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Volumn 2, Issue 6, 2011, Pages

The Escherichia coli protein YfeX functions as a porphyrinogen oxidase, not a heme dechelatase

Author keywords

[No Author keywords available]

Indexed keywords

COPROPORPHYRINOGEN; DYE DECOLORIZING PEROXIDASE; ESCHERICHIA COLI PROTEIN; IRON; PEROXIDASE; PROTEIN YFEX; PROTOPORPHYRIN; PROTOPORPHYRINOGEN OXIDASE; UNCLASSIFIED DRUG; ALIZARIN; ANTHRAQUINONE DERIVATIVE; CATION TRANSPORT PROTEIN; CIBACRON BLUE F 3GA; HEME; OXIDOREDUCTASE; PORPHYRINOGEN; PYROGALLOL; TRIAZINE DERIVATIVE; YFEX PROTEIN, E COLI;

EID: 84855228484     PISSN: None     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00248-11     Document Type: Article
Times cited : (46)

References (49)
  • 1
    • 67349235552 scopus 로고    scopus 로고
    • DyP-type peroxidases comprise a novel heme peroxidase family
    • Sugano Y. 2009. DyP-type peroxidases comprise a novel heme peroxidase family. Cell. Mol. Life Sci. 66:1387-1403.
    • (2009) Cell. Mol. Life Sci , vol.66 , pp. 1387-1403
    • Sugano, Y.1
  • 2
    • 37549031745 scopus 로고    scopus 로고
    • DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family: ASP171 replaces the distal histidine of classical peroxidases
    • Sugano Y, Muramatsu R, Ichiyanagi A, Sato T, Shoda M. 2007. DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family: ASP171 replaces the distal histidine of classical peroxidases. J. Biol. Chem. 282:36652-36658.
    • (2007) J. Biol. Chem , vol.282 , pp. 36652-36658
    • Sugano, Y.1    Muramatsu, R.2    Ichiyanagi, A.3    Sato, T.4    Shoda, M.5
  • 3
    • 0022389495 scopus 로고
    • Purification and characterization of an extracellular Mn(II)-dependent peroxidase from the lignin-degrading basidi-omycete, Phanerochaete chrysosporium
    • Glenn JK, Gold MH. 1985. Purification and characterization of an extracellular Mn(II)-dependent peroxidase from the lignin-degrading basidi-omycete, Phanerochaete chrysosporium. Arch. Biochem. Biophys. 242: 329-341.
    • (1985) Arch. Biochem. Biophys , vol.242 , pp. 329-341
    • Glenn, J.K.1    Gold, M.H.2
  • 4
    • 0021519023 scopus 로고
    • 2-requiring diarylpropane oxy-genase from the white rot basidiomycete, Phanerochaete chrysosporium
    • Gold MH, Kuwahara M, Chiu AA, Glenn JK. 1984. Purification and characterization of an extracellular H2O2-requiring diarylpropane oxy-genase from the white rot basidiomycete, Phanerochaete chrysosporium. Arch. Biochem. Biophys. 234:353-362.
    • (1984) Arch. Biochem. Biophys , vol.234 , pp. 353-362
    • Gold, M.H.1    Kuwahara, M.2    Chiu, A.A.3    Glenn, J.K.4
  • 5
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxi-dases
    • Welinder KG. 1992. Superfamily of plant, fungal and bacterial peroxi-dases. Curr. Opin. Struct. Biol. 2:388-393.
    • (1992) Curr. Opin. Struct. Biol , vol.2 , pp. 388-393
    • Welinder, K.G.1
  • 6
    • 79955445197 scopus 로고    scopus 로고
    • Crystal structure and biochemical features of EfeB/ YcdB from Escherichia coli O157: ASP235 plays divergent roles in different enzyme-catalyzed processes
    • Liu X, et al. 2011. Crystal structure and biochemical features of EfeB/ YcdB from Escherichia coli O157: ASP235 plays divergent roles in different enzyme-catalyzed processes. J. Biol. Chem. 286:14922-14931.
    • (2011) J. Biol. Chem , vol.286 , pp. 14922-14931
    • Liu, X.1
  • 7
    • 72949091861 scopus 로고    scopus 로고
    • Molecular characterization of a novel peroxidase from the cyanobacterium Anabaena sp. strain PCC 7120
    • Ogola HJ, et al. 2009. Molecular characterization of a novel peroxidase from the cyanobacterium Anabaena sp. strain PCC 7120. Appl. Environ. Microbiol. 75:7509-7518.
    • (2009) Appl. Environ. Microbiol , vol.75 , pp. 7509-7518
    • Ogola, H.J.1
  • 8
    • 34548810845 scopus 로고    scopus 로고
    • Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA
    • Zubieta C, et al. 2007. Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA. Proteins 69: 234-243.
    • (2007) Proteins , vol.69 , pp. 234-243
    • Zubieta, C.1
  • 9
    • 79953889758 scopus 로고    scopus 로고
    • Chlorite dismutases, DyPs, and EfeB: 3 microbial heme enzyme families comprise the CDE structural superfamily
    • Goblirsch B, Kurker RC, Streit BR, Wilmot CM, DuBois JL. 2011. Chlorite dismutases, DyPs, and EfeB: 3 microbial heme enzyme families comprise the CDE structural superfamily. J. Mol. Biol. 408:379-398.
    • (2011) J. Mol. Biol , vol.408 , pp. 379-398
    • Goblirsch, B.1    Kurker, R.C.2    Streit, B.R.3    Wilmot, C.M.4    Dubois, J.L.5
  • 10
    • 77956216729 scopus 로고    scopus 로고
    • Discovery and characterization of HemQ: An essential heme biosynthetic pathway component
    • Dailey TA, et al. 2010. Discovery and characterization of HemQ: an essential heme biosynthetic pathway component. J. Biol. Chem. 285: 25978-25986.
    • (2010) J. Biol. Chem , vol.285 , pp. 25978-25986
    • Dailey, T.A.1
  • 13
    • 77949416213 scopus 로고    scopus 로고
    • The IsdG-family of haem oxygenases degrades haem to a novel chromophore
    • Reniere ML, et al. 2010. The IsdG-family of haem oxygenases degrades haem to a novel chromophore. Mol. Microbiol. 75:1529-1538.
    • (2010) Mol. Microbiol , vol.75 , pp. 1529-1538
    • Reniere, M.L.1
  • 14
    • 0035949642 scopus 로고    scopus 로고
    • Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1
    • Schuller DJ, Zhu W, Stojiljkovic I, Wilks A, Poulos TL. 2001. Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1. Biochemistry 40:11552-11558.
    • (2001) Biochemistry , vol.40 , pp. 11552-11558
    • Schuller, D.J.1    Zhu, W.2    Stojiljkovic, I.3    Wilks, A.4    Poulos, T.L.5
  • 15
    • 77955215751 scopus 로고    scopus 로고
    • Porcine ferrochelatase: The relationship between iron-removal reaction and the conversion of heme to Zn-protoporphyrin
    • Chau TT, Ishigaki M, Kataoka T, Taketani S. 2010. Porcine ferrochelatase: the relationship between iron-removal reaction and the conversion of heme to Zn-protoporphyrin. Biosci. Biotechnol. Biochem. 74:1415-1420.
    • (2010) Biosci. Biotechnol. Biochem , vol.74 , pp. 1415-1420
    • Chau, T.T.1    Ishigaki, M.2    Kataoka, T.3    Taketani, S.4
  • 16
    • 0028147364 scopus 로고
    • Mammalian ferrochelatase. Expression and characterization of normal and two human protoporphy-ric ferrochelatases
    • Dailey HA, Sellers VM, Dailey TA. 1994. Mammalian ferrochelatase. Expression and characterization of normal and two human protoporphy-ric ferrochelatases. J. Biol. Chem. 269:390-395.
    • (1994) J. Biol. Chem , vol.269 , pp. 390-395
    • Dailey, H.A.1    Sellers, V.M.2    Dailey, T.A.3
  • 17
    • 0000385597 scopus 로고
    • Effect of diphenyl ether herbicides on oxidation of protoporphyrinogen to protoporphyrin in organellar and plasma membrane enriched fractions of barley
    • Jacobs JM, Jacobs NJ, Sherman TD, Duke SO. 1991. Effect of diphenyl ether herbicides on oxidation of protoporphyrinogen to protoporphyrin in organellar and plasma membrane enriched fractions of barley. Plant Physiol. 97:197-203.
    • (1991) Plant Physiol , vol.97 , pp. 197-203
    • Jacobs, J.M.1    Jacobs, N.J.2    Sherman, T.D.3    Duke, S.O.4
  • 18
    • 80055089802 scopus 로고    scopus 로고
    • The Heme-uptake Gene Cluster In Vibrio Fischeri is Regulated By Fur and Contributes to Symbiotic Colonization
    • In press
    • Septer AN, Wang Y, Ruby EG, Stabb EV, Dunn AK. The heme-uptake gene cluster in Vibrio fischeri is regulated by Fur and contributes to symbiotic colonization. Environ. Microbiol., in press.
    • Environ. Microbiol
    • Septer, A.N.1    Wang, Y.2    Ruby, E.G.3    Stab, E.V.4    Dunn, A.K.5
  • 19
    • 0030918517 scopus 로고    scopus 로고
    • Isolated Bacillus subtilis HemY has coproporphyrinogen III to copropor-phyrin III oxidase activity
    • Hansson M, Gustafsson MC, Kannangara CG, Hederstedt L. 1997. Isolated Bacillus subtilis HemY has coproporphyrinogen III to copropor-phyrin III oxidase activity. Biochim. Biophys. Acta 1340:97-104.
    • (1997) Biochim. Biophys. Acta , vol.1340 , pp. 97-104
    • Hansson, M.1    Gustafsson, M.C.2    Kannangara, C.G.3    Hederstedt, L.4
  • 20
    • 26444505976 scopus 로고    scopus 로고
    • Effect of RyhB small RNA on global iron use in Escherichia coli
    • Massé E, Vanderpool CK, Gottesman S. 2005. Effect of RyhB small RNA on global iron use in Escherichia coli. J. Bacteriol. 187:6962-6971.
    • (2005) J. Bacteriol , vol.187 , pp. 6962-6971
    • Massé, E.1    Vanderpool, C.K.2    Gottesman, S.3
  • 21
    • 0043032822 scopus 로고    scopus 로고
    • Global iron-dependent gene regulation in Escherichia coli. A new mechanism for iron homeostasis
    • McHugh JP, et al. 2003. Global iron-dependent gene regulation in Escherichia coli. A new mechanism for iron homeostasis. J. Biol. Chem. 278: 29478-29486.
    • (2003) J. Biol. Chem , vol.278 , pp. 29478-29486
    • McHugh, J.P.1
  • 22
    • 23944509113 scopus 로고    scopus 로고
    • Characterization of Vibrio cholerae RyhB: The RyhB regulon and role of ryhB in biofilm formation
    • Mey AR, Craig SA, Payne SM. 2005. Characterization of Vibrio cholerae RyhB: the RyhB regulon and role of ryhB in biofilm formation. Infect. Immun. 73:5706-5719.
    • (2005) Infect. Immun , vol.73 , pp. 5706-5719
    • Mey, A.R.1    Craig, S.A.2    Payne, S.M.3
  • 23
    • 28444438519 scopus 로고    scopus 로고
    • Iron and fur regulation in Vibrio cholerae and the role of fur in virulence
    • Mey AR, Wyckoff EE, Kanukurthy V, Fisher CR, Payne SM. 2005. Iron and fur regulation in Vibrio cholerae and the role of fur in virulence. Infect. Immun. 73:8167-8178.
    • (2005) Infect. Immun , vol.73 , pp. 8167-8178
    • Mey, A.R.1    Wyckoff, E.E.2    Kanukurthy, V.3    Fisher, C.R.4    Payne, S.M.5
  • 24
    • 0035982906 scopus 로고    scopus 로고
    • GeneChip expression analysis of the iron starvation response in Pseudomonas aeruginosa: Identification of novel pyoverdine biosynthesis genes
    • Ochsner UA, Wilderman PJ, Vasil AI, Vasil ML. 2002. GeneChip expression analysis of the iron starvation response in Pseudomonas aeruginosa: identification of novel pyoverdine biosynthesis genes. Mol. Microbiol. 45:1277-1287.
    • (2002) Mol. Microbiol , vol.45 , pp. 1277-1287
    • Ochsner, U.A.1    Wilderman, P.J.2    Vasil, A.I.3    Vasil, M.L.4
  • 25
    • 0027523116 scopus 로고
    • The Escherichia coli visA gene encodes ferrochelatase, the final enzyme of the heme biosynthetic pathway
    • Frustaci JM, O'Brian MR. 1993. The Escherichia coli visA gene encodes ferrochelatase, the final enzyme of the heme biosynthetic pathway. J. Bacteriol. 175:2154-2156.
    • (1993) J. Bacteriol , vol.175 , pp. 2154-2156
    • Frustaci, J.M.1    O'Brian, M.R.2
  • 26
    • 0024970331 scopus 로고
    • Protoporphyrinogen oxidase as a molecular target for diphenyl ether herbicides
    • Matringe M, Camadro JM, Labbe P, Scalla R. 1989. Protoporphyrinogen oxidase as a molecular target for diphenyl ether herbicides. Biochem. J. 260:231-235.
    • (1989) Biochem. J , vol.260 , pp. 231-235
    • Matringe, M.1    Camadro, J.M.2    Labbe, P.3    Scalla, R.4
  • 27
    • 84940927252 scopus 로고    scopus 로고
    • Protoporphyria
    • Kadish KM, Smith KM, Guilard R (ed.), Academic Press, New York, NY
    • Cox TM. 2003. Protoporphyria, p 121-150. In Kadish KM, Smith KM, Guilard R (ed.), The porphyrin handbook, vol 14. Academic Press, New York, NY.
    • (2003) The Porphyrin Handbook , vol.14 , pp. 121-150
    • Cox, T.M.1
  • 28
    • 69649083587 scopus 로고    scopus 로고
    • Porphyrin and nonpor-phyrin photosensitizers in oncology: Preclinical and clinical advances in photodynamic therapy
    • O'Connor AE, Gallagher WM, Byrne AT. 2009. Porphyrin and nonpor-phyrin photosensitizers in oncology: preclinical and clinical advances in photodynamic therapy. Photochem. Photobiol. 85:1053-1074.
    • (2009) Photochem. Photobiol , vol.85 , pp. 1053-1074
    • O'Connor, A.E.1    Gallagher, W.M.2    Byrne, A.T.3
  • 29
    • 12644252907 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae mutants defective in heme biosynthesis as a tool for studying the mechanism of phototoxicity of porphyrins
    • Zoładek T, Nguyen BN, Rytka J. 1996. Saccharomyces cerevisiae mutants defective in heme biosynthesis as a tool for studying the mechanism of phototoxicity of porphyrins. Photochem. Photobiol. 64:957-962.
    • (1996) Photochem. Photobiol , vol.64 , pp. 957-962
    • Zoładek, T.1    Nguyen, B.N.2    Rytka, J.3
  • 30
    • 23044503950 scopus 로고    scopus 로고
    • Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2
    • Cooperman SS, et al. 2005. Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2. Blood 106:1084-1091.
    • (2005) Blood , vol.106 , pp. 1084-1091
    • Cooperman, S.S.1
  • 31
    • 77954287921 scopus 로고    scopus 로고
    • Iron regulatory proteins secure mitochondrial iron sufficiency and function
    • Galy B, et al. 2010. Iron regulatory proteins secure mitochondrial iron sufficiency and function. CellMetab. 12:194-201.
    • (2010) CellMetab , vol.12 , pp. 194-201
    • Galy, B.1
  • 32
    • 23844555084 scopus 로고    scopus 로고
    • Characterization of pES213, a small mobilizable plasmid from Vibrio fischeri
    • Dunn AK, Martin MO, Stabb EV. 2005. Characterization of pES213, a small mobilizable plasmid from Vibrio fischeri. Plasmid 54:114-134.
    • (2005) Plasmid , vol.54 , pp. 114-134
    • Dunn, A.K.1    Martin, M.O.2    Stabb, E.V.3
  • 33
    • 34548809711 scopus 로고    scopus 로고
    • Crystal structures of two novel dye-decolorizing peroxidases reveal a beta-barrel fold with a conserved heme-binding motif
    • Zubieta, et al. 2007. Crystal structures of two novel dye-decolorizing peroxidases reveal a beta-barrel fold with a conserved heme-binding motif. Proteins 69:223-233.
    • (2007) Proteins , vol.69 , pp. 223-233
    • Zubieta1
  • 34
    • 70349309436 scopus 로고    scopus 로고
    • Cytochrome c biogenesis: Mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control
    • Table of Contents. doi: 10.1128/MMBR.00001-09. PubMed
    • Kranz RG, Richard-Fogal C, Taylor JS, Frawley ER. 2009. Cytochrome c biogenesis: mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control. Microbiol. Mol. Biol. Rev. 73: 510-528, Table of Contents. doi: 10.1128/MMBR.00001-09. PubMed.
    • (2009) Microbiol. Mol. Biol. Rev , vol.73 , pp. 510-528
    • Kranz, R.G.1    Richard-Fogal, C.2    Taylor, J.S.3    Frawley, E.R.4
  • 35
    • 69249205419 scopus 로고    scopus 로고
    • A conserved haem redox and trafficking pathway for cofactor attachment
    • Richard-Fogal CL, et al. 2009. A conserved haem redox and trafficking pathway for cofactor attachment. EMBO J. 28:2349-2359.
    • (2009) EMBO J , vol.28 , pp. 2349-2359
    • Richard-Fogal, C.L.1
  • 37
    • 31144454629 scopus 로고    scopus 로고
    • Conserved and variable functions of the sigmaE stress response in related genomes
    • Rhodius VA, Suh WC, Nonaka G, West J, Gross CA. 2006. Conserved and variable functions of the sigmaE stress response in related genomes. PLoS Biol. 4:e2.
    • (2006) PLoS Biol , vol.4
    • Rhodius, V.A.1    Suh, W.C.2    Nonaka, G.3    West, J.4    Gross, C.A.5
  • 38
    • 3042606663 scopus 로고    scopus 로고
    • HutZ is required for efficient heme utilization in Vibrio cholerae
    • Wyckoff EE, Schmitt M, Wilks A, Payne SM. 2004. HutZ is required for efficient heme utilization in Vibrio cholerae. J. Bacteriol. 186:4142-4151.
    • (2004) J. Bacteriol , vol.186 , pp. 4142-4151
    • Wyckoff, E.E.1    Schmitt, M.2    Wilks, A.3    Payne, S.M.4
  • 39
    • 0032575499 scopus 로고    scopus 로고
    • Evidence that the fourth ligand to the [2Fe-2S] cluster in animal ferrochelatase is a cysteine. Characterization of the enzyme from Drosophila melanogaster
    • Sellers VM, Wang KF, Johnson MK, Dailey HA. 1998. Evidence that the fourth ligand to the [2Fe-2S] cluster in animal ferrochelatase is a cysteine. Characterization of the enzyme from Drosophila melanogaster. J. Biol. Chem. 273:22311-22316.
    • (1998) J. Biol. Chem , vol.273 , pp. 22311-22316
    • Sellers, V.M.1    Wang, K.F.2    Johnson, M.K.3    Dailey, H.A.4
  • 40
    • 47349130530 scopus 로고    scopus 로고
    • Effects of luxCDABEG induction in Vibrio fischeri: Enhancement of symbiotic colonization and conditional attenuation of growth in culture
    • Bose JL, Rosenberg CS, Stabb EV. 2008. Effects of luxCDABEG induction in Vibrio fischeri: enhancement of symbiotic colonization and conditional attenuation of growth in culture. Arch. Microbiol. 190:169-183.
    • (2008) Arch. Microbiol , vol.190 , pp. 169-183
    • Bose, J.L.1    Rosenberg, C.S.2    Stabb, E.V.3
  • 41
    • 77954022304 scopus 로고    scopus 로고
    • The alternative oxidase (AOX) gene in Vibrio fischeri is controlled by NsrR and upregulated in response to nitric oxide
    • Dunn AK, et al. 2010. The alternative oxidase (AOX) gene in Vibrio fischeri is controlled by NsrR and upregulated in response to nitric oxide. Mol. Microbiol. 77:44-55.
    • (2010) Mol. Microbiol , vol.77 , pp. 44-55
    • Dunn, A.K.1
  • 42
    • 33644859966 scopus 로고    scopus 로고
    • New rfp-and pES213-derived tools for analyzing symbiotic Vibrio fischeri reveal patterns of infection and lux expression in situ
    • Dunn AK, Millikan DS, Adin DM, Bose JL, Stabb EV. 2006. New rfp-and pES213-derived tools for analyzing symbiotic Vibrio fischeri reveal patterns of infection and lux expression in situ. Appl. Environ. Microbiol. 72:802-810.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 802-810
    • Dunn, A.K.1    Millikan, D.S.2    Adin, D.M.3    Bose, J.L.4    Stabb, E.V.5
  • 43
    • 0018870393 scopus 로고
    • A fluorometric assay for measurement of protoporphyrinogen oxidase activity in mammalian tissue
    • Brenner DA, Bloomer JR. 1980. A fluorometric assay for measurement of protoporphyrinogen oxidase activity in mammalian tissue. Clin. Chim. Acta 100:259-266.
    • (1980) Clin. Chim. Acta , vol.100 , pp. 259-266
    • Brenner, D.A.1    Bloomer, J.R.2
  • 44
    • 0028174034 scopus 로고
    • Expression of a cloned protoporphyrinogen oxidase
    • Dailey TA, Meissner P, Dailey HA. 1994. Expression of a cloned protoporphyrinogen oxidase. J. Biol. Chem. 269:813-815.
    • (1994) J. Biol. Chem , vol.269 , pp. 813-815
    • Dailey, T.A.1    Meissner, P.2    Dailey, H.A.3
  • 45
    • 0031430858 scopus 로고    scopus 로고
    • Cytochrome P450 induction, uroporphyrinogen decarboxylase depression, porphyrin accumulation and excretion, and gender influence in a 3-week rat model of porphyria cutanea tarda
    • Franklin MR, Phillips JD, Kushner JP. 1997. Cytochrome P450 induction, uroporphyrinogen decarboxylase depression, porphyrin accumulation and excretion, and gender influence in a 3-week rat model of porphyria cutanea tarda. Toxicol. Appl. Pharmacol. 147:289-299.
    • (1997) Toxicol. Appl. Pharmacol , vol.147 , pp. 289-299
    • Franklin, M.R.1    Phillips, J.D.2    Kushner, J.P.3
  • 46
    • 0035191293 scopus 로고    scopus 로고
    • Vibrio fischeri genes hvnA and hvnB encode secreted NAD(+)-glycohydrolases
    • Stabb EV, Reich KA, Ruby EG. 2001. Vibrio fischeri genes hvnA and hvnB encode secreted NAD(+)-glycohydrolases. J. Bacteriol. 183:309-317.
    • (2001) J. Bacteriol , vol.183 , pp. 309-317
    • Stabb, E.V.1    Reich, K.A.2    Ruby, E.G.3
  • 47
    • 25644458211 scopus 로고    scopus 로고
    • The subsystems approach to genome annotation and its use in the project to annotate 1000 genomes
    • Overbeek R, et al. 2005. The subsystems approach to genome annotation and its use in the project to annotate 1000 genomes. Nucleic Acids Res. 33:5691-5702.
    • (2005) Nucleic Acids Res , vol.33 , pp. 5691-5702
    • Overbeek, R.1
  • 48
    • 9144257886 scopus 로고    scopus 로고
    • The Pfam protein families database
    • Bateman A, et al. 2004. The Pfam protein families database. Nucleic Acids Res. 32:D138-D141.
    • (2004) Nucleic Acids Res , vol.32
    • Bateman, A.1
  • 49
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N, Nei M. 1987. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:406-425.
    • (1987) Mol. Biol. Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2


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