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Volumn 467, Issue C, 2009, Pages 247-280

DynaFit-A Software Package for Enzymology

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITE; COMPUTER PROGRAM; ENZYME MECHANISM; ENZYMOLOGY; MATHEMATICAL MODEL; PRIORITY JOURNAL; QUANTITATIVE ANALYSIS; REVIEW; THERMODYNAMICS;

EID: 71549142265     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(09)67010-5     Document Type: Review
Times cited : (177)

References (75)
  • 3
    • 0026719686 scopus 로고
    • Global analysis of biochemical and biophysical data
    • Beechem J.M. Global analysis of biochemical and biophysical data. Methods Enzymol. 210 (1992) 37-54
    • (1992) Methods Enzymol. , vol.210 , pp. 37-54
    • Beechem, J.M.1
  • 4
    • 0023847706 scopus 로고
    • Insights into enzyme function from studies on mutants of dihydrofolate reductase
    • Benkovic S.J., Fierke C.A., and Naylor A.M. Insights into enzyme function from studies on mutants of dihydrofolate reductase. Science 239 (1988) 1105-1110
    • (1988) Science , vol.239 , pp. 1105-1110
    • Benkovic, S.J.1    Fierke, C.A.2    Naylor, A.M.3
  • 5
    • 34547572025 scopus 로고    scopus 로고
    • Kinetics of binding the mRNA cap analogues to the translation initiation factor eIF4E under second-order reaction conditions
    • Błachut-Okrasinska E., Bojarska E., Stepiński J., and Antosiewicz J. Kinetics of binding the mRNA cap analogues to the translation initiation factor eIF4E under second-order reaction conditions. Biophys. Chem. 129 (2007) 289-297
    • (2007) Biophys. Chem. , vol.129 , pp. 289-297
    • Błachut-Okrasinska, E.1    Bojarska, E.2    Stepiński, J.3    Antosiewicz, J.4
  • 6
    • 65249186465 scopus 로고    scopus 로고
    • Metal binding kinetics of Bi-Histidine sites used in ψ analysis: Evidence of high-energy protein folding intermediates
    • Bosco G., Baxa M., and Sosnick T. Metal binding kinetics of Bi-Histidine sites used in ψ analysis: Evidence of high-energy protein folding intermediates. Biochemistry 48 (2009) 2950-2959
    • (2009) Biochemistry , vol.48 , pp. 2950-2959
    • Bosco, G.1    Baxa, M.2    Sosnick, T.3
  • 9
    • 0028672974 scopus 로고
    • Determining confidence intervals for parameters derived from analysis of equilibrium analytical ultracentrifugation data
    • Brooks I., Watts D., Soneson K., and Hensley P. Determining confidence intervals for parameters derived from analysis of equilibrium analytical ultracentrifugation data. Methods Enzymol. 240 (1994) 459-478
    • (1994) Methods Enzymol. , vol.240 , pp. 459-478
    • Brooks, I.1    Watts, D.2    Soneson, K.3    Hensley, P.4
  • 11
    • 0037193172 scopus 로고    scopus 로고
    • Calf spleen purine nucleoside phosphorylase: Complex kinetic mechanism, hydrolysis of 7-methylguanosine, and oligomeric state in solution
    • Bzowska A. Calf spleen purine nucleoside phosphorylase: Complex kinetic mechanism, hydrolysis of 7-methylguanosine, and oligomeric state in solution. Bioch. Biophys. Acta 1596 (2002) 293-317
    • (2002) Bioch. Biophys. Acta , vol.1596 , pp. 293-317
    • Bzowska, A.1
  • 12
    • 4444273108 scopus 로고    scopus 로고
    • Crystal structure of calf spleen purine nucleoside phosphorylase with two full trimers in the asymmetric unit: Important implications for the mechanism of catalysis
    • Bzowska A., Koellner G., Stroh B.W.-K.A., Raszewski G., Holý A., Steiner T., and Frank J. Crystal structure of calf spleen purine nucleoside phosphorylase with two full trimers in the asymmetric unit: Important implications for the mechanism of catalysis. J. Mol. Biol. 342 (2004) 1015-1032
    • (2004) J. Mol. Biol. , vol.342 , pp. 1015-1032
    • Bzowska, A.1    Koellner, G.2    Stroh, B.W.-K.A.3    Raszewski, G.4    Holý, A.5    Steiner, T.6    Frank, J.7
  • 14
    • 56449128052 scopus 로고    scopus 로고
    • Detection of transglucosidase-catalyzed polysaccharide synthesis on a surface in real-time using surface plasmon resonance spectroscopy
    • Clé C., Gunning A.P., Syson K., Bowater L., Field R.A., and Bornemann S. Detection of transglucosidase-catalyzed polysaccharide synthesis on a surface in real-time using surface plasmon resonance spectroscopy. J. Am. Chem. Soc. 130 (2008) 15234-15235
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 15234-15235
    • Clé, C.1    Gunning, A.P.2    Syson, K.3    Bowater, L.4    Field, R.A.5    Bornemann, S.6
  • 16
    • 41249084268 scopus 로고    scopus 로고
    • CYP2E1 substrate inhibition: Mechanistic interpretation through an effector site for monocyclic compounds
    • Collom S.L., Laddusaw R.M., Burch A.M., Kuzmič P., Grover P.M., and Andand M.D.P. CYP2E1 substrate inhibition: Mechanistic interpretation through an effector site for monocyclic compounds. J. Biol. Chem. 383 (2008) 3487-3496
    • (2008) J. Biol. Chem. , vol.383 , pp. 3487-3496
    • Collom, S.L.1    Laddusaw, R.M.2    Burch, A.M.3    Kuzmič, P.4    Grover, P.M.5    Andand, M.D.P.6
  • 17
    • 0023416976 scopus 로고
    • Minimizing multimodal functions of continuous variables with the "simulated annealing" algorithm
    • Corana A., Marchesi M., Martini C., and Ridella S. Minimizing multimodal functions of continuous variables with the "simulated annealing" algorithm. ACM Trans. Math. Softw. 13 (1987) 262-280
    • (1987) ACM Trans. Math. Softw. , vol.13 , pp. 262-280
    • Corana, A.1    Marchesi, M.2    Martini, C.3    Ridella, S.4
  • 18
    • 3042722089 scopus 로고    scopus 로고
    • PRDM5 is silenced in human cancers and has growth suppressive activities
    • Deng Q., and Huang S. PRDM5 is silenced in human cancers and has growth suppressive activities. Oncogene 17 (2004) 4903-4910
    • (2004) Oncogene , vol.17 , pp. 4903-4910
    • Deng, Q.1    Huang, S.2
  • 19
    • 0033596742 scopus 로고    scopus 로고
    • Kinetic mechanism of tritrichomonas foetus inosine 5′-monophosphate dehydrogenase
    • Digits J.A., and Hedstrom L. Kinetic mechanism of tritrichomonas foetus inosine 5′-monophosphate dehydrogenase. Biochemistry 38 (1999) 2295-2306
    • (1999) Biochemistry , vol.38 , pp. 2295-2306
    • Digits, J.A.1    Hedstrom, L.2
  • 20
    • 0002205684 scopus 로고
    • Experimental designs for the distribution free analysis of enzyme kinetic data
    • Endrényi L. (Ed), Plenum Press, New York
    • Duggleby R. Experimental designs for the distribution free analysis of enzyme kinetic data. In: Endrényi L. (Ed). Kinetic Data Analysis (1981), Plenum Press, New York 169-181
    • (1981) Kinetic Data Analysis , pp. 169-181
    • Duggleby, R.1
  • 21
    • 0000816074 scopus 로고
    • Modified randomization tests for nonparametric hypotheses
    • Dwass M. Modified randomization tests for nonparametric hypotheses. Ann. Math. Stat. 28 (1957) 181-187
    • (1957) Ann. Math. Stat. , vol.28 , pp. 181-187
    • Dwass, M.1
  • 22
    • 0002255250 scopus 로고
    • Design of experiments for estimating enzyme and pharmacokinetic parameters
    • Endrényi L. (Ed), Plenum Press, New York
    • Endrényi L. Design of experiments for estimating enzyme and pharmacokinetic parameters. In: Endrényi L. (Ed). Kinetic Data Analysis (1981), Plenum Press, New York 137-169
    • (1981) Kinetic Data Analysis , pp. 137-169
    • Endrényi, L.1
  • 25
    • 0023668190 scopus 로고
    • Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
    • Fierke C.A., Johnson K.A., and Benkovic S.J. Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli. Biochemistry 26 (1987) 4085-4092
    • (1987) Biochemistry , vol.26 , pp. 4085-4092
    • Fierke, C.A.1    Johnson, K.A.2    Benkovic, S.J.3
  • 26
    • 0023050375 scopus 로고
    • A computer program for enzyme kinetics that combines model discrimination, parameter refinement and sequential experimental design
    • Franco R., Gavalda M.T., and Canela E.I. A computer program for enzyme kinetics that combines model discrimination, parameter refinement and sequential experimental design. Biochem. J. 238 (1986) 855-862
    • (1986) Biochem. J. , vol.238 , pp. 855-862
    • Franco, R.1    Gavalda, M.T.2    Canela, E.I.3
  • 27
    • 58649104886 scopus 로고    scopus 로고
    • Complexation between methyl viologen (paraquat) bis(hexafluorophosphate) and dibenzo[24]crown-8 revisited
    • Gasa T., Spruell J., Dichtel W., Srensen T., Philp D., Stoddart J., and Kuzmič P. Complexation between methyl viologen (paraquat) bis(hexafluorophosphate) and dibenzo[24]crown-8 revisited. Chem. Eur. J. 15 (2009) 106-116
    • (2009) Chem. Eur. J. , vol.15 , pp. 106-116
    • Gasa, T.1    Spruell, J.2    Dichtel, W.3    Srensen, T.4    Philp, D.5    Stoddart, J.6    Kuzmič, P.7
  • 29
    • 0013101606 scopus 로고
    • Über die chemische Affinität
    • Guldberg C.M., and Waage P. Über die chemische Affinität. J. Prakt. Chem. 127 (1879) 69-114
    • (1879) J. Prakt. Chem. , vol.127 , pp. 69-114
    • Guldberg, C.M.1    Waage, P.2
  • 31
    • 34548528384 scopus 로고    scopus 로고
    • Global analysis of protein-protein interactions reveals multiple cytochrome P450 2E1reductase complexes
    • Jamakhandi A.P., Kuzmič P., Sanders D.E., and Miller G.P. Global analysis of protein-protein interactions reveals multiple cytochrome P450 2E1reductase complexes. Biochemistry 46 (2007) 10192-10201
    • (2007) Biochemistry , vol.46 , pp. 10192-10201
    • Jamakhandi, A.P.1    Kuzmič, P.2    Sanders, D.E.3    Miller, G.P.4
  • 32
    • 0026486367 scopus 로고
    • Why, when, and how biochemists should use least squares
    • Johnson M.L. Why, when, and how biochemists should use least squares. Anal. Biochem. 206 (1992) 215-225
    • (1992) Anal. Biochem. , vol.206 , pp. 215-225
    • Johnson, M.L.1
  • 33
    • 0028672474 scopus 로고
    • Use of least-squares techniques in biochemistry
    • Johnson M.L. Use of least-squares techniques in biochemistry. Methods Enzymol. 240 (1994) 1-22
    • (1994) Methods Enzymol. , vol.240 , pp. 1-22
    • Johnson, M.L.1
  • 34
    • 77957095245 scopus 로고
    • Nonlinear least-squares analysis
    • Johnson M.L., and Frasier S.G. Nonlinear least-squares analysis. Methods Enzymol. 117 (1985) 301-342
    • (1985) Methods Enzymol. , vol.117 , pp. 301-342
    • Johnson, M.L.1    Frasier, S.G.2
  • 35
    • 60549105802 scopus 로고    scopus 로고
    • Global Kinetic Explorer: A new computer program for dynamic simulation and fitting of kinetic data
    • Johnson K.A., Simpson Z.B., and Blom T. Global Kinetic Explorer: A new computer program for dynamic simulation and fitting of kinetic data. Anal. Biochem. 387 (2009) 20-29
    • (2009) Anal. Biochem. , vol.387 , pp. 20-29
    • Johnson, K.A.1    Simpson, Z.B.2    Blom, T.3
  • 36
    • 33947472850 scopus 로고
    • A schematic method of deriving the rate laws for enzyme-catalyzed reactions
    • King E.L., and Altman C. A schematic method of deriving the rate laws for enzyme-catalyzed reactions. J. Phys. Chem. 60 (1956) 1375-1378
    • (1956) J. Phys. Chem. , vol.60 , pp. 1375-1378
    • King, E.L.1    Altman, C.2
  • 37
    • 26444479778 scopus 로고
    • Optimization by simulated annealing
    • Kirkpatrick S., Gelatt C., and Vecchi M.P. Optimization by simulated annealing. Science 220 (1983) 671-680
    • (1983) Science , vol.220 , pp. 671-680
    • Kirkpatrick, S.1    Gelatt, C.2    Vecchi, M.P.3
  • 38
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • Kuzmič P. Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase. Anal. Biochem. 237 (1996) 260-273
    • (1996) Anal. Biochem. , vol.237 , pp. 260-273
    • Kuzmič, P.1
  • 39
    • 33644907149 scopus 로고    scopus 로고
    • A generalized numerical approach to rapid-equilibrium enzyme kinetics: Application to 17β-HSD
    • Kuzmič P. A generalized numerical approach to rapid-equilibrium enzyme kinetics: Application to 17β-HSD. Mol. Cell. Endocrinol. 248 (2006) 172-181
    • (2006) Mol. Cell. Endocrinol. , vol.248 , pp. 172-181
    • Kuzmič, P.1
  • 40
    • 75349106266 scopus 로고    scopus 로고
    • A generalized numerical approach to steady-state enzyme kinetics: Applications to protein kinase inhibition
    • in press, doi:10.1016/j.bbapap.2009.07.028
    • Kuzmič P. A generalized numerical approach to steady-state enzyme kinetics: Applications to protein kinase inhibition. Biochim. Biophys. Acta-Prot. Proteom. (2009) in press, doi:10.1016/j.bbapap.2009.07.028
    • (2009) Biochim. Biophys. Acta-Prot. Proteom.
    • Kuzmič, P.1
  • 41
    • 69949100557 scopus 로고    scopus 로고
    • Application of the Van Slyke-Cullen irreversible mechanism in the analysis of enzymatic progress curves
    • Kuzmič P. Application of the Van Slyke-Cullen irreversible mechanism in the analysis of enzymatic progress curves. Anal. Biochem. 394 (2009) 287-289
    • (2009) Anal. Biochem. , vol.394 , pp. 287-289
    • Kuzmič, P.1
  • 43
    • 33745214233 scopus 로고    scopus 로고
    • Mixed-type noncompetitive inhibition of anthrax lethal factor protease by aminoglycosides
    • Kuzmič P., Cregar L., Millis S.Z., and Goldman M. Mixed-type noncompetitive inhibition of anthrax lethal factor protease by aminoglycosides. FEBS J. 273 (2006) 3054-3062
    • (2006) FEBS J. , vol.273 , pp. 3054-3062
    • Kuzmič, P.1    Cregar, L.2    Millis, S.Z.3    Goldman, M.4
  • 44
    • 70349142179 scopus 로고    scopus 로고
    • Analysis of residuals from enzyme kinetic and protein folding experiments in the presence of correlated experimental noise
    • Kuzmič P., Lorenz T., and Reinstein J. Analysis of residuals from enzyme kinetic and protein folding experiments in the presence of correlated experimental noise. Anal. Biochem. 395 (2009) 1-7
    • (2009) Anal. Biochem. , vol.395 , pp. 1-7
    • Kuzmič, P.1    Lorenz, T.2    Reinstein, J.3
  • 45
    • 33645064814 scopus 로고    scopus 로고
    • Selective binding of uranyl cation by a novel calmodulin peptide
    • Le Clainche L., and Vita C. Selective binding of uranyl cation by a novel calmodulin peptide. Environ. Chem. Lett. 4 (2006) 45-49
    • (2006) Environ. Chem. Lett. , vol.4 , pp. 45-49
    • Le Clainche, L.1    Vita, C.2
  • 47
    • 0013504052 scopus 로고
    • Design and analysis of kinetic experiments for discrimination between rival models
    • Endrényi L. (Ed), Plenum Press, New York
    • Mannervik B. Design and analysis of kinetic experiments for discrimination between rival models. In: Endrényi L. (Ed). Kinetic Data Analysis (1981), Plenum Press, New York 235-270
    • (1981) Kinetic Data Analysis , pp. 235-270
    • Mannervik, B.1
  • 48
    • 0020440235 scopus 로고
    • Regression analysis, experimental error, and statistical criteria in the design and analysis of experiments for discrimination between rival kinetic models
    • Mannervik B. Regression analysis, experimental error, and statistical criteria in the design and analysis of experiments for discrimination between rival kinetic models. Methods Enzymol. 87 (1982) 370-390
    • (1982) Methods Enzymol. , vol.87 , pp. 370-390
    • Mannervik, B.1
  • 49
    • 0000169232 scopus 로고
    • An algorithm for least-squares estimation of nonlinear parameters
    • Marquardt D.W. An algorithm for least-squares estimation of nonlinear parameters. J. Soc. Ind. Appl. Math. 11 (1963) 431-441
    • (1963) J. Soc. Ind. Appl. Math. , vol.11 , pp. 431-441
    • Marquardt, D.W.1
  • 50
    • 0032406131 scopus 로고    scopus 로고
    • Non-linear optimization of biochemical pathways: Applications to metabolic engineering and parameter estimation
    • Mendes P., and Kell D. Non-linear optimization of biochemical pathways: Applications to metabolic engineering and parameter estimation. Bioinformatics 14 (1998) 869-883
    • (1998) Bioinformatics , vol.14 , pp. 869-883
    • Mendes, P.1    Kell, D.2
  • 51
    • 0023728105 scopus 로고
    • The behavior and significance of slow-binding enzyme inhibitors
    • Morrison J.F., and Walsh C.T. The behavior and significance of slow-binding enzyme inhibitors. Adv. Enzymol. Relat. Areas Mol. Biol. 61 (1988) 201-301
    • (1988) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.61 , pp. 201-301
    • Morrison, J.F.1    Walsh, C.T.2
  • 52
    • 1642464789 scopus 로고    scopus 로고
    • Model comparison methods
    • Myung J.I., and Pitt M.A. Model comparison methods. Methods Enzymol. 383 (2004) 351-366
    • (2004) Methods Enzymol. , vol.383 , pp. 351-366
    • Myung, J.I.1    Pitt, M.A.2
  • 53
    • 59649086653 scopus 로고    scopus 로고
    • Evaluation and comparison of computational models
    • Myung J.I., Tang Y., and Pitt M.A. Evaluation and comparison of computational models. Methods Enzymol. 454 (2009) 287-304
    • (2009) Methods Enzymol. , vol.454 , pp. 287-304
    • Myung, J.I.1    Tang, Y.2    Pitt, M.A.3
  • 54
    • 0036136472 scopus 로고    scopus 로고
    • Nonparametric permutation tests for functional neuroimaging: A primer with examples
    • Nichols T.E., and Holmes A.P. Nonparametric permutation tests for functional neuroimaging: A primer with examples. Human Brain Map. 15 (2001) 1-25
    • (2001) Human Brain Map. , vol.15 , pp. 1-25
    • Nichols, T.E.1    Holmes, A.P.2
  • 58
    • 0028992812 scopus 로고
    • Increase in fluorescence upon the hydrolysis of tyrosine peptides: Application to proteinase assays
    • Peranteau A.G., Kuzmič P., Angell Y., García-Echeverría C., and Rich D.H. Increase in fluorescence upon the hydrolysis of tyrosine peptides: Application to proteinase assays. Anal. Biochem. 227 (1995) 242-245
    • (1995) Anal. Biochem. , vol.227 , pp. 242-245
    • Peranteau, A.G.1    Kuzmič, P.2    Angell, Y.3    García-Echeverría, C.4    Rich, D.H.5
  • 62
    • 4644298282 scopus 로고    scopus 로고
    • Substitution of the conserved Arg-Tyr dyad selectively disrupts the hydrolysis phase of the IMP dehydrogenase reaction
    • Schlippe Y.V.G., Riera T.V., Seyedsayamdost M.R., and Hedstrom L. Substitution of the conserved Arg-Tyr dyad selectively disrupts the hydrolysis phase of the IMP dehydrogenase reaction. Biochemistry 43 (2004) 4511-4521
    • (2004) Biochemistry , vol.43 , pp. 4511-4521
    • Schlippe, Y.V.G.1    Riera, T.V.2    Seyedsayamdost, M.R.3    Hedstrom, L.4
  • 64
    • 0007589020 scopus 로고
    • The mode of action of urease and of enzymes in general
    • Slyke D.D.V., and Cullen G.E. The mode of action of urease and of enzymes in general. J. Biol. Chem. 19 (1914) 141-180
    • (1914) J. Biol. Chem. , vol.19 , pp. 141-180
    • Slyke, D.D.V.1    Cullen, G.E.2
  • 65
    • 59649125837 scopus 로고    scopus 로고
    • New ifosfamide analogs designed for lower associated neurotoxicity and nephrotoxicity with modified alkylating kinetics leading to enhanced in vitro anticancer activity
    • Storme T., Deroussent A., Mercier L., Prost E., Re M., Munier F., Martens T., Bourget P., Vassal G., Royer J., and Paci A. New ifosfamide analogs designed for lower associated neurotoxicity and nephrotoxicity with modified alkylating kinetics leading to enhanced in vitro anticancer activity. J. Pharmacol. Exp. Ther. 328 (2009) 598-609
    • (2009) J. Pharmacol. Exp. Ther. , vol.328 , pp. 598-609
    • Storme, T.1    Deroussent, A.2    Mercier, L.3    Prost, E.4    Re, M.5    Munier, F.6    Martens, T.7    Bourget, P.8    Vassal, G.9    Royer, J.10    Paci, A.11
  • 66
    • 0026750648 scopus 로고
    • Monte Carlo method for determining complete confidence probability distributions of estimated model parameters
    • Straume M., and Johnson M.L. Monte Carlo method for determining complete confidence probability distributions of estimated model parameters. Methods Enzymol. 210 (1992) 117-129
    • (1992) Methods Enzymol. , vol.210 , pp. 117-129
    • Straume, M.1    Johnson, M.L.2
  • 67
    • 0028924136 scopus 로고
    • Kinetics of slow and tight-binding inhibitors
    • Szedlacsek S., and Duggleby R.G. Kinetics of slow and tight-binding inhibitors. Methods Enzymol. 249 (1995) 144-180
    • (1995) Methods Enzymol. , vol.249 , pp. 144-180
    • Szedlacsek, S.1    Duggleby, R.G.2
  • 68
    • 0033956652 scopus 로고    scopus 로고
    • Kinetic modelling in food science: A case study on chlorophyll degradation in olives
    • Van Boekel M. Kinetic modelling in food science: A case study on chlorophyll degradation in olives. J. Sci. Food Agric. 80 (2000) 3-9
    • (2000) J. Sci. Food Agric. , vol.80 , pp. 3-9
    • Van Boekel, M.1
  • 69
    • 0036023490 scopus 로고    scopus 로고
    • High-level production of d-mannitol with membrane cell-recycle bioreactor
    • Von Weymarn N., Kiviharju K., and Leisola M. High-level production of d-mannitol with membrane cell-recycle bioreactor. J. Ind. Microbiol. Biotechnol. 29 (2002) 44-49
    • (2002) J. Ind. Microbiol. Biotechnol. , vol.29 , pp. 44-49
    • Von Weymarn, N.1    Kiviharju, K.2    Leisola, M.3
  • 70
    • 0028672835 scopus 로고
    • Parameter estimates from nonlinear models
    • Watts D.G. Parameter estimates from nonlinear models. Methods Enzymol. 240 (1994) 23-36
    • (1994) Methods Enzymol. , vol.240 , pp. 23-36
    • Watts, D.G.1
  • 71
    • 33646533314 scopus 로고    scopus 로고
    • Probing the mechanism of purine nucleoside phosphorylase by steady-state kinetic studies and ligand binding characterization determined by fluorimetric titrations
    • Wielgus-Kutrowska B., and Bzowska A. Probing the mechanism of purine nucleoside phosphorylase by steady-state kinetic studies and ligand binding characterization determined by fluorimetric titrations. Biochim. Biophys. Acta 1764 (2006) 887-902
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 887-902
    • Wielgus-Kutrowska, B.1    Bzowska, A.2
  • 72
    • 0037014054 scopus 로고    scopus 로고
    • Purine nucleoside phosphorylase from cellulomonas sp.: Physicochemical properties and binding of substrates determined by ligand-dependent enhancement of enzyme intrinsic fluorescence, and by protective effects of ligands on thermal inactivation of the enzyme
    • Wielgus-Kutrowska B., Bzowska A., Tebbe J., Koellner G., and Shugar D. Purine nucleoside phosphorylase from cellulomonas sp.: Physicochemical properties and binding of substrates determined by ligand-dependent enhancement of enzyme intrinsic fluorescence, and by protective effects of ligands on thermal inactivation of the enzyme. Biochem. Biophys. Acta 1597 (2002) 320-334
    • (2002) Biochem. Biophys. Acta , vol.1597 , pp. 320-334
    • Wielgus-Kutrowska, B.1    Bzowska, A.2    Tebbe, J.3    Koellner, G.4    Shugar, D.5
  • 73
    • 33846452894 scopus 로고    scopus 로고
    • Towards the mechanism of trimeric purine nucleoside phosphorylases: Stopped-flow studies of binding of multisubstrate analogue inhibitor-2-amino-9-[2-(phosphonomethoxy)ethyl]-6-sulfanylpurine
    • Wielgus-Kutrowska B., Antosiewicz J., Dlugosz M., Holý A., and Bzowska A. Towards the mechanism of trimeric purine nucleoside phosphorylases: Stopped-flow studies of binding of multisubstrate analogue inhibitor-2-amino-9-[2-(phosphonomethoxy)ethyl]-6-sulfanylpurine. Biophys. Chem. 125 (2007) 260-268
    • (2007) Biophys. Chem. , vol.125 , pp. 260-268
    • Wielgus-Kutrowska, B.1    Antosiewicz, J.2    Dlugosz, M.3    Holý, A.4    Bzowska, A.5
  • 74
    • 0018699952 scopus 로고
    • The kinetics of reversible tight-binding inhibition
    • Williams J.W., and Morrison J.F. The kinetics of reversible tight-binding inhibition. Methods Enzymol. 63 (1979) 437-467
    • (1979) Methods Enzymol. , vol.63 , pp. 437-467
    • Williams, J.W.1    Morrison, J.F.2
  • 75
    • 1042301413 scopus 로고    scopus 로고
    • Mechanism of loading the Escherichia coli DNA polymerase III sliding clamp. I. Two distinct activities for individual ATP sites in the γ complex
    • Williams C.R., Snyder A.K., Kuzmič P., O'Donnell M., and Bloom L.B. Mechanism of loading the Escherichia coli DNA polymerase III sliding clamp. I. Two distinct activities for individual ATP sites in the γ complex. J. Biol. Chem. 279 (2004) 4376-4385
    • (2004) J. Biol. Chem. , vol.279 , pp. 4376-4385
    • Williams, C.R.1    Snyder, A.K.2    Kuzmič, P.3    O'Donnell, M.4    Bloom, L.B.5


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