메뉴 건너뛰기




Volumn 1666, Issue 1-2, 2004, Pages 142-157

Membrane fluidity and its roles in the perception of environmental signals

Author keywords

Cold sensor; DNA microarray; Environment; Membrane fluidity; Membrane lipid; Osmosensor; Temperature stress

Indexed keywords

DNA; MEMBRANE LIPID; UNSATURATED FATTY ACID;

EID: 7044224838     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2004.08.002     Document Type: Review
Times cited : (724)

References (170)
  • 1
    • 0031401113 scopus 로고    scopus 로고
    • Membrane fluidity and temperature perception
    • N. Murata, and D.A. Los Membrane fluidity and temperature perception Plant Physiol. 115 1997 875 879
    • (1997) Plant Physiol. , vol.115 , pp. 875-879
    • Murata, N.1    Los, D.A.2
  • 2
    • 11144223662 scopus 로고    scopus 로고
    • Regulation of enzymatic activity and gene expression by membrane fluidity
    • D.A. Los, and N. Murata Regulation of enzymatic activity and gene expression by membrane fluidity Sci. Signal Transduct. Knowl. Environ. 2000 (http://www.stke.org/cgi/content/full/OC_sigtrans;2000/62/pe1)
    • (2000) Sci. Signal Transduct. Knowl. Environ.
    • Los, D.A.1    Murata, N.2
  • 3
    • 0027379256 scopus 로고
    • The primary signal in the biological perception of temperature: Pd-catalyzed hydrogenation of membrane lipids stimulated the expression of the desA gene in Synechocystis PCC6803
    • L. Vigh, D.A. Los, I. Horvath, and N. Murata The primary signal in the biological perception of temperature: Pd-catalyzed hydrogenation of membrane lipids stimulated the expression of the desA gene in Synechocystis PCC6803 Proc. Natl. Acad. Sci. U. S. A. 90 1993 9090 9094
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 9090-9094
    • Vigh, L.1    Los, D.A.2    Horvath, I.3    Murata, N.4
  • 6
    • 0032945248 scopus 로고    scopus 로고
    • Mechanosensitive channels in bacteria as membrane tension reporters
    • S. Sukharev Mechanosensitive channels in bacteria as membrane tension reporters FASEB J. 13 1999 S55 S61 (Suppl.)
    • (1999) FASEB J. , vol.13
    • Sukharev, S.1
  • 7
    • 0033014719 scopus 로고    scopus 로고
    • Osmosensing by bacteria: Signals and membrane-based sensors
    • J.M. Wood Osmosensing by bacteria: signals and membrane-based sensors Microbiol. Mol. Biol. Rev. 63 1999 230 262
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 230-262
    • Wood, J.M.1
  • 8
    • 0036282743 scopus 로고    scopus 로고
    • Osmotic stress signaling and osmoadaptation in yeasts
    • S. Hohmann Osmotic stress signaling and osmoadaptation in yeasts Microbiol. Mol. Biol. Rev. 66 2003 300 372
    • (2003) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 300-372
    • Hohmann, S.1
  • 9
    • 0028170316 scopus 로고
    • Transmembrane signal transduction by the Escherichia coli osmotic sensor, EnvZ: Intermolecular complementation of transmembrane signaling
    • S. Tokishita, and T. Mizuno Transmembrane signal transduction by the Escherichia coli osmotic sensor, EnvZ: intermolecular complementation of transmembrane signaling Mol. Microbiol. 13 1994 435 444
    • (1994) Mol. Microbiol. , vol.13 , pp. 435-444
    • Tokishita, S.1    Mizuno, T.2
  • 10
    • 0028090288 scopus 로고
    • Signal-sensing mechanisms of the putative osmosensor KdpD in Escherichia coli
    • A. Sugiura, K. Hirokawa, K. Nakashima, and T. Mizuno Signal-sensing mechanisms of the putative osmosensor KdpD in Escherichia coli Mol. Microbiol. 14 1994 929 938
    • (1994) Mol. Microbiol. , vol.14 , pp. 929-938
    • Sugiura, A.1    Hirokawa, K.2    Nakashima, K.3    Mizuno, T.4
  • 11
    • 0020492830 scopus 로고
    • Resolution of plasma membrane lipid fluidity in intact cells labeled with diphenylhexatriene
    • D. Grunberger, R. Haimovitz, and M. Shinitzky Resolution of plasma membrane lipid fluidity in intact cells labeled with diphenylhexatriene Biochim. Biophys. Acta 688 1982 764 774
    • (1982) Biochim. Biophys. Acta , vol.688 , pp. 764-774
    • Grunberger, D.1    Haimovitz, R.2    Shinitzky, M.3
  • 12
    • 0027495558 scopus 로고
    • Use of fluorescent probes to monitor molecular order and motions within liposome bilayers
    • B.R. Lentz Use of fluorescent probes to monitor molecular order and motions within liposome bilayers Chem. Phys. Lipids 64 1993 99 116
    • (1993) Chem. Phys. Lipids , vol.64 , pp. 99-116
    • Lentz, B.R.1
  • 13
    • 0034918607 scopus 로고    scopus 로고
    • The effect of osmotic pressure on the membrane fluidity of Saccharomyces cerevisiae at different physiological temperatures
    • C. Laroche, L. Beney, P.A. Marechal, and P. Gervais The effect of osmotic pressure on the membrane fluidity of Saccharomyces cerevisiae at different physiological temperatures Appl. Microbiol. Biotechnol. 56 2001 249 254
    • (2001) Appl. Microbiol. Biotechnol. , vol.56 , pp. 249-254
    • Laroche, C.1    Beney, L.2    Marechal, P.A.3    Gervais, P.4
  • 14
    • 0034695106 scopus 로고    scopus 로고
    • Membrane dynamics as seen by Fourier transform infrared spectroscopy in a cyanobacterium, Synechocystis PCC 6803. The effects of lipid unsaturation and the protein-to-lipid ratio
    • B. Szalontai, Y. Nishiyama, Z. Gombos, and N. Murata Membrane dynamics as seen by Fourier transform infrared spectroscopy in a cyanobacterium, Synechocystis PCC 6803. The effects of lipid unsaturation and the protein-to-lipid ratio Biochim. Biophys. Acta 1509 2000 409 419
    • (2000) Biochim. Biophys. Acta , vol.1509 , pp. 409-419
    • Szalontai, B.1    Nishiyama, Y.2    Gombos, Z.3    Murata, N.4
  • 15
    • 0017889424 scopus 로고
    • Adaptation of biological membranes to temperature. The lack of homeoviscous adaptation in the sarcoplasmic reticulum
    • A.R. Cossins, J. Christiansen, and C.L. Prosser Adaptation of biological membranes to temperature. The lack of homeoviscous adaptation in the sarcoplasmic reticulum Biochim. Biophys. Acta 511 1978 442 452
    • (1978) Biochim. Biophys. Acta , vol.511 , pp. 442-452
    • Cossins, A.R.1    Christiansen, J.2    Prosser, C.L.3
  • 16
    • 0024298835 scopus 로고
    • Calorimetric and spectroscopic studies of lipid thermotropic phase behavior in liver inner mitochondrial membranes from a mammalian hibernator
    • D.J. Pehowich, P.M. Macdonald, R.N. McElhaney, A.R. Cossins, and L.C. Wang Calorimetric and spectroscopic studies of lipid thermotropic phase behavior in liver inner mitochondrial membranes from a mammalian hibernator Biochemistry 27 1988 4632 4638
    • (1988) Biochemistry , vol.27 , pp. 4632-4638
    • Pehowich, D.J.1    MacDonald, P.M.2    McElhaney, R.N.3    Cossins, A.R.4    Wang, L.C.5
  • 17
    • 0001380883 scopus 로고
    • Homeoviscous adaptation-a homeostatic process that regulates viscosity of membrane lipids in Escherichia coli
    • M. Sinensky Homeoviscous adaptation-a homeostatic process that regulates viscosity of membrane lipids in Escherichia coli Proc. Natl. Acad. Sci. U. S. A. 71 1974 522 525
    • (1974) Proc. Natl. Acad. Sci. U. S. A. , vol.71 , pp. 522-525
    • Sinensky, M.1
  • 18
    • 0038075310 scopus 로고    scopus 로고
    • Gene-engineered rigidification of membrane lipids enhances the cold inducibility of gene expression in Synechocystis
    • M. Inaba, I. Suzuki, B. Szalontai, Y. Kanesaki, D.A. Los, H. Hayashi, and N. Murata Gene-engineered rigidification of membrane lipids enhances the cold inducibility of gene expression in Synechocystis J. Biol. Chem. 278 2003 12191 12198
    • (2003) J. Biol. Chem. , vol.278 , pp. 12191-12198
    • Inaba, M.1    Suzuki, I.2    Szalontai, B.3    Kanesaki, Y.4    Los, D.A.5    Hayashi, H.6    Murata, N.7
  • 19
    • 0031786750 scopus 로고    scopus 로고
    • Does the membrane's physical state control the expression of heat shock and other genes?
    • L. Vigh, B. Maresca, and J.L. Harwood Does the membrane's physical state control the expression of heat shock and other genes? Trends Biochem. Sci. 23 1998 369 374
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 369-374
    • Vigh, L.1    Maresca, B.2    Harwood, J.L.3
  • 20
    • 0024505718 scopus 로고
    • Osmoelastic coupling in biological structures: Decrease in membrane fluidity and osmophobic association of phospholipid vesicles in response to osmotic stress
    • M. Yamazaki, S. Ohnishi, and T. Ito Osmoelastic coupling in biological structures: decrease in membrane fluidity and osmophobic association of phospholipid vesicles in response to osmotic stress Biochemistry 28 1989 3710 3715
    • (1989) Biochemistry , vol.28 , pp. 3710-3715
    • Yamazaki, M.1    Ohnishi, S.2    Ito, T.3
  • 21
    • 0032478310 scopus 로고    scopus 로고
    • Modulation of GTPase activity of G proteins by fluid shear stress and phospholipid composition
    • S. Gudi, J.P. Nolan, and J.A. Frangos Modulation of GTPase activity of G proteins by fluid shear stress and phospholipid composition Proc. Natl. Acad. Sci. U. S. A. 95 1998 2515 2519
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 2515-2519
    • Gudi, S.1    Nolan, J.P.2    Frangos, J.A.3
  • 22
    • 0037470964 scopus 로고    scopus 로고
    • Effect of aliphatic alcohols on growth and degree of saturation of membrane lipids in Acinetobacter calcoaceticus
    • N. Kabelitz, P.M. Santos, and H.J. Heipieper Effect of aliphatic alcohols on growth and degree of saturation of membrane lipids in Acinetobacter calcoaceticus FEMS Microbiol. Lett. 220 2003 223 227
    • (2003) FEMS Microbiol. Lett. , vol.220 , pp. 223-227
    • Kabelitz, N.1    Santos, P.M.2    Heipieper, H.J.3
  • 23
  • 24
    • 0029671331 scopus 로고    scopus 로고
    • Cold-induced expression of Î"9-desaturase in carp by transcriptional and posttranslational mechanisms
    • P.E. Tiku, A.Y. Gracey, A.I. Macartney, R.J. Beynon, and A.R. Cossins Cold-induced expression of Î"9-desaturase in carp by transcriptional and posttranslational mechanisms Science 271 1996 815 818
    • (1996) Science , vol.271 , pp. 815-818
    • Tiku, P.E.1    Gracey, A.Y.2    MacArtney, A.I.3    Beynon, R.J.4    Cossins, A.R.5
  • 25
    • 0030590213 scopus 로고    scopus 로고
    • An isothermal induction of Î"9-desaturase in cultured carp hepatocytes
    • A.I. Macartney, P.E. Tiku, and A.R. Cossins An isothermal induction of Î"9-desaturase in cultured carp hepatocytes Biochim. Biophys. Acta 1302 1996 207 216
    • (1996) Biochim. Biophys. Acta , vol.1302 , pp. 207-216
    • MacArtney, A.I.1    Tiku, P.E.2    Cossins, A.R.3
  • 26
    • 0027425922 scopus 로고
    • Changes in membrane fluidity modulate heat shock gene expression and produced attenuated strains in the dimorphic fungus Histoplasma capsulatum
    • B. Maresca, and G. Kobayashi Changes in membrane fluidity modulate heat shock gene expression and produced attenuated strains in the dimorphic fungus Histoplasma capsulatum Arch. Med. Res. 24 1993 247 249
    • (1993) Arch. Med. Res. , vol.24 , pp. 247-249
    • Maresca, B.1    Kobayashi, G.2
  • 27
    • 0024378751 scopus 로고
    • Nutritional regulation of yeast Î"9 fatty acid desaturase activity
    • M.A. Bossie, and C.E. Martin Nutritional regulation of yeast Î"9 fatty acid desaturase activity J. Bacteriol. 171 1989 6409 6413
    • (1989) J. Bacteriol. , vol.171 , pp. 6409-6413
    • Bossie, M.A.1    Martin, C.E.2
  • 28
    • 0014769128 scopus 로고
    • Oxidative activity of mitochondria isolated from plant tissues sensitive and resistant to chilling injury
    • J.M. Lyons, and J.K. Raison Oxidative activity of mitochondria isolated from plant tissues sensitive and resistant to chilling injury Plant Physiol. 45 1970 386 389
    • (1970) Plant Physiol. , vol.45 , pp. 386-389
    • Lyons, J.M.1    Raison, J.K.2
  • 29
    • 0001676540 scopus 로고    scopus 로고
    • Chilling sensitivity in plants and cyanobacteria: The crucial contribution of membrane lipids
    • I. Nishida, and N. Murata Chilling sensitivity in plants and cyanobacteria: the crucial contribution of membrane lipids Annu. Rev. Plant Physiol. Plant Mol. Biol. 47 1996 541 568
    • (1996) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.47 , pp. 541-568
    • Nishida, I.1    Murata, N.2
  • 30
    • 0036049785 scopus 로고    scopus 로고
    • Mechanism of membrane fluidity optimization: Isothermal control of the Bacillus subtilis acyl-lipid desaturase
    • L.E. Cybulski, M.C. Mansilla, P.S. Aguilar, and D. de Mendoza Mechanism of membrane fluidity optimization: isothermal control of the Bacillus subtilis acyl-lipid desaturase Mol. Microbiol. 45 2002 1379 1388
    • (2002) Mol. Microbiol. , vol.45 , pp. 1379-1388
    • Cybulski, L.E.1    Mansilla, M.C.2    Aguilar, P.S.3    De Mendoza, D.4
  • 31
    • 0031659941 scopus 로고    scopus 로고
    • Structure and expression of fatty acid desaturases
    • D.A. Los, and N. Murata Structure and expression of fatty acid desaturases Biochim. Biophys. Acta 1394 1998 3 15
    • (1998) Biochim. Biophys. Acta , vol.1394 , pp. 3-15
    • Los, D.A.1    Murata, N.2
  • 33
    • 0032996338 scopus 로고    scopus 로고
    • The Synechocystis model of stress: From molecular chaperones to membranes
    • A. Glatz, I. Vass, D.A. Los, and L. Vigh The Synechocystis model of stress: from molecular chaperones to membranes Plant Physiol. Biochem. 37 1999 1 12
    • (1999) Plant Physiol. Biochem. , vol.37 , pp. 1-12
    • Glatz, A.1    Vass, I.2    Los, D.A.3    Vigh, L.4
  • 34
    • 0025143880 scopus 로고
    • Enhancement of chilling tolerance of a cyanobacterium by genetic manipulation of fatty acid desaturation
    • H. Wada, Z. Gombos, and N. Murata Enhancement of chilling tolerance of a cyanobacterium by genetic manipulation of fatty acid desaturation Nature 347 1990 200 203
    • (1990) Nature , vol.347 , pp. 200-203
    • Wada, H.1    Gombos, Z.2    Murata, N.3
  • 35
    • 0029804115 scopus 로고    scopus 로고
    • Targeted mutagenesis of acyl-lipid desaturases in Synechocystis: Evidence for the important roles of polyunsaturated membrane lipids in growth, respiration and photosynthesis
    • Y. Tasaka, Z. Gombos, Y. Nishiyama, P. Mohanty, T. Ohba, K. Ohki, and N. Murata Targeted mutagenesis of acyl-lipid desaturases in Synechocystis: evidence for the important roles of polyunsaturated membrane lipids in growth, respiration and photosynthesis EMBO J. 15 1996 6416 6425
    • (1996) EMBO J. , vol.15 , pp. 6416-6425
    • Tasaka, Y.1    Gombos, Z.2    Nishiyama, Y.3    Mohanty, P.4    Ohba, T.5    Ohki, K.6    Murata, N.7
  • 36
    • 0029819934 scopus 로고    scopus 로고
    • Low-temperature resistance of higher plants is significantly enhanced by a nonspecific cyanobacterial desaturase
    • O. Ishizaki-Nishizawa, T. Fujii, M. Azuma, K. Sekiguchi, N. Murata, T. Ohtani, and T. Toguri Low-temperature resistance of higher plants is significantly enhanced by a nonspecific cyanobacterial desaturase Nat. Biotechnol. 14 1996 1003 1006
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1003-1006
    • Ishizaki-Nishizawa, O.1    Fujii, T.2    Azuma, M.3    Sekiguchi, K.4    Murata, N.5    Ohtani, T.6    Toguri, T.7
  • 38
    • 0027398750 scopus 로고
    • The temperature-dependent expression of the desaturase gene desA in Synechocystis PCC6803
    • D. Los, I. Horvath, L. Vigh, and N. Murata The temperature-dependent expression of the desaturase gene desA in Synechocystis PCC6803 FEBS Lett. 318 1993 57 60
    • (1993) FEBS Lett. , vol.318 , pp. 57-60
    • Los, D.1    Horvath, I.2    Vigh, L.3    Murata, N.4
  • 39
    • 0030929312 scopus 로고    scopus 로고
    • Differences in the control of the temperature-dependent expression of four genes for desaturases in Synechocystis sp., PCC 6803
    • D.A. Los, M.K. Ray, and N. Murata Differences in the control of the temperature-dependent expression of four genes for desaturases in Synechocystis sp., PCC 6803 Mol. Microbiol. 25 1997 1167 1175
    • (1997) Mol. Microbiol. , vol.25 , pp. 1167-1175
    • Los, D.A.1    Ray, M.K.2    Murata, N.3
  • 40
    • 0028916402 scopus 로고
    • Thermal adaptation in biological membranes: Is homeoviscous adaptation the explanation?
    • J.R. Hazel Thermal adaptation in biological membranes: is homeoviscous adaptation the explanation? Annu. Rev. Physiol. 57 1995 19 42
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 19-42
    • Hazel, J.R.1
  • 41
    • 0002361795 scopus 로고
    • Acyl-CoA desaturases and the adaptive regulation of membrane lipid composition
    • A.R. Cossins Portland Press London
    • A.I. Macartney, B. Maresca, and A.R. Cossins Acyl-CoA desaturases and the adaptive regulation of membrane lipid composition A.R. Cossins Temperature Adaptation of Biological Membranes 1994 Portland Press London 129 139
    • (1994) Temperature Adaptation of Biological Membranes , pp. 129-139
    • MacArtney, A.I.1    Maresca, B.2    Cossins, A.R.3
  • 42
    • 0025825208 scopus 로고
    • Rapid cold-induced changes of membrane order and Î"9- desaturase activity in endoplasmic reticulum of carp liver: A time-course study of thermal acclimation
    • E. Wodtke, and A.R. Cossins Rapid cold-induced changes of membrane order and Î"9-desaturase activity in endoplasmic reticulum of carp liver: a time-course study of thermal acclimation Biochim. Biophys. Acta 1064 1991 342 350
    • (1991) Biochim. Biophys. Acta , vol.1064 , pp. 342-350
    • Wodtke, E.1    Cossins, A.R.2
  • 43
    • 0036289674 scopus 로고    scopus 로고
    • Salt stress and hyperosmotic stress regulate the expression of different sets of genes in Synechocystis sp., PCC 6803
    • Y. Kanesaki, I. Suzuki, S.I. Allakhverdiev, K. Mikami, and N. Murata Salt stress and hyperosmotic stress regulate the expression of different sets of genes in Synechocystis sp., PCC 6803 Biochem. Biophys. Res. Commun. 290 2002 339 348
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 339-348
    • Kanesaki, Y.1    Suzuki, I.2    Allakhverdiev, S.I.3    Mikami, K.4    Murata, N.5
  • 44
  • 45
    • 0025313643 scopus 로고
    • A trans-unsaturated fatty acid in a psychrophilic bacterium, Vibrio sp. strain ABE-1
    • H. Okuyama, S. Sasaki, S. Higashi, and N. Murata A trans-unsaturated fatty acid in a psychrophilic bacterium, Vibrio sp. strain ABE-1 J. Bacteriol. 172 1990 3515 3518
    • (1990) J. Bacteriol. , vol.172 , pp. 3515-3518
    • Okuyama, H.1    Sasaki, S.2    Higashi, S.3    Murata, N.4
  • 46
    • 0025849745 scopus 로고
    • The cis/trans isomerization of the double bond of a fatty acid as a strategy for adaptation to changes in ambient temperature in the psychrophilic bacterium, Vibrio sp. strain ABE-1
    • H. Okuyama, N. Okajima, S. Sasaki, S. Higashi, and N. Murata The cis/trans isomerization of the double bond of a fatty acid as a strategy for adaptation to changes in ambient temperature in the psychrophilic bacterium, Vibrio sp. strain ABE-1 Biochim. Biophys. Acta 1084 1991 13 20
    • (1991) Biochim. Biophys. Acta , vol.1084 , pp. 13-20
    • Okuyama, H.1    Okajima, N.2    Sasaki, S.3    Higashi, S.4    Murata, N.5
  • 47
    • 0037371639 scopus 로고    scopus 로고
    • Mechanism of cis-trans isomerization of unsaturated fatty acids in Pseudomonas putida
    • A. von Wallbrunn, H.H. Richnow, G. Neumann, F. Meinhardt, and H.J. Heipieper Mechanism of cis-trans isomerization of unsaturated fatty acids in Pseudomonas putida J. Bacteriol. 185 2003 1730 1733
    • (2003) J. Bacteriol. , vol.185 , pp. 1730-1733
    • Von Wallbrunn, A.1    Richnow, H.H.2    Neumann, G.3    Meinhardt, F.4    Heipieper, H.J.5
  • 48
    • 0345490758 scopus 로고    scopus 로고
    • The cis-trans isomerase of unsaturated fatty acids in Pseudomonas and Vibrio: Biochemistry, molecular biology and physiological function of a unique stress-adaptive mechanism
    • H.J. Heipieper, F. Meinhardt, and A. Segura The cis-trans isomerase of unsaturated fatty acids in Pseudomonas and Vibrio: biochemistry, molecular biology and physiological function of a unique stress-adaptive mechanism FEMS Microbiol. Lett. 229 2003 1 7
    • (2003) FEMS Microbiol. Lett. , vol.229 , pp. 1-7
    • Heipieper, H.J.1    Meinhardt, F.2    Segura, A.3
  • 49
    • 0032851111 scopus 로고    scopus 로고
    • Sterols and isoprenoids: Signaling molecules derived from the cholesterol biosynthetic pathway
    • P.A. Edwards, and J. Ericsson Sterols and isoprenoids: signaling molecules derived from the cholesterol biosynthetic pathway Annu. Rev. Biochem. 68 1999 157 185
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 157-185
    • Edwards, P.A.1    Ericsson, J.2
  • 50
    • 0033613147 scopus 로고    scopus 로고
    • A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood
    • M.S. Brown, and J.L. Goldstein A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood Proc. Natl. Acad. Sci. U. S. A. 96 1999 11041 11048
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 11041-11048
    • Brown, M.S.1    Goldstein, J.L.2
  • 51
    • 0032892175 scopus 로고    scopus 로고
    • Sterol regulatory element-binding proteins: Activators of cholesterol and fatty acid biosynthesis
    • J.D. Horton, and I. Shimomura Sterol regulatory element-binding proteins: activators of cholesterol and fatty acid biosynthesis Curr. Opin. Lipidol. 10 1999 143 150
    • (1999) Curr. Opin. Lipidol. , vol.10 , pp. 143-150
    • Horton, J.D.1    Shimomura, I.2
  • 52
    • 0037082099 scopus 로고    scopus 로고
    • Mutant mammalian cells as tools to delineate the sterol regulatory element-binding protein pathway for feedback regulation of lipid synthesis
    • J.L. Goldstein, R.B. Rawson, and M.S. Brown Mutant mammalian cells as tools to delineate the sterol regulatory element-binding protein pathway for feedback regulation of lipid synthesis Arch. Biochem. Biophys. 397 2002 139 148
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 139-148
    • Goldstein, J.L.1    Rawson, R.B.2    Brown, M.S.3
  • 53
    • 0141591549 scopus 로고    scopus 로고
    • Cholesterol-induced conformational change in SCAP enhanced by Insig proteins and mimicked by cationic amphiphiles
    • C.M. Adams, J.L. Goldstein, and M.S. Brown Cholesterol-induced conformational change in SCAP enhanced by Insig proteins and mimicked by cationic amphiphiles Proc. Natl. Acad. Sci. U. S. A. 100 2003 10647 10652
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 10647-10652
    • Adams, C.M.1    Goldstein, J.L.2    Brown, M.S.3
  • 54
    • 0029060966 scopus 로고
    • Acyl-lipid desaturases and their importance in the tolerance and acclimatization to cold of cyanobacteria
    • N. Murata, and H. Wada Acyl-lipid desaturases and their importance in the tolerance and acclimatization to cold of cyanobacteria Biochem. J. 308 1995 1 8
    • (1995) Biochem. J. , vol.308 , pp. 1-8
    • Murata, N.1    Wada, H.2
  • 55
    • 0035051326 scopus 로고    scopus 로고
    • Cold-regulated genes under control of the cold sensor Hik33 in Synechocystis
    • I. Suzuki, Y. Kanesaki, K. Mikami, M. Kanehisa, and N. Murata Cold-regulated genes under control of the cold sensor Hik33 in Synechocystis Mol. Microbiol. 40 2001 235 244
    • (2001) Mol. Microbiol. , vol.40 , pp. 235-244
    • Suzuki, I.1    Kanesaki, Y.2    Mikami, K.3    Kanehisa, M.4    Murata, N.5
  • 56
    • 0342546000 scopus 로고    scopus 로고
    • The pathway for perception and transduction of low-temperature signals in Synechocystis
    • I. Suzuki, D.A. Los, Y. Kanesaki, K. Mikami, and N. Murata The pathway for perception and transduction of low-temperature signals in Synechocystis EMBO J. 19 2000 1327 1334
    • (2000) EMBO J. , vol.19 , pp. 1327-1334
    • Suzuki, I.1    Los, D.A.2    Kanesaki, Y.3    Mikami, K.4    Murata, N.5
  • 57
    • 0034471441 scopus 로고    scopus 로고
    • Perception and transduction of low-temperature signals to induce desaturation of fatty acids
    • I. Suzuki, D.A. Los, and N. Murata Perception and transduction of low-temperature signals to induce desaturation of fatty acids Biochem. Soc. Trans. 28 2000 628 630
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 628-630
    • Suzuki, I.1    Los, D.A.2    Murata, N.3
  • 58
    • 0032826834 scopus 로고    scopus 로고
    • Functional similarities among two-component sensors and methyl-accepting chemotaxis proteins suggest a role for linker region amphipathic helices in transmembrane signal transduction
    • S.B. Williams, and V. Stewart Functional similarities among two-component sensors and methyl-accepting chemotaxis proteins suggest a role for linker region amphipathic helices in transmembrane signal transduction Mol. Microbiol. 33 1999 1093 1102
    • (1999) Mol. Microbiol. , vol.33 , pp. 1093-1102
    • Williams, S.B.1    Stewart, V.2
  • 59
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • B.L. Taylor, and I.B. Zhulin PAS domains: internal sensors of oxygen, redox potential, and light Microbiol. Mol. Biol. Rev. 63 1999 479 506
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 60
    • 0032766134 scopus 로고    scopus 로고
    • The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins
    • L. Aravind, and C.P. Ponting The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins FEMS Microbiol. Lett. 176 1999 111 116
    • (1999) FEMS Microbiol. Lett. , vol.176 , pp. 111-116
    • Aravind, L.1    Ponting, C.P.2
  • 61
    • 0242354978 scopus 로고    scopus 로고
    • Evolutionary connections between bacterial and eukaryotic signaling systems: A genomic perspective
    • L. Aravind, V. Anantharaman, and L.M. Iyer Evolutionary connections between bacterial and eukaryotic signaling systems: a genomic perspective Curr. Opin. Microbiol. 6 2003 490 507
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 490-507
    • Aravind, L.1    Anantharaman, V.2    Iyer, L.M.3
  • 62
    • 0036273511 scopus 로고    scopus 로고
    • Cell signaling during cold, drought, and salt stress
    • L. Xiong, K.S. Schumaker, and J.K. Zhu Cell signaling during cold, drought, and salt stress Plant Cell 2002 S165 S183 (Suppl.)
    • (2002) Plant Cell
    • Xiong, L.1    Schumaker, K.S.2    Zhu, J.K.3
  • 63
    • 0036671216 scopus 로고    scopus 로고
    • Arabidopsis transcriptome profiling indicates that multiple regulatory pathways are activated during cold acclimation in addition to the CBF cold-response pathway
    • S. Fowler, and M.F. Thomashow Arabidopsis transcriptome profiling indicates that multiple regulatory pathways are activated during cold acclimation in addition to the CBF cold-response pathway Plant Cell 14 2003 1675 1690
    • (2003) Plant Cell , vol.14 , pp. 1675-1690
    • Fowler, S.1    Thomashow, M.F.2
  • 64
    • 0035794713 scopus 로고    scopus 로고
    • Molecular basis of thermosensing: A two-component signal transduction thermometer in Bacillus subtilis
    • P.S. Aguilar, A.M. Hernandez-Arriaga, L.E. Cybulski, A.C. Erazo, and D. de Mendoza Molecular basis of thermosensing: a two-component signal transduction thermometer in Bacillus subtilis EMBO J. 20 2001 1681 1691
    • (2001) EMBO J. , vol.20 , pp. 1681-1691
    • Aguilar, P.S.1    Hernandez-Arriaga, A.M.2    Cybulski, L.E.3    Erazo, A.C.4    De Mendoza, D.5
  • 65
    • 0027683430 scopus 로고
    • Cloning and sequencing of the cDNA for cas17, a cold acclimation-specific gene of alfalfa
    • L.A. Wolfraim, and R.S. Dhindsa Cloning and sequencing of the cDNA for cas17, a cold acclimation-specific gene of alfalfa Plant Physiol. 103 1993 667 668
    • (1993) Plant Physiol. , vol.103 , pp. 667-668
    • Wolfraim, L.A.1    Dhindsa, R.S.2
  • 66
    • 0029257293 scopus 로고
    • Low-temperature signal transduction: Induction of cold acclimation-specific genes of alfalfa by calcium at 25 °C
    • A.F. Monroy, and R.S. Dhindsa Low-temperature signal transduction: induction of cold acclimation-specific genes of alfalfa by calcium at 25 °C Plant Cell 7 1995 321 331
    • (1995) Plant Cell , vol.7 , pp. 321-331
    • Monroy, A.F.1    Dhindsa, R.S.2
  • 67
    • 0030844357 scopus 로고    scopus 로고
    • Low-temperature perception in plants: Effects of cold on protein phosphorylation in cell-free extracts
    • A.F. Monroy, E. Labbe, and R.S. Dhindsa Low-temperature perception in plants: effects of cold on protein phosphorylation in cell-free extracts FEBS Lett. 410 1997 206 209
    • (1997) FEBS Lett. , vol.410 , pp. 206-209
    • Monroy, A.F.1    Labbe, E.2    Dhindsa, R.S.3
  • 68
    • 0031465310 scopus 로고    scopus 로고
    • The induction of kin genes in cold-acclimating Arabidopsis thaliana, evidence of a role for calcium
    • S. Tahtiharju, V. Sangwan, A.F. Monroy, R.S. Dhindsa, and M. Borg The induction of kin genes in cold-acclimating Arabidopsis thaliana, evidence of a role for calcium Planta 203 1997 442 447
    • (1997) Planta , vol.203 , pp. 442-447
    • Tahtiharju, S.1    Sangwan, V.2    Monroy, A.F.3    Dhindsa, R.S.4    Borg, M.5
  • 69
    • 0033801589 scopus 로고    scopus 로고
    • Early steps in cold sensing by plant cells: The role of actin cytoskeleton and membrane fluidity
    • B.L. Orvar, V. Sangwan, F. Omann, and R.S. Dhindsa Early steps in cold sensing by plant cells: the role of actin cytoskeleton and membrane fluidity Plant J. 23 2000 785 794
    • (2000) Plant J. , vol.23 , pp. 785-794
    • Orvar, B.L.1    Sangwan, V.2    Omann, F.3    Dhindsa, R.S.4
  • 70
    • 0032144961 scopus 로고    scopus 로고
    • Two transcription factors, DREB1 and DREB2, with an EREBP/AP2 DNA-binding domain separate two cellular signal transduction pathways in drought- and low-temperature-responsive gene expression, respectively, in Arabidopsis
    • Q. Liu, M. Kasuga, Y. Sakuma, H. Abe, S. Miura, K. Yamaguchi-Shinozaki, and K. Shinozaki Two transcription factors, DREB1 and DREB2, with an EREBP/AP2 DNA-binding domain separate two cellular signal transduction pathways in drought- and low-temperature-responsive gene expression, respectively, in Arabidopsis Plant Cell 10 1998 1391 1406
    • (1998) Plant Cell , vol.10 , pp. 1391-1406
    • Liu, Q.1    Kasuga, M.2    Sakuma, Y.3    Abe, H.4    Miura, S.5    Yamaguchi-Shinozaki, K.6    Shinozaki, K.7
  • 72
    • 0034028259 scopus 로고    scopus 로고
    • Molecular responses to dehydration and low temperature: Differences and cross-talk between two stress signaling pathways
    • K. Shinozaki, and K. Yamaguchi-Shinozaki Molecular responses to dehydration and low temperature: differences and cross-talk between two stress signaling pathways Curr. Opin. Plant Biol. 3 2000 217 223
    • (2000) Curr. Opin. Plant Biol. , vol.3 , pp. 217-223
    • Shinozaki, K.1    Yamaguchi-Shinozaki, K.2
  • 73
    • 0035107803 scopus 로고    scopus 로고
    • Monitoring the expression pattern of 1300 Arabidopsis genes under drought and cold stresses by using a full-length cDNA microarray
    • M. Seki, M. Narusaka, H. Abe, M. Kasuga, K. Yamaguchi-Shinozaki, P. Carninci, Y. Hayashizaki, and K. Shinozaki Monitoring the expression pattern of 1300 Arabidopsis genes under drought and cold stresses by using a full-length cDNA microarray Plant Cell 13 2001 61 72
    • (2001) Plant Cell , vol.13 , pp. 61-72
    • Seki, M.1    Narusaka, M.2    Abe, H.3    Kasuga, M.4    Yamaguchi-Shinozaki, K.5    Carninci, P.6    Hayashizaki, Y.7    Shinozaki, K.8
  • 74
    • 0034865459 scopus 로고    scopus 로고
    • Cell signaling under salt, water and cold stresses
    • J.K. Zhu Cell signaling under salt, water and cold stresses Curr. Opin. Plant Biol. 4 2001 401 406
    • (2001) Curr. Opin. Plant Biol. , vol.4 , pp. 401-406
    • Zhu, J.K.1
  • 75
    • 0026481498 scopus 로고
    • CDNA sequence analysis and expression of two cold-regulated genes of Arabidopsis thaliana
    • S.J. Gilmour, N.N. Artus, and M.F. Thomashow cDNA sequence analysis and expression of two cold-regulated genes of Arabidopsis thaliana Plant Mol. Biol. 18 1992 13 21
    • (1992) Plant Mol. Biol. , vol.18 , pp. 13-21
    • Gilmour, S.J.1    Artus, N.N.2    Thomashow, M.F.3
  • 76
    • 0026684471 scopus 로고
    • A cold-regulated Arabidopsis gene encodes a polypeptide having potent cryoprotective activity
    • C. Lin, and M.F. Thomashow A cold-regulated Arabidopsis gene encodes a polypeptide having potent cryoprotective activity Biochem. Biophys. Res. Commun. 183 1992 1103 1108
    • (1992) Biochem. Biophys. Res. Commun. , vol.183 , pp. 1103-1108
    • Lin, C.1    Thomashow, M.F.2
  • 77
    • 0027750416 scopus 로고
    • Arabidopsis thaliana cor15b, an apparent homologue of cor15a, is strongly responsive to cold and ABA, but not drought
    • K.S. Wilhelm, and M.F. Thomashow Arabidopsis thaliana cor15b, an apparent homologue of cor15a, is strongly responsive to cold and ABA, but not drought Plant Mol. Biol. 23 1993 1073 1077
    • (1993) Plant Mol. Biol. , vol.23 , pp. 1073-1077
    • Wilhelm, K.S.1    Thomashow, M.F.2
  • 78
    • 0030138097 scopus 로고    scopus 로고
    • Effects of COR6.6 and COR15am polypeptides encoded by COR (cold-regulated) genes of Arabidopsis thaliana on dehydration-induced phase transitions of phospholipid membranes
    • M.S. Webb, S.J. Gilmour, M.F. Thomashow, and P.L. Steponkus Effects of COR6.6 and COR15am polypeptides encoded by COR (cold-regulated) genes of Arabidopsis thaliana on dehydration-induced phase transitions of phospholipid membranes Plant Physiol. 111 1996 301 312
    • (1996) Plant Physiol. , vol.111 , pp. 301-312
    • Webb, M.S.1    Gilmour, S.J.2    Thomashow, M.F.3    Steponkus, P.L.4
  • 79
    • 0032161654 scopus 로고    scopus 로고
    • Role of cold-responsive genes in plant freezing tolerance
    • M.F. Thomashow Role of cold-responsive genes in plant freezing tolerance Plant Physiol. 118 1998 1 8
    • (1998) Plant Physiol. , vol.118 , pp. 1-8
    • Thomashow, M.F.1
  • 80
    • 0028086460 scopus 로고
    • Cloning of a cDNA encoding tobacco ω3 fatty acid desaturase
    • T. Hamada, H. Kodama, M. Nishimura, and K. Iba Cloning of a cDNA encoding tobacco ω3 fatty acid desaturase Gene 147 1994 293 294
    • (1994) Gene , vol.147 , pp. 293-294
    • Hamada, T.1    Kodama, H.2    Nishimura, M.3    Iba, K.4
  • 81
    • 0015239776 scopus 로고
    • Temperature-induced phase changes in mitochondrial membranes detected by spin labeling
    • J.K. Raison, J.M. Lyons, R.J. Mehlhorn, and A.D. Keith Temperature-induced phase changes in mitochondrial membranes detected by spin labeling J. Biol. Chem. 246 1971 4036 4040
    • (1971) J. Biol. Chem. , vol.246 , pp. 4036-4040
    • Raison, J.K.1    Lyons, J.M.2    Mehlhorn, R.J.3    Keith, A.D.4
  • 82
    • 0015826523 scopus 로고
    • Temperature-induced phase changes in membrane lipids and their influence on metabolic regulation
    • J.K. Raison Temperature-induced phase changes in membrane lipids and their influence on metabolic regulation Symp. Soc. Exp. Biol. 27 1973 485 512
    • (1973) Symp. Soc. Exp. Biol. , vol.27 , pp. 485-512
    • Raison, J.K.1
  • 83
    • 0028370581 scopus 로고
    • A novel cis-acting element in an Arabidopsis gene is involved in responsiveness to drought, low-temperature, or high-salt stress
    • K. Yamaguchi-Shinozaki, and K. Shinozaki A novel cis-acting element in an Arabidopsis gene is involved in responsiveness to drought, low-temperature, or high-salt stress Plant Cell 6 1994 251 264
    • (1994) Plant Cell , vol.6 , pp. 251-264
    • Yamaguchi-Shinozaki, K.1    Shinozaki, K.2
  • 85
    • 0031017671 scopus 로고    scopus 로고
    • Arabidopsis thaliana CBF1 encodes an AP2 domain-containing transcriptional activator that binds to the C-repeat/DRE, a cis-acting DNA regulatory element that stimulates transcription in response to low temperature and water deficit
    • E.J. Stockinger, S.J. Gilmour, and M.F. Thomashow Arabidopsis thaliana CBF1 encodes an AP2 domain-containing transcriptional activator that binds to the C-repeat/DRE, a cis-acting DNA regulatory element that stimulates transcription in response to low temperature and water deficit Proc. Natl. Acad. Sci. U. S. A. 94 1997 1035 1040
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 1035-1040
    • Stockinger, E.J.1    Gilmour, S.J.2    Thomashow, M.F.3
  • 87
    • 0032213180 scopus 로고    scopus 로고
    • Low temperature regulation of the Arabidopsis CBF family of AP2 transcriptional activators as an early step in cold-induced COR gene expression
    • S.J. Gilmour, D.G. Zarka, E.J. Stockinger, M.P. Salazar, J.M. Houghton, and M.F. Thomashow Low temperature regulation of the Arabidopsis CBF family of AP2 transcriptional activators as an early step in cold-induced COR gene expression Plant J. 16 1998 433 442
    • (1998) Plant J. , vol.16 , pp. 433-442
    • Gilmour, S.J.1    Zarka, D.G.2    Stockinger, E.J.3    Salazar, M.P.4    Houghton, J.M.5    Thomashow, M.F.6
  • 88
    • 0034527513 scopus 로고    scopus 로고
    • Overexpression of the Arabidopsis CBF3 transcriptional activator mimics multiple biochemical changes associated with cold acclimation
    • S.J. Gilmour, A.M. Sebolt, M.P. Salazar, J.D. Everard, and M.F. Thomashow Overexpression of the Arabidopsis CBF3 transcriptional activator mimics multiple biochemical changes associated with cold acclimation Plant Physiol. 124 2000 1854 1865
    • (2000) Plant Physiol. , vol.124 , pp. 1854-1865
    • Gilmour, S.J.1    Sebolt, A.M.2    Salazar, M.P.3    Everard, J.D.4    Thomashow, M.F.5
  • 89
    • 0034016129 scopus 로고    scopus 로고
    • Organization and expression of two Arabidopsis DREB2 genes encoding DRE-binding proteins involved in dehydration- and high-salinity-responsive gene expression
    • K. Nakashima, Z.K. Shinwari, Y. Sakuma, M. Seki, S. Miura, K. Shinozaki, and K. Yamaguchi-Shinozaki Organization and expression of two Arabidopsis DREB2 genes encoding DRE-binding proteins involved in dehydration- and high-salinity-responsive gene expression Plant Mol. Biol. 42 2000 657 665
    • (2000) Plant Mol. Biol. , vol.42 , pp. 657-665
    • Nakashima, K.1    Shinwari, Z.K.2    Sakuma, Y.3    Seki, M.4    Miura, S.5    Shinozaki, K.6    Yamaguchi-Shinozaki, K.7
  • 91
    • 0036733251 scopus 로고    scopus 로고
    • Opposite changes in membrane fluidity mimic cold and heat stress activation of distinct plant MAP kinase pathways
    • V. Sangwan, B.L. Orvar, J. Beyerly, H. Hirt, and R.S. Dhindsa Opposite changes in membrane fluidity mimic cold and heat stress activation of distinct plant MAP kinase pathways Plant J. 31 2002 629 638
    • (2002) Plant J. , vol.31 , pp. 629-638
    • Sangwan, V.1    Orvar, B.L.2    Beyerly, J.3    Hirt, H.4    Dhindsa, R.S.5
  • 92
    • 0037034931 scopus 로고    scopus 로고
    • Identification of a cold receptor reveals a general role for TRP channels in thermosensation
    • D.D. McKemy, W.M. Neuhausser, and D. Julius Identification of a cold receptor reveals a general role for TRP channels in thermosensation Nature 416 2002 52 58
    • (2002) Nature , vol.416 , pp. 52-58
    • McKemy, D.D.1    Neuhausser, W.M.2    Julius, D.3
  • 93
    • 0041878279 scopus 로고    scopus 로고
    • Lessons from peppers and peppermint: The molecular logic of thermosensation
    • S.E. Jordt, D.D. McKemy, and D. Julius Lessons from peppers and peppermint: the molecular logic of thermosensation Curr. Opin. Neurobiol. 13 2003 487 492
    • (2003) Curr. Opin. Neurobiol. , vol.13 , pp. 487-492
    • Jordt, S.E.1    McKemy, D.D.2    Julius, D.3
  • 99
    • 0035321068 scopus 로고    scopus 로고
    • Signal processing and transduction in plant cells: The end of the beginning?
    • S. Gilroy, and A. Trewavas Signal processing and transduction in plant cells: the end of the beginning? Nat. Rev., Mol. Cell Biol. 2 2001 307 314
    • (2001) Nat. Rev., Mol. Cell Biol. , vol.2 , pp. 307-314
    • Gilroy, S.1    Trewavas, A.2
  • 100
    • 0030096580 scopus 로고    scopus 로고
    • Cold calcium signaling in Arabidopsis involves two cellular pools and a change in calcium signature after acclimation
    • H. Knight, A.J. Trewavas, and M.R. Knight Cold calcium signaling in Arabidopsis involves two cellular pools and a change in calcium signature after acclimation Plant Cell 8 1996 489 503
    • (1996) Plant Cell , vol.8 , pp. 489-503
    • Knight, H.1    Trewavas, A.J.2    Knight, M.R.3
  • 102
    • 12044259918 scopus 로고
    • Cold-induced changes in freezing tolerance, protein phosphorylation, and gene expression (evidence for a role of calcium)
    • A.F. Monroy, F. Sarhan, and R.S. Dhindsa Cold-induced changes in freezing tolerance, protein phosphorylation, and gene expression (evidence for a role of calcium) Plant Physiol. 102 1993 1227 1235
    • (1993) Plant Physiol. , vol.102 , pp. 1227-1235
    • Monroy, A.F.1    Sarhan, F.2    Dhindsa, R.S.3
  • 104
    • 0028951033 scopus 로고
    • The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP
    • P.N. Danese, W.B. Snyder, C.L. Cosma, L.J. Davis, and T.J. Silhavy The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP Genes Dev. 9 1995 387 398
    • (1995) Genes Dev. , vol.9 , pp. 387-398
    • Danese, P.N.1    Snyder, W.B.2    Cosma, C.L.3    Davis, L.J.4    Silhavy, T.J.5
  • 105
    • 0031905590 scopus 로고    scopus 로고
    • CpxP, a stress-combative member of the Cpx regulon
    • P.N. Danese, and T.J. Silhavy CpxP, a stress-combative member of the Cpx regulon J. Bacteriol. 180 1998 831 839
    • (1998) J. Bacteriol. , vol.180 , pp. 831-839
    • Danese, P.N.1    Silhavy, T.J.2
  • 106
    • 0034780493 scopus 로고    scopus 로고
    • Periplasmic stress and ECF sigma factors
    • T.L. Raivio, and T.J. Silhavy Periplasmic stress and ECF sigma factors Annu. Rev. Microbiol. 55 2001 591 624
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 591-624
    • Raivio, T.L.1    Silhavy, T.J.2
  • 107
    • 0037384456 scopus 로고    scopus 로고
    • Signal detection and target gene induction by the CpxRA two-component system
    • P.A. DiGiuseppe, and T.J. Silhavy Signal detection and target gene induction by the CpxRA two-component system J. Bacteriol. 185 2003 2432 2440
    • (2003) J. Bacteriol. , vol.185 , pp. 2432-2440
    • Digiuseppe, P.A.1    Silhavy, T.J.2
  • 108
    • 0030998321 scopus 로고    scopus 로고
    • The sigma(E) and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli
    • P.N. Danese, and T.J. Silhavy The sigma(E) and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli Genes Dev. 11 1997 1183 1193
    • (1997) Genes Dev. , vol.11 , pp. 1183-1193
    • Danese, P.N.1    Silhavy, T.J.2
  • 109
    • 0030763077 scopus 로고    scopus 로고
    • The response to extracytoplasmic stress in Escherichia coli is controlled by partially overlapping pathways
    • L. Connolly, A. De Las Penas, B.M. Alba, and C.A. Gross The response to extracytoplasmic stress in Escherichia coli is controlled by partially overlapping pathways Genes Dev. 11 1997 2012 2021
    • (1997) Genes Dev. , vol.11 , pp. 2012-2021
    • Connolly, L.1    De Las Penas, A.2    Alba, B.M.3    Gross, C.A.4
  • 110
    • 0030992719 scopus 로고    scopus 로고
    • Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system
    • J. Pogliano, A.S. Lynch, D. Belin, E.C. Lin, and J. Beckwith Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system Genes Dev. 11 1997 1169 1182
    • (1997) Genes Dev. , vol.11 , pp. 1169-1182
    • Pogliano, J.1    Lynch, A.S.2    Belin, D.3    Lin, E.C.4    Beckwith, J.5
  • 111
    • 0031039158 scopus 로고    scopus 로고
    • The Cpx two-component signal transduction pathway is activated in Escherichia coli mutant strains lacking phosphatidylethanolamine
    • E. Mileykovskaya, and W. Dowhan The Cpx two-component signal transduction pathway is activated in Escherichia coli mutant strains lacking phosphatidylethanolamine J. Bacteriol. 179 1997 1029 1034
    • (1997) J. Bacteriol. , vol.179 , pp. 1029-1034
    • Mileykovskaya, E.1    Dowhan, W.2
  • 112
    • 0033968654 scopus 로고    scopus 로고
    • Presence of the Cpx system in bacteria
    • P. De Wulf, B.J. Akerley, and E.C. Lin Presence of the Cpx system in bacteria Microbiology 146 2000 247 248
    • (2000) Microbiology , vol.146 , pp. 247-248
    • De Wulf, P.1    Akerley, B.J.2    Lin, E.C.3
  • 113
    • 0037155137 scopus 로고    scopus 로고
    • Transcriptional activation of a heat-shock gene, lonD, of Myxococcus xanthus by a two-component histidine-aspartate phosphorelay system
    • T. Ueki, and S. Inouye Transcriptional activation of a heat-shock gene, lonD, of Myxococcus xanthus by a two-component histidine-aspartate phosphorelay system J. Biol. Chem. 277 2002 6170 6177
    • (2002) J. Biol. Chem. , vol.277 , pp. 6170-6177
    • Ueki, T.1    Inouye, S.2
  • 115
    • 0030614762 scopus 로고    scopus 로고
    • The stpA gene from Synechocystis sp. strain PCC 6803 encodes the glucosylglycerol-phosphate phosphatase involved in cyanobacterial osmotic response to salt shock
    • M. Hagemann, A. Schoor, R. Jeanjean, E. Zuther, and F. Joset The stpA gene from Synechocystis sp. strain PCC 6803 encodes the glucosylglycerol- phosphate phosphatase involved in cyanobacterial osmotic response to salt shock J. Bacteriol. 179 1997 1727 1733
    • (1997) J. Bacteriol. , vol.179 , pp. 1727-1733
    • Hagemann, M.1    Schoor, A.2    Jeanjean, R.3    Zuther, E.4    Joset, F.5
  • 116
    • 0032731211 scopus 로고    scopus 로고
    • Expression of the ggpS gene, involved in osmolyte synthesis in the marine cyanobacterium Synechococcus sp. strain PCC 7002, revealed regulatory differences between this strain and the freshwater strain Synechocystis sp. strain PCC 6803
    • F. Engelbrecht, K. Marin, and M. Hagemann Expression of the ggpS gene, involved in osmolyte synthesis in the marine cyanobacterium Synechococcus sp. strain PCC 7002, revealed regulatory differences between this strain and the freshwater strain Synechocystis sp. strain PCC 6803 Appl. Environ. Microbiol. 65 1999 4822 4829
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 4822-4829
    • Engelbrecht, F.1    Marin, K.2    Hagemann, M.3
  • 119
    • 0034708436 scopus 로고    scopus 로고
    • The transcriptional response of Saccharomyces cerevisiae to osmotic shock. Hot1p and Msn2p/Msn4p are required for the induction of subsets of high-osmolarity glycerol pathway-dependent genes
    • M. Rep, M. Krantz, J.M. Thevelein, and S. Hohmann The transcriptional response of Saccharomyces cerevisiae to osmotic shock. Hot1p and Msn2p/Msn4p are required for the induction of subsets of high-osmolarity glycerol pathway-dependent genes J. Biol. Chem. 275 2000 8290 8300
    • (2000) J. Biol. Chem. , vol.275 , pp. 8290-8300
    • Rep, M.1    Krantz, M.2    Thevelein, J.M.3    Hohmann, S.4
  • 120
    • 0035844224 scopus 로고    scopus 로고
    • Transcript expression in Saccharomyces cerevisiae at high salinity
    • J. Yale, and H.J. Bohnert Transcript expression in Saccharomyces cerevisiae at high salinity J. Biol. Chem. 276 2001 15996 16007
    • (2001) J. Biol. Chem. , vol.276 , pp. 15996-16007
    • Yale, J.1    Bohnert, H.J.2
  • 121
    • 0035037364 scopus 로고    scopus 로고
    • DNA microarray analysis of cyanobacterial gene expression during acclimation to high light
    • Y. Hihara, A. Kamei, M. Kanehisa, A. Kaplan, and M. Ikeuchi DNA microarray analysis of cyanobacterial gene expression during acclimation to high light Plant Cell 13 2001 793 806
    • (2001) Plant Cell , vol.13 , pp. 793-806
    • Hihara, Y.1    Kamei, A.2    Kanehisa, M.3    Kaplan, A.4    Ikeuchi, M.5
  • 122
    • 0036433494 scopus 로고    scopus 로고
    • The histidine kinase Hik33 perceives osmotic stress and cold stress in Synechocystis sp., PCC 6803
    • K. Mikami, Y. Kanesaki, I. Suzuki, and N. Murata The histidine kinase Hik33 perceives osmotic stress and cold stress in Synechocystis sp., PCC 6803 Mol. Microbiol. 46 2003 905 915
    • (2003) Mol. Microbiol. , vol.46 , pp. 905-915
    • Mikami, K.1    Kanesaki, Y.2    Suzuki, I.3    Murata, N.4
  • 123
    • 0037369852 scopus 로고    scopus 로고
    • DNA microarray analysis of redox-responsive genes in the genome of the cyanobacterium Synechocystis sp. strain PCC 6803
    • Y. Hihara, K. Sonoike, M. Kanehisa, and M. Ikeuchi DNA microarray analysis of redox-responsive genes in the genome of the cyanobacterium Synechocystis sp. strain PCC 6803 J. Bacteriol. 185 2003 1719 1725
    • (2003) J. Bacteriol. , vol.185 , pp. 1719-1725
    • Hihara, Y.1    Sonoike, K.2    Kanehisa, M.3    Ikeuchi, M.4
  • 125
    • 0027454334 scopus 로고
    • Functional reconstitution of the putative Escherichia coli osmosensor, KdpD, into liposomes
    • K. Nakashima, A. Sugiura, and T. Mizuno Functional reconstitution of the putative Escherichia coli osmosensor, KdpD, into liposomes J. Biochem. 114 1993 615 621
    • (1993) J. Biochem. , vol.114 , pp. 615-621
    • Nakashima, K.1    Sugiura, A.2    Mizuno, T.3
  • 126
    • 0034074051 scopus 로고    scopus 로고
    • A monomeric histidine kinase derived from EnvZ, an Escherichia coli osmosensor
    • L. Qin, R. Dutta, H. Kurokawa, M. Ikura, and M. Inouye A monomeric histidine kinase derived from EnvZ, an Escherichia coli osmosensor Mol. Microbiol. 36 2000 24 32
    • (2000) Mol. Microbiol. , vol.36 , pp. 24-32
    • Qin, L.1    Dutta, R.2    Kurokawa, H.3    Ikura, M.4    Inouye, M.5
  • 127
    • 0025895382 scopus 로고
    • Transmembrane signal transduction and osmoregulation in Escherichia coli. Functional importance of the periplasmic domain of the membrane-located protein kinase, EnvZ
    • S. Tokishita, A. Kojima, H. Aiba, and T. Mizuno Transmembrane signal transduction and osmoregulation in Escherichia coli. Functional importance of the periplasmic domain of the membrane-located protein kinase, EnvZ J. Biol. Chem. 266 1991 6780 6785
    • (1991) J. Biol. Chem. , vol.266 , pp. 6780-6785
    • Tokishita, S.1    Kojima, A.2    Aiba, H.3    Mizuno, T.4
  • 128
    • 0027511120 scopus 로고
    • Signal transduction between the two regulatory components involved in the regulation of the kdpABC operon in Escherichia coli: Phosphorylation-dependent functioning of the positive regulator, KdpE
    • K. Nakashima, A. Sugiura, K. Kanamaru, and T. Mizuno Signal transduction between the two regulatory components involved in the regulation of the kdpABC operon in Escherichia coli: phosphorylation-dependent functioning of the positive regulator, KdpE Mol. Microbiol. 7 1993 109 116
    • (1993) Mol. Microbiol. , vol.7 , pp. 109-116
    • Nakashima, K.1    Sugiura, A.2    Kanamaru, K.3    Mizuno, T.4
  • 129
    • 0025785290 scopus 로고
    • Osmoregulatory expression of the porin genes in Escherichia coli: Evidence for signal titration in the signal transduction through EnvZ-OmpR phosphotransfer
    • K. Nakashima, K. Kanamaru, H. Aiba, and T. Mizuno Osmoregulatory expression of the porin genes in Escherichia coli: evidence for signal titration in the signal transduction through EnvZ-OmpR phosphotransfer FEMS Microbiol. Lett. 66 1991 43 47
    • (1991) FEMS Microbiol. Lett. , vol.66 , pp. 43-47
    • Nakashima, K.1    Kanamaru, K.2    Aiba, H.3    Mizuno, T.4
  • 130
    • 0034691129 scopus 로고    scopus 로고
    • Osmoregulated ABC-transport system of Lactococcus lactis senses water stress via changes in the physical state of the membrane
    • T. van der Heide, and B. Poolman Osmoregulated ABC-transport system of Lactococcus lactis senses water stress via changes in the physical state of the membrane Proc. Natl. Acad. Sci. U. S. A. 97 2000 7102 7106
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 7102-7106
    • Van Der Heide, T.1    Poolman, B.2
  • 131
    • 0037126588 scopus 로고    scopus 로고
    • On the osmotic signal and osmosensing mechanism of an ABC transport system for glycine betaine
    • T. van der Heide, M.C. Stuart, and B. Poolman On the osmotic signal and osmosensing mechanism of an ABC transport system for glycine betaine EMBO J. 20 2001 7022 7032
    • (2001) EMBO J. , vol.20 , pp. 7022-7032
    • Van Der Heide, T.1    Stuart, M.C.2    Poolman, B.3
  • 132
    • 0034282495 scopus 로고    scopus 로고
    • Yeast Cdc42 GTPase and Ste20 PAK-like kinase regulate Sho1-dependent activation of the Hog1 MAP kinase pathway
    • D.C. Raitt, F. Posas, and H. Saito Yeast Cdc42 GTPase and Ste20 PAK-like kinase regulate Sho1-dependent activation of the Hog1 MAP kinase pathway EMBO J. 19 2000 4623 4631
    • (2000) EMBO J. , vol.19 , pp. 4623-4631
    • Raitt, D.C.1    Posas, F.2    Saito, H.3
  • 133
    • 0027507956 scopus 로고
    • A yeast protein similar to bacterial two-component regulators
    • I.M. Ota, and A. Varshavsky A yeast protein similar to bacterial two-component regulators Science 262 1993 566 569
    • (1993) Science , vol.262 , pp. 566-569
    • Ota, I.M.1    Varshavsky, A.2
  • 134
    • 0028228109 scopus 로고
    • A two-component system that regulates an osmosensing MAP kinase cascade in yeast
    • T. Maeda, S.M. Wurgler-Murphy, and H. Saito A two-component system that regulates an osmosensing MAP kinase cascade in yeast Nature 369 1994 242 245
    • (1994) Nature , vol.369 , pp. 242-245
    • Maeda, T.1    Wurgler-Murphy, S.M.2    Saito, H.3
  • 135
    • 0030595378 scopus 로고    scopus 로고
    • Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN1-YPD1-SSK1 "two-component" osmosensor
    • F. Posas, S.M. Wurgler-Murphy, T. Maeda, E.A. Witten, T.C. Thai, and H. Saito Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN1-YPD1-SSK1 "two-component" osmosensor Cell 86 1996 865 875
    • (1996) Cell , vol.86 , pp. 865-875
    • Posas, F.1    Wurgler-Murphy, S.M.2    Maeda, T.3    Witten, E.A.4    Thai, T.C.5    Saito, H.6
  • 136
    • 0032814143 scopus 로고    scopus 로고
    • Osmotic stress-induced gene expression in Saccharomyces cerevisiae requires Msn1p and the novel nuclear factor Hot1p
    • M. Rep, V. Reiser, U. Gartner, J.M. Thevelein, S. Hohmann, G. Ammerer, and H. Ruis Osmotic stress-induced gene expression in Saccharomyces cerevisiae requires Msn1p and the novel nuclear factor Hot1p Mol. Cell. Biol. 19 1999 5474 5485
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5474-5485
    • Rep, M.1    Reiser, V.2    Gartner, U.3    Thevelein, J.M.4    Hohmann, S.5    Ammerer, G.6    Ruis, H.7
  • 137
    • 0033941856 scopus 로고    scopus 로고
    • Ionic and osmotic effects of NaCl-induced inactivation of photosystems I and II in Synechococcus sp.
    • S.I. Allakhverdiev, A. Sakamoto, Y. Nishiyama, M. Inaba, and N. Murata Ionic and osmotic effects of NaCl-induced inactivation of photosystems I and II in Synechococcus sp. Plant Physiol. 123 2000 1047 1056
    • (2000) Plant Physiol. , vol.123 , pp. 1047-1056
    • Allakhverdiev, S.I.1    Sakamoto, A.2    Nishiyama, Y.3    Inaba, M.4    Murata, N.5
  • 138
    • 0036886037 scopus 로고    scopus 로고
    • Formation of the stoichiometric complex of EnvZ, a histidine kinase, with its response regulator, OmpR
    • T. Yoshida, L. Qin, and M. Inouye Formation of the stoichiometric complex of EnvZ, a histidine kinase, with its response regulator, OmpR Mol. Microbiol. 46 2002 1273 1282
    • (2002) Mol. Microbiol. , vol.46 , pp. 1273-1282
    • Yoshida, T.1    Qin, L.2    Inouye, M.3
  • 139
    • 0038529775 scopus 로고    scopus 로고
    • Cysteine-scanning analysis of the dimerization domain of EnvZ, an osmosensing histidine kinase
    • L. Qin, S. Cai, Y. Zhu, and M. Inouye Cysteine-scanning analysis of the dimerization domain of EnvZ, an osmosensing histidine kinase J. Bacteriol. 185 2003 3429 3435
    • (2003) J. Bacteriol. , vol.185 , pp. 3429-3435
    • Qin, L.1    Cai, S.2    Zhu, Y.3    Inouye, M.4
  • 140
    • 0037589946 scopus 로고    scopus 로고
    • Analysis of the role of the EnvZ linker region in signal transduction using a chimeric Tar/EnvZ receptor protein, Tez1
    • Y. Zhu, and M. Inouye Analysis of the role of the EnvZ linker region in signal transduction using a chimeric Tar/EnvZ receptor protein, Tez1 J. Biol. Chem. 278 2003 22812 22819
    • (2003) J. Biol. Chem. , vol.278 , pp. 22812-22819
    • Zhu, Y.1    Inouye, M.2
  • 142
    • 0028224356 scopus 로고
    • A large-conductance mechanosensitive channel in E. coli encoded by mscL alone
    • S.I. Sukharev, P. Blount, B. Martinac, F.R. Blattner, and C. Kung A large-conductance mechanosensitive channel in E. coli encoded by mscL alone Nature 368 1994 265 268
    • (1994) Nature , vol.368 , pp. 265-268
    • Sukharev, S.I.1    Blount, P.2    Martinac, B.3    Blattner, F.R.4    Kung, C.5
  • 144
    • 0035825634 scopus 로고    scopus 로고
    • The gating mechanism of the large mechanosensitive channel MscL
    • S.I. Sukharev, M. Betanzos, C.S. Chiang, and H.R. Guy The gating mechanism of the large mechanosensitive channel MscL Nature 409 2001 720 724
    • (2001) Nature , vol.409 , pp. 720-724
    • Sukharev, S.I.1    Betanzos, M.2    Chiang, C.S.3    Guy, H.R.4
  • 145
    • 0034910316 scopus 로고    scopus 로고
    • Structural models of the MscL gating mechanism
    • S. Sukharev, S.R. Durell, and H.R. Guy Structural models of the MscL gating mechanism Biophys. J. 81 2001 917 936
    • (2001) Biophys. J. , vol.81 , pp. 917-936
    • Sukharev, S.1    Durell, S.R.2    Guy, H.R.3
  • 146
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • G. Chang, R.H. Spencer, A.T. Lee, M.T. Barclay, and D.C. Rees Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel Science 282 1998 2220 2226
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 149
    • 0032844441 scopus 로고    scopus 로고
    • Bacterial mechanosensitive channels: Integrating physiology, structure and function
    • P. Blount, and P.C. Moe Bacterial mechanosensitive channels: integrating physiology, structure and function Trends Microbiol. 7 1999 420 424
    • (1999) Trends Microbiol. , vol.7 , pp. 420-424
    • Blount, P.1    Moe, P.C.2
  • 150
    • 0034613258 scopus 로고    scopus 로고
    • Correlating a protein structure with function of a bacterial mechanosensitive channel
    • P.C. Moe, G. Levin, and P. Blount Correlating a protein structure with function of a bacterial mechanosensitive channel J. Biol. Chem. 275 2000 31121 31127
    • (2000) J. Biol. Chem. , vol.275 , pp. 31121-31127
    • Moe, P.C.1    Levin, G.2    Blount, P.3
  • 152
    • 0029116626 scopus 로고
    • Membrane mechanisms and intracellular signalling in cell volume regulation
    • E.K. Hoffmann, and P.B. Dunham Membrane mechanisms and intracellular signalling in cell volume regulation Int. Rev. Cyt. 161 1995 173 262
    • (1995) Int. Rev. Cyt. , vol.161 , pp. 173-262
    • Hoffmann, E.K.1    Dunham, P.B.2
  • 153
    • 0030901623 scopus 로고    scopus 로고
    • Mechanosensitive channels of Escherichia coli: The MscL gene, protein, and activities
    • S.I. Sukharev, P. Blount, B. Martinac, and C. Kung Mechanosensitive channels of Escherichia coli: the MscL gene, protein, and activities Annu. Rev. Physiol. 59 1997 633 657
    • (1997) Annu. Rev. Physiol. , vol.59 , pp. 633-657
    • Sukharev, S.I.1    Blount, P.2    Martinac, B.3    Kung, C.4
  • 154
    • 0030934771 scopus 로고    scopus 로고
    • Molecular dissection of gating in the ClC-2 chloride channel
    • S.-E. Jordt, and T.J. Jentsch Molecular dissection of gating in the ClC-2 chloride channel EMBO J. 16 1997 1582 1592
    • (1997) EMBO J. , vol.16 , pp. 1582-1592
    • Jordt, S.-E.1    Jentsch, T.J.2
  • 155
    • 0035339231 scopus 로고    scopus 로고
    • Channel gating: Twist to open
    • P.C. Biggin, and M.S. Sansom Channel gating: twist to open Curr. Biol. 11 2001 R364 R366
    • (2001) Curr. Biol. , vol.11
    • Biggin, P.C.1    Sansom, M.S.2
  • 156
    • 0035477802 scopus 로고    scopus 로고
    • The osmoreactive betaine carrier BetP from Corynebacterium glutamicum is a sensor for cytoplasmic K
    • R. Rubenhagen, S. Morbach, and R. Kramer The osmoreactive betaine carrier BetP from Corynebacterium glutamicum is a sensor for cytoplasmic K EMBO J. 20 2001 5412 5420
    • (2001) EMBO J. , vol.20 , pp. 5412-5420
    • Rubenhagen, R.1    Morbach, S.2    Kramer, R.3
  • 157
    • 0031277694 scopus 로고    scopus 로고
    • Genetic analysis of osmotic and cold stress signal transduction in Arabidopsis: Interactions and convergence of abscisic acid-dependent and abscisic acid-independent pathways
    • M. Ishitani, L. Xiong, B. Stevenson, and J.K. Zhu Genetic analysis of osmotic and cold stress signal transduction in Arabidopsis: interactions and convergence of abscisic acid-dependent and abscisic acid-independent pathways Plant Cell 9 1997 1935 1949
    • (1997) Plant Cell , vol.9 , pp. 1935-1949
    • Ishitani, M.1    Xiong, L.2    Stevenson, B.3    Zhu, J.K.4
  • 158
    • 0032841274 scopus 로고    scopus 로고
    • Interaction of osmotic stress, temperature, and abscisic acid in the regulation of gene expression in Arabidopsis
    • L. Xiong, M. Ishitani, and J.K. Zhu Interaction of osmotic stress, temperature, and abscisic acid in the regulation of gene expression in Arabidopsis Plant Physiol. 119 1999 205 221
    • (1999) Plant Physiol. , vol.119 , pp. 205-221
    • Xiong, L.1    Ishitani, M.2    Zhu, J.K.3
  • 160
    • 0032993342 scopus 로고    scopus 로고
    • Improving plant drought, salt, and freezing tolerance by gene transfer of a single stress-inducible transcription factor
    • M. Kasuga, Q. Liu, S. Miura, K. Yamaguchi-Shinozaki, and K. Shinozaki Improving plant drought, salt, and freezing tolerance by gene transfer of a single stress-inducible transcription factor Nat. Biotechnol. 17 1999 287 291
    • (1999) Nat. Biotechnol. , vol.17 , pp. 287-291
    • Kasuga, M.1    Liu, Q.2    Miura, S.3    Yamaguchi-Shinozaki, K.4    Shinozaki, K.5
  • 162
    • 0034502592 scopus 로고    scopus 로고
    • Various abiotic stresses rapidly activate Arabidopsis MAP kinases ATMPK4 and ATMPK6
    • K. Ichimura, T. Mizoguchi, R. Yoshida, T. Yuasa, and K. Shinozaki Various abiotic stresses rapidly activate Arabidopsis MAP kinases ATMPK4 and ATMPK6 Plant J. 24 2000 655 665
    • (2000) Plant J. , vol.24 , pp. 655-665
    • Ichimura, K.1    Mizoguchi, T.2    Yoshida, R.3    Yuasa, T.4    Shinozaki, K.5
  • 163
    • 0035222207 scopus 로고    scopus 로고
    • Improving plant drought, salt and freezing tolerance by gene transfer of a single stress-inducible transcription factor
    • K. Yamaguchi-Shinozaki, and K. Shinozaki Improving plant drought, salt and freezing tolerance by gene transfer of a single stress-inducible transcription factor Novartis Found. Symp. 236 2001 176 186
    • (2001) Novartis Found. Symp. , vol.236 , pp. 176-186
    • Yamaguchi-Shinozaki, K.1    Shinozaki, K.2
  • 165
    • 0028840498 scopus 로고
    • The dspA gene product of the cyanobacterium Synechocystis sp. strain PCC 6803 influences sensitivity to chemically different growth inhibitors and has amino acid similarity to histidine protein kinases
    • V.V. Bartsevich, and S.V. Shestakov The dspA gene product of the cyanobacterium Synechocystis sp. strain PCC 6803 influences sensitivity to chemically different growth inhibitors and has amino acid similarity to histidine protein kinases Microbiology 141 1995 2915 2920
    • (1995) Microbiology , vol.141 , pp. 2915-2920
    • Bartsevich, V.V.1    Shestakov, S.V.2
  • 166
    • 0029395010 scopus 로고
    • Stress signaling in yeast
    • H. Ruis, and C. Schuller Stress signaling in yeast BioEssays 17 1995 959 965
    • (1995) BioEssays , vol.17 , pp. 959-965
    • Ruis, H.1    Schuller, C.2
  • 167
    • 0033928677 scopus 로고    scopus 로고
    • Response of Saccharomyces cerevisiae to severe osmotic stress: Evidence for a novel activation mechanism of the HOG MAP kinase pathway
    • O. van Wuytswinkel, V. Reiser, M. Siderius, M.C. Kelders, G. Ammerer, H. Ruis, and W.H. Mager Response of Saccharomyces cerevisiae to severe osmotic stress: evidence for a novel activation mechanism of the HOG MAP kinase pathway Mol. Microbiol. 37 2000 382 397
    • (2000) Mol. Microbiol. , vol.37 , pp. 382-397
    • Van Wuytswinkel, O.1    Reiser, V.2    Siderius, M.3    Kelders, M.C.4    Ammerer, G.5    Ruis, H.6    Mager, W.H.7
  • 169
    • 0033884980 scopus 로고    scopus 로고
    • Cell-type-specific calcium responses to drought, salt and cold in the Arabidopsis root
    • E. Kiegle, C.A. Moore, J. Haseloff, M.A. Tester, and M.R. Knight Cell-type-specific calcium responses to drought, salt and cold in the Arabidopsis root Plant J. 23 2000 267 278
    • (2000) Plant J. , vol.23 , pp. 267-278
    • Kiegle, E.1    Moore, C.A.2    Haseloff, J.3    Tester, M.A.4    Knight, M.R.5
  • 170
    • 0035206163 scopus 로고    scopus 로고
    • Abiotic stress signalling pathways: Specificity and cross-talk
    • H. Knight, and M.R. Knight Abiotic stress signalling pathways: specificity and cross-talk Trends Plant Sci. 6 2001 262 267
    • (2001) Trends Plant Sci. , vol.6 , pp. 262-267
    • Knight, H.1    Knight, M.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.