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Volumn 6, Issue 8, 2008, Pages 1802-1810

An enzymatic atavist revealed in dual pathways for water activation

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; GUANINE NUCLEOTIDE; HYDROLASE; INOSINATE DEHYDROGENASE; TYROSINE; WATER; AMINO ACID;

EID: 50249144571     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.0060206     Document Type: Article
Times cited : (21)

References (53)
  • 1
    • 0035023450 scopus 로고    scopus 로고
    • Multimodular biocatalysts for natural product assembly
    • Schwarzer D, Marahiel MA (2001) Multimodular biocatalysts for natural product assembly. Naturwissenschaften 88: 93-101.
    • (2001) Naturwissenschaften , vol.88 , pp. 93-101
    • Schwarzer, D.1    Marahiel, M.A.2
  • 2
    • 0001747786 scopus 로고    scopus 로고
    • Genetic contributions to understanding polyketide synthases
    • Hopwood DA (1997) Genetic contributions to understanding polyketide synthases. Chem Rev 97: 2465-2498.
    • (1997) Chem Rev , vol.97 , pp. 2465-2498
    • Hopwood, D.A.1
  • 3
    • 33750428183 scopus 로고    scopus 로고
    • Natural biocombinatorics in the polyketide synthase genes of the actinobacterium Streptomyces avermitilis
    • doi:10.1371/journal.pcbi.0020132
    • Jenke-Kodama H, Borner T, Dittmann E (2006) Natural biocombinatorics in the polyketide synthase genes of the actinobacterium Streptomyces avermitilis. PLoS Comput Biol 2: e132. doi:10.1371/journal.pcbi.0020132
    • (2006) PLoS Comput Biol , vol.2
    • Jenke-Kodama, H.1    Borner, T.2    Dittmann, E.3
  • 4
    • 0037396345 scopus 로고    scopus 로고
    • Evolution of function in (beta/alpha)8-barrel enzymes
    • Gerlt JA, Raushel FM (2003) Evolution of function in (beta/alpha)8-barrel enzymes. Curr Opin Chem Biol 7: 252-264.
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 252-264
    • Gerlt, J.A.1    Raushel, F.M.2
  • 5
    • 13544274134 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the orotidine 5′-monophosphate decarboxylase suprafamily: Structural basis for catalytic promiscuity in wild-type and designed mutants of 3-keto-L-gulonate 6-phosphate decarboxylase
    • Wise EL, Yew WS, Akana J, Gerlt JA, Rayment I (2005) Evolution of enzymatic activities in the orotidine 5′-monophosphate decarboxylase suprafamily: structural basis for catalytic promiscuity in wild-type and designed mutants of 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry 44: 1816-1823.
    • (2005) Biochemistry , vol.44 , pp. 1816-1823
    • Wise, E.L.1    Yew, W.S.2    Akana, J.3    Gerlt, J.A.4    Rayment, I.5
  • 6
    • 36749083463 scopus 로고    scopus 로고
    • Ohno's dilemma: Evolution of new genes under continuous selection
    • Bergthorsson U, Andersson DI, Roth JR (2007) Ohno's dilemma: evolution of new genes under continuous selection. Proc Natl Acad Sci U S A 104: 17004-17009.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 17004-17009
    • Bergthorsson, U.1    Andersson, D.I.2    Roth, J.R.3
  • 7
    • 33748519900 scopus 로고    scopus 로고
    • IMP dehydrogenase: Structural schizophrenia and an unusual base
    • Hedstrom L, Gan L (2006) IMP dehydrogenase: structural schizophrenia and an unusual base. Curr Opin Chem Biol 10: 520-525.
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 520-525
    • Hedstrom, L.1    Gan, L.2
  • 8
    • 0032804406 scopus 로고    scopus 로고
    • IMP dehydrogenase: Mechanism of action and inhibition
    • Hedstrom L (1999) IMP dehydrogenase: mechanism of action and inhibition. Curr Med Chem 6: 545-560.
    • (1999) Curr Med Chem , vol.6 , pp. 545-560
    • Hedstrom, L.1
  • 9
    • 0037417754 scopus 로고    scopus 로고
    • The immunosuppressive agent mizoribine monophosphate forms a transition state analog complex with IMP dehydrogenase
    • Gan L, Seyedsayamdost MR, Shuto S, Matsuda A, Petsko GA, et al. (2003) The immunosuppressive agent mizoribine monophosphate forms a transition state analog complex with IMP dehydrogenase. Biochemistry 42: 857-863.
    • (2003) Biochemistry , vol.42 , pp. 857-863
    • Gan, L.1    Seyedsayamdost, M.R.2    Shuto, S.3    Matsuda, A.4    Petsko, G.A.5
  • 10
    • 4644298282 scopus 로고    scopus 로고
    • Substitution of the conserved Arg-Tyr dyad selectively disrupts the hydrolysis phase of the IMP dehydrogenase reaction
    • Guillén Schlippe YV, Riera TV, Seyedsayamdost MR, Hedstrom L (2004) Substitution of the conserved Arg-Tyr dyad selectively disrupts the hydrolysis phase of the IMP dehydrogenase reaction. Biochemistry 43: 4511-4521.
    • (2004) Biochemistry , vol.43 , pp. 4511-4521
    • Guillén Schlippe, Y.V.1    Riera, T.V.2    Seyedsayamdost, M.R.3    Hedstrom, L.4
  • 11
    • 24344510514 scopus 로고    scopus 로고
    • Is Arg418 the catalytic base required for the hydrolysis step of the IMP dehydrogenase reaction?
    • Guillén Schlippe YV, Hedstrom L (2005) Is Arg418 the catalytic base required for the hydrolysis step of the IMP dehydrogenase reaction? Biochemistry 44: 11700-11707.
    • (2005) Biochemistry , vol.44 , pp. 11700-11707
    • Guillén Schlippe, Y.V.1    Hedstrom, L.2
  • 12
    • 29244467407 scopus 로고    scopus 로고
    • Guanidine derivatives rescue the Arg418Ala mutation of Tritrichomonas foetus IMP dehydrogenase
    • Guillén Schlippe YV, Hedstrom L (2005) Guanidine derivatives rescue the Arg418Ala mutation of Tritrichomonas foetus IMP dehydrogenase. Biochemistry 44: 16695-16700.
    • (2005) Biochemistry , vol.44 , pp. 16695-16700
    • Guillén Schlippe, Y.V.1    Hedstrom, L.2
  • 13
    • 34249022037 scopus 로고    scopus 로고
    • On the convergence improvement in the metadynamics simulations: A Wang-Landau recursion approach
    • Min D, Liu Y, Carbone I, Yang W (2007) On the convergence improvement in the metadynamics simulations: a Wang-Landau recursion approach. J Chem Phys 126: 194104.
    • (2007) J Chem Phys , vol.126 , pp. 194104
    • Min, D.1    Liu, Y.2    Carbone, I.3    Yang, W.4
  • 14
    • 0017100947 scopus 로고
    • Theoretical studies of enzymic reactions: Dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme
    • Warshel A, Levitt M (1976) Theoretical studies of enzymic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme. J Mol Biol 103: 227-249.
    • (1976) J Mol Biol , vol.103 , pp. 227-249
    • Warshel, A.1    Levitt, M.2
  • 15
    • 84986512474 scopus 로고
    • CHARMM: A program for macromolecular energy, minimization, and dynamics calculations
    • Brooks BR, Bruccoleri RE, Olafson BD, States DJ, Swaminathan S, et al. (1983) CHARMM: a program for macromolecular energy, minimization, and dynamics calculations. J Comp Chem 4: 187-217.
    • (1983) J Comp Chem , vol.4 , pp. 187-217
    • Brooks, B.R.1    Bruccoleri, R.E.2    Olafson, B.D.3    States, D.J.4    Swaminathan, S.5
  • 16
    • 84986513644 scopus 로고
    • A combined quantum mechanical and molecular mechanical potential for molecular dynamics simulations
    • Field MJ, Bash PA, Karplus M (1990) A combined quantum mechanical and molecular mechanical potential for molecular dynamics simulations. J Comp Chem 11: 700-733.
    • (1990) J Comp Chem , vol.11 , pp. 700-733
    • Field, M.J.1    Bash, P.A.2    Karplus, M.3
  • 17
    • 33845376416 scopus 로고
    • Ab initio and Monte Carlo calculations for a nucleophilic addition reaction in the gas phase and in aqueous solution
    • Madura JD, Jorgensen WL (1986) Ab initio and Monte Carlo calculations for a nucleophilic addition reaction in the gas phase and in aqueous solution. J Am Chem Soc 108: 2517-2527.
    • (1986) J Am Chem Soc , vol.108 , pp. 2517-2527
    • Madura, J.D.1    Jorgensen, W.L.2
  • 18
    • 0032711930 scopus 로고    scopus 로고
    • Combined quantum mechanical/molecular mechanical methodologies applied to biomolecular systems
    • Monard G, Merz KM Jr (1999) Combined quantum mechanical/molecular mechanical methodologies applied to biomolecular systems. Acc Chem Res 32: 904-911.
    • (1999) Acc Chem Res , vol.32 , pp. 904-911
    • Monard, G.1    Merz Jr, K.M.2
  • 19
    • 0001491955 scopus 로고    scopus 로고
    • Hybrid quantum and molecular mechanical simulations: An alternative avenue to solvent effects in organic chemistry
    • Gao J (1996) Hybrid quantum and molecular mechanical simulations: an alternative avenue to solvent effects in organic chemistry. Acc Chem Res 29: 298-305.
    • (1996) Acc Chem Res , vol.29 , pp. 298-305
    • Gao, J.1
  • 21
    • 33644968698 scopus 로고    scopus 로고
    • Metadynamics as a tool for exploring free energy landscapes of chemical reactions
    • Ensing B, De Vivo M, Liu Z, Moore P, Klein ML (2006) Metadynamics as a tool for exploring free energy landscapes of chemical reactions. Acc Chem Res 39: 73-81.
    • (2006) Acc Chem Res , vol.39 , pp. 73-81
    • Ensing, B.1    De Vivo, M.2    Liu, Z.3    Moore, P.4    Klein, M.L.5
  • 22
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell AD Jr, Bashford D, Bellott M, Dunbrack RL, Evanseck JD, et al. (1998) All-atom empirical potential for molecular modeling and dynamics studies of proteins. J Phys Chem B 102: 3586-3616.
    • (1998) J Phys Chem B , vol.102 , pp. 3586-3616
    • MacKerell Jr, A.D.1    Bashford, D.2    Bellott, M.3    Dunbrack, R.L.4    Evanseck, J.D.5
  • 23
    • 1542779956 scopus 로고    scopus 로고
    • Self-consistent-charge density-functional tight-binding method for simulations of complex materials properties
    • Elstner M, Porezag D, Jungnickel G, Elsner J, Haugk M, et al. (1998) Self-consistent-charge density-functional tight-binding method for simulations of complex materials properties. Phys Rev B 58: 7260-7268.
    • (1998) Phys Rev B , vol.58 , pp. 7260-7268
    • Elstner, M.1    Porezag, D.2    Jungnickel, G.3    Elsner, J.4    Haugk, M.5
  • 24
    • 0035249196 scopus 로고    scopus 로고
    • Generalized solvent boundary potential for computer simulations
    • Im W, Berneche S, Roux B (2001) Generalized solvent boundary potential for computer simulations. J Chem Phys 114: 2924-2937.
    • (2001) J Chem Phys , vol.114 , pp. 2924-2937
    • Im, W.1    Berneche, S.2    Roux, B.3
  • 25
    • 34548059996 scopus 로고    scopus 로고
    • Reliable treatment of electrostatics in combined QM/MM simulation of macromolecules
    • Schaefer P, Riccardi D, Cui Q (2005) Reliable treatment of electrostatics in combined QM/MM simulation of macromolecules. J Chem Phys 123: 14905-14918.
    • (2005) J Chem Phys , vol.123 , pp. 14905-14918
    • Schaefer, P.1    Riccardi, D.2    Cui, Q.3
  • 26
    • 0035425380 scopus 로고    scopus 로고
    • Enzyme catalysis: Removing chemically 'essential' residues by site-directed mutagenesis
    • Peracchi A (2001) Enzyme catalysis: removing chemically 'essential' residues by site-directed mutagenesis. Trends Biochem Sci 26: 497-503.
    • (2001) Trends Biochem Sci , vol.26 , pp. 497-503
    • Peracchi, A.1
  • 27
    • 0025045326 scopus 로고
    • Histidine-40 of ribonuclease T1 acts as base catalyst when the true catalytic base, glutamic acid-58, is replaced by alanine
    • Steyaert J, Hallenga K, Wyns L, Stanssens P (1990) Histidine-40 of ribonuclease T1 acts as base catalyst when the true catalytic base, glutamic acid-58, is replaced by alanine. Biochemistry 29: 9064-9072.
    • (1990) Biochemistry , vol.29 , pp. 9064-9072
    • Steyaert, J.1    Hallenga, K.2    Wyns, L.3    Stanssens, P.4
  • 28
    • 0040182818 scopus 로고    scopus 로고
    • Catalytic activity of the D38A mutant of 3-oxo-Delta 5-steroid isomerase: Recruitment of aspartate-99 as the base
    • Henot F, Pollack RM (2000) Catalytic activity of the D38A mutant of 3-oxo-Delta 5-steroid isomerase: recruitment of aspartate-99 as the base. Biochemistry 39: 3351-3359.
    • (2000) Biochemistry , vol.39 , pp. 3351-3359
    • Henot, F.1    Pollack, R.M.2
  • 29
    • 0024280501 scopus 로고
    • Dissecting the catalytic triad of a serine protease
    • Carter P, Wells J (1988) Dissecting the catalytic triad of a serine protease. Nature 332: 564-568.
    • (1988) Nature , vol.332 , pp. 564-568
    • Carter, P.1    Wells, J.2
  • 30
    • 0037022810 scopus 로고    scopus 로고
    • Chemical rescue in catalysis by human carbonic anhydrases II and III
    • An H, Tu C, Duda D, Montanez-Clemente I, Math K, et al. (2002) Chemical rescue in catalysis by human carbonic anhydrases II and III. Biochemistry 41: 3235-3242.
    • (2002) Biochemistry , vol.41 , pp. 3235-3242
    • An, H.1    Tu, C.2    Duda, D.3    Montanez-Clemente, I.4    Math, K.5
  • 31
    • 0033596742 scopus 로고    scopus 로고
    • Kinetic mechanism of Tritrichomonas foetus inosine-5′-monophosphate dehydrogenase
    • Digits JA, Hedstrom L (1999) Kinetic mechanism of Tritrichomonas foetus inosine-5′-monophosphate dehydrogenase. Biochemistry 38: 2295-2306.
    • (1999) Biochemistry , vol.38 , pp. 2295-2306
    • Digits, J.A.1    Hedstrom, L.2
  • 32
    • 0033576251 scopus 로고    scopus 로고
    • Species-specific inhibition of inosine 5′-monophosphate dehydrogenase by mycophenolic acid
    • Digits JA, Hedstrom L (1999) Species-specific inhibition of inosine 5′-monophosphate dehydrogenase by mycophenolic acid. Biochemistry 38: 15388-15397.
    • (1999) Biochemistry , vol.38 , pp. 15388-15397
    • Digits, J.A.1    Hedstrom, L.2
  • 33
    • 29444450245 scopus 로고    scopus 로고
    • Crystal structure of human guanosine monophosphate reductase 2 (GMPR2) in complex with GMP
    • Li J, Wei Z, Zheng M, Gu X, Deng Y, et al. (2006) Crystal structure of human guanosine monophosphate reductase 2 (GMPR2) in complex with GMP. J Mol Biol 355: 980-988.
    • (2006) J Mol Biol , vol.355 , pp. 980-988
    • Li, J.1    Wei, Z.2    Zheng, M.3    Gu, X.4    Deng, Y.5
  • 34
    • 0014605363 scopus 로고
    • Recombination in Escherichia coli. 3. Mapping by the gradient of transmission
    • De Haan PG, Hoekstra WP, Verhoef C, Felix HS (1969) Recombination in Escherichia coli. 3. Mapping by the gradient of transmission. Mutat Res 8: 505-512.
    • (1969) Mutat Res , vol.8 , pp. 505-512
    • De Haan, P.G.1    Hoekstra, W.P.2    Verhoef, C.3    Felix, H.S.4
  • 35
    • 0023711405 scopus 로고
    • Nucleotide sequence of the gene encoding the GMP reductase of Escherichia coli K12
    • Andrews SC, Guest JR (1988) Nucleotide sequence of the gene encoding the GMP reductase of Escherichia coli K12. Biochem J 255: 35-43.
    • (1988) Biochem J , vol.255 , pp. 35-43
    • Andrews, S.C.1    Guest, J.R.2
  • 36
    • 0018374626 scopus 로고
    • Reaction mechanism and specificity of human GMP reductase
    • Spector T, Jones T, Miller R (1979) Reaction mechanism and specificity of human GMP reductase. J Biol Chem 254: 2308-2315.
    • (1979) J Biol Chem , vol.254 , pp. 2308-2315
    • Spector, T.1    Jones, T.2    Miller, R.3
  • 37
    • 18344364274 scopus 로고    scopus 로고
    • NADPH-dependent GMP reductase isoenzyme of human (GMPR2). Expression, purification, and kinetic properties
    • Deng Y, Wang Z, Ying K, Gu S, Ji C, et al. (2002) NADPH-dependent GMP reductase isoenzyme of human (GMPR2). Expression, purification, and kinetic properties. Int J Biochem Cell Biol 34: 1035-1050.
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 1035-1050
    • Deng, Y.1    Wang, Z.2    Ying, K.3    Gu, S.4    Ji, C.5
  • 38
    • 0028955737 scopus 로고
    • Divergent evolution of a beta/alpha-barrel subclass: Detection of numerous phosphate-binding sites by motif search
    • Bork P, Gellerich J, Groth H, Hooft R, Martin F (1995) Divergent evolution of a beta/alpha-barrel subclass: detection of numerous phosphate-binding sites by motif search. Protein Sci 4: 268-274.
    • (1995) Protein Sci , vol.4 , pp. 268-274
    • Bork, P.1    Gellerich, J.2    Groth, H.3    Hooft, R.4    Martin, F.5
  • 39
    • 0036384350 scopus 로고    scopus 로고
    • One fold with many functions: The evolutionary relationships between TIM barrel families based on their sequences, structures and functions
    • Nagano N, Orengo CA, Thornton JM (2002) One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions. J Mol Biol 321: 741-765.
    • (2002) J Mol Biol , vol.321 , pp. 741-765
    • Nagano, N.1    Orengo, C.A.2    Thornton, J.M.3
  • 40
    • 0034601917 scopus 로고    scopus 로고
    • Homology among (betaalpha)(8) barrels: Implications for the evolution of metabolic pathways
    • Copley RR, Bork P (2000) Homology among (betaalpha)(8) barrels: implications for the evolution of metabolic pathways. J Mol Biol 303: 627-641.
    • (2000) J Mol Biol , vol.303 , pp. 627-641
    • Copley, R.R.1    Bork, P.2
  • 41
    • 0036677932 scopus 로고    scopus 로고
    • A branch-and-bound algorithm for the inference of ancestral amino-acid sequences when the replacement rate varies among sites: Application to the evolution of five gene families
    • Pupko T, Pe'er I, Hasegawa M, Graur D, Friedman N (2002) A branch-and-bound algorithm for the inference of ancestral amino-acid sequences when the replacement rate varies among sites: application to the evolution of five gene families. Bioinformatics 18: 1116-1123.
    • (2002) Bioinformatics , vol.18 , pp. 1116-1123
    • Pupko, T.1    Pe'er, I.2    Hasegawa, M.3    Graur, D.4    Friedman, N.5
  • 42
    • 0002639348 scopus 로고
    • Microbial modification of mycophenolic acid
    • Jones DF, Moore RH, Crawley GC (1970) Microbial modification of mycophenolic acid. J Chem Soc (C): 1725-1737.
    • (1970) J Chem Soc , vol.100 , pp. 1725-1737
    • Jones, D.F.1    Moore, R.H.2    Crawley, G.C.3
  • 43
    • 15744377146 scopus 로고    scopus 로고
    • The functional basis of mycophenolic acid resistance in Candida albicans IMP dehydrogenase
    • Kohler GA, Gong X, Bentink S, Theiss S, Pagani GM, et al. (2005) The functional basis of mycophenolic acid resistance in Candida albicans IMP dehydrogenase. J Biol Chem 280: 11295-11302.
    • (2005) J Biol Chem , vol.280 , pp. 11295-11302
    • Kohler, G.A.1    Gong, X.2    Bentink, S.3    Theiss, S.4    Pagani, G.M.5
  • 45
    • 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
  • 46
    • 50249161484 scopus 로고    scopus 로고
    • Swofford DL (2003) PAUP*. Phylogenetic analysis using parsimony (*and other methods, Version 4. Sunderland Massachusetts, Sinauer Associates
    • Swofford DL (2003) PAUP*. Phylogenetic analysis using parsimony (*and other methods). Version 4. Sunderland (Massachusetts): Sinauer Associates.
  • 47
    • 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
  • 48
    • 33747829924 scopus 로고    scopus 로고
    • Expresso: Automatic incorporation of structural information in multiple sequence alignments using 3D-Coffee
    • Armougom F, Moretti S, Poirot O, Audic S, Dumas P, et al. (2006) Expresso: automatic incorporation of structural information in multiple sequence alignments using 3D-Coffee. Nucleic Acids Res 34: W604-608.
    • (2006) Nucleic Acids Res , vol.34
    • Armougom, F.1    Moretti, S.2    Poirot, O.3    Audic, S.4    Dumas, P.5
  • 49
    • 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
  • 50
    • 1342309210 scopus 로고    scopus 로고
    • Parallel Metropolis coupled Markov chain Monte Carlo for Bayesian phylogenetic inference
    • Altekar G, Dwarkadas S, Huelsenbeck JP, Ronquist F (2004) Parallel Metropolis coupled Markov chain Monte Carlo for Bayesian phylogenetic inference. Bioinformatics 20: 407-415.
    • (2004) Bioinformatics , vol.20 , pp. 407-415
    • Altekar, G.1    Dwarkadas, S.2    Huelsenbeck, J.P.3    Ronquist, F.4
  • 51
    • 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
  • 52
    • 0027132974 scopus 로고
    • Maximum-likelihood estimation of phylogeny from DNA sequences when substitution rates differ over sites
    • Yang Z (1993) Maximum-likelihood estimation of phylogeny from DNA sequences when substitution rates differ over sites. Mol Biol Evol 10: 1396-1401.
    • (1993) Mol Biol Evol , vol.10 , pp. 1396-1401
    • Yang, Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.