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Volumn 17, Issue 5, 2004, Pages 488-496

Large changes in cytoplasmic biopolymer concentration with osmolality indicate that macromolecular crowding may regulate protein-DNA interactions and growth rate in osmotically stressed Escherichia coli K-12

Author keywords

Crowding; Escherichia coli; Glycine betaine; Osmoprotection; Volume regulation

Indexed keywords

BACTERIAL DNA; BETAINE; BIOPOLYMER; DNA BINDING PROTEIN; ESCHERICHIA COLI PROTEIN;

EID: 4544363330     PISSN: 09523499     EISSN: None     Source Type: Journal    
DOI: 10.1002/jmr.695     Document Type: Conference Paper
Times cited : (51)

References (59)
  • 1
    • 0032716841 scopus 로고    scopus 로고
    • Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid
    • Azam TA, Iwata A, Nishimura A, Ueda S, Ishihama A. 1999. Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid. J. Bacteriol. 181: 6361-6370.
    • (1999) J. Bacteriol. , vol.181 , pp. 6361-6370
    • Azam, T.A.1    Iwata, A.2    Nishimura, A.3    Ueda, S.4    Ishihama, A.5
  • 2
    • 0028876607 scopus 로고
    • Growth and buoyant density of Escherichia coli at very low osmolarities
    • Baldwin WW, Myer R, Kung T, Anderson E, Koch AL. 1995. Growth and buoyant density of Escherichia coli at very low osmolarities. J. Bacteriol. 177: 235-237.
    • (1995) J. Bacteriol. , vol.177 , pp. 235-237
    • Baldwin, W.W.1    Myer, R.2    Kung, T.3    Anderson, E.4    Koch, A.L.5
  • 3
    • 0033118214 scopus 로고    scopus 로고
    • Managing hypoosmotic stress: Aquaporins and mechanosensitive channels in Escherichia coli
    • Booth IR, Louis P. 1999. Managing hypoosmotic stress: aquaporins and mechanosensitive channels in Escherichia coli. Curr. Opin. Microbiol. 2: 166-169.
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 166-169
    • Booth, I.R.1    Louis, P.2
  • 4
    • 0038760038 scopus 로고    scopus 로고
    • Free RNA polymerase and modeling global transcription in Escherichia coli
    • Bremer H, Dennis P, Ehrenberg M. 2003. Free RNA polymerase and modeling global transcription in Escherichia coli. Biochimie 85: 597-609.
    • (2003) Biochimie , vol.85 , pp. 597-609
    • Bremer, H.1    Dennis, P.2    Ehrenberg, M.3
  • 6
    • 0034028431 scopus 로고    scopus 로고
    • Biophysical characterization of changes in amounts and activity of Escherichia coli cell and compartment water and turgor pressure in response to osmotic stress
    • Cayley DS, Guttman HJ, Record MT Jr. 2000. Biophysical characterization of changes in amounts and activity of Escherichia coli cell and compartment water and turgor pressure in response to osmotic stress. Biophys J 78: 1748-1764.
    • (2000) Biophys. J. , vol.78 , pp. 1748-1764
    • Cayley, D.S.1    Guttman, H.J.2    Record Jr., M.T.3
  • 7
    • 0026559541 scopus 로고
    • Origins of the osmoprotective properties of betaine and proline in Escherichia coli K-12
    • Cayley S, Lewis BA, Record MT Jr. 1992. Origins of the osmoprotective properties of betaine and proline in Escherichia coli K-12. J. Bacteriol. 174: 1586-1595.
    • (1992) J. Bacteriol. , vol.174 , pp. 1586-1595
    • Cayley, S.1    Lewis, B.A.2    Record Jr., M.T.3
  • 8
    • 0242286667 scopus 로고    scopus 로고
    • Roles of cytoplasmic osmolytes, water, and crowding in the response of Escherichia coli to osmotic stress: Biophysical basis of osmoprotection by glycine betaine
    • Cayley S, Record MT Jr. 2003. Roles of cytoplasmic osmolytes, water, and crowding in the response of Escherichia coli to osmotic stress: biophysical basis of osmoprotection by glycine betaine. Biochemistry 42: 12596-12609.
    • (2003) Biochemistry , vol.42 , pp. 12596-12609
    • Cayley, S.1    Record Jr., M.T.2
  • 9
    • 0026409841 scopus 로고
    • Characterization of the cytoplasm of Escherichia coli-K-12 as a function of external osmolarity-implications for protein DNA interactions in vivo
    • Cayley S, Lewis BA, Guttman HJ, Record MTJ. 1991. Characterization of the cytoplasm of Escherichia coli-K-12 as a function of external osmolarity-implications for protein DNA interactions in vivo. J. of Mol. Biol. 222: 281-300.
    • (1991) J. of Mol. Biol. , vol.222 , pp. 281-300
    • Cayley, S.1    Lewis, B.A.2    Guttman, H.J.3    Record, M.T.J.4
  • 10
    • 0034681955 scopus 로고    scopus 로고
    • Vapor pressure osmometry studies of osmolyte-protein interactions: Implications for the action of osmoprotectants in vivo and for the interpretation of 'osmotic stress' experiments in vitro
    • Courtenay ES, Capp MW, Anderson CF, Record MT Jr. 2000. Vapor pressure osmometry studies of osmolyte-protein interactions: implications for the action of osmoprotectants in vivo and for the interpretation of 'osmotic stress' experiments in vitro. Biochemistry-Us 39: 4455-4471.
    • (2000) Biochemistry-Us , vol.39 , pp. 4455-4471
    • Courtenay, E.S.1    Capp, M.W.2    Anderson, C.F.3    Record Jr., M.T.4
  • 11
    • 0035176391 scopus 로고    scopus 로고
    • Thermodynamics of interactions of urea and guanidinium salts with protein surface: Relationship between solute effects on protein processes and changes in water-accessible surface area
    • Courtenay ES, Capp MW, Record MT Jr. 2001. Thermodynamics of interactions of urea and guanidinium salts with protein surface: relationship between solute effects on protein processes and changes in water-accessible surface area. Protein Sci. 10: 2485-2497.
    • (2001) Protein Sci. , vol.10 , pp. 2485-2497
    • Courtenay, E.S.1    Capp, M.W.2    Record Jr., M.T.3
  • 12
    • 0037389630 scopus 로고    scopus 로고
    • A soluble protein is immobile in dormant spores of Bacillus subtilis but is mobile in germinated spores: Implications for spore dormancy
    • Cowan AE, Koppel DE, Setlow B, Setlow P. 2003. A soluble protein is immobile in dormant spores of Bacillus subtilis but is mobile in germinated spores: implications for spore dormancy. Proc. Natl. Acad. Sci. USA 100: 4209-4214.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4209-4214
    • Cowan, A.E.1    Koppel, D.E.2    Setlow, B.3    Setlow, P.4
  • 13
    • 0037457916 scopus 로고    scopus 로고
    • Osmosensor ProP of Escherichia coli responds to the concentration, chemistry, and molecular size of osmolytes in the proteoliposome lumen
    • Culham DE, Henderson J, Crane RA, Wood JM. 2003. Osmosensor ProP of Escherichia coli responds to the concentration, chemistry, and molecular size of osmolytes in the proteoliposome lumen. Biochemistry 42: 410-420.
    • (2003) Biochemistry , vol.42 , pp. 410-420
    • Culham, D.E.1    Henderson, J.2    Crane, R.A.3    Wood, J.M.4
  • 15
    • 0035092041 scopus 로고    scopus 로고
    • Molecular confinement influences protein structure and enhances thermal protein stability
    • Eggers DK, Valentine JS. 2001. Molecular confinement influences protein structure and enhances thermal protein stability. Protein Sci. 10: 250-261.
    • (2001) Protein Sci. , vol.10 , pp. 250-261
    • Eggers, D.K.1    Valentine, J.S.2
  • 16
    • 0031239894 scopus 로고    scopus 로고
    • Molecular chaperones: Avoiding the crowd
    • Ellis RJ. 1997. Molecular chaperones: avoiding the crowd. Curr. Biol. 7: R531-R533.
    • (1997) Curr. Biol. , vol.7
    • Ellis, R.J.1
  • 17
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • Ellis RJ. 2001. Macromolecular crowding: obvious but underappreciated. Trends Biochem. Sci. 26: 597-604.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 18
    • 0041822089 scopus 로고    scopus 로고
    • Cell biology: Join the crowd
    • Ellis RJ, Minton AP. 2003. Cell biology: join the crowd. Nature 425: 27-28.
    • (2003) Nature , vol.425 , pp. 27-28
    • Ellis, R.J.1    Minton, A.P.2
  • 20
    • 0020184671 scopus 로고
    • How crowded is the cytoplasm?
    • Fulton AB. 1982. How crowded is the cytoplasm? Cell 30: 345-347.
    • (1982) Cell , vol.30 , pp. 345-347
    • Fulton, A.B.1
  • 21
    • 0028360796 scopus 로고
    • Macromolecular crowding and confinement in cells exposed to hypertonicity
    • Garner MM, Burg MB. 1994. Macromolecular crowding and confinement in cells exposed to hypertonicity. Am. J. Physiol. 266: C877-C892.
    • (1994) Am. J. Physiol. , vol.266
    • Garner, M.M.1    Burg, M.B.2
  • 22
    • 0034814860 scopus 로고    scopus 로고
    • Quantitative protein stability measurement in vivo
    • Ghaemmaghami S, Oas TG. 2001. Quantitative protein stability measurement in vivo. Nat. Struct. Biol. 8: 879-882.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 879-882
    • Ghaemmaghami, S.1    Oas, T.G.2
  • 23
    • 0037418563 scopus 로고    scopus 로고
    • Metabolic buffering exerted by macromolecular crowding on DNA-DNA interactions: Origin and physiological significance
    • Goobes R, Kahana N, Cohen O, Minsky A. 2003. Metabolic buffering exerted by macromolecular crowding on DNA-DNA interactions: origin and physiological significance. Biochemistry-Us 42: 2431-2440.
    • (2003) Biochemistry-Us , vol.42 , pp. 2431-2440
    • Goobes, R.1    Kahana, N.2    Cohen, O.3    Minsky, A.4
  • 24
    • 0037438344 scopus 로고    scopus 로고
    • Prospects of electron cryotomography to visualize macromolecular complexes inside cellular compartments: Implications of crowding
    • Grunewald K, Medalia O, Gross A, Steven AC, Baumeister W. 2003. Prospects of electron cryotomography to visualize macromolecular complexes inside cellular compartments: implications of crowding. Biophys. Chem. 100: 577-591.
    • (2003) Biophys. Chem. , vol.100 , pp. 577-591
    • Grunewald, K.1    Medalia, O.2    Gross, A.3    Steven, A.C.4    Baumeister, W.5
  • 25
    • 0026498015 scopus 로고
    • Thermodynamic stoichiometries of participation of water, cations and anions in specific and non-specific binding of lac repressor to DNA. Possible thermodynamic origins of the 'glutamate effect' on protein-DNA interactions
    • Ha JH, Capp MW, Hohenwalter MD, Baskerville M, Record MT Jr. 1992. Thermodynamic stoichiometries of participation of water, cations and anions in specific and non-specific binding of lac repressor to DNA. Possible thermodynamic origins of the 'glutamate effect' on protein-DNA interactions. J. Mol. Biol. 228: 252-264.
    • (1992) J. Mol. Biol. , vol.228 , pp. 252-264
    • Ha, J.H.1    Capp, M.W.2    Hohenwalter, M.D.3    Baskerville, M.4    Record Jr., M.T.5
  • 26
    • 0041931122 scopus 로고    scopus 로고
    • Macromolecular crowding: Qualitative and semiquantitative successes, quantitative challenges. Biochim
    • Hall D, Minton AP. 2003. Macromolecular crowding: qualitative and semiquantitative successes, quantitative challenges. Biochim. Biophys. Acta 1649: 127-139.
    • (2003) Biophys. Acta , vol.1649 , pp. 127-139
    • Hall, D.1    Minton, A.P.2
  • 27
    • 0027293090 scopus 로고
    • Macromolecular diffusion in crowded solutions
    • Han J, Herzfeld J. 1993. Macromolecular diffusion in crowded solutions. Biophys. J. 65: 1155-1161.
    • (1993) Biophys. J. , vol.65 , pp. 1155-1161
    • Han, J.1    Herzfeld, J.2
  • 28
    • 0037040878 scopus 로고    scopus 로고
    • Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II
    • Hatters DM, Minton AP, Howlett GJ. 2002. Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II. J. Biol. Chem. 277: 7824-7830.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7824-7830
    • Hatters, D.M.1    Minton, A.P.2    Howlett, G.J.3
  • 29
    • 2042475515 scopus 로고
    • Nonspecific DNA binding of genome-regulating proteins as a biological control mechanism: Measurement of DNA-bound Escherichia coli lac repressor in vivo
    • Kao-Huang Y, Revzin A, Butler AP, O'Conner P, Noble DW, von Hippel PH. 1977. Nonspecific DNA binding of genome-regulating proteins as a biological control mechanism: measurement of DNA-bound Escherichia coli lac repressor in vivo. Proc. Natl. Acad. Sci. USA 74: 4228-4232.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 4228-4232
    • Kao-Huang, Y.1    Revzin, A.2    Butler, A.P.3    O'Conner, P.4    Noble, D.W.5    Von Hippel, P.H.6
  • 30
  • 32
    • 0027510369 scopus 로고
    • In vivo thermodynamic analysis of repression with and without looping in lac constructs. Estimates of free and local lac repressor concentrations and of physical properties of a region of supercoiled plasmid DNA in vivo
    • Law SM, Bellomy GR, Schlax PJ, Record MT Jr. 1993. In vivo thermodynamic analysis of repression with and without looping in lac constructs. Estimates of free and local lac repressor concentrations and of physical properties of a region of supercoiled plasmid DNA in vivo. J. Mol. Biol. 230: 161-173.
    • (1993) J. Mol. Biol. , vol.230 , pp. 161-173
    • Law, S.M.1    Bellomy, G.R.2    Schlax, P.J.3    Record Jr., M.T.4
  • 33
    • 0002277822 scopus 로고
    • Molecular basis of the biological compatibility of nature's osmolytes
    • Giles V, Gilles-Baillien M (eds). Springer: Berlin
    • Low PS. 1985. Molecular basis of the biological compatibility of nature's osmolytes. In Transport Processes, lonos and Osmoregulation, Giles V, Gilles-Baillien M (eds). Springer: Berlin; 469-477.
    • (1985) Transport Processes, Lonos and Osmoregulation , pp. 469-477
    • Low, P.S.1
  • 34
    • 0025371320 scopus 로고
    • Involvement of gammaglutamyl peptides in osmoadaptation of Escherichia coli
    • McLaggan D, Logan TM, Lynn DG, Epstein W. 1990. Involvement of gammaglutamyl peptides in osmoadaptation of Escherichia coli. J. Bacteriol. 172: 3631-3636.
    • (1990) J. Bacteriol. , vol.172 , pp. 3631-3636
    • McLaggan, D.1    Logan, T.M.2    Lynn, D.G.3    Epstein, W.4
  • 35
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • Minton AP 2001. The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J. Biol. Chem. 276: 10577-10580.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10577-10580
    • Minton, A.P.1
  • 36
    • 0017069426 scopus 로고
    • The tentative identification in Escherichia coli of a multienzyme complex with glycolytic activity
    • Mowbray J, Moses V. 1976. The tentative identification in Escherichia coli of a multienzyme complex with glycolytic activity. Eur. J. Biochem. 66: 25-36.
    • (1976) Eur. J. Biochem. , vol.66 , pp. 25-36
    • Mowbray, J.1    Moses, V.2
  • 38
    • 0027948550 scopus 로고
    • Desiccation tolerance of prokaryotes
    • Potts M. 1994. Desiccation tolerance of prokaryotes. Microbiol. Rev. 58: 755-805.
    • (1994) Microbiol. Rev. , vol.58 , pp. 755-805
    • Potts, M.1
  • 39
    • 0032079008 scopus 로고    scopus 로고
    • Biophysical compensation mechanisms buffering E. coli protein-nucleic acid interactions against changing environments
    • Record MT Jr, Courtenay ES, Cayley S, Guttman HJ. 1998. Biophysical compensation mechanisms buffering E. coli protein-nucleic acid interactions against changing environments. Trends Biochem. Sci. 23: 190-194.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 190-194
    • Record Jr., M.T.1    Courtenay, E.S.2    Cayley, S.3    Guttman, H.J.4
  • 40
    • 0028894966 scopus 로고
    • Using macromolecular crowding agents to identify weak interactions within DNA replication complexes
    • Reddy MK, Weitzel SE, Daube SS, Jarvis TC, von Hippel PH. 1995. Using macromolecular crowding agents to identify weak interactions within DNA replication complexes. Meth. Enzymol. 262: 466-476.
    • (1995) Meth. Enzymol. , vol.262 , pp. 466-476
    • Reddy, M.K.1    Weitzel, S.E.2    Daube, S.S.3    Jarvis, T.C.4    Von Hippel, P.H.5
  • 41
    • 0023664450 scopus 로고
    • Variability of the intracellular ionic environment of Escherichia coli - Differences between in vitro and in vivo effects of ion concentrations on protein-DNA interactions and gene expression
    • Richey B, Cayley DS, Mossing MC, Kolka C, Anderson CF, Farrar TC, Record MT Jr. 1987. Variability of the intracellular ionic environment of Escherichia coli - differences between in vitro and in vivo effects of ion concentrations on protein-DNA interactions and gene expression. J. Biol. Chem. 262: 7157-7164.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7157-7164
    • Richey, B.1    Cayley, D.S.2    Mossing, M.C.3    Kolka, C.4    Anderson, C.F.5    Farrar, T.C.6    Record Jr., M.T.7
  • 42
    • 0032167971 scopus 로고    scopus 로고
    • Implications of macromolecular crowding for signal transduction and metabolite channeling
    • Rohwer JM, Postma PW, Kholodenko BN, Westerhoff HV. 1998. Implications of macromolecular crowding for signal transduction and metabolite channeling. Proc. Natl Acad. Sci. USA 95: 10547-10552.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10547-10552
    • Rohwer, J.M.1    Postma, P.W.2    Kholodenko, B.N.3    Westerhoff, H.V.4
  • 43
    • 0041931024 scopus 로고    scopus 로고
    • Impact of osmotic stress on volume regulation, cytoplasmic solute composition and lysine production in corynebacterium glutamicum MH20-22B
    • Ronsch H, Kramer R, Morback S. 2003. Impact of osmotic stress on volume regulation, cytoplasmic solute composition and lysine production in corynebacterium glutamicum MH20-22B. J. Biotechnology 104: 87-97.
    • (2003) J. Biotechnology , vol.104 , pp. 87-97
    • Ronsch, H.1    Kramer, R.2    Morback, S.3
  • 44
    • 0037470574 scopus 로고    scopus 로고
    • Effect of dextran on protein stability and conformation attributed to macromolecular crowding
    • Sasahara K, McPhie P, Minton AP. 2003. Effect of dextran on protein stability and conformation attributed to macromolecular crowding. J. Mol. Biol. 326: 1227-1237.
    • (2003) J. Mol. Biol. , vol.326 , pp. 1227-1237
    • Sasahara, K.1    McPhie, P.2    Minton, A.P.3
  • 45
    • 0037177250 scopus 로고    scopus 로고
    • Molecular crowding accelerates fibrillization of alpha-synuclein: Could an increase in the cytoplasmic protein concentration induce Parkinson's disease?
    • Shtilerman MD, Ding TT, Lansbury PT Jr. 2002. Molecular crowding accelerates fibrillization of alpha-synuclein: could an increase in the cytoplasmic protein concentration induce Parkinson's disease? Biochemistry 41: 3855-3860.
    • (2002) Biochemistry , vol.41 , pp. 3855-3860
    • Shtilerman, M.D.1    Ding, T.T.2    Lansbury Jr., P.T.3
  • 46
    • 0030032002 scopus 로고    scopus 로고
    • Changes in intracellular composition in response to hyperosmotic stress of NaCl, sucrose or glutamic acid in Brevibacterium lactofermentum and Corynebacterium glutamicum
    • Skjerdal OT, Sletta H, Flenstad SG, Josefsen KD, Levine DW, Ellingsen TE. 1996. Changes in intracellular composition in response to hyperosmotic stress of NaCl, sucrose or glutamic acid in Brevibacterium lactofermentum and Corynebacterium glutamicum. Applied Microbiology and Biotechnology 44: 635-642.
    • (1996) Applied Microbiology and Biotechnology , vol.44 , pp. 635-642
    • Skjerdal, O.T.1    Sletta, H.2    Flenstad, S.G.3    Josefsen, K.D.4    Levine, D.W.5    Ellingsen, T.E.6
  • 47
    • 0036239754 scopus 로고    scopus 로고
    • Bacterial osmoadaptation: The role of osmolytes in bacterial stress and virulence
    • Sleator RD, Hill C. 2001. Bacterial osmoadaptation: the role of osmolytes in bacterial stress and virulence. FEMS Mic. Rev. 26: 49-71.
    • (2001) FEMS Mic. Rev. , vol.26 , pp. 49-71
    • Sleator, R.D.1    Hill, C.2
  • 48
    • 0023061429 scopus 로고
    • Complexes of sequential metabolic enzymes
    • Srere PA. 1987. Complexes of sequential metabolic enzymes. A. Rev. Biochem. 56: 89-124.
    • (1987) A. Rev. Biochem. , vol.56 , pp. 89-124
    • Srere, P.A.1
  • 49
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • Timasheff SN. 1998. Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Adv. Protein Chem. 51: 355-432.
    • (1998) Adv. Protein Chem. , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 50
    • 0037181497 scopus 로고    scopus 로고
    • Accelerated alpha-synuclein fibrillation in crowded milieu
    • Uversky VN, Cooper E, Bower KS, Li J, Fink AL. 2002. Accelerated alpha-synuclein fibrillation in crowded milieu. FEBS Lett. 515: 99-103.
    • (2002) FEBS Lett. , vol.515 , pp. 99-103
    • Uversky, V.N.1    Cooper, E.2    Bower, K.S.3    Li, J.4    Fink, A.L.5
  • 51
    • 0037383369 scopus 로고    scopus 로고
    • Dimerization of the quorum sensing regulator RhIR: Development of a method using EGFP fluorescence anisotropy
    • Ventre I, Ledgham F, Prima V, Lazdunski A, Foglino M, Sturgis JN. 2003. Dimerization of the quorum sensing regulator RhIR: development of a method using EGFP fluorescence anisotropy. Mol. Microbiol. 48: 187-198.
    • (2003) Mol. Microbiol. , vol.48 , pp. 187-198
    • Ventre, I.1    Ledgham, F.2    Prima, V.3    Lazdunski, A.4    Foglino, M.5    Sturgis, J.N.6
  • 52
    • 0036164351 scopus 로고    scopus 로고
    • Solute and macromolecule diffusion in cellular aqueous compartments
    • Verkman AS. 2002. Solute and macromolecule diffusion in cellular aqueous compartments. Trends Biochem. Sci. 27: 27-33.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 27-33
    • Verkman, A.S.1
  • 54
    • 0033014719 scopus 로고    scopus 로고
    • Osmosensing by bacteria: Signals and membrane-based sensors
    • Wood JM. 1999. Osmosensing by bacteria: signals and membrane-based sensors. Microbiol. Mol. Biol. Rev. 63: 230-262.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 230-262
    • Wood, J.M.1
  • 56
    • 0000225096 scopus 로고
    • Macromolecular crowding increases binding of DNA polymerase to DNA: An adaptive effect
    • Zimmerman SB, Harrison B. 1987. Macromolecular crowding increases binding of DNA polymerase to DNA: an adaptive effect. Proc. Natl. Acad. Sci. USA 84: 1871-1875.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1871-1875
    • Zimmerman, S.B.1    Harrison, B.2
  • 57
    • 0027318513 scopus 로고
    • Macromolecular crowding - Biochemical, biophysical, and physiological consequences
    • Zimmerman SB, Minton AP. 1993. Macromolecular crowding - Biochemical, biophysical, and physiological consequences. A. Rev. Biophys. Biomol. Struct. 22: 27-65.
    • (1993) A. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 58
    • 0030605841 scopus 로고    scopus 로고
    • Macromolecular crowding and the mandatory condensation of DNA in bacteria
    • Zimmerman SB, Murphy LD. 1996. Macromolecular crowding and the mandatory condensation of DNA in bacteria. FEBS Lett. 390: 245-248.
    • (1996) FEBS Lett. , vol.390 , pp. 245-248
    • Zimmerman, S.B.1    Murphy, L.D.2
  • 59
    • 0026344818 scopus 로고
    • Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli
    • Zimmerman SB, Trach SO. 1991. Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli. J. Mol. Biol. 222: 599-620.
    • (1991) J. Mol. Biol. , vol.222 , pp. 599-620
    • Zimmerman, S.B.1    Trach, S.O.2


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