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Volumn 8, Issue 2, 2013, Pages

Biochemical Characterization of Uracil Phosphoribosyltransferase from Mycobacterium tuberculosis

Author keywords

[No Author keywords available]

Indexed keywords

PYROPHOSPHATE; URACIL PHOSPHORIBOSYLTRANSFERASE;

EID: 84873720437     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0056445     Document Type: Article
Times cited : (20)

References (55)
  • 2
    • 45149113341 scopus 로고    scopus 로고
    • Extensively drug-resistant tuberculosis: current challenges and threats
    • Jain A, Mondal R, (2008) Extensively drug-resistant tuberculosis: current challenges and threats. FEMS Immunol Med Microbiol 53: 145-50.
    • (2008) FEMS Immunol Med Microbiol , vol.53 , pp. 145-150
    • Jain, A.1    Mondal, R.2
  • 3
    • 71049135360 scopus 로고    scopus 로고
    • Totally drug-resistant tuberculosis strains: evidence of adaptation at the cellular level
    • Velayati AA, Farnia P, Masjedi MR, Ibrahim TA, Tabarsi P, et al. (2009) Totally drug-resistant tuberculosis strains: evidence of adaptation at the cellular level. Eur Respir J 34: 1202-1203.
    • (2009) Eur Respir J , vol.34 , pp. 1202-1203
    • Velayati, A.A.1    Farnia, P.2    Masjedi, M.R.3    Ibrahim, T.A.4    Tabarsi, P.5
  • 5
    • 44649128524 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis and the macrophage: maintaining a balance
    • Pieters J, (2008) Mycobacterium tuberculosis and the macrophage: maintaining a balance. Cell Host Microbe 3: 399-407.
    • (2008) Cell Host Microbe , vol.3 , pp. 399-407
    • Pieters, J.1
  • 7
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, et al. (1998) Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393: 537-544.
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3    Garnier, T.4    Churcher, C.5
  • 9
    • 79952804465 scopus 로고    scopus 로고
    • Purine Salvage Pathway in Mycobacterium tuberculosis
    • Ducati RG, Breda A, Basso LA, Santos DS, (2011) Purine Salvage Pathway in Mycobacterium tuberculosis. Curr Med Chem 18: 1258-1275.
    • (2011) Curr Med Chem , vol.18 , pp. 1258-1275
    • Ducati, R.G.1    Breda, A.2    Basso, L.A.3    Santos, D.S.4
  • 10
    • 83555169348 scopus 로고    scopus 로고
    • Purine Nucleoside Phosphorylase as a Molecular Target to Develop Active Compounds Against Mycobacterium tuberculosis
    • Ducati RG, Souto AA, Caceres RA, de Azevedo Jr WF, Basso LA, et al. (2010) Purine Nucleoside Phosphorylase as a Molecular Target to Develop Active Compounds Against Mycobacterium tuberculosis. Int Rev Biophys Chem 1: 34-40.
    • (2010) Int Rev Biophys Chem , vol.1 , pp. 34-40
    • Ducati, R.G.1    Souto, A.A.2    Caceres, R.A.3    de Azevedo Jr, W.F.4    Basso, L.A.5
  • 11
    • 77954217431 scopus 로고    scopus 로고
    • Crystallographic and docking studies of purine nucleoside phosphorylase from Mycobacterium tuberculosis
    • Ducati RG, Basso LA, Santos DS, de Azevedo WF Jr, (2010) Crystallographic and docking studies of purine nucleoside phosphorylase from Mycobacterium tuberculosis. Bioorg Med Chem 18: 4769-4774.
    • (2010) Bioorg Med Chem , vol.18 , pp. 4769-4774
    • Ducati, R.G.1    Basso, L.A.2    Santos, D.S.3    de Azevedo Jr., W.F.4
  • 12
    • 67349183401 scopus 로고    scopus 로고
    • Substrate specificity and kinetic mechanism of purine nucleoside phosphorylase from Mycobacterium tuberculosis
    • Ducati RG, Santos DS, Basso LA, (2009) Substrate specificity and kinetic mechanism of purine nucleoside phosphorylase from Mycobacterium tuberculosis. Arch Biochem Biophys 486: 155-164.
    • (2009) Arch Biochem Biophys , vol.486 , pp. 155-164
    • Ducati, R.G.1    Santos, D.S.2    Basso, L.A.3
  • 13
    • 33847705622 scopus 로고    scopus 로고
    • Mycobacterial shikimate pathway enzymes as targets for drug design
    • Ducati RG, Basso LA, Santos DS, (2007) Mycobacterial shikimate pathway enzymes as targets for drug design. Curr Drug Targets 8: 423-435.
    • (2007) Curr Drug Targets , vol.8 , pp. 423-435
    • Ducati, R.G.1    Basso, L.A.2    Santos, D.S.3
  • 14
    • 68849095530 scopus 로고    scopus 로고
    • Functional analysis of pyrimidine biosynthesis enzymes using the anticancer drug 5-fluorouracil in Caenorhabditis elegans
    • Kim S, Park DH, Kim TH, Hwang M, Shim J, (2009) Functional analysis of pyrimidine biosynthesis enzymes using the anticancer drug 5-fluorouracil in Caenorhabditis elegans. FEBS J 276: 4715-4726.
    • (2009) FEBS J , vol.276 , pp. 4715-4726
    • Kim, S.1    Park, D.H.2    Kim, T.H.3    Hwang, M.4    Shim, J.5
  • 15
    • 0003308915 scopus 로고    scopus 로고
    • Purine and pyrimidine nucleotide synthesis and metabolism
    • Moffatt BA, Ashihara H, (2002) Purine and pyrimidine nucleotide synthesis and metabolism. Arabidopsis Book 1: e0018.
    • (2002) Arabidopsis Book , vol.1
    • Moffatt, B.A.1    Ashihara, H.2
  • 16
    • 0036615470 scopus 로고    scopus 로고
    • Structure of product-bound Bacillus caldolyticus uracil phosphoribosyltransferase confirms ordered sequential substrate binding
    • Kadziola A, Neuhard J, Larsen S, (2002) Structure of product-bound Bacillus caldolyticus uracil phosphoribosyltransferase confirms ordered sequential substrate binding. Acta Crystallogr D Biol Crystallogr 58: 936-945.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 936-945
    • Kadziola, A.1    Neuhard, J.2    Larsen, S.3
  • 18
    • 34247578712 scopus 로고    scopus 로고
    • Identification and characterization of human uracil phosphoribosyltransferase (UPRTase)
    • Li J, Huang S, Chen J, Yang Z, Fei X, et al. (2007) Identification and characterization of human uracil phosphoribosyltransferase (UPRTase). J Hum Genet 52: 415-422.
    • (2007) J Hum Genet , vol.52 , pp. 415-422
    • Li, J.1    Huang, S.2    Chen, J.3    Yang, Z.4    Fei, X.5
  • 19
    • 77952554598 scopus 로고    scopus 로고
    • The kinetic mechanism of human uridine phosphorylase 1: Towards the development of enzyme inhibitors for cancer chemotherapy
    • Renck D, Ducati RG, Palma MS, Santos DS, Basso LA, (2010) The kinetic mechanism of human uridine phosphorylase 1: Towards the development of enzyme inhibitors for cancer chemotherapy. Arch Biochem Biophys 497: 35-42.
    • (2010) Arch Biochem Biophys , vol.497 , pp. 35-42
    • Renck, D.1    Ducati, R.G.2    Palma, M.S.3    Santos, D.S.4    Basso, L.A.5
  • 20
    • 2342600247 scopus 로고    scopus 로고
    • Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase
    • Suzuki NN, Koizumi K, Fukushima M, Matsuda A, Inagaki F, (2004) Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase. Structure 12: 751-764.
    • (2004) Structure , vol.12 , pp. 751-764
    • Suzuki, N.N.1    Koizumi, K.2    Fukushima, M.3    Matsuda, A.4    Inagaki, F.5
  • 21
    • 0029962912 scopus 로고    scopus 로고
    • Intrinsic activity and stability of bifunctional human UMP synthase and its two separate catalytic domains, orotate phosphoribosyltransferase and orotidine-5′-phosphate decarboxylase
    • Yablonski MJ, Pasek DA, Han BD, Jones ME, Traut TW, (1996) Intrinsic activity and stability of bifunctional human UMP synthase and its two separate catalytic domains, orotate phosphoribosyltransferase and orotidine-5′-phosphate decarboxylase. J Biol Chem 271: 10704-10708.
    • (1996) J Biol Chem , vol.271 , pp. 10704-10708
    • Yablonski, M.J.1    Pasek, D.A.2    Han, B.D.3    Jones, M.E.4    Traut, T.W.5
  • 22
    • 33748907720 scopus 로고    scopus 로고
    • Prediction of clinical outcome of fluoropyrimidine-based chemotherapy for gastric cancer patients, in terms of the 5-fluorouracil metabolic pathway
    • Ichikawa W, (2006) Prediction of clinical outcome of fluoropyrimidine-based chemotherapy for gastric cancer patients, in terms of the 5-fluorouracil metabolic pathway. Gastric Cancer 9: 145-155.
    • (2006) Gastric Cancer , vol.9 , pp. 145-155
    • Ichikawa, W.1
  • 23
    • 0242268400 scopus 로고    scopus 로고
    • Genetic requirements for mycobacterial survival during infection
    • Sassetti CM, Rubin EJ, (2003) Genetic requirements for mycobacterial survival during infection. Proc Natl Acad Sci U S A 100: 12989-12994.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 12989-12994
    • Sassetti, C.M.1    Rubin, E.J.2
  • 24
    • 0028953839 scopus 로고
    • Regulation of sCD4-183 gene expression from phage-T7-based vectors in Escherichia coli
    • Kelley KC, Huestis KJ, Austen DA, Sanderson CT, Donoghue MA, et al. (1995) Regulation of sCD4-183 gene expression from phage-T7-based vectors in Escherichia coli. Gene 156: 33-36.
    • (1995) Gene , vol.156 , pp. 33-36
    • Kelley, K.C.1    Huestis, K.J.2    Austen, D.A.3    Sanderson, C.T.4    Donoghue, M.A.5
  • 25
    • 0032536841 scopus 로고    scopus 로고
    • Spontaneous cAMP-dependent derepression of gene expression in stationary phase plays a role in recombinant expression instability
    • Grossman TH, Kawasaki ES, Punreddy SR, Osburne MS, (1998) Spontaneous cAMP-dependent derepression of gene expression in stationary phase plays a role in recombinant expression instability. Gene 209: 95-103.
    • (1998) Gene , vol.209 , pp. 95-103
    • Grossman, T.H.1    Kawasaki, E.S.2    Punreddy, S.R.3    Osburne, M.S.4
  • 26
    • 76749150421 scopus 로고    scopus 로고
    • Structural and functional analyses of Mycobacterium tuberculosis Rv3315c-encoded metal-dependent homotetrameric cytidine deaminase
    • Sánchez-Quitian ZA, Schneider CZ, Ducati RG, de Azevedo WF Jr, Bloch C Jr, et al. (2010) Structural and functional analyses of Mycobacterium tuberculosis Rv3315c-encoded metal-dependent homotetrameric cytidine deaminase. J Struct Biol 169: 413-423.
    • (2010) J Struct Biol , vol.169 , pp. 413-423
    • Sánchez-Quitian, Z.A.1    Schneider, C.Z.2    Ducati, R.G.3    de Azevedo Jr., W.F.4    Bloch Jr., C.5
  • 27
    • 78651254744 scopus 로고    scopus 로고
    • UMP kinase from Mycobacterium tuberculosis: Mode of action and allosteric interactions, and their likely role in pyrimidine metabolism regulation
    • Rostirolla DC, Breda A, Rosado LA, Palma MS, Basso LA, et al. (2011) UMP kinase from Mycobacterium tuberculosis: Mode of action and allosteric interactions, and their likely role in pyrimidine metabolism regulation. Arch Biochem Biophys 505: 202-212.
    • (2011) Arch Biochem Biophys , vol.505 , pp. 202-212
    • Rostirolla, D.C.1    Breda, A.2    Rosado, L.A.3    Palma, M.S.4    Basso, L.A.5
  • 28
    • 79960458435 scopus 로고    scopus 로고
    • Molecular, kinetic, thermodynamic, and structural analyses of Mycobacterium tuberculosis hisD-encoded metal-dependent dimeric histidinol dehydrogenase (EC 1.1.1.23)
    • Nunes JE, Ducati RG, Breda A, Rosado LA, de Souza BM, et al. (2011) Molecular, kinetic, thermodynamic, and structural analyses of Mycobacterium tuberculosis hisD-encoded metal-dependent dimeric histidinol dehydrogenase (EC 1.1.1.23). Arch Biochem Biophys 512: 143-153.
    • (2011) Arch Biochem Biophys , vol.512 , pp. 143-153
    • Nunes, J.E.1    Ducati, R.G.2    Breda, A.3    Rosado, L.A.4    de Souza, B.M.5
  • 29
    • 79952664822 scopus 로고    scopus 로고
    • Recombinant Escherichia coli GMP reductase: kinetic, catalytic and chemical mechanisms, and thermodynamics of enzyme-ligand binary complex formation
    • Martinelli LK, Ducati RG, Rosado LA, Breda A, Selbach BP, et al. (2011) Recombinant Escherichia coli GMP reductase: kinetic, catalytic and chemical mechanisms, and thermodynamics of enzyme-ligand binary complex formation. Mol Biosyst 7: 1289-1305.
    • (2011) Mol Biosyst , vol.7 , pp. 1289-1305
    • Martinelli, L.K.1    Ducati, R.G.2    Rosado, L.A.3    Breda, A.4    Selbach, B.P.5
  • 30
    • 78650153694 scopus 로고    scopus 로고
    • Kinetic mechanism determination and analysis of metal requirement of dehydroquinate synthase from Mycobacterium tuberculosis H37Rv: an essential step in the function-based rational design of anti-TB drugs
    • de Mendonça JD, Adachi O, Rosado LA, Ducati RG, Santos DS, et al. (2011) Kinetic mechanism determination and analysis of metal requirement of dehydroquinate synthase from Mycobacterium tuberculosis H37Rv: an essential step in the function-based rational design of anti-TB drugs. Mol Biosyst 7: 119-128.
    • (2011) Mol Biosyst , vol.7 , pp. 119-128
    • de Mendonça, J.D.1    Adachi, O.2    Rosado, L.A.3    Ducati, R.G.4    Santos, D.S.5
  • 31
    • 0037039462 scopus 로고    scopus 로고
    • The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase
    • Schumacher MA, Bashor CJ, Song MH, Otsu K, Zhu S, et al. (2002) The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase. Proc Natl Acad Sci U S A 99: 78-83.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 78-83
    • Schumacher, M.A.1    Bashor, C.J.2    Song, M.H.3    Otsu, K.4    Zhu, S.5
  • 32
    • 15944364698 scopus 로고    scopus 로고
    • Allosteric properties of the GTP activated and CTP inhibited uracil phosphoribosyltransferase from the thermoacidophilic archaeon Sulfolobus solfataricus
    • Jensen KF, Arent S, Larsen S, Schack L, (2005) Allosteric properties of the GTP activated and CTP inhibited uracil phosphoribosyltransferase from the thermoacidophilic archaeon Sulfolobus solfataricus. FEBS J 272: 1440-1453.
    • (2005) FEBS J , vol.272 , pp. 1440-1453
    • Jensen, K.F.1    Arent, S.2    Larsen, S.3    Schack, L.4
  • 33
    • 0030586769 scopus 로고    scopus 로고
    • Uracil phosphoribosyltransferase from the extreme thermoacidophilic archaebacterium Sulfolobus shibatae is an allosteric enzyme, activated by GTP and inhibited by CTP
    • Linde L, Jensen KF, (1996) Uracil phosphoribosyltransferase from the extreme thermoacidophilic archaebacterium Sulfolobus shibatae is an allosteric enzyme, activated by GTP and inhibited by CTP. Biochim Biophys Acta 1296: 16-22.
    • (1996) Biochim Biophys Acta , vol.1296 , pp. 16-22
    • Linde, L.1    Jensen, K.F.2
  • 34
    • 0028925513 scopus 로고
    • Properties of uracil phosphoribosyltransferase from Giardia intestinalis
    • Dai YP, Lee CS, O'Sullivan WJ, (1995) Properties of uracil phosphoribosyltransferase from Giardia intestinalis. Int J Parasitol 25: 207-214.
    • (1995) Int J Parasitol , vol.25 , pp. 207-214
    • Dai, Y.P.1    Lee, C.S.2    O'Sullivan, W.J.3
  • 35
    • 0031214160 scopus 로고    scopus 로고
    • Recombinant uracil phosphoribosyltransferase from the thermophile Bacillus caldolyticus: expression, purification, and partial characterization
    • Jensen HK, Mikkelsen N, Neuhard J, (1997) Recombinant uracil phosphoribosyltransferase from the thermophile Bacillus caldolyticus: expression, purification, and partial characterization. Protein Expr Purif 10: 356-364.
    • (1997) Protein Expr Purif , vol.10 , pp. 356-364
    • Jensen, H.K.1    Mikkelsen, N.2    Neuhard, J.3
  • 36
    • 0022621213 scopus 로고
    • Purification and some properties of uracil phosphoribosyltransferase from Escherichia coli K12
    • Rasmussen UB, Mygind B, Nygaard P, (1986) Purification and some properties of uracil phosphoribosyltransferase from Escherichia coli K12. Biochim Biophys Acta 881: 268-275.
    • (1986) Biochim Biophys Acta , vol.881 , pp. 268-275
    • Rasmussen, U.B.1    Mygind, B.2    Nygaard, P.3
  • 37
    • 0029768750 scopus 로고    scopus 로고
    • Different oligomeric states are involved in the allosteric behavior of uracil phosphoribosyltransferase from Escherichia coli
    • Jensen KF, Mygind B, (1996) Different oligomeric states are involved in the allosteric behavior of uracil phosphoribosyltransferase from Escherichia coli. Eur J Biochem 240: 637-645.
    • (1996) Eur J Biochem , vol.240 , pp. 637-645
    • Jensen, K.F.1    Mygind, B.2
  • 38
    • 51549113380 scopus 로고    scopus 로고
    • Screening for organic phosphorus compounds in aquatic sediments by liquid chromatography coupled to ICP-AES and ESI-MS/MS
    • De Brabandere H, Forsgard N, Israelsson L, Petterson J, Rydin E, et al. (2008) Screening for organic phosphorus compounds in aquatic sediments by liquid chromatography coupled to ICP-AES and ESI-MS/MS. Anal Chem 80: 6689-6697.
    • (2008) Anal Chem , vol.80 , pp. 6689-6697
    • De Brabandere, H.1    Forsgard, N.2    Israelsson, L.3    Petterson, J.4    Rydin, E.5
  • 40
    • 70349417705 scopus 로고    scopus 로고
    • Structural and kinetic studies of the allosteric transition in Sulfolobus solfataricus uracil phosphoribosyltransferase: Permanent activation by engineering of the C-terminus
    • Christoffersen S, Kadziola A, Johansson E, Rasmussen M, Willemoës M, et al. (2009) Structural and kinetic studies of the allosteric transition in Sulfolobus solfataricus uracil phosphoribosyltransferase: Permanent activation by engineering of the C-terminus. J Mol Biol 393: 464-477.
    • (2009) J Mol Biol , vol.393 , pp. 464-477
    • Christoffersen, S.1    Kadziola, A.2    Johansson, E.3    Rasmussen, M.4    Willemoës, M.5
  • 44
    • 69549137853 scopus 로고    scopus 로고
    • Analysis of cooperativity by isothermal titration calorimetry
    • Brown A, (2009) Analysis of cooperativity by isothermal titration calorimetry. Int J Mol Sci 10: 3457-3477.
    • (2009) Int J Mol Sci , vol.10 , pp. 3457-3477
    • Brown, A.1
  • 45
    • 0033574207 scopus 로고    scopus 로고
    • Kinetic mechanism of uracil phosphoribosyltransferase from Escherichia coli and catalytic importance of the conserved proline in the PRPP binding site
    • Lundegaard C, Jensen KF, (1999) Kinetic mechanism of uracil phosphoribosyltransferase from Escherichia coli and catalytic importance of the conserved proline in the PRPP binding site. Biochemistry 38: 3327-3334.
    • (1999) Biochemistry , vol.38 , pp. 3327-3334
    • Lundegaard, C.1    Jensen, K.F.2
  • 46
    • 0032526987 scopus 로고    scopus 로고
    • Crystal structures of Toxoplasma gondii uracil phosphoribosyltransferase reveal the atomic basis of pyrimidine discrimination and prodrug binding
    • Schumacher MA, Carter D, Scott DM, Roos DS, Ullman B, et al. (1998) Crystal structures of Toxoplasma gondii uracil phosphoribosyltransferase reveal the atomic basis of pyrimidine discrimination and prodrug binding. EMBO J 17: 3219-3232.
    • (1998) EMBO J , vol.17 , pp. 3219-3232
    • Schumacher, M.A.1    Carter, D.2    Scott, D.M.3    Roos, D.S.4    Ullman, B.5
  • 47
    • 12344255727 scopus 로고    scopus 로고
    • Allosteric regulation and communication between subunits in uracil phosphoribosyltransferase from Sulfolobus solfataricus
    • Arent S, Harris P, Jensen KF, Larsen S, (2005) Allosteric regulation and communication between subunits in uracil phosphoribosyltransferase from Sulfolobus solfataricus. Biochemistry 44: 883-892.
    • (2005) Biochemistry , vol.44 , pp. 883-892
    • Arent, S.1    Harris, P.2    Jensen, K.F.3    Larsen, S.4
  • 48
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 49
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 50
    • 33747051749 scopus 로고    scopus 로고
    • Bradykinin-related peptides from Phyllomedusa hypochondrialis
    • Brand GD, Krause FC, Silva LP, Leite JR, Melo JA, et al. (2006) Bradykinin-related peptides from Phyllomedusa hypochondrialis. Peptides 27: 2137-2146.
    • (2006) Peptides , vol.27 , pp. 2137-2146
    • Brand, G.D.1    Krause, F.C.2    Silva, L.P.3    Leite, J.R.4    Melo, J.A.5
  • 51
    • 79952787283 scopus 로고    scopus 로고
    • Analysis of molecular targets of Mycobacterium tuberculosis by analytical ultracentrifugation
    • Borges JC, Ramos CH, (2011) Analysis of molecular targets of Mycobacterium tuberculosis by analytical ultracentrifugation. Curr Med Chem 18: 1276-1285.
    • (2011) Curr Med Chem , vol.18 , pp. 1276-1285
    • Borges, J.C.1    Ramos, C.H.2
  • 52
    • 0018786292 scopus 로고
    • Baker's yeast UMP:pyrophosphate phosphoribosyltransferase. Purification, enzymatic and kinetic properties
    • Natalini P, Ruggieri S, Santarelli I, Vita A, Magni G, (1979) Baker's yeast UMP:pyrophosphate phosphoribosyltransferase. Purification, enzymatic and kinetic properties. J Biol Chem 254: 1558-1563.
    • (1979) J Biol Chem , vol.254 , pp. 1558-1563
    • Natalini, P.1    Ruggieri, S.2    Santarelli, I.3    Vita, A.4    Magni, G.5
  • 54
    • 20444448766 scopus 로고    scopus 로고
    • Live attenuated mutants of Mycobacterium tuberculosis as candidate vaccines against tuberculosis
    • Sambandamurthy VK, Jacobs WR Jr, (2005) Live attenuated mutants of Mycobacterium tuberculosis as candidate vaccines against tuberculosis. Microbes Infect 7: 955-961.
    • (2005) Microbes Infect , vol.7 , pp. 955-961
    • Sambandamurthy, V.K.1    Jacobs Jr., W.R.2
  • 55
    • 21044444574 scopus 로고    scopus 로고
    • New live mycobacterial vaccines: the Geneva consensus on essential steps towards clinical development
    • Kamath AT, Fruth U, Brennan MJ, Dobbelaer R, Hubrechts P, et al. (2005) New live mycobacterial vaccines: the Geneva consensus on essential steps towards clinical development. Vaccine 23: 3753-3761.
    • (2005) Vaccine , vol.23 , pp. 3753-3761
    • Kamath, A.T.1    Fruth, U.2    Brennan, M.J.3    Dobbelaer, R.4    Hubrechts, P.5


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