메뉴 건너뛰기




Volumn 109, Issue 5, 2012, Pages 1490-1493

β-Bulge triggers route-switching on the functional landscape of interleukin-1β

Author keywords

Geometric frustration; Pulse labeling

Indexed keywords

INTERLEUKIN 1BETA;

EID: 84857131739     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1114430109     Document Type: Article
Times cited : (25)

References (29)
  • 2
    • 48249140760 scopus 로고    scopus 로고
    • Multiple routes and structural heterogeneity in protein folding
    • Udgaonkar JB (2008) Multiple routes and structural heterogeneity in protein folding. Annu Rev Biophys 37:489-510.
    • (2008) Annu Rev Biophys , vol.37 , pp. 489-510
    • Udgaonkar, J.B.1
  • 3
    • 0034581317 scopus 로고    scopus 로고
    • The energy landscape theory of protein folding: Insights into folding mechanisms and scenarios
    • DOI 10.1016/S0065-3233(00)53003-4
    • Onuchic JN, Nymeyer H, Garcia AE, Chahine J, Socci ND (2000) The energy landscape theory of protein folding: Insights into folding mechanisms and scenarios. Adv Protein Chem 53:87-152. (Pubitemid 34194293)
    • (2000) Advances in Protein Chemistry , vol.53 , pp. 87-152
    • Onuchic, J.N.1    Nymeyer, H.2    Garcia, A.E.3    Chahine, J.4    Socci, N.D.5
  • 4
    • 0038329308 scopus 로고    scopus 로고
    • Folding at the speed limit
    • DOI 10.1038/nature01609
    • Yang WY, Gruebele M (2003) Folding at the speed limit. Nature 423:193-197. (Pubitemid 36569545)
    • (2003) Nature , vol.423 , Issue.6936 , pp. 193-197
    • Yang, W.Y.1    Gruebele, M.2
  • 6
    • 0028774340 scopus 로고
    • Stability and function: Two constraints in the evolution of barstar and other proteins
    • Schreiber G, Buckle AM, Fersht AR (1994) Stability and function: Two constraints in the evolution of barstar and other proteins. Structure 2:945-951.
    • (1994) Structure , vol.2 , pp. 945-951
    • Schreiber, G.1    Buckle, A.M.2    Fersht, A.R.3
  • 8
    • 78650486925 scopus 로고    scopus 로고
    • Energetics and mechanisms of folding and flipping the myristoyl switch in the β-trefoil protein, hisactophilin
    • Smith MT, Meissner J, Esmonde S, Wong HJ, Meiering EM (2010) Energetics and mechanisms of folding and flipping the myristoyl switch in the β-trefoil protein, hisactophilin. Proc Natl Acad Sci USA 107:20952-20957.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 20952-20957
    • Smith, M.T.1    Meissner, J.2    Esmonde, S.3    Wong, H.J.4    Meiering, E.M.5
  • 9
    • 33645030244 scopus 로고    scopus 로고
    • Topological frustration and the folding of interleukin-1?
    • Gosavi S, Chavez LL, Jennings PA, Onuchic JN (2006) Topological frustration and the folding of interleukin-1?. J Mol Biol 357:986-996.
    • (2006) J Mol Biol , vol.357 , pp. 986-996
    • Gosavi, S.1    Chavez, L.L.2    Jennings, P.A.3    Onuchic, J.N.4
  • 11
    • 0028085946 scopus 로고
    • Deletion mutants of human interleukin 1beta with significantly reduced agonist properties: Search for the agonist/antagonist switch in ligands to the interleukin 1 receptors
    • DOI 10.1016/1043-4666(94)90043-4
    • Simoncsits A, et al. (1994) Deletion mutants of human interleukin-1β with significantly reduced agonist properties: Search for the agonist/antagonist switch in ligands to the interleukin 1 receptors. Cytokines 6:206-214. (Pubitemid 24263860)
    • (1994) Cytokine , vol.6 , Issue.2 , pp. 206-214
    • Simoncsits, A.1    Bristulf, J.2    Tjornhammar, M.L.3    Cserzo, M.4    Pongor, S.5    Rybakina, E.6    Gatti, S.7    Bartfai, T.8
  • 12
    • 0026551727 scopus 로고
    • Functional implications of interleukin-1β based on the 3-dimensional structure
    • Veerapandian B, et al. (1992) Functional implications of interleukin-1β based on the 3-dimensional structure. Proteins 12:10-23.
    • (1992) Proteins , vol.12 , pp. 10-23
    • Veerapandian, B.1
  • 14
    • 0025109109 scopus 로고
    • 13C resonances of interleukin-1beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy
    • DOI 10.1021/bi00487a027
    • Clore GM, Bax A, Driscoll PC, Wingfield PT, Gronenborn AM (1990) Assignment of the side-chain H-1 and C-13 resonances of interleukin-1β using double-resonance and triple-resonance heteronuclear 3-dimensional NMR-spectroscopy. Biochemistry 29:8172-8184. (Pubitemid 20283306)
    • (1990) Biochemistry , vol.29 , Issue.35 , pp. 8172-8184
    • Clore, G.M.1    Bax, A.2    Driscoll, P.C.3    Wingfield, P.T.4    Gronenborn, A.M.5
  • 15
    • 0030772992 scopus 로고    scopus 로고
    • Evidence for an obligatory intermediate in the folding of interleukin- 1beta
    • DOI 10.1038/nsb0997-725
    • Heidary DK, Gross LA, Roy M, Jennings PA (1997) Evidence for an obligatory intermediate in the folding of interleukin-1β. Nat Struct Biol 4:725-731. (Pubitemid 27382432)
    • (1997) Nature Structural Biology , vol.4 , Issue.9 , pp. 725-731
    • Heidary, D.K.1    Gross, L.A.2    Roy, M.3    Jennings, P.A.4
  • 17
    • 27144438673 scopus 로고    scopus 로고
    • Long-range coupling between separate docking sites in interleukin-1beta
    • DOI 10.1016/j.jmb.2005.08.072, PII S0022283605010521
    • Heidary DK, Roy M, Daumy GO, Cong Y, Jennings PA (2005) Long-range coupling between separate docking sites in interleukin-1β. J Mol Biol 353:1187-1198. (Pubitemid 41503282)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.5 , pp. 1187-1198
    • Heidary, D.K.1    Roy, M.2    Daumy, G.O.3    Cong, Y.4    Jennings, P.A.5
  • 19
    • 0026096545 scopus 로고
    • Study of the molten globule intermediate state in protein folding by a hydrophobic fluorescent probe
    • Semisotnov GV, et al. (1991) Study of the molten globule intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers 31:119-128.
    • (1991) Biopolymers , vol.31 , pp. 119-128
    • Semisotnov, G.V.1
  • 20
    • 0028561835 scopus 로고
    • Development of nonpolar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by 1-anilinonaphthalene- 8-sulfonate binding
    • Jones BE, Jennings PA, Pierre RA, Matthews CR (1994) Development of nonpolar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by 1-anilinonaphthalene- 8-sulfonate binding. Biochemistry 33:15250-15258.
    • (1994) Biochemistry , vol.33 , pp. 15250-15258
    • Jones, B.E.1    Jennings, P.A.2    Pierre, R.A.3    Matthews, C.R.4
  • 21
    • 0035688271 scopus 로고    scopus 로고
    • Early aggregated states in the folding of interleukin-1beta
    • DOI 10.1023/A:1013178505077
    • Finke JM, Jennings PA (2001) Early aggregated states in the folding of interleukin-1β. J Biol Phys 27:119-131. (Pubitemid 34062478)
    • (2001) Journal of Biological Physics , vol.27 , Issue.2-3 , pp. 119-131
    • Finke, J.M.1    Jennings, P.A.2
  • 22
    • 0028947956 scopus 로고
    • Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR
    • Jones BE, Matthews CR (1995) Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR. Protein Sci 4:167-177.
    • (1995) Protein Sci , vol.4 , pp. 167-177
    • Jones, B.E.1    Matthews, C.R.2
  • 23
    • 0026653655 scopus 로고
    • Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR
    • Englander SW, Mayne L (1992) Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR. Annu Rev Biophys Biomol Struct 21:243-265.
    • (1992) Annu Rev Biophys Biomol Struct , vol.21 , pp. 243-265
    • Englander, S.W.1    Mayne, L.2
  • 24
    • 0028781460 scopus 로고
    • Experimental support for the 'hydrophogic zipper' hypothesis
    • Gronenborn AM, Clore GM (1994) Experimental support for the hydrophobic zipper hypothesis. Science 263:536. (Pubitemid 24082756)
    • (1994) Science , vol.263 , Issue.5146 , pp. 536
    • Gronenborn, A.M.1    Clore, G.M.2
  • 25
    • 27144510594 scopus 로고    scopus 로고
    • Symmetric connectivity of secondary structure elements enhances the diversity of folding pathways
    • DOI 10.1016/j.jmb.2005.09.029, PII S0022283605010946
    • Klimov DK, Thirumalai D (2005) Symmetric connectivity of secondary structure elements enhances the diversity of folding pathways. J Mol Biol 353:1171-1186. (Pubitemid 41503281)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.5 , pp. 1171-1186
    • Klimov, D.K.1    Thirumalai, D.2
  • 26
    • 54449086396 scopus 로고    scopus 로고
    • Backtracking on the folding landscape of the β-trefoil protein interleukin-1β?
    • Capraro DT, Roy M, Onuchic JN, Jennings PA (2008) Backtracking on the folding landscape of the β-trefoil protein interleukin-1β? Proc Natl Acad Sci USA 105:14844-14848.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14844-14848
    • Capraro, D.T.1    Roy, M.2    Onuchic, J.N.3    Jennings, P.A.4
  • 27
    • 0027426934 scopus 로고
    • Breakdown in the relationship between thermal and thermodynamic stability in an interleukin-1beta point mutant modified in a surface loop
    • Chrunyk BA, Wetzel R (1993) Breakdown in the relationship between thermal and thermodynamic stability in an interleukin-1β point mutant modified in a surface loop. Protein Eng 6:733-738. (Pubitemid 23293202)
    • (1993) Protein Engineering , vol.6 , Issue.7 , pp. 733-738
    • Chrunyk, B.A.1    Wetzel, R.2
  • 28


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.