메뉴 건너뛰기




Volumn 35, Issue 1, 2013, Pages 17-22

How is functional specificity achieved through disordered regions of proteins?

Author keywords

Disordered regions; Motifs

Indexed keywords

CALCIUM CHANNEL N TYPE; DNA TOPOISOMERASE (ATP HYDROLYSING); GLYCINE; LIGAND; POTASSIUM CHANNEL; SHAKER POTASSIUM CHANNEL; VOLTAGE DEPENDENT ANION CHANNEL;

EID: 84871012320     PISSN: 02659247     EISSN: 15211878     Source Type: Journal    
DOI: 10.1002/bies.201200115     Document Type: Article
Times cited : (13)

References (37)
  • 2
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, Wright PE. 2005. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6: 197- 208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 3
    • 84860510422 scopus 로고    scopus 로고
    • Stereospecific binding of a disordered peptide segment mediates BK channel inactivation
    • Gonzalez-Perez V, Zeng XH, Henzler-Wildman K, Lingle CJ. 2012. Stereospecific binding of a disordered peptide segment mediates BK channel inactivation. Nature 485: 133- 6.
    • (2012) Nature , vol.485 , pp. 133-136
    • Gonzalez-Perez, V.1    Zeng, X.H.2    Henzler-Wildman, K.3    Lingle, C.J.4
  • 4
    • 0029662315 scopus 로고    scopus 로고
    • Structural studies of p21(Waf1/Cip1/Sdi1) in the free and Cdk2-bound state: conformational disorder mediates binding diversity
    • Kriwacki RW, Hengst L, Tennant L, Reed SI, et al. 1996. Structural studies of p21(Waf1/Cip1/Sdi1) in the free and Cdk2-bound state: conformational disorder mediates binding diversity. Proc Natl Acad Sci USA 93: 11504- 9.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11504-11509
    • Kriwacki, R.W.1    Hengst, L.2    Tennant, L.3    Reed, S.I.4
  • 5
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson HJ, Wright PE. 2002. Coupling of folding and binding for unstructured proteins. Curr Opin Struct Biol 12: 54- 60.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 7
    • 84863979552 scopus 로고    scopus 로고
    • Rate constants and mechanisms of intrinsically disordered proteins binding to structured targets
    • Zhou HX, Pang XD, Lu C. 2012. Rate constants and mechanisms of intrinsically disordered proteins binding to structured targets. Phys Chem Chem Phys 14: 10466- 76.
    • (2012) Phys Chem Chem Phys , vol.14 , pp. 10466-10476
    • Zhou, H.X.1    Pang, X.D.2    Lu, C.3
  • 8
    • 34347235771 scopus 로고    scopus 로고
    • From "simple" DNA-protein interactions to the macromolecular machines of gene expression
    • von Hippel PH. 2007. From "simple" DNA-protein interactions to the macromolecular machines of gene expression. Annu Rev Biophys Biomol Struct 36: 79- 105.
    • (2007) Annu Rev Biophys Biomol Struct , vol.36 , pp. 79-105
    • von Hippel, P.H.1
  • 9
    • 80051927358 scopus 로고    scopus 로고
    • Incomplete folding upon binding mediates Cdk4/Cyclin D complex activation by tyrosine phosphorylation of inhibitor p27 protein
    • Ou L, Ferreira AM, Otieno S, Xiao LM, et al. 2011. Incomplete folding upon binding mediates Cdk4/Cyclin D complex activation by tyrosine phosphorylation of inhibitor p27 protein. J Biol Chem 286: 30142- 51.
    • (2011) J Biol Chem , vol.286 , pp. 30142-30151
    • Ou, L.1    Ferreira, A.M.2    Otieno, S.3    Xiao, L.M.4
  • 10
    • 84871021556 scopus 로고    scopus 로고
    • Fuzzy" complexes: how much disorder can a biologically relevant complex tolerate, and can it even be beneficial
    • Mittag T, Marsh J, Orlicky S, Borg M, et al. 2010. " Fuzzy" complexes: how much disorder can a biologically relevant complex tolerate, and can it even be beneficial? Biochem Cell Biol 88: 403.
    • (2010) Biochem Cell Biol , vol.88 , pp. 403
    • Mittag, T.1    Marsh, J.2    Orlicky, S.3    Borg, M.4
  • 11
    • 82655180384 scopus 로고    scopus 로고
    • Fuzziness: linking regulation to protein dynamics
    • Fuxreiter M. 2012. Fuzziness: linking regulation to protein dynamics. Mol Biosys 8: 168- 77.
    • (2012) Mol Biosys , vol.8 , pp. 168-177
    • Fuxreiter, M.1
  • 12
    • 80053441923 scopus 로고    scopus 로고
    • Dynamic protein-DNA recognition: beyond what can be seen
    • Fuxreiter M, Simon I, Bondos S. 2011. Dynamic protein-DNA recognition: beyond what can be seen. Trends Biochem Sci 36: 415- 23.
    • (2011) Trends Biochem Sci , vol.36 , pp. 415-423
    • Fuxreiter, M.1    Simon, I.2    Bondos, S.3
  • 13
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions
    • Tompa P, Fuxreiter M. 2008. Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends Biochem Sci 33: 2- 8.
    • (2008) Trends Biochem Sci , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 15
    • 69549120472 scopus 로고    scopus 로고
    • Conformational selection or induced fit: a flux description of reaction mechanism
    • Hammes GG, Chang YC, Oas TG. 2009. Conformational selection or induced fit: a flux description of reaction mechanism. Proc Natl Acad Sci USA 106: 13737- 41.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13737-13741
    • Hammes, G.G.1    Chang, Y.C.2    Oas, T.G.3
  • 16
    • 0038499698 scopus 로고    scopus 로고
    • Electrostatic interactions in a peptide-RNA complex
    • Garcia-Garcia C, Draper DE. 2003. Electrostatic interactions in a peptide-RNA complex. J Mol Biol 331: 75- 88.
    • (2003) J Mol Biol , vol.331 , pp. 75-88
    • Garcia-Garcia, C.1    Draper, D.E.2
  • 17
    • 84857492391 scopus 로고    scopus 로고
    • Residual structures, conformational fluctuations, and electrostatic interactions in the synergistic folding of two intrinsically disordered proteins
    • Zhang WH, Ganguly D, Chen JH. 2012. Residual structures, conformational fluctuations, and electrostatic interactions in the synergistic folding of two intrinsically disordered proteins. PLoS Comp Biol 8: e1002353.
    • (2012) PLoS Comp Biol , vol.8
    • Zhang, W.H.1    Ganguly, D.2    Chen, J.H.3
  • 18
    • 0025702333 scopus 로고
    • Potassium channels - mixing and matching
    • Aldrich RW. 1990. Potassium channels - mixing and matching. Nature 345: 475- 6.
    • (1990) Nature , vol.345 , pp. 475-476
    • Aldrich, R.W.1
  • 19
    • 0035822126 scopus 로고    scopus 로고
    • Fifty years of inactivation
    • Aldrich RW. 2001. Fifty years of inactivation. Nature 411: 643- 4.
    • (2001) Nature , vol.411 , pp. 643-644
    • Aldrich, R.W.1
  • 20
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • Hoshi T, Zagotta WN, Aldrich RW. 1990. Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science 250: 533- 8.
    • (1990) Science , vol.250 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 21
    • 33748997977 scopus 로고    scopus 로고
    • State-dependent block of BK channels by synthesized shaker ball peptides
    • Li WY, Aldrich RW. 2006. State-dependent block of BK channels by synthesized shaker ball peptides. J Gen Physiol 128: 423- 41.
    • (2006) J Gen Physiol , vol.128 , pp. 423-441
    • Li, W.Y.1    Aldrich, R.W.2
  • 22
    • 0027364807 scopus 로고
    • Functional stoichiometry of shaker potassium channel inactivation
    • Mackinnon R, Aldrich RW, Lee AW. 1993. Functional stoichiometry of shaker potassium channel inactivation. Science 262: 757- 9.
    • (1993) Science , vol.262 , pp. 757-759
    • Mackinnon, R.1    Aldrich, R.W.2    Lee, A.W.3
  • 23
    • 0027724707 scopus 로고
    • Interactions of amino-terminal domains of shaker K-channels with a pore blocking site studied with synthetic peptides
    • Murrell-Lagnado RD, Aldrich RW. 1993. Interactions of amino-terminal domains of shaker K-channels with a pore blocking site studied with synthetic peptides. J Gen Physiol 102: 949- 75.
    • (1993) J Gen Physiol , vol.102 , pp. 949-975
    • Murrell-Lagnado, R.D.1    Aldrich, R.W.2
  • 24
    • 0027753950 scopus 로고
    • Energetics of shaker K-channels block by inactivation peptides
    • Murrell-Lagnado RD, Aldrich RW. 1993. Energetics of shaker K-channels block by inactivation peptides. J Gen Physiol 102: 977- 1003.
    • (1993) J Gen Physiol , vol.102 , pp. 977-1003
    • Murrell-Lagnado, R.D.1    Aldrich, R.W.2
  • 25
    • 34247494332 scopus 로고    scopus 로고
    • BK channels with beta3a subunits generate use-dependent slow afterhyperpolarizing currents by an inactivation-coupled mechanism
    • Zeng XH, Benzinger GR, Xia XM, Lingle CJ. 2007. BK channels with beta3a subunits generate use-dependent slow afterhyperpolarizing currents by an inactivation-coupled mechanism. J Neurosci 27: 4707- 15.
    • (2007) J Neurosci , vol.27 , pp. 4707-4715
    • Zeng, X.H.1    Benzinger, G.R.2    Xia, X.M.3    Lingle, C.J.4
  • 26
    • 0032540008 scopus 로고    scopus 로고
    • Identifying Lys(359) as a critical residue for the ATP dependent reactions of Drosophila DNA topoisomerase II
    • Hu T, Chang S, Hsieh TS. 1998. Identifying Lys(359) as a critical residue for the ATP dependent reactions of Drosophila DNA topoisomerase II. J Biol Chem 273: 9586- 92.
    • (1998) J Biol Chem , vol.273 , pp. 9586-9592
    • Hu, T.1    Chang, S.2    Hsieh, T.S.3
  • 28
    • 84858267844 scopus 로고    scopus 로고
    • Proteome-wide discovery of evolutionary conserved sequences in disordered regions
    • Nguyen Ba AN, Yeh BJ, van Dyk D, Davidson AR, et al. 2012. Proteome-wide discovery of evolutionary conserved sequences in disordered regions. Sci Signal 5: rs1.
    • (2012) Sci Signal , vol.5
    • Nguyen Ba, A.N.1    Yeh, B.J.2    van Dyk, D.3    Davidson, A.R.4
  • 30
    • 42449123135 scopus 로고    scopus 로고
    • The effects of conformational heterogeneity on the binding of the Notch intracellular domain to effector proteins: a case of biologically tuned disorder
    • Bertagna A, Toptygin D, Brand L, Barrick D. 2008. The effects of conformational heterogeneity on the binding of the Notch intracellular domain to effector proteins: a case of biologically tuned disorder. Biochem Soc Trans 36: 157- 66.
    • (2008) Biochem Soc Trans , vol.36 , pp. 157-166
    • Bertagna, A.1    Toptygin, D.2    Brand, L.3    Barrick, D.4
  • 31
    • 77952335311 scopus 로고    scopus 로고
    • Net charge per residue modulates conformational ensembles of intrinsically disordered proteins
    • Mao AH, Crick SL, Vitalis A, Chicoine CL, et al. 2010. Net charge per residue modulates conformational ensembles of intrinsically disordered proteins. Proc Natl Acad Sci USA 107: 8183- 8.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 8183-8188
    • Mao, A.H.1    Crick, S.L.2    Vitalis, A.3    Chicoine, C.L.4
  • 32
    • 77957092799 scopus 로고    scopus 로고
    • Charge interactions can dominate the dimensions of intrinsically disordered proteins
    • Muller-Spath S, Soranno A, Hirschfeld V, Hofmann H, et al. 2010. Charge interactions can dominate the dimensions of intrinsically disordered proteins. Proc Natl Acad Sci USA 107: 14609- 14.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 14609-14614
    • Muller-Spath, S.1    Soranno, A.2    Hirschfeld, V.3    Hofmann, H.4
  • 33
    • 77951645923 scopus 로고    scopus 로고
    • Sequence determinants of compaction in intrinsically disordered proteins
    • Marsh JA, Forman-Kay JD. 2010. Sequence determinants of compaction in intrinsically disordered proteins. Biophys J 98: 2383- 90.
    • (2010) Biophys J , vol.98 , pp. 2383-2390
    • Marsh, J.A.1    Forman-Kay, J.D.2
  • 34
    • 78650453629 scopus 로고    scopus 로고
    • DNA search efficiency is modulated by charge composition and distribution in the intrinsically disordered tail
    • Vuzman D, Levy Y. 2010. DNA search efficiency is modulated by charge composition and distribution in the intrinsically disordered tail. Proc Natl Acad Sci USA 107: 21004- 9.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 21004-21009
    • Vuzman, D.1    Levy, Y.2
  • 35
    • 84856434005 scopus 로고    scopus 로고
    • N-terminal segments modulate the alpha-helical propensities of the intrinsically disordered basic regions of bZIP proteins
    • Das RK, Crick SL, Pappu RV. 2012. N-terminal segments modulate the alpha-helical propensities of the intrinsically disordered basic regions of bZIP proteins. J Mol Biol 416: 287- 99.
    • (2012) J Mol Biol , vol.416 , pp. 287-299
    • Das, R.K.1    Crick, S.L.2    Pappu, R.V.3
  • 36
    • 84859976535 scopus 로고    scopus 로고
    • Unmasking functional motifs within disordered regions of proteins
    • Das RK, Mao AH, Pappu RV. 2012. Unmasking functional motifs within disordered regions of proteins. Sci Signal 5: pe17.
    • (2012) Sci Signal , vol.5
    • Das, R.K.1    Mao, A.H.2    Pappu, R.V.3
  • 37
    • 84866463338 scopus 로고    scopus 로고
    • Versatility from protein disorder
    • Babu MM, Kriwacki RW, Pappu RV. 2012. Versatility from protein disorder. Science 337: 1460- 1.
    • (2012) Science , vol.337 , pp. 1460-1461
    • Babu, M.M.1    Kriwacki, R.W.2    Pappu, R.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.