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Volumn 108, Issue 25, 2011, Pages 10178-10183

Visualization of the nanospring dynamics of the IκBα ankyrin repeat domain in real time

Author keywords

Intrinsically disordered protein; NFkappaB; Protein dynamics; Transcription factor

Indexed keywords

ANKYRIN; I KAPPA B ALPHA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN;

EID: 79959946164     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1102226108     Document Type: Article
Times cited : (44)

References (36)
  • 1
  • 2
    • 77954217602 scopus 로고    scopus 로고
    • The protein kingdom extended: Ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation
    • Turoverov KK, Kuznetsova IM, Uversky VN (2010) The protein kingdom extended: Ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation. Prog Biophys Mol Biol 102:73-84.
    • (2010) Prog Biophys Mol Biol , vol.102 , pp. 73-84
    • Turoverov, K.K.1    Kuznetsova, I.M.2    Uversky, V.N.3
  • 3
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P (2002) Intrinsically unstructured proteins. Trends Biochem Sci 27:527-533.
    • (2002) Trends Biochem Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 4
    • 77749298990 scopus 로고    scopus 로고
    • Molecular mechanisms of system control of NF-kappaB signaling by IkappaBalpha
    • Ferreiro DU, Komives EA (2010) Molecular mechanisms of system control of NF-kappaB signaling by IkappaBalpha. Biochemistry 49:1560-1567.
    • (2010) Biochemistry , vol.49 , pp. 1560-1567
    • Ferreiro, D.U.1    Komives, E.A.2
  • 5
    • 0033596121 scopus 로고    scopus 로고
    • Activators and target genes of Rel/NF-kappaB transcription factors
    • Pahl HL (1999) Activators and target genes of Rel/NF-kappaB transcription factors. Oncogene 18:6853-6866.
    • (1999) Oncogene , vol.18 , pp. 6853-6866
    • Pahl, H.L.1
  • 6
    • 34248997836 scopus 로고    scopus 로고
    • A homeostatic model of IkappaB metabolism to control constitutive NF-kappaB activity
    • O'Dea EL, et al. (2007) A homeostatic model of IkappaB metabolism to control constitutive NF-kappaB activity. Mol Syst Biol 3:111 (1-7).
    • (2007) Mol Syst Biol , vol.3
    • O'Dea, E.L.1
  • 8
    • 43249110701 scopus 로고    scopus 로고
    • NF-kappaB dictates the degradation pathway of IkappaBalpha
    • DOI 10.1038/emboj.2008.73, PII EMBOJ200873
    • Mathes E, O'Dea EL, Hoffmann A, Ghosh G (2008) NF-kappaB dictates the degradation pathway of IkappaBalpha. EMBO J 27:1357-1367. (Pubitemid 351655185)
    • (2008) EMBO Journal , vol.27 , Issue.9 , pp. 1357-1367
    • Mathes, E.1    O'Dea, E.L.2    Hoffmann, A.3    Ghosh, G.4
  • 10
    • 0027168948 scopus 로고
    • The p65 subunit of NF-kappa B regulates I kappa B by two distinct mechanisms
    • Scott ML, Fujita T, Liou HC, Nolan GP, Baltimore D (1993) The p65 subunit of NF-kappa B regulates I kappa B by two distinct mechanisms. Genes Dev 7:1266-1276. (Pubitemid 23207416)
    • (1993) Genes and Development , vol.7 , Issue.7 A , pp. 1266-1276
    • Scott, M.L.1    Fujita, T.2    Liou, H.-C.3    Nolan, G.P.4    Baltimore, D.5
  • 11
    • 0027168447 scopus 로고
    • NF-kappa B controls expression of inhibitor I kappa B alpha: Evidence for an inducible autoregulatory pathway
    • Sun SC, Ganchi PA, Ballard DW, Greene WC (1993) NF-kappa B controls expression of inhibitor I kappa B alpha: Evidence for an inducible autoregulatory pathway. Science 259:1912-1915. (Pubitemid 23124465)
    • (1993) Science , vol.259 , Issue.5103 , pp. 1912-1915
    • Sun, S.-C.1    Ganchi, P.A.2    Ballard, D.W.3    Greene, W.C.4
  • 13
    • 0037044575 scopus 로고    scopus 로고
    • The IkappaB-NF-kappaB signaling module: Temporal control and selective gene activation
    • DOI 10.1126/science.1071914
    • Hoffmann A, Levchenko A, Scott ML, Baltimore D (2002) The IkappaB-NF-kappaB 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
  • 14
    • 73349107491 scopus 로고    scopus 로고
    • Kinetic enhancement of NF-kappaB•DNA dissociation by IkappaBalpha
    • Bergqvist S, et al. (2009) Kinetic enhancement of NF-kappaB•DNA dissociation by IkappaBalpha. Proc Natl Acad Sci USA 106:19328-19333.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 19328-19333
    • Bergqvist, S.1
  • 15
    • 0032217268 scopus 로고    scopus 로고
    • The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation
    • DOI 10.1016/S0092-8674(00)81699-2
    • Huxford T, Huang DB, Malek S, Ghosh G (1998) The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation. Cell 95:759-770. (Pubitemid 29014456)
    • (1998) Cell , vol.95 , Issue.6 , pp. 759-770
    • Huxford, T.1    Huang, D.-B.2    Malek, S.3    Ghosh, G.4
  • 16
    • 0032217264 scopus 로고    scopus 로고
    • Structure of an IkappaBalpha/NF-kappaB complex
    • Jacobs MD, Harrison SC (1998) Structure of an IkappaBalpha/NF-kappaB complex. Cell 95:749-758.
    • (1998) Cell , vol.95 , pp. 749-758
    • Jacobs, M.D.1    Harrison, S.C.2
  • 17
    • 14844342815 scopus 로고    scopus 로고
    • The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins
    • Dosztányi Z, Csizmók V, Tompa P, I S (2005) The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. J Mol Biol 347:827-839.
    • (2005) J Mol Biol , vol.347 , pp. 827-839
    • Dosztányi, Z.1    Csizmók, V.2    Tompa, P.I.S.3
  • 18
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • DOI 10.1093/bioinformatics/bti541
    • Dosztányi Z, Csizmók V, Tompa P, Simon I (2005) IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 21:3433-3434. (Pubitemid 41222453)
    • (2005) Bioinformatics , vol.21 , Issue.16 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 21
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life
    • DOI 10.1016/j.jmb.2004.02.002, PII S0022283604001482
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337:635-645. (Pubitemid 38326883)
    • (2004) Journal of Molecular Biology , vol.337 , Issue.3 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 22
    • 3042628330 scopus 로고    scopus 로고
    • Biophysical characterization of the free IkappaBalpha ankyrin repeat domain in solution
    • DOI 10.1110/ps.04731004
    • Croy CH, Bergqvist S, Huxford T, Ghosh G, Komives EA (2004) Biophysical characterization of the free IkappaBalpha ankyrin repeat domain in solution. Protein Sci 13:1767-1777. (Pubitemid 38822116)
    • (2004) Protein Science , vol.13 , Issue.7 , pp. 1767-1777
    • Croy, C.H.1    Bergqvist, S.2    Huxford, T.3    Ghosh, G.4    Komives, E.A.5
  • 23
    • 34447628760 scopus 로고    scopus 로고
    • Regions of IkappaBalpha that are critical for its inhibition of NF-kappaB. DNA interaction fold upon binding to NF-kappaB
    • Truhlar SM, Torpey JW, Komives EA (2006) Regions of IkappaBalpha that are critical for its inhibition of NF-kappaB. DNA interaction fold upon binding to NF-kappaB. Proc Natl Acad Sci USA 103:18951-18956.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18951-18956
    • Truhlar, S.M.1    Torpey, J.W.2    Komives, E.A.3
  • 24
    • 45849140515 scopus 로고    scopus 로고
    • Transfer of flexibility between ankyrin repeats in IkappaB* upon formation of the NF-kappaB complex
    • Sue SC, Cervantes C, Komives EA, Dyson HJ (2008) Transfer of flexibility between ankyrin repeats in IkappaB* upon formation of the NF-kappaB 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
  • 25
    • 33845731817 scopus 로고    scopus 로고
    • Stabilizing IkappaBalpha by "consensus" design
    • Ferreiro DU, et al. (2007) Stabilizing IkappaBalpha by "consensus" design. J Mol Biol 365:1201-1216.
    • (2007) J Mol Biol , vol.365 , pp. 1201-1216
    • Ferreiro, D.U.1
  • 26
    • 65249185574 scopus 로고    scopus 로고
    • Interplay of alpha-synuclein binding and conformational switching probed by single-molecule fluorescence
    • Ferreon AC, Gambin Y, Lemke EA, Deniz AA (2009) Interplay of alpha-synuclein binding and conformational switching probed by single-molecule fluorescence. Proc Natl Acad Sci USA 106:5645-5650.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 5645-5650
    • Ferreon, A.C.1    Gambin, Y.2    Lemke, E.A.3    Deniz, A.A.4
  • 27
    • 78249280020 scopus 로고    scopus 로고
    • Single molecule characterization of α-synuclein in aggregation-prone states
    • Trexler AJ, Rhoades E (2010) Single molecule characterization of α-synuclein in aggregation-prone states. Biophys J 99:3048-3055.
    • (2010) Biophys J , vol.99 , pp. 3048-3055
    • Trexler, A.J.1    Rhoades, E.2
  • 28
    • 73949127938 scopus 로고    scopus 로고
    • Multiple conformations of full-length p53 detected with single-molecule fluorescence resonance energy transfer
    • Huang F, et al. (2009) Multiple conformations of full-length p53 detected with single-molecule fluorescence resonance energy transfer. Proc Natl Acad Sci USA 106:20758-20763.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20758-20763
    • Huang, F.1
  • 29
    • 44449134820 scopus 로고    scopus 로고
    • A practical guide to single-molecule FRET
    • DOI 10.1038/nmeth.1208, PII NMETH.1208
    • Roy R, Hohng S, Ha T (2008) A practical guide to single-molecule FRET. Nat Methods 5:507-516. (Pubitemid 351761757)
    • (2008) Nature Methods , vol.5 , Issue.6 , pp. 507-516
    • Roy, R.1    Hohng, S.2    Ha, T.3
  • 34
    • 0034807927 scopus 로고    scopus 로고
    • Single Molecule Fluorescence Resonance Transfer
    • Ha T (2001) Single Molecule Fluorescence Resonance Transfer. Methods 25:78-86.
    • (2001) Methods , vol.25 , pp. 78-86
    • Ha, T.1
  • 35
    • 0141534308 scopus 로고    scopus 로고
    • Sequence-dependent pausing of single lambda exonuclease molecules
    • DOI 10.1126/science.1088047
    • Perkins TT, Dalal RV, Mitsis PG, Block SM (2003) Sequence-dependent pausing of single lambda exonuclease molecules. Science 301:1914-1918. (Pubitemid 37221398)
    • (2003) Science , vol.301 , Issue.5641 , pp. 1914-1918
    • Perkins, T.T.1    Dalal, R.V.2    Mitsis, P.G.3    Block, S.M.4
  • 36
    • 77955605175 scopus 로고    scopus 로고
    • PcrA helicase dismantles RecA filaments by reeling in DNA in uniform steps
    • Park J, et al. (2010) PcrA helicase dismantles RecA filaments by reeling in DNA in uniform steps. Cell 142:544-555.
    • (2010) Cell , vol.142 , pp. 544-555
    • Park, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.