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Volumn 29, Issue 11, 2012, Pages 3553-3561

Widespread occurrence of N-terminal acylation in animal globins and possible origin of respiratory globins from a membrane-bound ancestor

Author keywords

acylation; adaptive evolution; cytoglobin; gene duplication; hemoglobin; neuroglobin

Indexed keywords

CYTOGLOBIN; GLOBIN; GLOBIN E; GLOBIN Y; HEMOGLOBIN; MYOGLOBIN; UNCLASSIFIED DRUG;

EID: 84867830765     PISSN: 07374038     EISSN: 15371719     Source Type: Journal    
DOI: 10.1093/molbev/mss164     Document Type: Article
Times cited : (45)

References (68)
  • 1
    • 33745256005 scopus 로고    scopus 로고
    • Approximate likelihood-ratio test for branches: A fast, accurate, and powerful alternative
    • Anisimova M, Gascuel O. 2006. Approximate likelihood-ratio test for branches: a fast, accurate, and powerful alternative. Syst Biol. 55: 539-552.
    • (2006) Syst Biol , vol.55 , pp. 539-552
    • Anisimova, M.1    Gascuel, O.2
  • 2
    • 84863576090 scopus 로고    scopus 로고
    • The bilatarian sea urchin and the radial starlet sea anemone globins share strong homologies with vertebrate neuroglobins
    • Bolognesi M, di Prisco G, Verde C, editors New York: Springer
    • Bailly X, Vinogradov S. 2008. The bilatarian sea urchin and the radial starlet sea anemone globins share strong homologies with vertebrate neuroglobins. In: Bolognesi M, di Prisco G, Verde C, editors. Dioxygen binding and sensing proteins: a tribute to Beatrice and Jonathan Wittenberg. New York: Springer. p. 191-201.
    • (2008) Dioxygen Binding and Sensing Proteins: A Tribute to Beatrice and Jonathan Wittenberg , pp. 191-201
    • Bailly, X.1    Vinogradov, S.2
  • 3
    • 20144378666 scopus 로고    scopus 로고
    • Divergent distribution in vascular and avascular mammalian retinae links neuroglobin to cellular respiration
    • Bentmann A, Schmidt M, Reuss S, Wolfrum U, Hankeln T, Burmester T. 2005. Divergent distribution in vascular and avascular mammalian retinae links neuroglobin to cellular respiration. J Biol Chem. 280: 20660-20665.
    • (2005) J Biol Chem , vol.280 , pp. 20660-20665
    • Bentmann, A.1    Schmidt, M.2    Reuss, S.3    Wolfrum, U.4    Hankeln, T.5    Burmester, T.6
  • 4
    • 79960662890 scopus 로고    scopus 로고
    • Oxygen supply from the bird's eye perspective: Globin e is a respiratory protein in the chicken retina
    • Blank M, Kiger L, Thielebein A, Gerlach F, Hankeln T, Marden MC, Burmester T. 2011. Oxygen supply from the bird's eye perspective: globin E is a respiratory protein in the chicken retina. J Biol Chem. 286:26507-26515.
    • (2011) J Biol Chem , vol.286 , pp. 26507-26515
    • Blank, M.1    Kiger, L.2    Thielebein, A.3    Gerlach, F.4    Hankeln, T.5    Marden, M.C.6    Burmester, T.7
  • 6
    • 2942564436 scopus 로고    scopus 로고
    • N-terminal myristoylation predictions by ensembles of neural networks
    • Bologna G, Yvon C, Duvaud S, Veuthey AL. 2004. N-terminal myristoylation predictions by ensembles of neural networks. Proteomics 4: 1626-1632.
    • (2004) Proteomics , vol.4 , pp. 1626-1632
    • Bologna, G.1    Yvon, C.2    Duvaud, S.3    Veuthey, A.L.4
  • 8
    • 0038629108 scopus 로고    scopus 로고
    • Interaction with membrane lipids and heme ligand binding properties of Escherichia coli flavohemoglobin
    • Bonamore A, Farina A, Gattoni M, Schinina ME, Bellelli A, Boffi A. 2003. Interaction with membrane lipids and heme ligand binding properties of Escherichia coli flavohemoglobin. Biochemistry 42: 5792-5801.
    • (2003) Biochemistry , vol.42 , pp. 5792-5801
    • Bonamore, A.1    Farina, A.2    Gattoni, M.3    Schinina, M.E.4    Bellelli, A.5    Boffi, A.6
  • 9
    • 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
  • 11
    • 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
  • 13
    • 33745599891 scopus 로고    scopus 로고
    • Multiple sequence elements facilitate Chp Rho GTPase subcellular location, membrane association, and transforming activity
    • Chenette EJ, Mitin NY, Der CJ. 2006. Multiple sequence elements facilitate Chp Rho GTPase subcellular location, membrane association, and transforming activity. Mol Biol Cell. 17:3108-3121.
    • (2006) Mol Biol Cell , vol.17 , pp. 3108-3121
    • Chenette, E.J.1    Mitin, N.Y.2    Der, C.J.3
  • 14
    • 42949117860 scopus 로고    scopus 로고
    • Globin interactions with lipids and membranes
    • Di Giulio A, Bonamore A. 2008. Globin interactions with lipids and membranes. Methods Enzymol. 436:239-253.
    • (2008) Methods Enzymol , vol.436 , pp. 239-253
    • Di Giulio, A.1    Bonamore, A.2
  • 16
    • 80054065944 scopus 로고    scopus 로고
    • Phylogenetic analysis reveals wide distribution of globin X
    • Dröge J, Makalowski W. 2011. Phylogenetic analysis reveals wide distribution of globin X. Biol Direct. 6:54.
    • (2011) Biol Direct , vol.6 , pp. 54
    • Dröge, J.1    Makalowski, W.2
  • 17
    • 0042335879 scopus 로고    scopus 로고
    • Globin genes are present in Ciona intestinalis
    • Ebner B, Burmester T, Hankeln T. 2003. Globin genes are present in Ciona intestinalis. Mol Biol Evol. 20:1521-1525.
    • (2003) Mol Biol Evol , vol.20 , pp. 1521-1525
    • Ebner, B.1    Burmester, T.2    Hankeln, T.3
  • 19
    • 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
  • 20
    • 79952796717 scopus 로고    scopus 로고
    • A membranebound hemoglobin from gills of the green shore crab Carcinus maenas
    • Ertas B, Kiger L, Blank M,MardenMC, Burmester T. 2011. A membranebound hemoglobin from gills of the green shore crab Carcinus maenas. J Biol Chem. 286:3185-3193.
    • (2011) J Biol Chem , vol.286 , pp. 3185-3193
    • Ertas, B.1    Kiger, L.2    Blank, M.3    Marden, M.C.4    Burmester, T.5
  • 22
    • 0035955697 scopus 로고    scopus 로고
    • The biology and enzymology of protein N-myristoylation
    • Farazi TA,Waksman G, Gordon JI. 2001. The biology and enzymology of protein N-myristoylation. J Biol Chem. 276:39501-39504.
    • (2001) J Biol Chem , vol.276 , pp. 39501-39504
    • Farazi, T.A.1    Waksman, G.2    Gordon, J.I.3
  • 23
    • 10444268100 scopus 로고    scopus 로고
    • Globin-coupled sensors, protoglobins, and the last universal common ancestor: Hemediatomic interactions, Part 1
    • Freitas TAK, Saito JA, Hou S, Alam M. 2005. Globin-coupled sensors, protoglobins, and the last universal common ancestor: hemediatomic interactions, Part 1. J Inorg Biochem. 99:23-33.
    • (2005) J Inorg Biochem , vol.99 , pp. 23-33
    • Freitas, T.A.K.1    Saito, J.A.2    Hou, S.3    Alam, M.4
  • 24
    • 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
  • 26
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximumlikelihood phylogenies: Assessing the performance of PhyML 3.0
    • Guindon S, Dufayard JF, Lefort V, Anisimova M, Hordijk W, Gascuel O. 2010. New algorithms and methods to estimate maximumlikelihood phylogenies: assessing the performance of PhyML 3.0. Syst Biol. 59:307-321.
    • (2010) Syst Biol , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6
  • 27
    • 10444267310 scopus 로고    scopus 로고
    • Neuroglobin and cytoglobin in search of their role in the vertebrate globin family
    • (23 co-authors)
    • Hankeln T, Ebner B, Fuchs C, et al. (23 co-authors). 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    Ebner, B.2    Fuchs, C.3
  • 28
    • 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
  • 29
    • 0029893918 scopus 로고    scopus 로고
    • A brief history of hemoglobins: Plant, animal, protist, and bacteria
    • Hardison RC. 1996. A brief history of hemoglobins: plant, animal, protist, and bacteria. Proc Natl Acad Sci USA. 93:5675-5679.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5675-5679
    • Hardison, R.C.1
  • 31
    • 77956272960 scopus 로고    scopus 로고
    • Gene cooption and convergent evolution of oxygen transport hemoglobins in jawed and jawless vertebrates
    • Hoffmann FG, Opazo JC, Storz JF. 2010. Gene cooption and convergent evolution of oxygen transport hemoglobins in jawed and jawless vertebrates. Proc Natl Acad Sci USA. 107: 14274-14279.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 14274-14279
    • Hoffmann, F.G.1    Opazo, J.C.2    Storz, J.F.3
  • 32
    • 84856397079 scopus 로고    scopus 로고
    • Differential loss and retention of cytoglobin, myoglobin, and globin-E during the radiation of vertebrates
    • Hoffmann FG, Opazo JC, Storz JF. 2011. Differential loss and retention of cytoglobin, myoglobin, and globin-E during the radiation of vertebrates. Genome Biol Evol. 3:588-600.
    • (2011) Genome Biol Evol , vol.3 , pp. 588-600
    • Hoffmann, F.G.1    Opazo, J.C.2    Storz, J.F.3
  • 33
    • 84861376715 scopus 로고    scopus 로고
    • Whole-genome duplications spurred the functional diversification of the globin gene superfamily in vertebrates
    • Hoffmann FG, Opazo JC, Storz JF. 2012. Whole-genome duplications spurred the functional diversification of the globin gene superfamily in vertebrates. Mol Biol Evol. 29:303-312.
    • (2012) Mol Biol Evol , vol.29 , pp. 303-312
    • Hoffmann, F.G.1    Opazo, J.C.2    Storz, J.F.3
  • 36
    • 0034849408 scopus 로고    scopus 로고
    • MRBAYES: Bayesian inference of phylogenetic trees
    • Huelsenbeck JP, Ronquist F. 2001. MRBAYES: Bayesian inference of phylogenetic trees. Bioinformatics 17:754-755.
    • (2001) Bioinformatics , vol.17 , pp. 754-755
    • Huelsenbeck, J.P.1    Ronquist, F.2
  • 37
    • 82555187208 scopus 로고    scopus 로고
    • Neuroglobin-deficiency exacerbates Hif1A and c-FOS response, but does not affect neuronal survival during severe hypoxia in vivo
    • Hundahl CA, Luuk H, Ilmjarv S, Falktoft B, Raida Z, Vikesaa J, Friis-Hansen L, Hay-Schmidt A. 2011. Neuroglobin-deficiency exacerbates Hif1A and c-FOS response, but does not affect neuronal survival during severe hypoxia in vivo. PLoS One 6:e28160.
    • (2011) PLoS One , vol.6
    • Hundahl, C.A.1    Luuk, H.2    Ilmjarv, S.3    Falktoft, B.4    Raida, Z.5    Vikesaa, J.6    Friis-Hansen, L.7    Hay-Schmidt, A.8
  • 38
    • 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
  • 39
    • 13744252890 scopus 로고    scopus 로고
    • MAFFT version 5: Improvement in accuracy of multiple sequence alignment
    • Katoh K, Kuma K, Toh H, Miyata T. 2005. MAFFT version 5: improvement in accuracy of multiple sequence alignment. Nucleic Acids Res. 33:511-518.
    • (2005) Nucleic Acids Res , vol.33 , pp. 511-518
    • Katoh, K.1    Kuma, K.2    Toh, H.3    Miyata, T.4
  • 40
    • 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
  • 41
    • 0035816696 scopus 로고    scopus 로고
    • Characterization of a stellate cell activationassociated protein (STAP) with peroxidase activity found in rat hepatic stellate cells
    • Kawada N, Kristensen DB, Asahina K, Nakatani K,Minamiyama Y, Seki S, Yoshizato K. 2001. Characterization of a stellate cell activationassociated 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    Kristensen, D.B.2    Asahina, K.3    Nakatani, K.4    Minamiyama, Y.5    Seki, S.6    Yoshizato, K.7
  • 42
    • 36448991500 scopus 로고    scopus 로고
    • Clustal W and Clustal X version 2.0
    • (13 co-authors)
    • Larkin MA, Blackshields G, Brown NP, et al. (13 co-authors). 2007. Clustal W and Clustal X version 2.0. Bioinformatics 23: 2947-2948.
    • (2007) Bioinformatics , vol.23 , pp. 2947-2948
    • Larkin, M.A.1    Blackshields, G.2    Brown, N.P.3
  • 43
    • 31144442881 scopus 로고    scopus 로고
    • Automatic assessment of alignment quality
    • Lassmann T, Sonnhammer EL. 2005. Automatic assessment of alignment quality. Nucleic Acids Res. 33:7120-7128.
    • (2005) Nucleic Acids Res , vol.33 , pp. 7120-7128
    • Lassmann, T.1    Sonnhammer, E.L.2
  • 44
    • 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
  • 45
    • 33845794047 scopus 로고    scopus 로고
    • Palmitoylation: Policing protein stability and traffic
    • Linder ME, Deschenes RJ. 2007. Palmitoylation: policing protein stability and traffic. Nat Rev Mol Cell Biol. 8:74-84.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 74-84
    • Linder, M.E.1    Deschenes, R.J.2
  • 46
    • 1642327485 scopus 로고    scopus 로고
    • Truncated hemoglobin o of Mycobacterium tuberculosis: The oligomeric state change and the interaction with membrane components
    • Liu C, He Y, Chang Z. 2004. Truncated hemoglobin o of Mycobacterium tuberculosis: the oligomeric state change and the interaction with membrane components. Biochem Biophys Res Commun. 316: 1163-1172.
    • (2004) Biochem Biophys Res Commun , vol.316 , pp. 1163-1172
    • Liu, C.1    He, Y.2    Chang, Z.3
  • 47
    • 78651285748 scopus 로고    scopus 로고
    • CDD: A conserved domain database for the functional annotation of proteins
    • (27 co-authors)
    • Marchler-Bauer A, Lu S, Anderson JB, et al. (27 co-authors). 2011. CDD: a conserved domain database for the functional annotation of proteins. Nucleic Acids Res. 39:D225-D229.
    • (2011) Nucleic Acids Res , vol.39
    • Marchler-Bauer, A.1    Lu, S.2    Anderson, J.B.3
  • 48
    • 0036290648 scopus 로고    scopus 로고
    • N-terminal N-myristoylation of proteins: Prediction of substrate proteins from amino acid sequence
    • Maurer-Stroh S, Eisenhaber B, Eisenhaber F. 2002. N-terminal N-myristoylation of proteins: prediction of substrate proteins from amino acid sequence. J Mol Biol. 317:541-557.
    • (2002) J Mol Biol , vol.317 , pp. 541-557
    • Maurer-Stroh, S.1    Eisenhaber, B.2    Eisenhaber, F.3
  • 50
    • 69249208538 scopus 로고    scopus 로고
    • When the brain goes diving: Glial oxidative metabolism may confer hypoxia tolerance to the seal brain
    • Mitz SA, Reuss S, Folkow LP, Blix AS, Ramirez JM, Hankeln T, Burmester T. 2009. When the brain goes diving: glial oxidative metabolism may confer hypoxia tolerance to the seal brain. Neuroscience 163: 552-560.
    • (2009) Neuroscience , vol.163 , pp. 552-560
    • Mitz, S.A.1    Reuss, S.2    Folkow, L.P.3    Blix, A.S.4    Ramirez, J.M.5    Hankeln, T.6    Burmester, T.7
  • 51
    • 0031571632 scopus 로고    scopus 로고
    • Electrostatic interaction of myristoylated proteins with membranes: Simple physics, complicated biology
    • Murray D, Ben-Tal N, Honig B, McLaughlin S. 1997. Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology. Structure 5:985-989.
    • (1997) Structure , vol.5 , pp. 985-989
    • Murray, D.1    Ben-Tal, N.2    Honig, B.3    McLaughlin, S.4
  • 52
    • 34848907786 scopus 로고    scopus 로고
    • Protein lipidation
    • Nadolski MJ, Linder ME. 2007. Protein lipidation. FEBS J. 274: 5202-5210.
    • (2007) FEBS J , vol.274 , pp. 5202-5210
    • Nadolski, M.J.1    Linder, M.E.2
  • 54
    • 0034623005 scopus 로고    scopus 로고
    • T-coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame C, Higgins DG, Heringa J. 2000. T-coffee: a novel method for fast and accurate multiple sequence alignment. J Mol Biol. 302: 205-217.
    • (2000) J Mol Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 55
    • 42449090264 scopus 로고    scopus 로고
    • PROMALS3D: A tool for multiple protein sequence and structure alignments
    • Pei J, Kim BH, Grishin NV. 2008. PROMALS3D: a tool for multiple protein sequence and structure alignments. Nucleic Acids Res. 36: 2295-2300.
    • (2008) Nucleic Acids Res , vol.36 , pp. 2295-2300
    • Pei, J.1    Kim, B.H.2    Grishin, N.V.3
  • 56
    • 0018654083 scopus 로고
    • Regulation of oxygen affinity of hemoglobin: Influence of structure of the globin on the heme iron
    • Perutz MF. 1979. Regulation of oxygen affinity of hemoglobin: influence of structure of the globin on the heme iron. Annu Rev Biochem. 48: 327-386.
    • (1979) Annu Rev Biochem , vol.48 , pp. 327-386
    • Perutz, M.F.1
  • 59
    • 79952144810 scopus 로고    scopus 로고
    • Lipid binding to cytoglobin leads to a change in heme coordination: A role for cytoglobin in lipid signalling of oxidative stress
    • Reeder BJ, Svistunenko D, Wilson M. 2011. Lipid binding to cytoglobin leads to a change in heme coordination: a role for cytoglobin in lipid signalling of oxidative stress. Biochem J. 43:483-492.
    • (2011) Biochem J , vol.43 , pp. 483-492
    • Reeder, B.J.1    Svistunenko, D.2    Wilson, M.3
  • 60
    • 54249148026 scopus 로고    scopus 로고
    • CSS-Palm 2.0: An updated software for palmitoylation sites prediction
    • Ren J,Wen L, Gao X, Jin C, Xue Y, Yao X. 2008. CSS-Palm 2.0: an updated software for palmitoylation sites prediction. Protein Eng Des Sel. 21: 639-644.
    • (2008) Protein Eng des Sel , vol.21 , pp. 639-644
    • Ren, J.1    Wen, L.2    Gao, X.3    Jin, C.4    Xue, Y.5    Yao, X.6
  • 61
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh MD. 1999. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim Biophy Acta. 1451:1-16.
    • (1999) Biochim Biophy Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 63
    • 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
  • 64
    • 10744220623 scopus 로고    scopus 로고
    • Cytoglobin is a respiratory protein in connective tissue and neurons, which is up-regulated by hypoxia
    • (11 co-authors)
    • Schmidt M, Gerlach F, Avivi A, et al. (11 co-authors). 2004. Cytoglobin is a respiratory protein in connective tissue and neurons, which is up-regulated by hypoxia. J Biol Chem. 279:8063-8069.
    • (2004) J Biol Chem , vol.279 , pp. 8063-8069
    • Schmidt, M.1    Gerlach, F.2    Avivi, A.3
  • 65
    • 79958043184 scopus 로고    scopus 로고
    • Phylogenetic diversification of the globin gene superfamily in chordates
    • Storz JF, Opazo JC, Hoffmann FG. 2011. Phylogenetic diversification of the globin gene superfamily in chordates. IUBMB Life 63:313-322.
    • (2011) IUBMB Life , vol.63 , pp. 313-322
    • Storz, J.F.1    Opazo, J.C.2    Hoffmann, F.G.3
  • 66
    • 0037205447 scopus 로고    scopus 로고
    • A ubiquitously expressed human hexacoordinate hemoglobin
    • Trent JT, 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, J.T.1    Hargrove, M.S.2
  • 67
    • 0035066385 scopus 로고    scopus 로고
    • Nonvertebrate hemoglobins: Functions and molecular adaptations
    • Weber RE, Vinogradov SN. 2001. Nonvertebrate hemoglobins: functions and molecular adaptations. Physiol Rev. 81:569-628.
    • (2001) Physiol Rev , vol.81 , pp. 569-628
    • Weber, R.E.1    Vinogradov, S.N.2
  • 68
    • 0035031966 scopus 로고    scopus 로고
    • A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach
    • Whelan S, Goldman N. 2001. A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach. Mol Biol Evol. 18:691-699.
    • (2001) Mol Biol Evol , vol.18 , pp. 691-699
    • Whelan, S.1    Goldman, N.2


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