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Volumn 99, Issue 22, 2015, Pages 9577-9589

Increased riboflavin production by manipulation of inosine 5′-monophosphate dehydrogenase in Ashbya gossypii

Author keywords

Ashbya gossypii; Inosine 5 monophosphate dehydrogenase; Metabolic engineering; Riboflavin

Indexed keywords

ENZYMES; METABOLISM; MOBILE SECURITY; NUCLEIC ACIDS; NUCLEOTIDES; POSITIVE IONS;

EID: 84946479566     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-015-6710-2     Document Type: Article
Times cited : (35)

References (64)
  • 2
    • 0034045586 scopus 로고    scopus 로고
    • Mycophenolate mofetil and its mechanisms of action
    • COI: 1:CAS:528:DC%2BD3cXktlKkt7o%3D, PID: 10878285
    • Allison AC, Eugui EM (2000) Mycophenolate mofetil and its mechanisms of action. Immunopharmacology 47(2–3):85–118
    • (2000) Immunopharmacology , vol.47 , Issue.2-3 , pp. 85-118
    • Allison, A.C.1    Eugui, E.M.2
  • 3
    • 68349144268 scopus 로고    scopus 로고
    • Structure of the calx-β domain of the integrin β4 subunit: insights into function and cation-independent stability
    • PID: 19622870
    • Alonso-García N, Inglés-Prieto A, Sonnenberg A, de Pereda JM (2009) Structure of the calx-β domain of the integrin β4 subunit: insights into function and cation-independent stability. Acta Crystallogr D Biol Crystallogr 65(Pt 8):858–871. doi:10.1107/S0907444909018745
    • (2009) Acta Crystallogr D Biol Crystallogr , vol.65 , pp. 858-871
    • Alonso-García, N.1    Inglés-Prieto, A.2    Sonnenberg, A.3    de Pereda, J.M.4
  • 4
    • 0000678343 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin
    • Neidhardt FC, Curtiss R, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE, (eds), ASM Press, Washington DC
    • Bacher A, Eberhardt S, Richter G (1996) Biosynthesis of riboflavin. In: Neidhardt FC, Curtiss III R, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (eds) Escherichia coli and Salmonella: cellular and molecular biology. ASM Press, Washington DC, pp. 657–664
    • (1996) Escherichia coli and Salmonella: cellular and molecular biology , pp. 657-664
    • Bacher, A.1    Eberhardt, S.2    Richter, G.3
  • 5
    • 0033624686 scopus 로고    scopus 로고
    • Biosynthesis of vitamin B2 (riboflavin)
    • COI: 1:CAS:528:DC%2BD3cXmsVKmu7o%3D, PID: 10940330
    • Bacher A, Eberhardt S, Fischer M, Kis K, Richter G (2000) Biosynthesis of vitamin B2 (riboflavin). Annu Rev Nutr 20:153–167. doi:10.1146/annurev.nutr.20.1.153
    • (2000) Annu Rev Nutr , vol.20 , pp. 153-167
    • Bacher, A.1    Eberhardt, S.2    Fischer, M.3    Kis, K.4    Richter, G.5
  • 6
    • 0031016272 scopus 로고    scopus 로고
    • The structure of a domain common to archaebacteria and the homocystinuria disease protein
    • COI: 1:CAS:528:DyaK2sXhtVOqsr0%3D, PID: 9020585
    • Bateman A (1997) The structure of a domain common to archaebacteria and the homocystinuria disease protein. Trends Biochem Sci 22(1):12–13
    • (1997) Trends Biochem Sci , vol.22 , Issue.1 , pp. 12-13
    • Bateman, A.1
  • 8
    • 77953426717 scopus 로고    scopus 로고
    • Inosine monophosphate dehydrogenase as a target for antiviral, anticancer, antimicrobial and immunosuppressive therapeutics
    • COI: 1:CAS:528:DC%2BC3cXosVSquw%3D%3D, PID: 21426047
    • Braun-Sand SB, Peetz M (2010) Inosine monophosphate dehydrogenase as a target for antiviral, anticancer, antimicrobial and immunosuppressive therapeutics. Future Med Chem 2(1):81–92. doi:10.4155/fmc.09.147
    • (2010) Future Med Chem , vol.2 , Issue.1 , pp. 81-92
    • Braun-Sand, S.B.1    Peetz, M.2
  • 9
    • 0034043778 scopus 로고    scopus 로고
    • Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis
    • COI: 1:CAS:528:DC%2BD3cXisVSgt7g%3D, PID: 10742046
    • Castresana J (2000) Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis. Mol Biol Evol 17(4):540–552
    • (2000) Mol Biol Evol , vol.17 , Issue.4 , pp. 540-552
    • Castresana, J.1
  • 10
    • 33646439982 scopus 로고    scopus 로고
    • Identification of type 1 inosine monophosphate dehydrogenase as an antiangiogenic drug target
    • COI: 1:CAS:528:DC%2BD28XjtVaqurc%3D, PID: 16640327
    • Chong CR, Qian DZ, Pan F, Wei Y, Pili R, Sullivan Jr DJ, Liu JO (2006) Identification of type 1 inosine monophosphate dehydrogenase as an antiangiogenic drug target. J Med Chem 49(9):2677–2680. doi:10.1021/jm051225t
    • (2006) J Med Chem , vol.49 , Issue.9 , pp. 2677-2680
    • Chong, C.R.1    Qian, D.Z.2    Pan, F.3    Wei, Y.4    Pili, R.5    Sullivan, D.J.6    Liu, J.O.7
  • 11
    • 0031172735 scopus 로고    scopus 로고
    • Folates and one-carbon metabolism in plants and fungi
    • COI: 1:CAS:528:DyaK2sXjsl2rtLs%3D, PID: 9190084
    • Cossins EA, Chen L (1997) Folates and one-carbon metabolism in plants and fungi. Phytochemistry 45(3):437–452
    • (1997) Phytochemistry , vol.45 , Issue.3 , pp. 437-452
    • Cossins, E.A.1    Chen, L.2
  • 13
    • 33846339422 scopus 로고    scopus 로고
    • Kinetic characterization of inosine monophosphate dehydrogenase of Leishmania donovani
    • COI: 1:CAS:528:DC%2BD2sXnslGmsQ%3D%3D, PID: 17173987
    • Dobie F, Berg A, Boitz J, Jardim A (2007) Kinetic characterization of inosine monophosphate dehydrogenase of Leishmania donovani. Mol Biochem Parasitol 152(1):11–21. doi:10.1016/j.molbiopara.2006.11.007
    • (2007) Mol Biochem Parasitol , vol.152 , Issue.1 , pp. 11-21
    • Dobie, F.1    Berg, A.2    Boitz, J.3    Jardim, A.4
  • 15
    • 0037940408 scopus 로고    scopus 로고
    • Physiological consequence of disruption of the VMA1 gene in the riboflavin overproducer Ashbya gossypii
    • COI: 1:CAS:528:DyaK1MXisVWltLs%3D, PID: 10092625
    • Forster C, Santos MA, Ruffert S, Kramer R, Revuelta JL (1999) Physiological consequence of disruption of the VMA1 gene in the riboflavin overproducer Ashbya gossypii. J Biol Chem 274(14):9442–9448
    • (1999) J Biol Chem , vol.274 , Issue.14 , pp. 9442-9448
    • Forster, C.1    Santos, M.A.2    Ruffert, S.3    Kramer, R.4    Revuelta, J.L.5
  • 16
    • 0037417754 scopus 로고    scopus 로고
    • The immunosuppressive agent mizoribine monophosphate forms a transition state analogue complex with inosine monophosphate dehydrogenase
    • COI: 1:CAS:528:DC%2BD3sXlsFyk, PID: 12549902
    • Gan L, Seyedsayamdost M, Shuto S, Matsuda A, Petsko G, Hedstrom L (2003) The immunosuppressive agent mizoribine monophosphate forms a transition state analogue complex with inosine monophosphate dehydrogenase. Biochemistry 42(4):857–863. doi:10.1021/bi0271401
    • (2003) Biochemistry , vol.42 , Issue.4 , pp. 857-863
    • Gan, L.1    Seyedsayamdost, M.2    Shuto, S.3    Matsuda, A.4    Petsko, G.5    Hedstrom, L.6
  • 18
    • 0018600265 scopus 로고
    • Inosine 5′-monophosphate dehydrogenase of Escherichia coli. Purification by affinity chromatography, subunit structure and inhibition by guanosine 5′-monophosphate
    • COI: 1:CAS:528:DyaL3cXht1ertbw%3D, PID: 44191
    • Gilbert H, Lowe C, Drabble W (1979) Inosine 5′-monophosphate dehydrogenase of Escherichia coli. Purification by affinity chromatography, subunit structure and inhibition by guanosine 5′-monophosphate. Biochem J 183(3):481–494
    • (1979) Biochem J , vol.183 , Issue.3 , pp. 481-494
    • Gilbert, H.1    Lowe, C.2    Drabble, W.3
  • 19
    • 0027101755 scopus 로고
    • Tetrahydrobiopterin synthesis. An absolute requirement for cytokine-induced nitric oxide generation by vascular smooth muscle
    • COI: 1:CAS:528:DyaK38XmtlSqsbY%3D, PID: 1281471
    • Gross SS, Levi R (1992) Tetrahydrobiopterin synthesis. An absolute requirement for cytokine-induced nitric oxide generation by vascular smooth muscle. J Biol Chem 267(36):25722–25729
    • (1992) J Biol Chem , vol.267 , Issue.36 , pp. 25722-25729
    • Gross, S.S.1    Levi, R.2
  • 20
    • 67650649489 scopus 로고    scopus 로고
    • IMP dehydrogenase: structure, mechanism, and inhibition
    • COI: 1:CAS:528:DC%2BD1MXmsFamtbo%3D, PID: 19480389
    • Hedstrom L (2009) IMP dehydrogenase: structure, mechanism, and inhibition. Chem Rev 109(7):2903–2928. doi:10.1021/cr900021w
    • (2009) Chem Rev , vol.109 , Issue.7 , pp. 2903-2928
    • Hedstrom, L.1
  • 21
    • 79957938394 scopus 로고    scopus 로고
    • The antibiotic potential of prokaryotic IMP dehydrogenase inhibitors
    • COI: 1:CAS:528:DC%2BC3MXmvFehurw%3D, PID: 21517780
    • Hedstrom L, Liechti G, Goldberg JB, Gollapalli DR (2011) The antibiotic potential of prokaryotic IMP dehydrogenase inhibitors. Curr Med Chem 18(13):1909–1918
    • (2011) Curr Med Chem , vol.18 , Issue.13 , pp. 1909-1918
    • Hedstrom, L.1    Liechti, G.2    Goldberg, J.B.3    Gollapalli, D.R.4
  • 22
    • 0042208190 scopus 로고    scopus 로고
    • Functional distinctions between IMP dehydrogenase genes in providing mycophenolate resistance and guanine prototrophy to yeast
    • COI: 1:CAS:528:DC%2BD3sXlsl2nt7k%3D, PID: 12746440
    • Hyle J, Shaw R, Reines D (2003) Functional distinctions between IMP dehydrogenase genes in providing mycophenolate resistance and guanine prototrophy to yeast. J Biol Chem 278(31):28470–28478. doi:10.1074/jbc.M303736200
    • (2003) J Biol Chem , vol.278 , Issue.31 , pp. 28470-28478
    • Hyle, J.1    Shaw, R.2    Reines, D.3
  • 23
    • 79960001809 scopus 로고    scopus 로고
    • FFAS server: novel features and applications
    • Jaroszewski L, Li Z, Cai XH, Weber C, Godzik A (2011) FFAS server: novel features and applications. Nucleic Acids Res 39 (Web Server issue):W38-44 doi:10.1093/nar/gkr441
    • (2011) Nucleic Acids Res , vol.39 , Issue.Web Server issue , pp. 38-44
    • Jaroszewski, L.1    Li, Z.2    Cai, X.H.3    Weber, C.4    Godzik, A.5
  • 24
    • 28844493927 scopus 로고    scopus 로고
    • Dissection of the molecular basis of mycophenolate resistance in Saccharomyces cerevisiae
    • COI: 1:CAS:528:DC%2BD2MXhtlSqs7%2FK, PID: 16278936
    • Jenks MH, Reines D (2005) Dissection of the molecular basis of mycophenolate resistance in Saccharomyces cerevisiae. Yeast 22(15):1181–1190. doi:10.1002/yea.1300
    • (2005) Yeast , vol.22 , Issue.15 , pp. 1181-1190
    • Jenks, M.H.1    Reines, D.2
  • 25
    • 26844495569 scopus 로고    scopus 로고
    • Metabolic engineering of the purine pathway for riboflavin production in Ashbya gossypii
    • PID: 16204483
    • Jiménez A, Santos MA, Pompejus M, Revuelta JL (2005) Metabolic engineering of the purine pathway for riboflavin production in Ashbya gossypii. Appl Environ Microbiol 71(10):5743–5751. doi:10.1128/AEM.71.10.5743-5751.2005
    • (2005) Appl Environ Microbiol , vol.71 , Issue.10 , pp. 5743-5751
    • Jiménez, A.1    Santos, M.A.2    Pompejus, M.3    Revuelta, J.L.4
  • 26
    • 52649091290 scopus 로고    scopus 로고
    • Phosphoribosyl pyrophosphate synthetase activity affects growth and riboflavin production in Ashbya gossypii
    • PID: 18782443
    • Jiménez A, Santos MA, Revuelta JL (2008) Phosphoribosyl pyrophosphate synthetase activity affects growth and riboflavin production in Ashbya gossypii. BMC Biotechnol 8:67. doi:10.1186/1472-6750-8-67
    • (2008) BMC Biotechnol , vol.8 , pp. 67
    • Jiménez, A.1    Santos, M.A.2    Revuelta, J.L.3
  • 27
    • 84903614317 scopus 로고    scopus 로고
    • Developments in optics and performance at BL13-XALOC, the macromolecular crystallography beamline at the ALBA synchrotron
    • COI: 1:CAS:528:DC%2BC2cXhtVGksr7J, PID: 24971961
    • Juanhuix J, Gil-Ortiz F, Cuni G, Colldelram C, Nicolas J, Lidon J, Boter E, Ruget C, Ferrer S, Benach J (2014) Developments in optics and performance at BL13-XALOC, the macromolecular crystallography beamline at the ALBA synchrotron. J Synchrotron Radiat 21(Pt 4):679–689. doi:10.1107/S160057751400825X
    • (2014) J Synchrotron Radiat , vol.21 , pp. 679-689
    • Juanhuix, J.1    Gil-Ortiz, F.2    Cuni, G.3    Colldelram, C.4    Nicolas, J.5    Lidon, J.6    Boter, E.7    Ruget, C.8    Ferrer, S.9    Benach, J.10
  • 28
    • 76449099287 scopus 로고    scopus 로고
    • Xds
    • COI: 1:CAS:528:DC%2BC3cXhs1SisLc%3D, PID: 20124692
    • Kabsch W (2010) Xds. Acta Crystallogr D Biol Crystallogr 66(Pt 2):125–132. doi:10.1107/S0907444909047337
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 125-132
    • Kabsch, W.1
  • 29
    • 84858005266 scopus 로고    scopus 로고
    • Riboflavin production by Ashbya gossypii
    • COI: 1:CAS:528:DC%2BC38Xjs1Olu7c%3D, PID: 22187081
    • Kato T, Park E (2012) Riboflavin production by Ashbya gossypii. Biotechnol Lett 34(4):611–618. doi:10.1007/s10529-011-0833-z
    • (2012) Biotechnol Lett , vol.34 , Issue.4 , pp. 611-618
    • Kato, T.1    Park, E.2
  • 31
  • 32
    • 84893351015 scopus 로고    scopus 로고
    • Strain design of Ashbya gossypii for single-cell oil production
    • COI: 1:CAS:528:DC%2BC2cXjtVSkt70%3D, PID: 24317081
    • Ledesma-Amaro R, Santos MA, Jiménez A, Revuelta JL (2014a) Strain design of Ashbya gossypii for single-cell oil production. Appl Environ Microbiol 80(4):1237–1244. doi:10.1128/AEM.03560-13
    • (2014) Appl Environ Microbiol , vol.80 , Issue.4 , pp. 1237-1244
    • Ledesma-Amaro, R.1    Santos, M.A.2    Jiménez, A.3    Revuelta, J.L.4
  • 33
    • 84904904888 scopus 로고    scopus 로고
    • Tuning single-cell oil production in Ashbya gossypii by engineering the elongation and desaturation systems
    • COI: 1:CAS:528:DC%2BC2cXnt1eksr8%3D, PID: 24668265
    • Ledesma-Amaro R, Santos MA, Jiménez A, Revuelta JL (2014b) Tuning single-cell oil production in Ashbya gossypii by engineering the elongation and desaturation systems. Biotechnol Bioeng 111(9):1782–1791. doi:10.1002/bit.25245
    • (2014) Biotechnol Bioeng , vol.111 , Issue.9 , pp. 1782-1791
    • Ledesma-Amaro, R.1    Santos, M.A.2    Jiménez, A.3    Revuelta, J.L.4
  • 34
    • 84928561536 scopus 로고    scopus 로고
    • Increased production of inosine and guanosine by means of metabolic engineering of the purine pathway in Ashbya gossypii
    • PID: 25889888
    • Ledesma-Amaro R, Buey RM, Revuelta JL (2015) Increased production of inosine and guanosine by means of metabolic engineering of the purine pathway in Ashbya gossypii. Microb Cell Fact 14:58. doi:10.1186/s12934-015-0234-4
    • (2015) Microb Cell Fact , vol.14 , pp. 58
    • Ledesma-Amaro, R.1    Buey, R.M.2    Revuelta, J.L.3
  • 35
    • 33645227485 scopus 로고    scopus 로고
    • De novo GMP synthesis is required for axon guidance in Drosophila
    • COI: 1:CAS:528:DC%2BD28XjvV2ltL8%3D, PID: 16322525
    • Long H, Cameron S, Yu L, Rao Y (2006) De novo GMP synthesis is required for axon guidance in Drosophila. Genetics 172(3):1633–1642. doi:10.1534/genetics.105.042911
    • (2006) Genetics , vol.172 , Issue.3 , pp. 1633-1642
    • Long, H.1    Cameron, S.2    Yu, L.3    Rao, Y.4
  • 38
    • 4344656352 scopus 로고    scopus 로고
    • Detection of the mycophenolate-inhibited form of IMP dehydrogenase in vivo
    • COI: 1:CAS:528:DC%2BD2cXntFeksbg%3D, PID: 15292516
    • McPhillips C, Hyle J, Reines D (2004) Detection of the mycophenolate-inhibited form of IMP dehydrogenase in vivo. Proc Natl Acad Sci U S A 101(33):12171–12176. doi:10.1073/pnas.0403341101
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.33 , pp. 12171-12176
    • McPhillips, C.1    Hyle, J.2    Reines, D.3
  • 40
    • 0015180175 scopus 로고
    • The biological significance of purine salvage
    • COI: 1:CAS:528:DyaE3MXltVCqu7g%3D, PID: 4330582
    • Murray AW (1971) The biological significance of purine salvage. Annu Rev Biochem 40:811–826. doi:10.1146/annurev.bi.40.070171.004115
    • (1971) Annu Rev Biochem , vol.40 , pp. 811-826
    • Murray, A.W.1
  • 41
    • 0036384350 scopus 로고    scopus 로고
    • One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions
    • COI: 1:CAS:528:DC%2BD38Xms1Wmurg%3D, PID: 12206759
    • 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(5):741–765
    • (2002) J Mol Biol , vol.321 , Issue.5 , pp. 741-765
    • Nagano, N.1    Orengo, C.A.2    Thornton, J.M.3
  • 42
    • 36849021519 scopus 로고    scopus 로고
    • Inosine monophosphate dehydrogenase as a probe in antiviral drug discovery
    • COI: 1:CAS:528:DC%2BD2sXhsVaksr7E, PID: 18046958
    • Nair V, Shu Q (2007) Inosine monophosphate dehydrogenase as a probe in antiviral drug discovery. Antivir Chem Chemother 18(5):245–258
    • (2007) Antivir Chem Chemother , vol.18 , Issue.5 , pp. 245-258
    • Nair, V.1    Shu, Q.2
  • 43
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: an application to display phylogenetic trees on personal computers
    • COI: 1:STN:280:DyaK2s%2FlvVSgtg%3D%3D, PID: 8902363
    • Page RD (1996) TreeView: an application to display phylogenetic trees on personal computers. Comput Appl Biosci 12(4):357–358
    • (1996) Comput Appl Biosci , vol.12 , Issue.4 , pp. 357-358
    • Page, R.D.1
  • 44
    • 80052627796 scopus 로고    scopus 로고
    • The improvement of riboflavin production in Ashbya gossypii via disparity mutagenesis and DNA microarray analysis
    • COI: 1:CAS:528:DC%2BC3MXhtVSitb3E, PID: 21573938
    • Park EY, Ito Y, Nariyama M, Sugimoto T, Lies D, Kato T (2011) The improvement of riboflavin production in Ashbya gossypii via disparity mutagenesis and DNA microarray analysis. Appl Microbiol Biotechnol 91(5):1315–1326. doi:10.1007/s00253-011-3325-0
    • (2011) Appl Microbiol Biotechnol , vol.91 , Issue.5 , pp. 1315-1326
    • Park, E.Y.1    Ito, Y.2    Nariyama, M.3    Sugimoto, T.4    Lies, D.5    Kato, T.6
  • 45
    • 41049085632 scopus 로고    scopus 로고
    • The CBS subdomain of inosine 5′-monophosphate dehydrogenase regulates purine nucleotide turnover
    • COI: 1:CAS:528:DC%2BD1cXkvVyqtb4%3D, PID: 18312263
    • Pimkin M, Markham G (2008) The CBS subdomain of inosine 5′-monophosphate dehydrogenase regulates purine nucleotide turnover. Mol Microbiol 68(2):342–359. doi:10.1111/j.1365-2958.2008.06153.x
    • (2008) Mol Microbiol , vol.68 , Issue.2 , pp. 342-359
    • Pimkin, M.1    Markham, G.2
  • 47
    • 0347297575 scopus 로고    scopus 로고
    • Crystal structure of Tritrichomonas foetus inosine monophosphate dehydrogenase in complex with the inhibitor ribavirin monophosphate reveals a catalysis-dependent ion-binding site
    • Prosise GL, Wu JZ, Luecke H (2002) Crystal structure of Tritrichomonas foetus inosine monophosphate dehydrogenase in complex with the inhibitor ribavirin monophosphate reveals a catalysis-dependent ion-binding site. J Biol Chem 277(52):50654-50659 doi:10.1074/jbc.M208330200
    • (2002) J Biol Chem , vol.277 , Issue.52 , pp. 50654-50659
    • Prosise, G.L.1    Wu, J.Z.2    Luecke, H.3
  • 48
    • 84875506155 scopus 로고    scopus 로고
    • Structure of Pseudomonas aeruginosa inosine 5′-monophosphate dehydrogenase
    • COI: 1:CAS:528:DC%2BC3sXlt1ahu7g%3D, PID: 23519796
    • Rao V, Shepherd S, Owen R, Hunter W (2013) Structure of Pseudomonas aeruginosa inosine 5′-monophosphate dehydrogenase. Acta Crystallogr Sect F Struct Biol Cryst Commun 69(Pt 3):243–247. doi:10.1107/s1744309113002352
    • (2013) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.69 , pp. 243-247
    • Rao, V.1    Shepherd, S.2    Owen, R.3    Hunter, W.4
  • 49
    • 33748604738 scopus 로고    scopus 로고
    • Inosine 5′-monophosphate dehydrogenase inhibitors for the treatment of autoimmune diseases
    • COI: 1:CAS:528:DC%2BD28XpsFKntbc%3D, PID: 17002220
    • Ratcliffe AJ (2006) Inosine 5′-monophosphate dehydrogenase inhibitors for the treatment of autoimmune diseases. Curr Opin Drug Discov Devel 9(5):595–605
    • (2006) Curr Opin Drug Discov Devel , vol.9 , Issue.5 , pp. 595-605
    • Ratcliffe, A.J.1
  • 50
    • 84946486310 scopus 로고    scopus 로고
    • Revuelta JL, Buitrago MJ, Santos MA (1998) Riboflavin biosynthesis in fungi. Patent nr WO9526406 In., C12N15/52(edn: BASF AG (DE))
    • Revuelta JL, Buitrago MJ, Santos MA (1998) Riboflavin biosynthesis in fungi. Patent nr WO9526406 In., C12N15/52(edn: BASF AG (DE))
  • 51
    • 80053409626 scopus 로고    scopus 로고
    • Allosteric activation via kinetic control: potassium accelerates a conformational change in IMP dehydrogenase
    • COI: 1:CAS:528:DC%2BC3MXhtFelurbE, PID: 21870820
    • Riera TV, Zheng L, Josephine HR, Min D, Yang W, Hedstrom L (2011) Allosteric activation via kinetic control: potassium accelerates a conformational change in IMP dehydrogenase. Biochemistry 50(39):8508–8518. doi:10.1021/bi200785s
    • (2011) Biochemistry , vol.50 , Issue.39 , pp. 8508-8518
    • Riera, T.V.1    Zheng, L.2    Josephine, H.R.3    Min, D.4    Yang, W.5    Hedstrom, L.6
  • 52
    • 0034091478 scopus 로고    scopus 로고
    • Three biotechnical processes using Ashbya gossypii, Candida famata, or Bacillus subtilis compete with chemical riboflavin production
    • Stahmann K, Revuelta J, Seulberger H (2000) Three biotechnical processes using Ashbya gossypii, Candida famata, or Bacillus subtilis compete with chemical riboflavin production. Appl Microbiol Biotechnol 53(5):509-516 doi:10.1007/s002530051649
    • (2000) Appl Microbiol Biotechnol , vol.53 , Issue.5 , pp. 509-516
    • Stahmann, K.1    Revuelta, J.2    Seulberger, H.3
  • 54
    • 0028143584 scopus 로고
    • Physiological concentrations of purines and pyrimidines
    • Traut TW (1994) Physiological concentrations of purines and pyrimidines. Mol Cell Biochem 140(1):1-22
    • (1994) Mol Cell Biochem , vol.140 , Issue.1 , pp. 1-22
    • Traut, T.W.1
  • 55
    • 0042038217 scopus 로고
    • Imidazole-2-thiones: synthesis, structure and properties
    • COI: 1:CAS:528:DyaK3MXlsFyqu78%3D
    • Trzhtsinskaya BV, Abramova ND (1991) Imidazole-2-thiones: synthesis, structure and properties. Sulfur Reports 10:389–421
    • (1991) Sulfur Reports , vol.10 , pp. 389-421
    • Trzhtsinskaya, B.V.1    Abramova, N.D.2
  • 56
    • 38349082511 scopus 로고    scopus 로고
    • Targeting a prokaryotic protein in a eukaryotic pathogen: identification of lead compounds against cryptosporidiosis
    • COI: 1:CAS:528:DC%2BD1cXpt12qug%3D%3D, PID: 18215774
    • Umejiego NN, Gollapalli D, Sharling L, Volftsun A, Lu J, Benjamin NN, Stroupe AH, Riera TV, Striepen B, Hedstrom L (2008) Targeting a prokaryotic protein in a eukaryotic pathogen: identification of lead compounds against cryptosporidiosis. Chem Biol 15(1):70–77. doi:10.1016/j.chembiol.2007.12.010
    • (2008) Chem Biol , vol.15 , Issue.1 , pp. 70-77
    • Umejiego, N.N.1    Gollapalli, D.2    Sharling, L.3    Volftsun, A.4    Lu, J.5    Benjamin, N.N.6    Stroupe, A.H.7    Riera, T.V.8    Striepen, B.9    Hedstrom, L.10
  • 57
    • 0026530031 scopus 로고
    • Production of vitamins, coenzymes and related biochemicals by biotechnological processes
    • COI: 1:CAS:528:DyaK38Xitleku7w%3D, PID: 1368195
    • Vandamme EJ (1992) Production of vitamins, coenzymes and related biochemicals by biotechnological processes. J Chem Technol Biotechnol 53(4):313–327
    • (1992) J Chem Technol Biotechnol , vol.53 , Issue.4 , pp. 313-327
    • Vandamme, E.J.1
  • 58
    • 84883747519 scopus 로고    scopus 로고
    • Molecular determinants of sporulation in Ashbya gossypii
    • COI: 1:CAS:528:DC%2BC3sXhvVCjt7%2FF, PID: 23833180
    • Wasserstrom L, Lengeler KB, Walther A, Wendland J (2013) Molecular determinants of sporulation in Ashbya gossypii. Genetics 195(1):87–99. doi:10.1534/genetics.113.151019
    • (2013) Genetics , vol.195 , Issue.1 , pp. 87-99
    • Wasserstrom, L.1    Lengeler, K.B.2    Walther, A.3    Wendland, J.4
  • 59
    • 0033971416 scopus 로고    scopus 로고
    • PCR-based gene targeting in the filamentous fungus Ashbya gossypii
    • COI: 1:CAS:528:DC%2BD3cXhsFCjuro%3D, PID: 10721732
    • Wendland J, Ayad-Durieux Y, Knechtle P, Rebischung C, Philippsen P (2000) PCR-based gene targeting in the filamentous fungus Ashbya gossypii. Gene 242(1–2):381–391
    • (2000) Gene , vol.242 , Issue.1-2 , pp. 381-391
    • Wendland, J.1    Ayad-Durieux, Y.2    Knechtle, P.3    Rebischung, C.4    Philippsen, P.5
  • 60
    • 79960285649 scopus 로고    scopus 로고
    • Characterization of α-factor pheromone and pheromone receptor genes of Ashbya gossypii
    • COI: 1:CAS:528:DC%2BC3MXpvVyhs7o%3D, PID: 21489136
    • Wendland J, Dunkler A, Walther A (2011) Characterization of α-factor pheromone and pheromone receptor genes of Ashbya gossypii. FEMS Yeast Res 11(5):418–429. doi:10.1111/j.1567-1364.2011.00732.x
    • (2011) FEMS Yeast Res , vol.11 , Issue.5 , pp. 418-429
    • Wendland, J.1    Dunkler, A.2    Walther, A.3
  • 61
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • COI: 1:STN:280:DC%2BD3M7hvFCrsg%3D%3D, PID: 11134934
    • Winn MD, Isupov MN, Murshudov GN (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr D Biol Crystallogr 57(Pt 1):122–133
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 62
    • 0026474089 scopus 로고
    • De novo purine nucleotide biosynthesis
    • COI: 1:CAS:528:DyaK3sXhsFCq, PID: 1574589
    • Zalkin H, Dixon JE (1992) De novo purine nucleotide biosynthesis. Prog Nucleic Acid Res Mol Biol 42:259–287
    • (1992) Prog Nucleic Acid Res Mol Biol , vol.42 , pp. 259-287
    • Zalkin, H.1    Dixon, J.E.2
  • 63
    • 0032795294 scopus 로고    scopus 로고
    • Differential signatures of bacterial and mammalian IMP dehydrogenase enzymes
    • COI: 1:CAS:528:DyaK1MXks1Onsrg%3D, PID: 10390599
    • Zhang R, Evans G, Rotella F, Westbrook E, Huberman E, Joachimiak A, Collart FR (1999a) Differential signatures of bacterial and mammalian IMP dehydrogenase enzymes. Curr Med Chem 6(7):537–543
    • (1999) Curr Med Chem , vol.6 , Issue.7 , pp. 537-543
    • Zhang, R.1    Evans, G.2    Rotella, F.3    Westbrook, E.4    Huberman, E.5    Joachimiak, A.6    Collart, F.R.7
  • 64
    • 0033551092 scopus 로고    scopus 로고
    • Characteristics and crystal structure of bacterial inosine-5′-monophosphate dehydrogenase
    • COI: 1:CAS:528:DyaK1MXhvFOmtb8%3D, PID: 10200156
    • Zhang R, Evans G, Rotella FJ, Westbrook EM, Beno D, Huberman E, Joachimiak A, Collart FR (1999b) Characteristics and crystal structure of bacterial inosine-5′-monophosphate dehydrogenase. Biochemistry 38(15):4691–4700. doi:10.1021/bi982858v
    • (1999) Biochemistry , vol.38 , Issue.15 , pp. 4691-4700
    • Zhang, R.1    Evans, G.2    Rotella, F.J.3    Westbrook, E.M.4    Beno, D.5    Huberman, E.6    Joachimiak, A.7    Collart, F.R.8


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