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Volumn 9, Issue 4, 2012, Pages

Effects of multiple enzyme-substrate interactions in basic units of cellular signal processing

Author keywords

[No Author keywords available]

Indexed keywords

ALGORITHM; ANIMAL; ARTICLE; BIOCATALYSIS; BIOLOGICAL MODEL; COMPUTER SIMULATION; ENZYME SPECIFICITY; HUMAN; PROTEIN PROTEIN INTERACTION; SIGNAL TRANSDUCTION;

EID: 84864939949     PISSN: 14783967     EISSN: 14783975     Source Type: Journal    
DOI: 10.1088/1478-3975/9/4/045009     Document Type: Article
Times cited : (8)

References (61)
  • 3
    • 0030445778 scopus 로고    scopus 로고
    • Tripping the switch fantastic: How a protein kinase cascade can convert graded inputs into switch-like outputs
    • DOI 10.1016/S0968-0004(96)20026-X, PII S096800049620026X
    • Ferrell J E 1996 Tripping the switch fantastic: how a protein kinase cascade can convert graded inputs into switch-like outputs Trends Biochem. Sci. 21 460-6 (Pubitemid 27018812)
    • (1996) Trends in Biochemical Sciences , vol.21 , Issue.12 , pp. 460-466
    • Ferrell Jr., J.E.1
  • 4
    • 0034019315 scopus 로고    scopus 로고
    • Negative feedback and ultrasensitivity can bring about oscillations in the mitogen-activated protein kinase cascades
    • DOI 10.1046/j.1432-1327.2000.01197.x
    • Kholodenko B N 2000 Negative feedback and ultrasensitivity can bring about oscillations in the mitogen-activated protein kinase cascades Eur. J. Biochem. 267 1583-8 (Pubitemid 30165509)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.6 , pp. 1583-1588
    • Kholodenko, B.N.1
  • 5
    • 32044463378 scopus 로고    scopus 로고
    • Kinetic models of phosphorylation cycles: A systematic approach using the rapid-equilibrium approximation for protein-protein interactions
    • DOI 10.1016/j.biosystems.2005.05.015, PII S0303264705001280
    • Salazar C and Hfer T 2006 Kinetic models of phosphorylation cycles: a systematic approach using the rapid-equilibrium approximation for protein-protein interactions Biosystems 83 195-206 (Pubitemid 43199820)
    • (2006) BioSystems , vol.83 , Issue.2-3 SPEC. ISS. , pp. 195-206
    • Salazar, C.1    Hofer, T.2
  • 6
    • 30344466977 scopus 로고    scopus 로고
    • The processivity of multiubiquitination by the APC determines the order of substrate degradation
    • DOI 10.1016/j.cell.2005.10.032, PII S0092867405012328
    • Rape M, Reddy S K and Kirschner M W 2006 The processivity of multiubiquitination by the APC determines the order of substrate degradation Cell 124 89-103 (Pubitemid 43069312)
    • (2006) Cell , vol.124 , Issue.1 , pp. 89-103
    • Rape, M.1    Reddy, S.K.2    Kirschner, M.W.3
  • 7
    • 34047240610 scopus 로고    scopus 로고
    • Modeling networks of coupled enzymatic reactions using the total quasi-steady state approximation
    • DOI 10.1371/journal.pcbi.0030045
    • Ciliberto A, Capuani F and Tyson J J 2007 Modeling networks of coupled enzymatic reactions using the total quasi-steady state approximation PLoS Comput. Biol. 3 e45 (Pubitemid 46535738)
    • (2007) PLoS Computational Biology , vol.3 , Issue.3 , pp. 0463-0472
    • Ciliberto, A.1    Capuani, F.2    Tyson, J.J.3
  • 8
    • 33947304756 scopus 로고    scopus 로고
    • Substrate Competition as a Source of Ultrasensitivity in the Inactivation of Wee1
    • DOI 10.1016/j.cell.2007.01.039, PII S0092867407002024
    • Kim S Y and Ferrell J E Jr 2007 Substrate competition as a source of ultrasensitivity in the inactivation of Wee1 Cell 128 1133-45 (Pubitemid 46437260)
    • (2007) Cell , vol.128 , Issue.6 , pp. 1133-1145
    • Kim, S.Y.1    Ferrell Jr., J.E.2
  • 9
    • 39149113411 scopus 로고    scopus 로고
    • Modular cell biology: Retroactivity and insulation
    • DOI 10.1038/msb4100204, PII MSB4100204
    • Del Vecchio D, Ninfa A J and Sontag E D 2008 Modular cell biology: retroactivity and insulation Mol. Syst. Biol. 4 161 (Pubitemid 351253202)
    • (2008) Molecular Systems Biology , vol.4 , pp. 161
    • Del Vecchio, D.1    Ninfa, A.J.2    Sontag, E.D.3
  • 10
    • 77649190430 scopus 로고    scopus 로고
    • MAPK substrate competition integrates patterning signals in the drosophila embryo
    • 10.1016/j.cub.2010.01.019 0960-9822
    • Kim Y, Coppey M, Grossman R, Ajuria L, Jiménez G, Paroush Z and Shvartsman S Y 2010 MAPK substrate competition integrates patterning signals in the drosophila embryo Curr. Biol. 20 446-51
    • (2010) Curr. Biol. , vol.20 , Issue.5 , pp. 446-451
    • Kim, Y.1    Coppey, M.2    Grossman, R.3    Ajuria, L.4    Jiménez, G.5    Paroush, Z.6    Shvartsman, S.Y.7
  • 11
    • 79959652892 scopus 로고    scopus 로고
    • The coupling of pathways and processes through shared components
    • 10.1186/1752-0509-5-103 1752-0509
    • Seaton D D and Krishnan J 2011 The coupling of pathways and processes through shared components BMC Syst. Biol. 5 103
    • (2011) BMC Syst. Biol. , vol.5 , Issue.1 , pp. 103
    • Seaton, D.D.1    Krishnan, J.2
  • 12
    • 33746363486 scopus 로고    scopus 로고
    • Domains, motifs, and scaffolds: The role of modular interactions in the evolution and wiring of cell signaling circuits
    • DOI 10.1146/annurev.biochem.75.103004.142710
    • Bhattacharyya R P, Reményi A, Yeh B J and Lim W A 2006 Domains, motifs, and scaffolds: the role of modular interactions in the evolution and wiring of cell signaling circuits Annu. Rev. Biochem. 75 655-80 (Pubitemid 44118047)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 655-680
    • Bhattacharyya, R.P.1    Remenyi, A.2    Yeh, B.J.3    Lim, W.A.4
  • 13
    • 36849043083 scopus 로고    scopus 로고
    • Substrate and docking interactions in serine/threonine protein kinases
    • DOI 10.1021/cr068221w
    • Goldsmith E J, Akella R, Min X, Zhou T and Humphreys J M 2007 Substrate and docking interactions in serine/threonine protein kinases Chem. Rev. 107 5065-81 (Pubitemid 350225869)
    • (2007) Chemical Reviews , vol.107 , Issue.11 , pp. 5065-5081
    • Goldsmith, E.J.1    Akella, R.2    Min, X.3    Zhou, T.4    Humphreys, J.M.5
  • 14
    • 84861859600 scopus 로고    scopus 로고
    • The structural basis for control of eukaryotic protein kinases
    • 10.1146/annurev-biochem-052410-090317 0066-4154
    • Endicott J A, Noble M E M and Johnson L N 2012 The structural basis for control of eukaryotic protein kinases Annu. Rev. Biochem. 81 1-27
    • (2012) Annu. Rev. Biochem. , vol.81 , Issue.1 , pp. 587-627
    • Endicott, J.A.1    Noble, M.E.M.2    Johnson, L.N.3
  • 15
    • 47649125643 scopus 로고    scopus 로고
    • Allosteric regulation and catalysis emerge via a common route
    • DOI 10.1038/nchembio.98, PII NCHEMBIO98
    • Goodey N M and Benkovic S J 2008 Allosteric regulation and catalysis emerge via a common route Nature Chem. Biol. 4 474-82 (Pubitemid 352019763)
    • (2008) Nature Chemical Biology , vol.4 , Issue.8 , pp. 474-482
    • Goodey, N.M.1    Benkovic, S.J.2
  • 16
  • 17
    • 83555176323 scopus 로고    scopus 로고
    • Allosteric regulation of PKCθ: Understanding multistep phosphorylation and priming by ligands in AGC kinases
    • 10.1002/prot.23205 0887-3585
    • Seco J, Ferrer-Costa C, Campanera J M, Soliva R and Barril X 2012 Allosteric regulation of PKCθ: understanding multistep phosphorylation and priming by ligands in AGC kinases Proteins 80 269-80
    • (2012) Proteins , vol.80 , Issue.1 , pp. 269-280
    • Seco, J.1    Ferrer-Costa, C.2    Campanera, J.M.3    Soliva, R.4    Barril, X.5
  • 18
    • 64549122329 scopus 로고    scopus 로고
    • Computational studies of protein regulation by post-translational phosphorylation
    • 10.1016/j.sbi.2009.02.007 0959-440X
    • Narayanan A and Jacobson M P 2009 Computational studies of protein regulation by post-translational phosphorylation Curr. Opin. Struct. Biol. 19 156-63
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , Issue.2 , pp. 156-163
    • Narayanan, A.1    Jacobson, M.P.2
  • 19
    • 63749127483 scopus 로고    scopus 로고
    • Kinome signaling through regulated protein-protein interactions in normal and cancer cells
    • 10.1016/j.ceb.2009.02.005 0955-0674
    • Pawson T and Kofler M 2009 Kinome signaling through regulated protein-protein interactions in normal and cancer cells Curr. Opin. Cell. Biol. 21 147-53
    • (2009) Curr. Opin. Cell. Biol. , vol.21 , Issue.2 , pp. 147-153
    • Pawson, T.1    Kofler, M.2
  • 20
    • 80053132089 scopus 로고    scopus 로고
    • Deciphering arginine methylation: Tudor tells the tale
    • 10.1038/nrm3185 1471-0072
    • Chen C, Nott T J, Jin J and Pawson T 2011 Deciphering arginine methylation: Tudor tells the tale Nature Rev. Mol. Cell Biol. 12 629-42
    • (2011) Nature Rev. Mol. Cell Biol. , vol.12 , Issue.10 , pp. 629-642
    • Chen, C.1    Nott, T.J.2    Jin, J.3    Pawson, T.4
  • 21
    • 79151471921 scopus 로고    scopus 로고
    • Kinetic mechanisms of Ca2+/calmodulin dependent protein kinases
    • 10.1016/j.abb.2010.11.008 0003-9861
    • Huynh Q K and Pagratis N 2011 Kinetic mechanisms of Ca2+/calmodulin dependent protein kinases Arch. Biochem. Biophys. 506 130-6
    • (2011) Arch. Biochem. Biophys. , vol.506 , Issue.2 , pp. 130-136
    • Huynh, Q.K.1    Pagratis, N.2
  • 23
    • 33744910065 scopus 로고    scopus 로고
    • Protein kinase D directly phosphorylates histone deacetylase 5 via a random sequential kinetic mechanism
    • DOI 10.1016/j.abb.2006.02.014, PII S0003986106000671
    • Huynh Q K and McKinsey T A 2006 Protein kinase D directly phosphorylates histone deacetylase 5 via a random sequential kinetic mechanism Arch. Biochem. Biophys. 450 141-8 (Pubitemid 43849620)
    • (2006) Archives of Biochemistry and Biophysics , vol.450 , Issue.2 , pp. 141-148
    • Huynh, Q.K.1    McKinsey, T.A.2
  • 24
    • 64549137956 scopus 로고    scopus 로고
    • Activation loop phosphorylation modulates brutons tyrosine kinase (Btk) kinase domain activity
    • 10.1021/bi8019756 0006-2960
    • Lin L, Czerwinski R, Kelleher K, Siegel M M, Wu P, Kriz R, Aulabaugh A and Stahl M 2009 Activation loop phosphorylation modulates brutons tyrosine kinase (Btk) kinase domain activity Biochemistry 48 2021-32
    • (2009) Biochemistry , vol.48 , Issue.9 , pp. 2021-2032
    • Lin, L.1    Czerwinski, R.2    Kelleher, K.3    Siegel, M.M.4    Wu, P.5    Kriz, R.6    Aulabaugh, A.7    Stahl, M.8
  • 25
    • 77950482089 scopus 로고    scopus 로고
    • Global consequences of activation loop phosphorylation on protein kinase a
    • 10.1074/jbc.M109.061820 0021-9258
    • Steichen J M, Iyer G H, Li S, Saldanha S A, Deal M S, Woods V L Jr and Taylor S S 2010 Global consequences of activation loop phosphorylation on protein kinase a J. Biol. Chem. 285 3825-32
    • (2010) J. Biol. Chem. , vol.285 , Issue.6 , pp. 3825-3832
    • Steichen, J.M.1    Iyer, G.H.2    Li, S.3    Saldanha, S.A.4    Deal Jr., M.S.5    Taylor, S.S.6
  • 26
    • 84859744067 scopus 로고    scopus 로고
    • Enzyme kinetics and interaction studies for human JNK1β1 and substrates activating transcription factor 2 (ATF2) and c-Jun N-terminal kinase (c-Jun)
    • 10.1074/jbc.M111.323766 0021-9258
    • Figuera-Losada M and LoGrasso P V 2012 Enzyme kinetics and interaction studies for human JNK1β1 and substrates activating transcription factor 2 (ATF2) and c-Jun N-terminal kinase (c-Jun) J. Biol. Chem. 287 13291-302
    • (2012) J. Biol. Chem. , vol.287 , Issue.16 , pp. 13291-13302
    • Figuera-Losada, M.1    Lograsso, P.V.2
  • 28
    • 79551594605 scopus 로고    scopus 로고
    • Protein kinases: Evolution of dynamic regulatory proteins
    • 10.1016/j.tibs.2010.09.006 0968-0004
    • Taylor S S and Kornev A P 2011 Protein kinases: evolution of dynamic regulatory proteins Trends Biochem. Sci. 36 65-77
    • (2011) Trends Biochem. Sci. , vol.36 , Issue.2 , pp. 65-77
    • Taylor, S.S.1    Kornev, A.P.2
  • 29
    • 0034383949 scopus 로고    scopus 로고
    • The regulation of protein function by multisite phosphorylation - A 25 year update
    • 10.1016/S0968-0004(00)01712-6 0968-0004
    • Cohen P 2000 The regulation of protein function by multisite phosphorylation - a 25 year update Trends Biochem. Sci. 25 596-601
    • (2000) Trends Biochem. Sci. , vol.25 , Issue.12 , pp. 596-601
    • Cohen, P.1
  • 30
    • 2342477917 scopus 로고    scopus 로고
    • The novel functions of ubiquitination in signaling
    • DOI 10.1016/j.ceb.2004.02.005, PII S0955067404000146
    • Sun L and Chen Z J 2004 The novel functions of ubiquitination in signaling Curr. Opin. Cell Biol. 16 119-26 (Pubitemid 38757287)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.2 , pp. 119-126
    • Sun, L.1    Chen, Z.J.2
  • 32
    • 67650360968 scopus 로고    scopus 로고
    • Unlimited multistability in multisite phosphorylation systems
    • 10.1038/nature08102 0028-0836
    • Thomson M and Gunawardena J 2009 Unlimited multistability in multisite phosphorylation systems Nature 460 274-7
    • (2009) Nature , vol.460 , Issue.7252 , pp. 274-277
    • Thomson, M.1    Gunawardena, J.2
  • 33
    • 78650788495 scopus 로고    scopus 로고
    • Multisite phosphorylation provides an effective and flexible mechanism for switch-like protein degradation
    • 10.1371/journal.pone.0014029 1932-6203
    • Varedi K S M, Ventura A C, Merajver S D and Lin X N 2010 Multisite phosphorylation provides an effective and flexible mechanism for switch-like protein degradation PLoS One 5 e14029
    • (2010) PLoS One , vol.5 , Issue.12
    • Varedi, K.S.M.1    Ventura, A.C.2    Merajver, S.D.3    Lin, X.N.4
  • 34
    • 78049274795 scopus 로고    scopus 로고
    • Timing control in regulatory networks by multisite protein modifications
    • 10.1016/j.tcb.2010.08.012 0962-8924
    • Salazar C, Brümmer A, Alberghina L and Höfer T 2010 Timing control in regulatory networks by multisite protein modifications Trends Cell Biol. 20 634-41
    • (2010) Trends Cell Biol. , vol.20 , Issue.11 , pp. 634-641
    • Salazar, C.1    Brümmer, A.2    Alberghina, L.3    Höfer, T.4
  • 35
    • 79960137914 scopus 로고    scopus 로고
    • Scaffold-mediated nucleation of protein signaling complexes: Elementary principles
    • 10.1016/j.mbs.2011.06.003 0025-5564
    • Yang J and Hlavacek W S 2011 Scaffold-mediated nucleation of protein signaling complexes: elementary principles Math. Biosci. 232 164-73
    • (2011) Math. Biosci. , vol.232 , Issue.2 , pp. 164-173
    • Yang, J.1    Hlavacek, W.S.2
  • 38
    • 73149111973 scopus 로고    scopus 로고
    • Quantitative effect of scaffold abundance on signal propagation
    • 10.1038/msb.2009.73 1744-4292
    • Chapman S A and Asthagiri A R 2009 Quantitative effect of scaffold abundance on signal propagation Mol. Syst. Biol. 5 313
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 313
    • Chapman, S.A.1    Asthagiri, A.R.2
  • 39
    • 77955353912 scopus 로고    scopus 로고
    • Signal response sensitivity in the yeast mitogen-activated protein kinase cascade
    • 10.1371/journal.pone.0011568 1932-6203
    • Thalhauser C J and Komarova N L 2010 Signal response sensitivity in the yeast mitogen-activated protein kinase cascade PLoS One 5 e11568
    • (2010) PLoS One , vol.5 , Issue.7
    • Thalhauser, C.J.1    Komarova, N.L.2
  • 40
    • 79955770162 scopus 로고    scopus 로고
    • Scaffold proteins: Hubs for controlling the flow of cellular information
    • 10.1126/science.1198701 0036-8075
    • Good M C, Zalatan J G and Lim W A 2011 Scaffold proteins: hubs for controlling the flow of cellular information Science 332 680-6
    • (2011) Science , vol.332 , Issue.6030 , pp. 680-686
    • Good, M.C.1    Zalatan, J.G.2    Lim, W.A.3
  • 41
    • 78650929625 scopus 로고    scopus 로고
    • Tunable signal processing in synthetic MAP kinase cascades
    • 10.1016/j.cell.2010.12.014 0092-8674
    • OShaughnessy E C, Palani S, Collins J J and Sarkar C A 2011 Tunable signal processing in synthetic MAP kinase cascades Cell 144 119-31
    • (2011) Cell , vol.144 , Issue.1 , pp. 119-131
    • Oshaughnessy, E.C.1    Palani, S.2    Collins, J.J.3    Sarkar, C.A.4
  • 43
    • 0842288229 scopus 로고    scopus 로고
    • Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades
    • DOI 10.1083/jcb.200308060
    • Markevich N I, Hoek J B and Kholodenko B N 2004 Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades J. Cell Biol. 164 353-9 (Pubitemid 38174763)
    • (2004) Journal of Cell Biology , vol.164 , Issue.3 , pp. 353-359
    • Markevich, N.I.1    Hoek, J.B.2    Kholodenko, B.N.3
  • 45
    • 0029992810 scopus 로고    scopus 로고
    • Signaling in the yeast pheromone response pathway: Specific and high-affinity interaction of the mitogen-activated protein (MAP) kinases Kss1 and Fus3 with the upstream MAP kinase kinase Ste7
    • Bardwell L, Cook J G, Chang E C, Cairns B R, Thorner J, Bardwell L E E, Cook J G, Chang E C and Cairns B R 1996 Signaling in the yeast pheromone response pathway: specific and high-affinity interaction of the mitogen-activated protein (MAP) kinases Kss1 and Fus3 with the upstream MAP kinase kinase Ste7 Mol. Cell. Biol. 16 3637-50
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3637-3650
    • Bardwell, L.1    Cook, J.G.2    Chang, E.C.3    Cairns, B.R.4    Thorner, J.5    Bardwell, L.E.E.6    Cook, J.G.7    Chang, E.C.8    Cairns, B.R.9
  • 46
    • 73149115306 scopus 로고    scopus 로고
    • Allosteric interactions direct binding and phosphorylation of asf/sf2 by srpk1
    • 10.1021/bi901107q 0006-2960
    • Huynh N, Ma C-T, Giang N, Hagopian J, Ngo J, Adams J and Ghosh G 2009 Allosteric interactions direct binding and phosphorylation of asf/sf2 by srpk1 Biochemistry 48 11432-40
    • (2009) Biochemistry , vol.48 , Issue.48 , pp. 11432-11440
    • Huynh, N.1    Ma, C.-T.2    Giang, N.3    Hagopian, J.4    Ngo, J.5    Adams, J.6    Ghosh, G.7
  • 47
    • 68049110634 scopus 로고    scopus 로고
    • The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site
    • 10.1016/j.cell.2009.05.028 0092-8674
    • Bae J H, Lew E D, Yuzawa S, Tomé F, Lax I and Schlessinger J 2009 The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site Cell 138 514-24
    • (2009) Cell , vol.138 , Issue.3 , pp. 514-524
    • Bae, J.H.1    Lew, E.D.2    Yuzawa, S.3    Tomé, F.4    Lax, I.5    Schlessinger, J.6
  • 48
    • 30544449081 scopus 로고    scopus 로고
    • A quantitative protein interaction network for the ErbB receptors using protein microarrays
    • DOI 10.1038/nature04177, PII NATURE04177
    • Jones R B, Gordus A, Krall J A and MacBeath G 2006 A quantitative protein interaction network for the ErbB receptors using protein microarrays Nature 439 168-74 (Pubitemid 43083134)
    • (2006) Nature , vol.439 , Issue.7073 , pp. 168-174
    • Jones, R.B.1    Gordus, A.2    Krall, J.A.3    MacBeath, G.4
  • 51
    • 70349156763 scopus 로고    scopus 로고
    • Dissecting protein function and signaling using protein microarrays
    • 10.1016/j.cbpa.2009.06.027 1367-5931
    • Wolf-Yadlin A, Sevecka M and MacBeath G 2009 Dissecting protein function and signaling using protein microarrays Curr. Opin. Chem. Biol. 13 398-405
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , Issue.4 , pp. 398-405
    • Wolf-Yadlin, A.1    Sevecka, M.2    MacBeath, G.3
  • 52
    • 78650590282 scopus 로고    scopus 로고
    • Graded enhancement of p53 binding to creb-binding protein (CBP) by multisite phosphorylation
    • 10.1073/pnas.1013078107 0027-8424
    • Lee C W, Ferreon J C, Ferreon A C M, Arai M and Wright P E 2010 Graded enhancement of p53 binding to creb-binding protein (CBP) by multisite phosphorylation Proc. Natl Acad. Sci. USA 107 19290-5
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , Issue.45 , pp. 19290-19295
    • Lee, C.W.1    Ferreon, J.C.2    Ferreon, A.C.M.3    Arai, M.4    Wright, P.E.5
  • 53
    • 58149145777 scopus 로고    scopus 로고
    • The biphasic behavior of incoherent feed-forward loops in biomolecular regulatory networks
    • 10.1002/bies.20839 0265-9247
    • Kim D, Kwon Y-K and Cho K-H 2008 The biphasic behavior of incoherent feed-forward loops in biomolecular regulatory networks Bioessays 30 1204-11
    • (2008) Bioessays , vol.30 , Issue.11-12 , pp. 1204-1211
    • Kim, D.1    Kwon, Y.-K.2    Cho, K.-H.3
  • 54
    • 47349095809 scopus 로고    scopus 로고
    • The incoherent feed-forward loop can generate non-monotonic input functions for genes
    • DOI 10.1038/msb.2008.43, PII MSB200843
    • Kaplan S, Bren A, Dekel E and Alon U 2008 The incoherent feed-forward loop can generate non-monotonic input functions for genes Mol. Syst. Biol. 4 203 (Pubitemid 352001262)
    • (2008) Molecular Systems Biology , vol.4 , pp. 203
    • Kaplan, S.1    Bren, A.2    Dekel, E.3    Alon, U.4
  • 55
    • 56949098506 scopus 로고    scopus 로고
    • Molecular titration and ultrasensitivity in regulatory networks
    • 10.1016/j.jmb.2008.09.079 0022-2836
    • Buchler N E and Louis M 2008 Molecular titration and ultrasensitivity in regulatory networks J. Mol. Biol. 384 1106-19
    • (2008) J. Mol. Biol. , vol.384 , Issue.5 , pp. 1106-1119
    • Buchler, N.E.1    Louis, M.2
  • 56
    • 79960942832 scopus 로고    scopus 로고
    • Effects of saturation and enzyme limitation in feedforward adaptive signal transduction
    • 10.1049/iet-syb.2010.0048 1751-8849
    • Krishnan J 2011 Effects of saturation and enzyme limitation in feedforward adaptive signal transduction IET Syst. Biol. 5 208-19
    • (2011) IET Syst. Biol. , vol.5 , Issue.3 , pp. 208-219
    • Krishnan, J.1
  • 57
    • 34848887670 scopus 로고    scopus 로고
    • Competing docking interactions can bring about bistability in the MAPK cascade
    • DOI 10.1529/biophysj.107.109132
    • Legewie S, Schoeberl B, Blüthgen N and Herzel H 2007 Competing docking interactions can bring about bistability in the MAPK cascade Biophys. J. 93 2279-88 (Pubitemid 47511127)
    • (2007) Biophysical Journal , vol.93 , Issue.7 , pp. 2279-2288
    • Legewie, S.1    Schoeberl, B.2    Bluthgen, N.3    Herzel, H.4
  • 58
    • 67149138163 scopus 로고    scopus 로고
    • Protein sequestration generates a flexible ultrasensitive response in a genetic network
    • 10.1038/msb.2009.30 1744-4292
    • Buchler N E and Cross F R 2009 Protein sequestration generates a flexible ultrasensitive response in a genetic network Mol. Syst. Biol. 5 272
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 272
    • Buchler, N.E.1    Cross, F.R.2
  • 59
    • 79961038741 scopus 로고    scopus 로고
    • Multiplexing biochemical signals
    • 10.1103/PhysRevLett.107.048101 0031-9007 048101
    • de Ronde W, Tostevin F and ten Wolde P R 2011 Multiplexing biochemical signals Phys. Rev. Lett. 107 048101
    • (2011) Phys. Rev. Lett. , vol.107 , Issue.4
    • De Ronde, W.1    Tostevin, F.2    Ten Wolde, P.R.3
  • 61
    • 84859933685 scopus 로고    scopus 로고
    • Bell-shaped and ultrasensitive dose-response in phosphorylation- dephosphorylation cycles: The role of kinase-phosphatase complex formation
    • 10.1186/1752-0509-6-26 1752-0509
    • Szomolay B and Shahrezaei V 2012 Bell-shaped and ultrasensitive dose-response in phosphorylation-dephosphorylation cycles: the role of kinase-phosphatase complex formation BMC Syst. Biol. 6 26
    • (2012) BMC Syst. Biol. , vol.6 , Issue.1 , pp. 26
    • Szomolay, B.1    Shahrezaei, V.2


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