney, R.M.1    Shashikant, J.B.2    Kao, M.H.3    Hew, C.L.4
  • 25
    • 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
    • DOI 10.1074/jbc.271.8.4106
    • Gong Z, Ewart KV, Hu Z, Fletcher GL, &, Hew CL, (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. (Pubitemid 26070507)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.8 , pp. 4106-4112
    • Gong, Z.1    Ewart, K.V.2    Hu, Z.3    Fletcher, G.L.4    Hew, C.L.5
  • 26
    • 0029929966 scopus 로고    scopus 로고
    • A natural variant of type I antifreeze protein with four ice-binding repeats is a particularly potent antifreeze
    • Chao H, Hodges RS, Kay CM, Gauthier SY, &, Davies PL, (1996) A natural variant of type I antifreeze protein with four ice-binding repeats is a particularly potent antifreeze. Protein Sci 5, 1150-1156. (Pubitemid 26172903)
    • (1996) Protein Science , vol.5 , Issue.6 , pp. 1150-1156
    • Chao, H.1    Hodges, R.S.2    Kay, C.M.3    Gauthier, S.Y.4    Davies, P.L.5
  • 27
    • 0031934222 scopus 로고    scopus 로고
    • Antifreeze proteins bind independently to ice
    • DeLuca CI, Comley R, &, Davies PL, (1998) Antifreeze proteins bind independently to ice. Biophys J 74, 1502-1508. (Pubitemid 28108558)
    • (1998) Biophysical Journal , vol.74 , Issue.3 , pp. 1502-1508
    • DeLuca, C.I.1    Comley, R.2    Davies, P.L.3
  • 28
    • 0036188648 scopus 로고    scopus 로고
    • Rational design of α-helical antifreeze peptides
    • DOI 10.1046/j.1397-002x.2001.00001.x
    • Kuiper MJ, Fecondo JV, &, Wong MG, (2002) Rational design of alpha-helical antifreeze peptides. J Pept Res 59, 1-8. (Pubitemid 34185255)
    • (2002) Journal of Peptide Research , vol.59 , Issue.1 , pp. 1-8
    • Kuiper, M.J.1    Fecondo, J.V.2    Wong, M.G.3
  • 29
    • 0032506091 scopus 로고    scopus 로고
    • Isolation and characterization of an antifreeze protein from the longhorn sculpin, Myoxocephalus octodecimspinosis
    • DOI 10.1016/S0167-4838(98)00180-0, PII S0167483898001800
    • Deng G, &, Laursen RA, (1998) Isolation and characterization of an antifreeze protein from the longhorn sculpin, Myoxocephalus octodecimspinosis. Biochim Biophys Acta 1388, 305-314. (Pubitemid 28526594)
    • (1998) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1388 , Issue.2 , pp. 305-314
    • Deng, G.1    Laursen, R.A.2
  • 30
    • 0037419824 scopus 로고    scopus 로고
    • Dual wavelength parametric test of two-state models for circular dichroism spectra of helical polypeptides: Anomalous dichroic properties of alanine-rich peptides
    • DOI 10.1021/ja0275360
    • Wallimann P, Kennedy RJ, Miller JS, Shalongo W, &, Kemp DS, (2003) Dual wavelength parametric test of two-state models for circular dichroism spectra of helical polypeptides: anomalous dichroic properties of alanine-rich peptides. J Am Chem Soc 125, 1203-1220. (Pubitemid 36159832)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.5 , pp. 1203-1220
    • Wallimann, P.1    Kennedy, R.J.2    Miller, J.S.3    Shalongo, W.4    Kemp, D.S.5
  • 32
    • 39649112169 scopus 로고    scopus 로고
    • Hyperactive antifreeze protein from fish contains multiple ice-binding sites
    • DOI 10.1021/bi7020316
    • Graham LA, Marshall CB, Lin FH, Campbell RL, &, Davies PL, (2008) Hyperactive antifreeze protein from fish contains multiple ice-binding sites. Biochemistry 47, 2051-2063. (Pubitemid 351287131)
    • (2008) Biochemistry , vol.47 , Issue.7 , pp. 2051-2063
    • Graham, L.A.1    Marshall, C.B.2    Lin, F.-H.3    Campbell, R.L.4    Davies, P.L.5
  • 34
    • 0033457363 scopus 로고    scopus 로고
    • New ice-binding face for type I antifreeze protein
    • DOI 10.1016/S0014-5793(99)01588-4, PII S0014579399015884
    • Baardsnes J, Kondejewski LH, Hodges RS, Chao H, Kay C, &, Davies PL, (1999) New ice-binding face for type I antifreeze protein. FEBS Lett 463, 87-91. (Pubitemid 30001724)
    • (1999) FEBS Letters , vol.463 , Issue.1-2 , pp. 87-91
    • Baardsnes, J.1    Kondejewski, L.H.2    Hodges, R.S.3    Chao, H.4    Kay, C.5    Davies, P.L.6
  • 35
    • 0023050471 scopus 로고
    • Biosynthesis of antifreeze polypeptides in the winter flounder. Characterization and seasonal occurrence of precursor polypeptides
    • Hew CL, Wang NC, Yan S, Cai H, Sclater A, &, Fletcher GL, (1986) Biosynthesis of antifreeze polypeptides in the winter flounder. Characterization and seasonal occurrence of precursor polypeptides. Eur J Biochem 160, 267-272.
    • (1986) Eur J Biochem , vol.160 , pp. 267-272
    • Hew, C.L.1    Wang, N.C.2    Yan, S.3    Cai, H.4    Sclater, A.5    Fletcher, G.L.6
  • 36
    • 77950609104 scopus 로고    scopus 로고
    • Structures and ice-binding faces of the alanine-rich type i antifreeze proteins
    • Patel SN, &, Graether SP, (2010) Structures and ice-binding faces of the alanine-rich type I antifreeze proteins. Biochem Cell Biol 88, 223-229.
    • (2010) Biochem Cell Biol , vol.88 , pp. 223-229
    • Patel, S.N.1    Graether, S.P.2
  • 37
    • 0034065261 scopus 로고    scopus 로고
    • Extracellular expression, purification, and characterization of a winter flounder antifreeze polypeptide from Escherichia coil
    • DOI 10.1006/prep.1999.1176
    • Tong L, Lin Q, Wong WK, Ali A, Lim D, Sung WL, Hew CL, &, Yang DS, (2000) Extracellular expression, purification, and characterization of a winter flounder antifreeze polypeptide from Escherichia coli. Protein Expr Purif 18, 175-181. (Pubitemid 30172223)
    • (2000) Protein Expression and Purification , vol.18 , Issue.2 , 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
  • 38
    • 71849116289 scopus 로고    scopus 로고
    • The peptide hormone pQDLDHVFLRFamide (crustacean myosuppressin) modulates the Homarus americanus cardiac neuromuscular system at multiple sites
    • Stevens JS, Cashman CR, Smith CM, Beale KM, Towle DW, Christie AE, &, Dickinson PS, (2009) The peptide hormone pQDLDHVFLRFamide (crustacean myosuppressin) modulates the Homarus americanus cardiac neuromuscular system at multiple sites. J Exp Biol 212, 3961-3976.
    • (2009) J Exp Biol , vol.212 , pp. 3961-3976
    • Stevens, J.S.1    Cashman, C.R.2    Smith, C.M.3    Beale, K.M.4    Towle, D.W.5    Christie, A.E.6    Dickinson, P.S.7
  • 40
    • 0023701419 scopus 로고
    • Prohormone processing and the secretory pathway
    • Fisher J, &, Scheller R, (1988) Prohormone processing and the secretory pathway. J Biol Chem 263, 16515-16518. (Pubitemid 18268825)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.32 , pp. 16515-16518
    • Fisher, J.M.1    Scheller, R.H.2
  • 42
    • 0034711184 scopus 로고    scopus 로고
    • N alpha-terminal acetylation of eukaryotic proteins
    • Polevoda B, &, Sherman F, (2000) N alpha-terminal acetylation of eukaryotic proteins. J Biol Chem 275, 36479-36482.
    • (2000) J Biol Chem , vol.275 , pp. 36479-36482
    • Polevoda, B.1    Sherman, F.2
  • 43
    • 0037025376 scopus 로고    scopus 로고
    • Type I shorthorn sculpin antifreeze protein: Recombinant synthesis, solution conformation, and ice growth inhibition studies
    • DOI 10.1074/jbc.M200307200
    • Fairley K, Westman BJ, Pham LH, Haymet AD, Harding MM, &, Mackay JP, (2002) Type I shorthorn sculpin antifreeze protein: recombinant synthesis, solution conformation, and ice growth inhibition studies. J Biol Chem 277, 24073-24080. (Pubitemid 34951920)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.27 , pp. 24073-24080
    • Fairley, K.1    Westman, B.J.2    Pham, L.H.3    Haymet, A.D.J.4    Harding, M.M.5    Mackay, J.P.6
  • 44
    • 0036185246 scopus 로고    scopus 로고
    • Localization of cells from the winter flounder gill expressing a skin type antifreeze protein gene
    • DOI 10.1139/z01-209
    • Murray HM, Hew CL, Kao KR, &, Fletcher GL, (2002) Localization of cells from winter flounder gill expressing a skin type antifreeze protein gene. Can J Zool 80, 110-119. (Pubitemid 34190571)
    • (2002) Canadian Journal of Zoology , vol.80 , Issue.1 , pp. 110-119
    • Murray, H.M.1    Hew, C.L.2    Kao, K.R.3    Fletcher, G.L.4
  • 45
    • 0036621962 scopus 로고    scopus 로고
    • Skin-type antifreeze protein expression in integumental cells of larval winter flounder
    • Murray HM, Hew CL, &, Fletcher GL, (2002) Skin-type antifreeze protein expression in integumental cells of larval winter flounder. J Fish Biol 60, 1391-1406.
    • (2002) J Fish Biol , vol.60 , pp. 1391-1406
    • Murray, H.M.1    Hew, C.L.2    Fletcher, G.L.3
  • 46
    • 0038084267 scopus 로고    scopus 로고
    • Spatial expression patterns of skin-type antifreeze protein in winter flounder (Pseudopleuronectes americanus) epidermis following metamorphosis
    • DOI 10.1002/jmor.10109
    • Murray HM, Hew CL, &, Fletcher GL, (2003) Spatial expression patterns of skin-type antifreeze protein in winter flounder (Pseudopleuronectes americanus) epidermis following metamorphosis. J Morphol 257, 78-86. (Pubitemid 36803587)
    • (2003) Journal of Morphology , vol.257 , Issue.1 , pp. 78-86
    • Murray, H.M.1    Hew, C.L.2    Fletcher, G.L.3
  • 47
    • 26244439851 scopus 로고    scopus 로고
    • Type I antifreeze proteins: Possible origins from chorion and keratin genes in Atlantic snailfish
    • DOI 10.1007/s00239-004-0067-y
    • Evans RP, &, Fletcher GL, (2005) Type I antifreeze proteins: possible origins from chorion and keratin genes in Atlantic snailfish. J Mol Evol 61, 417-424. (Pubitemid 41416886)
    • (2005) Journal of Molecular Evolution , vol.61 , Issue.4 , pp. 417-424
    • Evans, R.P.1    Fletcher, G.L.2
  • 48
    • 27144445310 scopus 로고    scopus 로고
    • Type I antifreeze proteins expressed in snailfish skin are identical to their plasma counterparts
    • DOI 10.1111/j.1742-4658.2005.04929.x
    • Evans RP, &, Fletcher GL, (2005) Type I antifreeze proteins expressed in snailfish skin are identical to their plasma counterparts. FEBS J 272, 5327-5336. (Pubitemid 41503161)
    • (2005) FEBS Journal , vol.272 , Issue.20 , pp. 5327-5336
    • Evans, R.P.1    Fletcher, G.L.2
  • 50
    • 24044495554 scopus 로고    scopus 로고
    • Hyperactive antifreeze protein from winter flounder is a very long rod-like dimer of α-helices
    • DOI 10.1074/jbc.M500622200
    • Marshall CB, Chakrabartty A, &, Davies PL, (2005) Hyperactive antifreeze protein from winter flounder is a very long rod-like dimer of alpha-helices. J Biol Chem 280, 17920-17929. (Pubitemid 41389033)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.18 , pp. 17920-17929
    • Marshall, C.B.1    Chakrabartty, A.2    Davies, P.L.3
  • 51
    • 0027220703 scopus 로고
    • Structure-function relationships in an antifreeze polypeptide. The role of charged amino acids
    • Wen D, &, Laursen RA, (1993) Structure-function relationships in an antifreeze polypeptide. The role of charged amino acids. J Biol Chem 268, 16396-16400. (Pubitemid 23229943)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.22 , pp. 16396-16400
    • Wen, D.1    Laursen, R.A.2
  • 52
    • 0017126510 scopus 로고
    • The synthesis of freezing-point-depressing protein of the winter flounder Pseudopleuronectus americanus in Xenopus laevis oocytes
    • Hew CL, &, Yip C, (1976) The synthesis of freezing-point-depressing protein of the winter flounder Pseudopleuronectus americanus in Xenopus laevis oocytes. Biochem Biophys Res Commun 71, 845-850.
    • (1976) Biochem Biophys Res Commun , vol.71 , pp. 845-850
    • Hew, C.L.1    Yip, C.2
  • 54
    • 0023682265 scopus 로고
    • Multiple genes provide the basis for antifreeze protein diversity and dosage in the ocean pout, Macrozoarces americanus
    • Hew CL, Wang NC, Joshi S, Fletcher GL, Scott GK, Hayes PH, Buettner B, &, Davies PL, (1988) Multiple genes provide the basis for antifreeze protein diversity and dosage in the ocean pout, Macrozoarces americanus. J Biol Chem 263, 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
  • 55
    • 0033082638 scopus 로고    scopus 로고
    • Increased gene dosage augments antifreeze protein levels in transgenic Drosophila melanogaster
    • DOI 10.1023/A:1008873906177
    • Duncker BP, Davies PL, &, Walker VK, (1999) Increased gene dosage augments antifreeze protein levels in transgenic Drosophila melanogaster. Transgenic Res 8, 45-50. (Pubitemid 29298286)
    • (1999) Transgenic Research , vol.8 , Issue.1 , pp. 45-50
    • Duncker, B.P.1    Davies, P.L.2    Walker, V.K.3
  • 56
    • 2442688072 scopus 로고    scopus 로고
    • Hyperactive antifreeze protein in a fish
    • DOI 10.1038/429153a
    • Marshall CB, Fletcher GL, &, Davies PL, (2004) Hyperactive antifreeze protein in a fish. Nature 429, 153. (Pubitemid 38656182)
    • (2004) Nature , vol.429 , Issue.6988 , pp. 153
    • Marshall, C.B.1    Fletcher, G.L.2    Davies, P.L.3
  • 57
    • 0019017081 scopus 로고
    • Antifreeze proteins from the shorthorn sculpin, Myoxocephalus scorpius: Isolation and characterization
    • Hew CL, Fletcher GL, &, Ananthanarayanan VS, (1980) Antifreeze proteins from the shorthorn sculpin, Myoxocephalus scorpius: isolation and characterization. Can J Biochem 58, 377-383.
    • (1980) Can J Biochem , vol.58 , pp. 377-383
    • Hew, C.L.1    Fletcher, G.L.2    Ananthanarayanan, V.S.3
  • 58
    • 4143134275 scopus 로고    scopus 로고
    • Freeze resistance in rainbow smelt (Osmerus mordax): Seasonal pattern of glycerol and antifreeze protein levels and liver enzyme activity associated with glycerol production
    • DOI 10.1086/383509
    • Lewis JM, Ewart KV, &, Driedzic WR, (2004) Freeze resistance in rainbow smelt (Osmerus mordax): seasonal pattern of glycerol and antifreeze protein levels and liver enzyme activity associated with glycerol production. Physiol Biochem Zool 77, 415-422. (Pubitemid 39098528)
    • (2004) Physiological and Biochemical Zoology , vol.77 , Issue.3 , pp. 415-422
    • Lewis, J.M.1    Ewart, K.V.2    Driedzic, W.R.3
  • 60
    • 0026499249 scopus 로고
    • Antifreeze production, freeze resistance and overwintering of juvenile northern Atlantic cod (Gadus morhua)
    • Goddard SV, Kao MH, &, Fletcher GL, (1992) Antifreeze production, freeze resistance and overwintering of juvenile northern Atlantic cod (Gadus morhua). Can J Fish Aquat Sci 49, 516-522.
    • (1992) Can J Fish Aquat Sci , vol.49 , pp. 516-522
    • Goddard, S.V.1    Kao, M.H.2    Fletcher, G.L.3
  • 61
    • 0001483179 scopus 로고
    • Winter habits of the cunner, Tautogolabrus adspersus (Walbaum) in Newfoundland
    • Green JM, &, Farwell ML, (1971) Winter habits of the cunner, Tautogolabrus adspersus (Walbaum) in Newfoundland. Can J Zool 49, 1497-1499.
    • (1971) Can J Zool , vol.49 , pp. 1497-1499
    • Green, J.M.1    Farwell, M.L.2
  • 62
    • 34447624465 scopus 로고    scopus 로고
    • Tissue-specific changes in protein synthesis associated with seasonal metabolic depression and recovery in the north temperate labrid, Tautogolabrus adspersus
    • DOI 10.1152/ajpregu.00594.2006
    • Lewis JM, &, Driedzic WR, (2007) Tissue-specific changes in protein synthesis associated with seasonal metabolic depression and recovery in the north temperate labrid, Tautogolabrus adspersus. Am J Physiol Regul Integr Comp Physiol 293, R474-R481. (Pubitemid 47092206)
    • (2007) American Journal of Physiology - Regulatory Integrative and Comparative Physiology , vol.293 , Issue.1
    • Lewis, J.M.1    Driedzic, W.R.2
  • 63
    • 0001831616 scopus 로고
    • A localized mass winter kill of cunners in Newfoundland
    • Green JM, (1974) A localized mass winter kill of cunners in Newfoundland. Can Field Nat 88, 96-97.
    • (1974) Can Field Nat , vol.88 , pp. 96-97
    • Green, J.M.1
  • 64
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • DOI 10.1016/0003-2697(87)90587-2
    • Schagger H, &, von Jagow G, (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166, 368-379. (Pubitemid 18004907)
    • (1987) Analytical Biochemistry , vol.166 , Issue.2 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 65
    • 0023511413 scopus 로고
    • Copper staining: A five-minute protein stain for sodium dodecyl sulfate-polyacrylamide gels
    • DOI 10.1016/0003-2697(87)90579-3
    • Lee C, Levin A, &, Branton D, (1987) Copper staining: a five-minute protein stain for sodium dodecyl sulfate-polyacrylamide gels. Anal Biochem 166, 308-312. (Pubitemid 18004904)
    • (1987) Analytical Biochemistry , vol.166 , Issue.2 , pp. 308-312
    • Lee, C.1    Levin, A.2    Branton, D.3
  • 68
    • 0016169865 scopus 로고
    • Determination of the helix and beta form of proteins in aqueous solution by circular dichroism
    • Chen YH, Yang JT, &, Chau KH, (1974) Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. Biochemistry 13, 3350-3359.
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.