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1
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0015219684
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Glycoproteins as biological antifreeze agents in Antarctic fishes
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DeVries AL. Glycoproteins as biological antifreeze agents in Antarctic fishes. Science. 172:1971;1152-1155.
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Science
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Devries, A.L.1
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2
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0031026370
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Amino acid sequence of a new type of antifreeze protein, from the longhorn sculpin Myoxocephalus octodecimspinosis
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of outstanding interest. The authors report the discovery of a new type of fish AFP (type IV). It shares sequence similarity with members of the exchangeable apolioproteins super-family and is unrelated to the type I AFP in the sister species - short-horn and grubby sculpins.
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Deng G, Andrews DW, Laursen RA. Amino acid sequence of a new type of antifreeze protein, from the longhorn sculpin Myoxocephalus octodecimspinosis. of outstanding interest FEBS Lett. 402:1997;17-20 The authors report the discovery of a new type of fish AFP (type IV). It shares sequence similarity with members of the exchangeable apolioproteins super-family and is unrelated to the type I AFP in the sister species - short-horn and grubby sculpins.
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(1997)
FEBS Lett
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Deng, G.1
Andrews, D.W.2
Laursen, R.A.3
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3
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0002037107
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The role of antifreeze glycopeptides and peptides in the freezing avoidance of cold-water fish
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di Prisco G. Berlin-Heidelberg: Springer-Verlag
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Cheng CC, DeVries AL. The role of antifreeze glycopeptides and peptides in the freezing avoidance of cold-water fish. di Prisco G. Life Under Extreme Conditions. 1991;1-14 Springer-Verlag, Berlin-Heidelberg.
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Life under Extreme Conditions
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Cheng, C.C.1
Devries, A.L.2
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5
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0000286513
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Comparison of antifreeze glycopeptides from Arctic and Antarctic fishes
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O'Grady SM, Schrag JD, Raymond JA, DeVries AL. Comparison of antifreeze glycopeptides from Arctic and Antarctic fishes. J Exp Zool. 224:1982;177-185.
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J Exp Zool
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O'Grady, S.M.1
Schrag, J.D.2
Raymond, J.A.3
Devries, A.L.4
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6
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0030970280
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Evolution of antifreeze glycoprotein from a trypsinogen gene in Antarctic notothenioid fish
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of outstanding interest. The origin of the notothenioid AFGP gene is determined. Sequence analyses show that the protease to AFGP conversion involved recruitment of the two ends of the protease gene and expansion of a 9 nt sequence in the middle to provide the new AFGP coding region.
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Chen L, DeVries AL, Cheng CHC. Evolution of antifreeze glycoprotein from a trypsinogen gene in Antarctic notothenioid fish. of outstanding interest Proc Natl Acad Sci USA. 94:1997;3811-3816 The origin of the notothenioid AFGP gene is determined. Sequence analyses show that the protease to AFGP conversion involved recruitment of the two ends of the protease gene and expansion of a 9 nt sequence in the middle to provide the new AFGP coding region.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 3811-3816
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Chen, L.1
Devries, A.L.2
Cheng, C.H.C.3
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7
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0030890706
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Convergent evolution of antifreeze glycoproteins in Antarctic notothenioid fish and Arctic cod
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of outstanding interest. Comparative sequence analyses are presented that strongly support a rare case of protein sequence convergence for the near-identical AFGPs in these two unrelated fishes inhabiting opposite poles of the Earth.
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Chen L, DeVries AL, Cheng CHC. Convergent evolution of antifreeze glycoproteins in Antarctic notothenioid fish and Arctic cod. of outstanding interest Proc Natl Acad Sci USA. 94:1997;3817-3822 Comparative sequence analyses are presented that strongly support a rare case of protein sequence convergence for the near-identical AFGPs in these two unrelated fishes inhabiting opposite poles of the Earth.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 3817-3822
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Chen, L.1
Devries, A.L.2
Cheng, C.H.C.3
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8
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0027551726
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Herring antifreeze protein: Primary structure and evidence for a C-type lectin evolutionary origin
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Ewart KV, Fletcher GL. Herring antifreeze protein: primary structure and evidence for a C-type lectin evolutionary origin. Mol Mar Biol Biotech. 2:1993;20-27.
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Mol Mar Biol Biotech
, vol.2
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Ewart, K.V.1
Fletcher, G.L.2
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9
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0030760436
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Hyperactive antifreeze protein from beetles
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of special interest. First of three complete insect AFP sequences that were reported within months of each other. This Cys-rich repetitive mealworm AFP represents yet another new type in the antifreeze superfamily and is much more active than fish AFPS.
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Graham LA, Liou LC, Walker VK, Davies PL. Hyperactive antifreeze protein from beetles. of special interest Nature. 388:1997;727-728 First of three complete insect AFP sequences that were reported within months of each other. This Cys-rich repetitive mealworm AFP represents yet another new type in the antifreeze superfamily and is much more active than fish AFPS.
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(1997)
Nature
, vol.388
, pp. 727-728
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Graham, L.A.1
Liou, L.C.2
Walker, V.K.3
Davies, P.L.4
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10
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0032054774
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Molecular characterization and sequencing of antifreeze proteins from larvae of the beetle Dendroides canadensis
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of special interest. This beetle larvae AFP shares high sequence identity with the mealworm AFP, and has the same repetitive structure, and thus belongs to the same type.
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Duman JG, Li N, Verleye D, Goetz FW, Wu DW, Andorfer CA, Benjamin T, Parmelee DC. Molecular characterization and sequencing of antifreeze proteins from larvae of the beetle Dendroides canadensis. of special interest J Comp Physiol B. 168:1998;225-232 This beetle larvae AFP shares high sequence identity with the mealworm AFP, and has the same repetitive structure, and thus belongs to the same type.
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(1998)
J Comp Physiol B
, vol.168
, pp. 225-232
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Duman, J.G.1
Li, N.2
Verleye, D.3
Goetz, F.W.4
Wu, D.W.5
Andorfer, C.A.6
Benjamin, T.7
Parmelee, D.C.8
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11
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0030828487
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The antifreeze potential of the spruce budworm thermal hysteresis protein
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of special interest. This paper reports an AFP from a moth larva which, thought similar in amino acid bias as the beetle larvae AFPs, does not have a repeat sequence and thus may not be homologus to the latter.
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Tyshenko MG, Doucet D, Davies PL, Walker VK. The antifreeze potential of the spruce budworm thermal hysteresis protein. of special interest Nat Biotechnol. 15:1997;887-890 This paper reports an AFP from a moth larva which, thought similar in amino acid bias as the beetle larvae AFPs, does not have a repeat sequence and thus may not be homologus to the latter.
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(1997)
Nat Biotechnol
, vol.15
, pp. 887-890
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Tyshenko, M.G.1
Doucet, D.2
Davies, P.L.3
Walker, V.K.4
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12
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0028232701
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Purification and characterization of a thermal hysteresis protein from a plant, the bittersweet nightshade Solanum dulacamara
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Duman JG. Purification and characterization of a thermal hysteresis protein from a plant, the bittersweet nightshade Solanum dulacamara. Biochim Biophys Acta. 1206:1994;129-135.
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Biochim Biophys Acta
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Duman, J.G.1
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13
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0029411516
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Antifreeze proteins in winter rye are similar to pathogenesis-related proteins
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Hon WC, Griffith M, Mlynarz A, Kwok YC, Yang DS. Antifreeze proteins in winter rye are similar to pathogenesis-related proteins. Plant Physiol. 109:1995;879-889.
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Plant Physiol
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Hon, W.C.1
Griffith, M.2
Mlynarz, A.3
Kwok, Y.C.4
Yang, D.S.5
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14
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0042183228
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Adsorption inhibition as a mechanism of freezing resistance in polar fishes
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Raymond JA, DeVries AL. Adsorption inhibition as a mechanism of freezing resistance in polar fishes. Proc Natl Acad Sci USA. 74:1977;2589-2593.
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Proc Natl Acad Sci USA
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Raymond, J.A.1
Devries, A.L.2
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15
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0025959821
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Adsorption of α-helical antifreeze peptides on specific ice crystal surface planes
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Knight CA, Cheng CC, DeVries AL. Adsorption of α-helical antifreeze peptides on specific ice crystal surface planes. Biophys J. 59:1991;409-418.
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(1991)
Biophys J
, vol.59
, pp. 409-418
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Knight, C.A.1
Cheng, C.C.2
Devries, A.L.3
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16
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0028761625
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Effects of a polymeric, non-equilibrium 'antifreeze' upon ice growth from water
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Knight CA, DeVries AL. Effects of a polymeric, non-equilibrium 'antifreeze' upon ice growth from water. J Crystal Growth. 143:1994;301-310.
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J Crystal Growth
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Knight, C.A.1
Devries, A.L.2
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17
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0000814617
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Structure determination of a lone α-helical antifreeze protein from winter flounder
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Sichieri F, Yang DSC. Structure determination of a lone α-helical antifreeze protein from winter flounder. Acta Crystallogr D. 52:1996;486-498.
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Acta Crystallogr D
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Sichieri, F.1
Yang, D.S.C.2
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18
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0032485929
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Mapping of disulfide bridges in antifreeze proteins from overwintering larvae of the beetle Dendroides canadensis
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of outstanding interest. Exhaustive peptide fragment analyses are here used to identify the disulfide linkages of all the 16 Cys residues in this AFP, laying the ground work for future structural and mechanistic studies.
-
Li N, Chibber BAK, Castellino FJ, Duman JG. Mapping of disulfide bridges in antifreeze proteins from overwintering larvae of the beetle Dendroides canadensis. of outstanding interest Biochemistry. 37:1998;6343-6350 Exhaustive peptide fragment analyses are here used to identify the disulfide linkages of all the 16 Cys residues in this AFP, laying the ground work for future structural and mechanistic studies.
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(1998)
Biochemistry
, vol.37
, pp. 6343-6350
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Li, N.1
Chibber, B.A.K.2
Castellino, F.J.3
Duman, J.G.4
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19
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0023943675
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The apolipoprotein multigene family: Biosynthesis, structure, structure-function relationships, and evolution
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Li WH, Tanimura M, Luo CC, Datta S, Chan L. The apolipoprotein multigene family: biosynthesis, structure, structure-function relationships, and evolution. J Lipid Res. 29:1988;245-271.
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Li, W.H.1
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Chan, L.5
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0030732162
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Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation
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Borhani W, Rogers DP, Engler JA, Brouillette CG. Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Proc Natl Acad Sci USA. 94:1997;12291-12296.
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Borhani, W.1
Rogers, D.P.2
Engler, J.A.3
Brouillette, C.G.4
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0025860481
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Three-dimensional structure of the LDL receptor binding domain of human apolipoprotein E
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Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA. Three-dimensional structure of the LDL receptor binding domain of human apolipoprotein E. Science. 252:1991;1817-1822.
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Wilson, C.1
Wardell, M.R.2
Weisgraber, K.H.3
Mahley, R.W.4
Agard, D.A.5
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22
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0032492659
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The solution structure of type II antifreeze protein reveals a new member of the lectin family
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of outstanding interest. The paper reports the first NMR solution structure sea raven type II AFP confirming a global fold homologous to the C-type lectins and pancreatic stone proteins. It lays the ground work for identifying the putative ice-binding residues of fish type II AFPs and the structural basis for the binding of ice.
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Gronwald W, Loewen MC, Lix B, Daugulis A, Sönnichsen F, Davies PL, Sykes BD. The solution structure of type II antifreeze protein reveals a new member of the lectin family. of outstanding interest Biochemistry. 37:1998;4712-4721 The paper reports the first NMR solution structure sea raven type II AFP confirming a global fold homologous to the C-type lectins and pancreatic stone proteins. It lays the ground work for identifying the putative ice-binding residues of fish type II AFPs and the structural basis for the binding of ice.
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(1998)
Biochemistry
, vol.37
, pp. 4712-4721
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Gronwald, W.1
Loewen, M.C.2
Lix, B.3
Daugulis, A.4
Sönnichsen, F.5
Davies, P.L.6
Sykes, B.D.7
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23
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0026772705
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Structural and functional similarity between fish antifreeze proteins and calcium-dependent lectins
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Ewart KV, Rubinsky B, Fletcher GL. Structural and functional similarity between fish antifreeze proteins and calcium-dependent lectins. Biochem Biophys Res Comm. 185:1992;335-340.
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Ewart, K.V.1
Rubinsky, B.2
Fletcher, G.L.3
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24
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0001044156
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The ice binding site of Atlantic herring antifreeze protein corresponds to the carbohydrate-binding site of C-type lectins
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2+-dependent type II fish AFP is localized by site-directed mutagenesis to the sequence segment that is homologous to the carbohydrate-binding site of its evolutionary precursor, the C-type lectins.
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2+-dependent type II fish AFP is localized by site-directed mutagenesis to the sequence segment that is homologous to the carbohydrate-binding site of its evolutionary precursor, the C-type lectins.
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(1998)
Biochemistry
, vol.37
, pp. 4080-4085
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Vanda Ewart, K.1
Li, Z.2
Yang, D.S.C.3
Fletcher, G.L.4
Hew, C.L.5
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25
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0027490930
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Plant 'pathogenesis-related' proteins and their role in defense against pathogens
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Stintzi A, Heitz T, Prasad V, Wiedermann-Merdinoglu S, Kauffmann S, Geoffroy P, Legrand M, Fritig B. Plant 'pathogenesis-related' proteins and their role in defense against pathogens. Biochimie. 75:1993;687-706.
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Stintzi, A.1
Heitz, T.2
Prasad, V.3
Wiedermann-Merdinoglu, S.4
Kauffmann, S.5
Geoffroy, P.6
Legrand, M.7
Fritig, B.8
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0030908453
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Antifreeze proteins in winter rye
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Griffith M, Antikainen M, Hon WC, Pihakaski-Maunsbach K, Yu XM, Chun J, Yang DSC. Antifreeze proteins in winter rye. Physiologic Planetarium. 100:1997;327-332.
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Griffith, M.1
Antikainen, M.2
Hon, W.C.3
Pihakaski-Maunsbach, K.4
Yu, X.M.5
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Yang, D.S.C.7
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Clarke A, Johnston IA. Evolution and adaptive radiation of antarctic fishes. Trends Ecol Evol. 11:1996;212-218.
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Bargelloni L, Ritchie PA, Patarnello T, Battaglia B, Lambert DM, Meyer A. Molecular evolution at subzero temperature: mitochondrial and nuclear phylogenies of fishes from Antarctica (suborder Notothenioidei), and the evolution of antifreeze glycopeptides. Mol Biol Ecol. 11:1994;854-863.
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Shackleton NJ, Backman J, Zimmerman J, Kent DV, Hall MA, Roberts DG, Schnitker D, Baldauf JG, Desprairies A, Homrighausen R, et al. Oxygen isotope calibration of the onset of ice-rafting and history of glaciation in the North Atlantic region. Nature. 307:1984;620-623.
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Shackleton, N.J.1
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Schnitker, D.7
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Phillips RL, Grants A. Quaternary history of sea ice and peleoclimate in the Amerasia basin, Arctic Ocean, as recorded in the cyclical strata of Northwind Ridge. Geol Soc Am Bull. 109:1997;1110-1115.
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