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Volumn 49, Issue 8, 2010, Pages 1560-1567

Molecular mechanisms of system control of NF-κB signaling by IκBα

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN-REPEAT DOMAIN; BIOPHYSICAL PROPERTIES; BOUND STATE; CELL BIOLOGY; COMBINED SOLUTION; FOLDING DYNAMICS; FREE STATE; IN-VITRO; INFLAMMATORY CYTOKINES; MOLECULAR MECHANISM; NUCLEAR LOCALIZATION; RESTING CELLS; SIGNAL ACTIVATION; SYSTEM CONTROL; TRANSCRIPTIONAL ACTIVATIONS; TRANSCRIPTIONAL CONTROL;

EID: 77749298990     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi901948j     Document Type: Review
Times cited : (118)

References (64)
  • 1
    • 0037044575 scopus 로고    scopus 로고
    • The IκB-NF-κB signaling module: Temporal control and selective gene activation
    • DOI 10.1126/science.1071914
    • 1. Hoffmann, A., Levchenko, A., Scott, M. L., and Baltimore, D. (2002) The IκB-NF-κB signaling module: Temporal control and selective gene activation, Science 298, 1241-1245. (Pubitemid 35285493)
    • (2002) Science , vol.298 , Issue.5596 , pp. 1241-1245
    • Hoffmann, A.1    Levchenko, A.2    Scott, M.L.3    Baltimore, D.4
  • 2
    • 0031897632 scopus 로고    scopus 로고
    • NF-κB and Rel proteins: Evolutionarily conserved mediators of immune responses
    • Ghosh, S., May, M. J., and Kopp, E. B. (1998) NF-κB and Rel proteins: Evolutionarily conserved mediators of immune responses. Annu. Rev. Immunol. 16, 225-260.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 225-260
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 3
    • 3843052483 scopus 로고    scopus 로고
    • Nuclear factor-κB: Its role in health and disease
    • Kumar, A., Takada, Y., Boriek, A. M., and Aggarwal, B. B. (2004) Nuclear factor-κB: Its role in health and disease. J. Mol. Med. 82,434-448.
    • (2004) J. Mol. Med. , vol.82 , pp. 434-448
    • Kumar, A.1    Takada, Y.2    Boriek, A.M.3    Aggarwal, B.B.4
  • 4
    • 33645312379 scopus 로고    scopus 로고
    • Circuitry of nuclear factor κB signaling
    • Hoffmann, A., and Baltimore, D. (2006) Circuitry of nuclear factor κB signaling, Immunol. Rev. 210, 171-186.
    • (2006) Immunol. Rev. , vol.210 , pp. 171-186
    • Hoffmann, A.1    Baltimore, D.2
  • 5
    • 0028971289 scopus 로고
    • Rel/NF-κ B/I κB family: Intimate tales of association and dissociation
    • Verma, I. M., Stevenson, J. K., Schwarz, E. M, Van Antwerp, D., and Miyamoto, S. (1995) Rel/NF-κ B/I κB family: Intimate tales of association and dissociation, Genes Dev. 9, 2723-2735.
    • (1995) Genes Dev. , vol.9 , pp. 2723-2735
    • Verma, I.M.1    Stevenson, J.K.2    Schwarz, E.M.3    Van Antwerp, D.4    Miyamoto, S.5
  • 7
    • 0032217267 scopus 로고    scopus 로고
    • IκB-NF-κKB structures: At the interface of inflammation control
    • Baeuerle, P. A. (1998) IκB-NF-κKB structures: At the interface of inflammation control, Cell 95, 729-731.
    • (1998) Cell , vol.95 , pp. 729-731
    • Baeuerle, P.A.1
  • 8
    • 33745276259 scopus 로고    scopus 로고
    • Thermodynamics reveal that helix four in the NLS of NF-κB p65 anchors IκBα, forming a very stable complex
    • Bergqvist, S., Croy, C. H., Kjaergaard, M., Huxford, T., Ghosh, G., and Komives, E. A. (2006) Thermodynamics reveal that helix four in the NLS of NF-κB p65 anchors IκBα, forming a very stable complex. J. Mol. Biol. 360,421-434.
    • (2006) J. Mol. Biol. , vol.360 , pp. 421-434
    • Bergqvist, S.1    Croy, C.H.2    Kjaergaard, M.3    Huxford, T.4    Ghosh, G.5    Komives, E.A.6
  • 9
    • 0029442332 scopus 로고
    • Appearance of apparently ubiquitin-conjugated IκB-α during its phosphorylation-induced degradation in intact cells
    • Traenckner, E. B., and Baeuerle, P. A. (1995) Appearance of apparently ubiquitin-conjugated IκB-α during its phosphorylation-induced degradation in intact cells. J. Cell Sci. Suppl. 19, 79-84.
    • (1995) J. Cell Sci. Suppl. , vol.19 , pp. 79-84
    • Traenckner, E.B.1    Baeuerle, P.A.2
  • 10
    • 0033596121 scopus 로고    scopus 로고
    • Activators and target genes of Rel/NF-κB transcription factors
    • Pahl, H. L. (1999) Activators and target genes of Rel/NF-κB transcription factors. Oncogene 18, 6853-6866.
    • (1999) Oncogene , vol.18 , pp. 6853-6866
    • Pahl, H.L.1
  • 11
    • 0142105387 scopus 로고    scopus 로고
    • Genetic analysis of NF-κB/Rel transcription factors defines functional specificities
    • Hoffmann, A., Leung, T. H., and Baltimore, D. (2003) Genetic analysis of NF-κB/Rel transcription factors defines functional specificities. EMBO J. 22, 5530-5539.
    • (2003) EMBO J. , vol.22 , pp. 5530-5539
    • Hoffmann, A.1    Leung, T.H.2    Baltimore, D.3
  • 12
    • 24944489952 scopus 로고    scopus 로고
    • Stimulus specificity of gene expression programs determined by temporal control of IKK activity
    • Werner, S. L., Barken, D., and Hoffmann, A. (2005) Stimulus specificity of gene expression programs determined by temporal control of IKK activity. Science 309, 1857-1861.
    • (2005) Science , vol.309 , pp. 1857-1861
    • Werner, S.L.1    Barken, D.2    Hoffmann, A.3
  • 13
    • 0027462682 scopus 로고
    • Mutual regulation of the transcriptional activator NF-κB and its inhibitor, IκB-α
    • Brown, K., Park, S., Kanno, T., Franzoso, G., and Siebenlist, U. (1993) Mutual regulation of the transcriptional activator NF-κB and its inhibitor, IκB-α. Proc. Natl. Acad. Sci. U.S.A. 90, 2532-2536.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 2532-2536
    • Brown, K.1    Park, S.2    Kanno, T.3    Franzoso, G.4    Siebenlist, U.5
  • 14
    • 0027168948 scopus 로고
    • The p65 subunit of NF-κB regulates IκB by two distinct mechanisms
    • Scott, M. L., Fujita, T., Liou, H. C., Nolan, G. P., and Baltimore, D. (1993) The p65 subunit of NF-κB regulates IκB by two distinct mechanisms, Genes Dev. 7, 1266-1276.
    • (1993) Genes Dev. , vol.7 , pp. 1266-1276
    • Scott, M.L.1    Fujita, T.2    Liou, H.C.3    Nolan, G.P.4    Baltimore, D.5
  • 15
    • 0027168447 scopus 로고
    • NF-κB controls expression of inhibitor IκBα: Evidence for an inducible autoregulatory pathway
    • Sun, S. C., Ganchi, P. A., Ballard, D. W., and Greene, W. C. (1993) NF-κB controls expression of inhibitor IκBα: Evidence for an inducible autoregulatory pathway, Science 259, 912-1915.
    • (1993) Science , vol.259 , pp. 912-1915
    • Sun, S.C.1    Ganchi, P.A.2    Ballard, D.W.3    Greene, W.C.4
  • 18
    • 43249110701 scopus 로고    scopus 로고
    • NF-κB dictates the degradation pathway of IκBα
    • Mathes, E., O'Dea, E. L., Hoffmann, A., and Ghosh, G. (2008) NF-κB dictates the degradation pathway of IκBα. EMBO J. 27, 1357-1367.
    • (2008) EMBO J. , vol.27 , pp. 1357-1367
    • Mathes, E.1    O'Dea, E.L.2    Hoffmann, A.3    Ghosh, G.4
  • 19
    • 0032217264 scopus 로고    scopus 로고
    • Structure of an IκBα/NF-κB complex
    • Jacobs, M. D., and Harrison, S. C. (1998) Structure of an IκBα/NF-κB complex. Cell 95, 749-758.
    • (1998) Cell , vol.95 , pp. 749-758
    • Jacobs, M.D.1    Harrison, S.C.2
  • 20
    • 0032217268 scopus 로고    scopus 로고
    • The crystal structure of the IκBα/NF-κB complex reveals mechanisms of NF-κB inactivation
    • Huxford, T., Huang, D. B., Malek, S., and Ghosh, G. (1998) The crystal structure of the IκBα/NF-κB complex reveals mechanisms of NF-κB inactivation. Cell 95, 759-770.
    • (1998) Cell , vol.95 , pp. 759-770
    • Huxford, T.1    Huang, D.B.2    Malek, S.3    Ghosh, G.4
  • 23
    • 3042628330 scopus 로고    scopus 로고
    • Biophysical characterization of the free IκBa ankyrin repeat domain in solution
    • Croy, C. H., Bergqvist, S., Huxford, T., Ghosh, G., and Komives, E. A. (2004) Biophysical characterization of the free IκBa ankyrin repeat domain in solution, Protein Sci. 13, 1767-1777.
    • (2004) Protein Sci. , vol.13 , pp. 1767-1777
    • Croy, C.H.1    Bergqvist, S.2    Huxford, T.3    Ghosh, G.4    Komives, E.A.5
  • 24
    • 4644306518 scopus 로고    scopus 로고
    • An experimentally determined protein folding energy landscape
    • Mello, C. C., and Barrick, D. (2004) An experimentally determined protein folding energy landscape. Proc. Natl. Acad. Sci. U.S.A. 101, 14102-14107.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 14102-14107
    • Mello, C.C.1    Barrick, D.2
  • 25
    • 44949165528 scopus 로고    scopus 로고
    • The energy landscapes of repeat-containing proteins: Topology, cooperativity, and the folding funnels of one-dimensional architectures
    • Ferreiro, D. U., Walczak, A. M., Komives, E. A., and Wolynes, P. G. (2008) The energy landscapes of repeat-containing proteins: Topology, cooperativity, and the folding funnels of one-dimensional architectures. PLoS Comput. Biol. 16, e1000070.
    • (2008) PLoS Comput. Biol. , vol.16
    • Ferreiro, D.U.1    Walczak, A.M.2    Komives, E.A.3    Wolynes, P.G.4
  • 26
    • 27744531924 scopus 로고    scopus 로고
    • The energy landscape of modular repeat proteins: Topology determines folding mechanism, in the ankyrin family
    • Ferreiro, D. U., Cho, S. S., Komives, E. A., and Wolynes, P. G. (2005) The energy landscape of modular repeat proteins: Topology determines folding mechanism, in the ankyrin family. J. Mol. Biol. 354, 679-692.
    • (2005) J. Mol. Biol. , vol.354 , pp. 679-692
    • Ferreiro, D.U.1    Cho, S.S.2    Komives, E.A.3    Wolynes, P.G.4
  • 28
    • 0035807936 scopus 로고    scopus 로고
    • Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor. 2. Solution stability and cooperativity of unfolding
    • Zweifel, M. E., and Barrick, D. (2001) Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor. 2. Solution stability and cooperativity of unfolding. Biochemistry 40, 14357-14367.
    • (2001) Biochemistry , vol.40 , pp. 14357-14367
    • Zweifel, M.E.1    Barrick, D.2
  • 30
    • 39149097794 scopus 로고    scopus 로고
    • Folding landscapes of ankyrin repeat proteins: Experiments meet theory
    • Barrick, D., Ferreiro, D. U., and Komives, E. A. (2008) Folding landscapes of ankyrin repeat proteins: Experiments meet theory. Curr. Opin. Struct. Biol. 18, 27-34.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 27-34
    • Barrick, D.1    Ferreiro, D.U.2    Komives, E.A.3
  • 31
    • 33847328451 scopus 로고    scopus 로고
    • Rational redesign of the folding pathway of a modular protein
    • Lowe, A. R., and Itzhaki, L. S. (2007) Rational redesign of the folding pathway of a modular protein. Proc. Natl. Acad. Sci. U.S.A. 104, 2679-2684.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 2679-2684
    • Lowe, A.R.1    Itzhaki, L.S.2
  • 32
    • 34548559078 scopus 로고    scopus 로고
    • Folding Mechanism of an Ankyrin Repeat Protein: Scaffold and Active Site Formation of Human CDK Inhibitor pl9INK4d
    • Löw, C., Weininger, U., Zeeb, M., Zhang, W., Laue, E. D., Schmid, F. X., and Balbach, J. (2007) Folding Mechanism of an Ankyrin Repeat Protein: Scaffold and Active Site Formation of Human CDK Inhibitor pl9INK4d. J. Mol. Biol. 373, 219-231.
    • (2007) J. Mol. Biol. , vol.373 , pp. 219-231
    • Löw, C.1    Weininger, U.2    Zeeb, M.3    Zhang, W.4    Laue, E.D.5    Schmid, F.X.6    Balbach, J.7
  • 33
    • 34249941075 scopus 로고    scopus 로고
    • Probing a moving target with a plastic unfolding intermediate of an ankyrin repeat protein
    • Werbeck, N. D., and Itzhaki, L. S. (2007) Probing a moving target with a plastic unfolding intermediate of an ankyrin repeat protein. Proc. Natl. Acad. Sci. U.S.A. 104, 7863-7868.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 7863-7868
    • Werbeck, N.D.1    Itzhaki, L.S.2
  • 34
    • 0026607234 scopus 로고
    • The ANK repeat: A ubiquitous motif involved in macromolecular recognition
    • Michaely, P., and Bennett, V. (1992) The ANK repeat: A ubiquitous motif involved in macromolecular recognition, Trends Cell Biol. 2, 127-129.
    • (1992) Trends Cell Biol. , vol.2 , pp. 127-129
    • Michaely, P.1    Bennett, V.2
  • 35
    • 0032792551 scopus 로고    scopus 로고
    • The ankyrin repeat: A diversity of interactions on a common structural framework
    • Sedgwick, S. G., and Smerdon, S. J. (1999) The ankyrin repeat: A diversity of interactions on a common structural framework. Trends Biochem. Sci. 24, 311-316.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 311-316
    • Sedgwick, S.G.1    Smerdon, S.J.2
  • 36
    • 18744380008 scopus 로고    scopus 로고
    • Consensusderived structural determinants of the ankyrin repeat motif Proc
    • Mosavi, L. K., Minor, D. L., Jr., and Peng, Z. Y. (2002) Consensusderived structural determinants of the ankyrin repeat motif Proc. Natl. Acad. Sci. U.S.A. 99, 16029-16034.
    • (2002) Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16029-16034
    • Mosavi, L.K.1    Minor Jr., D.L.2    Peng, Z.Y.3
  • 37
    • 0042780350 scopus 로고    scopus 로고
    • Designing repeat proteins: Well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins
    • Binz, H. K., Stumpp, M. T., Forrer, P., Amstutz, P., and Pluckthun, A. (2003) Designing repeat proteins: Well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J. Mol. Biol. 332, 489-503.
    • (2003) J. Mol. Biol. , vol.332 , pp. 489-503
    • Binz, H.K.1    Stumpp, M.T.2    Forrer, P.3    Amstutz, P.4    Pluckthun, A.5
  • 39
    • 33845797576 scopus 로고    scopus 로고
    • Enhancing the stability and folding rate of a repeat protein through the addition of consensus repeats
    • Tripp, K. W., and Barrick, D. (2007) Enhancing the stability and folding rate of a repeat protein through the addition of consensus repeats. J. Mol. Biol. 365,1187-1200.
    • (2007) J. Mol. Biol. , vol.365 , pp. 1187-1200
    • Tripp, K.W.1    Barrick, D.2
  • 41
    • 37349036497 scopus 로고    scopus 로고
    • Characterization and further stabilization of designed ankyrin repeat proteins by combining molecular dynamics simulations and experiments
    • Interlandi, G., Wetzel, S. K., Settanni, G., Pluckthun, A., and Caflisch, A. (2008) Characterization and further stabilization of designed ankyrin repeat proteins by combining molecular dynamics simulations and experiments. J. Mol. Biol. 375, 837-854.
    • (2008) J. Mol. Biol. , vol.375 , pp. 837-854
    • Interlandi, G.1    Wetzel, S.K.2    Settanni, G.3    Pluckthun, A.4    Caflisch, A.5
  • 42
    • 38049063892 scopus 로고    scopus 로고
    • Folding and unfolding mechanism of highly stable fullconsensus ankyrin repeat proteins
    • Wetzel, S. K., Settanni, G., Kenig, M., Binz, H. K., and Pluckthun, A. (2008) Folding and unfolding mechanism of highly stable fullconsensus ankyrin repeat proteins. J. Mol. Biol. 376, 241-257.
    • (2008) J. Mol. Biol. , vol.376 , pp. 241-257
    • Wetzel, S.K.1    Settanni, G.2    Kenig, M.3    Binz, H.K.4    Pluckthun, A.5
  • 45
    • 34447628760 scopus 로고    scopus 로고
    • Regions of IκkBα that are critical for its inhibition of NF-κB·DNA interaction fold upon binding to NF-κB
    • Truhlar, S. M., Torpey, J. W., and Komives, E. A. (2006) Regions of IκkBα that are critical for its inhibition of NF-κB·DNA interaction fold upon binding to NF-κB. Proc. Natl. Acad. Sci. U.S.A. 103, 18951-18956.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 18951-18956
    • Truhlar, S.M.1    Torpey, J.W.2    Komives, E.A.3
  • 46
    • 0032556894 scopus 로고    scopus 로고
    • Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA
    • Chen, F. E., Huang, D. B., Chen, Y. Q., and Ghosh, G. (1998) Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA. Nature 391, 410-413.
    • (1998) Nature , vol.391 , pp. 410-413
    • Chen, F.E.1    Huang, D.B.2    Chen, Y.Q.3    Ghosh, G.4
  • 49
    • 0024378717 scopus 로고
    • Role of the hydrophobic effect in stability of site-specific protein-DNA complexes
    • Ha, J. H., Spolar, R. S., and Record, M. T. (1989) Role of the Hydrophobic Effect in Stability of Site-Specific Protein-DNA Complexes. J.Mol. Biol. 209, 801-816.
    • (1989) J.Mol. Biol. , vol.209 , pp. 801-816
    • Ha, J.H.1    Spolar, R.S.2    Record, M.T.3
  • 50
    • 0025906146 scopus 로고
    • Contribution to the thermodynamics of protein folding from the reduction in wateraccessible nonpolar surface area
    • Livingstone, J. R., Spolar, R. S., and Record, M. T. (1991) Contribution to the Thermodynamics of Protein Folding from the Reduction in WaterAccessible Nonpolar Surface Area. Biochemistry 30, 4237-4244.
    • (1991) Biochemistry , vol.30 , pp. 4237-4244
    • Livingstone, J.R.1    Spolar, R.S.2    Record, M.T.3
  • 51
    • 0026684671 scopus 로고
    • Use of liquid-hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water
    • Spolar, R. S., Livingstone, J. R., and Record, M. T. (1992) Use of Liquid-Hydrocarbon and Amide Transfer Data to Estimate Contributions to Thermodynamic Functions of Protein Folding from the Removal of Nonpolar and Polar Surface from Water. Biochemistry 31, 3947-3955.
    • (1992) Biochemistry , vol.31 , pp. 3947-3955
    • Spolar, R.S.1    Livingstone, J.R.2    Record, M.T.3
  • 52
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar, R. S., and Record, J. M. T. (1994) Coupling of Local Folding to Site-Specific Binding of Proteins to DNA.Science 263, 777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record, J.M.T.2
  • 53
    • 33847165830 scopus 로고    scopus 로고
    • Induced fit, folding, and recognition of the NF-KB-nuclear localization signals by IκBα and IκBβ
    • Latzer, J., Papoian, G. A., Prentiss, M. C., Komives, E. A., and Wolynes, P. G. (2007) Induced fit, folding, and recognition of the NF-KB-nuclear localization signals by IκBα and IκBβ. J. Mol. Biol. 367, 262-274.
    • (2007) J. Mol. Biol. , vol.367 , pp. 262-274
    • Latzer, J.1    Papoian, G.A.2    Prentiss, M.C.3    Komives, E.A.4    Wolynes, P.G.5
  • 54
    • 56749183334 scopus 로고    scopus 로고
    • The IκBα/NF-κB complex has two hot-spots, one at either end of the interface
    • Bergqvist, S., Ghosh, G., and Komives, E. A. (2008) The IκBα/NF-κB complex has two hot-spots, one at either end of the interface. Protein Sci. 17, 2051-2058.
    • (2008) Protein Sci. , vol.17 , pp. 2051-2058
    • Bergqvist, S.1    Ghosh, G.2    Komives, E.A.3
  • 55
    • 66149093818 scopus 로고    scopus 로고
    • Interaction of the IκBα C-terminal PEST sequence with NF-κB: Insights into the inhibition of NF-κB DNA binding by IκBα
    • Sue, S. C., and Dyson, H. J. (2009) Interaction of the IκBα C-terminal PEST sequence with NF-κB: Insights into the inhibition of NF-κB DNA binding by IκBα. J. Mol. Biol. 388, 824-838.
    • (2009) J. Mol. Biol. , vol.388 , pp. 824-838
    • Sue, S.C.1    Dyson, H.J.2
  • 56
    • 45849140515 scopus 로고    scopus 로고
    • Transfer of Flexibility between Ankyrin Repeats in IκBa upon Formation of the NF-κB Complex
    • Sue, S. C., Cervantes, C., Komives, E. A., and Dyson, H. J. (2008) Transfer of Flexibility between Ankyrin Repeats in IκBa upon Formation of the NF-κB Complex. J. Mol. Biol. 380, 917-931.
    • (2008) J. Mol. Biol. , vol.380 , pp. 917-931
    • Sue, S.C.1    Cervantes, C.2    Komives, E.A.3    Dyson, H.J.4
  • 57
    • 69049094038 scopus 로고    scopus 로고
    • Functional dynamics of the folded ankyrin repeats of IκBα revealed by nuclear magnetic resonance
    • Cervantes, C. F., Markwick, P. R. L., Sue, S. C., McCammon, J. A., Dyson, H. J., and Komives, E. A. (2009) Functional dynamics of the folded ankyrin repeats of IκBα revealed by nuclear magnetic resonance. Biochemistry 48, 8023-8031.
    • (2009) Biochemistry , vol.48 , pp. 8023-8031
    • Cervantes, C.F.1    Markwick, P.R.L.2    Sue, S.C.3    McCammon, J.A.4    Dyson, H.J.5    Komives, E.A.6
  • 58
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers, S., Wells, R., and Rechsteiner, M. (1986) Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis. Science 234, 364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 59
    • 0027451924 scopus 로고
    • In vivo control of NF-κB activation by IκBα
    • Rice, N. R., and Ernst, M. K. (1993) In vivo control of NF-κB activation by IκBα. EMBO J. 12, 4685-4695.
    • (1993) EMBO J. , vol.12 , pp. 4685-4695
    • Rice, N.R.1    Ernst, M.K.2
  • 60
    • 0034647693 scopus 로고    scopus 로고
    • Signal-dependent and independent degradation of free and NF-κB bound IκBα
    • Pando, M. P., and Verma, I. M. (2000) Signal-dependent and independent degradation of free and NF-κB bound IκBα. J. Biol. Chem 275, 21278-21286.
    • (2000) J. Biol. Chem , vol.275 , pp. 21278-21286
    • Pando, M.P.1    Verma, I.M.2
  • 62
    • 57949097314 scopus 로고    scopus 로고
    • Counting proteins in living cells by quantitative fluorescence microscopy with internal standards
    • Wu, J. Q., McCormick, C. D., and Pollard, T. D. (2008) Counting proteins in living cells by quantitative fluorescence microscopy with internal standards. Methods Cell Biol. 89, 253-273.
    • (2008) Methods Cell Biol. , vol.89 , pp. 253-273
    • Wu, J.Q.1    McCormick, C.D.2    Pollard, T.D.3
  • 63
    • 65549139791 scopus 로고    scopus 로고
    • Mathematical models and simulations of cellular processes based on actin filaments
    • Pollard, T. D., and Berro, J. (2009) Mathematical models and simulations of cellular processes based on actin filaments. J. Biol. Chem 284, 5433-5437.
    • (2009) J. Biol. Chem , vol.284 , pp. 5433-5437
    • Pollard, T.D.1    Berro, J.2


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