메뉴 건너뛰기




Volumn 358, Issue 1, 2006, Pages 330-345

Computational study of the fibril organization of polyglutamine repeats reveals a common motif identified in β-helices

Author keywords

Huntingtin protein; Polyglutamine repeats; Protofibril conformation; Structural analysis; helices

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; POLYGLUTAMINE;

EID: 33645101164     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.01.070     Document Type: Article
Times cited : (45)

References (42)
  • 1
    • 0038701684 scopus 로고    scopus 로고
    • Huntingtin aggregation and toxicity in Huntington's disease
    • G. Bates Huntingtin aggregation and toxicity in Huntington's disease Lancet 361 2003 1642 1644
    • (2003) Lancet , vol.361 , pp. 1642-1644
    • Bates, G.1
  • 2
    • 3543022080 scopus 로고    scopus 로고
    • Scrambled prion domains form prions and amyloid
    • E.D. Ross, U. Baxa, and R.B. Wickner Scrambled prion domains form prions and amyloid Mol. Cell. Biol. 24 2004 7206 7213
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7206-7213
    • Ross, E.D.1    Baxa, U.2    Wickner, R.B.3
  • 3
    • 8544260320 scopus 로고    scopus 로고
    • Characterization of the structure and the amyloidogenic properties of the Josephin domain of the polyglutamine-containing protein ataxin-3
    • L. Masino, G. Nicastro, R.P. Menon, F. Dal Piaz, L. Calder, and A. Pastore Characterization of the structure and the amyloidogenic properties of the Josephin domain of the polyglutamine-containing protein ataxin-3 J. Mol. Biol. 344 2004 1021 1035
    • (2004) J. Mol. Biol. , vol.344 , pp. 1021-1035
    • Masino, L.1    Nicastro, G.2    Menon, R.P.3    Dal Piaz, F.4    Calder, L.5    Pastore, A.6
  • 5
    • 0037062561 scopus 로고    scopus 로고
    • Amyloid-like features of polyglutamine aggregates and their assembly kinetics
    • S. Chen, V. Berthelier, J.B. Hamilton, B. O'Nuallain, and R. Wetzel Amyloid-like features of polyglutamine aggregates and their assembly kinetics Biochemistry 41 2002 7391 7399
    • (2002) Biochemistry , vol.41 , pp. 7391-7399
    • Chen, S.1    Berthelier, V.2    Hamilton, J.B.3    O'Nuallain, B.4    Wetzel, R.5
  • 6
    • 0037415751 scopus 로고    scopus 로고
    • From Alzheimer to Huntington: Why is a structural understanding so difficult?
    • P.A. Temussi, L. Masino, and A. Pastore From Alzheimer to Huntington: why is a structural understanding so difficult? EMBO J. 22 2003 355 361
    • (2003) EMBO J. , vol.22 , pp. 355-361
    • Temussi, P.A.1    Masino, L.2    Pastore, A.3
  • 7
    • 0041656292 scopus 로고    scopus 로고
    • The hunt for huntingtin function: Interaction partners tell many different stories
    • P. Harjes, and E.E. Wanker The hunt for huntingtin function: interaction partners tell many different stories Tibs 28 2003 425 433
    • (2003) Tibs , vol.28 , pp. 425-433
    • Harjes, P.1    Wanker, E.E.2
  • 9
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases
    • M. Perutz, T. Johnson, M. Suzuki, and J.T. Finch Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases Proc. Natl Acad. Sci. USA 91 1994 5355 5358
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5355-5358
    • Perutz, M.1    Johnson, T.2    Suzuki, M.3    Finch, J.T.4
  • 10
    • 0033450855 scopus 로고    scopus 로고
    • Folding of oligoglutamines: A theoretical approach based upon thermodynamics and molecular mechanics
    • E.B. Starikov, H. Lehrach, and E.E. Wanker Folding of oligoglutamines: a theoretical approach based upon thermodynamics and molecular mechanics J. Biomol. Struct. Dynam. 17 1999 409 427
    • (1999) J. Biomol. Struct. Dynam. , vol.17 , pp. 409-427
    • Starikov, E.B.1    Lehrach, H.2    Wanker, E.E.3
  • 11
    • 33645104343 scopus 로고    scopus 로고
    • Molecular modeling of poly-L-glutamine
    • Pinoli, M. L. & Busath, D. D. (2004). Molecular modeling of poly-l-glutamine. Biophys. J. 86 (Abstracts Supplemental, 616a).
    • (2004) Biophys. J. , vol.86 , Issue.ABSTRACTS SUPPL. 616A
    • Pinoli, M.L.1    Busath, D.D.2
  • 13
    • 14044278010 scopus 로고    scopus 로고
    • New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils
    • P. Sikorski, and E. Atkins New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils Biomacromolecules 6 2005 425 432
    • (2005) Biomacromolecules , vol.6 , pp. 425-432
    • Sikorski, P.1    Atkins, E.2
  • 15
    • 0037195098 scopus 로고    scopus 로고
    • Stabilities and conformations of Alzheimer's β-amyloid peptide oligomers (Aβ16-22, Aβ16-35, Aβ10-35)
    • B. Ma, and R. Nussinov Stabilities and conformations of Alzheimer's β-amyloid peptide oligomers (Aβ16-22, Aβ16-35, Aβ10-35) Proc. Natl Acad. Sci. USA 99 2002 14126 14131
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 14126-14131
    • Ma, B.1    Nussinov, R.2
  • 17
    • 0029764093 scopus 로고    scopus 로고
    • Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors
    • S. Steinbacher, U. Baxa, S. Miller, A. Weintraub, R. Seckler, and R. Huber Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors Proc. Natl Acad. Sci. USA 93 1996 10584 10588
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10584-10588
    • Steinbacher, S.1    Baxa, U.2    Miller, S.3    Weintraub, A.4    Seckler, R.5    Huber, R.6
  • 18
    • 0032539573 scopus 로고    scopus 로고
    • Amyloid fibrils may be assembled from β-helical protofibrils
    • N.D. Lazo, and D.T. Downing Amyloid fibrils may be assembled from β-helical protofibrils Biochemistry 37 1998 1731 1735
    • (1998) Biochemistry , vol.37 , pp. 1731-1735
    • Lazo, N.D.1    Downing, D.T.2
  • 19
    • 0035543109 scopus 로고    scopus 로고
    • The architecture of parallel β-helices and related folds
    • J. Jenkinsa, and R. Pickersgill The architecture of parallel β-helices and related folds Prog. Biophys. Mol. Biol. 77 2001 111 175
    • (2001) Prog. Biophys. Mol. Biol. , vol.77 , pp. 111-175
    • Jenkinsa, J.1    Pickersgill, R.2
  • 20
    • 0036052739 scopus 로고    scopus 로고
    • Ideas of order for amyloid fibril structure
    • R. Wetzel Ideas of order for amyloid fibril structure Structure 10 2002 1031 1036
    • (2002) Structure , vol.10 , pp. 1031-1036
    • Wetzel, R.1
  • 22
    • 4544335325 scopus 로고    scopus 로고
    • Molecular modeling of the core of Aβ amyloid fibrils
    • J. Guo, R. Wetzel, and Y. Xu Molecular modeling of the core of Aβ amyloid fibrils Proteins: Struct. Funct. Genet. 57 2004 357 364
    • (2004) Proteins: Struct. Funct. Genet. , vol.57 , pp. 357-364
    • Guo, J.1    Wetzel, R.2    Xu, Y.3
  • 23
    • 0028841116 scopus 로고
    • Stereochemical analysis of the antigenic tip of the V3 loop peptide of HIV-1 gp120
    • K. Gunasekaran, C. Ramakrishnan, and P. Balaram Stereochemical analysis of the antigenic tip of the V3 loop peptide of HIV-1 gp120 Int. J. Pept. Protein Res. 46 1995 359 365
    • (1995) Int. J. Pept. Protein Res. , vol.46 , pp. 359-365
    • Gunasekaran, K.1    Ramakrishnan, C.2    Balaram, P.3
  • 24
    • 0035874146 scopus 로고    scopus 로고
    • Analysis of a data set of paired uncomplexed protein structures: New metrics for side-chain flexibility and model evaluation
    • S. Zhao, D.S. Goodsell, and A.J. Olson Analysis of a data set of paired uncomplexed protein structures: new metrics for side-chain flexibility and model evaluation Proteins: Struct. Funct. Genet. 43 2001 271 279
    • (2001) Proteins: Struct. Funct. Genet. , vol.43 , pp. 271-279
    • Zhao, S.1    Goodsell, D.S.2    Olson, A.J.3
  • 25
    • 0028120050 scopus 로고
    • Comparison of two crystal structures of TGF-β2: The accuracy of refined protein structures
    • S. Daopin, D.R. Davies, M.P. Schlunegger, and M.G. Grütter Comparison of two crystal structures of TGF-β2: the accuracy of refined protein structures Acta Crystallog. sect. D 50 1994 85 92
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 85-92
    • Daopin, S.1    Davies, D.R.2    Schlunegger, M.P.3    Grütter, M.G.4
  • 27
    • 0032545165 scopus 로고    scopus 로고
    • Conformational interconversions in peptide β-turns: Analysis of turns in proteins and computational estimates of barriers
    • K. Gunasekaran, L. Gomathi, C. Ramakrishnan, J. Chandrasekhar, and P. Balaram Conformational interconversions in peptide β-turns: analysis of turns in proteins and computational estimates of barriers J. Mol. Biol. 284 1998 1505 1516
    • (1998) J. Mol. Biol. , vol.284 , pp. 1505-1516
    • Gunasekaran, K.1    Gomathi, L.2    Ramakrishnan, C.3    Chandrasekhar, J.4    Balaram, P.5
  • 28
    • 0037168642 scopus 로고    scopus 로고
    • Mutational analysis of the structural organization of polyglutamine aggregates
    • A.K. Thakur, and R. Wetzel Mutational analysis of the structural organization of polyglutamine aggregates Proc. Natl Acad. Sci. USA 99 2002 17014 17019
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 17014-17019
    • Thakur, A.K.1    Wetzel, R.2
  • 29
    • 0037015081 scopus 로고    scopus 로고
    • Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
    • S. Chen, F.A. Ferrone, and R. Wetzel Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation Proc. Natl Acad. Sci. USA 99 2002 11884 11889
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 11884-11889
    • Chen, S.1    Ferrone, F.A.2    Wetzel, R.3
  • 30
    • 27344435254 scopus 로고    scopus 로고
    • Polyglutamine aggregation nucleation: Thermodynamics of a highly unfavorable protein folding reaction
    • A.M. Bhattacharyya, A.K. Thakur, and R. Wetzel Polyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reaction Proc. Natl Acad. Sci. USA 102 2005 15400 15405
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 15400-15405
    • Bhattacharyya, A.M.1    Thakur, A.K.2    Wetzel, R.3
  • 32
    • 2542542833 scopus 로고    scopus 로고
    • A model for Ure2p prion filaments and other amyloids: The parallel superpleated-structure
    • V. Andrey, A.V. Kajava, U. Baxa, R.B. Wickner, and A.C. Steven A model for Ure2p prion filaments and other amyloids: the parallel superpleated- structure Proc. Natl Acad. Sci. USA 101 2004 7885 7890
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 7885-7890
    • Andrey, V.1    Kajava, A.V.2    Baxa, U.3    Wickner, R.B.4    Steven, A.C.5
  • 33
    • 84962473612 scopus 로고    scopus 로고
    • Binding in complex ionic systems: Anticooperative effects in systems stabilized by electrostatic interactions
    • C. Aleman, and D. Zanuy Binding in complex ionic systems: anticooperative effects in systems stabilized by electrostatic interactions Chem. Phys. Letters 343 2001 390 396
    • (2001) Chem. Phys. Letters , vol.343 , pp. 390-396
    • Aleman, C.1    Zanuy, D.2
  • 34
    • 0037339326 scopus 로고    scopus 로고
    • Short peptide amyloid organization: Stabilities and conformations of the islet amyloid peptide NFGAIL
    • D. Zanuy, B. Ma, and R. Nussinov Short peptide amyloid organization: stabilities and conformations of the islet amyloid peptide NFGAIL Biophys. J. 84 2003 1 11
    • (2003) Biophys. J. , vol.84 , pp. 1-11
    • Zanuy, D.1    Ma, B.2    Nussinov, R.3
  • 35
    • 1542686314 scopus 로고    scopus 로고
    • Peptide sequence and amyloid formation: Molecular simulations and experimental study of a human islet amyloid polypeptide fragment and its analogs
    • D. Zanuy, Y. Porat, E. Gazit, and R. Nussinov Peptide sequence and amyloid formation: molecular simulations and experimental study of a human islet amyloid polypeptide fragment and its analogs Structure 12 2004 439 455
    • (2004) Structure , vol.12 , pp. 439-455
    • Zanuy, D.1    Porat, Y.2    Gazit, E.3    Nussinov, R.4
  • 37
    • 0041784950 scopus 로고    scopus 로고
    • All-hydrogen empirical potential for molecular modeling and dynamics studies of proteins using the CHARMM22 force field
    • J.A.D. MacKerell, D. Bashford, M. Bellott, R.L. Dunbrack Jr, J. Evanseck, and M.J. Field All-hydrogen empirical potential for molecular modeling and dynamics studies of proteins using the CHARMM22 force field J. Phys. Chem. B 102 1998 3586 3616
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586-3616
    • MacKerell, J.A.D.1    Bashford, D.2    Bellott, M.3    Dunbrack Jr., R.L.4    Evanseck, J.5    Field, M.J.6
  • 39
    • 0033520751 scopus 로고    scopus 로고
    • Folding free energy surface of three-stranded β-sheet protein
    • B.D. Bursulaya, and C.L. Brooks III Folding free energy surface of three-stranded β-sheet protein J. Am. Chem. Soc. 121 1999 9946 9951
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9946-9951
    • Bursulaya, B.D.1    Brooks III, C.L.2
  • 40
    • 0000036869 scopus 로고    scopus 로고
    • Simulation of activation free energies in molecular systems
    • E. Neria, S. Fischer, and M. Karplus Simulation of activation free energies in molecular systems J. Chem. Phys. 105 1996 1902 1921
    • (1996) J. Chem. Phys. , vol.105 , pp. 1902-1921
    • Neria, E.1    Fischer, S.2    Karplus, M.3
  • 41
  • 42
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • J.P. Ryckaert, G. Ciccoti, and H.J.C. Berendsen Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes J. Comput. Phys. 23 1977 327 341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccoti, G.2    Berendsen, H.J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.