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Volumn 185, Issue , 2014, Pages 47-57

Length-dependent conformational transitions of polyglutamine repeats as molecular origin of fibril initiation

Author keywords

CD; Conformation; Fibril formation; IR; Peptides; Polyglutamine

Indexed keywords

CARBONYL DERIVATIVE; GLUTAMINE; POLYGLUTAMINE;

EID: 84889572610     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2013.11.008     Document Type: Article
Times cited : (15)

References (29)
  • 1
    • 77956184558 scopus 로고    scopus 로고
    • Neurotoxic protein oligomerisation associated with polyglutamine diesease
    • A. Wyttenbach, and S.L. Hands Neurotoxic protein oligomerisation associated with polyglutamine diesease Acta Neuropathol. 120 2010 419 437
    • (2010) Acta Neuropathol. , vol.120 , pp. 419-437
    • Wyttenbach, A.1    Hands, S.L.2
  • 4
    • 2542422018 scopus 로고    scopus 로고
    • Polyglutamine and neurodegeneration: Structural aspects
    • DOI 10.2174/0929866043407147
    • L. Masino Polyglutamine and neurodegeneration: structural aspects Proteins and Peptide Lett. 11 2004 239 248 (Pubitemid 38689027)
    • (2004) Protein and Peptide Letters , vol.11 , Issue.3 , pp. 239-248
    • Masino, L.1
  • 5
    • 0013906079 scopus 로고
    • Synthetic polypeptides containing side-chain amide groups. Water-soluble polymers
    • L.H. Krull, and J.S. Wall Synthetic polypeptides containing side-chain amide groups. water-soluble polymers Biochemistry 5 1966 1521 1527
    • (1966) Biochemistry , vol.5 , pp. 1521-1527
    • Krull, L.H.1    Wall, J.S.2
  • 8
    • 0035800572 scopus 로고    scopus 로고
    • Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity
    • DOI 10.1006/jmbi.2001.4850
    • S. Chen, V. Berthelier, W. Yang, and R. Wetzel Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity J. Mol. Biol. 311 2001 173 182 (Pubitemid 32735322)
    • (2001) Journal of Molecular Biology , vol.311 , Issue.1 , pp. 173-182
    • Chen, S.1    Berthelier, V.2    Yang, W.3    Wetzel, R.4
  • 9
    • 0035084096 scopus 로고    scopus 로고
    • Solubilization and disaggregation of polyglutamine peptides
    • DOI 10.1110/ps.42301
    • S. Chen, and R. Wetzel Solubilization and disaggregation of polyglutamine peptides Protein Sci. 10 2001 887 891 (Pubitemid 32240515)
    • (2001) Protein Science , vol.10 , Issue.4 , pp. 887-891
    • Chen, S.1    Wetzel, R.2
  • 12
    • 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 452-432
    • (2005) Biomacromolecules , vol.6 , pp. 452-432
    • Sikorski, P.1    Atkins, E.2
  • 14
    • 70349838220 scopus 로고    scopus 로고
    • Examining polyglutamine peptide length: A connection between collapsed conformation and increased aggregation
    • R.H. Walters, and R.M. Murphy Examining polyglutamine peptide length: a connection between collapsed conformation and increased aggregation J. Mol. Biol. 393 2009 978 992
    • (2009) J. Mol. Biol. , vol.393 , pp. 978-992
    • Walters, R.H.1    Murphy, R.M.2
  • 16
    • 33646794342 scopus 로고    scopus 로고
    • Polyglutamine repeats and β-helix structure: Molecular dynamics study
    • DOI 10.1002/prot.20941
    • A. Merlino, L. Esposito, and L. Vitagliano Polyglutamine repeats and b-helix structure: molecular dynamics study Proteins Struct. Funct. Bioinf. 63 2006 918 927 (Pubitemid 43765143)
    • (2006) Proteins: Structure, Function and Genetics , vol.63 , Issue.4 , pp. 918-927
    • Merlino, A.1    Esposito, L.2    Vitagliano, L.3
  • 17
    • 55449095000 scopus 로고    scopus 로고
    • Molecular origin of polyglutamine aggregation in neurodegenerative diseases
    • S.D. Khare, F. Ding, K.N. Gwanmesia, and N.V. Dokholyan Molecular origin of polyglutamine aggregation in neurodegenerative diseases PLoS Comput. Biol. 1 2005 230 235
    • (2005) PLoS Comput. Biol. , vol.1 , pp. 230-235
    • Khare, S.D.1    Ding, F.2    Gwanmesia, K.N.3    Dokholyan, N.V.4
  • 19
  • 20
    • 84863990252 scopus 로고    scopus 로고
    • Physical chemistry of polyglutamine: Intriguing tales of a monotonous sequence
    • R. Wetzel Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence J. Mol. Biol. 421 2012 466 490
    • (2012) J. Mol. Biol. , vol.421 , pp. 466-490
    • Wetzel, R.1
  • 21
    • 0001591464 scopus 로고
    • Use of the glass electrode in deuterium oxide and the relation between the standardized pD (paD) scale and the operational pH in heavy water
    • A.K. Covington, M. Paabo, R.A. Robinson, and R.G. Bates Use of the glass electrode in deuterium oxide and the relation between the standardized pD (paD) scale and the operational pH in heavy water Anal. Chem. 40 1968 700 706
    • (1968) Anal. Chem. , vol.40 , pp. 700-706
    • Covington, A.K.1    Paabo, M.2    Robinson, R.A.3    Bates, R.G.4
  • 22
    • 0347130904 scopus 로고    scopus 로고
    • Heterogeneous Folding of the trpzip Hairpin: Full Atom Simulation and Experiment
    • DOI 10.1016/j.jmb.2003.11.033
    • W.Y. Yang, J.W. Pitera, W.S. Swope, and M. Gruebele Heterogenous folding of the trpzip hairpin: full atom simulation and experiment J. Mol. Biol. 336 2004 241 251 (Pubitemid 38102345)
    • (2004) Journal of Molecular Biology , vol.336 , Issue.1 , pp. 241-251
    • Yang, W.Y.1    Pitera, J.W.2    Swope, W.C.3    Gruebele, M.4
  • 23
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • DOI 10.1017/S0033583502003815
    • A. Barth, and C. Zscherp What vibrations tell us about proteins Q. Rev. Biophys. 35 2002 369 430 (Pubitemid 36207229)
    • (2002) Quarterly Reviews of Biophysics , vol.35 , Issue.4 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 24
    • 84890163302 scopus 로고    scopus 로고
    • Millisecond-to-minute protein folding/misfolding events monitored by FTIR spectroscopy
    • H. Fabian, D. Naumann, Springer Berlin Heidelberg
    • H. Fabian, and D. Naumann Millisecond-to-minute protein folding/misfolding events monitored by FTIR spectroscopy H. Fabian, D. Naumann, Protein Folding and Misfolding 2012 Springer Berlin Heidelberg 53 89
    • (2012) Protein Folding and Misfolding , pp. 53-89
    • Fabian, H.1    Naumann, D.2
  • 25
    • 0034473318 scopus 로고    scopus 로고
    • The infrared absorption of amino acid side chains
    • DOI 10.1016/S0079-6107(00)00021-3, PII S0079610700000213
    • A. Barth The infrared absorption of amino acid side chains Prog. Biophys. Mol. Biol. 74 2000 141 173 (Pubitemid 32168153)
    • (2000) Progress in Biophysics and Molecular Biology , vol.74 , Issue.3-5 , pp. 141-173
    • Barth, A.1
  • 26
    • 84856226648 scopus 로고    scopus 로고
    • Slow amyloid nucleation via a-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments
    • M. Jayaraman, R. Kodali, B. Sahoo, A.K. Thakur, A. Mayasundari, R. Mishra, C.B. Peterson, and R. Wetzel Slow amyloid nucleation via a-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments J. Mol. Biol. 415 2012 881 899
    • (2012) J. Mol. Biol. , vol.415 , pp. 881-899
    • Jayaraman, M.1    Kodali, R.2    Sahoo, B.3    Thakur, A.K.4    Mayasundari, A.5    Mishra, R.6    Peterson, C.B.7    Wetzel, R.8
  • 27
    • 41449088536 scopus 로고    scopus 로고
    • Site-specific relaxation kinetics of a tryptophan zipper hairpin peptide using temperature-jump IR spectroscopy and isotopic labeling
    • DOI 10.1021/ja074215l
    • K. Hauser, C. Krejtschi, R. Huang, L. Wu, and T.A. Keiderling Site-specific relaxation kinetics of a tryptophan zipper hairpin peptide using temperature-jump ir-spectroscopy and isotopic labeling J. Am. Chem. Soc. 130 2008 2984 2992 (Pubitemid 351455969)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.10 , pp. 2984-2992
    • Hauser, K.1    Krejtschi, C.2    Huang, R.3    Wu, L.4    Keiderling, T.A.5
  • 28
    • 77956329441 scopus 로고    scopus 로고
    • Comparison of isotopic substitution methods for equilibrium and T-jump infrared studies of b-hairpin peptide conformation
    • K. Hauser, O. Ridderbusch, A. Roy, A. Hellerbach, R. Huang, and T.A. Keiderling Comparison of isotopic substitution methods for equilibrium and T-jump infrared studies of b-hairpin peptide conformation J. Phys. Chem. B 114 2010 11628 11637
    • (2010) J. Phys. Chem. B , vol.114 , pp. 11628-11637
    • Hauser, K.1    Ridderbusch, O.2    Roy, A.3    Hellerbach, A.4    Huang, R.5    Keiderling, T.A.6
  • 29
    • 0032776447 scopus 로고    scopus 로고
    • Peptide models for inherited neurodegenerative disorders: Conformation and aggregation properties of long polyglutamine peptides with and without interruptions
    • DOI 10.1016/S0014-5793(99)00933-3, PII S0014579399009333
    • D. Sharma, S. Sharma, S. Pasha, and S.K. Brahmachari Peptide models for inherited neurodegenerative disorders: conformation and aggregation properties of polyglutamine peptides with and without interruptions FEBS Lett. 456 1999 181 185 (Pubitemid 29339065)
    • (1999) FEBS Letters , vol.456 , Issue.1 , pp. 181-185
    • Sharma, D.1    Sharma, S.2    Pasha, S.3    Brahmachari, S.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.