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Volumn 17, Issue 11, 2010, Pages 1426-1435

Effect of mixed crowding on refolding of human muscle creatine kinase

Author keywords

Dextran; Folding; Human muscle creatine kinase; Macromolecule crowding; Mixed crowding; Osmolytes; Sucrose

Indexed keywords


EID: 78650676114     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/0929866511009011426     Document Type: Article
Times cited : (8)

References (33)
  • 1
    • 33750806263 scopus 로고    scopus 로고
    • Mixed macromolecular crowding accelerates the refolding of rabbit muscle creatine kinase: Implications for protein folding in physiological environments
    • Du, F.; Zhou, Z.; Mo, Z. Y.; Shi, J. Z.; Chen, J.; Liang, Y. Mixed macromolecular crowding accelerates the refolding of rabbit muscle creatine kinase: Implications for protein folding in physiological environments. J. Mol. Biol., 2006, 364(3), 469-482.
    • (2006) J. Mol. Biol. , vol.364 , Issue.3 , pp. 469-482
    • Du, F.1    Zhou, Z.2    Mo, Z.Y.3    Shi, J.Z.4    Chen, J.5    Liang, Y.6
  • 3
    • 0041822089 scopus 로고    scopus 로고
    • Cell biology: Join the crowd
    • Ellis, R. J.; Minton, A. P. Cell biology: join the crowd. Nature, 2003, 425(6953), 27-28.
    • (2003) Nature , vol.425 , Issue.6953 , pp. 27-28
    • Ellis, R.J.1    Minton, A.P.2
  • 4
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • Ellis, R. J. Macromolecular crowding: obvious but underappreciated. Trends Biochem. Sci., 2001b, 26(10), 597-604.
    • (2001) Trends Biochem. Sci. , vol.26 , Issue.10 , pp. 597-604
    • Ellis, R.J.1
  • 5
    • 42249107315 scopus 로고    scopus 로고
    • Effects of solution crowding on actin polymerization reveal the energetic basis for nu-cleotide-dependent filament stability
    • Frederick, K. B.; Sept, D.; De La Cruz, E. M. Effects of solution crowding on actin polymerization reveal the energetic basis for nu-cleotide-dependent filament stability. J. Mol. Biol., 2008, 378(3), 540-550.
    • (2008) J. Mol. Biol. , vol.378 , Issue.3 , pp. 540-550
    • Frederick, K.B.1    Sept, D.2    De La Cruz, E.M.3
  • 6
    • 0035253217 scopus 로고    scopus 로고
    • Macromolecular crowding: An important but neglected aspect of the intracellular environment
    • Ellis, R. J. Macromolecular crowding: an important but neglected aspect of the intracellular environment. Curr. Opin. Struct. Biol., 2001a, 77(1), 114-119.
    • (2001) Curr. Opin. Struct. Biol. , vol.77 , Issue.1 , pp. 114-119
    • Ellis, R.J.1
  • 7
    • 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, 78(24), 6927-6933.
    • (1999) EMBO J. , vol.78 , Issue.24 , pp. 6927-6933
    • Van Den Berg, B.1    Ellis, R.J.2    Dobson, C.M.3
  • 8
    • 0035860681 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on the refolding of glucose-6-phosphate dehydrogenase and protein disulfide isomerase
    • Li, J.; Zhang, S.; Wang, C. C. Effects of macromolecular crowding on the refolding of glucose-6-phosphate dehydrogenase and protein disulfide isomerase. J. Biol. Chem., 2001, 276(37), 34396-34401.
    • (2001) J. Biol. Chem. , vol.276 , Issue.37 , pp. 34396-34401
    • Li, J.1    Zhang, S.2    Wang, C.C.3
  • 9
    • 0345602004 scopus 로고    scopus 로고
    • Effects of macromo-lecular crowding on the unfolding and the refolding of D-glyceraldehyde-3-phosophospate dehydrogenase
    • Ren, G. P.; Lin, Z.; Tsou, C. L.; Wang, C. C. Effects of macromo-lecular crowding on the unfolding and the refolding of D-glyceraldehyde-3-phosophospate dehydrogenase. J. Protein Chem., 2003, 22(5), 431-439.
    • (2003) J. Protein Chem. , vol.22 , Issue.5 , pp. 431-439
    • Ren, G.P.1    Lin, Z.2    Tsou, C.L.3    Wang, C.C.4
  • 10
    • 0035847097 scopus 로고    scopus 로고
    • Excluded volume effects on the refolding and assembly of an oligomeric protein-GroEL, a case study
    • Galan, A.; Sot, B.; Llorca, O.; Carrascosa, J. L.; Valpuesta, J. M.; Muga, A. Excluded volume effects on the refolding and assembly of an oligomeric protein-GroEL, a case study. J. Biol. Chem., 2001, 276(2), 957-964.
    • (2001) J. Biol. Chem. , vol.276 , Issue.2 , pp. 957-964
    • Galan, A.1    Sot, B.2    Llorca, O.3    Carrascosa, J.L.4    Valpuesta, J.M.5    Muga, A.6
  • 11
    • 36348979413 scopus 로고    scopus 로고
    • Effect of High Concentration of Inert Cosolutes on the Refolding of an Enzyme: Carbonic anhydrase B in sucrose and ficoll 70
    • Monterroso, B.; Minton, A. P. Effect of High Concentration of Inert Cosolutes on the Refolding of an Enzyme: carbonic anhydrase B in sucrose and ficoll 70. J. Biol. Chem., 2007, 282(46), 33452-33458.
    • (2007) J. Biol. Chem. , vol.282 , Issue.46 , pp. 33452-33458
    • Monterroso, B.1    Minton, A.P.2
  • 12
    • 0037418340 scopus 로고    scopus 로고
    • Atomic-level observation of macromolecular crowding effects: Escape of a protein from the GroEL cage
    • Elcock, A. H. Atomic-level observation of macromolecular crowding effects: escape of a protein from the GroEL cage. Proc. Natl. Acad. Sci. USA, 2003, 700(5), 2340-2344.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.700 , Issue.5 , pp. 2340-2344
    • Elcock, A.H.1
  • 13
    • 11244296161 scopus 로고    scopus 로고
    • Mixed macromo-lecular crowding accelerates the oxidative refolding of reduced, denatured lysozyme-Implications for protein folding in intracellu-lar environments
    • Zhou, B. R.; Yi, L.; Fen, D.; Zheng, Z.; Jie, C. Mixed macromo-lecular crowding accelerates the oxidative refolding of reduced, denatured lysozyme-Implications for protein folding in intracellu-lar environments. J. Biol. Chem., 2004, 279(53), 55109-55116.
    • (2004) J. Biol. Chem. , vol.279 , Issue.53 , pp. 55109-55116
    • Zhou, B.R.1    Yi, L.2    Fen, D.3    Zheng, Z.4    Jie, C.5
  • 14
    • 0036152775 scopus 로고    scopus 로고
    • Effect of osmolytes as folding aids on creatine kinase refolding pathway
    • Ou, W. B.; Park, Y. D.; Zhou, H. M. Effect of osmolytes as folding aids on creatine kinase refolding pathway. Int. J. Biochem. Cell B, 2002, 34(2), 136-147.
    • (2002) Int. J. Biochem. Cell B , vol.34 , Issue.2 , pp. 136-147
    • Ou, W.B.1    Park, Y.D.2    Zhou, H.M.3
  • 15
    • 34547590372 scopus 로고    scopus 로고
    • Effects of osmolytes on hexokinase kinetics combined with macromolecular crowding: Test of the os-molyte compatibility hypothesis towards crowded systems
    • Olsen, S. N.; H, R.; Westh, P. Effects of osmolytes on hexokinase kinetics combined with macromolecular crowding: Test of the os-molyte compatibility hypothesis towards crowded systems. Comp. Biochem. Phys. A, 2007, 148(2), 339-345.
    • (2007) Comp. Biochem. Phys. A , vol.148 , Issue.2 , pp. 339-345
    • Olsen, S.N.1    H, R.2    Westh, P.3
  • 16
    • 0035958656 scopus 로고    scopus 로고
    • The osmophobic effect: Natural selection of a thermodynamic force in protein folding
    • Bolen, D. W.; Baskakov, I. V. The osmophobic effect: Natural selection of a thermodynamic force in protein folding. J. Mol. Biol., 2001, 370(5), 955-963.
    • (2001) J. Mol. Biol. , vol.370 , Issue.5 , pp. 955-963
    • Bolen, D.W.1    Baskakov, I.V.2
  • 17
    • 51349126098 scopus 로고    scopus 로고
    • Effect of mixed macromolecular crowding agents on protein folding
    • Zhou, H. X. Effect of mixed macromolecular crowding agents on protein folding. Proteins, 2008, 72(4), 1109-1113.
    • (2008) Proteins , vol.72 , Issue.4 , pp. 1109-1113
    • Zhou, H.X.1
  • 18
    • 0019811128 scopus 로고
    • Improved radioimmunoas-say for creatine kinase isoenzymes in plasma
    • Ritter, C. S.; Mumm, S. R.; Roberts, R. Improved radioimmunoas-say for creatine kinase isoenzymes in plasma. Clin. Chem., 1981, 27(11), 1878-1887.
    • (1981) Clin. Chem. , vol.27 , Issue.11 , pp. 1878-1887
    • Ritter, C.S.1    Mumm, S.R.2    Roberts, R.3
  • 19
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 1976, 72(1-2), 248-254.
    • (1976) Anal. Biochem. , vol.72 , Issue.1-2 , pp. 248-254
    • Bradford, M.M.1
  • 20
    • 0020212384 scopus 로고
    • Conformational changes of creatine kinase during guanidine denaturation
    • Yao, Q. Z.; Hou, L. X.; Zhou, H. M.; Tsou, C. L. Conformational changes of creatine kinase during guanidine denaturation. Sci. Sin., Ser. B, 1982, 25(11), 1186-1198.
    • (1982) Sci. Sin. Ser. B , vol.25 , Issue.11 , pp. 1186-1198
    • Yao, Q.Z.1    Hou, L.X.2    Zhou, H.M.3    Tsou, C.L.4
  • 21
    • 0035052766 scopus 로고    scopus 로고
    • Aggregation of creatine kinase during refolding and chaperonin-mediated folding of creatine kinase
    • Li, S.; Bai, J.-H.; Park, Y.-D.; Zhou, H.-M. Aggregation of creatine kinase during refolding and chaperonin-mediated folding of creatine kinase. Int. J. Biochem. Cell B, 2001, 33(3), 279-286.
    • (2001) Int. J. Biochem. Cell B , vol.33 , Issue.3 , pp. 279-286
    • Li, S.1    Bai, J.-H.2    Park, Y.-D.3    Zhou, H.-M.4
  • 22
    • 0031672564 scopus 로고    scopus 로고
    • Unfolding and refolding of dimeric creatine kinase equilibrium and kinetic studies
    • Ying-Xin, F.; Jun-Mei, Z.; Chen-Lu, T.; Hiroshi, K. Unfolding and refolding of dimeric creatine kinase equilibrium and kinetic studies. Protein Sci., 1998, 7(12), 2631-2641.
    • (1998) Protein Sci. , vol.7 , Issue.12 , pp. 2631-2641
    • Ying-Xin, F.1    Jun-Mei, Z.2    Chen-Lu, T.3    Hiroshi, K.4
  • 23
    • 0022645377 scopus 로고
    • Comparison of activity and conformation changes during refolding of urea-denatured creatine kinase
    • Zhou, H. M.; Tsou, C. L. Comparison of activity and conformation changes during refolding of urea-denatured creatine kinase. BBA-Protein Struct. M., 1986, 869(1), 69-74.
    • (1986) BBA-protein Struct. M. , vol.869 , Issue.1 , pp. 69-74
    • Zhou, H.M.1    Tsou, C.L.2
  • 24
    • 0034254189 scopus 로고    scopus 로고
    • Macromo-lecular crowding perturbs protein refolding kinetics: Implications for folding inside the cell
    • van den Berg, B.; Wain, R.; Dobson, C. M.; Ellis, R. J. Macromo-lecular crowding perturbs protein refolding kinetics: implications for folding inside the cell. EMBO J., 2000, 79(15), 3870-3875.
    • (2000) EMBO J. , vol.79 , Issue.15 , pp. 3870-3875
    • Van Den Berg, B.1    Wain, R.2    Dobson, C.M.3    Ellis, R.J.4
  • 25
    • 0033199237 scopus 로고    scopus 로고
    • The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase
    • van den Berg, B.; Chung, E. W.; Robinson, C. V.; Mateo, P. L.; Dobson, C. M. The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase. EMBO J., 1999, 78(17), 4794-4803.
    • (1999) EMBO J. , vol.78 , Issue.17 , pp. 4794-4803
    • Van Den Berg, B.1    Chung, E.W.2    Robinson, C.V.3    Mateo, P.L.4    Dobson, C.M.5
  • 26
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • Minton, A. P. The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J. Biol. Chem., 2001, 276(14), 10577-10580.
    • (2001) J. Biol. Chem. , vol.276 , Issue.14 , pp. 10577-10580
    • Minton, A.P.1
  • 27
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical, and physiological consequences
    • Zimmerman, S. B.; Minton, A. P. Macromolecular crowding: biochemical, biophysical, and physiological consequences. Annu. Rev. Biophs. Biom., 1993, 22(1), 27-65.
    • (1993) Annu. Rev. Biophs. Biom. , vol.22 , Issue.1 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 28
    • 0031013887 scopus 로고    scopus 로고
    • Mechanism of the stabilization of ribonu-clease a by sorbitol: Preferential hydration is greater for the denatured than for the native protein
    • Guifu, X.; Serge, N. T. Mechanism of the stabilization of ribonu-clease a by sorbitol: Preferential hydration is greater for the denatured than for the native protein. Protein Sci., 1997, 6(1), 211-221.
    • (1997) Protein Sci. , vol.6 , Issue.1 , pp. 211-221
    • Guifu, X.1    Serge, N.T.2
  • 29
    • 0037178811 scopus 로고    scopus 로고
    • Kinetics and energetics of assembly, nucleation, and growth of aggre-gates and fibrils for an amyloidogenic protein-Insights into transition states from pressure, temperature, and co-solute studies
    • Kim, Y. S.; Randolph, T. W.; Stevens, F. J.; Carpenter, J. F. Kinetics and energetics of assembly, nucleation, and growth of aggre-gates and fibrils for an amyloidogenic protein-Insights into transition states from pressure, temperature, and co-solute studies. J. Biol. Chem., 2002, 277(30), 27240-27246.
    • (2002) J. Biol. Chem. , vol.277 , Issue.30 , pp. 27240-27246
    • Kim, Y.S.1    Randolph, T.W.2    Stevens, F.J.3    Carpenter, J.F.4
  • 30
    • 33645415019 scopus 로고    scopus 로고
    • Role of osmolytes as chemical chaperones during the refolding of aminoacylase
    • Kim, S. H.; Yan, Y. B.; Zhou, H. M. Role of osmolytes as chemical chaperones during the refolding of aminoacylase. Biochem. Cell Biol., 2006, 84(1), 30-38.
    • (2006) Biochem. Cell Biol. , vol.84 , Issue.1 , pp. 30-38
    • Kim, S.H.1    Yan, Y.B.2    Zhou, H.M.3
  • 31
    • 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, 70(1), 34-39.
    • (2000) Curr. Opin. Struct. Biol. , vol.70 , Issue.1 , pp. 34-39
    • Minton, A.P.1
  • 32
    • 29344453598 scopus 로고    scopus 로고
    • Capture of monomeric refolding intermediate of human muscle creatine kinase
    • Li, S.; Bai, J. H.; Park, Y. D.; Zhou, H. M. Capture of monomeric refolding intermediate of human muscle creatine kinase. Protein Sci., 2006, 75(1), 171-181.
    • (2006) Protein Sci. , vol.75 , Issue.1 , pp. 171-181
    • Li, S.1    Bai, J.H.2    Park, Y.D.3    Zhou, H.M.4
  • 33
    • 0037117720 scopus 로고    scopus 로고
    • Requirement for GroEL/GroES-dependent protein folding under nonpermissive conditions of macromolecular crowding
    • Martin, J. Requirement for GroEL/GroES-dependent protein folding under nonpermissive conditions of macromolecular crowding. Biochemistry-US, 2002, 47(15), 5050-5055.
    • (2002) Biochemistry-uS , vol.47 , Issue.15 , pp. 5050-5055
    • Martin, J.1


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