메뉴 건너뛰기




Volumn 1824, Issue 5, 2012, Pages 769-784

Thermal stabilty of glucokinase (GK) as influenced by the substrate glucose, an allosteric glucokinase activator drug (GKA) and the osmolytes glycerol and urea

Author keywords

Calorimetry; Denaturation; Diabetes; Glucokinase; Protein stability; Tryptophan fluorescence

Indexed keywords

APOENZYME; ENZYME ACTIVATOR; GLUCOKINASE; GLUCOKINASE ACTIVATOR; GLUCOSE; GLYCEROL; SURFACE WATER; UNCLASSIFIED DRUG; UREA; ADENOSINE TRIPHOSPHATE; HYBRID PROTEIN; WATER;

EID: 84859779953     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.03.003     Document Type: Article
Times cited : (15)

References (68)
  • 1
    • 33644749337 scopus 로고    scopus 로고
    • The network of glucokinase-expressing cells in glucose homeostasis and the potential of glucokinase activators for diabetes therapy
    • F.M. Matschinsky, M.A. Magnuson, D. Zelent, T.L. Jetton, N. Doliba, Y. Han, R. Taub, and J. Grimsby The network of glucokinase-expressing cells in glucose homeostasis and the potential of glucokinase activators for diabetes therapy Diabetes 55 2006 1 12
    • (2006) Diabetes , vol.55 , pp. 1-12
    • Matschinsky, F.M.1    Magnuson, M.A.2    Zelent, D.3    Jetton, T.L.4    Doliba, N.5    Han, Y.6    Taub, R.7    Grimsby, J.8
  • 2
    • 49649099805 scopus 로고    scopus 로고
    • Glucokinase and molecular aspects of liver glycogen metabolism
    • L. Agius Glucokinase and molecular aspects of liver glycogen metabolism Biochem. J. 414 2008 1 18
    • (2008) Biochem. J. , vol.414 , pp. 1-18
    • Agius, L.1
  • 3
    • 58149525327 scopus 로고    scopus 로고
    • Molecular physiology of mammalian glucokinase
    • P.B. Iynedjian Molecular physiology of mammalian glucokinase Cell. Mol. Life Sci. 66 2008 27 42
    • (2008) Cell. Mol. Life Sci. , vol.66 , pp. 27-42
    • Iynedjian, P.B.1
  • 4
    • 67349139275 scopus 로고    scopus 로고
    • Assessing the potential of glucokinase activators in diabetes therapy
    • F.M. Matschinsky Assessing the potential of glucokinase activators in diabetes therapy Nature Rev. Drug Discov. 8 2009 399 416
    • (2009) Nature Rev. Drug Discov. , vol.8 , pp. 399-416
    • Matschinsky, F.M.1
  • 5
    • 70350741368 scopus 로고    scopus 로고
    • Update on mutations in glucokinase (GCK), which cause maturity-onset diabetes of the young, permanent neonatal diabetes, and hyperinsulinemic hypoglycemia
    • K.K. Osbak, K. Colclough, C. Saint-Martin, N.L. Beer, C. Bellane-Chantelot, S. Ellard, and A.L. Gloyn Update on mutations in glucokinase (GCK), which cause maturity-onset diabetes of the young, permanent neonatal diabetes, and hyperinsulinemic hypoglycemia Hum. Mutat. 30 2009 1512 1516
    • (2009) Hum. Mutat. , vol.30 , pp. 1512-1516
    • Osbak, K.K.1    Colclough, K.2    Saint-Martin, C.3    Beer, N.L.4    Bellane-Chantelot, C.5    Ellard, S.6    Gloyn, A.L.7
  • 11
    • 0032880513 scopus 로고    scopus 로고
    • Structural model of human glucokinase in complex with glucose and ATP. Implications for the mutants that cause hypo-and hyperglycemia
    • B. Manhalingam, A. Cuesta-Munoz, E.A. Davis, F.M. Matschinsky, R.W. Harrison, and I.T. Weber Structural model of human glucokinase in complex with glucose and ATP. Implications for the mutants that cause hypo-and hyperglycemia Diabetes 48 1999 1698 1705
    • (1999) Diabetes , vol.48 , pp. 1698-1705
    • Manhalingam, B.1    Cuesta-Munoz, A.2    Davis, E.A.3    Matschinsky, F.M.4    Harrison, R.W.5    Weber, I.T.6
  • 12
    • 0029034723 scopus 로고
    • Variable effects of maturity-onset-diabetes-of-youth (MODY)-associated glucokinase mutations on substrate interactions and stability of the enzyme
    • Y. Liang, P. Kesavan, L.Q. Wang, K. Niswender, Y. Tanizawa, M.A. Permutt, M.A. Magnuson, and F.M. Matschinsky Variable effects of maturity-onset- diabetes-of-youth (MODY)-associated glucokinase mutations on substrate interactions and stability of the enzyme Biochem. J. 309 1995 167 173
    • (1995) Biochem. J. , vol.309 , pp. 167-173
    • Liang, Y.1    Kesavan, P.2    Wang, L.Q.3    Niswender, K.4    Tanizawa, Y.5    Permutt, M.A.6    Magnuson, M.A.7    Matschinsky, F.M.8
  • 13
    • 0032875616 scopus 로고    scopus 로고
    • Mutants of glucokinase cause hypoglycaemia and hyperglycaemia syndromes and their analysis illuminates fundamental quantitative concepts of glucose homeostasis
    • E.A. Davis, A. Cuesta-Munoz, M. Raoul, C. Buettger, I. Sweet, M. Moates, M.A. Magnuson, and F.M. Matschinsky Mutants of glucokinase cause hypoglycaemia and hyperglycaemia syndromes and their analysis illuminates fundamental quantitative concepts of glucose homeostasis Diabetologia 42 1999 1175 1186
    • (1999) Diabetologia , vol.42 , pp. 1175-1186
    • Davis, E.A.1    Cuesta-Munoz, A.2    Raoul, M.3    Buettger, C.4    Sweet, I.5    Moates, M.6    Magnuson, M.A.7    Matschinsky, F.M.8
  • 17
    • 34347384781 scopus 로고    scopus 로고
    • Cell biology assessment of glucokinase mutations V62M and G72R in pancreatic β-cells: Evidence for cellular instability of catalytic activity
    • C. Arden, A. Trainer, N. de la Iglesia, K.T. Scougall, A.L. Gloyn, A.J. Lange, J.A.M. Shaw, F.M. Matschinsky, and L. Agius Cell biology assessment of glucokinase mutations V62M and G72R in pancreatic β-cells: evidence for cellular instability of catalytic activity Diabetes 56 2007 1773 1782
    • (2007) Diabetes , vol.56 , pp. 1773-1782
    • Arden, C.1    Trainer, A.2    De La Iglesia, N.3    Scougall, K.T.4    Gloyn, A.L.5    Lange, A.J.6    Shaw, J.A.M.7    Matschinsky, F.M.8    Agius, L.9
  • 18
    • 82255181834 scopus 로고    scopus 로고
    • Susceptibility of glucokinase-MODY mutants to inactivation by oxidative stress in pancreatic beta-cells
    • K.S. Cullen, F.M. Matschinsky, L. Agius, and C. Arden Susceptibility of glucokinase-MODY mutants to inactivation by oxidative stress in pancreatic beta-cells Diabetes October 25 2011 1 11
    • (2011) Diabetes , pp. 1-11
    • Cullen, K.S.1    Matschinsky, F.M.2    Agius, L.3    Arden, C.4
  • 19
    • 48149093497 scopus 로고    scopus 로고
    • Sugar binding to recombinant wild-type and mutant glucokinase monitored by kinetic measurement and tryptophan fluorescence
    • B. Zelent, S. Odili, C. Buettger, C. Shiota, M.A. Magnuson, J.M. Vanderkooi, and F.M. Matschinsky Sugar binding to recombinant wild-type and mutant glucokinase monitored by kinetic measurement and tryptophan fluorescence Biochem. J. 413 2008 269 280
    • (2008) Biochem. J. , vol.413 , pp. 269-280
    • Zelent, B.1    Odili, S.2    Buettger, C.3    Shiota, C.4    Magnuson, M.A.5    Vanderkooi, J.M.6    Matschinsky, F.M.7
  • 20
    • 42649094123 scopus 로고    scopus 로고
    • Catalytic activation of human glucokinase by substrate binding - Residue contacts involved in the binding of d-glucose to the super-open form and conformational transitions
    • J. Molnes, L. Bjorkhaug, O. Sovik, P.R. Njolstad, and T. Flatmark Catalytic activation of human glucokinase by substrate binding - residue contacts involved in the binding of d-glucose to the super-open form and conformational transitions FEBS J. 275 2008 2467 2481
    • (2008) FEBS J. , vol.275 , pp. 2467-2481
    • Molnes, J.1    Bjorkhaug, L.2    Sovik, O.3    Njolstad, P.R.4    Flatmark, T.5
  • 21
    • 72749102457 scopus 로고    scopus 로고
    • Mechanisms of protein stabilization and prevention of protein aggregation by glycerol
    • V. Vagenende, M.G.S. Yap, and B.L. Trout Mechanisms of protein stabilization and prevention of protein aggregation by glycerol Biochemistry 48 2009 11084 11096
    • (2009) Biochemistry , vol.48 , pp. 11084-11096
    • Vagenende, V.1    Yap, M.G.S.2    Trout, B.L.3
  • 22
    • 0025169812 scopus 로고
    • Observation of a kinetic slow transition in monomeric glucokinase
    • K.E. Neet, P.S. Tippett, and R.P. Keenan Observation of a kinetic slow transition in monomeric glucokinase Biochemistry 29 1990 770 777
    • (1990) Biochemistry , vol.29 , pp. 770-777
    • Neet, K.E.1    Tippett, P.S.2    Keenan, R.P.3
  • 23
    • 0025285220 scopus 로고
    • Demonstration of a slow conformational change in liver glucokinase by fluorescence spectroscopy
    • S.-X. Lin, and K.E. Neet Demonstration of a slow conformational change in liver glucokinase by fluorescence spectroscopy J. Biol. Chem. 265 1990 9670 9675
    • (1990) J. Biol. Chem. , vol.265 , pp. 9670-9675
    • Lin, S.-X.1    Neet, K.E.2
  • 24
    • 0018401599 scopus 로고
    • Slow transitions and hysteretic behavior in enzymes
    • C. Frieden Slow transitions and hysteretic behavior in enzymes Annu. Rev. Biochem. 48 1979 471 489
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 471-489
    • Frieden, C.1
  • 26
    • 0021911866 scopus 로고
    • Effect of glycerol on glucokinase activity: Loss of cooperative behavior with respect to glucose
    • D. Pollard-Knight, B.A. Connolly, A. Cornish-Bowden, and I.P. Trayer Effect of glycerol on glucokinase activity: loss of cooperative behavior with respect to glucose Arch. Biochem. Biophys. 237 1985 328 334
    • (1985) Arch. Biochem. Biophys. , vol.237 , pp. 328-334
    • Pollard-Knight, D.1    Connolly, B.A.2    Cornish-Bowden, A.3    Trayer, I.P.4
  • 27
    • 0015317386 scopus 로고
    • Rat hepatic glucokinase: Improved purification and some properties
    • S.J. Pilkis Rat hepatic glucokinase: improved purification and some properties Arch. Biochem. Biophys. 149 1972 349 360
    • (1972) Arch. Biochem. Biophys. , vol.149 , pp. 349-360
    • Pilkis, S.J.1
  • 30
    • 33750927821 scopus 로고
    • Fluorescence decay of tryptophan conformers in aqueous solutions
    • A.G. Szabo, and D.M. Rayner Fluorescence decay of tryptophan conformers in aqueous solutions J. Am. Chem. Soc. 102 1980 554 563
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 554-563
    • Szabo, A.G.1    Rayner, D.M.2
  • 31
    • 0344734168 scopus 로고    scopus 로고
    • Time-resolved and steady-state fluorescence quenching of N-acetyl-L-trytophanamide by acrylamide and iodide
    • B. Zelent, J. Kusba, I. Gryczynski, M.L. Johnson, and J.R. Lakowicz Time-resolved and steady-state fluorescence quenching of N-acetyl-L- trytophanamide by acrylamide and iodide Biophys. Chem. 73 1998 53 75
    • (1998) Biophys. Chem. , vol.73 , pp. 53-75
    • Zelent, B.1    Kusba, J.2    Gryczynski, I.3    Johnson, M.L.4    Lakowicz, J.R.5
  • 33
    • 0017288499 scopus 로고
    • Exposure of tryptophanyl residues in proteins, quantitative determination by fluorescence quenching studies
    • M.R. Eftink, and C.A. Ghiron Exposure of tryptophanyl residues in proteins, quantitative determination by fluorescence quenching studies Biochemistry 15 1976 672 680
    • (1976) Biochemistry , vol.15 , pp. 672-680
    • Eftink, M.R.1    Ghiron, C.A.2
  • 35
    • 0033649068 scopus 로고    scopus 로고
    • Linear extrapolation method of analyzing solvent denaturation curves
    • Suppl.
    • C.N. Pace, and K.L. Shaw Linear extrapolation method of analyzing solvent denaturation curves Proteins: Struct. Funct. Genet. 4 2000 1 7 Suppl.
    • (2000) Proteins: Struct. Funct. Genet. , vol.4 , pp. 1-7
    • Pace, C.N.1    Shaw, K.L.2
  • 36
    • 0024281290 scopus 로고
    • Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin
    • J.M. Sánchez-Ruiz, J.L. López-Lacomba, M. Cortijo, and P.L. Mateo Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin Biochemistry 27 1988 1648 1652
    • (1988) Biochemistry , vol.27 , pp. 1648-1652
    • Sánchez-Ruiz, J.M.1    López-Lacomba, J.L.2    Cortijo, M.3    Mateo, P.L.4
  • 37
    • 0026586591 scopus 로고
    • Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry
    • J.M. Sanchez-Ruiz Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry Biophys. J. 61 1992 921 935
    • (1992) Biophys. J. , vol.61 , pp. 921-935
    • Sanchez-Ruiz, J.M.1
  • 38
    • 1542791635 scopus 로고    scopus 로고
    • Structural basis for allosteric regulation of the monomeric allosteric enzyme human glucokinase
    • K. Kamata, M. Mitsuya, T. Nishimura, J. Eiki, and Y. Nagata Structural basis for allosteric regulation of the monomeric allosteric enzyme human glucokinase Structure 12 2004 429 438
    • (2004) Structure , vol.12 , pp. 429-438
    • Kamata, K.1    Mitsuya, M.2    Nishimura, T.3    Eiki, J.4    Nagata, Y.5
  • 39
    • 79959287490 scopus 로고    scopus 로고
    • Binding of ATP at the active site of human pancreatic glucokinase-nucleotide-induced conformational changes with possible implications for its kinetic cooperativity
    • J. Molnes, K. Teigen, I. Aukrust, L. Bjorkhaug, O. Sovik, T. Flatmark, and P.R. Njolstad Binding of ATP at the active site of human pancreatic glucokinase-nucleotide-induced conformational changes with possible implications for its kinetic cooperativity FEBS J. 278 2011 2372 2386
    • (2011) FEBS J. , vol.278 , pp. 2372-2386
    • Molnes, J.1    Teigen, K.2    Aukrust, I.3    Bjorkhaug, L.4    Sovik, O.5    Flatmark, T.6    Njolstad, P.R.7
  • 40
    • 0035028745 scopus 로고    scopus 로고
    • Mechanisms of tryptophan fluorescence shifts in proteins
    • J.T. Vivian, and P.R. Callis Mechanisms of tryptophan fluorescence shifts in proteins Biophys. J. 80 2001 2093 2109
    • (2001) Biophys. J. , vol.80 , pp. 2093-2109
    • Vivian, J.T.1    Callis, P.R.2
  • 41
    • 34848821695 scopus 로고    scopus 로고
    • Solvatochromic study of excited state dipole moments of some biologically active indoles and tryptamines
    • S. Sharma, S.K. Jain, and R.C. Rastogi Solvatochromic study of excited state dipole moments of some biologically active indoles and tryptamines Spectrochim. Acta A. Mol. Biomol. Spectrosc. 66 2007 171 176
    • (2007) Spectrochim. Acta A. Mol. Biomol. Spectrosc. , vol.66 , pp. 171-176
    • Sharma, S.1    Jain, S.K.2    Rastogi, R.C.3
  • 43
    • 0041320729 scopus 로고    scopus 로고
    • Protein in sugar and glycerol/water as examined by IR spectroscopy and by the fluorescence and phosphorescence properties of tryptophan
    • W.W. Wright, G.T. Guffanti, and J.M. Vanderkooi Protein in sugar and glycerol/water as examined by IR spectroscopy and by the fluorescence and phosphorescence properties of tryptophan Biophys. J. 85 2003 1980 1995
    • (2003) Biophys. J. , vol.85 , pp. 1980-1995
    • Wright, W.W.1    Guffanti, G.T.2    Vanderkooi, J.M.3
  • 44
    • 15544379587 scopus 로고    scopus 로고
    • Tryptophan interactions with glycerol/water and trehalose/sucrose cryosolvents: Infrared and fluorescence spectroscopy and ab initio calculations
    • J.L. Dashnau, B. Zelent, and J.M. Vanderkooi Tryptophan interactions with glycerol/water and trehalose/sucrose cryosolvents: infrared and fluorescence spectroscopy and ab initio calculations Biophys. Chem. 114 2005 71 83
    • (2005) Biophys. Chem. , vol.114 , pp. 71-83
    • Dashnau, J.L.1    Zelent, B.2    Vanderkooi, J.M.3
  • 45
    • 42449159741 scopus 로고    scopus 로고
    • Glucose modulation of glucokinase activation by small molecules
    • E.C. Raph, J. Thomson, J. Almaden, and S. Sun Glucose modulation of glucokinase activation by small molecules Biochemistry 47 2008 5028 5036
    • (2008) Biochemistry , vol.47 , pp. 5028-5036
    • Raph, E.C.1    Thomson, J.2    Almaden, J.3    Sun, S.4
  • 46
    • 64849102053 scopus 로고    scopus 로고
    • Biochemical characterization of MODY2 glucokinase variants V62M and G72R reveals reduced enzymatic activities relative to wild type
    • E.C. Ralph, and S. Sun Biochemical characterization of MODY2 glucokinase variants V62M and G72R reveals reduced enzymatic activities relative to wild type Biochemistry 48 2009 2514 2521
    • (2009) Biochemistry , vol.48 , pp. 2514-2521
    • Ralph, E.C.1    Sun, S.2
  • 47
    • 0017135383 scopus 로고
    • A note on the dual role of glucose in the protection of glucokinase against inactivation
    • S.H. Grossman A note on the dual role of glucose in the protection of glucokinase against inactivation Biochim. Biophys. Acta 452 1976 392 397
    • (1976) Biochim. Biophys. Acta , vol.452 , pp. 392-397
    • Grossman, S.H.1
  • 48
    • 33846622066 scopus 로고    scopus 로고
    • Ligand effects on protein thermodynamic stability
    • J.M. Sanchez-Ruiz Ligand effects on protein thermodynamic stability Biophys. Chem. 126 2007 43 49
    • (2007) Biophys. Chem. , vol.126 , pp. 43-49
    • Sanchez-Ruiz, J.M.1
  • 49
    • 10944261571 scopus 로고    scopus 로고
    • Liquid and ice water and glycerol/water glasses compared by infrared spectroscopy from 295 to 12 K
    • B. Zelent, N.V. Nucci, and J.M. Vanderkooi Liquid and ice water and glycerol/water glasses compared by infrared spectroscopy from 295 to 12 K J. Phys. Chem. A 108 2004 11141 11150
    • (2004) J. Phys. Chem. A , vol.108 , pp. 11141-11150
    • Zelent, B.1    Nucci, N.V.2    Vanderkooi, J.M.3
  • 50
    • 30544448347 scopus 로고    scopus 로고
    • Stereochemical aspects of aldohexopyranose hydration as studied by water-water hydrogen bond angle analysis
    • J.L. Dashnau, K.A. Sharp, and J.M. Vanderkooi Stereochemical aspects of aldohexopyranose hydration as studied by water-water hydrogen bond angle analysis J. Phys. Chem. 109 2005 24152 24159
    • (2005) J. Phys. Chem. , vol.109 , pp. 24152-24159
    • Dashnau, J.L.1    Sharp, K.A.2    Vanderkooi, J.M.3
  • 51
    • 0015402739 scopus 로고
    • Glycerol as an enzyme-stabilizing agent: Effects on aldehyde dehydrogenase
    • S.L. Bradbury, and W.B. Jakoby Glycerol as an enzyme-stabilizing agent: effects on aldehyde dehydrogenase Proc. Natl. Acad. Sci. U. S. A. 69 1972 2373 2376
    • (1972) Proc. Natl. Acad. Sci. U. S. A. , vol.69 , pp. 2373-2376
    • Bradbury, S.L.1    Jakoby, W.B.2
  • 52
    • 0018789680 scopus 로고
    • Increased thermal stability of proteins in the presence of sugars and polyols
    • J.F. Back, D. Oakenfull, and M.B. Smith Increased thermal stability of proteins in the presence of sugars and polyols Biochemistry 18 1979 5191 5196
    • (1979) Biochemistry , vol.18 , pp. 5191-5196
    • Back, J.F.1    Oakenfull, D.2    Smith, M.B.3
  • 53
    • 0019872622 scopus 로고
    • Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol-water mixtures
    • K. Gekko, and S.N. Timasheff Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures Biochemistry 18 1981 4667 4676
    • (1981) Biochemistry , vol.18 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2
  • 55
    • 0031048189 scopus 로고    scopus 로고
    • Probing protein hydration and conformational states in solution
    • C. Reid, and R.P. Rand Probing protein hydration and conformational states in solution Biophys. J. 72 1997 1022 1030
    • (1997) Biophys. J. , vol.72 , pp. 1022-1030
    • Reid, C.1    Rand, R.P.2
  • 57
    • 27744475204 scopus 로고    scopus 로고
    • Glucokinase: A monomeric enzyme with positive cooperativity. in glucokinase and glycemic disease: From basics to novel therapeutics
    • F.M. Matschinsky, M.A. Magnuson, Basel, Karger
    • A. Cornish-Bowden, and M.L. Cárdenas Glucokinase: a monomeric enzyme with positive cooperativity. In glucokinase and glycemic disease: from basics to novel therapeutics F.M. Matschinsky, M.A. Magnuson, Front Diabetes vol. 16 2004 Basel, Karger 125 134
    • (2004) Front Diabetes , vol.16 , pp. 125-134
    • Cornish-Bowden, A.1    Cárdenas, M.L.2
  • 58
    • 0022392190 scopus 로고
    • Cooperative interactions in hexokinase D ("glucokinase"). Kinetic and fluorescence studies
    • M.L. Cardenas, E. Rabajille, I.P. Trayer, and H. Niemeyer Cooperative interactions in hexokinase D ("glucokinase"). Kinetic and fluorescence studies Arch. Biol. Med. Exp. 18 1985 273 284
    • (1985) Arch. Biol. Med. Exp. , vol.18 , pp. 273-284
    • Cardenas, M.L.1    Rabajille, E.2    Trayer, I.P.3    Niemeyer, H.4
  • 60
    • 77249111728 scopus 로고    scopus 로고
    • Water in the half shell: Structure of water, focusing on angular structure and solvation
    • K.A. Sharp, and J.M. Vanderkooi Water in the half shell: structure of water, focusing on angular structure and solvation Acc. Chem. Res. 43 2010 231 239
    • (2010) Acc. Chem. Res. , vol.43 , pp. 231-239
    • Sharp, K.A.1    Vanderkooi, J.M.2
  • 61
    • 84859960841 scopus 로고    scopus 로고
    • A new hydrogen bond angle/distance potential energy surface of the quantum water dimer
    • J.N. Scott, and J.M. Vanderkooi A new hydrogen bond angle/distance potential energy surface of the quantum water dimer Water12 2 2010 14 28
    • (2010) Water12 , vol.2 , pp. 14-28
    • Scott, J.N.1    Vanderkooi, J.M.2
  • 62
    • 77957922049 scopus 로고    scopus 로고
    • Global fit analysis of glucose binding curves reveals a minimal model for kinetic cooperativity in human glucokinase
    • M. Larion, and B.G. Miller Global fit analysis of glucose binding curves reveals a minimal model for kinetic cooperativity in human glucokinase Biochemistry 49 2010 8902 8911
    • (2010) Biochemistry , vol.49 , pp. 8902-8911
    • Larion, M.1    Miller, B.G.2
  • 63
    • 77956565207 scopus 로고    scopus 로고
    • Direct evidence of conformational heterogeneity in human pancreatic glucokinase from high-resolution nuclear magnetic resonance
    • M. Larion, R.K. Salinas, L. Bruschweiler-Li, R. Bruschweiler, and B.G. Miller Direct evidence of conformational heterogeneity in human pancreatic glucokinase from high-resolution nuclear magnetic resonance Biochemistry 49 2010 7969 7971
    • (2010) Biochemistry , vol.49 , pp. 7969-7971
    • Larion, M.1    Salinas, R.K.2    Bruschweiler-Li, L.3    Bruschweiler, R.4    Miller, B.G.5
  • 64
    • 84857803612 scopus 로고    scopus 로고
    • Homotropic allosteric regulation in monomeric mammalian glucokinase
    • 10.1016/j.abb.2011.11.007
    • M. Larion, and B.G. Miller Homotropic allosteric regulation in monomeric mammalian glucokinase Arch. Biochem. Biophys. 2011 10.1016/j.abb.2011.11.007
    • (2011) Arch. Biochem. Biophys.
    • Larion, M.1    Miller, B.G.2
  • 66
    • 0025341608 scopus 로고
    • The mechanism by which liver glucokinase is inhibited by the regulatorty protein
    • A. Vanderkammen, and E. Van Schaftingen The mechanism by which liver glucokinase is inhibited by the regulatorty protein Eur. J. Biochem. 191 1990 483 489
    • (1990) Eur. J. Biochem. , vol.191 , pp. 483-489
    • Vanderkammen, A.1    Van Schaftingen, E.2
  • 68
    • 67049098985 scopus 로고    scopus 로고
    • Binding kinetics of glucose and allosteric activators reveal multiple conformational states
    • M. Antoine, J.A. Boutin, and G. Ferry Binding kinetics of glucose and allosteric activators reveal multiple conformational states Biochemistry 48 2009 5466 5482
    • (2009) Biochemistry , vol.48 , pp. 5466-5482
    • Antoine, M.1    Boutin, J.A.2    Ferry, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.