메뉴 건너뛰기




Volumn 348, Issue 5, 2005, Pages 1199-1210

Alternative IMP binding in feedback inhibition of hypoxanthine-guanine phosphoribosyltransferase from Thermoanaerobacter tengcongensis

Author keywords

Crystal structure; Feedback inhibition; HGPRT; IMP; Thermostability

Indexed keywords

5' PHOSPHATE; ALPHA DEXTRO PHOSPHORIBOSYL 1 PYROPHOSPHATE; APOENZYME; ASPARTIC ACID; ENZYME; GLUTAMIC ACID; HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE; INOSINE PHOSPHATE; MAGNESIUM ION; PHOSPHATE; PHOSPHORIBOSYLTRANSFERASE; PYROPHOSPHORIC ACID DERIVATIVE; SERINE; TETRAMER; UNCLASSIFIED DRUG; WATER;

EID: 18044392590     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.02.064     Document Type: Article
Times cited : (17)

References (48)
  • 1
    • 0030859943 scopus 로고    scopus 로고
    • Amidophosphoribosyltransferase limits the rate of cell growth-linked de novo purine biosynthesis in the presence of constant capacity of salvage purine biosynthesis
    • T. Yamaoka, M. Kondo, S. Honda, H. Iwahana, M. Moritani, and S. Ii Amidophosphoribosyltransferase limits the rate of cell growth-linked de novo purine biosynthesis in the presence of constant capacity of salvage purine biosynthesis J. Biol. Chem. 272 1997 17719 17725
    • (1997) J. Biol. Chem. , vol.272 , pp. 17719-17725
    • Yamaoka, T.1    Kondo, M.2    Honda, S.3    Iwahana, H.4    Moritani, M.5    Ii, S.6
  • 2
    • 0141984160 scopus 로고
    • HPRT and the Lesch-Nyhan syndrome
    • P.I. Patel, and C.T. Caskey HPRT and the Lesch-Nyhan syndrome Bioassays 2 1985 4 8
    • (1985) Bioassays , vol.2 , pp. 4-8
    • Patel, P.I.1    Caskey, C.T.2
  • 3
    • 0021332120 scopus 로고
    • Parasite enzymes as potential targets for antiparasitic chemotherapy
    • C.C. Wang Parasite enzymes as potential targets for antiparasitic chemotherapy J. Med. Chem. 27 1984 1 9
    • (1984) J. Med. Chem. , vol.27 , pp. 1-9
    • Wang, C.C.1
  • 4
    • 0028836011 scopus 로고
    • Hypoxanthine-guanine phosphoribosyltransferase as a therapeutic target in protozoal infections
    • B. Ullman, and D. Carter Hypoxanthine-guanine phosphoribosyltransferase as a therapeutic target in protozoal infections Infect. Agents Dis. 4 1995 29 40
    • (1995) Infect. Agents Dis. , vol.4 , pp. 29-40
    • Ullman, B.1    Carter, D.2
  • 5
    • 0034617303 scopus 로고    scopus 로고
    • Purine phosphoribosyltransferases
    • S.P. Craig 3rd, and A.E. Eakin Purine phosphoribosyltransferases J. Biol. Chem. 275 2000 20231 20234
    • (2000) J. Biol. Chem. , vol.275 , pp. 20231-20234
    • Craig III, S.P.1    Eakin, A.E.2
  • 6
    • 0033517848 scopus 로고    scopus 로고
    • Crystal structures of the Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase-GMP and -IMP complexes: Comparison of purine binding interactions with the XMP complex
    • A. Heroux, E.L. White, L.J. Ross, and D.W. Borhani Crystal structures of the Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase-GMP and -IMP complexes: comparison of purine binding interactions with the XMP complex Biochemistry 38 1999 14485 14494
    • (1999) Biochemistry , vol.38 , pp. 14485-14494
    • Heroux, A.1    White, E.L.2    Ross, L.J.3    Borhani, D.W.4
  • 7
    • 0033517729 scopus 로고    scopus 로고
    • Crystal structure of Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase with XMP, pyrophosphate, and two Mg(2+) ions bound: Insights into the catalytic mechanism
    • A. Heroux, E.L. White, L.J. Ross, R.L. Davis, and D.W. Borhani Crystal structure of Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase with XMP, pyrophosphate, and two Mg(2+) ions bound: insights into the catalytic mechanism Biochemistry 38 1999 14495 14506
    • (1999) Biochemistry , vol.38 , pp. 14495-14506
    • Heroux, A.1    White, E.L.2    Ross, L.J.3    Davis, R.L.4    Borhani, D.W.5
  • 8
    • 0034483903 scopus 로고    scopus 로고
    • Substrate deformation in a hypoxanthine-guanine phosphoribosyltransferase ternary complex: The structural basis for catalysis
    • A. Heroux, E.L. White, L.J. Ross, A.P. Kuzin, and D.W. Borhani Substrate deformation in a hypoxanthine-guanine phosphoribosyltransferase ternary complex: the structural basis for catalysis Struct. Fold. Des. 8 2000 1309 1318
    • (2000) Struct. Fold. Des. , vol.8 , pp. 1309-1318
    • Heroux, A.1    White, E.L.2    Ross, L.J.3    Kuzin, A.P.4    Borhani, D.W.5
  • 9
    • 0036084604 scopus 로고    scopus 로고
    • Crystal structures of free, IMP-, and GMP-bound Escherichia coli hypoxanthine phosphoribosyltransferase
    • L.W. Guddat, S. Vos, J.L. Martin, D.T. Keough, and J. de Jersey Crystal structures of free, IMP-, and GMP-bound Escherichia coli hypoxanthine phosphoribosyltransferase Protein Sci. 11 2002 1626 1638
    • (2002) Protein Sci. , vol.11 , pp. 1626-1638
    • Guddat, L.W.1    Vos, S.2    Martin, J.L.3    Keough, D.T.4    De Jersey, J.5
  • 10
    • 0032497936 scopus 로고    scopus 로고
    • Approaching the transition state in the crystal structure of a phosphoribosyltransferase
    • P.J. Focia, S.P. Craig 3rd, and A.E. Eakin Approaching the transition state in the crystal structure of a phosphoribosyltransferase Biochemistry 37 1998 17120 17127
    • (1998) Biochemistry , vol.37 , pp. 17120-17127
    • Focia, P.J.1    Craig III, S.P.2    Eakin, A.E.3
  • 11
    • 0034643828 scopus 로고    scopus 로고
    • Crystal structures of Giardia lamblia guanine phosphoribosyltransferase at 1.75 Å
    • W. Shi, N.R. Munagala, C.C. Wang, C.M. Li, P.C. Tyler, and R.H. Furneaux Crystal structures of Giardia lamblia guanine phosphoribosyltransferase at 1.75 Å Biochemistry 39 2000 6781 6790
    • (2000) Biochemistry , vol.39 , pp. 6781-6790
    • Shi, W.1    Munagala, N.R.2    Wang, C.C.3    Li, C.M.4    Tyler, P.C.5    Furneaux, R.H.6
  • 13
    • 0032573013 scopus 로고    scopus 로고
    • A 1.4Å crystal structure for the hypoxanthine phosphoribosyltransferase of Trypanosoma cruzi
    • P.J. Focia, S.P. Craig 3rd, R. Nieves-Alicea, R.J. Fletterick, and A.E. Eakin A 1.4Å crystal structure for the hypoxanthine phosphoribosyltransferase of Trypanosoma cruzi Biochemistry 37 1998 15066 15075
    • (1998) Biochemistry , vol.37 , pp. 15066-15075
    • Focia, P.J.1    Craig III, S.P.2    Nieves-Alicea, R.3    Fletterick, R.J.4    Eakin, A.E.5
  • 14
    • 0033519996 scopus 로고    scopus 로고
    • The 2.0 Å structure of malarial purine phosphoribosyltransferase in complex with a transition-state analogue inhibitor
    • W. Shi, C.M. Li, P.C. Tyler, R.H. Furneaux, S.M. Cahill, and M.E. Girvin The 2.0 Å structure of malarial purine phosphoribosyltransferase in complex with a transition-state analogue inhibitor Biochemistry 38 1999 9872 9880
    • (1999) Biochemistry , vol.38 , pp. 9872-9880
    • Shi, W.1    Li, C.M.2    Tyler, P.C.3    Furneaux, R.H.4    Cahill, S.M.5    Girvin, M.E.6
  • 15
    • 0032587578 scopus 로고    scopus 로고
    • The 2.0 Å structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor
    • W. Shi, C.M. Li, P.C. Tyler, R.H. Furneaux, C. Grubmeyer, V.L. Schramm, and S.C. Almo The 2.0 Å structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor Nature Struct. Biol. 6 1999 588 593
    • (1999) Nature Struct. Biol. , vol.6 , pp. 588-593
    • Shi, W.1    Li, C.M.2    Tyler, P.C.3    Furneaux, R.H.4    Grubmeyer, C.5    Schramm, V.L.6    Almo, S.C.7
  • 16
    • 0032475913 scopus 로고    scopus 로고
    • Structures of free and complexed forms of Escherichia coli xanthine-guanine phosphoribosyltransferase
    • S. Vos, R.J. Parry, M.R. Burns, J. de Jersey, and J.L. Martin Structures of free and complexed forms of Escherichia coli xanthine-guanine phosphoribosyltransferase J. Mol. Biol. 282 1998 875 889
    • (1998) J. Mol. Biol. , vol.282 , pp. 875-889
    • Vos, S.1    Parry, R.J.2    Burns, M.R.3    De Jersey, J.4    Martin, J.L.5
  • 17
    • 0030950226 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli xanthine phosphoribosyltransferase
    • S. Vos, J. de Jersey, and J.L. Martin Crystal structure of Escherichia coli xanthine phosphoribosyltransferase Biochemistry 36 1997 4125 4134
    • (1997) Biochemistry , vol.36 , pp. 4125-4134
    • Vos, S.1    De Jersey, J.2    Martin, J.L.3
  • 18
    • 0029898439 scopus 로고    scopus 로고
    • Crystal structure of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from the protozoan parasite Tritrichomonas foetus
    • J.R. Somoza, M.S. Chin, P.J. Focia, C.C. Wang, and R.J. Fletterick Crystal structure of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from the protozoan parasite Tritrichomonas foetus Biochemistry 35 1996 7032 7040
    • (1996) Biochemistry , vol.35 , pp. 7032-7040
    • Somoza, J.R.1    Chin, M.S.2    Focia, P.J.3    Wang, C.C.4    Fletterick, R.J.5
  • 19
    • 0029742013 scopus 로고    scopus 로고
    • Crystal structures of Toxoplasma gondii HGXPRTase reveal the catalytic role of a long flexible loop
    • M.A. Schumacher, D. Carter, D.S. Ross, B. Ullman, and R.G. Brennan Crystal structures of Toxoplasma gondii HGXPRTase reveal the catalytic role of a long flexible loop Nature Struct. Biol. 3 1996 881 887
    • (1996) Nature Struct. Biol. , vol.3 , pp. 881-887
    • Schumacher, M.A.1    Carter, D.2    Ross, D.S.3    Ullman, B.4    Brennan, R.G.5
  • 20
    • 0028083309 scopus 로고
    • The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP
    • J.C. Eads, G. Scapin, Y. Xu, C. Grubmeyer, and J.C. Sacchettini The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP Cell 78 1994 325 334
    • (1994) Cell , vol.78 , pp. 325-334
    • Eads, J.C.1    Scapin, G.2    Xu, Y.3    Grubmeyer, C.4    Sacchettini, J.C.5
  • 21
    • 0035877810 scopus 로고    scopus 로고
    • Feedback inhibition of amidophosphoribosyltransferase regulates the rate of cell growth via purine nucleotide, DNA, and protein syntheses
    • T. Yamaoka, M. Yano, M. Kondo, H. Sasaki, S. Hino, and R. Katashima Feedback inhibition of amidophosphoribosyltransferase regulates the rate of cell growth via purine nucleotide, DNA, and protein syntheses J. Biol. Chem. 276 2001 21285 21291
    • (2001) J. Biol. Chem. , vol.276 , pp. 21285-21291
    • Yamaoka, T.1    Yano, M.2    Kondo, M.3    Sasaki, H.4    Hino, S.5    Katashima, R.6
  • 22
    • 0030935658 scopus 로고    scopus 로고
    • Kinetic mechanism of human hypoxanthine-guanine phosphoribosyltransferase: Rapid phosphoribosyl transfer chemistry
    • Y. Xu, J. Eads, J.C. Sacchettini, and C. Grubmeyer Kinetic mechanism of human hypoxanthine-guanine phosphoribosyltransferase: rapid phosphoribosyl transfer chemistry Biochemistry 36 1997 3700 3712
    • (1997) Biochemistry , vol.36 , pp. 3700-3712
    • Xu, Y.1    Eads, J.2    Sacchettini, J.C.3    Grubmeyer, C.4
  • 23
    • 0346936003 scopus 로고    scopus 로고
    • Cloning, purification and characterization of thermostable hypoxanthine-guanine phosphoribosyltransferase from Thermoanaerobacter tengcongensis
    • Q. Chen, D.L. You, M.H. Hu, X.C. Gu, M. Luo, and S.Y. Lu Cloning, purification and characterization of thermostable hypoxanthine-guanine phosphoribosyltransferase from Thermoanaerobacter tengcongensis Protein Expr. Purif. 32 2003 239 245
    • (2003) Protein Expr. Purif. , vol.32 , pp. 239-245
    • Chen, Q.1    You, D.L.2    Hu, M.H.3    Gu, X.C.4    Luo, M.5    Lu, S.Y.6
  • 24
    • 0028281205 scopus 로고
    • Crystal structure of orotate phosphoribosyltransferase
    • G. Scapin, C. Grubmeyer, and J.C. Sacchettini Crystal structure of orotate phosphoribosyltransferase Biochemistry 33 1994 1287 1294
    • (1994) Biochemistry , vol.33 , pp. 1287-1294
    • Scapin, G.1    Grubmeyer, C.2    Sacchettini, J.C.3
  • 25
    • 0037134790 scopus 로고    scopus 로고
    • A point mutation at the subunit interface of hypoxanthine-guanine- xanthine phosphoribosyltransferase impairs activity: Role of oligomerization in catalysis
    • I.N. Subbayya, and H. Balaram A point mutation at the subunit interface of hypoxanthine-guanine-xanthine phosphoribosyltransferase impairs activity: role of oligomerization in catalysis FEBS Letters 521 2002 72 76
    • (2002) FEBS Letters , vol.521 , pp. 72-76
    • Subbayya, I.N.1    Balaram, H.2
  • 26
    • 0346493091 scopus 로고    scopus 로고
    • Interactions at the dimer interface influence the relative efficiencies for purine nucleotide synthesis and pyrophosphorolysis in a phosphoribosyltransferase
    • B. Canyuk, F.J. Medrano, M.A. Wenck, P.J. Focia, A.E. Eakin, and S.P. Craig Interactions at the dimer interface influence the relative efficiencies for purine nucleotide synthesis and pyrophosphorolysis in a phosphoribosyltransferase J. Mol. Biol. 335 2004 905 921
    • (2004) J. Mol. Biol. , vol.335 , pp. 905-921
    • Canyuk, B.1    Medrano, F.J.2    Wenck, M.A.3    Focia, P.J.4    Eakin, A.E.5    Craig, S.P.6
  • 27
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: A mechanism of protein structure stabilization
    • S.K. Burley, and G.A. Petsko Aromatic-aromatic interaction: a mechanism of protein structure stabilization Science 229 1985 23 28
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 28
    • 0035814901 scopus 로고    scopus 로고
    • The role for an invariant aspartic acid in hypoxanthine phosphoribosyltransferases is examined using saturation mutagenesis, functional analysis, and X-ray crystallography
    • B. Canyuk, P.J. Focia, and A.E. Eakin The role for an invariant aspartic acid in hypoxanthine phosphoribosyltransferases is examined using saturation mutagenesis, functional analysis, and X-ray crystallography Biochemistry 40 2001 2754 2765
    • (2001) Biochemistry , vol.40 , pp. 2754-2765
    • Canyuk, B.1    Focia, P.J.2    Eakin, A.E.3
  • 30
    • 0025299887 scopus 로고
    • Occurrence and role of cis peptide bonds in protein structures
    • D.E. Stewart, A. Sarkar, and J.E. Wampler Occurrence and role of cis peptide bonds in protein structures J. Mol. Biol. 214 1990 253 260
    • (1990) J. Mol. Biol. , vol.214 , pp. 253-260
    • Stewart, D.E.1    Sarkar, A.2    Wampler, J.E.3
  • 31
    • 0141890964 scopus 로고    scopus 로고
    • Protein preparation, crystallization and preliminary X-ray crystallographic studies of a thermostable hypoxanthine-guanine phosphoribosyltransferase from Thermoanaerobacter tengcongensis
    • D. You, Q. Chen, Y. Liang, J. An, R. Li, and X. Gu Protein preparation, crystallization and preliminary X-ray crystallographic studies of a thermostable hypoxanthine-guanine phosphoribosyltransferase from Thermoanaerobacter tengcongensis Acta Crystallog. sect. D 59 2003 1863 1865
    • (2003) Acta Crystallog. Sect. D , vol.59 , pp. 1863-1865
    • You, D.1    Chen, Q.2    Liang, Y.3    An, J.4    Li, R.5    Gu, X.6
  • 32
    • 0033168676 scopus 로고    scopus 로고
    • Crystal structures of adenine phosphoribosyltransferase from Leishmania donovani
    • C.L. Phillips, B. Ullman, R.G. Brennan, and C.P. Hill Crystal structures of adenine phosphoribosyltransferase from Leishmania donovani EMBO J. 18 1999 3533 3545
    • (1999) EMBO J. , vol.18 , pp. 3533-3545
    • Phillips, C.L.1    Ullman, B.2    Brennan, R.G.3    Hill, C.P.4
  • 33
    • 0342894815 scopus 로고    scopus 로고
    • Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site
    • J.M. Krahn, J.H. Kim, M.R. Burns, R.J. Parry, H. Zalkin, and J.L. Smith Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site Biochemistry 36 1997 11061 11068
    • (1997) Biochemistry , vol.36 , pp. 11061-11068
    • Krahn, J.M.1    Kim, J.H.2    Burns, M.R.3    Parry, R.J.4    Zalkin, H.5    Smith, J.L.6
  • 34
    • 1242273769 scopus 로고    scopus 로고
    • Functional roles for amino acids in active site loop II of a hypoxanthine phosphoribosyltransferase
    • F.J. Medrano, M.A. Wenck, A.E. Eakin, and S.P. Craig 3rd Functional roles for amino acids in active site loop II of a hypoxanthine phosphoribosyltransferase Biochim. Biophys. Acta 1650 2003 105 116
    • (2003) Biochim. Biophys. Acta , vol.1650 , pp. 105-116
    • Medrano, F.J.1    Wenck, M.A.2    Eakin, A.E.3    Craig III, S.P.4
  • 35
    • 0032905985 scopus 로고    scopus 로고
    • Purification and characterization of Plasmodium falciparum hypoxanthine-guanine-xanthine phosphoribosyltransferase and comparison with the human enzyme
    • D.T. Keough, A.L. Ng, D.J. Winzor, B.T. Emmerson, and J. de Jersey Purification and characterization of Plasmodium falciparum hypoxanthine-guanine- xanthine phosphoribosyltransferase and comparison with the human enzyme Mol. Biochem. Parasitol. 98 1999 29 41
    • (1999) Mol. Biochem. Parasitol. , vol.98 , pp. 29-41
    • Keough, D.T.1    Ng, A.L.2    Winzor, D.J.3    Emmerson, B.T.4    De Jersey, J.5
  • 36
    • 0027479744 scopus 로고
    • Comparing the human and schistosomal hypoxanthine-guanine phosphoribosyltransferases by circular dichroism
    • L. Yuan, C.S. Wu, S.P. Craig 3rd, A.F. Liu, and C.C. Wang Comparing the human and schistosomal hypoxanthine-guanine phosphoribosyltransferases by circular dichroism Biochim. Biophys. Acta 1162 1993 10 16
    • (1993) Biochim. Biophys. Acta , vol.1162 , pp. 10-16
    • Yuan, L.1    Wu, C.S.2    Craig III, S.P.3    Liu, A.F.4    Wang, C.C.5
  • 37
    • 0038492663 scopus 로고    scopus 로고
    • Crystal structure of d-hydantoinase from Burkholderia pickettii at a resolution of 2.7 Angstroms: Insights into the molecular basis of enzyme thermostability
    • Z. Xu, Y. Liu, Y. Yang, W. Jiang, E. Arnold, and J. Ding Crystal structure of d-hydantoinase from Burkholderia pickettii at a resolution of 2.7 Angstroms: insights into the molecular basis of enzyme thermostability J. Bacteriol. 185 2003 4038 4049
    • (2003) J. Bacteriol. , vol.185 , pp. 4038-4049
    • Xu, Z.1    Liu, Y.2    Yang, Y.3    Jiang, W.4    Arnold, E.5    Ding, J.6
  • 38
    • 0018094892 scopus 로고
    • Electrostatic effects in proteins
    • M.F. Perutz Electrostatic effects in proteins Science 201 1978 1187 1191
    • (1978) Science , vol.201 , pp. 1187-1191
    • Perutz, M.F.1
  • 39
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey
    • A. Szilagyi, and P. Zavodszky Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey Struct. Fold. Des. 8 2000 493 504
    • (2000) Struct. Fold. Des. , vol.8 , pp. 493-504
    • Szilagyi, A.1    Zavodszky, P.2
  • 40
    • 0027216310 scopus 로고
    • The hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus has unique properties
    • J.T. Beck, and C.C. Wang The hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus has unique properties Mol. Biochem. Parasitol. 60 1993 187 194
    • (1993) Mol. Biochem. Parasitol. , vol.60 , pp. 187-194
    • Beck, J.T.1    Wang, C.C.2
  • 41
    • 0019748203 scopus 로고
    • Structural features of the phosphoribosyltransferases and their relationship to the human deficiency disorders of purine and pyrimidine metabolism
    • W.D.L. Musick Structural features of the phosphoribosyltransferases and their relationship to the human deficiency disorders of purine and pyrimidine metabolism CRC Crit. Rev. Biochem. 11 1981 1 34
    • (1981) CRC Crit. Rev. Biochem. , vol.11 , pp. 1-34
    • Musick, W.D.L.1
  • 42
    • 0025096451 scopus 로고
    • Expression of active human hypoxanthine-guanine phosphoribosyltransferase in Escherichia coli and characterisation of the recombinant enzyme
    • M.L. Free, R.B. Gordon, D.T. Keough, I.R. Beacham, B.T. Emmerson, and J. Jersey Expression of active human hypoxanthine-guanine phosphoribosyltransferase in Escherichia coli and characterisation of the recombinant enzyme Biochim. Biophys. Acta 1087 1990 205 211
    • (1990) Biochim. Biophys. Acta , vol.1087 , pp. 205-211
    • Free, M.L.1    Gordon, R.B.2    Keough, D.T.3    Beacham, I.R.4    Emmerson, B.T.5    Jersey, J.6
  • 43
    • 0029916298 scopus 로고    scopus 로고
    • Thermal stability of Artemia HGPRT: Effect of substrates on inactivation kinetics
    • C. Montero, P. Llorente, L. Argomaniz, and M. Menendez Thermal stability of Artemia HGPRT: effect of substrates on inactivation kinetics Int. J. Biol. Macromol. 18 1996 255 262
    • (1996) Int. J. Biol. Macromol. , vol.18 , pp. 255-262
    • Montero, C.1    Llorente, P.2    Argomaniz, L.3    Menendez, M.4
  • 45
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallog. sect. A 47 1991 110 119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 46
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallog. 24 1991 946 950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 47
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • J.D. Thompson, T.J. Gibson, F. Plewniak, F. Jeanmougin, and D.G. Higgins The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools Nucl. Acids Res. 25 1997 4876 4882
    • (1997) Nucl. Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 48
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • P. Gouet, E. Courcelle, D.I. Stuart, and F. Metoz ESPript: analysis of multiple sequence alignments in PostScript Bioinformatics 15 1999 305 308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.