메뉴 건너뛰기




Volumn 192, Issue , 1999, Pages 303-318

Mechanisms for Cytoplasmic Organization: An Overview

Author keywords

Compartmentation; Cytoplasm; Cytoplasmic organization; Macromolecular interactions; Targeting; Trafficking

Indexed keywords

CELL ENZYME; CYTOSKELETON PROTEIN; MULTIENZYME COMPLEX;

EID: 0033991760     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0074-7696(08)60531-8     Document Type: Article
Times cited : (18)

References (70)
  • 3
    • 0030272292 scopus 로고    scopus 로고
    • Myofibril-bound muscle phosphofructokinase is less sensitive to inhibition by ATP than the free enzyme, but retains its sensitivity to stimulation by bisphosphorylated hexoses
    • Andres, V., Carreras, J., and Cusso, R. (1996). Myofibril-bound muscle phosphofructokinase is less sensitive to inhibition by ATP than the free enzyme, but retains its sensitivity to stimulation by bisphosphorylated hexoses. Int. J. Blochem. Cell Biol. 28, 1179-1184.
    • (1996) Int. J. Blochem. Cell Biol. , vol.28 , pp. 1179-1184
    • Andres, V.1    Carreras, J.2    Cusso, R.3
  • 4
    • 0014349824 scopus 로고
    • Binding of glycolytic enzymes to structure proteins of the muscle
    • Arnold, H., and Pette, D. (1968). Binding of glycolytic enzymes to structure proteins of the muscle. Eur. J. Biochem. 6,163-171.
    • (1968) Eur. J. Biochem. , vol.6 , pp. 163-171
    • Arnold, H.1    Pette, D.2
  • 6
    • 0022375108 scopus 로고
    • Is the "soluble" phase of cells structured?
    • Bhargava, P. M. (1985). Is the "soluble" phase of cells structured? BioSystems 18, 135-139.
    • (1985) BioSystems , vol.18 , pp. 135-139
    • Bhargava, P.M.1
  • 7
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • Blobel, G. (1980). Intracellular protein topogenesis. Proc. Natl. Acad. Sci U.S.A 77, 1496-1500.
    • (1980) Proc. Natl. Acad. Sci U.S.A , vol.77 , pp. 1496-1500
    • Blobel, G.1
  • 8
    • 0019814008 scopus 로고
    • Interaction of muscle glycolytic enzymes with thin filament proteins
    • Bronstein, W. W., and Knull, H. R. (1981). Interaction of muscle glycolytic enzymes with thin filament proteins. Can. J. Biochem. 59, 494-499.
    • (1981) Can. J. Biochem. , vol.59 , pp. 494-499
    • Bronstein, W.W.1    Knull, H.R.2
  • 9
    • 0022411305 scopus 로고
    • Packing volume of sedimented microtubules: Regulation and potential relationship to an intracellular matrix
    • Brown, P. A., and Berlin, R. D. (1985). Packing volume of sedimented microtubules: Regulation and potential relationship to an intracellular matrix. J. Cell. Biol. 101, 1492-1500.
    • (1985) J. Cell. Biol. , vol.101 , pp. 1492-1500
    • Brown, P.A.1    Berlin, R.D.2
  • 10
    • 0027199655 scopus 로고
    • Aldolase-tubulin interactions: Removal of tubulin C-terminals impairs interactions
    • Carr, D., and Knull, H. (1993). Aldolase-tubulin interactions: Removal of tubulin C-terminals impairs interactions. Biochem. Biophys. Res. Commun. 195, 289-293.
    • (1993) Biochem. Biophys. Res. Commun. , vol.195 , pp. 289-293
    • Carr, D.1    Knull, H.2
  • 11
    • 0021381587 scopus 로고
    • Properties and metabolism of the aqueous cytoplasm and its boundaries
    • Clegg, J. S. (1984a). Properties and metabolism of the aqueous cytoplasm and its boundaries. Am. J. Physiol. 246, R133-R151.
    • (1984) Am. J. Physiol. , vol.246
    • Clegg, J.S.1
  • 12
    • 0021159838 scopus 로고
    • Intracellular water and the cytomatrix: Some methods of study and current views
    • Clegg, J. S. (1984b). Intracellular water and the cytomatrix: Some methods of study and current views J. Cell Biol. 99, 167s-171s.
    • (1984) J. Cell Biol. , vol.99
    • Clegg, J.S.1
  • 13
    • 0026061391 scopus 로고
    • Metabolic organization and the ultrastructure of animal cells
    • Clegg, J. S. (1991). Metabolic organization and the ultrastructure of animal cells. Biochem. Soc. Trans. 19, 985-991.
    • (1991) Biochem. Soc. Trans. , vol.19 , pp. 985-991
    • Clegg, J.S.1
  • 14
    • 34447261118 scopus 로고
    • Scientific American Book, New York
    • DeDuve, C. (1984). "A Guided Tour of the Living Cell," Vol. 1, p. 17. Scientific American Book, New York.
    • (1984) A Guided Tour of the Living Cell , vol.1 , pp. 17
    • DeDuve, C.1
  • 15
    • 0025373570 scopus 로고
    • The theory of diazymes and functional coupling of pyruvate kinase and creatine kinase
    • Dillon, P. F., and dark, J. F. (1990). The theory of diazymes and functional coupling of pyruvate kinase and creatine kinase. J. Theor. Biol. 143, 275-284.
    • (1990) J. Theor. Biol. , vol.143 , pp. 275-284
    • Dillon, P.F.1    Dark, J.F.2
  • 16
    • 0026802334 scopus 로고
    • Metabolic control analysis: A survey of its theoretical and experimental development
    • Fell, D. A. (1992). Metabolic control analysis: A survey of its theoretical and experimental development. Biochem. J. 286, 313-330.
    • (1992) Biochem. J. , vol.286 , pp. 313-330
    • Fell, D.A.1
  • 17
    • 0027490576 scopus 로고
    • Formation of liquid crystals from actin filaments
    • Furukawa, R., Kundra, R., and Fechheimer, M. (1993). Formation of liquid crystals from actin filaments. Biochemistry 32, 12346-12352.
    • (1993) Biochemistry , vol.32 , pp. 12346-12352
    • Furukawa, R.1    Kundra, R.2    Fechheimer, M.3
  • 18
    • 0028482991 scopus 로고
    • Enzymes on immobilized substrate surfaces: Diffusion
    • Gaspers, P. B., Robertson, C. R., and Gast, A. P. (1994). Enzymes on immobilized substrate surfaces: Diffusion. Langmuir 10, 2699-2704.
    • (1994) Langmuir , vol.10 , pp. 2699-2704
    • Gaspers, P.B.1    Robertson, C.R.2    Gast, A.P.3
  • 19
    • 0000728710 scopus 로고
    • The cytoplasmic matrix: Its volume and surface area and the diffusion of molecules through it
    • Gershon, N. D., Porter, K. R., and Trus, B. L. (1985). The cytoplasmic matrix: Its volume and surface area and the diffusion of molecules through it. Proc. Natl. Acad. Sci. U.S.A. 82, 5030-5034.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 5030-5034
    • Gershon, N.D.1    Porter, K.R.2    Trus, B.L.3
  • 21
    • 0031128196 scopus 로고    scopus 로고
    • Differential regulation of glucose and glycogen metabolism in vascular smooth muscle by exogenous substrates
    • Hardin, C. D., and Roberts, T. M. (1997). Differential regulation of glucose and glycogen metabolism in vascular smooth muscle by exogenous substrates. J. Mol. Cell. Cardiol. 29, 1207-1216.
    • (1997) J. Mol. Cell. Cardiol. , vol.29 , pp. 1207-1216
    • Hardin, C.D.1    Roberts, T.M.2
  • 22
    • 0028363594 scopus 로고
    • Self-organization in living cells
    • Hess, B., and Mikhailov, A. (1994). Self-organization in living cells. Science 264, 223-224.
    • (1994) Science , vol.264 , pp. 223-224
    • Hess, B.1    Mikhailov, A.2
  • 23
    • 0029113793 scopus 로고
    • Microscopic self-organization in living cells: A study of time matching
    • Hess, B., and Mikhailov, A. (1995). Microscopic self-organization in living cells: A study of time matching. J. Theor. Biol. 176, 181-184.
    • (1995) J. Theor. Biol. , vol.176 , pp. 181-184
    • Hess, B.1    Mikhailov, A.2
  • 24
    • 0025138656 scopus 로고
    • Microtubule solutions display nematic liquid crystalline structure
    • Hitt, A. L., Cross, A. R., and Williams, R. C. (1990). Microtubule solutions display nematic liquid crystalline structure. J. Biol. Chem. 265, 1639-1647.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1639-1647
    • Hitt, A.L.1    Cross, A.R.2    Williams, R.C.3
  • 25
    • 0023960318 scopus 로고
    • Dynamic spatial distribution of proteins in the cell
    • Kaprelyants, A. S. (1988). Dynamic spatial distribution of proteins in the cell. Trends Biochem. Sci. 13, 43-46.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 43-46
    • Kaprelyants, A.S.1
  • 26
    • 0023669162 scopus 로고
    • Demonstration of tubulin-glycolytic enzyme interactions using a novel electrophoretic approach
    • Karkhoff-Schweizer, R., and Knull, H. R. (1987). Demonstration of tubulin-glycolytic enzyme interactions using a novel electrophoretic approach. Biochem. Biophys. Res. Commun. 146, 827-831.
    • (1987) Biochem. Biophys. Res. Commun. , vol.146 , pp. 827-831
    • Karkhoff-Schweizer, R.1    Knull, H.R.2
  • 28
    • 0008477969 scopus 로고
    • On the direction of pyridine nucleotide oxidation-reduction reactions in gluconeogenesis and lipogenesis
    • B. Chance, R. W. Estabrook, and J. R. Williamson, eds., Academic Press, New York
    • Lardy, H. A. (1965). On the direction of pyridine nucleotide oxidation-reduction reactions in gluconeogenesis and lipogenesis. In "Control of Energy Metabolism" (B. Chance, R. W. Estabrook, and J. R. Williamson, eds.), pp. 245-248. Academic Press, New York.
    • (1965) Control of Energy Metabolism , pp. 245-248
    • Lardy, H.A.1
  • 29
    • 0023375957 scopus 로고
    • Hindered diffusion of inert tracer particles in the cytoplasm of mouse 3T3 cells
    • Luby-Phelps, K., Castle, P. E., Taylor, D. L., and Lanni, F. (1987). Hindered diffusion of inert tracer particles in the cytoplasm of mouse 3T3 cells. Proc. Natl. Acad. Sci. U.S.A. 84, 4910-4913.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 4910-4913
    • Luby-Phelps, K.1    Castle, P.E.2    Taylor, D.L.3    Lanni, F.4
  • 30
    • 0023770546 scopus 로고
    • The submicroscopic properties of cytoplasm as a determinant of cellular function
    • Luby-Phelps, K., Lanni, F., and Taylor, D. L. (1988). The submicroscopic properties of cytoplasm as a determinant of cellular function. Annu. Rev. Biophys. Biophys. Chem. 17, 369-396.
    • (1988) Annu. Rev. Biophys. Biophys. Chem. , vol.17 , pp. 369-396
    • Luby-Phelps, K.1    Lanni, F.2    Taylor, D.L.3
  • 31
    • 0014518953 scopus 로고
    • Reversible adsorption of enzymes as a possible allosteric control mechanism
    • Masters, C. J., Sheedy, R. J., Winzor, D. J., and Nichol, L. W. (1969). Reversible adsorption of enzymes as a possible allosteric control mechanism. Biochem. J. 112, 806-808.
    • (1969) Biochem. J. , vol.112 , pp. 806-808
    • Masters, C.J.1    Sheedy, R.J.2    Winzor, D.J.3    Nichol, L.W.4
  • 32
    • 0026510711 scopus 로고
    • Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
    • Mattevi, A., Obmolova, G., Schulze, E., Kalk, K. H., Westphal, A. H., de Kok A., and Hol, W. G. J. (1992). Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex. Science 255, 1544-1550.
    • (1992) Science , vol.255 , pp. 1544-1550
    • Mattevi, A.1    Obmolova, G.2    Schulze, E.3    Kalk, K.H.4    Westphal, A.H.5    De Kok, A.6    Hol, W.G.J.7
  • 33
    • 0020135896 scopus 로고
    • Molecular evolution, intracellular organization, and the quinary structure of proteins
    • McConkey, E. H. (1982). Molecular evolution, intracellular organization, and the quinary structure of proteins. Proc. Natl. Acad. Sci. U.S.A 79, 3236-3240.
    • (1982) Proc. Natl. Acad. Sci. U.S.A , vol.79 , pp. 3236-3240
    • McConkey, E.H.1
  • 35
    • 0029101542 scopus 로고
    • Fluctuations in living cells and intracellular traffic
    • Mikhailov, A. and Hess, B. (1995). Fluctuations in living cells and intracellular traffic. J. Theor. Biol. 176, 181-184.
    • (1995) J. Theor. Biol. , vol.176 , pp. 181-184
    • Mikhailov, A.1    Hess, B.2
  • 36
    • 0020668187 scopus 로고
    • The effect of volume occupancy upon the thermodynamic activity of proteins: Some biochemical consequences
    • Minton, A. P. (1983). The effect of volume occupancy upon the thermodynamic activity of proteins: Some biochemical consequences. Mol. Cell. Biochem. 55, 119-140.
    • (1983) Mol. Cell. Biochem. , vol.55 , pp. 119-140
    • Minton, A.P.1
  • 37
    • 0026730739 scopus 로고
    • Confinement as a determinant of macromolecular structure and reactivity
    • Minton, A. P. (1992). Confinement as a determinant of macromolecular structure and reactivity. Biophys. J. 63, 1090-1100.
    • (1992) Biophys. J. , vol.63 , pp. 1090-1100
    • Minton, A.P.1
  • 38
    • 0026266260 scopus 로고
    • Cytoskeletal functions in membrane traffic in olarized epithelial cells
    • Nelson, W. J. (1991). Cytoskeletal functions in membrane traffic in olarized epithelial cells. Semin. Cell Biol. 2, 375-385.
    • (1991) Semin. Cell Biol. , vol.2 , pp. 375-385
    • Nelson, W.J.1
  • 39
    • 0023768225 scopus 로고
    • Old pathway-new concept: Control of glycolysis by metabolite-modulated dynamic enzyme associations
    • Ovádi, J. (1988). Old pathway-new concept: Control of glycolysis by metabolite-modulated dynamic enzyme associations. Trends Biochem. Sci. 13, 486-490.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 486-490
    • Ovádi, J.1
  • 41
    • 21144476377 scopus 로고
    • Glycolysis revisited-a funny thing happened on the way to the Krebs cycle
    • R. G. Landes, Austin, TX. Pagliaro, L. (1993). Glycolysis revisited-a funny thing happened on the way to the Krebs cycle. News Physiol. Sci. 8, 219-223.
    • (1993) News Physiol. Sci. , vol.8 , pp. 219-223
    • Landes, R.G.1    Austin, T.X.2    Pagliaro, L.3
  • 42
    • 0024077125 scopus 로고
    • Aldolase exists in both the fluid and solid phases of cytoplasm
    • erratum: ibid., p. 2463.
    • Pagliaro, L., and Taylor, D. L. (1988). Aldolase exists in both the fluid and solid phases of cytoplasm. J. Cell Biol. 107, 981-991; erratum: ibid., p. 2463.
    • (1988) J. Cell Biol. , vol.107 , pp. 981-991
    • Pagliaro, L.1    Taylor, D.L.2
  • 43
    • 0026698574 scopus 로고
    • 2-Deoxyglucose and cytochalasin D modulate aldolase mobility in living 3T3 cells
    • Pagliaro, L., and Taylor, D. L. (1992). 2-Deoxyglucose and cytochalasin D modulate aldolase mobility in living 3T3 cells. J. Cell Biol. 118, 859-863.
    • (1992) J. Cell Biol. , vol.118 , pp. 859-863
    • Pagliaro, L.1    Taylor, D.L.2
  • 44
    • 0025221771 scopus 로고
    • Molecular biology and biochemistry of pyruvate dehydrogenase complexes
    • Patel, M. S., and Roche, T. E. (1990). Molecular biology and biochemistry of pyruvate dehydrogenase complexes. FASEB J. 4, 3224-3233.
    • (1990) FASEB J. , vol.4 , pp. 3224-3233
    • Patel, M.S.1    Roche, T.E.2
  • 45
    • 0037756877 scopus 로고
    • Surface structure in the integration of cell activity
    • Peters, R. A. (1930). Surface structure in the integration of cell activity. Trans. Faraday Soc. 26, 797-809.
    • (1930) Trans. Faraday Soc. , vol.26 , pp. 797-809
    • Peters, R.A.1
  • 46
    • 0026471714 scopus 로고
    • Transport of proteins across the endoplasmic reticulum membrane
    • Rapoport, T. A. (1992). Transport of proteins across the endoplasmic reticulum membrane. Science 258, 931-936
    • (1992) Science , vol.258 , pp. 931-936
    • Rapoport, T.A.1
  • 47
    • 85012732607 scopus 로고
    • Pyruvate dehydrogenase complex
    • Reed, L. J. (1969). Pyruvate dehydrogenase complex. Curr. Top. Cell. Regul. 1, 233-251.
    • (1969) Curr. Top. Cell. Regul. , vol.1 , pp. 233-251
    • Reed, L.J.1
  • 48
    • 0022233869 scopus 로고
    • Organization of Krebs tricarboxylic acid cycle enzymes in mitochondria
    • Robinson, J. B., Jr., and Srere, P. A. (1985). Organization of Krebs tricarboxylic acid cycle enzymes in mitochondria. J. Biol. Chem. 262, 10800-10805.
    • (1985) J. Biol. Chem. , vol.262 , pp. 10800-10805
    • Robinson Jr., J.B.1    Srere, P.A.2
  • 49
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J. E. (1994). Mechanisms of intracellular protein transport. Nature (London) 372, 59-67.
    • (1994) Nature (London) , vol.372 , pp. 59-67
    • Rothman, J.E.1
  • 50
    • 0023724348 scopus 로고
    • Organization of soluble enzymes in the cell. Relay at the surface
    • Ryazanov, A. G. (1988). Organization of soluble enzymes in the cell. Relay at the surface. FEBS Lett. 237, 1-3.
    • (1988) FEBS Lett. , vol.237 , pp. 1-3
    • Ryazanov, A.G.1
  • 51
    • 0004146634 scopus 로고
    • Cambridge University Press, Cambridge, UK
    • Schródinger, E. (1944). "What Is Life?" Cambridge University Press, Cambridge, UK.
    • (1944) What Is Life?
    • Schródinger, E.1
  • 54
    • 0014209716 scopus 로고
    • Enzyme concentrations in tissues
    • Srere, P. A. (1967). Enzyme concentrations in tissues. Science 158, 936-937.
    • (1967) Science , vol.158 , pp. 936-937
    • Srere, P.A.1
  • 55
    • 48549111326 scopus 로고
    • Why are enzymes so big?
    • Srere, P. A. (1984). Why are enzymes so big? Trends Biochem. Sci. 9, 387-390.
    • (1984) Trends Biochem. Sci. , vol.9 , pp. 387-390
    • Srere, P.A.1
  • 57
    • 0022816351 scopus 로고
    • Metabolite transfer via enzyme-enzyme complexes
    • Srivastava, D. K., and Bernhard, S. A. (1986). Metabolite transfer via enzyme-enzyme complexes. Science 234, 1081-1086.
    • (1986) Science , vol.234 , pp. 1081-1086
    • Srivastava, D.K.1    Bernhard, S.A.2
  • 59
    • 0023663113 scopus 로고
    • Nuclear reassembly excludes large macromolecules
    • Swanson, J. A., and McNeil, P. L. (1987). Nuclear reassembly excludes large macromolecules. Science 238, 548-550.
    • (1987) Science , vol.238 , pp. 548-550
    • Swanson, J.A.1    McNeil, P.L.2
  • 60
    • 0027792058 scopus 로고
    • Glycolytic enzyme-tubulin interactions: Role of tubulin carboxy terminals
    • Volker, K. W., and Knull, H. R. (1993). Glycolytic enzyme-tubulin interactions: Role of tubulin carboxy terminals. J. Mol. Recognition 6, 167-177.
    • (1993) J. Mol. Recognition , vol.6 , pp. 167-177
    • Volker, K.W.1    Knull, H.R.2
  • 62
    • 0024342987 scopus 로고
    • Glycolytic enzyme interactions with tubulin and microtubules
    • Walsh, J. L., Keith, T. J., and Knull, H. R. (1989). Glycolytic enzyme interactions with tubulin and microtubules. Biochim. Biophys. Acta 999, 64-70.
    • (1989) Biochim. Biophys. Acta , vol.999 , pp. 64-70
    • Walsh, J.L.1    Keith, T.J.2    Knull, H.R.3
  • 63
    • 0017644623 scopus 로고
    • Modification of the kinetic parameters of aldolase on binding to the actin-containing filaments of skeletal muscle
    • Walsh, T. P., Clarke, F. M., and Masters, C. J. (1977). Modification of the kinetic parameters of aldolase on binding to the actin-containing filaments of skeletal muscle. Biochem. J. 165, 165-167.
    • (1977) Biochem. J. , vol.165 , pp. 165-167
    • Walsh, T.P.1    Clarke, F.M.2    Masters, C.J.3
  • 64
    • 0022827170 scopus 로고
    • Mechanism of protein translocation across the endoplasmic reticulum membrane
    • Walter, P., and Lingappa, V. R. (1986). Mechanism of protein translocation across the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 2, 499-516.
    • (1986) Annu. Rev. Cell Biol. , vol.2 , pp. 499-516
    • Walter, P.1    Lingappa, V.R.2
  • 65
    • 0029975931 scopus 로고    scopus 로고
    • The molecular nature of the F-actin binding activity of aldolase revealed with site-directed mutants
    • Wang, J., Morris, A. J., Tolan, D. R., and Pagliaro, L. (1996). The molecular nature of the F-actin binding activity of aldolase revealed with site-directed mutants. J. Biol. Chem. 271, 6861-6865.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6861-6865
    • Wang, J.1    Morris, A.J.2    Tolan, D.R.3    Pagliaro, L.4
  • 66
    • 0031574256 scopus 로고    scopus 로고
    • Metabolic compartmentation in living cells: Structural association of aldolase
    • Wang, J., Tolan, D. R., and Pagliaro L. (1997). Metabolic compartmentation in living cells: Structural association of aldolase. Exp. Cell Res. 237, 445-451.
    • (1997) Exp. Cell Res. , vol.237 , pp. 445-451
    • Wang, J.1    Tolan, D.R.2    Pagliaro, L.3
  • 67
    • 0017900492 scopus 로고
    • Ambiquitous enzymes: Variation in intracellular distribution as a regulatory mechanism
    • Wilson, J. E. (1978). Ambiquitous enzymes: Variation in intracellular distribution as a regulatory mechanism. Trends Biochim. Sci. 3, 124-125.
    • (1978) Trends Biochim. Sci. , vol.3 , pp. 124-125
    • Wilson, J.E.1
  • 68
    • 0018899917 scopus 로고
    • Brain hexokinase, the prototype ambiquitous enzyme
    • Wilson, J. E. (1980). Brain hexokinase, the prototype ambiquitous enzyme. Curr. Top. Cell. Regul. 16, 1-54.
    • (1980) Curr. Top. Cell. Regul. , vol.16 , pp. 1-54
    • Wilson, J.E.1
  • 69
    • 0027496418 scopus 로고
    • Macromolecular crowding effects on macromolecular interactions: Some implications for genome structure and function
    • Zimmerman, S. B. (1993). Macromolecular crowding effects on macromolecular interactions: Some implications for genome structure and function. Biochem. Biophys. Acta 1216, 175-185.
    • (1993) Biochem. Biophys. Acta , vol.1216 , pp. 175-185
    • Zimmerman, S.B.1
  • 70
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical, and physiological consequences
    • Zimmerman, S. B., and Minton, A. P. (1993). Macromolecular crowding: Biochemical, biophysical, and physiological consequences. Anna. Rev. Biophys. Biomol. Struct. 22, 27-65.
    • (1993) Anna. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.