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Volumn 10, Issue 1, 2000, Pages 34-39

Implications of macromolecular crowding for protein assembly

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 0033969150     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(99)00045-7     Document Type: Review
Times cited : (579)

References (49)
  • 1
    • 0026344818 scopus 로고
    • Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of E. coli
    • Zimmerman S.B., Trach S.O. Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of E. coli. J Mol Biol. 222:1991;599-620.
    • (1991) J Mol Biol , vol.222 , pp. 599-620
    • Zimmerman, S.B.1    Trach, S.O.2
  • 2
    • 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 Biophys Biomol Struct. 22:1993;27-65.
    • (1993) Annu Rev Biophys Biomol Struct , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 3
    • 0031022118 scopus 로고    scopus 로고
    • Influence of excluded volume upon macromolecular structure and associations in 'crowded' media
    • Minton A.P. Influence of excluded volume upon macromolecular structure and associations in 'crowded' media. Curr Opin Biotechnol. 8:1997;65-69.
    • (1997) Curr Opin Biotechnol , vol.8 , pp. 65-69
    • Minton, A.P.1
  • 4
    • 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. 20:1981;2093-2120.
    • (1981) Biopolymers , vol.20 , pp. 2093-2120
    • Minton, A.P.1
  • 5
    • 0032311227 scopus 로고    scopus 로고
    • Molecular crowding: Analysis of effects of high concentrations of inert co-solutes on biochemical equilibria and rates in terms of volume exclusion
    • A concise description of thermodynamic relations and statistical/thermodynamic models for the quantitative estimation of excluded volume effects on various types of macromolecular reaction.
    • Minton A.P. Molecular crowding: analysis of effects of high concentrations of inert co-solutes on biochemical equilibria and rates in terms of volume exclusion. Methods Enzymol. 295:1998;127-149. A concise description of thermodynamic relations and statistical/thermodynamic models for the quantitative estimation of excluded volume effects on various types of macromolecular reaction.
    • (1998) Methods Enzymol , vol.295 , pp. 127-149
    • Minton, A.P.1
  • 6
    • 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 USA. 85:1988;2984-2988.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2984-2988
    • Muramatsu, N.1    Minton, A.P.2
  • 7
    • 0027293090 scopus 로고
    • Macromolecular diffusion in crowded solutions
    • Han J., Herzfeld J. Macromolecular diffusion in crowded solutions. Biophys J. 65:1993;1155-1161.
    • (1993) Biophys J , vol.65 , pp. 1155-1161
    • Han, J.1    Herzfeld, J.2
  • 8
    • 0032846363 scopus 로고    scopus 로고
    • Folding and binding: The biological consequences of physical principles
    • Dobson C.M., Ptitsyn O.B. Folding and binding: the biological consequences of physical principles. Curr Opin Struct Biol. 9:1999;89-91.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 89-91
    • Dobson, C.M.1    Ptitsyn, O.B.2
  • 9
    • 0031923551 scopus 로고    scopus 로고
    • Protein self-organization in vitro and in vivo: Partitioning between physical biochemistry and cell biology
    • Jaenicke R. Protein self-organization in vitro and in vivo: partitioning between physical biochemistry and cell biology. Biol Chem. 379:1998;237-243.
    • (1998) Biol Chem , vol.379 , pp. 237-243
    • Jaenicke, R.1
  • 11
    • 0000146709 scopus 로고
    • Kinetic evidence for protein clustering at a surface
    • Ramsden J.J., Bachmanova G.I., Archakov A.I. Kinetic evidence for protein clustering at a surface. Phys Rev E. 50:1994;5072-5076.
    • (1994) Phys Rev e , vol.50 , pp. 5072-5076
    • Ramsden, J.J.1    Bachmanova, G.I.2    Archakov, A.I.3
  • 12
    • 0029841451 scopus 로고    scopus 로고
    • Structure within eukaryotic cytoplasm and its relationship to glycolytic metabolism
    • Knull H., Minton A.P. Structure within eukaryotic cytoplasm and its relationship to glycolytic metabolism. Cell Biochem Funct. 14:1996;237-248.
    • (1996) Cell Biochem Funct , vol.14 , pp. 237-248
    • Knull, H.1    Minton, A.P.2
  • 15
    • 0028923789 scopus 로고
    • Confinement as a determinant of macromolecular structure and reactivity. II. Effects of weakly attractive interactions between confined macrosolutes and confining structures
    • Minton A.P. Confinement as a determinant of macromolecular structure and reactivity. II. Effects of weakly attractive interactions between confined macrosolutes and confining structures. Biophys J. 68:1995;1311-1322.
    • (1995) Biophys J , vol.68 , pp. 1311-1322
    • Minton, A.P.1
  • 16
    • 0034039755 scopus 로고    scopus 로고
    • Effect of a concentrated "inert" macromolecular cosolute on the stability of a globular protein with respect to denaturation by heat and by chaotropes: A statistical-thermodynamic model
    • Minton A.P. Effect of a concentrated "inert" macromolecular cosolute on the stability of a globular protein with respect to denaturation by heat and by chaotropes: a statistical-thermodynamic model. Biophys J. 78:2000;101-109.
    • (2000) Biophys J , vol.78 , pp. 101-109
    • Minton, A.P.1
  • 17
    • 0020828094 scopus 로고
    • The influence of polyethylene glycol 6000 on the properties of skeletal-muscle actin
    • Tellam R.L., Sculley M.J., Nichol L.W., Wills P.R. The influence of polyethylene glycol 6000 on the properties of skeletal-muscle actin. Biochem J. 213:1983;651-659.
    • (1983) Biochem J , vol.213 , pp. 651-659
    • Tellam, R.L.1    Sculley, M.J.2    Nichol, L.W.3    Wills, P.R.4
  • 19
    • 0033039815 scopus 로고    scopus 로고
    • Folding and unfolding of a giant duplex-DNA in a mixed solution with polycations, polyanions and crowding neutral polymers
    • Kidoaki S., Yoshikawa K. Folding and unfolding of a giant duplex-DNA in a mixed solution with polycations, polyanions and crowding neutral polymers. Biophys Chem. 76:1999;133-143.
    • (1999) Biophys Chem , vol.76 , pp. 133-143
    • Kidoaki, S.1    Yoshikawa, K.2
  • 20
    • 0028177243 scopus 로고
    • Enhancement of self-association of human spectrin by polyethylene glycol
    • Cole N., Ralston G.B. Enhancement of self-association of human spectrin by polyethylene glycol. Int J Biochem. 26:1994;799-804.
    • (1994) Int J Biochem , vol.26 , pp. 799-804
    • Cole, N.1    Ralston, G.B.2
  • 21
    • 0028809986 scopus 로고
    • Effects of dextran on the self-association of human spectrin
    • Lindner R., Ralston G. Effects of dextran on the self-association of human spectrin. Biophys Chem. 57:1995;15-25.
    • (1995) Biophys Chem , vol.57 , pp. 15-25
    • Lindner, R.1    Ralston, G.2
  • 22
    • 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. 38:1999;9379-9388.
    • (1999) Biochemistry , vol.38 , pp. 9379-9388
    • Rivas, G.1    Fernandez, J.A.2    Minton, A.P.3
  • 23
    • 0024277329 scopus 로고
    • Heteromerous interactions among glycolytic enzymes and of glycolytic enzymes with F-actin: Effects of polyethylene glycol
    • Walsh J.L., Knull H.R. Heteromerous interactions among glycolytic enzymes and of glycolytic enzymes with F-actin: effects of polyethylene glycol. Biochim Biophys Acta. 952:1988;83-91.
    • (1988) Biochim Biophys Acta , vol.952 , pp. 83-91
    • Walsh, J.L.1    Knull, H.R.2
  • 24
    • 0024342987 scopus 로고
    • Glycolytic enzyme interactions with tubulin and microtubules
    • Walsh J.L., Keith T.J., Knull H.R. Glycolytic enzyme interactions with tubulin and microtubules. Biochim Biophys Acta. 999:1989;64-70.
    • (1989) Biochim Biophys Acta , vol.999 , pp. 64-70
    • Walsh, J.L.1    Keith, T.J.2    Knull, H.R.3
  • 25
    • 0031030690 scopus 로고    scopus 로고
    • The effect of macromolecular crowding on chaperonin-mediated protein folding
    • Martin J., Hartl F.U. The effect of macromolecular crowding on chaperonin-mediated protein folding. Proc Natl Acad Sci USA. 94:1997;1107-1112.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1107-1112
    • Martin, J.1    Hartl, F.U.2
  • 26
    • 0031239894 scopus 로고    scopus 로고
    • Molecular chaperones: Avoiding the crowd
    • Ellis R.J. Molecular chaperones: avoiding the crowd. Curr Biol. 7:1997;R531-R533.
    • (1997) Curr Biol , vol.7
    • Ellis, R.J.1
  • 27
    • 0025276708 scopus 로고
    • Sickle cell hemoglobin polymerization
    • Eaton W.A., Hofrichter J. Sickle cell hemoglobin polymerization. Adv Protein Chem. 40:1990;63-279.
    • (1990) Adv Protein Chem , vol.40 , pp. 63-279
    • Eaton, W.A.1    Hofrichter, J.2
  • 28
    • 0020123666 scopus 로고
    • Actin polymerization and its regulation by proteins from nonmuscle cells
    • Korn E.D. Actin polymerization and its regulation by proteins from nonmuscle cells. Physiol Rev. 12:1982;672-737.
    • (1982) Physiol Rev , vol.12 , pp. 672-737
    • Korn, E.D.1
  • 29
    • 0020655262 scopus 로고
    • Mechanisms of assembly and disassembly of microtubules
    • Correia J.J., Williams R.C. Mechanisms of assembly and disassembly of microtubules. Annu Rev Biophys Bioeng. 12:1983;211-235.
    • (1983) Annu Rev Biophys Bioeng , vol.12 , pp. 211-235
    • Correia, J.J.1    Williams, R.C.2
  • 30
    • 78651138927 scopus 로고
    • The interaction between polysaccharides and other macromolecules. The solubility of proteins in the presence of dextran
    • Laurent T.C. The interaction between polysaccharides and other macromolecules. The solubility of proteins in the presence of dextran. Biochem J. 89:1963;253-257.
    • (1963) Biochem J , vol.89 , pp. 253-257
    • Laurent, T.C.1
  • 31
    • 0018646920 scopus 로고
    • The effect of non-aggregating proteins upon the gelation of sickle cell hemoglobin: Model calculations and data analysis
    • Ross P.D., Minton A.P. The effect of non-aggregating proteins upon the gelation of sickle cell hemoglobin: model calculations and data analysis. Biochem Biophys Res Commun. 88:1979;1308-1314.
    • (1979) Biochem Biophys Res Commun , vol.88 , pp. 1308-1314
    • Ross, P.D.1    Minton, A.P.2
  • 32
    • 0027235856 scopus 로고
    • Crowding-induced organization of cytoskeletal elements: I. Spontaneous demixing of cytosolic proteins and model filaments to form filament bundles
    • Madden T.L., Herzfeld J. Crowding-induced organization of cytoskeletal elements: I. Spontaneous demixing of cytosolic proteins and model filaments to form filament bundles. Biophys J. 65:1993;1147-1154.
    • (1993) Biophys J , vol.65 , pp. 1147-1154
    • Madden, T.L.1    Herzfeld, J.2
  • 33
    • 0018098584 scopus 로고
    • Sickle hemoglobin gelation: Reaction order and critical nucleus size
    • Behe M., Englander S.W. Sickle hemoglobin gelation: reaction order and critical nucleus size. Biophys J. 23:1978;129-145.
    • (1978) Biophys J , vol.23 , pp. 129-145
    • Behe, M.1    Englander, S.W.2
  • 34
    • 0022993466 scopus 로고
    • Elongation of actin filaments is a diffusion-limited reaction at the barbed end and is accelerated by inert macromolecules
    • Drenckhahn D., Pollard T.D. Elongation of actin filaments is a diffusion-limited reaction at the barbed end and is accelerated by inert macromolecules. J Biol Chem. 261:1986;12754-12758.
    • (1986) J Biol Chem , vol.261 , pp. 12754-12758
    • Drenckhahn, D.1    Pollard, T.D.2
  • 35
    • 0030981013 scopus 로고    scopus 로고
    • Macromolecular crowding: Effects on actin polymerization
    • Lindner R.A., Ralston G.B. Macromolecular crowding: effects on actin polymerization. Biophys Chem. 66:1997;57-66.
    • (1997) Biophys Chem , vol.66 , pp. 57-66
    • Lindner, R.A.1    Ralston, G.B.2
  • 36
    • 0018114175 scopus 로고
    • Microtubule formation by pure brain tubulin in vitro. The influence of dextran and polyethylene glycol
    • Herzog W., Weber K. Microtubule formation by pure brain tubulin in vitro. The influence of dextran and polyethylene glycol. Eur J Biochem. 91:1978;249-254.
    • (1978) Eur J Biochem , vol.91 , pp. 249-254
    • Herzog, W.1    Weber, K.2
  • 37
    • 0021925129 scopus 로고
    • Acceleration of fibrin gel formation by unrelated proteins
    • Wilf J., Gladner J.A., Minton A.P. Acceleration of fibrin gel formation by unrelated proteins. Thromb Res. 37:1985;681-688.
    • (1985) Thromb Res , vol.37 , pp. 681-688
    • Wilf, J.1    Gladner, J.A.2    Minton, A.P.3
  • 38
    • 0020435643 scopus 로고
    • Nonspecific stabilization of stress-susceptible proteins by stress-resistant proteins: A model for the biological role of heat shock proteins
    • Minton K.W., Karmin P., Hahn G.M., Minton A.P. Nonspecific stabilization of stress-susceptible proteins by stress-resistant proteins: a model for the biological role of heat shock proteins. Proc Natl Acad Sci USA. 79:1982;7107-7111.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 7107-7111
    • Minton, K.W.1    Karmin, P.2    Hahn, G.M.3    Minton, A.P.4
  • 39
    • 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. 18:1999;6927-6933.
    • (1999) EMBO J , vol.18 , pp. 6927-6933
    • Van Den Berg, B.1    Ellis, R.J.2    Dobson, C.M.3
  • 40
    • 0033621165 scopus 로고    scopus 로고
    • Amyloid diseases: Abnormal protein aggregation in neurodegeneration
    • Koo E.H., Lansbury P.T., Kelly J.W. Amyloid diseases: abnormal protein aggregation in neurodegeneration. Proc Natl Acad Sci USA. 96:1999;9989-9990.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9989-9990
    • Koo, E.H.1    Lansbury, P.T.2    Kelly, J.W.3
  • 41
    • 0033616682 scopus 로고    scopus 로고
    • Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease
    • Lansbury P.T. Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease. Proc Natl Acad Sci USA. 96:1999;3342-3344.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3342-3344
    • Lansbury, P.T.1
  • 42
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem Sci. 24:1999;329-332.
    • (1999) Trends Biochem Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 43
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper J.D., Lansbury P.T. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu Rev Biochem. 66:1997;385-407.
    • (1997) Annu Rev Biochem , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury, P.T.2
  • 46
    • 0002229936 scopus 로고
    • Influence of macromolecular crowding on intracellular association reactions: Possible role in volume regulation
    • K. Strange. Boca Raton: CRC Press
    • Minton A.P. Influence of macromolecular crowding on intracellular association reactions: possible role in volume regulation. Strange K. Cellular and Molecular Physiology of Cell Volume Regulation. 1994;181-190 CRC Press, Boca Raton.
    • (1994) Cellular and Molecular Physiology of Cell Volume Regulation , pp. 181-190
    • Minton, A.P.1
  • 47
    • 0018357987 scopus 로고
    • Content of water-soluble and total proteins in the aging human brain
    • Naber D., Korte U., Krack K. Content of water-soluble and total proteins in the aging human brain. Exp Gerontol. 14:1979;59-63.
    • (1979) Exp Gerontol , vol.14 , pp. 59-63
    • Naber, D.1    Korte, U.2    Krack, K.3
  • 48
    • 0019513425 scopus 로고
    • Alterations in total content and solubility characteristics of proteins in rat brain and liver during aging and centrophenoxine treatment
    • Zs-Nagy I., Nagy K., Zs-Nagy V., Kalmar A., Nagy E. Alterations in total content and solubility characteristics of proteins in rat brain and liver during aging and centrophenoxine treatment. Exp Gerontol. 16:1981;229-240.
    • (1981) Exp Gerontol , vol.16 , pp. 229-240
    • Zs-Nagy, I.1    Nagy, K.2    Zs-Nagy, V.3    Kalmar, A.4    Nagy, E.5
  • 49
    • 0020347231 scopus 로고
    • Protein and water contents of aging brain
    • suppl 5
    • Zs-Nagy I., Nagy K., Lustyik G. Protein and water contents of aging brain. Exp Brain Res. 1982;118-122. suppl 5.
    • (1982) Exp Brain Res , pp. 118-122
    • Zs-Nagy, I.1    Nagy, K.2    Lustyik, G.3


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