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Volumn 9, Issue 3, 2014, Pages

Proteomic analysis of carbon concentrating chemolithotrophic bacteria serratia sp. for sequestration of carbon dioxide

Author keywords

[No Author keywords available]

Indexed keywords

CARBONATE DEHYDRATASE; AMINO ACID; CARBON; CARBON DIOXIDE; FATTY ACID; NUCLEOTIDE; PROTEOME; RIBOSOME PROTEIN; RNA 16S;

EID: 84897525527     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0091300     Document Type: Article
Times cited : (27)

References (57)
  • 1
    • 33745346664 scopus 로고    scopus 로고
    • Ecosystem carbon budgeting and soil carbon sequestration in reclaimed mine soil
    • DOI 10.1016/j.envint.2006.05.001, PII S0160412006000596
    • Shrestha RK, Lal R (2006) Ecosystem carbon budgeting and soil carbon sequestration in reclaimed mine soil. Environ Int 32: 781-796. (Pubitemid 43947219)
    • (2006) Environment International , vol.32 , Issue.6 , pp. 781-796
    • Shrestha, R.K.1    Lal, R.2
  • 2
    • 0742302617 scopus 로고    scopus 로고
    • Prospects for enhancing carbon sequestration and reclamation of degraded lands with fossil-fuel combustion by-products
    • DOI 10.1016/S1093-0191(02)00124-7, PII S1093019102001247
    • Palumbo AV, McCarthy JF, Amonette JE, Fisher LS, Wullschleger SD, et al. (2004) Prospects for enhancing carbon sequestration and reclamation of degraded lands with fossil-fuel combustion by-products. Adv Environ Res 8: 425-438. (Pubitemid 38153036)
    • (2004) Advances in Environmental Research , vol.8 , Issue.3-4 , pp. 425-438
    • Palumbo, A.V.1    McCarthy, J.F.2    Amonette, J.E.3    Fisher, L.S.4    Wullschleger, S.D.5    Lee, D.W.6
  • 3
    • 0000066404 scopus 로고    scopus 로고
    • 2 concentrating mechanism in several cyanobacterial strains: A review of general physiological characteristics, genes, proteins and recent advances
    • 2 concentrating mechanism in several cyanobacterial strains: a review of general physiological characteristics, genes, proteins and recent advances. Can J Bot 76: 973-1002.
    • (1998) Can J Bot , vol.76 , pp. 973-1002
    • Price, G.D.1    Sültemeyer, D.2    Klughammer, B.3    Ludwig, M.4    Badger, M.R.5
  • 4
    • 84859216547 scopus 로고    scopus 로고
    • Biomineralization-based conversion of carbon dioxide to calcium carbonate using recombinant carbonic anhydrase
    • Kim G, Jo BH, Kang DG, Kim CS, Choi YS, et al. (2012) Biomineralization-based conversion of carbon dioxide to calcium carbonate using recombinant carbonic anhydrase. Chemosphere 87: 1091-1096.
    • (2012) Chemosphere , vol.87 , pp. 1091-1096
    • Kim, G.1    Jo, B.H.2    Kang, D.G.3    Kim, C.S.4    Choi, Y.S.5
  • 7
    • 30344474899 scopus 로고    scopus 로고
    • 2 concentrating mechanism
    • DOI 10.1093/jxb/eri286
    • Badger MR, Price GD, Long BM, Woodger FJ (2006) The environmental plasticity and ecological genomics of the cyanobacterial CO2 concentrating mechanism. J Exp Bot 57: 249-265. (Pubitemid 43063780)
    • (2006) Journal of Experimental Botany , vol.57 , Issue.2 SPEC. ISS. , pp. 249-265
    • Badger, M.R.1    Price, G.D.2    Long, B.M.3    Woodger, F.J.4
  • 8
    • 84861208627 scopus 로고    scopus 로고
    • Elucidating Essential Role of Conserved Carboxysomal Protein CcmN Reveals Common Feature of Bacterial Microcompartment Assembly
    • Kinney JN, Salmeen A, Cai F, Kerfeld CA (2012) Elucidating Essential Role of Conserved Carboxysomal Protein CcmN Reveals Common Feature of Bacterial Microcompartment Assembly. J Biol Chem. 18: 17729-17736.
    • (2012) J Biol Chem , vol.18 , pp. 17729-17736
    • Kinney, J.N.1    Salmeen, A.2    Cai, F.3    Kerfeld, C.A.4
  • 11
    • 77953959830 scopus 로고    scopus 로고
    • 2 fixation and biofuel production via microalgae: Recent developments and future directions
    • 2 fixation and biofuel production via microalgae: recent developments and future directions. Trends Biotechnol. 28: 371-380.
    • (2010) Trends Biotechnol , vol.28 , pp. 371-380
    • Kumar, A.1    Ergas, S.2    Yuan, X.3    Sahu, A.4    Zhang, Q.5
  • 14
    • 84860488672 scopus 로고    scopus 로고
    • Substrate-Controlled Succession of Marine Bacterioplankton Populations Induced by a Phytoplankton Bloom
    • Teeling H, Fuchs BM, Becher D, Klockow C, Gardebrecht A, et al. (2012) Substrate-Controlled Succession of Marine Bacterioplankton Populations Induced by a Phytoplankton Bloom. Science 336: 608-611.
    • (2012) Science , vol.336 , pp. 608-611
    • Teeling, H.1    Fuchs, B.M.2    Becher, D.3    Klockow, C.4    Gardebrecht, A.5
  • 15
    • 80051624900 scopus 로고    scopus 로고
    • Deep and highly sensitive proteome coverage by LC-MS/MS without pre fractionation
    • doi: 10.1074/mcp.M110.003699
    • Thakur SS, Geiger T, Chatterjee B, Bandilla P, Frohlich F, et al. (2011) Deep and highly sensitive proteome coverage by LC-MS/MS without pre fractionation. Mol. Cell Proteomics 10.8. 17, 2011, doi: 10.1074/mcp.M110. 003699.
    • (2011) Mol. Cell Proteomics 10.8 , vol.17 , pp. 2011
    • Thakur, S.S.1    Geiger, T.2    Chatterjee, B.3    Bandilla, P.4    Frohlich, F.5
  • 16
    • 33645089172 scopus 로고    scopus 로고
    • Proteomic analysis of heterotrophy in Synechocystis sp. PCC 6803
    • Kurian D, Jansèn T, Mäenpaa P (2006) Proteomic analysis of heterotrophy in Synechocystis sp. PCC 6803. Proteomics 6: 1483-1494.
    • (2006) Proteomics , vol.6 , pp. 1483-1494
    • Kurian, D.1    Jansèn, T.2    Mäenpaa, P.3
  • 18
    • 84868628441 scopus 로고    scopus 로고
    • Systematic characterization of hypothetical proteins in Synechocystis sp. PCC 6803 reveals proteins functionally relevant to stress responses
    • Qiao J, Shao M, Chen L, Wang J, Wu G, et al. (2013) Systematic characterization of hypothetical proteins in Synechocystis sp. PCC 6803 reveals proteins functionally relevant to stress responses. Gene 512: 6-15.
    • (2013) Gene , vol.512 , pp. 6-15
    • Qiao, J.1    Shao, M.2    Chen, L.3    Wang, J.4    Wu, G.5
  • 19
    • 84858860295 scopus 로고    scopus 로고
    • Physiological homogeneity among the endosymbionts of Riftia pachyptila and Tevnia jerichonana revealed by proteogenomics
    • Gardebrecht A, Markert S, Sievert SM, Felbeck H, Thürmer A, et al. (2012) Physiological homogeneity among the endosymbionts of Riftia pachyptila and Tevnia jerichonana revealed by proteogenomics. ISME J 6: 766-776.
    • (2012) ISME J , vol.6 , pp. 766-776
    • Gardebrecht, A.1    Markert, S.2    Sievert, S.M.3    Felbeck, H.4    Thürmer, A.5
  • 22
    • 34547231198 scopus 로고    scopus 로고
    • 18O-labeling mass spectrometry
    • DOI 10.1021/pr060621c
    • Wu WW, Wang G, Yu MJ, Knepper MA, Shen RF (2007) Identification and quantification of basic and acidic proteins using solution-based two-dimensional protein fractionation and label-free or 18O-labeling mass spectrometry. J Proteome Res 6: 2447-2459. (Pubitemid 47122341)
    • (2007) Journal of Proteome Research , vol.6 , Issue.7 , pp. 2447-2459
    • Wu, W.W.1    Wang, G.2    Yu, M.-J.3    Knepper, M.A.4    Shen, R.-F.5
  • 23
    • 0029199628 scopus 로고
    • Structural and functional characterization of a stable, 4 chlorosalicylic acid degrading, bacterial community in a chemostat
    • Thakur IS (1995) Structural and functional characterization of a stable, 4 chlorosalicylic acid degrading, bacterial community in a chemostat. World J Microbiol Biotechnol 11: 643-645.
    • (1995) World J Microbiol Biotechnol , vol.11 , pp. 643-645
    • Thakur, I.S.1
  • 24
    • 79956030498 scopus 로고    scopus 로고
    • Isolation and characterization of alkalotolerant Pseudomonas sp. Strain ISTDF1 for degradation of dibenzofuran
    • Jaiswal PK, Kohli S, Gopal M, Thakur IS (2011) Isolation and characterization of alkalotolerant Pseudomonas sp. strain ISTDF1 for degradation of dibenzofuran. J Ind Microbiol Biotechnol 38: 503-511.
    • (2011) J Ind Microbiol Biotechnol , vol.38 , pp. 503-511
    • Jaiswal, P.K.1    Kohli, S.2    Gopal, M.3    Thakur, I.S.4
  • 25
    • 3242810318 scopus 로고    scopus 로고
    • MEGA 3 integrated software for molecular evolutionary genetics analysis and sequence alignment brief
    • Kumar S, Tamura K, Nei M (2004) MEGA 3 integrated software for molecular evolutionary genetics analysis and sequence alignment brief. Bioinformatics 5: 150-163.
    • (2004) Bioinformatics , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 26
    • 41149141063 scopus 로고    scopus 로고
    • Investigations of the esterase, phosphatase, and sulfatase activities of the cytosolic mammalian carbonic anhydrase isoforms I, II, and XIII with 4-nitrophenyl esters as substrates
    • DOI 10.1016/j.bmcl.2008.03.012, PII S0960894X08002710
    • Innocenti A, Scozzafava A, Parkkila S, Puccetti L, Simone GD, et al. (2008) Investigation of the esterase, phosphate, and sulfatase activities of the cytosolic mammalian carbonic anhydrase isoform I, II and XIII with 4-nitrophenyl esters as substrates. Bioorg Med Chem Lett 18: 2267-2271. (Pubitemid 351442910)
    • (2008) Bioorganic and Medicinal Chemistry Letters , vol.18 , Issue.7 , pp. 2267-2271
    • Innocenti, A.1    Scozzafava, A.2    Parkkila, S.3    Puccetti, L.4    De Simone, G.5    Supuran, C.T.6
  • 27
    • 1942456901 scopus 로고    scopus 로고
    • A new method for purification of carbonic anhydrase isozymes by affinity chromatography
    • Ozensoy O, Arslan O, Sinan SO (2004) A new method for purification of carbonic anhydrase isozymes by affinity chromatography. Biochemistry 69: 216-219.
    • (2004) Biochemistry , vol.69 , pp. 216-219
    • Ozensoy, O.1    Arslan, O.2    Sinan, S.O.3
  • 28
    • 79951577953 scopus 로고    scopus 로고
    • Purification, characterization and mass spectroscopic analysis of thermo-alkalotolerant beta-1, 4 endoxylanase from Bacillus sp. And its potential for dye decolorization
    • Mishra M, Thakur IS (2011) Purification, characterization and mass spectroscopic analysis of thermo-alkalotolerant beta-1, 4 endoxylanase from Bacillus sp. and its potential for dye decolorization. Int Biodeterioration Biodegrad 65: 301-308.
    • (2011) Int Biodeterioration Biodegrad , vol.65 , pp. 301-308
    • Mishra, M.1    Thakur, I.S.2
  • 29
    • 0000041586 scopus 로고
    • Photometric method for routine determination of Kcat and carbamylation of Rubisco
    • Sharkey TD, Savitch LV, Butz ND (1991) Photometric method for routine determination of Kcat and carbamylation of Rubisco. Photosynth Res 28: 41-48.
    • (1991) Photosynth Res , vol.28 , pp. 41-48
    • Sharkey, T.D.1    Savitch, L.V.2    Butz, N.D.3
  • 30
    • 0019882018 scopus 로고
    • Silver staining of proteins in polyacrylamide gels
    • Wray W, Boulikas T, Wray VP, Hancock R (1981) Silver staining of proteins in polyacrylamide gels. Anal Biochem 118: 197-203.
    • (1981) Anal Biochem , vol.118 , pp. 197-203
    • Wray, W.1    Boulikas, T.2    Wray, V.P.3    Hancock, R.4
  • 31
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • DOI 10.1002/pmic.200401031
    • Görg A, Weiss W, Dunn MJ (2004) Current two-dimensional electrophoresis technology for proteomics. Proteomics 4: 3665-3685. (Pubitemid 39657447)
    • (2004) Proteomics , vol.4 , Issue.12 , pp. 3665-3685
    • Gorg, A.1    Weiss, W.2    Dunn, M.J.3
  • 32
    • 79551592386 scopus 로고    scopus 로고
    • Plasma peptidome profiling of acute hepatitis E patients by MALDI-TOF/TOF
    • Taneja S, Ahmad I, Sen S, Kumar S, Arora R, et al. (2011) Plasma peptidome profiling of acute hepatitis E patients by MALDI-TOF/TOF. Proteome Sci 9: 5.
    • (2011) Proteome Sci , vol.9 , pp. 5
    • Taneja, S.1    Ahmad, I.2    Sen, S.3    Kumar, S.4    Arora, R.5
  • 33
    • 79551502223 scopus 로고    scopus 로고
    • A new b-carbonic anhydrase from Brucella suis, its cloning, characterization, and inhibition with sulfonamides and sulfamates, leading to impaired pathogen growth
    • Joseph P, Bettache SO, Montero JL, Nishimori I, Minakuchi T, et al. (2011) A new b-carbonic anhydrase from Brucella suis, its cloning, characterization, and inhibition with sulfonamides and sulfamates, leading to impaired pathogen growth. Bioorg Med Chem 19: 1172-1178.
    • (2011) Bioorg Med Chem , vol.19 , pp. 1172-1178
    • Joseph, P.1    Bettache, S.O.2    Montero, J.L.3    Nishimori, I.4    Minakuchi, T.5
  • 34
    • 0342596598 scopus 로고
    • High specific activity ribulose-1,5-bisphosphate carboxylase/oxygenase from Nicotiana tabacum
    • Bahr JT, Johal S, Bourque DP, (1981) High specific activity ribulose-1,5-bisphosphate carboxylase/oxygenase from Nicotiana tabacum. Photosyn Res 2: 235-242.
    • (1981) Photosyn Res , vol.2 , pp. 235-242
    • Bahr, J.T.1    Johal, S.2    Bourque, D.P.3
  • 35
    • 1842552279 scopus 로고
    • Ribulose Bisphosphate Carboxylase/Oxygenase from microalgae: Proteolysis during extraction and properties of enzyme from Porphyra umbilicalis
    • Hilditch CM, Jones PB, Balding P, Smith AJ, Rogers LJ, et al. (1991) Ribulose Bisphosphate Carboxylase/Oxygenase from microalgae: proteolysis during extraction and properties of enzyme from Porphyra umbilicalis. Phytochemistry 30: 745-750.
    • (1991) Phytochemistry , vol.30 , pp. 745-750
    • Hilditch, C.M.1    Jones, P.B.2    Balding, P.3    Smith, A.J.4    Rogers, L.J.5
  • 36
    • 0027181983 scopus 로고
    • 2 fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus, the 3-hydroxypropionate cycle
    • 2 fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus, the 3-hydroxypropionate cycle. Eur J Biochem 215: 633-643.
    • (1993) Eur J Biochem , vol.215 , pp. 633-643
    • Strauss, G.1    Fuchs, G.2
  • 37
    • 58249113952 scopus 로고    scopus 로고
    • Acidithiobacillus ferrooxidans metabolism: From genome sequence to industrial applications
    • Valdés J, Pedroso I, Quatrini R, Dodson RJ, Tettelin H, et al. (2008) Acidithiobacillus ferrooxidans metabolism: from genome sequence to industrial applications. BMC Genomics 9: 597-621.
    • (2008) BMC Genomics , vol.9 , pp. 597-621
    • Valdés, J.1    Pedroso, I.2    Quatrini, R.3    Dodson, R.J.4    Tettelin, H.5
  • 38
    • 0015441506 scopus 로고
    • Metabolism of glucose by unicellular blue-green algae
    • Pelroy RA, Rippka R, Stanier RY (1972) Metabolism of glucose by unicellular blue-green algae. Arch Mikrobiol 87: 303-322.
    • (1972) Arch Mikrobiol , vol.87 , pp. 303-322
    • Pelroy, R.A.1    Rippka, R.2    Stanier, R.Y.3
  • 39
    • 0027934197 scopus 로고
    • Cloning and analysis of the C4 photosynthetic NAD-dependent malic enzyme of amaranth mitochondria
    • Long JJ, Wang JL, Berry JO (1994) Cloning and analysis of the C4 photosynthetic NAD-dependent malic enzyme of amaranth mitochondria. J Biol Chem 269: 2827-2833. (Pubitemid 24235786)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.4 , pp. 2827-2833
    • Long, J.J.1    Wang, J.-L.2    Berry, J.O.3
  • 40
    • 1642424402 scopus 로고    scopus 로고
    • Malate valves to balance cellular energy supply
    • Scheibe R (2004) Malate valves to balance cellular energy supply. Physiologia Plantarum 120: 21-26.
    • (2004) Physiologia Plantarum , vol.120 , pp. 21-26
    • Scheibe, R.1
  • 41
    • 0013901576 scopus 로고
    • A new ferredoxin-dependent carbon reduction cycle in a photosynthetic bacterium
    • Evans MC, Buchanan BB, Arnon DI (1966) A new ferredoxin-dependent carbon reduction cycle in a photosynthetic bacterium. Proc Natl Acad Sci 55: 928-934.
    • (1966) Proc Natl Acad Sci , vol.55 , pp. 928-934
    • Evans, M.C.1    Buchanan, B.B.2    Arnon, D.I.3
  • 42
    • 0029619395 scopus 로고
    • 2 for growth
    • Burns BP, Hazell SL, Mendz GL (1995) Acetyl-CoA carboxylase in Helicobacter pylori and the requirement for increased CO2 for growth. Microbiology 141: 3113-3118. (Pubitemid 26011350)
    • (1995) Microbiology , vol.141 , Issue.12 , pp. 3113-3118
    • Burns, B.P.1    Hazell, S.L.2    Mendz, G.L.3
  • 44
    • 0034615788 scopus 로고    scopus 로고
    • Assessment of the metabolic capabilities of Haemophilus influenzae Rd through a genome-scale pathway analysis
    • Schilling CH, Palsson BO (2000) Assessment of the metabolic capabilities of Haemophilus influenzae Rd through a genome-scale pathway analysis. J Theor Biol 203: 249-283.
    • (2000) J Theor Biol , vol.203 , pp. 249-283
    • Schilling, C.H.1    Palsson, B.O.2
  • 45
    • 0022425494 scopus 로고
    • The purification of shikimate dehydrogenase from Escherichia coli
    • Chaudhuri S, Coggins JR (1985) The purification of shikimate dehydrogenase from Escherichia coli. Biochem J 226: 217-23.
    • (1985) Biochem J , vol.226 , pp. 217-223
    • Chaudhuri, S.1    Coggins, J.R.2
  • 46
    • 0024578239 scopus 로고
    • The 2-oxo acid dehydrogenase complexes: Recent advances
    • Yeaman SJ (1989) The 2-oxo acid dehydrogenase complexes: recent advances. Biochem J 257: 625-632.
    • (1989) Biochem J , vol.257 , pp. 625-632
    • Yeaman, S.J.1
  • 47
    • 0022987822 scopus 로고
    • Regulation of branched-chain alpha-ketoacid dehydrogenase complex by covalent modification
    • Harris RA, Paxton R, Powell SM, Goodwin GW, Kuntz MJ, et al. (1986) Regulation of branched-chain alpha-ketoacid dehydrogenase complex by covalent modification. Adv Enzyme Regul 25: 219-237.
    • (1986) Adv Enzyme Regul , vol.25 , pp. 219-237
    • Harris, R.A.1    Paxton, R.2    Powell, S.M.3    Goodwin, G.W.4    Kuntz, M.J.5
  • 48
    • 50549155424 scopus 로고
    • The role of isoleucine in the biosynthesis of branched-chain fatty acids by Micrococcus lysodeikticus
    • Lennarz WJ (1961) The role of isoleucine in the biosynthesis of branched-chain fatty acids by Micrococcus lysodeikticus. Biochem Biophys Res Commun 6:112-116.
    • (1961) Biochem Biophys Res Commun , vol.6 , pp. 112-116
    • Lennarz, W.J.1
  • 49
    • 0009821484 scopus 로고
    • The complete amino acid sequence of Escherichia coli 5- enolpyruvylshikimate 3-phosphate synthase
    • Duncan K, Lewendon A, Coggins JR (1984) The complete amino acid sequence of Escherichia coli 5-enolpyruvylshikimate 3-phosphate synthase. FEBS Lett 170: 59-63.
    • (1984) FEBS Lett , vol.170 , pp. 59-63
    • Duncan, K.1    Lewendon, A.2    Coggins, J.R.3
  • 50
    • 23944509003 scopus 로고    scopus 로고
    • Acetyl-coenzyme A carboxylase: Crucial metabolic enzyme and attractive target for drug discovery
    • Tong L (2005) Acetyl-coenzyme A carboxylase: crucial metabolic enzyme and attractive target for drug discovery. Cell Mol Life Sci 62:1784-1803.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1784-1803
    • Tong, L.1
  • 51
    • 0033004435 scopus 로고    scopus 로고
    • Biosynthesis of polyhydroxyalkanoates (PHA) by recombinant Ralstonia eutropha and effects of PHA synthase activity on in vivo PHA biosynthesis
    • DOI 10.1016/S0141-8130(99)00017-3, PII S0141813099000173
    • Kichise T, Fukui T, Yoshida Y, Doi Y (1999) Biosynthesis of polyhydroxyalkanoates (PHA) by recombinant Ralstonia eutropha and effects of PHA synthase activity on in vivo PHA biosynthesis. Int J Biol Macromol 25: 69-77. (Pubitemid 29301984)
    • (1999) International Journal of Biological Macromolecules , vol.25 , Issue.1-3 , pp. 69-77
    • Kichise, T.1    Fukui, T.2    Yoshida, Y.3    Doi, Y.4
  • 52
    • 0034663212 scopus 로고    scopus 로고
    • 2,4-Dienoyl-CoA reductase from Escherichia coli is a novel iron-sulfur flavoprotein that functions in fatty acid beta-oxidation
    • DOI 10.1006/abbi.2000.1941
    • Liang X, Thorpe C, Schulz H (2000) 2,4-Dienoyl-CoA reductase from Escherichia coli is a novel iron-sulfur flavoprotein that functions in fatty acid beta-oxidation. Arch Biochem Biophys 380: 373-379. (Pubitemid 30659109)
    • (2000) Archives of Biochemistry and Biophysics , vol.380 , Issue.2 , pp. 373-379
    • Liang, X.1    Thorpe, C.2    Schulz, H.3
  • 53
    • 0842330598 scopus 로고    scopus 로고
    • Acyl-CoA dehydrogenases. A mechanistic overview
    • Ghisla S, Thorpe C (2004) Acyl-CoA dehydrogenases. A mechanistic overview. Eur J Biochem 271: 494-508.
    • (2004) Eur J Biochem , vol.271 , pp. 494-508
    • Ghisla, S.1    Thorpe, C.2
  • 54
    • 0031801906 scopus 로고    scopus 로고
    • Transcriptional analysis of essential genes of the Escherichia coli fatty acid biosynthesis gene cluster by functional replacement with the analogous Salmonella typhimurium gene cluster
    • Zhang Y, Cronan JE (1998) Transcriptional analysis of essential genes of the Escherichia coli fatty acid biosynthesis gene cluster by functional replacement with the analogous Salmonella typhimurium gene cluster. J Bacteriol 13: 3295-3303. (Pubitemid 28307200)
    • (1998) Journal of Bacteriology , vol.180 , Issue.13 , pp. 3295-3303
    • Zhang, Y.1    Cronan Jr., J.E.2
  • 55
    • 0033551092 scopus 로고    scopus 로고
    • Characteristics and Crystal Structure of Bacterial Inosine-5′- monophosphate Dehydrogenase
    • Zhang R, Evans G, Rotella FJ, Westbrook EM, Beno D, et al. (1999) Characteristics and Crystal Structure of Bacterial Inosine-5′- monophosphate Dehydrogenase. Biochemistry 15: 4691-4700.
    • (1999) Biochemistry , vol.15 , pp. 4691-4700
    • Zhang, R.1    Evans, G.2    Rotella, F.J.3    Westbrook, E.M.4    Beno, D.5
  • 56
    • 0026668882 scopus 로고
    • Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts
    • Lacroute F, Thomas D, Nagy M (1992) Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts. Proc Natl Acad Sci U.S.A 89: 8966-8970.
    • (1992) Proc Natl Acad Sci U.S.A , vol.89 , pp. 8966-8970
    • Lacroute, F.1    Thomas, D.2    Nagy, M.3
  • 57
    • 0031609161 scopus 로고    scopus 로고
    • Inosine-5′-monophosphate dehydrogenase: Regulation of expression and role in cellular proliferation and T lymphocyte activation
    • Zimmermann AG, Gu J-J, Laliberte J, Mitchell BS (1998) Inosine-5′-monophosphate dehydrogenase: Regulation of expression and role in cellular proliferation and T lymphocyte activation. Proc Nucleic Acid Res Mol Biol 61: 181-209.
    • (1998) Proc Nucleic Acid Res Mol Biol , vol.61 , pp. 181-209
    • Zimmermann, A.G.1    Gu, J.-J.2    Laliberte, J.3    Mitchell, B.S.4


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