메뉴 건너뛰기




Volumn 111, Issue 37, 2014, Pages E3860-E3869

Utilization of extracellular information before ligand-receptor binding reaches equilibrium expands and shifts the input dynamic range

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; LIGAND; PROTEIN BINDING;

EID: 84907289342     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1322761111     Document Type: Article
Times cited : (29)

References (84)
  • 2
    • 0015397646 scopus 로고
    • The gradient-sensing mechanism in bacterial chemotaxis
    • Macnab RM, Koshland DE, Jr (1972) The gradient-sensing mechanism in bacterial chemotaxis. Proc Natl Acad Sci USA 69(9):2509-2512.
    • (1972) Proc Natl Acad Sci USA , vol.69 , Issue.9 , pp. 2509-2512
    • Macnab, R.M.1    Koshland, D.E.2
  • 3
    • 77952911072 scopus 로고    scopus 로고
    • Eukaryotic chemotaxis: A network of signaling pathways controls motility, directional sensing, and polarity
    • Swaney KF, Huang CH, Devreotes PN (2010) Eukaryotic chemotaxis: A network of signaling pathways controls motility, directional sensing, and polarity. Annu Rev Biophys 39:265-289.
    • (2010) Annu Rev Biophys , vol.39 , pp. 265-289
    • Swaney, K.F.1    Huang, C.H.2    Devreotes, P.N.3
  • 4
    • 0027218647 scopus 로고
    • Polarization of yeast cells in spatial gradients of alpha mating factor
    • Segall JE (1993) Polarization of yeast cells in spatial gradients of alpha mating factor. Proc Natl Acad Sci USA 90(18):8332-8336.
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.18 , pp. 8332-8336
    • Segall, J.E.1
  • 5
    • 0024817426 scopus 로고
    • Chemotactic response of neutrophils
    • Zigmond SH (1989) Chemotactic response of neutrophils. Am J Respir Cell Mol Biol 1(6):451-453.
    • (1989) Am J Respir Cell Mol Biol , vol.1 , Issue.6 , pp. 451-453
    • Zigmond, S.H.1
  • 6
    • 77957266177 scopus 로고    scopus 로고
    • Chemical gradients and chemotropism in yeast
    • Arkowitz RA (2009) Chemical gradients and chemotropism in yeast. Cold Spring Harb Perspect Biol 1(2):a001958.
    • (2009) Cold Spring Harb Perspect Biol , vol.1 , Issue.2 , pp. a001958
    • Arkowitz, R.A.1
  • 7
  • 8
    • 0025598073 scopus 로고
    • Courtship in S. Cerevisiae: Both cell types choose mating partners by responding to the strongest pheromone signal
    • Jackson CL, Hartwell LH (1990) Courtship in S. cerevisiae: Both cell types choose mating partners by responding to the strongest pheromone signal. Cell 63(5): 1039-1051.
    • (1990) Cell , vol.63 , Issue.5 , pp. 1039-1051
    • Jackson, C.L.1    Hartwell, L.H.2
  • 9
    • 0021070404 scopus 로고
    • Binding of alpha-factor pheromone to yeast a cells: Chemical and genetic evidence for an alpha-factor receptor
    • Jenness DD, Burkholder AC, Hartwell LH (1983) Binding of alpha-factor pheromone to yeast a cells: Chemical and genetic evidence for an alpha-factor receptor. Cell 35(2 Pt 1):521-529.
    • (1983) Cell , vol.35 , Issue.2 , pp. 521-529
    • Jenness, D.D.1    Burkholder, A.C.2    Hartwell, L.H.3
  • 10
    • 13144302852 scopus 로고    scopus 로고
    • A role for the yeast actin cytoskeleton in pheromone receptor clustering and signalling
    • Ayscough KR, Drubin DG (1998) A role for the yeast actin cytoskeleton in pheromone receptor clustering and signalling. Curr Biol 8(16):927-930.
    • (1998) Curr Biol , vol.8 , Issue.16 , pp. 927-930
    • Ayscough, K.R.1    Drubin, D.G.2
  • 11
    • 57349179035 scopus 로고    scopus 로고
    • Robust spatial sensing of mating pheromone gradients by yeast cells
    • Moore TI, Chou CS, Nie Q, Jeon NL, Yi TM (2008) Robust spatial sensing of mating pheromone gradients by yeast cells. PLoS ONE 3(12):e3865.
    • (2008) PLoS ONE , vol.3 , Issue.12 , pp. e3865
    • Moore, T.I.1    Chou, C.S.2    Nie, Q.3    Jeon, N.L.4    Yi, T.M.5
  • 12
    • 26944476331 scopus 로고    scopus 로고
    • Regulated cell-to-cell variation in a cell-fate decision system
    • Colman-Lerner A, et al. (2005) Regulated cell-to-cell variation in a cell-fate decision system. Nature 437(7059):699-706.
    • (2005) Nature , vol.437 , Issue.7059 , pp. 699-706
    • Colman-Lerner, A.1
  • 13
    • 0141703270 scopus 로고    scopus 로고
    • A quantitative characterization of the yeast heterotrimeric G protein cycle
    • Yi TM, Kitano H, Simon MI (2003) A quantitative characterization of the yeast heterotrimeric G protein cycle. Proc Natl Acad Sci USA 100(19):10764-10769.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.19 , pp. 10764-10769
    • Yi, T.M.1    Kitano, H.2    Simon, M.I.3
  • 14
    • 57649130757 scopus 로고    scopus 로고
    • Negative feedback that improves information transmission in yeast signalling
    • Yu RC, et al. (2008) Negative feedback that improves information transmission in yeast signalling. Nature 456(7223):755-761.
    • (2008) Nature , vol.456 , Issue.7223 , pp. 755-761
    • Yu, R.C.1
  • 15
    • 0022630554 scopus 로고
    • Binding of alpha-factor pheromone to Saccharomyces cerevisiae a cells: Dissociation constant and number of binding sites
    • Jenness DD, Burkholder AC, Hartwell LH (1986) Binding of alpha-factor pheromone to Saccharomyces cerevisiae a cells: Dissociation constant and number of binding sites. Mol Cell Biol 6(1):318-320.
    • (1986) Mol Cell Biol , vol.6 , Issue.1 , pp. 318-320
    • Jenness, D.D.1    Burkholder, A.C.2    Hartwell, L.H.3
  • 16
    • 6344228392 scopus 로고    scopus 로고
    • A fluorescent alpha-factor analogue exhibits multiple steps on binding to its G protein coupled receptor in yeast
    • Bajaj A, et al. (2004) A fluorescent alpha-factor analogue exhibits multiple steps on binding to its G protein coupled receptor in yeast. Biochemistry 43(42):13564-13578.
    • (2004) Biochemistry , vol.43 , Issue.42 , pp. 13564-13578
    • Bajaj, A.1
  • 17
    • 0022572297 scopus 로고
    • Binding constants of IgE receptors on human blood basophils for IgE
    • Pruzansky JJ, Patterson R (1986) Binding constants of IgE receptors on human blood basophils for IgE. Immunology 58(2):257-262.
    • (1986) Immunology , vol.58 , Issue.2 , pp. 257-262
    • Pruzansky, J.J.1    Patterson, R.2
  • 18
    • 0018910131 scopus 로고
    • Purification of a functional mouse Fc receptor through the use of a monoclonal antibody
    • Mellman IS, Unkeless JC (1980) Purification of a functional mouse Fc receptor through the use of a monoclonal antibody. J Exp Med 152(4):1048-1069.
    • (1980) J Exp Med , vol.152 , Issue.4 , pp. 1048-1069
    • Mellman, I.S.1    Unkeless, J.C.2
  • 19
    • 0025236913 scopus 로고
    • Cannabinoid receptor localization in brain
    • HerkenhamM, et al. (1990) Cannabinoid receptor localization in brain. Proc Natl Acad Sci USA 87(5):1932-1936.
    • (1990) Proc Natl Acad Sci USA , vol.87 , Issue.5 , pp. 1932-1936
    • Herkenham, M.1
  • 20
    • 0023601839 scopus 로고
    • The interleukin 2 receptor. Functional consequences of its bimolecular structure
    • Wang HM, Smith KA (1987) The interleukin 2 receptor. Functional consequences of its bimolecular structure. J Exp Med 166(4):1055-1069.
    • (1987) J Exp Med , vol.166 , Issue.4 , pp. 1055-1069
    • Wang, H.M.1    Smith, K.A.2
  • 21
    • 0019945739 scopus 로고
    • Characterization of coexisting alpha 1- and beta 2-adrenergic receptors on a cloned muscle cell line, BC3H-1
    • Hughes RJ, Boyle MR, Brown RD, Taylor P, Insel PA (1982) Characterization of coexisting alpha 1- and beta 2-adrenergic receptors on a cloned muscle cell line, BC3H-1. Mol Pharmacol 22(2):258-266.
    • (1982) Mol Pharmacol , vol.22 , Issue.2 , pp. 258-266
    • Hughes, R.J.1    Boyle, M.R.2    Brown, R.D.3    Taylor, P.4    Insel, P.A.5
  • 22
    • 0022406361 scopus 로고
    • Kinetic identification of a twostate glucagon receptor system in isolated hepatocytes. Interconversion of homogeneous receptors
    • Horwitz EM, Jenkins WT, Hoosein NM, Gurd RS (1985) Kinetic identification of a twostate glucagon receptor system in isolated hepatocytes. Interconversion of homogeneous receptors. J Biol Chem 260(16):9307-9315.
    • (1985) J Biol Chem , vol.260 , Issue.16 , pp. 9307-9315
    • Horwitz, E.M.1    Jenkins, W.T.2    Hoosein, N.M.3    Gurd, R.S.4
  • 23
    • 0021992301 scopus 로고
    • Formyl peptide chemotaxis receptors on the rat neutrophil: Experimental evidence for negative cooperativity
    • Marasco WA, Feltner DE, Ward PA (1985) Formyl peptide chemotaxis receptors on the rat neutrophil: Experimental evidence for negative cooperativity. J Cell Biochem27(4):359-375.
    • (1985) J Cell Biochem , vol.27 , Issue.4 , pp. 359-375
    • Marasco, W.A.1    Feltner, D.E.2    Ward, P.A.3
  • 24
    • 0024364294 scopus 로고
    • Binding, internalization, and intracellular processing of proteins interacting with recycling receptors. A kinetic analysis
    • Bajzer Z, Myers AC, Vuk-Pavlovic S (1989) Binding, internalization, and intracellular processing of proteins interacting with recycling receptors. A kinetic analysis. J Biol Chem 264(23):13623-13631.
    • (1989) J Biol Chem , vol.264 , Issue.23 , pp. 13623-13631
    • Bajzer, Z.1    Myers, A.C.2    Vuk-Pavlovic, S.3
  • 25
    • 0020550999 scopus 로고
    • Kinetics of internalization and recycling of transferrin and the transferrin receptor in a human hepatoma cell line. Effect of lysosomotropic agents
    • Ciechanover A, Schwartz AL, Dautry-Varsat A, Lodish HF (1983) Kinetics of internalization and recycling of transferrin and the transferrin receptor in a human hepatoma cell line. Effect of lysosomotropic agents. J Biol Chem 258(16):9681-9689.
    • (1983) J Biol Chem , vol.258 , Issue.16 , pp. 9681-9689
    • Ciechanover, A.1    Schwartz, A.L.2    Dautry-Varsat, A.3    Lodish, H.F.4
  • 26
    • 0025240654 scopus 로고
    • Rate constants for binding, dissociation, and internalization of EGF: Effect of receptor occupancy and ligand concentration
    • Waters CM, Oberg KC, Carpenter G, Overholser KA (1990) Rate constants for binding, dissociation, and internalization of EGF: Effect of receptor occupancy and ligand concentration. Biochemistry 29(14):3563-3569.
    • (1990) Biochemistry , vol.29 , Issue.14 , pp. 3563-3569
    • Waters, C.M.1    Oberg, K.C.2    Carpenter, G.3    Overholser, K.A.4
  • 27
    • 0022973333 scopus 로고
    • Kinetics of insulin binding to rat white fat cells at 15 degrees C
    • Lipkin EW, Teller DC, de Haën C (1986) Kinetics of insulin binding to rat white fat cells at 15 degrees C. J Biol Chem 261(4):1702-1711.
    • (1986) J Biol Chem , vol.261 , Issue.4 , pp. 1702-1711
    • Lipkin, E.W.1    Teller, D.C.2    De Haën, C.3
  • 28
    • 0020026141 scopus 로고
    • Kinetic analysis of chemotactic peptide receptor modulation
    • Zigmond SH, Sullivan SJ, Lauffenburger DA (1982) Kinetic analysis of chemotactic peptide receptor modulation. J Cell Biol 92(1):34-43.
    • (1982) J Cell Biol , vol.92 , Issue.1 , pp. 34-43
    • Zigmond, S.H.1    Sullivan, S.J.2    Lauffenburger, D.A.3
  • 29
    • 0021979244 scopus 로고
    • The interaction of plasma fibronectin with fibroblastic cells in suspension
    • Akiyama SK, Yamada KM (1985) The interaction of plasma fibronectin with fibroblastic cells in suspension. J Biol Chem 260(7):4492-4500.
    • (1985) J Biol Chem , vol.260 , Issue.7 , pp. 4492-4500
    • Akiyama, S.K.1    Yamada, K.M.2
  • 30
    • 0028589333 scopus 로고
    • Kinetics of T-cell receptor binding to peptide/I-Ek complexes: Correlation of the dissociation rate with T-cell responsiveness
    • Matsui K, Boniface JJ, Steffner P, Reay PA, Davis MM (1994) Kinetics of T-cell receptor binding to peptide/I-Ek complexes: Correlation of the dissociation rate with T-cell responsiveness. Proc Natl Acad Sci USA 91(26):12862-12866.
    • (1994) Proc Natl Acad Sci USA , vol.91 , Issue.26 , pp. 12862-12866
    • Matsui, K.1    Boniface, J.J.2    Steffner, P.3    Reay, P.A.4    Davis, M.M.5
  • 31
    • 0022386033 scopus 로고
    • Competitive binding kinetics in ligandreceptor- competitor systems. Rate parameters for unlabeled ligands for the formyl peptide receptor
    • Sklar LA, Sayre J, McNeil VM, Finney DA (1985) Competitive binding kinetics in ligandreceptor- competitor systems. Rate parameters for unlabeled ligands for the formyl peptide receptor. Mol Pharmacol 28(4):323-330.
    • (1985) Mol Pharmacol , vol.28 , Issue.4 , pp. 323-330
    • Sklar, L.A.1    Sayre, J.2    McNeil, V.M.3    Finney, D.A.4
  • 32
    • 0035955356 scopus 로고    scopus 로고
    • Single-molecule analysis of chemotactic signaling in Dictyostelium cells
    • Ueda M, Sako Y, Tanaka T, Devreotes P, Yanagida T (2001) Single-molecule analysis of chemotactic signaling in Dictyostelium cells. Science 294(5543):864-867.
    • (2001) Science , vol.294 , Issue.5543 , pp. 864-867
    • Ueda, M.1    Sako, Y.2    Tanaka, T.3    Devreotes, P.4    Yanagida, T.5
  • 33
    • 0028793124 scopus 로고
    • Mutagenesis in the C-terminal region of human interleukin 5 reveals a central patch for receptor alpha chain recognition
    • Morton T, Li J, Cook R, Chaiken I (1995) Mutagenesis in the C-terminal region of human interleukin 5 reveals a central patch for receptor alpha chain recognition. Proc Natl Acad Sci USA 92(24):10879-10883.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.24 , pp. 10879-10883
    • Morton, T.1    Li, J.2    Cook, R.3    Chaiken, I.4
  • 35
    • 20844434337 scopus 로고    scopus 로고
    • A FlAsH-based FRET approach to determine G proteincoupled receptor activation in living cells
    • Hoffmann C, et al. (2005) A FlAsH-based FRET approach to determine G proteincoupled receptor activation in living cells. Nat Methods 2(3):171-176.
    • (2005) Nat Methods , vol.2 , Issue.3 , pp. 171-176
    • Hoffmann, C.1
  • 36
    • 0036460594 scopus 로고    scopus 로고
    • Control of kinetic properties of GluR2 flop AMPA-type channels: Impact of R/G nuclear editing
    • Krampfl K, et al. (2002) Control of kinetic properties of GluR2 flop AMPA-type channels: Impact of R/G nuclear editing. Eur J Neurosci 15(1):51-62.
    • (2002) Eur J Neurosci , vol.15 , Issue.1 , pp. 51-62
    • Krampfl, K.1
  • 37
    • 33645801592 scopus 로고    scopus 로고
    • Spatial dynamics of receptor-mediated endocytic trafficking in budding yeast revealed by using fluorescent alpha-factor derivatives
    • Toshima JY, et al. (2006) Spatial dynamics of receptor-mediated endocytic trafficking in budding yeast revealed by using fluorescent alpha-factor derivatives. Proc Natl Acad Sci USA 103(15):5793-5798.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.15 , pp. 5793-5798
    • Toshima, J.Y.1
  • 38
    • 0023724429 scopus 로고
    • The C-terminus of the S. Cerevisiae alphapheromone receptor mediates an adaptive response to pheromone
    • Konopka JB, Jenness DD, Hartwell LH (1988) The C-terminus of the S. cerevisiae alphapheromone receptor mediates an adaptive response to pheromone. Cell 54(5):609-620.
    • (1988) Cell , vol.54 , Issue.5 , pp. 609-620
    • Konopka, J.B.1    Jenness, D.D.2    Hartwell, L.H.3
  • 39
    • 0019996706 scopus 로고
    • Amplification and adaptation in regulatory and sensory systems
    • Koshland DE, Jr, Goldbeter A, Stock JB (1982) Amplification and adaptation in regulatory and sensory systems. Science 217(4556):220-225.
    • (1982) Science , vol.217 , Issue.4556 , pp. 220-225
    • Koshland, D.E.1    Goldbeter, A.2    Stock, J.B.3
  • 40
    • 2342578714 scopus 로고    scopus 로고
    • Spatiotemporal control of gene expression with pulse-generating networks
    • Basu S, Mehreja R, Thiberge S, Chen M-TT, Weiss R (2004) Spatiotemporal control of gene expression with pulse-generating networks. Proc Natl Acad Sci USA 101(17):6355-6360.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.17 , pp. 6355-6360
    • Basu, S.1    Mehreja, R.2    Thiberge, S.3    Chen, M.-T.T.4    Weiss, R.5
  • 41
    • 0030025395 scopus 로고    scopus 로고
    • The impact of receptor desensitization on fast synaptic transmission
    • Jones MV, Westbrook GL (1996) The impact of receptor desensitization on fast synaptic transmission. Trends Neurosci 19(3):96-101.
    • (1996) Trends Neurosci , vol.19 , Issue.3 , pp. 96-101
    • Jones, M.V.1    Westbrook, G.L.2
  • 42
    • 77951681944 scopus 로고    scopus 로고
    • Functional motifs in biochemical reaction networks
    • Tyson JJ, Novák B (2010) Functional motifs in biochemical reaction networks. Annu Rev Phys Chem 61:219-240.
    • (2010) Annu Rev Phys Chem , vol.61 , pp. 219-240
    • Tyson, J.J.1    Novák, B.2
  • 44
    • 0028805208 scopus 로고
    • Saccharomyces cerevisiae cells execute a default pathway to select a mate in the absence of pheromone gradients
    • Dorer R, Pryciak PM, Hartwell LH (1995) Saccharomyces cerevisiae cells execute a default pathway to select a mate in the absence of pheromone gradients. J Cell Biol 131(4):845-861.
    • (1995) J Cell Biol , vol.131 , Issue.4 , pp. 845-861
    • Dorer, R.1    Pryciak, P.M.2    Hartwell, L.H.3
  • 45
    • 0029146796 scopus 로고
    • Association of the yeast pheromone response G protein beta gamma subunits with the MAP kinase scaffold Ste5p
    • Whiteway MS, et al. (1995) Association of the yeast pheromone response G protein beta gamma subunits with the MAP kinase scaffold Ste5p. Science 269(5230): 1572-1575.
    • (1995) Science , vol.269 , Issue.5230 , pp. 1572-1575
    • Whiteway, M.S.1
  • 46
    • 0032168881 scopus 로고    scopus 로고
    • Membrane recruitment of the kinase cascade scaffold protein Ste5 by the Gbetagamma complex underlies activation of the yeast pheromone response pathway
    • Pryciak PM, Huntress FA (1998) Membrane recruitment of the kinase cascade scaffold protein Ste5 by the Gbetagamma complex underlies activation of the yeast pheromone response pathway. Genes Dev 12(17):2684-2697.
    • (1998) Genes Dev , vol.12 , Issue.17 , pp. 2684-2697
    • Pryciak, P.M.1    Huntress, F.A.2
  • 47
    • 33748686182 scopus 로고    scopus 로고
    • Microfluidic "jets" for generating steadystate gradients of soluble molecules on open surfaces
    • Keenan TM, Hsu C-H, Folch A (2006) Microfluidic "jets"f for generating steadystate gradients of soluble molecules on open surfaces. Appl Phys Lett 89(11): 114103-1-114103-3.
    • (2006) Appl Phys Lett , vol.89 , Issue.11 , pp. 1141031-1141033
    • Keenan, T.M.1    Hsu, C.-H.2    Folch, A.3
  • 48
    • 84877578867 scopus 로고    scopus 로고
    • A bright monomeric green fluorescent protein derived from Branchiostoma lanceolatum
    • Shaner NC, et al. (2013) A bright monomeric green fluorescent protein derived from Branchiostoma lanceolatum. Nat Methods 10(5):407-409.
    • (2013) Nat Methods , vol.10 , Issue.5 , pp. 407-409
    • Shaner, N.C.1
  • 49
    • 0037007225 scopus 로고    scopus 로고
    • A positive feedback loop stabilizes the guanine-nucleotide exchange factor Cdc24 at sites of polarization
    • Butty AC, et al. (2002) A positive feedback loop stabilizes the guanine-nucleotide exchange factor Cdc24 at sites of polarization. EMBO J 21(7):1565-1576.
    • (2002) EMBO J , vol.21 , Issue.7 , pp. 1565-1576
    • Butty, A.C.1
  • 50
    • 0344394312 scopus 로고    scopus 로고
    • Scaffold-mediated symmetry breaking by Cdc42p
    • Irazoqui JE, Gladfelter AS, Lew DJ (2003) Scaffold-mediated symmetry breaking by Cdc42p. Nat Cell Biol 5(12):1062-1070.
    • (2003) Nat Cell Biol , vol.5 , Issue.12 , pp. 1062-1070
    • Irazoqui, J.E.1    Gladfelter, A.S.2    Lew, D.J.3
  • 51
    • 0026586631 scopus 로고
    • A yeast gene (BEM1) necessary for cell polarization whose product contains two SH3 domains
    • Chenevert J, Corrado K, Bender A, Pringle J, Herskowitz I (1992) A yeast gene (BEM1) necessary for cell polarization whose product contains two SH3 domains. Nature 356(6364):77-79.
    • (1992) Nature , vol.356 , Issue.6364 , pp. 77-79
    • Chenevert, J.1    Corrado, K.2    Bender, A.3    Pringle, J.4    Herskowitz, I.5
  • 52
    • 0036220079 scopus 로고    scopus 로고
    • Bud-site selection and cell polarity in budding yeast
    • Casamayor A, Snyder M (2002) Bud-site selection and cell polarity in budding yeast. Curr Opin Microbiol 5(2):179-186.
    • (2002) Curr Opin Microbiol , vol.5 , Issue.2 , pp. 179-186
    • Casamayor, A.1    Snyder, M.2
  • 53
    • 0029912384 scopus 로고    scopus 로고
    • Genetic analysis of the bipolar pattern of bud site selection in the yeast Saccharomyces cerevisiae
    • Zahner JE, Harkins HA, Pringle JR (1996) Genetic analysis of the bipolar pattern of bud site selection in the yeast Saccharomyces cerevisiae. Mol Cell Biol 16(4):1857-1870.
    • (1996) Mol Cell Biol , vol.16 , Issue.4 , pp. 1857-1870
    • Zahner, J.E.1    Harkins, H.A.2    Pringle, J.R.3
  • 54
    • 49649089500 scopus 로고    scopus 로고
    • On the spontaneous emergence of cell polarity
    • Altschuler SJ, Angenent SB, Wang Y, Wu LF (2008) On the spontaneous emergence of cell polarity. Nature 454(7206):886-889.
    • (2008) Nature , vol.454 , Issue.7206 , pp. 886-889
    • Altschuler, S.J.1    Angenent, S.B.2    Wang, Y.3    Wu, L.F.4
  • 55
    • 0032495489 scopus 로고    scopus 로고
    • A GTP-exchange factor required for cell orientation
    • Nern A, Arkowitz RA (1998) A GTP-exchange factor required for cell orientation. Nature 391(6663):195-198.
    • (1998) Nature , vol.391 , Issue.6663 , pp. 195-198
    • Nern, A.1    Arkowitz, R.A.2
  • 56
    • 0033593974 scopus 로고    scopus 로고
    • A Cdc24p-Far1p-Gbetagamma protein complex required for yeast orientation during mating
    • Nern A, Arkowitz RA (1999) A Cdc24p-Far1p-Gbetagamma protein complex required for yeast orientation during mating. J Cell Biol 144(6):1187-1202.
    • (1999) J Cell Biol , vol.144 , Issue.6 , pp. 1187-1202
    • Nern, A.1    Arkowitz, R.A.2
  • 57
    • 34447625042 scopus 로고    scopus 로고
    • The sequence of events that underlie quantal transmission at central glutamatergic synapses
    • Lisman JE, Raghavachari S, Tsien RW (2007) The sequence of events that underlie quantal transmission at central glutamatergic synapses. Nat Rev Neurosci 8(8):597-609.
    • (2007) Nat Rev Neurosci , vol.8 , Issue.8 , pp. 597-609
    • Lisman, J.E.1    Raghavachari, S.2    Tsien, R.W.3
  • 58
    • 0032080837 scopus 로고    scopus 로고
    • Switching of chemoattractant receptors programs development and morphogenesis in Dictyostelium: Receptor subtypes activate common responses at different agonist concentrations
    • Kim JY, Borleis JA, Devreotes PN (1998) Switching of chemoattractant receptors programs development and morphogenesis in Dictyostelium: Receptor subtypes activate common responses at different agonist concentrations. Dev Biol 197(1):117-128.
    • (1998) Dev Biol , vol.197 , Issue.1 , pp. 117-128
    • Kim, J.Y.1    Borleis, J.A.2    Devreotes, P.N.3
  • 59
    • 84861836686 scopus 로고    scopus 로고
    • Responding to chemical gradients: Bacterial chemotaxis
    • Sourjik V, Wingreen NS (2012) Responding to chemical gradients: Bacterial chemotaxis. Curr Opin Cell Biol 24(2):262-268.
    • (2012) Curr Opin Cell Biol , vol.24 , Issue.2 , pp. 262-268
    • Sourjik, V.1    Wingreen, N.S.2
  • 60
    • 79954998877 scopus 로고    scopus 로고
    • Adaptive response and enlargement of dynamic range
    • Friedlander T, Brenne N (2011) Adaptive response and enlargement of dynamic range. Math Biosci Eng 8(2):515-528.
    • (2011) Math Biosci Eng , vol.8 , Issue.2 , pp. 515-528
    • Friedlander, T.1    Brenne, N.2
  • 61
    • 77953582302 scopus 로고    scopus 로고
    • Covering a broad dynamic range: Information processing at the erythropoietin receptor
    • Becker V, et al. (2010) Covering a broad dynamic range: Information processing at the erythropoietin receptor. Science 328(5984):1404-1408.
    • (2010) Science , vol.328 , Issue.5984 , pp. 1404-1408
    • Becker, V.1
  • 62
    • 55449086053 scopus 로고    scopus 로고
    • Dose-to-duration encoding and signaling beyond saturation in intracellular signaling networks
    • Behar M, Hao N, Dohlman HG, Elston TC (2008) Dose-to-duration encoding and signaling beyond saturation in intracellular signaling networks. PLOS Comput Biol 4(10):e1000197.
    • (2008) PLOS Comput Biol , vol.4 , Issue.10 , pp. e1000197
    • Behar, M.1    Hao, N.2    Dohlman, H.G.3    Elston, T.C.4
  • 63
    • 77649086371 scopus 로고    scopus 로고
    • Ligand depletion in vivo modulates the dynamic range and cooperativity of signal transduction
    • Edelstein SJ, Stefan MI, Le Novère N (2010) Ligand depletion in vivo modulates the dynamic range and cooperativity of signal transduction. PLoS ONE 5(1):e8449.
    • (2010) PLoS ONE , vol.5 , Issue.1 , pp. e8449
    • Edelstein, S.J.1    Stefan, M.I.2    Le Novère, N.3
  • 64
    • 62549083590 scopus 로고    scopus 로고
    • Negative autoregulation linearizes the dose-response and suppresses the heterogeneity of gene expression
    • Nevozhay D, Adams RM, Murphy KF, Josic K, Balázsi G (2009) Negative autoregulation linearizes the dose-response and suppresses the heterogeneity of gene expression. Proc Natl Acad Sci USA 106(13):5123-5128.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.13 , pp. 5123-5128
    • Nevozhay, D.1    Adams, R.M.2    Murphy, K.F.3    Josic, K.4    Balázsi, G.5
  • 65
    • 79960165588 scopus 로고    scopus 로고
    • Negative auto-regulation increases the input dynamic-range of the arabinose system of Escherichia coli
    • Madar D, Dekel E, Bren A, Alon U (2011) Negative auto-regulation increases the input dynamic-range of the arabinose system of Escherichia coli. BMC Syst Biol 5:111.
    • (2011) BMC Syst Biol , vol.5 , pp. 111
    • Madar, D.1    Dekel, E.2    Bren, A.3    Alon, U.4
  • 66
    • 33846958053 scopus 로고    scopus 로고
    • Pre-steady-state decoding of the Bicoid morphogen gradient
    • Bergmann S, et al. (2007) Pre-steady-state decoding of the Bicoid morphogen gradient. PLoS Biol 5(2):e46.
    • (2007) PLoS Biol , vol.5 , Issue.2 , pp. e46
    • Bergmann, S.1
  • 67
    • 84863875681 scopus 로고    scopus 로고
    • Improved readout precision of the Bicoid morphogen gradient by early decoding
    • Tamari Z, Barkai N (2012) Improved readout precision of the Bicoid morphogen gradient by early decoding. J Biol Phys 38(2):317-329.
    • (2012) J Biol Phys , vol.38 , Issue.2 , pp. 317-329
    • Tamari, Z.1    Barkai, N.2
  • 68
    • 0023800138 scopus 로고
    • The Saccharomyces cerevisiae BAR1 gene encodes an exported protein with homology to pepsin
    • MacKay VL, et al. (1988) The Saccharomyces cerevisiae BAR1 gene encodes an exported protein with homology to pepsin. Proc Natl Acad Sci USA 85(1):55-59.
    • (1988) Proc Natl Acad Sci USA , vol.85 , Issue.1 , pp. 55-59
    • Mackay, V.L.1
  • 69
    • 77950833499 scopus 로고    scopus 로고
    • Detailed simulations of cell biology with Smoldyn 2. 1
    • Andrews SS, Addy NJ, Brent R, Arkin AP (2010) Detailed simulations of cell biology with Smoldyn 2. 1. PLOS Comput Biol 6(3):e1000705.
    • (2010) PLOS Comput Biol , vol.6 , Issue.3 , pp. e1000705
    • Andrews, S.S.1    Addy, N.J.2    Brent, R.3    Arkin, A.P.4
  • 70
    • 84863870994 scopus 로고    scopus 로고
    • Disentangling signaling gradients generated by equivalent sources
    • Rappaport N, Barkai N (2012) Disentangling signaling gradients generated by equivalent sources. J Biol Phys 38(2):267-278.
    • (2012) J Biol Phys , vol.38 , Issue.2 , pp. 267-278
    • Rappaport, N.1    Barkai, N.2
  • 71
    • 84898057561 scopus 로고    scopus 로고
    • Inhibitory GEF phosphorylation provides negative feedback in the yeast polarity circuit
    • Kuo C-CC, et al. (2014) Inhibitory GEF phosphorylation provides negative feedback in the yeast polarity circuit. Curr Biol 24(7):753-759.
    • (2014) Curr Biol , vol.24 , Issue.7 , pp. 753-759
    • Kuo, C.-C.C.1
  • 72
    • 84884417598 scopus 로고    scopus 로고
    • Beyond symmetry-breaking: Competition and negative feedback in GTPase regulation
    • Wu C-FF, Lew DJ (2013) Beyond symmetry-breaking: Competition and negative feedback in GTPase regulation. Trends Cell Biol 23(10):476-483.
    • (2013) Trends Cell Biol , vol.23 , Issue.10 , pp. 476-483
    • Wu, C.-F.F.1    Lew, D.J.2
  • 74
    • 68749118345 scopus 로고    scopus 로고
    • Defining network topologies that can achieve biochemical adaptation
    • Ma W, Trusina A, El-Samad H, Lim WA, Tang C (2009) Defining network topologies that can achieve biochemical adaptation. Cell 138(4):760-773.
    • (2009) Cell , vol.138 , Issue.4 , pp. 760-773
    • Ma, W.1    Trusina, A.2    El-Samad, H.3    Lim, W.A.4    Tang, C.5
  • 77
    • 33947355325 scopus 로고    scopus 로고
    • Single-cell quantification of molecules and rates using opensource microscope-based cytometry
    • Gordon, et al. (2007) Single-cell quantification of molecules and rates using opensource microscope-based cytometry. Nat Methods 4(2):175-181.
    • (2007) Nat Methods , vol.4 , Issue.2 , pp. 175-181
    • Gordon1
  • 78
    • 84873358881 scopus 로고    scopus 로고
    • Quantitative measurement of protein relocalization in live cells
    • Bush A, Colman-Lerner A (2013) Quantitative measurement of protein relocalization in live cells. Biophys J 104(3):727-736.
    • (2013) Biophys J , vol.104 , Issue.3 , pp. 727-736
    • Bush, A.1    Colman-Lerner, A.2
  • 79
    • 0035387449 scopus 로고    scopus 로고
    • A method for filling complex polymeric microfluidic devices and arrays
    • Monahan J, Gewirth AA, Nuzzo RG (2001) A method for filling complex polymeric microfluidic devices and arrays. Anal Chem 73(13):3193-3197.
    • (2001) Anal Chem , vol.73 , Issue.13 , pp. 3193-3197
    • Monahan, J.1    Gewirth, A.A.2    Nuzzo, R.G.3
  • 80
    • 84887712571 scopus 로고    scopus 로고
    • Parts-per-million of polyethylene glycol as a non-interfering blocking agent for homogeneous biosensor development
    • Liu B, et al. (2013) Parts-per-million of polyethylene glycol as a non-interfering blocking agent for homogeneous biosensor development. Anal Chem 85(21): 10045-10050.
    • (2013) Anal Chem , vol.85 , Issue.21 , pp. 10045-10050
    • Liu, B.1
  • 82
    • 58849162806 scopus 로고    scopus 로고
    • Systems biology: Model based evaluation and comparison of potential explanations for given biological data
    • Cedersund G, Roll J (2009) Systems biology: Model based evaluation and comparison of potential explanations for given biological data. FEBS J 276(4):903-922.
    • (2009) FEBS J , vol.276 , Issue.4 , pp. 903-922
    • Cedersund, G.1    Roll, J.2
  • 83
    • 0032553474 scopus 로고    scopus 로고
    • The role of Far1p in linking the heterotrimeric G protein to polarity establishment proteins during yeast mating
    • Butty AC, Pryciak PM, Huang LS, Herskowitz I, Peter M (1998) The role of Far1p in linking the heterotrimeric G protein to polarity establishment proteins during yeast mating. Science 282(5393):1511-1516.
    • (1998) Science , vol.282 , Issue.5393 , pp. 1511-1516
    • Butty, A.C.1    Pryciak, P.M.2    Huang, L.S.3    Herskowitz, I.4    Peter, M.5
  • 84
    • 0028884447 scopus 로고
    • Pheromone response in yeast: Association of Bem1p with proteins of the MAP kinase cascade and actin
    • Leeuw T, et al. (1995) Pheromone response in yeast: Association of Bem1p with proteins of the MAP kinase cascade and actin. Science 270(5239):1210-1213.
    • (1995) Science , vol.270 , Issue.5239 , pp. 1210-1213
    • Leeuw, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.