메뉴 건너뛰기




Volumn 9, Issue 1, 2009, Pages

Acclimatory responses of the Daphnia pulex proteome to environmental changes. II. Chronic exposure to different temperatures (10 and 20°C) mainly affects protein metabolism

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATASE; ASTACIN; CARBOXYPEPTIDASE; CHYMOTRYPSIN; PROTEOME; TRYPSIN; VITELLOGENIN; CYTOSKELETON PROTEIN; MUSCLE PROTEIN; PEPTIDE HYDROLASE;

EID: 65549107937     PISSN: None     EISSN: 14726793     Source Type: Journal    
DOI: 10.1186/1472-6793-9-8     Document Type: Article
Times cited : (65)

References (59)
  • 3
    • 34447295607 scopus 로고    scopus 로고
    • Temporal environmental change, clonal physiology and the genetic structure of a Daphnia assemblage (D. galeata-hyalina hybrid species complex)
    • DOI 10.1111/j.1365-2427.2007.01786.x
    • Temporal environmental change, clonal physiology and the genetic structure of a Daphnia assemblage (D. galeata-hyalina hybrid species complex). O Pinkhaus S Schwerin R Pirow B Zeis I Buchen U Gigengack M Koch W Horn RJ Paul, Freshwater Biol 2007 52 1537 1554 10.1111/j.1365-2427.2007.01786.x (Pubitemid 47052265)
    • (2007) Freshwater Biology , vol.52 , Issue.8 , pp. 1537-1554
    • Pinkhaus, O.1    Schwerin, S.2    Pirow, R.3    Zeis, B.4    Buchen, I.5    Gigengack, U.6    Koch, M.7    Horn, W.8    Paul, R.J.9
  • 4
    • 0038732457 scopus 로고    scopus 로고
    • Temperature acclimation influences temperature-related behaviour as well as oxygen-transport physiology and biochemistry in the water flea Daphnia magna
    • DOI 10.1139/z03-001
    • Temperature acclimation influences temperature-related behaviour as well as oxygen-transport physiology and biochemistry in the water flea Daphnia magna. T Lamkemeyer B Zeis RJ Paul, Can J Zool 2003 81 237 249 10.1139/z03-001 (Pubitemid 36562499)
    • (2003) Canadian Journal of Zoology , vol.81 , Issue.2 , pp. 237-249
    • Lamkemeyer, T.1    Zeis, B.2    Paul, R.J.3
  • 5
    • 4744368281 scopus 로고    scopus 로고
    • Thermal acclimation in the microcrustacean Daphnia: A survey of behavioural, physiological and biochemical mechanisms
    • DOI 10.1016/j.jtherbio.2004.08.035, PII S0306456504001147
    • Thermal acclimation in the microcrustacean Daphnia: a survey of behavioural, physiological and biochemical mechanisms. RJ Paul T Lamkemeyer J Maurer O Pinkhaus R Pirow M Seidl B Zeis, J Therm Biol 2004 29 655 662 10.1016/j.jtherbio.2004.08.035 (Pubitemid 39311194)
    • (2004) Journal of Thermal Biology , vol.29 , Issue.7-8 SPEC. ISS. , pp. 655-662
    • Paul, R.J.1    Lamkemeyer, T.2    Maurer, J.3    Pinkhaus, O.4    Pirow, R.5    Seidl, M.6    Zeis, B.7
  • 6
    • 22744457721 scopus 로고    scopus 로고
    • A swimming activity assay shows that the thermal tolerance of Daphnia magna is influenced by temperature acclimation
    • DOI 10.1139/z04-141
    • A swimming activity assay shows that the thermal tolerance of Daphnia magna is influenced by temperature acclimation. B Zeis J Maurer O Pinkhaus E Bongartz RJ Paul, Can J Zool 2004 82 1605 1613 10.1139/z04-141 (Pubitemid 41026322)
    • (2004) Canadian Journal of Zoology , vol.82 , Issue.10 , pp. 1605-1613
    • Zeis, B.1    Maurer, J.2    Pinkhaus, O.3    Bongartz, E.4    Paul, R.J.5
  • 8
    • 0001298577 scopus 로고
    • Feeding and nutrition in Daphnia
    • Pallanza: Istituto Italiano di Idrobiologia Peters RH, DeBernardi R
    • Feeding and nutrition in Daphnia. W Lampert, Memorie dell'Istituto Italiano di Idrobiologia, Daphnia Pallanza: Istituto Italiano di Idrobiologia, Peters RH, DeBernardi R, 1987 45 143 192
    • (1987) Memorie dell'Istituto Italiano di Idrobiologia, Daphnia , vol.45 , pp. 143-192
    • Lampert, W.1
  • 9
    • 0000536260 scopus 로고
    • Daphnia development and reproduction - Responses to temperature
    • 10.1016/0306-4565(83)90025-6
    • Daphnia development and reproduction - responses to temperature. LB Goss DL Bunting, J Therm Biol 1983 8 375 380 10.1016/0306-4565(83)90025-6
    • (1983) J Therm Biol , vol.8 , pp. 375-380
    • Goss, L.B.1    Bunting, D.L.2
  • 10
    • 0030303297 scopus 로고    scopus 로고
    • Juvenile growth rate as a measure of fitness in Daphnia
    • 10.2307/2390173
    • Juvenile growth rate as a measure of fitness in Daphnia. W Lampert I Trubetskova, Funct Ecol 1996 10 631 635 10.2307/2390173
    • (1996) Funct Ecol , vol.10 , pp. 631-635
    • Lampert, W.1    Trubetskova, I.2
  • 11
    • 0035082373 scopus 로고    scopus 로고
    • Temperature reaction norms of Daphnia magna: The effect of food concentration
    • DOI 10.1046/j.1365-2427.2001.00630.x
    • Temperature reaction norms of Daphnia magna: the effect of food concentration. B Giebelhausen W Lampert, Freshwater Biol 2001 46 281 289 10.1046/j.1365-2427.2001.00630.x (Pubitemid 32241471)
    • (2001) Freshwater Biology , vol.46 , Issue.3 , pp. 281-289
    • Giebelhausen, B.1    Lampert, W.2
  • 12
    • 65549129637 scopus 로고    scopus 로고
    • Acclimatory responses of the Daphnia pulex proteome to environmental changes. I. Chronic exposure to hypoxia affects the oxygen transport system and carbohydrate metabolism
    • 19383146
    • Acclimatory responses of the Daphnia pulex proteome to environmental changes. I. Chronic exposure to hypoxia affects the oxygen transport system and carbohydrate metabolism. B Zeis T Lamkemeyer RJ Paul F Nunes S Schwerin M Koch W Schütz J Madlung C Fladerer R Pirow, BMC Physiol 2009 9 7 19383146
    • (2009) BMC Physiol , vol.9 , pp. 7
    • Zeis, B.1    Lamkemeyer, T.2    Paul, R.J.3    Nunes, F.4    Schwerin, S.5    Koch, M.6    Schütz, W.7    Madlung, J.8    Fladerer, C.9    Pirow, R.10
  • 14
    • 33846946171 scopus 로고    scopus 로고
    • Information available at cut rates: Structure and mechanism of ribonucleases
    • DOI 10.1016/j.sbi.2006.12.001, PII S0959440X06002119, Foldinf and Binding / Protein-Nucleic Interactions
    • Information available at cut rates: structure and mechanism of ribonucleases. JAR Worrall BF Luisi, Curr Opin Struct Biol 2007 17 128 137 10.1016/j.sbi.2006.12.001 17189683 (Pubitemid 46242189)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.1 , pp. 128-137
    • Worrall, J.A.1    Luisi, B.F.2
  • 15
    • 35948947822 scopus 로고    scopus 로고
    • AAA+ ATPases: Achieving diversity of function with conserved machinery
    • DOI 10.1111/j.1600-0854.2007.00642.x
    • AAA+ ATPases: Achieving diversity of function with conserved machinery. S Roehl White B Lauring, Traffic 2007 8 1657 1667 10.1111/j.1600-0854.2007.00642. x 17897320 (Pubitemid 350066678)
    • (2007) Traffic , vol.8 , Issue.12 , pp. 1657-1667
    • White, S.R.1    Lauring, B.2
  • 16
    • 0032078463 scopus 로고    scopus 로고
    • Molecular characteristics of insect vitellogenins and vitellogenin receptors
    • DOI 10.1016/S0965-1748(97)00110-0, PII S0965174897001100
    • Molecular characteristics of insect vitellogenins and vitellogenin receptors. TW Sappington AS Raikhel, Insect Biochem Mol Biol 1998 28 277 300 10.1016/S0965-1748(97)00110-0 9692232 (Pubitemid 28328322)
    • (1998) Insect Biochemistry and Molecular Biology , vol.28 , Issue.5-6 , pp. 277-300
    • Sappington, T.W.1    Raikhel A, S.2
  • 18
    • 0038112171 scopus 로고    scopus 로고
    • Relationship between vitellogenin and vitellin in a marine shrimp (Penaeus semisulcatus) and molecular characterization of vitellogenin complementary DNAs
    • DOI 10.1095/biolreprod.102.011627
    • Relationship between vitellogenin and vitellin in a marine shrimp (Penaeus semisulcatus) and molecular characterization of vitellogenin complementary DNAs. J-C Avarre R Michelis A Tietz E Lubzens, Biol Reprod 2003 69 355 364 10.1095/biolreprod.102.011627 12672675 (Pubitemid 36806842)
    • (2003) Biology of Reproduction , vol.69 , Issue.1 , pp. 355-364
    • Avarre, J.-C.1    Michelis, R.2    Tietz, A.3    Lubzens, E.4
  • 19
    • 3142609030 scopus 로고    scopus 로고
    • A vitellogenin chain containing a superoxide dismutase-like domain is the major component of yolk proteins in cladoceran crustacean Daphnia magna
    • DOI 10.1016/j.gene.2004.03.030, PII S0378111904002033
    • A vitellogenin chain containing a superoxide dismutase-like domain is the major component of yolk proteins in cladoceran crustacean Daphnia magna. Y Kato S Tokishita T Ohta H Yamagata, Gene 2004 334 157 165 10.1016/j.gene.2004.03.030 15256265 (Pubitemid 38902725)
    • (2004) Gene , vol.334 , Issue.1-2 , pp. 157-165
    • Kato, Y.1    Tokishita, S.-I.2    Ohta, T.3    Yamagata, H.4
  • 20
    • 33947190010 scopus 로고    scopus 로고
    • Molecular diversity and evolution of the large lipid transfer protein superfamily
    • 10.1194/jlr.R600028-JLR200 17148551
    • Molecular diversity and evolution of the large lipid transfer protein superfamily. MMW Smolenaars O Madsen KW Rodenburg DJ Van der Horst, J Lipid Res 2006 48 489 502 10.1194/jlr.R600028-JLR200 17148551
    • (2006) J Lipid Res , vol.48 , pp. 489-502
    • Smolenaars, M.M.W.1    Madsen, O.2    Rodenburg, K.W.3    Der Van J., H.D.4
  • 21
    • 33846565430 scopus 로고    scopus 로고
    • Apolipocrustacein, formerly vitellogenin, is the major egg yolk precursor protein in decapod crustaceans and is homologous to insect apolipophorin II/I and vertebrate apolipoprotein B
    • DOI 10.1186/1471-2148-7-3
    • Apolipocrustacein, formerly vitellogenin, is the major egg yolk precursor in decapod crustaceans and is homologous to insect apolipophorin II/I and vertebrate apolipoprotein B. J-C Avarre E Lubzens PJ Babin, BMC Evol Biol 2007 7 3 17241455 10.1186/1471-2148-7-3 (Pubitemid 46178294)
    • (2007) BMC Evolutionary Biology , vol.7 , pp. 3
    • Avarre, J.-C.1    Lubzens, E.2    Babin, P.J.3
  • 22
    • 0008310466 scopus 로고
    • Considerations on some cytological and ultrastructural observations on fat cells in Daphnia (Crustacea, Cladocera)
    • Considerations on some cytological and ultrastructural observations on fat cells in Daphnia (Crustacea, Cladocera). F Zaffagnini C Zeni, Boll Zool 1986 53 33 39
    • (1986) Boll Zool , vol.53 , pp. 33-39
    • Zaffagnini, F.1    Zeni, C.2
  • 23
    • 0009546179 scopus 로고
    • Ueber den Fettkörper von Daphnia magna
    • 10.1007/BF00387983
    • Ueber den Fettkörper von Daphnia magna. G Jäger, Z Zellforsch 1935 22 89 131 10.1007/BF00387983
    • (1935) Z Zellforsch , vol.22 , pp. 89-131
    • Jäger, G.1
  • 24
    • 0009521630 scopus 로고
    • Zytologische Untersuchungen an grosskernigen Fettzellen von Daphnia pulex unter besonderer Berücksichtigung des Mitochondrien-Formwechsels
    • 13393350
    • Zytologische Untersuchungen an grosskernigen Fettzellen von Daphnia pulex unter besonderer Berücksichtigung des Mitochondrien-Formwechsels. G Sterba, Z Zellforsch 1956 44 456 487 13393350
    • (1956) Z Zellforsch , vol.44 , pp. 456-487
    • Sterba, G.1
  • 25
    • 33646395148 scopus 로고    scopus 로고
    • Organization and repression by juvenile hormone of a vitellogenin gene cluster in the crustacean, Daphnia magna
    • 10.1016/j.bbrc.2006.04.102 16681994
    • Organization and repression by juvenile hormone of a vitellogenin gene cluster in the crustacean, Daphnia magna. S Tokishita Y Kato T Kobayashi S Nakamura T Ohta H Yamagata, Biochem Biophys Res Commun 2006 345 362 370 10.1016/j.bbrc.2006.04.102 16681994
    • (2006) Biochem Biophys Res Commun , vol.345 , pp. 362-370
    • Tokishita, S.1    Kato, Y.2    Kobayashi, T.3    Nakamura, S.4    Ohta, T.5    Yamagata, H.6
  • 26
    • 0029662389 scopus 로고    scopus 로고
    • The interactive effects of temperature, food level and maternal phenotype on offspring size in Daphnia magna
    • The interactive effects of temperature, food level and maternal phenotype on offspring size in Daphnia magna. D McKee D Ebert, Oecologia 1996 107 189 196 10.1007/BF00327902 (Pubitemid 27017239)
    • (1996) Oecologia , vol.107 , Issue.2 , pp. 189-196
    • McKee, D.1    Ebert, D.2
  • 27
    • 0028228085 scopus 로고
    • Conserved patterns in the Cu,Zn superoxide dismutase family
    • DOI 10.1006/jmbi.1994.1298
    • Conserved patterns in the Cu, Zn superoxide dismutase family. D Bordo K Djinovic M Bolognesi, J Mol Biol 1994 238 366 386 10.1006/jmbi.1994.1298 8176730 (Pubitemid 24154718)
    • (1994) Journal of Molecular Biology , vol.238 , Issue.3 , pp. 366-386
    • Bordo, D.1    Djinovic, K.2    Bolognesi, M.3
  • 28
    • 26244446828 scopus 로고    scopus 로고
    • Contribution of sequence variation in Drosophila actins to their incorporation into actin-based structures in vivo
    • DOI 10.1242/jcs.02517
    • Contribution of sequence variation in Drosophila actins to their incorporation into actin-based structures in vivo. K Röper Y Mao NH Brown, J Cell Sci 2005 118 3937 3948 10.1242/jcs.02517 16105877 (Pubitemid 41410277)
    • (2005) Journal of Cell Science , vol.118 , Issue.17 , pp. 3937-3948
    • Roper, K.1    Mao, Y.2    Brown, N.H.3
  • 29
    • 21244459182 scopus 로고    scopus 로고
    • Invertebrate muscles: Muscle specific genes and proteins
    • DOI 10.1152/physrev.00019.2004
    • Invertebrate muscles: muscle specific genes and peptides. SI Hooper JB Thuma, Physiol Rev 2005 85 1001 1060 10.1152/physrev.00019.2004 15987801 (Pubitemid 40885222)
    • (2005) Physiological Reviews , vol.85 , Issue.3 , pp. 1001-1060
    • Hooper, S.L.1    Thuma, J.B.2
  • 31
    • 0024366590 scopus 로고
    • Functional domains of the Drosophila melanogaster muscle myosin heavy-chain gene are encoded by alternatively spliced exons
    • Functional domains of the Drosophila melanogaster muscle myosin heavy-chain gene are encoded by alternatively spliced exons. E George MB Ober CP Emerson, Mol Cell Biol 1989 9 2957 2974 2506434 (Pubitemid 19163060)
    • (1989) Molecular and Cellular Biology , vol.9 , Issue.7 , pp. 2957-2974
    • George, E.L.1    Ober, M.B.2    Emerson Jr., C.P.3
  • 32
    • 0034665602 scopus 로고    scopus 로고
    • Determining structure/function relationships for sarcomeric myosin heavy chain by genetic and transgenic manipulation of Drosophila
    • 10.1002/1097-0029(20000915)50:6<430::AID-JEMT2>3.0.CO;2-E
    • Determining structure/function relationships for sarcomeric myosin heavy chain by genetic and transgenic manipulation of Drosophila. DM Swank L Wells WA Kronert GE Morrill SI Bernstein, Microsc Res Techniq 2000 50 430 442 10.1002/1097-0029(20000915)50:6<430::AID-JEMT2>3.0.CO;2-E
    • (2000) Microsc Res Techniq , vol.50 , pp. 430-442
    • Swank, D.M.1    Wells, L.2    Kronert, W.A.3    Morrill, G.E.4    Bernstein, S.I.5
  • 34
    • 0034470147 scopus 로고    scopus 로고
    • Sequence determinants of function and evolution in serine proteases
    • DOI 10.1016/S1050-1738(00)00068-2, PII S1050173800000682
    • Sequence determinants of function and evolution in serine proteases. MM Krem T Rose E Di Cera, Trends Cardiovasc Med 2000 10 171 176 10.1016/S1050-1738(00)00068-2 11239798 (Pubitemid 32178193)
    • (2000) Trends in Cardiovascular Medicine , vol.10 , Issue.4 , pp. 171-176
    • Krem, M.M.1    Rose, T.2    Di Cera, E.3
  • 35
    • 34547828023 scopus 로고    scopus 로고
    • Sampling Daphnia's expressed genes: Preservation, expansion and invention of crustacean genes with reference to insect genomes
    • DOI 10.1186/1471-2164-8-217
    • Sampling Daphnia's expressed genes: preservation, expansion and invention of crustacean genes with reference to insect. JK Colbourne BD Eads J Shaw E Bohuski DJ Bauer J Andrews, BMC Genomics 2007 8 217 17612412 10.1186/1471-2164-8-217 (Pubitemid 47244079)
    • (2007) BMC Genomics , vol.8 , pp. 217
    • Colbourne, J.K.1    Eads, B.D.2    Shaw, J.3    Bohuski, E.4    Bauer, D.J.5    Andrews, J.6
  • 36
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • 10.1021/cr000033x 12475199
    • Serine protease mechanism and specificity. L Hedstrom, Chem Rev 2002 102 4501 4523 10.1021/cr000033x 12475199
    • (2002) Chem Rev , vol.102 , pp. 4501-4523
    • Hedstrom, L.1
  • 37
    • 0028914722 scopus 로고
    • Structural basis of substrate specificity in the serine proteases
    • 7795518
    • Structural basis of substrate specificity in the serine proteases. JJ Perona CS Craik, Protein Sci 1995 4 337 360 7795518
    • (1995) Protein Sci , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 38
    • 0035161999 scopus 로고    scopus 로고
    • Increasing the thermal stability of euphauserase: A cold-active and multifunctional serine protease from Antarctic krill
    • DOI 10.1046/j.1432-1327.2001.01857.x
    • Increasing the thermal stability of euphauserase. A cold-active and multifunctional serine protease from antarctic krill. DC Benjamin S Kristjánsdáttir Á Gudmundsdáttir, Eur J Biochem 2001 268 131 10.1046/j.1432-1327.2001.01857.x (Pubitemid 32052255)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.1 , pp. 127-131
    • Benjamin, D.C.1    Kristjansdottir, S.2    Gudmundsdottir, A.3
  • 39
    • 0034075954 scopus 로고    scopus 로고
    • Propeptide dependent activation of the Antarctic krill euphauserase precursor produced in yeast
    • DOI 10.1046/j.1432-1327.2000.01273.x
    • Propeptide dependent activation of the antarctic krill euphauserase precursor produced in yeast. S Kristjánsdáttir Á Gudmundsdáttir, Eur J Biochem 2000 267 2632 2639 10.1046/j.1432-1327. 2000.01273.x 10785384 (Pubitemid 30304259)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.9 , pp. 2632-2639
    • Kristjansdottir, S.1    Gudmundsdottir, A.2
  • 40
    • 0036660659 scopus 로고    scopus 로고
    • Cold-adapted and mesophilic brachyurins
    • DOI 10.1515/BC.2002.122
    • Cold-adapted and mesophilic brachyurins. Á Gudmundsdáttir, Biol Chem 2002 383 1125 1131 10.1515/BC.2002.122 12437096 (Pubitemid 35215058)
    • (2002) Biological Chemistry , vol.383 , Issue.7-8 , pp. 1125-1131
    • Gudmundsdottir, A.1
  • 41
    • 0037262316 scopus 로고    scopus 로고
    • Brachyurins, Serine Collagenolytic Enzymes from Crabs
    • DOI 10.1023/A:1023248113184
    • Brachyurins, serine collagenolytic enzymes from crabs. GN Rudenskaya, Rus J Bioorg Chem 2003 29 101 111 10.1023/A:1023248113184 (Pubitemid 36447027)
    • (2003) RUSSIAN JOURNAL of BIOORGANIC CHEMISTRY , vol.29 , Issue.2 , pp. 101-111
    • Rudenskaya, G.N.1
  • 42
    • 2642518135 scopus 로고    scopus 로고
    • Collagenolytic serine protease PC and trypsin PC from king crab Paralithodes camtschaticus: CDNA cloning and primary structure of the enzymes
    • DOI 10.1186/1472-6807-4-1, 1
    • Collagenolytic serine protease PC and trypsin PC from king crab Paralithodes camtschaticus: cDNA cloning and primary structure of the enzymes. GN Rudenskaya YA Kislitsin DV Rebrikov, BMC Struct Biol 2004 4 2 14731305 10.1186/1472-6807-4-2 (Pubitemid 38729447)
    • (2004) BMC Structural Biology , vol.4 , pp. 1-9
    • Rudenskaya, G.N.1    Kislitsin, Y.A.2    Rebrikov, D.V.3
  • 44
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Probability-based protein identification by searching sequence data bases using mass spectrometric data. DN Perkins DJC Pappin DM Creasy JS Cottrell, Electrophoresis 1999 20 3551 3567 10.1002/(SICI)1522-2683(19991201)20: 18<3551::AID-ELPS3551>3.0.CO;2-2 10612281 (Pubitemid 30007252)
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 45
    • 84872270834 scopus 로고    scopus 로고
    • SignalP 3.0. http://www.cbs.dtu.dk/services/SignalP/
    • SignalP 3.0
  • 46
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • 10.1016/j.jmb.2004.05.028 15223320
    • Improved prediction of signal peptides: SignalP 3.0. JD Bendtsen H Nielsen G von Heijne S Brunak, J Mol Biol 2004 340 783 795 10.1016/j.jmb.2004. 05.028 15223320
    • (2004) J Mol Biol , vol.340 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    Von Heijne, G.3    Brunak, S.4
  • 47
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • DOI 10.1038/nprot.2007.131, PII NPROT.2007.131
    • Locating proteins in the cell using TargetP, SignalP, and related tools. O Emanuelsson S Brunak G von Heijne H Nielsen, Nature Protocols 2007 2 953 971 10.1038/nprot.2007.131 17446895 (Pubitemid 46745592)
    • (2007) Nature Protocols , vol.2 , Issue.4 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 48
  • 49
    • 0028302337 scopus 로고
    • Reference points for comparisons of two-dimensional maps of proteins from different human cell types defined in a pH scale where isoelectric points correlate with polypeptide compositions
    • Reference points for comparisons of two-dimensional maps of proteins from different human cell types defined in a pH scale where isoelectric points correlate with polypeptide compositions. B Bjellqvist B Basse E Olsen JE Celis, Electrophoresis 1994 15 529 539 10.1002/elps.1150150171 8055880 (Pubitemid 24151853)
    • (1994) Electrophoresis , vol.15 , Issue.3-4 , pp. 529-539
    • Bjellqvist, B.1    Basse, B.2    Olsen, E.3    Celis, J.E.4
  • 54
    • 65549130191 scopus 로고    scopus 로고
    • TCoffee. http://www.tcoffee.org/
    • TCoffee
  • 55
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence aligment
    • 10.1006/jmbi.2000.4042 10964570
    • T-Coffee: a novel method for fast and accurate multiple sequence aligment. C Notredame DG Higgins J Heringa, J Mol Biol 2000 302 205 217 10.1006/jmbi.2000.4042 10964570
    • (2000) J Mol Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 56
    • 0043123123 scopus 로고    scopus 로고
    • Tcoffee@igs: A web server for computing, evaluating and combining multiple sequence alignments
    • 12824354 10.1093/nar/gkg522
    • Tcoffee@igs: a web server for computing, evaluating and combining multiple sequence alignments. O Poirot E O'Toole C Notredame, Nucleic Acids Res 2003 31 3503 3506 12824354 10.1093/nar/gkg522
    • (2003) Nucleic Acids Res , vol.31 , pp. 3503-3506
    • Poirot, O.1    O'Toole, E.2    Notredame, C.3
  • 57
    • 0023375195 scopus 로고
    • The neighbor-joining method - A new method for reconstructing phylogenetic trees
    • 3447015
    • The neighbor-joining method - a new method for reconstructing phylogenetic trees. N Saitou M Nei, Mol Biol Evol 1987 4 406 425 3447015
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 58
    • 0042622583 scopus 로고    scopus 로고
    • Contribution of myosin rod protein to structural organization of adult and embryonic muscles in Drosophila
    • 10.1016/S0022-2836(03)00827-1 12927543
    • Contribution of myosin rod protein to structural organization of adult and embryonic muscles in Drosophila. E Polyák DM Standiford V Yakopson CP Emerson C Franzini-Armstrong, J Mol Biol 2003 331 1077 1091 10.1016/S0022-2836(03)00827-1 12927543
    • (2003) J Mol Biol , vol.331 , pp. 1077-1091
    • Polyák, E.1    Standiford, D.M.2    Yakopson, V.3    Emerson, C.P.4    Franzini-Armstrong, C.5
  • 59
    • 0025287330 scopus 로고
    • Comparative modeling methods: Application to the family of the mammalian serine proteases
    • 10.1002/prot.340070404 2381905
    • Comparative modeling methods: Application to the family of the mammalian serine proteases. J Greer, Proteins Struct Funct Genet 1990 7 317 334 10.1002/prot.340070404 2381905
    • (1990) Proteins Struct Funct Genet , vol.7 , pp. 317-334
    • Greer, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.