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Volumn 107, Issue 32, 2010, Pages 14274-14279

Gene cooption and convergent evolution of oxygen transport hemoglobins in jawed and jawless vertebrates

Author keywords

Cytoglobin; Gene family evolution; Globin; Hagfish; Lamprey

Indexed keywords

CYTOGLOBIN; HEMOGLOBIN; MYOGLOBIN; GLOBIN; OXYGEN;

EID: 77956272960     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1006756107     Document Type: Article
Times cited : (67)

References (78)
  • 1
    • 0032942822 scopus 로고    scopus 로고
    • Evolutionary change in the functional specificity of genes
    • Eizinger A, Jungblut B, Sommer RJ (1999) Evolutionary change in the functional specificity of genes. Trends Genet 15:197-202.
    • (1999) Trends Genet , vol.15 , pp. 197-202
    • Eizinger, A.1    Jungblut, B.2    Sommer, R.J.3
  • 2
    • 0345161806 scopus 로고    scopus 로고
    • Generation of evolutionary novelty by functional shift
    • Ganfornina MD, Sánchez D (1999) Generation of evolutionary novelty by functional shift. Bioessays 21:432-439.
    • (1999) Bioessays , vol.21 , pp. 432-439
    • Ganfornina, M.D.1    Sánchez, D.2
  • 3
    • 0035931911 scopus 로고    scopus 로고
    • Chance and necessity: The evolution of morphological complexity and diversity
    • Carroll SB (2001) Chance and necessity: The evolution of morphological complexity and diversity. Nature 409:1102-1109.
    • (2001) Nature , vol.409 , pp. 1102-1109
    • Carroll, S.B.1
  • 4
    • 0036439421 scopus 로고    scopus 로고
    • Gene co-option in physiological and morphological evolution
    • True JR, Carroll SB (2002) Gene co-option in physiological and morphological evolution. Annu Rev Cell Dev Biol 18:53-80.
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 53-80
    • True, J.R.1    Carroll, S.B.2
  • 6
    • 56549119570 scopus 로고    scopus 로고
    • Turning a hobby into a job: How duplicated genes find new functions
    • Conant GC, Wolfe KH (2008) Turning a hobby into a job: How duplicated genes find new functions. Nat Rev Genet 9:938-950.
    • (2008) Nat Rev Genet , vol.9 , pp. 938-950
    • Conant, G.C.1    Wolfe, K.H.2
  • 8
    • 0032052216 scopus 로고    scopus 로고
    • Hemoglobins from bacteria to man: Evolution of different patterns of gene expression
    • Hardison R (1998) Hemoglobins from bacteria to man: Evolution of different patterns of gene expression. J Exp Biol 201:1099-1117.
    • (1998) J Exp Biol , vol.201 , pp. 1099-1117
    • Hardison, R.1
  • 9
    • 40349116061 scopus 로고    scopus 로고
    • Genomic evidence for independent origins of β-like globin genes in monotremes and therian mammals
    • Opazo JC, Hoffmann FG, Storz JF (2008) Genomic evidence for independent origins of β-like globin genes in monotremes and therian mammals. Proc Natl Acad Sci USA 105:1590-1595.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 1590-1595
    • Opazo, J.C.1    Hoffmann, F.G.2    Storz, J.F.3
  • 10
    • 77951546469 scopus 로고    scopus 로고
    • Lineage-specific patterns of functional diversification in the α- And β-globin gene families of tetrapod vertebrates
    • Hoffmann FG, Storz JF, Gorr TA, Opazo JC (2010) Lineage-specific patterns of functional diversification in the α- and β-globin gene families of tetrapod vertebrates. Mol Biol Evol 27:1126-1138.
    • (2010) Mol Biol Evol , vol.27 , pp. 1126-1138
    • Hoffmann, F.G.1    Storz, J.F.2    Gorr, T.A.3    Opazo, J.C.4
  • 11
    • 0023752534 scopus 로고
    • An evolutionary tree for invertebrate globin sequences
    • Goodman M, et al. (1988) An evolutionary tree for invertebrate globin sequences. J Mol Evol 27:236-249.
    • (1988) J Mol Evol , vol.27 , pp. 236-249
    • Goodman, M.1
  • 12
    • 44049108195 scopus 로고    scopus 로고
    • Diversity of globin function: Enzymatic, transport, storage, and sensing
    • Vinogradov SN, Moens L (2008) Diversity of globin function: Enzymatic, transport, storage, and sensing. J Biol Chem 283:8773-8777.
    • (2008) J Biol Chem , vol.283 , pp. 8773-8777
    • Vinogradov, S.N.1    Moens, L.2
  • 13
    • 34447526069 scopus 로고    scopus 로고
    • A model of globin evolution
    • Vinogradov SN, et al. (2007) A model of globin evolution. Gene 398:132-142.
    • (2007) Gene , vol.398 , pp. 132-142
    • Vinogradov, S.N.1
  • 16
    • 0035816696 scopus 로고    scopus 로고
    • Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells
    • Kawada N, et al. (2001) Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells. J Biol Chem 276:25318-25323.
    • (2001) J Biol Chem , vol.276 , pp. 25318-25323
    • Kawada, N.1
  • 17
    • 0037205447 scopus 로고    scopus 로고
    • A ubiquitously expressed human hexacoordinate hemoglobin
    • 3rd
    • Trent JTIII, 3rd, Hargrove MS (2002) A ubiquitously expressed human hexacoordinate hemoglobin. J Biol Chem 277:19538-19545.
    • (2002) J Biol Chem , vol.277 , pp. 19538-19545
    • Trent III, J.T.1    Hargrove, M.S.2
  • 18
    • 0036219963 scopus 로고    scopus 로고
    • Cytoglobin: A novel globin type ubiquitously expressed in vertebrate tissues
    • Burmester T, Ebner B, Weich B, Hankeln T (2002) Cytoglobin: A novel globin type ubiquitously expressed in vertebrate tissues. Mol Biol Evol 19:416-421.
    • (2002) Mol Biol Evol , vol.19 , pp. 416-421
    • Burmester, T.1    Ebner, B.2    Weich, B.3    Hankeln, T.4
  • 20
    • 10344243985 scopus 로고    scopus 로고
    • A globin gene of ancient evolutionary origin in lower vertebrates: Evidence for two distinct globin families in animals
    • Roesner A, Fuchs C, Hankeln T, Burmester T (2005) A globin gene of ancient evolutionary origin in lower vertebrates: Evidence for two distinct globin families in animals. Mol Biol Evol 22:12-20.
    • (2005) Mol Biol Evol , vol.22 , pp. 12-20
    • Roesner, A.1    Fuchs, C.2    Hankeln, T.3    Burmester, T.4
  • 21
    • 32944462917 scopus 로고    scopus 로고
    • The amphibian globin gene repertoire as revealed by the Xenopus genome
    • Fuchs C, Burmester T, Hankeln T (2006) The amphibian globin gene repertoire as revealed by the Xenopus genome. Cytogenet Genome Res 112:296-306.
    • (2006) Cytogenet Genome Res , vol.112 , pp. 296-306
    • Fuchs, C.1    Burmester, T.2    Hankeln, T.3
  • 22
    • 17144392212 scopus 로고    scopus 로고
    • Neuroglobin and cytoglobin: Genes, proteins and evolution
    • Burmester T, et al. (2004) Neuroglobin and cytoglobin: Genes, proteins and evolution. IUBMB Life 56:703-707.
    • (2004) IUBMB Life , vol.56 , pp. 703-707
    • Burmester, T.1
  • 23
    • 17144420129 scopus 로고    scopus 로고
    • Functional properties of neuroglobin and cytoglobin. Insights into the ancestral physiological roles of globins
    • Fago A, Hundahl C, Malte H, Weber RE (2004) Functional properties of neuroglobin and cytoglobin. Insights into the ancestral physiological roles of globins. IUBMB Life 56:689-696.
    • (2004) IUBMB Life , vol.56 , pp. 689-696
    • Fago, A.1    Hundahl, C.2    Malte, H.3    Weber, R.E.4
  • 24
    • 17144382480 scopus 로고    scopus 로고
    • Reversible hexa- To penta-coordination of the heme Fe atom modulates ligand binding properties of neuroglobin and cytoglobin
    • Pesce A, et al. (2004) Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of neuroglobin and cytoglobin. IUBMB Life 56:657-664.
    • (2004) IUBMB Life , vol.56 , pp. 657-664
    • Pesce, A.1
  • 25
    • 0012231458 scopus 로고    scopus 로고
    • Neuroglobin and cytoglobin. Fresh blood for the vertebrate globin family
    • Pesce A, et al. (2002) Neuroglobin and cytoglobin. Fresh blood for the vertebrate globin family. EMBO Rep 3:1146-1151.
    • (2002) EMBO Rep , vol.3 , pp. 1146-1151
    • Pesce, A.1
  • 26
    • 10444267310 scopus 로고    scopus 로고
    • Neuroglobin and cytoglobin in search of their role in the vertebrate globin family
    • Hankeln T, et al. (2005) Neuroglobin and cytoglobin in search of their role in the vertebrate globin family. J Inorg Biochem 99:110-119.
    • (2005) J Inorg Biochem , vol.99 , pp. 110-119
    • Hankeln, T.1
  • 28
    • 66149086544 scopus 로고    scopus 로고
    • What is the function of neuroglobin?
    • Burmester T, Hankeln T (2009) What is the function of neuroglobin? J Exp Biol 212:1423-1428.
    • (2009) J Exp Biol , vol.212 , pp. 1423-1428
    • Burmester, T.1    Hankeln, T.2
  • 29
    • 0019986337 scopus 로고
    • Phylogenetic origins and adaptive evolution of avian and mammalian haemoglobin genes
    • Czelusniak J, et al. (1982) Phylogenetic origins and adaptive evolution of avian and mammalian haemoglobin genes. Nature 298:297-300.
    • (1982) Nature , vol.298 , pp. 297-300
    • Czelusniak, J.1
  • 30
    • 0016436505 scopus 로고
    • Darwinian evolution in the genealogy of haemoglobin
    • Goodman M, Moore GW, Matsuda G (1975) Darwinian evolution in the genealogy of haemoglobin. Nature 253:603-608.
    • (1975) Nature , vol.253 , pp. 603-608
    • Goodman, M.1    Moore, G.W.2    Matsuda, G.3
  • 32
    • 0016802593 scopus 로고
    • Hemoglobin function in the vertebrates: An evolutionary model
    • Coates ML (1975) Hemoglobin function in the vertebrates: An evolutionary model. J Mol Evol 6:285-307.
    • (1975) J Mol Evol , vol.6 , pp. 285-307
    • Coates, M.L.1
  • 33
    • 0013507248 scopus 로고
    • The six hemoglobins of the sea lamprey (Petromyzon marinus)
    • Rumen NM, Love WE (1963) The six hemoglobins of the sea lamprey (Petromyzon marinus). Arch Biochem Biophys 103:24-35.
    • (1963) Arch Biochem Biophys , vol.103 , pp. 24-35
    • Rumen, N.M.1    Love, W.E.2
  • 34
    • 0014962912 scopus 로고
    • The amino acid sequence of hemoglobin V from the lamprey, Petromyzon marinus
    • Li SL, Riggs A (1970) The amino acid sequence of hemoglobin V from the lamprey, Petromyzon marinus. J Biol Chem 245:6149-6169.
    • (1970) J Biol Chem , vol.245 , pp. 6149-6169
    • Li, S.L.1    Riggs, A.2
  • 35
    • 0015218355 scopus 로고
    • Sedimentation equilibriujm experiments on the self-assocation of hemoglobin from the lamprey Petromyzon marinus. A model for oxygen transport in the lamprey
    • Andersen ME (1971) Sedimentation equilibriujm experiments on the self-assocation of hemoglobin from the lamprey Petromyzon marinus. A model for oxygen transport in the lamprey. J Biol Chem 246:4800-4806.
    • (1971) J Biol Chem , vol.246 , pp. 4800-4806
    • Andersen, M.E.1
  • 36
    • 0023017352 scopus 로고
    • Characterization of the changes in the state of aggregation induced by ligand binding in the hemoglobin system of a primitive vertebrate, the hagfish Eptatretus cirrhatus
    • Brittain T, Wells RM (1986) Characterization of the changes in the state of aggregation induced by ligand binding in the hemoglobin system of a primitive vertebrate, the hagfish Eptatretus cirrhatus. Comp Biochem Physiol Comp Physiol 85:785-790.
    • (1986) Comp Biochem Physiol Comp Physiol , vol.85 , pp. 785-790
    • Brittain, T.1    Wells, R.M.2
  • 37
    • 0029042065 scopus 로고
    • The hemoglobin system of the hagfish Myxine glutinosa: Aggregation state and functional properties
    • Fago A, Weber RE (1995) The hemoglobin system of the hagfish Myxine glutinosa: Aggregation state and functional properties. Biochim Biophys Acta 1249:109-115.
    • (1995) Biochim Biophys Acta , vol.1249 , pp. 109-115
    • Fago, A.1    Weber, R.E.2
  • 39
    • 0035920240 scopus 로고    scopus 로고
    • Hagfish hemoglobins: Structure, function, and oxygen-linked association
    • Fago A, et al. (2001) Hagfish hemoglobins: Structure, function, and oxygen-linked association. J Biol Chem 276:27415-27423.
    • (2001) J Biol Chem , vol.276 , pp. 27415-27423
    • Fago, A.1
  • 40
    • 0038035496 scopus 로고    scopus 로고
    • Water regulates oxygen binding in hagfish (Myxine glutinosa) hemoglobin
    • Müller G, Fago A, Weber RE (2003) Water regulates oxygen binding in hagfish (Myxine glutinosa) hemoglobin. J Exp Biol 206:1389-1395.
    • (2003) J Exp Biol , vol.206 , pp. 1389-1395
    • Müller, G.1    Fago, A.2    Weber, R.E.3
  • 41
    • 0036304164 scopus 로고    scopus 로고
    • Cyclostome hemoglobins are possibly paralogous to gnathostome hemoglobins
    • Katoh K, Miyata T (2002) Cyclostome hemoglobins are possibly paralogous to gnathostome hemoglobins. J Mol Evol 55:246-249.
    • (2002) J Mol Evol , vol.55 , pp. 246-249
    • Katoh, K.1    Miyata, T.2
  • 42
    • 7944231804 scopus 로고    scopus 로고
    • Functional adaptation and its molecular basis in vertebrate hemoglobins, neuroglobins and cytoglobins
    • Weber RE, Fago A (2004) Functional adaptation and its molecular basis in vertebrate hemoglobins, neuroglobins and cytoglobins. Respir Physiol Neurobiol 144:141-159.
    • (2004) Respir Physiol Neurobiol , vol.144 , pp. 141-159
    • Weber, R.E.1    Fago, A.2
  • 43
    • 0017648202 scopus 로고
    • Primitive haemoglobin
    • Tiplady B, Goodman M (1977) Primitive haemoglobin. J Mol Evol 9:343-347.
    • (1977) J Mol Evol , vol.9 , pp. 343-347
    • Tiplady, B.1    Goodman, M.2
  • 44
    • 0036623258 scopus 로고    scopus 로고
    • An approximately unbiased test of phylogenetic tree selection
    • Shimodaira H (2002) An approximately unbiased test of phylogenetic tree selection. Syst Biol 51:492-508.
    • (2002) Syst Biol , vol.51 , pp. 492-508
    • Shimodaira, H.1
  • 45
    • 0032766857 scopus 로고    scopus 로고
    • Multiple comparisons of log-likelihoods with applications to phylogenetic inference
    • Shimodaira H, Hasegawa M (1999) Multiple comparisons of log-likelihoods with applications to phylogenetic inference. Mol Biol Evol 16:1114-1116.
    • (1999) Mol Biol Evol , vol.16 , pp. 1114-1116
    • Shimodaira, H.1    Hasegawa, M.2
  • 47
    • 0034351387 scopus 로고    scopus 로고
    • Likelihood-based tests of topologies in phylogenetics
    • Goldman N, Anderson JP, Rodrigo AG (2000) Likelihood-based tests of topologies in phylogenetics. Syst Biol 49:652-670.
    • (2000) Syst Biol , vol.49 , pp. 652-670
    • Goldman, N.1    Anderson, J.P.2    Rodrigo, A.G.3
  • 48
    • 26444482460 scopus 로고    scopus 로고
    • Molecular phylogeny and divergence times of deuterostome animals
    • Blair JE, Hedges SB (2005) Molecular phylogeny and divergence times of deuterostome animals. Mol Biol Evol 22:2275-2284.
    • (2005) Mol Biol Evol , vol.22 , pp. 2275-2284
    • Blair, J.E.1    Hedges, S.B.2
  • 49
    • 34147130163 scopus 로고    scopus 로고
    • Time scale for cyclostome evolution inferred with a phylogenetic diagnosis of hagfish and lamprey cDNA sequences
    • Kuraku S, Kuratani S (2006) Time scale for cyclostome evolution inferred with a phylogenetic diagnosis of hagfish and lamprey cDNA sequences. Zoolog Sci 23:1053-1064.
    • (2006) Zoolog Sci , vol.23 , pp. 1053-1064
    • Kuraku, S.1    Kuratani, S.2
  • 50
    • 0015522422 scopus 로고
    • Studies on hemoglobin from the hagfish Epatatretus burgeri
    • Bannai S, Sugita Y, Yoneyama Y (1972) Studies on hemoglobin from the hagfish Epatatretus burgeri. J Biol Chem 247:505-510.
    • (1972) J Biol Chem , vol.247 , pp. 505-510
    • Bannai, S.1    Sugita, Y.2    Yoneyama, Y.3
  • 52
    • 0022806770 scopus 로고
    • Molecular models for the putative dimer of sea lamprey hemoglobin
    • Honzatko RB, Hendrickson WA (1986) Molecular models for the putative dimer of sea lamprey hemoglobin. Proc Natl Acad Sci USA 83:8487-8491.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8487-8491
    • Honzatko, R.B.1    Hendrickson, W.A.2
  • 53
    • 0032052760 scopus 로고    scopus 로고
    • Self-association, cooperativity and supercooperativity of oxygen binding by hemoglobins
    • Riggs AF (1998) Self-association, cooperativity and supercooperativity of oxygen binding by hemoglobins. J Exp Biol 201:1073-1084.
    • (1998) J Exp Biol , vol.201 , pp. 1073-1084
    • Riggs, A.F.1
  • 54
    • 34548520171 scopus 로고    scopus 로고
    • The 2.7 a crystal structure of deoxygenated hemoglobin from the sea lamprey (Petromyzon marinus): Structural basis for a lowered oxygen affinity and Bohr effect
    • Heaslet HA, Royer WEJ, Jr (1999) The 2.7 A crystal structure of deoxygenated hemoglobin from the sea lamprey (Petromyzon marinus): Structural basis for a lowered oxygen affinity and Bohr effect. Structure 7:517-526.
    • (1999) Structure , vol.7 , pp. 517-526
    • Heaslet, H.A.1    Royer Jr., W.E.J.2
  • 55
    • 0037077231 scopus 로고    scopus 로고
    • Crystal structures of deoxy- And carbonmonoxyhemoglobin F1 from the hagfish Eptatretus burgeri
    • Mito M, et al. (2002) Crystal structures of deoxy- and carbonmonoxyhemoglobin F1 from the hagfish Eptatretus burgeri. J Biol Chem 277:21898-21905.
    • (2002) J Biol Chem , vol.277 , pp. 21898-21905
    • Mito, M.1
  • 56
    • 2542450912 scopus 로고    scopus 로고
    • Structural basis of human cytoglobin for ligand binding
    • Sugimoto H, et al. (2004) Structural basis of human cytoglobin for ligand binding. J Mol Biol 339:873-885.
    • (2004) J Mol Biol , vol.339 , pp. 873-885
    • Sugimoto, H.1
  • 57
    • 33744468238 scopus 로고    scopus 로고
    • High-resolution structure of human cytoglobin: Identification of extra N- And C-termini and a new dimerization mode
    • Makino M, et al. (2006) High-resolution structure of human cytoglobin: Identification of extra N- and C-termini and a new dimerization mode. Acta Crystallogr D Biol Crystallogr 62:671-677.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 671-677
    • Makino, M.1
  • 58
    • 7944219982 scopus 로고    scopus 로고
    • The Bohr effect of haemoglobin in vertebrates: An example of molecular adaptation to different physiological requirements
    • Giardina B, Mosca D, De Rosa MC (2004) The Bohr effect of haemoglobin in vertebrates: An example of molecular adaptation to different physiological requirements. Acta Physiol Scand 182:229-244.
    • (2004) Acta Physiol Scand , vol.182 , pp. 229-244
    • Giardina, B.1    Mosca, D.2    De Rosa, M.C.3
  • 59
    • 7944237674 scopus 로고    scopus 로고
    • Red blood cell pH, the Bohr effect, and other oxygenation-linked phenomena in blood O2 and CO2 transport
    • Jensen FB (2004) Red blood cell pH, the Bohr effect, and other oxygenation-linked phenomena in blood O2 and CO2 transport. Acta Physiol Scand 182:215-227.
    • (2004) Acta Physiol Scand , vol.182 , pp. 215-227
    • Jensen, F.B.1
  • 60
    • 0027458791 scopus 로고
    • Haemoglobin function in intact Lampetra fluviatilis erythrocytes
    • Nikinmaa M (1993) Haemoglobin function in intact Lampetra fluviatilis erythrocytes. Respir Physiol 91:283-293.
    • (1993) Respir Physiol , vol.91 , pp. 283-293
    • Nikinmaa, M.1
  • 61
    • 0006571672 scopus 로고    scopus 로고
    • eds Jørgensen JM, Lomholt JP, Weber RE, Malte H (Chapman & Hall, London)
    • Fago A, Weber RE (1998) The Biology of Hagfishes, eds Jørgensen JM, Lomholt JP, Weber RE, Malte H (Chapman & Hall, London), pp 321-329.
    • (1998) The Biology of Hagfishes , pp. 321-329
    • Fago, A.1    Weber, R.E.2
  • 62
    • 0033036755 scopus 로고    scopus 로고
    • Bicarbonate binding to hemoglobin links oxygen and carbon dioxide transport in hagfish
    • Fago A, Malte H, Dohn N (1999) Bicarbonate binding to hemoglobin links oxygen and carbon dioxide transport in hagfish. Respir Physiol 115:309-315.
    • (1999) Respir Physiol , vol.115 , pp. 309-315
    • Fago, A.1    Malte, H.2    Dohn, N.3
  • 63
    • 0032774667 scopus 로고    scopus 로고
    • Haemoglobin H+ equilibria in lamprey (Lampetra fluviatilis) and hagfish (Myxine glutinosa)
    • Jensen FB (1999) Haemoglobin H+ equilibria in lamprey (Lampetra fluviatilis) and hagfish (Myxine glutinosa). J Exp Biol 202:1963-1968.
    • (1999) J Exp Biol , vol.202 , pp. 1963-1968
    • Jensen, F.B.1
  • 65
    • 38549135938 scopus 로고    scopus 로고
    • Alignment uncertainty and genomic analysis
    • Wong KM, Suchard MA, Huelsenbeck JP (2008) Alignment uncertainty and genomic analysis. Science 319:473-476.
    • (2008) Science , vol.319 , pp. 473-476
    • Wong, K.M.1    Suchard, M.A.2    Huelsenbeck, J.P.3
  • 66
    • 3242891684 scopus 로고    scopus 로고
    • DIALIGN: Multiple DNA and protein sequence alignment at BiBiServ
    • Web Server issue
    • Morgenstern B (2004) DIALIGN: Multiple DNA and protein sequence alignment at BiBiServ. Nucleic Acids Res 32 (Web Server issue):W33-W36.
    • (2004) Nucleic Acids Res , vol.32
    • Morgenstern, B.1
  • 67
    • 63349085641 scopus 로고    scopus 로고
    • Kalign2: High-performance multiple alignment of protein and nucleotide sequences allowing external features
    • Lassmann T, Frings O, Sonnhammer ELL (2009) Kalign2: High-performance multiple alignment of protein and nucleotide sequences allowing external features. Nucleic Acids Res 37:858-865.
    • (2009) Nucleic Acids Res , vol.37 , pp. 858-865
    • Lassmann, T.1    Frings, O.2    Sonnhammer, E.L.L.3
  • 68
    • 45949107473 scopus 로고    scopus 로고
    • Recent developments in the MAFFT multiple sequence alignment program
    • Katoh K, Toh H (2008) Recent developments in the MAFFT multiple sequence alignment program. Brief Bioinform 9:286-298.
    • (2008) Brief Bioinform , vol.9 , pp. 286-298
    • Katoh, K.1    Toh, H.2
  • 69
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar RC (2004) MUSCLE: Multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32:1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 70
    • 23044471766 scopus 로고    scopus 로고
    • An algorithm for progressive multiple alignment of sequences with insertions
    • Löytynoja A, Goldman N (2005) An algorithm for progressive multiple alignment of sequences with insertions. Proc Natl Acad Sci USA 102:10557-10562.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 10557-10562
    • Löytynoja, A.1    Goldman, N.2
  • 71
    • 34547567393 scopus 로고    scopus 로고
    • EProbalign: Generation and manipulation of multiple sequence alignments using partition function posterior probabilities
    • Web Server issue
    • Chikkagoudar S, Roshan U, Livesay D (2007) eProbalign: Generation and manipulation of multiple sequence alignments using partition function posterior probabilities. Nucleic Acids Res 35 (Web Server issue):W675-W677.
    • (2007) Nucleic Acids Res , vol.35
    • Chikkagoudar, S.1    Roshan, U.2    Livesay, D.3
  • 72
    • 14644430471 scopus 로고    scopus 로고
    • ProbCons: Probabilistic consistency-based multiple sequence alignment
    • Do CB, Mahabhashyam MSP, Brudno M, Batzoglou S (2005) ProbCons: Probabilistic consistency-based multiple sequence alignment. Genome Res 15:330-340.
    • (2005) Genome Res , vol.15 , pp. 330-340
    • Do, C.B.1    Mahabhashyam, M.S.P.2    Brudno, M.3    Batzoglou, S.4
  • 73
    • 48449087960 scopus 로고    scopus 로고
    • PROMALS3D web server for accurate multiple protein sequence and structure alignments
    • Web Server issue
    • Pei J, Tang M, Grishin NV (2008) PROMALS3D web server for accurate multiple protein sequence and structure alignments. Nucleic Acids Res 36 (Web Server issue):W30-W34.
    • (2008) Nucleic Acids Res , vol.36
    • Pei, J.1    Tang, M.2    Grishin, N.V.3
  • 74
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones DT, Taylor WR, Thornton JM (1992) The rapid generation of mutation data matrices from protein sequences. Comput Appl Biosci 8:275-282.
    • (1992) Comput Appl Biosci , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 75
    • 45849154166 scopus 로고    scopus 로고
    • An improved general amino acid replacement matrix
    • Le SQ, Gascuel O (2008) An improved general amino acid replacement matrix. Mol Biol Evol 25:1307-1320.
    • (2008) Mol Biol Evol , vol.25 , pp. 1307-1320
    • Le, S.Q.1    Gascuel, O.2
  • 76
    • 13444259388 scopus 로고    scopus 로고
    • TREEFINDE3R: A powerful graphical analysis environment for molecular phylogenetics
    • Jobb G, von Haeseler A, Strimmer K (2004) TREEFINDE3R: A powerful graphical analysis environment for molecular phylogenetics. BMC Evol Biol 4:18.
    • (2004) BMC Evol Biol , vol.4 , pp. 18
    • Jobb, G.1    Von Haeseler, A.2    Strimmer, K.3
  • 77
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • Ronquist F, Huelsenbeck JP (2003) MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19:1572-1574.
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 78
    • 70350495471 scopus 로고    scopus 로고
    • eds Kumar S, Hedges S (Oxford University Press, Oxford, UK)
    • Hedges S (2009) The Timetree of Life, eds Kumar S, Hedges S (Oxford University Press, Oxford, UK), pp 309-314.
    • (2009) The Timetree of Life , pp. 309-314
    • Hedges, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.