메뉴 건너뛰기




Volumn 118, Issue 15, 2014, Pages 4062-4068

Macromolecular crowding effect upon in vitro enzyme kinetics: Mixed activation-diffusion control of the oxidation of NADH by pyruvate catalyzed by lactate dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; DEXTRAN; MACROMOLECULES;

EID: 84899019693     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp4118858     Document Type: Article
Times cited : (54)

References (57)
  • 1
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular Crowding: Obvious but Underappreciated
    • Ellis, R. J. Macromolecular Crowding: Obvious but Underappreciated Trends Biochem. Sci. 2001, 26, 577-604
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 577-604
    • Ellis, R.J.1
  • 2
    • 0024006767 scopus 로고
    • Tracer Diffusion of Globular Proteins in Concentrated Protein Solutions
    • Muramatsu, N.; Minton, A. P. Tracer Diffusion of Globular Proteins in Concentrated Protein Solutions Proc. Natl. Acad. Sci. U. S. A. 1988, 85, 2984-2988
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 2984-2988
    • Muramatsu, N.1    Minton, A.P.2
  • 3
    • 0034640133 scopus 로고    scopus 로고
    • Anomalous Diffusion of Fluorescent Probes inside Living Cell Nuclei Investigated by Spatially-Resolved Fluorescence Correlation Spectroscopy
    • Wachsmuth, M.; Waldeck, W.; Langowski, J. Anomalous Diffusion of Fluorescent Probes inside Living Cell Nuclei Investigated by Spatially-Resolved Fluorescence Correlation Spectroscopy J. Mol. Biol. 2000, 298, 677-689
    • (2000) J. Mol. Biol. , vol.298 , pp. 677-689
    • Wachsmuth, M.1    Waldeck, W.2    Langowski, J.3
  • 4
    • 0034077947 scopus 로고    scopus 로고
    • Translational Diffusion of Globular Proteins in the Cytoplasm of Cultured Muscle Cells
    • Arrio-Dupont, M.; Foucault, G.; Vacher, M.; Devaux, P. F.; Cribier, S. Translational Diffusion of Globular Proteins in the Cytoplasm of Cultured Muscle Cells Biophys. J. 2001, 78, 901-907
    • (2001) Biophys. J. , vol.78 , pp. 901-907
    • Arrio-Dupont, M.1    Foucault, G.2    Vacher, M.3    Devaux, P.F.4    Cribier, S.5
  • 5
    • 0036164351 scopus 로고    scopus 로고
    • Solute and Macromolecular Diffusion in Cellular Aqueous Compartments
    • Verkman, A. S. Solute and Macromolecular Diffusion in Cellular Aqueous Compartments Trends Biochem. Sci. 2002, 27, 27-32
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 27-32
    • Verkman, A.S.1
  • 6
    • 14844331313 scopus 로고    scopus 로고
    • Anomalous Subdiffusion is a Measure for Cytoplasmic Crowding in Living Cells
    • Weiss, M.; Elsner, M.; Kartberg, F.; Nilsson, T. Anomalous Subdiffusion is a Measure for Cytoplasmic Crowding in Living Cells Biophys. J. 2004, 87, 3518-3524
    • (2004) Biophys. J. , vol.87 , pp. 3518-3524
    • Weiss, M.1    Elsner, M.2    Kartberg, F.3    Nilsson, T.4
  • 7
    • 48249124302 scopus 로고    scopus 로고
    • Crowding Effects on Diffusion in Solutions
    • Dix, J. A.; Verkman, A. S. Crowding Effects on Diffusion in Solutions Annu. Rev. Biophys. 2008, 37, 247-263
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 247-263
    • Dix, J.A.1    Verkman, A.S.2
  • 8
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular Crowding and Confinement: Biochemical, Biophysical and Potential Physiological Consequences
    • Zhou, H. X.; Rivas, G.; Minton, A. P. Macromolecular Crowding and Confinement: Biochemical, Biophysical and Potential Physiological Consequences Annu. Rev. Biophys. 2008, 37, 375-397
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 375-397
    • Zhou, H.X.1    Rivas, G.2    Minton, A.P.3
  • 9
    • 0019883893 scopus 로고
    • Effect of Macromolecular Crowding upon the Structure and Function of an Enzyme: Glyceraldehyde-3-phosphate dehydrogenase
    • Minton, A. P.; Wilf, J. Effect of Macromolecular Crowding upon the Structure and Function of an Enzyme: Glyceraldehyde-3-phosphate dehydrogenase Biochemistry 1981, 20, 4821-4826
    • (1981) Biochemistry , vol.20 , pp. 4821-4826
    • Minton, A.P.1    Wilf, J.2
  • 10
    • 84985735713 scopus 로고
    • Excluded Volume as a Determinant of Macromolecular Structure and Reactivity
    • Minton, A. P. Excluded Volume as a Determinant of Macromolecular Structure and Reactivity Biopolymers 1981, 20, 2093-2120
    • (1981) Biopolymers , vol.20 , pp. 2093-2120
    • Minton, A.P.1
  • 11
    • 0027318513 scopus 로고
    • Macromolecular Crowding: Biophysical, Biochemical, and Physiological Consequences
    • Zimmerman, S. B.; Minton, A. P. Macromolecular Crowding: Biophysical, Biochemical, and Physiological Consequences Annu. Rev. Biophys. Biomol. Struct. 1993, 22, 27-65
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 12
    • 0033587619 scopus 로고    scopus 로고
    • Direct Observation of the Self-Association of Dilute Proteins in the Presence of Inert Macromolecules at High Concentration via Tracer Sedimentation Equilibrium: Theory, Experiment, and Biological Significance
    • Rivas, G.; Fernandez, J. A.; Minton, A. P. Direct Observation of the Self-Association of Dilute Proteins in the Presence of Inert Macromolecules at High Concentration via Tracer Sedimentation Equilibrium: Theory, Experiment, and Biological Significance Biochemistry 1999, 38, 9379-9388
    • (1999) Biochemistry , vol.38 , pp. 9379-9388
    • Rivas, G.1    Fernandez, J.A.2    Minton, A.P.3
  • 13
    • 0033572725 scopus 로고    scopus 로고
    • Effects of Macromolecular Crowding on Protein Folding and Aggregation
    • Van den Berg, B.; Ellis, R. J.; Dobson, C. M. Effects of Macromolecular Crowding on Protein Folding and Aggregation EMBO J. 1999, 18, 6927-6933
    • (1999) EMBO J. , vol.18 , pp. 6927-6933
    • Van Den Berg, B.1    Ellis, R.J.2    Dobson, C.M.3
  • 14
    • 0033969150 scopus 로고    scopus 로고
    • Implications of Macromolecular Crowding for Protein Assembly
    • Minton, A. P. Implications of Macromolecular Crowding for Protein Assembly Curr. Opin. Struct. Biol. 2000, 10, 34-39
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 34-39
    • Minton, A.P.1
  • 15
    • 0035853141 scopus 로고    scopus 로고
    • Direct Observation of the Enhancement of Non-Cooperative Protein Assembly by Macromolecular Crowding: Indefinite Self-Association of the Bacterial Cell Division Protein FtsZ
    • Rivas, G.; Fernandez, J. A.; Minton, A. P. Direct Observation of the Enhancement of Non-Cooperative Protein Assembly by Macromolecular Crowding: Indefinite Self-Association of the Bacterial Cell Division Protein FtsZ Roc. Natl. Acad. Sci. U. S. A. 2001, 98, 3150-3155
    • (2001) Roc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 3150-3155
    • Rivas, G.1    Fernandez, J.A.2    Minton, A.P.3
  • 16
    • 0842268058 scopus 로고    scopus 로고
    • Effect of Crowding on Protein-Protein Association Rates: Fundamental Differences between Low and High Mass Crowding Agents
    • Kozer, N.; Schreiber, G. Effect of Crowding on Protein-Protein Association Rates: Fundamental Differences between Low and High Mass Crowding Agents J. Mol. Biol. 2004, 336, 763-774
    • (2004) J. Mol. Biol. , vol.336 , pp. 763-774
    • Kozer, N.1    Schreiber, G.2
  • 17
    • 4544252011 scopus 로고    scopus 로고
    • The Effect of Macromolecular Crowding on Protein Aggregation and Amyloid Fibril Formation
    • Munishkina, L. A.; Cooper, E. M.; Uversky, V.; Fink, A. The Effect of Macromolecular Crowding on Protein Aggregation and Amyloid Fibril Formation J. Mol. Recognit. 2004, 17, 456-464
    • (2004) J. Mol. Recognit. , vol.17 , pp. 456-464
    • Munishkina, L.A.1    Cooper, E.M.2    Uversky, V.3    Fink, A.4
  • 19
    • 4544278751 scopus 로고    scopus 로고
    • Protein Folding and Binding in Confined Spaces and in Crowded Solutions
    • Zhou, H.-X. Protein Folding and Binding in Confined Spaces and in Crowded Solutions J. Mol. Recognit. 2004, 17, 368-375
    • (2004) J. Mol. Recognit. , vol.17 , pp. 368-375
    • Zhou, H.-X.1
  • 20
    • 25444487734 scopus 로고    scopus 로고
    • Influence of Macromolecular Crowding upon the Stability and State of Association of Proteins: Predictions and Observations
    • Minton, A. P. Influence of Macromolecular Crowding upon the Stability and State of Association of Proteins: Predictions and Observations J. Pharm. Sci. 2005, 94, 1668-1675
    • (2005) J. Pharm. Sci. , vol.94 , pp. 1668-1675
    • Minton, A.P.1
  • 21
    • 65249099497 scopus 로고    scopus 로고
    • Fundamental Aspects of Protein-Protein Association Kinetics
    • Schreiber, G.; Haran, G.; Zhou, H.-X. Fundamental Aspects of Protein-Protein Association Kinetics Chem. Rev. 2009, 109, 839-860
    • (2009) Chem. Rev. , vol.109 , pp. 839-860
    • Schreiber, G.1    Haran, G.2    Zhou, H.-X.3
  • 22
    • 78049249046 scopus 로고    scopus 로고
    • Effects of Macromolecular Crowding on Protein Conformational Changes
    • e1000833
    • Dong, H.; Qin, S.; Zhou, H.-X. Effects of Macromolecular Crowding on Protein Conformational Changes PLoS Comput. Biol. 2010, 6 e1000833
    • (2010) PLoS Comput. Biol. , vol.6
    • Dong, H.1    Qin, S.2    Zhou, H.-X.3
  • 23
    • 0015239903 scopus 로고
    • Enzyme Reactions in Polymer Media
    • Laurent, T. C. Enzyme Reactions in Polymer Media Eur. J. Biochem. 1971, 21, 498-506
    • (1971) Eur. J. Biochem. , vol.21 , pp. 498-506
    • Laurent, T.C.1
  • 24
    • 0032762645 scopus 로고    scopus 로고
    • Crowding Effects on EcoRV Kinetics and Binding
    • Wenner, J. R.; Bloomfield, V. A. Crowding Effects on EcoRV Kinetics and Binding Biophys. J. 1999, 77, 3234-3241
    • (1999) Biophys. J. , vol.77 , pp. 3234-3241
    • Wenner, J.R.1    Bloomfield, V.A.2
  • 25
    • 0037939764 scopus 로고    scopus 로고
    • Cytosol-Mimetic Chemistry: Kinetics of the Trypsin-Catalyzed Hydrolysis of p -Nitrophenyl Acetate upon Addition of Polyethylene Glycol and N - Tert -Butyl Acetoacetamide
    • Asaad, N.; Engberts, J. B. F. N. Cytosol-Mimetic Chemistry: Kinetics of the Trypsin-Catalyzed Hydrolysis of p -Nitrophenyl Acetate upon Addition of Polyethylene Glycol and N-tert -Butyl Acetoacetamide J. Am. Chem. Soc. 2003, 125, 6874-6875
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6874-6875
    • Asaad, N.1    Engberts, J.B.F.N.2
  • 26
    • 33745215602 scopus 로고    scopus 로고
    • The Effect of the Presence of Globular Proteins and Elongated Polymers on Enzyme Activity
    • Derham, B. K.; Harding, J. J. The Effect of the Presence of Globular Proteins and Elongated Polymers on Enzyme Activity Biochim. Biophys. Acta 2006, 1764, 1000-1006
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1000-1006
    • Derham, B.K.1    Harding, J.J.2
  • 27
    • 33746868886 scopus 로고    scopus 로고
    • Applications of Isothermal Titration Calorimetry to Measure Enzyme Kinetics and Activity in Complex Solutions
    • Olsen, S. N. Applications of Isothermal Titration Calorimetry to Measure Enzyme Kinetics and Activity in Complex Solutions Thermochim. Acta 2006, 448, 12-18
    • (2006) Thermochim. Acta , vol.448 , pp. 12-18
    • Olsen, S.N.1
  • 28
    • 33750590948 scopus 로고    scopus 로고
    • Effect of Molecular Crowding on DNA Polymerase Activity
    • Sasaki, Y.; Miyoshi, D.; Sugimoto, N. Effect of Molecular Crowding on DNA Polymerase Activity Biotechnol. J. 2006, 1, 440-446
    • (2006) Biotechnol. J. , vol.1 , pp. 440-446
    • Sasaki, Y.1    Miyoshi, D.2    Sugimoto, N.3
  • 29
    • 33845218867 scopus 로고    scopus 로고
    • Effect of Crowding by Dextrans and Ficolls on the Rate of Alkaline Phosphatase-Catalyzed Hydrolysis: A Size-Dependent Investigation
    • Homchaudhuri, L.; Sarma, N.; Swaminathan, R. Effect of Crowding by Dextrans and Ficolls on the Rate of Alkaline Phosphatase-Catalyzed Hydrolysis: A Size-Dependent Investigation Biopolymers 2006, 83, 477-485
    • (2006) Biopolymers , vol.83 , pp. 477-485
    • Homchaudhuri, L.1    Sarma, N.2    Swaminathan, R.3
  • 30
    • 34547590372 scopus 로고    scopus 로고
    • Effects of Osmolytes on Hexokinase Kinetics Combined with Macromolecular Crowding Test of the Osmolyte Compatibility Hypothesis Towards Crowded Systems
    • Olsen, S. N.; Ramløv, H.; Westh, P. Effects of Osmolytes on Hexokinase Kinetics Combined with Macromolecular Crowding Test of the Osmolyte Compatibility Hypothesis Towards Crowded Systems Comp. Biochem. Physiol., A: Mol. Integr. Physiol. 2007, 148, 339-345
    • (2007) Comp. Biochem. Physiol., A: Mol. Integr. Physiol. , vol.148 , pp. 339-345
    • Olsen, S.N.1    Ramløv, H.2    Westh, P.3
  • 31
    • 33847127877 scopus 로고    scopus 로고
    • Escherichia coli AspP Activity is Enhanced by Macromolecular Crowding and by Both Glucose-1,6-bisphosphate and Nucleotide-Sugars
    • Moran-Zorzano, M. T.; Viale, A.; Muñoz, F.; Alonso-Casajas, N.; Eydaltm, G. Escherichia coli AspP Activity is Enhanced by Macromolecular Crowding and by Both Glucose-1,6-bisphosphate and Nucleotide-Sugars FEBS Lett. 2007, 581, 1035-1040
    • (2007) FEBS Lett. , vol.581 , pp. 1035-1040
    • Moran-Zorzano, M.T.1    Viale, A.2    Muñoz, F.3    Alonso-Casajas, N.4    Eydaltm, G.5
  • 32
    • 33846569091 scopus 로고    scopus 로고
    • Effects of Macromolecular Crowding on the Intrinsic Catalytic Efficiency and Structure of Enterobactin-Specific Isochorismate Synthase
    • Jiang, M.; Gou, Z. H. Effects of Macromolecular Crowding on the Intrinsic Catalytic Efficiency and Structure of Enterobactin-Specific Isochorismate Synthase J. Am. Chem. Soc. 2007, 129, 730-731
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 730-731
    • Jiang, M.1    Gou, Z.H.2
  • 33
    • 34547613317 scopus 로고    scopus 로고
    • Regulation of DNA Nucleases by Molecular Crowding
    • Sasaki, Y.; Miyoshi, D.; Sungimoto, N. Regulation of DNA Nucleases by Molecular Crowding Nucleic Acids Res. 2007, 35, 4086-4093
    • (2007) Nucleic Acids Res. , vol.35 , pp. 4086-4093
    • Sasaki, Y.1    Miyoshi, D.2    Sungimoto, N.3
  • 34
    • 79951575052 scopus 로고    scopus 로고
    • What is the True Enzyme Kinetics in the Biological System? An Investigation of Macromolecular Crowding Effect upon Enzyme Kinetics of Glucose-6-phosphate Dehydrogenase
    • Norris, M. G. S.; Malys, N. What is the True Enzyme Kinetics in the Biological System? An Investigation of Macromolecular Crowding Effect upon Enzyme Kinetics of Glucose-6-phosphate Dehydrogenase Biochem. Biophys. Res. Commun. 2011, 405, 388-392
    • (2011) Biochem. Biophys. Res. Commun. , vol.405 , pp. 388-392
    • Norris, M.G.S.1    Malys, N.2
  • 35
    • 79960843920 scopus 로고    scopus 로고
    • Role of Hydration on the Functionality of a Proteolytic Enzyme α-Chymotrypsin under Crowded Environment
    • Verma, P. K.; Rakshit, S.; Mitra, R. K.; Pal, S. K. Role of Hydration on the Functionality of a Proteolytic Enzyme α-Chymotrypsin under Crowded Environment Biochimie 2011, 93, 1424-1433
    • (2011) Biochimie , vol.93 , pp. 1424-1433
    • Verma, P.K.1    Rakshit, S.2    Mitra, R.K.3    Pal, S.K.4
  • 36
    • 79955841588 scopus 로고    scopus 로고
    • Influence of Nano-Viscosity and Depletion Interactions on Cleavage of DNA by Enzymes in Glycerol and Poly(Ethylene Glycol) Solutions: Qualitative Analysis
    • Hou, S.; Ziebacz, N.; Kalwarczyk, T.; Kaminski, T. S.; Wieczoreka, S. A.; Holyst, R. Influence of Nano-Viscosity and Depletion Interactions on Cleavage of DNA by Enzymes in Glycerol and Poly(Ethylene Glycol) Solutions: Qualitative Analysis Soft Matter 2011, 7, 3092-3099
    • (2011) Soft Matter , vol.7 , pp. 3092-3099
    • Hou, S.1    Ziebacz, N.2    Kalwarczyk, T.3    Kaminski, T.S.4    Wieczoreka, S.A.5    Holyst, R.6
  • 37
    • 79952849764 scopus 로고    scopus 로고
    • Effect of Crowding by Dextrans on the Hydrolysis of N -Succinyl-l-phenyl-Ala- p -nitroanilide Catalyzed by α-Chymotrypsin
    • Pastor, I.; Vilaseca, E.; Madurga, S.; Garces, J. L.; Cascante, M.; Mas, F. Effect of Crowding by Dextrans on the Hydrolysis of N -Succinyl-l-phenyl-Ala- p -nitroanilide Catalyzed by α-Chymotrypsin J. Phys. Chem. B 2011, 115, 1115-1121
    • (2011) J. Phys. Chem. B , vol.115 , pp. 1115-1121
    • Pastor, I.1    Vilaseca, E.2    Madurga, S.3    Garces, J.L.4    Cascante, M.5    Mas, F.6
  • 38
    • 84880004592 scopus 로고    scopus 로고
    • Molecular Crowding Enhanced ATPase Activity of the RNA Helicase elF4A Correlates with Compaction of Its Quaternary Structure and Association with elF4G
    • Akabayov, S. R.; Akabayov, B.; Richardson, C. C.; Wagner, G. Molecular Crowding Enhanced ATPase Activity of the RNA Helicase elF4A Correlates with Compaction of Its Quaternary Structure and Association with elF4G J. Am. Chem. Soc. 2013, 135, 10040-10047
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 10040-10047
    • Akabayov, S.R.1    Akabayov, B.2    Richardson, C.C.3    Wagner, G.4
  • 40
    • 84873668144 scopus 로고    scopus 로고
    • Enzyme Entrapped in Polymer-Modified Nanopores: The Effects of Macromolecular Crowding and Surface Hydrophobicity
    • Liu, J.; Peng, J.; Shen, S.; Jin, Q.; Li, C.; Yang, Q. Enzyme Entrapped in Polymer-Modified Nanopores: The Effects of Macromolecular Crowding and Surface Hydrophobicity Chem.-Eur. J. 2013, 19, 2711-2719
    • (2013) Chem.-Eur. J. , vol.19 , pp. 2711-2719
    • Liu, J.1    Peng, J.2    Shen, S.3    Jin, Q.4    Li, C.5    Yang, Q.6
  • 41
    • 84889254114 scopus 로고    scopus 로고
    • Influence of Macromolecular Crowding on the Oxidation of ABTS by Hydrogen Peroxide Catalyzed by HRP
    • doi: 10.4172/2324-9099.1000107
    • Pitulice, L.; Pastor, I.; Vilaseca, E.; Madurga, S.; Isvoran, A.; Cascante, M.; Mas, F. Influence of Macromolecular Crowding on the Oxidation of ABTS by Hydrogen Peroxide Catalyzed by HRP. J. Biocatal. Biotransformation 2013, 2, 1, doi: 10.4172/2324-9099.1000107.
    • (2013) J. Biocatal. Biotransformation , vol.2 , Issue.1
    • Pitulice, L.1    Pastor, I.2    Vilaseca, E.3    Madurga, S.4    Isvoran, A.5    Cascante, M.6    Mas, F.7
  • 43
    • 4544382556 scopus 로고    scopus 로고
    • A Potential Role for Isothermal Calorimetry in Studies of the Effects of Thermodynamic Non-Ideality in Enzyme-Catalyzed Reactions
    • Lonhienne, T. G. A.; Winzor, D. A Potential Role for Isothermal Calorimetry in Studies of the Effects of Thermodynamic Non-Ideality in Enzyme-Catalyzed Reactions J. Mol. Recognit. 2004, 17, 351-361
    • (2004) J. Mol. Recognit. , vol.17 , pp. 351-361
    • Lonhienne, T.G.A.1    Winzor, D.2
  • 44
    • 33646536078 scopus 로고    scopus 로고
    • The Influence of Macromolecular Crowding on HIV-1 Protease Molecular Dynamics
    • Minh, D. D.; Chang, C.; Trylska, J.; Tozzini, V.; McCammon, J. A. The Influence of Macromolecular Crowding on HIV-1 Protease Molecular Dynamics J. Am. Chem. Soc. 2006, 128, 6006-6007
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 6006-6007
    • Minh, D.D.1    Chang, C.2    Trylska, J.3    Tozzini, V.4    McCammon, J.A.5
  • 45
    • 0036789480 scopus 로고    scopus 로고
    • Monte-Carlo Simulations of Enzyme Kinetics in Two Dimensions: Fractal Kinetics and Spatial Segregation
    • Berry, H. Monte-Carlo Simulations of Enzyme Kinetics in Two Dimensions: Fractal Kinetics and Spatial Segregation Biophys. J. 2002, 83, 1891-1901
    • (2002) Biophys. J. , vol.83 , pp. 1891-1901
    • Berry, H.1
  • 46
    • 2442543316 scopus 로고    scopus 로고
    • Reaction Kinetics in Intracellular Environments with Macromolecular Crowding: Simulations and Rate Laws
    • Schnell, S.; Turner, T. E. Reaction Kinetics in Intracellular Environments with Macromolecular Crowding: Simulations and Rate Laws Prog. Biophys. Mol. Biol. 2004, 85, 235-260
    • (2004) Prog. Biophys. Mol. Biol. , vol.85 , pp. 235-260
    • Schnell, S.1    Turner, T.E.2
  • 48
    • 84898994134 scopus 로고    scopus 로고
    • Monte Carlo Simulations of Enzymatic Reactions in Crowded Media. Effect of the Enzyme-Obstacle Relative Size
    • 10.1016/j.mbs.2014.03.012
    • Pitulice, L.; Vilaseca, E.; Pastor, I.; Madurga, S.; Garcés, J. L.; Isvoran, A.; Mas, F. Monte Carlo Simulations of Enzymatic Reactions in Crowded Media. Effect of the Enzyme-Obstacle Relative Size Math. Biosci. 2014, 10.1016/j.mbs.2014.03.012
    • (2014) Math. Biosci.
    • Pitulice, L.1    Vilaseca, E.2    Pastor, I.3    Madurga, S.4    Garcés, J.L.5    Isvoran, A.6    Mas, F.7
  • 49
    • 0000039143 scopus 로고
    • Kinetics Studies of Rabbit Muscle Lactate Dehydrogenase
    • Zewe, V.; Fromm, H. J. Kinetics Studies of Rabbit Muscle Lactate Dehydrogenase J. Biol. Chem. 1962, 237, 1668-1675
    • (1962) J. Biol. Chem. , vol.237 , pp. 1668-1675
    • Zewe, V.1    Fromm, H.J.2
  • 50
    • 0007285384 scopus 로고
    • Kinetics Studies of Rabbit Muscle Lactate Dehydrogenase II. Mechanism of Reaction
    • Zewe, V.; Fromm, H. J. Kinetics Studies of Rabbit Muscle Lactate Dehydrogenase II. Mechanism of Reaction Biochemistry 1965, 4, 782-792
    • (1965) Biochemistry , vol.4 , pp. 782-792
    • Zewe, V.1    Fromm, H.J.2
  • 52
    • 0014930842 scopus 로고
    • Substrate-Inhibited Lactate Dehydrogenase. Reaction Mechanism and Essential Role of Dissociated Subunits
    • Griffin, J. H.; Criddle, R. S. Substrate-Inhibited Lactate Dehydrogenase. Reaction Mechanism and Essential Role of Dissociated Subunits Biochemistry 1970, 9, 1195-1205
    • (1970) Biochemistry , vol.9 , pp. 1195-1205
    • Griffin, J.H.1    Criddle, R.S.2
  • 53
    • 0028140412 scopus 로고
    • Anomalous Diffusion Due to Obstacles: A Monte Carlo Study
    • Saxton, M. J. Anomalous Diffusion Due to Obstacles: A Monte Carlo Study Biophys. J. 1994, 66, 394-401
    • (1994) Biophys. J. , vol.66 , pp. 394-401
    • Saxton, M.J.1
  • 54
    • 77949783433 scopus 로고    scopus 로고
    • Diffusion of α-Chymotrypsin in Solution-Crowded Media. A Fluorescence Recovery after Photobleaching Study
    • Pastor, I.; Vilaseca, E.; Madurga, S.; Garcés, J. L.; Cascante, M.; Mas, F. Diffusion of α-Chymotrypsin in Solution-Crowded Media. A Fluorescence Recovery after Photobleaching Study J. Phys. Chem. B 2010, 114, 4028-4034
    • (2010) J. Phys. Chem. B , vol.114 , pp. 4028-4034
    • Pastor, I.1    Vilaseca, E.2    Madurga, S.3    Garcés, J.L.4    Cascante, M.5    Mas, F.6
  • 55
    • 77956767037 scopus 로고    scopus 로고
    • (erratum)
    • J. Phys. Chem. B 2010, 114, 12182. (erratum)
    • (2010) J. Phys. Chem. B , vol.114 , pp. 12182
  • 56
    • 79953903082 scopus 로고    scopus 로고
    • New Insights into Diffusion in 3D Crowded Media by Monte Carlo Simulations: Effect of Size, Mobility and Spatial Distribution of Obstacles
    • Vilaseca, E.; Isvoran, A.; Madurga, S.; Garcés, J. L.; Pastor, I.; Mas, F. New Insights into Diffusion in 3D Crowded Media by Monte Carlo Simulations: Effect of Size, Mobility and Spatial Distribution of Obstacles Phys. Chem. Chem. Phys. 2011, 13, 7396-7407
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 7396-7407
    • Vilaseca, E.1    Isvoran, A.2    Madurga, S.3    Garcés, J.L.4    Pastor, I.5    Mas, F.6
  • 57
    • 79952141087 scopus 로고    scopus 로고
    • Diffusion in Macromolecular Crowded Media. Monte Carlo Simulation of Obstructed Diffusion vs. FRAP Experiments
    • Vilaseca, E.; Pastor, I.; Isvoran, A.; Madurga, S.; Garcés, J. L.; Mas, F. Diffusion in Macromolecular Crowded Media. Monte Carlo Simulation of Obstructed Diffusion vs. FRAP Experiments Theor. Chem. Acc. 2011, 128, 795-805
    • (2011) Theor. Chem. Acc. , vol.128 , pp. 795-805
    • Vilaseca, E.1    Pastor, I.2    Isvoran, A.3    Madurga, S.4    Garcés, J.L.5    Mas, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.