메뉴 건너뛰기




Volumn 30, Issue 1, 1999, Pages 35-70

Establishment of order in the flow of genetic information in cells

Author keywords

Autoregulation; Dynamic physiological state; Functional integrity; Gene regulation

Indexed keywords

BOVINAE;

EID: 0032609344     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02737884     Document Type: Article
Times cited : (1)

References (67)
  • 2
    • 0020474084 scopus 로고
    • Variety in the level of gene control in eukaryotic cells
    • Darnell, J. E. (1982) Variety in the level of gene control in eukaryotic cells. Nature 297, 365-371.
    • (1982) Nature , vol.297 , pp. 365-371
    • Darnell, J.E.1
  • 3
    • 0019878975 scopus 로고
    • Gene expression in eukaryotes
    • Brown, D. D. (1981) Gene expression in eukaryotes. Science 211, 667-674.
    • (1981) Science , vol.211 , pp. 667-674
    • Brown, D.D.1
  • 5
    • 0026323912 scopus 로고
    • Analysis of equilibrium and kinetic measurements to determine thermodynamic origins of stability and specificity and mechanism of formation of site-specific complexes between proteins and helical DNA
    • Record, T. M., Ha, J-H., Fisher, M. A. (1991) Analysis of equilibrium and kinetic measurements to determine thermodynamic origins of stability and specificity and mechanism of formation of site-specific complexes between proteins and helical DNA. Methods Enzymol. 208, 291-343.
    • (1991) Methods Enzymol. , vol.208 , pp. 291-343
    • Record, T.M.1    Ha, J.-H.2    Fisher, M.A.3
  • 6
    • 0004194541 scopus 로고
    • Cell Press, Cambridge, MA
    • Ptashne, M. (1987) Genetic Switch, Cell Press, Cambridge, MA.
    • (1987) Genetic Switch
    • Ptashne, M.1
  • 7
    • 3042953934 scopus 로고
    • Bioenergetics
    • Elsevier, Amsterdam, The Netherlands
    • Ernster, L. (1984) Bioenergetics (New Comprehensive Biochemistry, vol. 9), Elsevier, Amsterdam, The Netherlands.
    • (1984) New Comprehensive Biochemistry , vol.9
    • Ernster, L.1
  • 10
    • 0028076124 scopus 로고
    • Complexities of metabolic regulation
    • Srere, P. (1994) Complexities of metabolic regulation. Trends Biochem. Sci. 19, 519,520.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 519
    • Srere, P.1
  • 11
    • 0004146634 scopus 로고
    • Cambridge University Press, Cambridge, UK
    • Schrodinger, E. (1944) What is Life. Cambridge University Press, Cambridge, UK.
    • (1944) What Is Life
    • Schrodinger, E.1
  • 12
    • 20444433942 scopus 로고
    • The study of energy levels in biochemistry
    • Szent-Gyorgyi, A. (1941) The study of energy levels in biochemistry. Nature 148, 157-159.
    • (1941) Nature , vol.148 , pp. 157-159
    • Szent-Gyorgyi, A.1
  • 15
    • 0141950921 scopus 로고
    • From quantum chemistry to quantum biochemistry
    • (Kasha, M. and Pullman, B. eds.), Academic Press, NY
    • Pullman, A. and Pullman, B. (1962) From quantum chemistry to quantum biochemistry, in Horizons in Biochemistry (Kasha, M. and Pullman, B. eds.), Academic Press, NY, pp. 553-582.
    • (1962) Horizons in Biochemistry , pp. 553-582
    • Pullman, A.1    Pullman, B.2
  • 16
    • 3042986069 scopus 로고
    • Quantum chemistry in molecular biology
    • (Kasha, M. and Pullman, B., eds.), Academic, New York
    • Kasha, M. (1962) Quantum chemistry in molecular biology, in Horizons in Biochemistry (Kasha, M. and Pullman, B., eds.), Academic, New York, pp. 583-599.
    • (1962) Horizons in Biochemistry , pp. 583-599
    • Kasha, M.1
  • 17
    • 0023277545 scopus 로고
    • Single step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. and Sacchi, N. (1987) Single step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 18
    • 0025050735 scopus 로고
    • Oxygen tension regulates the expression of the platelet-derived growth factor-B chain gene in human endothelial cells
    • Kourembanas, S., Hannan, R. L., and Faller, D. V. (1990) Oxygen tension regulates the expression of the platelet-derived growth factor-B chain gene in human endothelial cells. J. Clin. Invest. 86, 670-674.
    • (1990) J. Clin. Invest. , vol.86 , pp. 670-674
    • Kourembanas, S.1    Hannan, R.L.2    Faller, D.V.3
  • 19
    • 0026002686 scopus 로고
    • Hypoxia induces endothelin gene expression and secretion in cultured human endothelium
    • Kourembanas, S., Marsden, P. A., McQuillan, L. P., and Faller, D. V. (1991) Hypoxia induces endothelin gene expression and secretion in cultured human endothelium. J. Invest. Clin. 88, 1054-1057.
    • (1991) J. Invest. Clin. , vol.88 , pp. 1054-1057
    • Kourembanas, S.1    Marsden, P.A.2    McQuillan, L.P.3    Faller, D.V.4
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0018413113 scopus 로고
    • Ethidium dimer: A new reagent for the fluorimetric determination of nucleic acids
    • Markovits, J., Rooques, B. P., and LePecq, J-B. (1979) Ethidium dimer: A new reagent for the fluorimetric determination of nucleic acids. Anal Biochem. 94, 259-264.
    • (1979) Anal Biochem. , vol.94 , pp. 259-264
    • Markovits, J.1    Rooques, B.P.2    Lepecq, J.-B.3
  • 22
    • 0008169184 scopus 로고
    • Adenosine-5′-triphosphate and creatine phosphate determination with luciferase
    • (Bergmeyer, H.-U., ed.), Academic, New York
    • Strehler, B. L. (1963) Adenosine-5′-triphosphate and creatine phosphate determination with luciferase, in Methods of Enzymatic Analysis, (Bergmeyer, H.-U., ed.), Academic, New York, pp. 559-572.
    • (1963) Methods of Enzymatic Analysis , pp. 559-572
    • Strehler, B.L.1
  • 23
    • 0023651349 scopus 로고
    • A thousand and one protein kinases
    • Hunter, T. (1987) A thousand and one protein kinases. Cell 50, 823-829.
    • (1987) Cell , vol.50 , pp. 823-829
    • Hunter, T.1
  • 24
    • 0029020282 scopus 로고
    • The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S. K. and Hunter, T. (1995) The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9, 576-596.
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 25
    • 0026324811 scopus 로고
    • Staurosporine inhibits the soluble and membrane-bound protein tyrosine kinases of human neutrophils
    • Badway, J. A., Erickson, R. W., and Curnutte, J. T. (1991) Staurosporine inhibits the soluble and membrane-bound protein tyrosine kinases of human neutrophils. Biochem. Biophys. Res. Comm. 178, 423-429.
    • (1991) Biochem. Biophys. Res. Comm. , vol.178 , pp. 423-429
    • Badway, J.A.1    Erickson, R.W.2    Curnutte, J.T.3
  • 27
    • 0024996471 scopus 로고
    • Staurosporine inhibits a tyrosine protein kinase in human hepatoma cell membranes
    • Fallon, R. J. (1990) Staurosporine inhibits a tyrosine protein kinase in human hepatoma cell membranes. Biochem. Biophys. Res. Comm. 170, 1191-1196.
    • (1990) Biochem. Biophys. Res. Comm. , vol.170 , pp. 1191-1196
    • Fallon, R.J.1
  • 28
  • 31
    • 0026504147 scopus 로고
    • Social controls on cell survival and cell death
    • Raff, M. C. (1992) Social controls on cell survival and cell death. Nature 356, 397-400.
    • (1992) Nature , vol.356 , pp. 397-400
    • Raff, M.C.1
  • 32
    • 0019225636 scopus 로고
    • Cell death: The significance of apoptosis
    • Wyllie, A. H. (1980) Cell death: the significance of apoptosis. Int. Rev. Cytol. 68, 251-306.
    • (1980) Int. Rev. Cytol. , vol.68 , pp. 251-306
    • Wyllie, A.H.1
  • 33
    • 0030980797 scopus 로고    scopus 로고
    • Regulation of c-jun gene expression in endothelial cells by the protein kinase inhibitor staurosporine
    • Bandyopadhyay, R. S. and Faller, D. V. (1997) Regulation of c-jun gene expression in endothelial cells by the protein kinase inhibitor staurosporine. Endothelium 5, 95-105.
    • (1997) Endothelium , vol.5 , pp. 95-105
    • Bandyopadhyay, R.S.1    Faller, D.V.2
  • 34
    • 0343828468 scopus 로고
    • Energy metabolism
    • (Ruch, T. C. and Patton, H. D., eds.), Saunders, New York
    • Brown, A. C. and Brengelmann, G. (1966) Energy metabolism, in Physiology and Biophysics (Ruch, T. C. and Patton, H. D., eds.), Saunders, New York, pp. 1030-1049.
    • (1966) Physiology and Biophysics , pp. 1030-1049
    • Brown, A.C.1    Brengelmann, G.2
  • 36
    • 0026466703 scopus 로고
    • Intracellular pH changes induced by hypoxia and anoxia in isolated sheep heart Purkinje fibres
    • Bright, C. M., and Ellis, D. (1992) Intracellular pH changes induced by hypoxia and anoxia in isolated sheep heart Purkinje fibres. Exp. Physiol. 77, 165-175.
    • (1992) Exp. Physiol. , vol.77 , pp. 165-175
    • Bright, C.M.1    Ellis, D.2
  • 37
    • 0019497941 scopus 로고
    • Frequency encoded biochemical regulation is more accurate than amplitude dependent control
    • Rapp, P. E., Mees, A. I., and Sparrow, C. T. (1981) Frequency encoded biochemical regulation is more accurate than amplitude dependent control. J. Theor. Biol. 90, 531-544.
    • (1981) J. Theor. Biol. , vol.90 , pp. 531-544
    • Rapp, P.E.1    Mees, A.I.2    Sparrow, C.T.3
  • 41
    • 0020698476 scopus 로고
    • Dynamics of proteins: Elements and function
    • Karplus, M. and McCammon, J. A. (1983) Dynamics of proteins: elements and function. Ann. Rev. Biochem. 53, 263-300.
    • (1983) Ann. Rev. Biochem. , vol.53 , pp. 263-300
    • Karplus, M.1    McCammon, J.A.2
  • 42
    • 0026600019 scopus 로고
    • Chromatin dynamics and the modulation of genetic activity
    • Hansen, J. C. and Ausio, J. (1992) Chromatin dynamics and the modulation of genetic activity. Trends Biochem. Sci. 17, 187-191.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 187-191
    • Hansen, J.C.1    Ausio, J.2
  • 43
    • 0017820499 scopus 로고
    • Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: The roles of ion association or release, screening, and ion effects on water activity
    • Record, T. M., Anderson, C. F., Lohman, T. M. (1978) Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity. Q. Rev. Biophys. 11, 103-178.
    • (1978) Q. Rev. Biophys. , vol.11 , pp. 103-178
    • Record, T.M.1    Anderson, C.F.2    Lohman, T.M.3
  • 44
    • 0022332472 scopus 로고
    • Ions as regulators of protein-nucleic acid interactions in vitro and in vivo
    • Record, T. M., Anderson, C. F., Mills, P., Mossing, M., and Roe, J-H. (1985) Ions as regulators of protein-nucleic acid interactions in vitro and in vivo. Adv. Biophys. 20, 109-135.
    • (1985) Adv. Biophys. , vol.20 , pp. 109-135
    • Record, T.M.1    Anderson, C.F.2    Mills, P.3    Mossing, M.4    Roe, J.-H.5
  • 45
    • 0026433721 scopus 로고
    • Molecular self-assembly and nanochemistry: A chemical strategy for the synthesis of nanostructures
    • Whitesides, G. M., Mathias, J. P., and Seto, C. T. (1991) Molecular self-assembly and nanochemistry: a chemical strategy for the synthesis of nanostructures. Science 254, 1312-1319.
    • (1991) Science , vol.254 , pp. 1312-1319
    • Whitesides, G.M.1    Mathias, J.P.2    Seto, C.T.3
  • 46
    • 77956800551 scopus 로고
    • The geometry of molecules: Basic principles and nomenclatures
    • (Tamm, C. ed.), Elsevier Biomedical, Amsterdam, The Netherlands
    • Testa B. (1982) The geometry of molecules: Basic principles and nomenclatures, in Steriochemistry (Tamm, C. ed.), Elsevier Biomedical, Amsterdam, The Netherlands, pp. 1-47.
    • (1982) Steriochemistry , pp. 1-47
    • Testa, B.1
  • 47
    • 0015101072 scopus 로고
    • Biological order, structure and instabilities
    • Prigogine, I. and Nicolis, G. (1971) Biological order, structure and instabilities. Q. Rev. Biophys. 4, 107-148.
    • (1971) Q. Rev. Biophys. , vol.4 , pp. 107-148
    • Prigogine, I.1    Nicolis, G.2
  • 49
    • 0024373683 scopus 로고
    • Eukaryotic transcriptional regulatory proteins
    • Johnson, P. F. and McKnight, S. L. (1989) Eukaryotic transcriptional regulatory proteins. Ann. Rev. Biochem. 58, 799-839.
    • (1989) Ann. Rev. Biochem. , vol.58 , pp. 799-839
    • Johnson, P.F.1    McKnight, S.L.2
  • 50
    • 0027197725 scopus 로고
    • General initiation factors for RNA polymerase II
    • Conaway, R. C. and Conaway, J. W. (1993) General initiation factors for RNA polymerase II. Ann. Rev. Biochem. 62, 161-190.
    • (1993) Ann. Rev. Biochem. , vol.62 , pp. 161-190
    • Conaway, R.C.1    Conaway, J.W.2
  • 51
    • 0026682657 scopus 로고
    • Transcription factors: Structural families and principles of DNA recognition
    • Pabo, C. O. and Sauer, R. T. (1992) Transcription factors: Structural families and principles of DNA recognition. Ann. Rev. Biochem. 61, 1053-1095.
    • (1992) Ann. Rev. Biochem. , vol.61 , pp. 1053-1095
    • Pabo, C.O.1    Sauer, R.T.2
  • 52
    • 0025052069 scopus 로고
    • How do transcription factors work?
    • Berk, A. J. and Schmidt, M. C. (1990) How do transcription factors work? Genes Development 4, 151-155.
    • (1990) Genes Development , vol.4 , pp. 151-155
    • Berk, A.J.1    Schmidt, M.C.2
  • 53
    • 0023288548 scopus 로고
    • Splicing of messenger RNA precursors
    • Sharp, P. A. (1987) Splicing of messenger RNA precursors. Science 235, 766-771.
    • (1987) Science , vol.235 , pp. 766-771
    • Sharp, P.A.1
  • 54
    • 0021891865 scopus 로고
    • Eukaryotic protein synthesis
    • Moldave, K. (1985) Eukaryotic protein synthesis. Ann. Rev. Biochem. 54, 1109-1149.
    • (1985) Ann. Rev. Biochem. , vol.54 , pp. 1109-1149
    • Moldave, K.1
  • 55
    • 0023919931 scopus 로고
    • Ribonucleoprotein particles in cellular processes
    • Dreyfuss, G., Philipson, L., and Mattaj, I. W. (1988) Ribonucleoprotein particles in cellular processes. J. Cell Biol. 106, 1419-1425.
    • (1988) J. Cell Biol. , vol.106 , pp. 1419-1425
    • Dreyfuss, G.1    Philipson, L.2    Mattaj, I.W.3
  • 56
    • 0025199669 scopus 로고
    • Mechanisms of mRNA decay
    • Brawerman, G. (1990) Mechanisms of mRNA decay. Trends Biotech. 8, 171-174.
    • (1990) Trends Biotech. , vol.8 , pp. 171-174
    • Brawerman, G.1
  • 57
    • 0025342519 scopus 로고
    • A nuclease activity associated with mammalian messenger RNA in its native state: Possible basis for selectivity in mRNA decay
    • Bandyopadhyay, R., Coutts, M., Krowczynska, A., and Brawerman, G. (1990) A nuclease activity associated with mammalian messenger RNA in its native state: Possible basis for selectivity in mRNA decay. Mol. Cell. Biol. 10, 2060-2069.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2060-2069
    • Bandyopadhyay, R.1    Coutts, M.2    Krowczynska, A.3    Brawerman, G.4
  • 58
    • 73049167504 scopus 로고
    • Teleonomic mechanisms in cellular metabolism, growth, and differentiation
    • Monod, J. and Jacob, F. (1961) Teleonomic mechanisms in cellular metabolism, growth, and differentiation. Cold Spring Harbor Symp. Q. Biol. 26, 380-401.
    • (1961) Cold Spring Harbor Symp. Q. Biol. , vol.26 , pp. 380-401
    • Monod, J.1    Jacob, F.2
  • 59
    • 0342669395 scopus 로고
    • Kinetic and thermodynamic aspects of biological and biochemical control mechanisms
    • (Kun, E. and Grisolia, S., eds.), Wiley-Interscience, New York
    • Walter, C. F. (1970) Kinetic and thermodynamic aspects of biological and biochemical control mechanisms, in Biochemical Regulatory Mechanisms in Eukaryotic Cells (Kun, E. and Grisolia, S., eds.), Wiley-Interscience, New York, pp. 255-489.
    • (1970) Biochemical Regulatory Mechanisms in Eukaryotic Cells , pp. 255-489
    • Walter, C.F.1
  • 60
    • 0024276523 scopus 로고
    • The jun protooncogene is positively autoregulated by its product, jun/AP1
    • Angel, P., Hattori, K., Smeal, T., and Karin, M. (1988) The jun protooncogene is positively autoregulated by its product, jun/AP1. Cell 55, 875-885.
    • (1988) Cell , vol.55 , pp. 875-885
    • Angel, P.1    Hattori, K.2    Smeal, T.3    Karin, M.4
  • 61
    • 0028088580 scopus 로고
    • Rhythmic transcription and autoregulatory loops: Winding up the biological clock
    • Sassone-Corsi, P. (1994) Rhythmic transcription and autoregulatory loops: winding up the biological clock. Cell 78, 361-364.
    • (1994) Cell , vol.78 , pp. 361-364
    • Sassone-Corsi, P.1
  • 62
    • 0025044560 scopus 로고
    • Feed back of the Drosophila period gene product on circadian cycling of its messenger RNA levels
    • Hardin, P. E., Hall, J. C., and Rosbash, M. (1990) Feed back of the Drosophila period gene product on circadian cycling of its messenger RNA levels. Nature 343, 536-540.
    • (1990) Nature , vol.343 , pp. 536-540
    • Hardin, P.E.1    Hall, J.C.2    Rosbash, M.3
  • 63
    • 0028258994 scopus 로고
    • Negative feedback defining a circadian clock: Autoregulation of the clock gene frequency
    • Aronson, B. D., Johnson, K. A., Loros, J. J., and Dunlop, J. C. (1994) Negative feedback defining a circadian clock: autoregulation of the clock gene frequency. Science 263, 1578-1584.
    • (1994) Science , vol.263 , pp. 1578-1584
    • Aronson, B.D.1    Johnson, K.A.2    Loros, J.J.3    Dunlop, J.C.4
  • 64
    • 0025825895 scopus 로고
    • Modular structure of transcription factors: Implications for gene regulation
    • Frankel, A. D. and Kim, P. S. (1991) Modular structure of transcription factors: Implications for gene regulation. Cell 65, 717-719.
    • (1991) Cell , vol.65 , pp. 717-719
    • Frankel, A.D.1    Kim, P.S.2
  • 66
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J., and Changeux, J. P. (1965) On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12, 88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.