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Volumn 114, Issue 8, 2017, Pages E1336-E1344

Reaction dynamics analysis of a reconstituted Escherichia coli protein translation system by computational modeling

Author keywords

Cell free protein synthesis; Computational modeling; Network analysis; Protein translation; Quasi stationary state

Indexed keywords

ESCHERICHIA COLI PROTEIN; MESSENGER RNA; METHIONYLGLYCYLGLYCINE PEPTIDE; TRIPEPTIDE; UNCLASSIFIED DRUG; DIPEPTIDE; METHIONYLGLYCINE;

EID: 85013230506     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1615351114     Document Type: Article
Times cited : (37)

References (64)
  • 1
    • 0024803111 scopus 로고
    • The NK model of rugged fitness landscapes and its application to maturation of the immune response
    • Kauffman SA, Weinberger ED (1989) The NK model of rugged fitness landscapes and its application to maturation of the immune response. J Theor Biol 141(2):211-245.
    • (1989) J Theor Biol , vol.141 , Issue.2 , pp. 211-245
    • Kauffman, S.A.1    Weinberger, E.D.2
  • 3
    • 84930062103 scopus 로고    scopus 로고
    • Zipf's law in gene expression
    • Furusawa C, Kaneko K (2003) Zipf's law in gene expression. Phys Rev Lett 90(8):088102.
    • (2003) Phys Rev Lett , vol.90 , Issue.8
    • Furusawa, C.1    Kaneko, K.2
  • 4
    • 70449096312 scopus 로고    scopus 로고
    • Ubiquitous "glassy" relaxation in catalytic reaction networks
    • Awazu A, Kaneko K (2009) Ubiquitous "glassy" relaxation in catalytic reaction networks. Phys Rev E Stat Nonlin Soft Matter Phys 80(4 Pt 1):041931.
    • (2009) Phys Rev E Stat Nonlin Soft Matter Phys , vol.80 , Issue.4
    • Awazu, A.1    Kaneko, K.2
  • 6
    • 84864258618 scopus 로고    scopus 로고
    • A whole-cell computational model predicts phenotype from genotype
    • Karr JR, et al. (2012) A whole-cell computational model predicts phenotype from genotype. Cell 150(2):389-401.
    • (2012) Cell , vol.150 , Issue.2 , pp. 389-401
    • Karr, J.R.1
  • 8
    • 0141455111 scopus 로고    scopus 로고
    • Chaotic itinerancy
    • Kaneko K, Tsuda I (2003) Chaotic itinerancy. Chaos 13(3):926-936.
    • (2003) Chaos , vol.13 , Issue.3 , pp. 926-936
    • Kaneko, K.1    Tsuda, I.2
  • 9
    • 84907693728 scopus 로고    scopus 로고
    • Chaotic itinerancy and its roles in cognitive neurodynamics
    • Tsuda I (2015) Chaotic itinerancy and its roles in cognitive neurodynamics. Curr Opin Neurobiol 31:67-71.
    • (2015) Curr Opin Neurobiol , vol.31 , pp. 67-71
    • Tsuda, I.1
  • 10
    • 0141678045 scopus 로고    scopus 로고
    • Evidence from human scalp electroencephalograms of global chaotic itinerancy
    • Freeman WJ (2003) Evidence from human scalp electroencephalograms of global chaotic itinerancy. Chaos 13(3):1067-1077.
    • (2003) Chaos , vol.13 , Issue.3 , pp. 1067-1077
    • Freeman, W.J.1
  • 11
    • 0141678049 scopus 로고    scopus 로고
    • A challenge to chaotic itinerancy from brain dynamics
    • Kay LM (2003) A challenge to chaotic itinerancy from brain dynamics. Chaos 13(3):1057-1066.
    • (2003) Chaos , vol.13 , Issue.3 , pp. 1057-1066
    • Kay, L.M.1
  • 12
    • 0035925930 scopus 로고    scopus 로고
    • Theory of robustness of irreversible differentiation in a stem cell system: Chaos hypothesis
    • Furusawa C, Kaneko K (2001) Theory of robustness of irreversible differentiation in a stem cell system: Chaos hypothesis. J Theor Biol 209(4):395-416.
    • (2001) J Theor Biol , vol.209 , Issue.4 , pp. 395-416
    • Furusawa, C.1    Kaneko, K.2
  • 13
    • 84857131710 scopus 로고    scopus 로고
    • Optimizing ring assembly reveals the strength of weak interactions
    • Deeds EJ, Bachman JA, Fontana W (2012) Optimizing ring assembly reveals the strength of weak interactions. Proc Natl Acad Sci USA 109(7):2348-2353.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.7 , pp. 2348-2353
    • Deeds, E.J.1    Bachman, J.A.2    Fontana, W.3
  • 14
    • 84927976278 scopus 로고    scopus 로고
    • Kinetic memory based on the enzyme-limited competition
    • Hatakeyama TS, Kaneko K (2014) Kinetic memory based on the enzyme-limited competition. PLOS Comput Biol 10(8):e1003784.
    • (2014) PLOS Comput Biol , vol.10 , Issue.8
    • Hatakeyama, T.S.1    Kaneko, K.2
  • 15
    • 0034904102 scopus 로고    scopus 로고
    • Cell-free translation reconstituted with purified components
    • Shimizu Y, et al. (2001) Cell-free translation reconstituted with purified components. Nat Biotechnol 19(8):751-755.
    • (2001) Nat Biotechnol , vol.19 , Issue.8 , pp. 751-755
    • Shimizu, Y.1
  • 16
    • 84927174869 scopus 로고    scopus 로고
    • Synthesis of milligram quantities of proteins using a reconstituted in vitro protein synthesis system
    • Kazuta Y, Matsuura T, Ichihashi N, Yomo T (2014) Synthesis of milligram quantities of proteins using a reconstituted in vitro protein synthesis system. J Biosci Bioeng 118(5):554-557.
    • (2014) J Biosci Bioeng , vol.118 , Issue.5 , pp. 554-557
    • Kazuta, Y.1    Matsuura, T.2    Ichihashi, N.3    Yomo, T.4
  • 17
    • 0029873397 scopus 로고    scopus 로고
    • Rate of translation of natural mRNAs in an optimized in vitro system
    • Pavlov MY, Ehrenberg M (1996) Rate of translation of natural mRNAs in an optimized in vitro system. Arch Biochem Biophys 328(1):9-16.
    • (1996) Arch Biochem Biophys , vol.328 , Issue.1 , pp. 9-16
    • Pavlov, M.Y.1    Ehrenberg, M.2
  • 18
    • 84860443532 scopus 로고    scopus 로고
    • Experiment and mathematical modeling of gene expression dynamics in a cell-free system
    • Stögbauer T, Windhager L, Zimmer R, Rädler JO (2012) Experiment and mathematical modeling of gene expression dynamics in a cell-free system. Integr Biol 4(5):494-501.
    • (2012) Integr Biol , vol.4 , Issue.5 , pp. 494-501
    • Stögbauer, T.1    Windhager, L.2    Zimmer, R.3    Rädler, J.O.4
  • 19
    • 79251480753 scopus 로고    scopus 로고
    • Coarse-grained dynamics of protein synthesis in a cell-free system
    • Karzbrun E, Shin J, Bar-Ziv RH, Noireaux V (2011) Coarse-grained dynamics of protein synthesis in a cell-free system. Phys Rev Lett 106(4):048104.
    • (2011) Phys Rev Lett , vol.106 , Issue.4
    • Karzbrun, E.1    Shin, J.2    Bar-Ziv, R.H.3    Noireaux, V.4
  • 20
    • 84931574253 scopus 로고    scopus 로고
    • A simple protein synthesis model for the PURE system operation
    • Mavelli F, Marangoni R, Stano P (2015) A simple protein synthesis model for the PURE system operation. Bull Math Biol 77(6):1185-1212.
    • (2015) Bull Math Biol , vol.77 , Issue.6 , pp. 1185-1212
    • Mavelli, F.1    Marangoni, R.2    Stano, P.3
  • 21
    • 21544479394 scopus 로고    scopus 로고
    • Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition
    • Nakayama Y, Kinoshita A, Tomita M (2005) Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model 2:18.
    • (2005) Theor Biol Med Model , vol.2 , pp. 18
    • Nakayama, Y.1    Kinoshita, A.2    Tomita, M.3
  • 22
    • 84930227327 scopus 로고    scopus 로고
    • Using genome-scale models to predict biological capabilities
    • O'Brien EJ, Monk JM, Palsson BO (2015) Using genome-scale models to predict biological capabilities. Cell 161(5):971-987.
    • (2015) Cell , vol.161 , Issue.5 , pp. 971-987
    • O'Brien, E.J.1    Monk, J.M.2    Palsson, B.O.3
  • 23
    • 1542720448 scopus 로고    scopus 로고
    • Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis
    • Jewett MC, Swartz JR (2004) Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis. Biotechnol Bioeng 86(1):19-26.
    • (2004) Biotechnol Bioeng , vol.86 , Issue.1 , pp. 19-26
    • Jewett, M.C.1    Swartz, J.R.2
  • 24
    • 4344670572 scopus 로고    scopus 로고
    • Substrate replenishment extends protein synthesis with an in vitro translation system designed to mimic the cytoplasm
    • Jewett MC, Swartz JR (2004) Substrate replenishment extends protein synthesis with an in vitro translation system designed to mimic the cytoplasm. Biotechnol Bioeng 87(4):465-472.
    • (2004) Biotechnol Bioeng , vol.87 , Issue.4 , pp. 465-472
    • Jewett, M.C.1    Swartz, J.R.2
  • 25
    • 84864953230 scopus 로고    scopus 로고
    • Cell-free protein synthesis: Applications come of age
    • Carlson ED, Gan R, Hodgman CE, Jewett MC (2012) Cell-free protein synthesis: Applications come of age. Biotechnol Adv 30(5):1185-1194.
    • (2012) Biotechnol Adv , vol.30 , Issue.5 , pp. 1185-1194
    • Carlson, E.D.1    Gan, R.2    Hodgman, C.E.3    Jewett, M.C.4
  • 26
    • 0037342537 scopus 로고    scopus 로고
    • The systems biology markup language (SBML): A medium for representation and exchange of biochemical network models
    • Hucka M, et al.; SBML Forum (2003) The systems biology markup language (SBML): A medium for representation and exchange of biochemical network models. Bioinformatics 19(4):524-531.
    • (2003) Bioinformatics , vol.19 , Issue.4 , pp. 524-531
    • Hucka, M.1
  • 27
    • 33644542727 scopus 로고    scopus 로고
    • EF-G-dependent GTPase on the ribosome. Conformational change and fusidic acid inhibition
    • Seo HS, et al. (2006) EF-G-dependent GTPase on the ribosome. conformational change and fusidic acid inhibition. Biochemistry 45(8):2504-2514.
    • (2006) Biochemistry , vol.45 , Issue.8 , pp. 2504-2514
    • Seo, H.S.1
  • 28
  • 30
    • 33645965566 scopus 로고    scopus 로고
    • Unfolding of mRNA secondary structure by the bacterial translation initiation complex
    • Studer SM, Joseph S (2006) Unfolding of mRNA secondary structure by the bacterial translation initiation complex. Mol Cell 22(1):105-115.
    • (2006) Mol Cell , vol.22 , Issue.1 , pp. 105-115
    • Studer, S.M.1    Joseph, S.2
  • 31
    • 23444439817 scopus 로고    scopus 로고
    • Using process diagrams for the graphical representation of biological networks
    • Kitano H, Funahashi A, Matsuoka Y, Oda K (2005) Using process diagrams for the graphical representation of biological networks. Nat Biotechnol 23(8):961-966.
    • (2005) Nat Biotechnol , vol.23 , Issue.8 , pp. 961-966
    • Kitano, H.1    Funahashi, A.2    Matsuoka, Y.3    Oda, K.4
  • 33
    • 33748785471 scopus 로고    scopus 로고
    • Role and timing of GTP binding and hydrolysis during EF-G-dependent tRNA translocation on the ribosome
    • Wilden B, Savelsbergh A, Rodnina MV, Wintermeyer W (2006) Role and timing of GTP binding and hydrolysis during EF-G-dependent tRNA translocation on the ribosome. Proc Natl Acad Sci USA 103(37):13670-13675.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.37 , pp. 13670-13675
    • Wilden, B.1    Savelsbergh, A.2    Rodnina, M.V.3    Wintermeyer, W.4
  • 34
    • 57349132462 scopus 로고    scopus 로고
    • The pretranslocation ribosome is targeted by GTP-bound EF-G in partially activated form
    • Hauryliuk V, et al. (2008) The pretranslocation ribosome is targeted by GTP-bound EF-G in partially activated form. Proc Natl Acad Sci USA 105(41):15678-15683.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.41 , pp. 15678-15683
    • Hauryliuk, V.1
  • 35
    • 84878924244 scopus 로고    scopus 로고
    • Structural basis of the translational elongation cycle
    • Voorhees RM, Ramakrishnan V (2013) Structural basis of the translational elongation cycle. Annu Rev Biochem 82:203-236.
    • (2013) Annu Rev Biochem , vol.82 , pp. 203-236
    • Voorhees, R.M.1    Ramakrishnan, V.2
  • 36
    • 34249323754 scopus 로고    scopus 로고
    • RF3 induces ribosomal conformational changes responsible for dissociation of class I release factors
    • Gao H, et al. (2007) RF3 induces ribosomal conformational changes responsible for dissociation of class I release factors. Cell 129(5):929-941.
    • (2007) Cell , vol.129 , Issue.5 , pp. 929-941
    • Gao, H.1
  • 37
    • 84896739794 scopus 로고    scopus 로고
    • Timing of GTP binding and hydrolysis by translation termination factor RF3
    • Peske F, Kuhlenkoetter S, Rodnina MV, Wintermeyer W (2014) Timing of GTP binding and hydrolysis by translation termination factor RF3. Nucleic Acids Res 42(3):1812-1820.
    • (2014) Nucleic Acids Res , vol.42 , Issue.3 , pp. 1812-1820
    • Peske, F.1    Kuhlenkoetter, S.2    Rodnina, M.V.3    Wintermeyer, W.4
  • 38
    • 0034681174 scopus 로고    scopus 로고
    • A highly efficient and robust cell-free protein synthesis system prepared from wheat embryos: Plants apparently contain a suicide system directed at ribosomes
    • Madin K, Sawasaki T, Ogasawara T, Endo Y (2000) A highly efficient and robust cell-free protein synthesis system prepared from wheat embryos: Plants apparently contain a suicide system directed at ribosomes. Proc Natl Acad Sci USA 97(2):559-564.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.2 , pp. 559-564
    • Madin, K.1    Sawasaki, T.2    Ogasawara, T.3    Endo, Y.4
  • 39
    • 23044504786 scopus 로고    scopus 로고
    • Protein synthesis by pure translation systems
    • Shimizu Y, Kanamori T, Ueda T (2005) Protein synthesis by pure translation systems. Methods 36(3):299-304.
    • (2005) Methods , vol.36 , Issue.3 , pp. 299-304
    • Shimizu, Y.1    Kanamori, T.2    Ueda, T.3
  • 40
    • 33751410139 scopus 로고    scopus 로고
    • Efficient protein selection based on ribosome display system with purified components
    • Ohashi H, Shimizu Y, Ying BW, Ueda T (2007) Efficient protein selection based on ribosome display system with purified components. Biochem Biophys Res Commun 352(1):270-276.
    • (2007) Biochem Biophys Res Commun , vol.352 , Issue.1 , pp. 270-276
    • Ohashi, H.1    Shimizu, Y.2    Ying, B.W.3    Ueda, T.4
  • 41
    • 34247642630 scopus 로고    scopus 로고
    • Mechanism of EF-Ts-catalyzed guanine nucleotide exchange in EF-Tu: Contribution of interactions mediated by helix B of EF-Tu
    • Schümmer T, Gromadski KB, Rodnina MV (2007) Mechanism of EF-Ts-catalyzed guanine nucleotide exchange in EF-Tu: Contribution of interactions mediated by helix B of EF-Tu. Biochemistry 46(17):4977-4984.
    • (2007) Biochemistry , vol.46 , Issue.17 , pp. 4977-4984
    • Schümmer, T.1    Gromadski, K.B.2    Rodnina, M.V.3
  • 42
    • 84869198253 scopus 로고    scopus 로고
    • GTPases IF2 and EF-G bind GDP and the SRL RNA in a mutually exclusive manner
    • Mitkevich VA, et al. (2012) GTPases IF2 and EF-G bind GDP and the SRL RNA in a mutually exclusive manner. Sci Rep 2:843.
    • (2012) Sci Rep , vol.2 , pp. 843
    • Mitkevich, V.A.1
  • 43
    • 77950371305 scopus 로고    scopus 로고
    • The ribosome-bound initiation factor 2 recruits initiator tRNA to the 30S initiation complex
    • Milon P, et al. (2010) The ribosome-bound initiation factor 2 recruits initiator tRNA to the 30S initiation complex. EMBO Rep 11(4):312-316.
    • (2010) EMBO Rep , vol.11 , Issue.4 , pp. 312-316
    • Milon, P.1
  • 44
    • 0020369597 scopus 로고
    • Kinetic studies on the interaction of chain initiation factor 3 with 70 S Escherichia coli ribosomes and subunits
    • Goss DJ, Parkhurst LJ, Wahba AJ (1982) Kinetic studies on the interaction of chain initiation factor 3 with 70 S Escherichia coli ribosomes and subunits. J Biol Chem 257(17):10119-10127.
    • (1982) J Biol Chem , vol.257 , Issue.17 , pp. 10119-10127
    • Goss, D.J.1    Parkhurst, L.J.2    Wahba, A.J.3
  • 45
    • 34748843156 scopus 로고    scopus 로고
    • A quantitative kinetic scheme for 70 S translation initiation complex formation
    • Grigoriadou C, Marzi S, Kirillov S, Gualerzi CO, Cooperman BS (2007) A quantitative kinetic scheme for 70 S translation initiation complex formation. J Mol Biol 373(3):562-572.
    • (2007) J Mol Biol , vol.373 , Issue.3 , pp. 562-572
    • Grigoriadou, C.1    Marzi, S.2    Kirillov, S.3    Gualerzi, C.O.4    Cooperman, B.S.5
  • 46
    • 0022412615 scopus 로고
    • Kinetic studies of Escherichia coli elongation factor Tu-guanosine 5′-triphosphate-aminoacyl-tRNA complexes
    • Louie A, Jurnak F (1985) Kinetic studies of Escherichia coli elongation factor Tu-guanosine 5′-triphosphate-aminoacyl-tRNA complexes. Biochemistry 24(23):6433-6439.
    • (1985) Biochemistry , vol.24 , Issue.23 , pp. 6433-6439
    • Louie, A.1    Jurnak, F.2
  • 47
    • 0038381426 scopus 로고    scopus 로고
    • Common location of determinants in initiator transfer RNAs for initiator-elongator discrimination in bacteria and in eukaryotes
    • Stortchevoi A, Varshney U, RajBhandary UL (2003) Common location of determinants in initiator transfer RNAs for initiator-elongator discrimination in bacteria and in eukaryotes. J Biol Chem 278(20):17672-17679.
    • (2003) J Biol Chem , vol.278 , Issue.20 , pp. 17672-17679
    • Stortchevoi, A.1    Varshney, U.2    RajBhandary, U.L.3
  • 48
    • 0036810254 scopus 로고    scopus 로고
    • Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3
    • Zavialov AV, Mora L, Buckingham RH, Ehrenberg M (2002) Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3. Mol Cell 10(4):789-798.
    • (2002) Mol Cell , vol.10 , Issue.4 , pp. 789-798
    • Zavialov, A.V.1    Mora, L.2    Buckingham, R.H.3    Ehrenberg, M.4
  • 49
    • 0035812714 scopus 로고    scopus 로고
    • A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3
    • Zavialov AV, Buckingham RH, Ehrenberg M (2001) A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3. Cell 107(1):115-124.
    • (2001) Cell , vol.107 , Issue.1 , pp. 115-124
    • Zavialov, A.V.1    Buckingham, R.H.2    Ehrenberg, M.3
  • 50
    • 4944227490 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of RRF, EF-G, and thiostrepton interaction on the Escherichia coli ribosome
    • Seo HS, et al. (2004) Kinetics and thermodynamics of RRF, EF-G, and thiostrepton interaction on the Escherichia coli ribosome. Biochemistry 43(40):12728-12740.
    • (2004) Biochemistry , vol.43 , Issue.40 , pp. 12728-12740
    • Seo, H.S.1
  • 51
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba M, Soll D (2000) Aminoacyl-tRNA synthesis. Annu Rev Biochem 69:617-650.
    • (2000) Annu Rev Biochem , vol.69 , pp. 617-650
    • Ibba, M.1    Soll, D.2
  • 52
    • 84867060238 scopus 로고    scopus 로고
    • Catalysis of tRNA aminoacylation: Single turnover to steady-state kinetics of tRNA synthetases
    • Santra M, Bagchi B (2012) Catalysis of tRNA aminoacylation: Single turnover to steady-state kinetics of tRNA synthetases. J Phys Chem B 116(39):11809-11817.
    • (2012) J Phys Chem B , vol.116 , Issue.39 , pp. 11809-11817
    • Santra, M.1    Bagchi, B.2
  • 53
    • 0033610808 scopus 로고    scopus 로고
    • Characterization of isoleucyl-tRNA synthetase from Staphylococcus aureus. I: Kinetic mechanism of the substrate activation reaction studied by transient and steady-state techniques
    • Pope AJ, et al. (1998) Characterization of isoleucyl-tRNA synthetase from Staphylococcus aureus. I: Kinetic mechanism of the substrate activation reaction studied by transient and steady-state techniques. J Biol Chem 273(48):31680-31690.
    • (1998) J Biol Chem , vol.273 , Issue.48 , pp. 31680-31690
    • Pope, A.J.1
  • 54
    • 0346963227 scopus 로고    scopus 로고
    • Induced fit and kinetic mechanism of adenylation catalyzed by Escherichia coli threonyl-tRNA synthetase
    • Bovee ML, Pierce MA, Francklyn CS (2003) Induced fit and kinetic mechanism of adenylation catalyzed by Escherichia coli threonyl-tRNA synthetase. Biochemistry 42(51):15102-15113.
    • (2003) Biochemistry , vol.42 , Issue.51 , pp. 15102-15113
    • Bovee, M.L.1    Pierce, M.A.2    Francklyn, C.S.3
  • 55
    • 14844357908 scopus 로고    scopus 로고
    • A substrate-assisted concerted mechanism for aminoacylation by a class II aminoacyl-tRNA synthetase
    • Guth E, Connolly SH, Bovee M, Francklyn CS (2005) A substrate-assisted concerted mechanism for aminoacylation by a class II aminoacyl-tRNA synthetase. Biochemistry 44(10):3785-3794.
    • (2005) Biochemistry , vol.44 , Issue.10 , pp. 3785-3794
    • Guth, E.1    Connolly, S.H.2    Bovee, M.3    Francklyn, C.S.4
  • 56
    • 0018957648 scopus 로고
    • Methionyl-transfer-RNA transformylase from Escherichia coli. Purification and characterisation
    • Kahn D, Fromant M, Fayat G, Dessen P, Blanquet S (1980) Methionyl-transfer-RNA transformylase from Escherichia coli. Purification and characterisation. Eur J Biochem 105(3):489-497.
    • (1980) Eur J Biochem , vol.105 , Issue.3 , pp. 489-497
    • Kahn, D.1    Fromant, M.2    Fayat, G.3    Dessen, P.4    Blanquet, S.5
  • 57
    • 0034008531 scopus 로고    scopus 로고
    • Escherichia coli methionyl-tRNA formyltransferase: Role of amino acids conserved in the linker region and in the C-terminal domain on the specific recognition of the initiator tRNA
    • Gite S, Li Y, Ramesh V, RajBhandary UL (2000) Escherichia coli methionyl-tRNA formyltransferase: Role of amino acids conserved in the linker region and in the C-terminal domain on the specific recognition of the initiator tRNA. Biochemistry 39(9):2218-2226.
    • (2000) Biochemistry , vol.39 , Issue.9 , pp. 2218-2226
    • Gite, S.1    Li, Y.2    Ramesh, V.3    RajBhandary, U.L.4
  • 58
    • 0016720206 scopus 로고
    • Studies of energy transport in heart cells. Mitochondrial isoenzyme of creatine phosphokinase: Kinetic properties and regulatory action of Mg2+ ions
    • Saks VA, Chernousova GB, Gukovsky DE, Smirnov VN, Chazov EI (1975) Studies of energy transport in heart cells. Mitochondrial isoenzyme of creatine phosphokinase: Kinetic properties and regulatory action of Mg2+ ions. Eur J Biochem 57(1):273-290.
    • (1975) Eur J Biochem , vol.57 , Issue.1 , pp. 273-290
    • Saks, V.A.1    Chernousova, G.B.2    Gukovsky, D.E.3    Smirnov, V.N.4    Chazov, E.I.5
  • 59
    • 0028176032 scopus 로고
    • Recombinant rat nucleoside diphosphate kinase isoforms (alpha and beta): Purification, properties and application to immunological detection of native isoforms in rat tissues
    • Fukuchi T, et al. (1994) Recombinant rat nucleoside diphosphate kinase isoforms (alpha and beta): Purification, properties and application to immunological detection of native isoforms in rat tissues. Biochim Biophys Acta 1205(1):113-122.
    • (1994) Biochim Biophys Acta , vol.1205 , Issue.1 , pp. 113-122
    • Fukuchi, T.1
  • 60
    • 0000398122 scopus 로고    scopus 로고
    • An iso-random Bi Bi mechanism for adenylate kinase
    • Sheng XR, Li X, Pan XM (1999) An iso-random Bi Bi mechanism for adenylate kinase. J Biol Chem 274(32):22238-22242.
    • (1999) J Biol Chem , vol.274 , Issue.32 , pp. 22238-22242
    • Sheng, X.R.1    Li, X.2    Pan, X.M.3
  • 61
    • 0028948711 scopus 로고
    • Effect of D97E substitution on the kinetic and thermodynamic properties of Escherichia coli inorganic pyrophosphatase
    • Käpylä J, et al. (1995) Effect of D97E substitution on the kinetic and thermodynamic properties of Escherichia coli inorganic pyrophosphatase. Biochemistry 34(3):792-800.
    • (1995) Biochemistry , vol.34 , Issue.3 , pp. 792-800
    • Käpylä, J.1
  • 63
    • 33746189733 scopus 로고    scopus 로고
    • Distinct kinetic mechanisms of the two classes of Aminoacyl-tRNA synthetases
    • Zhang CM, Perona JJ, Ryu K, Francklyn C, Hou YM (2006) Distinct kinetic mechanisms of the two classes of Aminoacyl-tRNA synthetases. J Mol Biol 361(2):300-311.
    • (2006) J Mol Biol , vol.361 , Issue.2 , pp. 300-311
    • Zhang, C.M.1    Perona, J.J.2    Ryu, K.3    Francklyn, C.4    Hou, Y.M.5
  • 64
    • 9444266171 scopus 로고    scopus 로고
    • CellDesigner: A process diagram editor for gene-regulatory and biochemical networks
    • Funahashi A, Morohashi M, Kitano H, Tanimura N (2003) CellDesigner: A process diagram editor for gene-regulatory and biochemical networks. BIOCILICO 1:159-162.
    • (2003) BIOCILICO , vol.1 , pp. 159-162
    • Funahashi, A.1    Morohashi, M.2    Kitano, H.3    Tanimura, N.4


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