메뉴 건너뛰기




Volumn 33, Issue 1, 2009, Pages 41-45

Aggregation mechanism investigation of the GIFQINS cross-β amyloid fibril

Author keywords

Aggregation mechanism; Amyloid like fibril; Intermediate state; Transition state

Indexed keywords

DISSOLUTION; DYNAMICS; MOLECULAR DYNAMICS; POLYPEPTIDES; QUANTUM CHEMISTRY;

EID: 57749195950     PISSN: 14769271     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.compbiolchem.2008.07.023     Document Type: Article
Times cited : (21)

References (32)
  • 2
    • 33751104733 scopus 로고    scopus 로고
    • Aggregating the amyloid Abeta(11-25) peptide into a four-stranded beta-sheet structure
    • Boucher G., Mousseau N., and Derreumaux P. Aggregating the amyloid Abeta(11-25) peptide into a four-stranded beta-sheet structure. Proteins 65 (2006) 877-888
    • (2006) Proteins , vol.65 , pp. 877-888
    • Boucher, G.1    Mousseau, N.2    Derreumaux, P.3
  • 3
    • 0028264860 scopus 로고
    • Molecular-dynamics simulation of protein denaturation-solvation of the hydrophobic cores and secondary structure of barnase
    • Caflisch A., and Karplus M. Molecular-dynamics simulation of protein denaturation-solvation of the hydrophobic cores and secondary structure of barnase. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 1746-1750
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1746-1750
    • Caflisch, A.1    Karplus, M.2
  • 4
    • 57749174350 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding in the siRNA-PAZ complex
    • Chen H.F. Mechanism of coupled folding and binding in the siRNA-PAZ complex. J. Chem. Theory Comput. 4 (2008) 1360-1368
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 1360-1368
    • Chen, H.F.1
  • 5
    • 33947252405 scopus 로고    scopus 로고
    • Binding induced folding in p53-MDM2 complex
    • Chen H.F., and Luo R. Binding induced folding in p53-MDM2 complex. J. Am. Chem. Soc. 129 (2007) 2930-2937
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 2930-2937
    • Chen, H.F.1    Luo, R.2
  • 6
    • 10044265557 scopus 로고    scopus 로고
    • Dimerization of the p53 oligomerization domain: identification of a folding nucleus by molecular dynamics simulations
    • Chong L.T., Snow C.D., Rhee Y.M., and Pande V.S. Dimerization of the p53 oligomerization domain: identification of a folding nucleus by molecular dynamics simulations. J. Mol. Biol. 345 (2005) 869-878
    • (2005) J. Mol. Biol. , vol.345 , pp. 869-878
    • Chong, L.T.1    Snow, C.D.2    Rhee, Y.M.3    Pande, V.S.4
  • 7
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: amyloid growth occurs by monomer addition
    • Collins S.R., Douglass A., Vale R.D., and Weissman J.S. Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol. 2 (2004) e321
    • (2004) PLoS Biol. , vol.2
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3    Weissman, J.S.4
  • 8
    • 0029981188 scopus 로고    scopus 로고
    • Structure of the transition state for folding of a protein derived from experiment and simulation
    • Daggett V., Li A.J., Itzhaki L.S., Otzen D.E., and Fersht A.R. Structure of the transition state for folding of a protein derived from experiment and simulation. J. Mol. Biol. 257 (1996) 430-440
    • (1996) J. Mol. Biol. , vol.257 , pp. 430-440
    • Daggett, V.1    Li, A.J.2    Itzhaki, L.S.3    Otzen, D.E.4    Fersht, A.R.5
  • 9
    • 1442330474 scopus 로고    scopus 로고
    • From conversion to aggregation: protofibril formation of the prion protein
    • DeMarco M.L., and Daggett V. From conversion to aggregation: protofibril formation of the prion protein. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 2293-2298
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 2293-2298
    • DeMarco, M.L.1    Daggett, V.2
  • 10
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24 (1999) 329-332
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 11
    • 33746800825 scopus 로고    scopus 로고
    • Molecular dynamics analyses of cross-beta-spine steric zipper models: beta-sheet twisting and aggregation
    • Esposito L., Pedone C., and Vitagliano L. Molecular dynamics analyses of cross-beta-spine steric zipper models: beta-sheet twisting and aggregation. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 11533-11538
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 11533-11538
    • Esposito, L.1    Pedone, C.2    Vitagliano, L.3
  • 12
    • 33644536691 scopus 로고    scopus 로고
    • Atomic-level description of amyloid beta-dimer formation
    • Gnanakaran S., Nussinov R., and Garcia A.E. Atomic-level description of amyloid beta-dimer formation. J. Am. Chem. Soc. 128 (2006) 2158-2159
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 2158-2159
    • Gnanakaran, S.1    Nussinov, R.2    Garcia, A.E.3
  • 13
    • 0035946940 scopus 로고    scopus 로고
    • Role of native topology investigated by multiple unfolding simulations of four SH3 domains
    • Gsponer J., and Caflisch A. Role of native topology investigated by multiple unfolding simulations of four SH3 domains. J. Mol. Biol. 309 (2001) 285-298
    • (2001) J. Mol. Biol. , vol.309 , pp. 285-298
    • Gsponer, J.1    Caflisch, A.2
  • 14
    • 0037076334 scopus 로고    scopus 로고
    • Molecular dynamics simulations of protein folding from the transition state
    • Gsponer J., and Caflisch A. Molecular dynamics simulations of protein folding from the transition state. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 6719-6724
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 6719-6724
    • Gsponer, J.1    Caflisch, A.2
  • 16
    • 44949166524 scopus 로고    scopus 로고
    • Benchmarking implicit solvent folding simulations of the amyloid beta(10-35) fragment
    • Kent A., Jha A.K., Fitzgerald J.E., and Freed K.F. Benchmarking implicit solvent folding simulations of the amyloid beta(10-35) fragment. J. Phys. Chem. B 112 (2008) 6175-6186
    • (2008) J. Phys. Chem. B , vol.112 , pp. 6175-6186
    • Kent, A.1    Jha, A.K.2    Fitzgerald, J.E.3    Freed, K.F.4
  • 17
    • 0032555115 scopus 로고    scopus 로고
    • Synergy between simulation and experiment in describing the energy landscape of protein folding
    • Ladurner A.G., Itzhaki L.S., Daggett V., and Fersht A.R. Synergy between simulation and experiment in describing the energy landscape of protein folding. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 8473-8478
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 8473-8478
    • Ladurner, A.G.1    Itzhaki, L.S.2    Daggett, V.3    Fersht, A.R.4
  • 18
    • 19444380574 scopus 로고    scopus 로고
    • Protein misfolding and amyloid formation for the peptide GNNQQNY from yeast prion protein Sup35: simulation by reaction path annealing
    • Lipfert J., Franklin J., Wu F., and Doniach S. Protein misfolding and amyloid formation for the peptide GNNQQNY from yeast prion protein Sup35: simulation by reaction path annealing. J. Mol. Biol. 349 (2005) 648-658
    • (2005) J. Mol. Biol. , vol.349 , pp. 648-658
    • Lipfert, J.1    Franklin, J.2    Wu, F.3    Doniach, S.4
  • 19
    • 0034610360 scopus 로고    scopus 로고
    • Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation
    • Mayor U., Johnson C.M., Daggett V., and Fersht A.R. Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 13518-13522
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13518-13522
    • Mayor, U.1    Johnson, C.M.2    Daggett, V.3    Fersht, A.R.4
  • 21
    • 28844499140 scopus 로고    scopus 로고
    • Exploring the early steps of amyloid peptide aggregation by computers
    • Mousseau N., and Derreumaux P. Exploring the early steps of amyloid peptide aggregation by computers. Acc. Chem. Res. 38 (2005) 885-891
    • (2005) Acc. Chem. Res. , vol.38 , pp. 885-891
    • Mousseau, N.1    Derreumaux, P.2
  • 23
    • 9244260521 scopus 로고    scopus 로고
    • Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides
    • Nguyen H.D., and Hall C.K. Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 16180-16185
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 16180-16185
    • Nguyen, H.D.1    Hall, C.K.2
  • 24
    • 0033529908 scopus 로고    scopus 로고
    • Molecular dynamics simulations of unfolding and refolding of a beta-hairpin fragment of protein G
    • Pande V.S., and Rokhsar D.S. Molecular dynamics simulations of unfolding and refolding of a beta-hairpin fragment of protein G. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 9062-9067
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 9062-9067
    • Pande, V.S.1    Rokhsar, D.S.2
  • 26
    • 0033849738 scopus 로고    scopus 로고
    • Review: history of the amyloid fibril
    • Sipe J.D., and Cohen A.S. Review: history of the amyloid fibril. J. Struct. Biol. 130 (2000) 88-98
    • (2000) J. Struct. Biol. , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 29
    • 16344367783 scopus 로고    scopus 로고
    • Formation of partially ordered oligomers of amyloidogenic hexapeptide (NFGAIL) in aqueous solution observed in molecular dynamics simulations
    • Wu C., Lei H., and Duan Y. Formation of partially ordered oligomers of amyloidogenic hexapeptide (NFGAIL) in aqueous solution observed in molecular dynamics simulations. Biophys. J. 87 (2004) 3000-3009
    • (2004) Biophys. J. , vol.87 , pp. 3000-3009
    • Wu, C.1    Lei, H.2    Duan, Y.3
  • 30
    • 25844456992 scopus 로고    scopus 로고
    • Elongation of ordered peptide aggregate of an amyloidogenic hexapeptide NFGAIL observed in molecular dynamics simulations with explicit solvent
    • Wu C., Lei H., and Duan Y. Elongation of ordered peptide aggregate of an amyloidogenic hexapeptide NFGAIL observed in molecular dynamics simulations with explicit solvent. J. Am. Chem. Soc. 127 (2005) 13530-13537
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 13530-13537
    • Wu, C.1    Lei, H.2    Duan, Y.3
  • 31
    • 33746765060 scopus 로고    scopus 로고
    • Structural stability and dynamics of an amyloid-forming peptide GNNQQNY from the yeast prion sup-35
    • Zheng J., Ma B., Tsai C.J., and Nussinov R. Structural stability and dynamics of an amyloid-forming peptide GNNQQNY from the yeast prion sup-35. Biophys. J. 91 (2006) 824-833
    • (2006) Biophys. J. , vol.91 , pp. 824-833
    • Zheng, J.1    Ma, B.2    Tsai, C.J.3    Nussinov, R.4
  • 32
    • 39749090561 scopus 로고    scopus 로고
    • Beta2-microglobulin amyloid fragment organization and morphology and its comparison to Abeta suggests that amyloid aggregation pathways are sequence specific
    • Zheng J., Jang H., and Nussinov R. Beta2-microglobulin amyloid fragment organization and morphology and its comparison to Abeta suggests that amyloid aggregation pathways are sequence specific. Biochemistry 47 (2008) 2497-2509
    • (2008) Biochemistry , vol.47 , pp. 2497-2509
    • Zheng, J.1    Jang, H.2    Nussinov, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.