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Volumn 105, Issue 39, 2008, Pages 14844-14848

Backtracking on the folding landscape of the β-trefoil protein interleukin-1β?

Author keywords

Protein folding; Real time NMR

Indexed keywords

INTERLEUKIN 1BETA; TREFOIL PEPTIDE;

EID: 54449086396     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0807812105     Document Type: Article
Times cited : (65)

References (34)
  • 1
    • 33745931359 scopus 로고    scopus 로고
    • Multiple routes lead to the native state in the energy landscape of the β-trefoil family
    • Chavez LL, Gosavi S, Jennings PA, Onuchic JN (2006) Multiple routes lead to the native state in the energy landscape of the β-trefoil family. Proc Natl Acad Sci USA 103:10254-10258.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10254-10258
    • Chavez, L.L.1    Gosavi, S.2    Jennings, P.A.3    Onuchic, J.N.4
  • 2
    • 33645030244 scopus 로고    scopus 로고
    • Topological frustration and the folding of interleukin-1β
    • Gosavi S, Chavez LL, Jennings PA, Onuchic JN (2006) Topological frustration and the folding of interleukin-1β. 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
  • 3
    • 0026556882 scopus 로고
    • β-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1β and 1α and fibroblast growth factors
    • Murzin AG, Lesk AM, Chothia C (1992) β-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1β and 1α and fibroblast growth factors. J Mol Biol 223:531-543.
    • (1992) J Mol Biol , vol.223 , pp. 531-543
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 4
    • 0028330220 scopus 로고
    • Principles determining the structure of β-sheet barrels in proteins. II. The observed structures
    • Murzin AG, Lesk AM, Chothia C (1994) Principles determining the structure of β-sheet barrels in proteins. II. The observed structures. J Mol Biol 236:1382-1400.
    • (1994) J Mol Biol , vol.236 , pp. 1382-1400
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 5
    • 24344443170 scopus 로고    scopus 로고
    • Redesigning symmetry-related "mini-core" regions of FGF-1 to increase primary structure symmetry: Thermodynamic and functional consequences of structural symmetry
    • Dubey VK, Lee J, Blaber M (2005) Redesigning symmetry-related "mini-core" regions of FGF-1 to increase primary structure symmetry: Thermodynamic and functional consequences of structural symmetry. Protein Sci 14:2315-2323.
    • (2005) Protein Sci , vol.14 , pp. 2315-2323
    • Dubey, V.K.1    Lee, J.2    Blaber, M.3
  • 6
    • 4544298192 scopus 로고    scopus 로고
    • Toward the detection and validation of repeats in protein structure
    • Murray KB, Taylor WR, Thornton JM (2004) Toward the detection and validation of repeats in protein structure. Proteins 57:365-380.
    • (2004) Proteins , vol.57 , pp. 365-380
    • Murray, K.B.1    Taylor, W.R.2    Thornton, J.M.3
  • 7
    • 0036183061 scopus 로고    scopus 로고
    • Conserved and nonconserved features of the folding pathway of hisactophilin, a β-trefoil protein
    • Liu C, Gaspar JA, Wong HJ, Meiering EM (2002) Conserved and nonconserved features of the folding pathway of hisactophilin, a β-trefoil protein. Protein Sci 11:669-679.
    • (2002) Protein Sci , vol.11 , pp. 669-679
    • Liu, C.1    Gaspar, J.A.2    Wong, H.J.3    Meiering, E.M.4
  • 8
    • 0035799360 scopus 로고    scopus 로고
    • Thermodynamics of denaturation of hisactophilin, a β-trefoil protein
    • Liu C, et al. (2001) Thermodynamics of denaturation of hisactophilin, a β-trefoil protein. Biochemistry 40:3817-3827.
    • (2001) Biochemistry , vol.40 , pp. 3817-3827
    • Liu, C.1
  • 9
    • 0038043276 scopus 로고    scopus 로고
    • Amyloid-like fibril formation in an all β-barrel protein: Partially structured intermediate state (s) is a precursor for fibril formation
    • Srisailam S, et al. (2003) Amyloid-like fibril formation in an all β-barrel protein: Partially structured intermediate state (s) is a precursor for fibril formation. J Biol Chem 278:17701-17709.
    • (2003) J Biol Chem , vol.278 , pp. 17701-17709
    • Srisailam, S.1
  • 10
    • 0035954372 scopus 로고    scopus 로고
    • Thermodynamic characterization of the human acidic fibroblast growth factor: Evidence for cold denaturation
    • Chi Y, et al. (2001) Thermodynamic characterization of the human acidic fibroblast growth factor: Evidence for cold denaturation. Biochemistry 40:7746-7753.
    • (2001) Biochemistry , vol.40 , pp. 7746-7753
    • Chi, Y.1
  • 11
    • 0030772992 scopus 로고    scopus 로고
    • Evidence for an obligatory intermediate in the folding of interleukin-1β
    • 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.
    • (1997) Nat Struct Biol , vol.4 , pp. 725-731
    • Heidary, D.K.1    Gross, L.A.2    Roy, M.3    Jennings, P.A.4
  • 12
    • 0027190613 scopus 로고
    • Kinetics of folding of the all β-sheet protein interleukin-1-β
    • Varley P, et al. (1993) Kinetics of folding of the all β-sheet protein interleukin-1-β. Science 260:1110-1113.
    • (1993) Science , vol.260 , pp. 1110-1113
    • Varley, P.1
  • 13
    • 0034705115 scopus 로고    scopus 로고
    • How native-state topology affects the folding of dihydrofolate reductase and interleukin-1β
    • Clementi C, Jennings PA, Onuchic JN (2000) How native-state topology affects the folding of dihydrofolate reductase and interleukin-1β. Proc Natl Acad Sci USA 97:5871-5876.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5871-5876
    • Clementi, C.1    Jennings, P.A.2    Onuchic, J.N.3
  • 14
    • 0037414459 scopus 로고    scopus 로고
    • Real-time NMR kinetic studies provide global and residue-specific information on the noncooperative unfolding of the β-trefoil protein, interleukin-1β
    • Roy M, Jennings PA (2003) Real-time NMR kinetic studies provide global and residue-specific information on the noncooperative unfolding of the β-trefoil protein, interleukin-1β. J Mol Biol 328:693-703.
    • (2003) J Mol Biol , vol.328 , pp. 693-703
    • Roy, M.1    Jennings, P.A.2
  • 15
    • 0029001090 scopus 로고
    • Direct Nmr evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A
    • Kiefhaber T, Labhardt AM, Baldwin RL (1995) Direct Nmr evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A. Nature 375:513-515.
    • (1995) Nature , vol.375 , pp. 513-515
    • Kiefhaber, T.1    Labhardt, A.M.2    Baldwin, R.L.3
  • 16
    • 0009806775 scopus 로고
    • Novel method for Nmr spectral correlation between the native and the denatured states of a protein: Application to ribonuclease A
    • Akasaka K, Naito A, Imanari M (1991) Novel method for Nmr spectral correlation between the native and the denatured states of a protein: Application to ribonuclease A. J Am Chem Soc 113:4688-4689.
    • (1991) J Am Chem Soc , vol.113 , pp. 4688-4689
    • Akasaka, K.1    Naito, A.2    Imanari, M.3
  • 17
    • 0024278405 scopus 로고
    • Structural studies of a folding intermediate of bovine pancreatic ribonuclease A by continuous recycled flow
    • Adler M, Scheraga HA (1988) Structural studies of a folding intermediate of bovine pancreatic ribonuclease A by continuous recycled flow. Biochemistry 27:2471-2480.
    • (1988) Biochemistry , vol.27 , pp. 2471-2480
    • Adler, M.1    Scheraga, H.A.2
  • 18
    • 0027489831 scopus 로고
    • Nmr and protein folding: Equilibrium and stopped-flow studies
    • Frieden C, Hoeltzli SD, Ropson IJ (1993) Nmr and protein folding: Equilibrium and stopped-flow studies. Protein Sci 2:2007-2014.
    • (1993) Protein Sci , vol.2 , pp. 2007-2014
    • Frieden, C.1    Hoeltzli, S.D.2    Ropson, I.J.3
  • 19
    • 0027370063 scopus 로고
    • Characterization of a folding intermediate of apoplastocyanin trapped by proline isomerization
    • Koide S, Dyson HJ, Wright PE (1993) Characterization of a folding intermediate of apoplastocyanin trapped by proline isomerization. Biochemistry 32:12299-12310.
    • (1993) Biochemistry , vol.32 , pp. 12299-12310
    • Koide, S.1    Dyson, H.J.2    Wright, P.E.3
  • 20
    • 34547463005 scopus 로고    scopus 로고
    • Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy
    • Schanda P, Forge V, Brutscher B (2007) Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy. Proc Natl Acad Sci USA 104:11257-11262.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 11257-11262
    • Schanda, P.1    Forge, V.2    Brutscher, B.3
  • 21
    • 0029123975 scopus 로고
    • Following protein folding in real time using Nmr spectroscopy
    • Balbach J, et al. (1995) Following protein folding in real time using Nmr spectroscopy. Nat Struct Biol 2:865-870.
    • (1995) Nat Struct Biol , vol.2 , pp. 865-870
    • Balbach, J.1
  • 22
    • 0037397705 scopus 로고    scopus 로고
    • Emerging ideas on the molecular basis of protein and peptide aggregation
    • Thirumalai D, Klimov DK, Dima RI (2003) Emerging ideas on the molecular basis of protein and peptide aggregation. Curr Opin Struct Biol 13:146-159.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 146-159
    • Thirumalai, D.1    Klimov, D.K.2    Dima, R.I.3
  • 23
    • 16244417212 scopus 로고    scopus 로고
    • The native energy landscape for interleukin-1β. Modulation of the population ensemble through native-state topology
    • Roy M, et al. (2005) The native energy landscape for interleukin-1β. Modulation of the population ensemble through native-state topology. J Mol Biol 348:335-347.
    • (2005) J Mol Biol , vol.348 , pp. 335-347
    • Roy, M.1
  • 24
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement, and the refolding rates of single domain proteins
    • Plaxco KW, Simons KT, Baker D (1998) Contact order, transition state placement, and the refolding rates of single domain proteins. J Mol Biol 277:985-994.
    • (1998) J Mol Biol , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 25
    • 0032708771 scopus 로고    scopus 로고
    • Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding
    • Chiti F, et al. (1999) Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat Struct Biol 6:1005-1009.
    • (1999) Nat Struct Biol , vol.6 , pp. 1005-1009
    • Chiti, F.1
  • 26
    • 0032474460 scopus 로고    scopus 로고
    • Folding of circular and permuted chymotrypsin inhibitor 2: Retention of the folding nucleus
    • Otzen DE, Fersht AR (1998) Folding of circular and permuted chymotrypsin inhibitor 2: Retention of the folding nucleus. Biochemistry 37:8139-8146.
    • (1998) Biochemistry , vol.37 , pp. 8139-8146
    • Otzen, D.E.1    Fersht, A.R.2
  • 27
    • 0035850732 scopus 로고    scopus 로고
    • Roles of native topology and chain-length scaling in protein folding: A simulation study with a Go-like model
    • Koga N, Takada S (2001) Roles of native topology and chain-length scaling in protein folding: A simulation study with a Go-like model. J Mol Biol 313:171-180.
    • (2001) J Mol Biol , vol.313 , pp. 171-180
    • Koga, N.1    Takada, S.2
  • 28
    • 0034652206 scopus 로고    scopus 로고
    • Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism
    • Fersht AR (2000) Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism. Proc Natl Acad Sci USA 97:1525-1529.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1525-1529
    • Fersht, A.R.1
  • 29
    • 33947312118 scopus 로고    scopus 로고
    • Intermediates and transition states in protein folding
    • Thirumalai D, Klimov DK (2007) Intermediates and transition states in protein folding. Methods Mol Biol 350:277-303.
    • (2007) Methods Mol Biol , vol.350 , pp. 277-303
    • Thirumalai, D.1    Klimov, D.K.2
  • 30
    • 0021095334 scopus 로고
    • Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor
    • Goldenberg DP, Creighton TE (1983) Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor. J Mol Biol 165:407-413.
    • (1983) J Mol Biol , vol.165 , pp. 407-413
    • Goldenberg, D.P.1    Creighton, T.E.2
  • 31
    • 1942505822 scopus 로고    scopus 로고
    • Alteration of the disulfide-coupled folding pathway of BPTI by circular permutation
    • Bulaj G, Koehn RE, Goldenberg DP (2004) Alteration of the disulfide-coupled folding pathway of BPTI by circular permutation. Protein Sci 13:1182-1196.
    • (2004) Protein Sci , vol.13 , pp. 1182-1196
    • Bulaj, G.1    Koehn, R.E.2    Goldenberg, D.P.3
  • 32
    • 27144438673 scopus 로고    scopus 로고
    • Long-range coupling between separate docking sites in interleukin-1β
    • 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.
    • (2005) J Mol Biol , vol.353 , pp. 1187-1198
    • Heidary, D.K.1    Roy, M.2    Daumy, G.O.3    Cong, Y.4    Jennings, P.A.5
  • 33
    • 0345804601 scopus 로고
    • A spin-echo technique for separation of multiplets in crowded spectra
    • Miao XJ, Freeman R (1995) A spin-echo technique for separation of multiplets in crowded spectra. J Magn Reson Ser A 116:273-276.
    • (1995) J Magn Reson Ser A , vol.116 , pp. 273-276
    • Miao, X.J.1    Freeman, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.