메뉴 건너뛰기




Volumn 8, Issue 12, 2013, Pages

Helical antifreeze proteins have independently evolved in fishes on four occasions

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ANTIFREEZE PROTEIN;

EID: 84891906963     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0081285     Document Type: Article
Times cited : (44)

References (71)
  • 2
    • 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
  • 3
    • 0031771585 scopus 로고    scopus 로고
    • Evolution of the diverse antifreeze proteins
    • Cheng CH (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.1
  • 4
    • 0014666651 scopus 로고
    • Freezing resistance in some Antarctic fishes
    • DeVries AL, Wohlschlag DE (1969) Freezing resistance in some Antarctic fishes. Science 163: 1073-1075.
    • (1969) Science , vol.163 , pp. 1073-1075
    • Devries, A.L.1    Wohlschlag, D.E.2
  • 5
    • 0000641685 scopus 로고
    • Freezing resistance in winter flounder
    • Duman JG, DeVries AL (1974) Freezing resistance in winter flounder. Nature 274: 237-238.
    • (1974) Nature , vol.274 , pp. 237-238
    • Duman, J.G.1    Devries, A.L.2
  • 6
    • 0017118163 scopus 로고
    • Isolation, characterization, and physical properties of protein antifreezes from the winter flounder, Pseudopleuronectes americanus
    • Duman JG, de Vries AL (1976) Isolation, characterization, and physical properties of protein antifreezes from the winter flounder, Pseudopleuronectes americanus. Comp Biochem Physiol B 54: 375-380.
    • (1976) Comp Biochem Physiol B , vol.54 , pp. 375-380
    • Duman, J.G.1    De Vries, A.L.2
  • 7
    • 0019524267 scopus 로고
    • Antifreeze proteins from the sea raven, Hemitripterus americanus. Further evidence for diversity among fish polypeptide antifreezes
    • Slaughter D, Fletcher GL, Ananthanarayanan VS, Hew CL (1981) Antifreeze proteins from the sea raven, Hemitripterus americanus. Further evidence for diversity among fish polypeptide antifreezes. J Biol Chem 256: 2022-2026. (Pubitemid 11106712)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.4 , pp. 2022-2026
    • Slaughter, D.1    Fletcher, G.L.2    Ananthanarayanan, V.S.3    Hew, C.L.4
  • 9
    • 0022371514 scopus 로고
    • Structure of an antifreeze polypeptide and its precursor from the ocean pout, Macrozoarces americanus
    • Li XM, Trinh KY, Hew CL, Buettner B, Baenziger J, et al. (1985) Structure of an antifreeze polypeptide and its precursor from the ocean pout, Macrozoarces americanus. J Biol Chem 260: 12904-12909. (Pubitemid 16209749)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.24 , pp. 12904-12909
    • Li, X.-M.1    Trinh, K.-Y.2    Hew, C.L.3
  • 11
    • 84864107809 scopus 로고    scopus 로고
    • Widespread recurrent evolution of genomic features
    • Maeso I, Roy SW, Irimia M (2012) Widespread recurrent evolution of genomic features. Genome Biol Evol 4: 486-500.
    • (2012) Genome Biol Evol , vol.4 , pp. 486-500
    • Maeso, I.1    Roy, S.W.2    Irimia, M.3
  • 12
    • 17844367344 scopus 로고    scopus 로고
    • Hybridization as an invasion of the genome
    • DOI 10.1016/j.tree.2005.02.010, Invasions
    • Mallet J (2005) Hybridization as an invasion of the genome. Trends Ecol Evol 20: 229-237. (Pubitemid 40588907)
    • (2005) Trends in Ecology and Evolution , vol.20 , Issue.5 , pp. 229-237
    • Mallet, J.1
  • 13
    • 0027983037 scopus 로고
    • Convergent evolution: The need to be explicit
    • DOI 10.1016/0968-0004(94)90167-8
    • Doolittle RF (1994) Convergent evolution: the need to be explicit. Trends Biochem Sci 19: 15-18. (Pubitemid 24028725)
    • (1994) Trends in Biochemical Sciences , vol.19 , Issue.1 , pp. 15-18
    • Doolittle, R.F.1
  • 14
    • 79959981709 scopus 로고    scopus 로고
    • Convergence, adaptation, and constraint
    • Losos JB (2011) Convergence, adaptation, and constraint. Evolution 65: 1827-1840.
    • (2011) Evolution , vol.65 , pp. 1827-1840
    • Losos, J.B.1
  • 15
    • 21144441817 scopus 로고    scopus 로고
    • Lateral gene transfer in eukaryotes
    • Andersson JO (2005) Lateral gene transfer in eukaryotes. Cell Mol Life Sci 62: 1-16.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1-16
    • Andersson, J.O.1
  • 16
    • 0035425519 scopus 로고    scopus 로고
    • Sialic acid synthase: The origin of fish type III antifreeze protein?
    • DOI 10.1016/S0968-0004(01)01879-5, PII S0968000401018795
    • Baardsnes J, Davies PL (2001) Sialic acid synthase: the origin of fish type III antifreeze protein? Trends Biochem Sci 26: 468-469. (Pubitemid 32735443)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.8 , pp. 468-469
    • Baardsnes, J.1    Davies, P.L.2
  • 17
    • 78650751202 scopus 로고    scopus 로고
    • Evolution of an antifreeze protein by neofunctionalization under escape from adaptive conflict
    • Deng C, Cheng CH, Ye H, He X, Chen L (2010) Evolution of an antifreeze protein by neofunctionalization under escape from adaptive conflict. Proc Natl Acad Sci U S A.
    • (2010) Proc Natl Acad Sci U S A
    • Deng, C.1    Cheng, C.H.2    Ye, H.3    He, X.4    Chen, L.5
  • 18
    • 0242274599 scopus 로고    scopus 로고
    • Functional Antifreeze Glycoprotein Genes in Temperate-Water New Zealand Nototheniid Fish Infer an Antarctic Evolutionary Origin
    • DOI 10.1093/molbev/msg208
    • Cheng CH, Chen L, Near TJ, Jin Y (2003) Functional antifreeze glycoprotein genes in temperate-water New Zealand nototheniid fish infer an Antarctic evolutionary origin. Mol Biol Evol 20: 1897-1908. (Pubitemid 37420943)
    • (2003) Molecular Biology and Evolution , vol.20 , Issue.11 , pp. 1897-1908
    • Cheng, C.-H.C.1    Chen, L.2    Near, T.J.3    Jin, Y.4
  • 21
    • 38849181532 scopus 로고    scopus 로고
    • Structure and evolutionary origin of Ca2+-dependent herring type II antifreeze protein
    • Liu Y, Li Z, Lin Q, Kosinski J, Seetharaman J, et al. (2007) Structure and evolutionary origin of Ca2+-dependent herring type II antifreeze protein. PLoS ONE 2: e548.
    • (2007) PLoS ONE , vol.2
    • Liu, Y.1    Li, Z.2    Lin, Q.3    Kosinski, J.4    Seetharaman, J.5
  • 22
    • 49949083546 scopus 로고    scopus 로고
    • Lateral transfer of a lectin-like antifreeze protein gene in fishes
    • Graham LA, Lougheed SC, Ewart KV, Davies PL (2008) Lateral transfer of a lectin-like antifreeze protein gene in fishes. PLoS ONE 3: e2616.
    • (2008) PLoS ONE , vol.3
    • Graham, L.A.1    Lougheed, S.C.2    Ewart, K.V.3    Davies, P.L.4
  • 24
    • 0023010888 scopus 로고
    • Structure of an antifreeze polypeptide precursor from the sea raven, Hemitripterus americanus
    • Ng NF, Trinh KY, Hew CL (1986) Structure of an antifreeze polypeptide precursor from the sea raven, Hemitripterus americanus. J Biol Chem 261: 15690-15695. (Pubitemid 17208805)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.33 , pp. 15690-15695
    • Ng, N.F.1    Trinh, K.-Y.2    Hew, C.L.3
  • 25
    • 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, et al. (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
  • 28
    • 38649099075 scopus 로고    scopus 로고
    • Glacio-epochs and the supercontinent cycle after ,3.0 Ga: Tectonic boundary conditions for glaciation
    • Eyles N (2008) Glacio-epochs and the supercontinent cycle after ,3.0 Ga: Tectonic boundary conditions for glaciation. Palaeogeography Palaeoclimatology Palaeoecology 258: 89-129.
    • (2008) Palaeogeography Palaeoclimatology Palaeoecology , vol.258 , pp. 89-129
    • Eyles, N.1
  • 30
    • 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
  • 31
    • 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
  • 32
    • 80052963229 scopus 로고    scopus 로고
    • Isolation and characterization of type i antifreeze proteins from cunner, Tautogolabrus adspersus, order Perciformes
    • Hobbs RS, Shears MA, Graham LA, Davies PL, Fletcher GL (2011) Isolation and characterization of type I antifreeze proteins from cunner, Tautogolabrus adspersus, order Perciformes. FEBS J 278: 3699-3710.
    • (2011) FEBS J , vol.278 , pp. 3699-3710
    • Hobbs, R.S.1    Shears, M.A.2    Graham, L.A.3    Davies, P.L.4    Fletcher, G.L.5
  • 33
    • 0021682997 scopus 로고
    • Winter flounder antifreeze proteins: A multigene family
    • Gourlie B, Lin Y, Price J, DeVries AL, Powers D, et al. (1984) Winter flounder antifreeze proteins: a multigene family. J Biol Chem 259: 14960-14965. (Pubitemid 15222232)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.23 , pp. 14960-14965
    • Gourlie, B.1    Lin, Y.2    Price, J.3
  • 34
    • 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
  • 35
    • 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
  • 36
    • 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
  • 37
    • 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
  • 39
    • 0032483453 scopus 로고    scopus 로고
    • Skin-type antifreeze protein from the shorthorn sculpin, Myoxocephalus scorpius: Expression and characterization of a M(r) 9,700 recombinant protein
    • DOI 10.1074/jbc.273.36.23098
    • Low WK, Miao M, Ewart KV, Yang DS, Fletcher GL, et al. (1998) Skin-type antifreeze protein from the shorthorn sculpin, Myoxocephalus scorpius. Expression and characterization of a Mr 9, 700 recombinant protein. J Biol Chem 273: 23098-23103. (Pubitemid 28417491)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.36 , pp. 23098-23103
    • Low, W.-K.1    Miao, M.2    Vanya Ewart, K.3    Yang, D.S.C.4    Fletcher, G.L.5    Hew, C.L.6
  • 40
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: The european molecular biology open software suite
    • Rice P, Longden I, Bleasby A (2000) EMBOSS: the European Molecular Biology Open Software Suite. Trends Genet 16: 276-277.
    • (2000) Trends Genet , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 41
    • 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, et al. (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
  • 42
    • 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
  • 44
    • 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
  • 45
    • 79955156793 scopus 로고    scopus 로고
    • On the origin and trigger of the notothenioid adaptive radiation
    • Matschiner M, Hanel R, Salzburger W (2011) On the origin and trigger of the notothenioid adaptive radiation. PLoS One 6: e18911.
    • (2011) PLoS One , vol.6
    • Matschiner, M.1    Hanel, R.2    Salzburger, W.3
  • 46
    • 33644853817 scopus 로고    scopus 로고
    • Mitochondrial molecular clocks and the origin of the major Otocephalan clades (Pisces: Teleostei): A new insight
    • DOI 10.1016/j.gene.2005.11.024, PII S0378111905007304
    • Peng Z, He S, Wang J, Wang W, Diogo R (2006) Mitochondrial molecular clocks and the origin of the major Otocephalan clades (Pisces: Teleostei): A new insight. Gene 370: 113-124. (Pubitemid 43375907)
    • (2006) Gene , vol.370 , Issue.1-2 , pp. 113-124
    • Peng, Z.1    He, S.2    Wang, J.3    Wang, W.4    Diogo, R.5
  • 47
    • 33646878378 scopus 로고    scopus 로고
    • Novel relationships among ten fish model species revealed based on a phylogenomic analysis using ESTs
    • DOI 10.1007/s00239-005-0170-8
    • Steinke D, Salzburger W, Meyer A (2006) Novel relationships among ten fish model species revealed based on a phylogenomic analysis using ESTs. J Mol Evol 62: 772-784. (Pubitemid 43847227)
    • (2006) Journal of Molecular Evolution , vol.62 , Issue.6 , pp. 772-784
    • Steinke, D.1    Salzburger, W.2    Meyer, A.3
  • 48
    • 84866564577 scopus 로고    scopus 로고
    • Smelt was the likely beneficiary of an antifreeze gene laterally transferred between fishes
    • Graham LA, Li J, Davidson WS, Davies PL (2012) Smelt was the likely beneficiary of an antifreeze gene laterally transferred between fishes. BMC Evol Biol 12: 190.
    • (2012) BMC Evol Biol , vol.12 , pp. 190
    • Graham, L.A.1    Li, J.2    Davidson, W.S.3    Davies, P.L.4
  • 49
    • 84866749278 scopus 로고    scopus 로고
    • Evolution of type II antifreeze protein genes in teleost fish: A complex scenario involving lateral gene transfers and episodic directional selection
    • Sorhannus U (2012) Evolution of Type II Antifreeze Protein Genes in Teleost Fish: A Complex Scenario Involving Lateral Gene Transfers and Episodic Directional Selection. Evol Bioinform Online 8: 535-544.
    • (2012) Evol Bioinform Online , vol.8 , pp. 535-544
    • Sorhannus, U.1
  • 50
    • 0028814457 scopus 로고
    • The antifreeze protein genes of the winter flounder, Pleuronectus americanus, are differentially regulated in liver and non-liver tissues
    • Gong Z, King MJ, Fletcher GL, Hew CL (1995) The antifreeze protein genes of the winter flounder, Pleuronectus americanus, are differentially regulated in liver and non-liver tissues. Biochem Biophys Res Commun 206: 387-392.
    • (1995) Biochem Biophys Res Commun , vol.206 , pp. 387-392
    • Gong, Z.1    King, M.J.2    Fletcher, G.L.3    Hew, C.L.4
  • 52
    • 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
  • 53
    • 0031808074 scopus 로고    scopus 로고
    • A helix propensity scale based on experimental studies of peptides and proteins
    • Pace CN, Scholtz JM (1998) A helix propensity scale based on experimental studies of peptides and proteins. Biophys J 75: 422-427. (Pubitemid 28311831)
    • (1998) Biophysical Journal , vol.75 , Issue.1 , pp. 422-427
    • Pace, C.N.1    Scholtz, J.M.2
  • 54
    • 0024962169 scopus 로고
    • Structure-function relationships in a winter flounder antifreeze polypeptide. I. Stabilization of an alpha-helical antifreeze polypeptide by charged-group and hydrophobic interactions
    • Chakrabartty A, Ananthanarayanan VS, Hew CL (1989) Structure-function relationships in a winter flounder antifreeze polypeptide. I. Stabilization of an alpha-helical antifreeze polypeptide by charged-group and hydrophobic interactions. J Biol Chem 264: 11307-11312.
    • (1989) J Biol Chem , vol.264 , pp. 11307-11312
    • Chakrabartty, A.1    Ananthanarayanan, V.S.2    Hew, C.L.3
  • 55
    • 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
  • 56
    • 0034691568 scopus 로고    scopus 로고
    • Mimicry of ice structure by surface hydroxyls and water of a β-helix antifreeze protein
    • DOI 10.1038/35018604
    • Liou YC, Tocilj A, Davies PL, Jia Z (2000) Mimicry of ice structure by surface hydroxyls and water of a beta-helix antifreeze protein. Nature 406: 322-324. (Pubitemid 30604412)
    • (2000) Nature , vol.406 , Issue.6793 , pp. 322-324
    • Liou, Y.-C.1    Tocilj, A.2    Davies, P.L.3    Jia, Z.4
  • 57
    • 0034691594 scopus 로고    scopus 로고
    • β-Helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect
    • DOI 10.1038/35018610
    • Graether SP, Kuiper MJ, Gagne SM, Walker VK, Jia Z, et al. (2000) Beta-helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect. Nature 406: 325-328. (Pubitemid 30604413)
    • (2000) Nature , vol.406 , Issue.6793 , pp. 325-328
    • Graethert, S.P.1    Kulper, M.J.2    Gagne, S.M.3    Walker, V.K.4    Jia, Z.5    Sykes, B.D.6    Davies, P.L.7
  • 58
    • 0036093824 scopus 로고    scopus 로고
    • Crystal structure of β-Helical antifreeze protein points to a general ice binding model
    • DOI 10.1016/S0969-2126(02)00745-1, PII S0969212602007451
    • Leinala EK, Davies PL, Jia Z (2002) Crystal structure of beta-helical antifreeze protein points to a general ice binding model. Structure (Camb) 10: 619-627. (Pubitemid 34520466)
    • (2002) Structure , vol.10 , Issue.5 , pp. 619-627
    • Leinala, E.K.1    Davies, P.L.2    Jia, Z.3
  • 60
    • 84857528147 scopus 로고    scopus 로고
    • Antifreeze protein from freeze-tolerant grass has a beta-roll fold with an irregularly structured ice-binding site
    • Middleton AJ, Marshall CB, Faucher F, Bar-Dolev M, Braslavsky I, et al. (2012) Antifreeze protein from freeze-tolerant grass has a beta-roll fold with an irregularly structured ice-binding site. J Mol Biol 416: 713-724.
    • (2012) J Mol Biol , vol.416 , pp. 713-724
    • Middleton, A.J.1    Marshall, C.B.2    Faucher, F.3    Bar-Dolev, M.4    Braslavsky, I.5
  • 61
    • 84862182041 scopus 로고    scopus 로고
    • Icebinding site of snow mold fungus antifreeze protein deviates from structural regularity and high conservation
    • Kondo H, Hanada Y, Sugimoto H, Hoshino T, Garnham CP, et al. (2012) Icebinding site of snow mold fungus antifreeze protein deviates from structural regularity and high conservation. Proc Natl Acad Sci U S A 109: 9360-9365.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 9360-9365
    • Kondo, H.1    Hanada, Y.2    Sugimoto, H.3    Hoshino, T.4    Garnham, C.P.5
  • 63
    • 48249101260 scopus 로고    scopus 로고
    • X-ray structure of snow flea antifreeze protein determined by racemic crystallization of synthetic protein enantiomers
    • Pentelute BL, Gates ZP, Tereshko V, Dashnau JL, Vanderkooi JM, et al. (2008) X-ray structure of snow flea antifreeze protein determined by racemic crystallization of synthetic protein enantiomers. J Am Chem Soc 130: 9695-9701.
    • (2008) J Am Chem Soc , vol.130 , pp. 9695-9701
    • Pentelute, B.L.1    Gates, Z.P.2    Tereshko, V.3    Dashnau, J.L.4    Vanderkooi, J.M.5
  • 64
    • 77949606411 scopus 로고    scopus 로고
    • Structural basis for the superior activity of the large isoform of snow flea antifreeze protein
    • Mok YF, Lin FH, Graham LA, Celik Y, Braslavsky I, et al. (2010) Structural basis for the superior activity of the large isoform of snow flea antifreeze protein. Biochemistry 49: 2593-2603.
    • (2010) Biochemistry , vol.49 , pp. 2593-2603
    • Mok, Y.F.1    Lin, F.H.2    Graham, L.A.3    Celik, Y.4    Braslavsky, I.5
  • 65
    • 39749196163 scopus 로고    scopus 로고
    • Investigation of loss and gain of introns in the compact genomes of pufferfishes (Fugu and Tetraodon)
    • DOI 10.1093/molbev/msm278
    • Loh YH, Brenner S, Venkatesh B (2008) Investigation of loss and gain of introns in the compact genomes of pufferfishes (Fugu and Tetraodon). Mol Biol Evol 25: 526-535. (Pubitemid 351301907)
    • (2008) Molecular Biology and Evolution , vol.25 , Issue.3 , pp. 526-535
    • Loh, Y.-H.1    Brenner, S.2    Venkatesh, B.3
  • 66
    • 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
  • 68
    • 33847030645 scopus 로고    scopus 로고
    • Independent evolution of the specialized pharyngeal jaw apparatus in cichlid and labrid fishes
    • Mabuchi K, Miya M, Azuma Y, Nishida M (2007) Independent evolution of the specialized pharyngeal jaw apparatus in cichlid and labrid fishes. BMC Evol Biol 7: 10.
    • (2007) BMC Evol Biol , vol.7 , pp. 10
    • Mabuchi, K.1    Miya, M.2    Azuma, Y.3    Nishida, M.4
  • 69
    • 34248641399 scopus 로고    scopus 로고
    • Phylogenetic relationships among anchovies, sardines, herrings and their relatives (Clupeiformes), inferred from whole mitogenome sequences
    • DOI 10.1016/j.ympev.2006.09.018, PII S1055790306003770
    • Lavoue S, Miya M, Saitoh K, Ishiguro NB, Nishida M (2007) Phylogenetic relationships among anchovies, sardines, herrings and their relatives (Clupeiformes), inferred from whole mitogenome sequences. Mol Phylogenet Evol 43: 1096-1105. (Pubitemid 46777380)
    • (2007) Molecular Phylogenetics and Evolution , vol.43 , Issue.3 , pp. 1096-1105
    • Lavoue, S.1    Miya, M.2    Saitoh, K.3    Ishiguro, N.B.4    Nishida, M.5
  • 70
    • 0023461350 scopus 로고
    • Helix stabilization by Glu-.Lys+ salt bridges in short peptides of de novo design
    • Marqusee S, Baldwin RL (1987) Helix stabilization by Glu-.Lys+ salt bridges in short peptides of de novo design. Proc Natl Acad Sci U S A 84: 8898-8902.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 8898-8902
    • Marqusee, S.1    Baldwin, R.L.2
  • 71
    • 84870193123 scopus 로고    scopus 로고
    • Epithelial dominant expression of antifreeze proteins in cunner suggests recent entry into a high freeze-risk ecozone
    • Hobbs RS, Fletcher GL (2013) Epithelial dominant expression of antifreeze proteins in cunner suggests recent entry into a high freeze-risk ecozone. Comp Biochem Physiol A Mol Integr Physiol 164: 111-118.
    • (2013) Comp Biochem Physiol A Mol Integr Physiol , vol.164 , pp. 111-118
    • Hobbs, R.S.1    Fletcher, G.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.