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Volumn 109, Issue 51, 2012, Pages 20913-20918

Out-of-register β-sheets suggest a pathway to toxic amyloid aggregates

Author keywords

BAMs; X ray crystallography

Indexed keywords

AMYLOID; CYLINDRIN; HYDROGEN; OLIGOMER; UNCLASSIFIED DRUG;

EID: 84871398573     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1218792109     Document Type: Article
Times cited : (169)

References (50)
  • 1
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • Eisenberg D, Jucker M (2012) The amyloid state of proteins in human diseases. Cell 148(6):1188-1203.
    • (2012) Cell , vol.148 , Issue.6 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 2
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333-366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 84863987464 scopus 로고    scopus 로고
    • Inhibition of amyloid formation
    • Härd T, Lendel C (2012) Inhibition of amyloid formation. J Mol Biol 421(4-5):441-465.
    • (2012) J Mol Biol , vol.421 , Issue.4-5 , pp. 441-465
    • Härd, T.1    Lendel, C.2
  • 4
    • 79959887638 scopus 로고    scopus 로고
    • A diversity of assembly mechanisms of a generic amyloid fold
    • Eichner T, Radford SE (2011) A diversity of assembly mechanisms of a generic amyloid fold. Mol Cell 43(1):8-18.
    • (2011) Mol Cell , vol.43 , Issue.1 , pp. 8-18
    • Eichner, T.1    Radford, S.E.2
  • 5
    • 84860377014 scopus 로고    scopus 로고
    • Selective molecular recognition in amyloid growth and transmission and cross-species barriers
    • Ma B, Nussinov R (2012) Selective molecular recognition in amyloid growth and transmission and cross-species barriers. J Mol Biol 421(2-3):172-184.
    • (2012) J Mol Biol , vol.421 , Issue.2-3 , pp. 172-184
    • Ma, B.1    Nussinov, R.2
  • 6
    • 77951271571 scopus 로고    scopus 로고
    • Principles governing oligomer formation in amyloidogenic peptides
    • Straub JE, Thirumalai D (2010) Principles governing oligomer formation in amyloidogenic peptides. Curr Opin Struct Biol 20(2):187-195.
    • (2010) Curr Opin Struct Biol , vol.20 , Issue.2 , pp. 187-195
    • Straub, J.E.1    Thirumalai, D.2
  • 7
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe CG (2008) Structural classification of toxic amyloid oligomers. J Biol Chem 283(44):29639-29643.
    • (2008) J Biol Chem , vol.283 , Issue.44 , pp. 29639-29643
    • Glabe, C.G.1
  • 8
    • 79953245314 scopus 로고    scopus 로고
    • Amyloid structure: Conformational diversity and consequences
    • Toyama BH, Weissman JS (2011) Amyloid structure: Conformational diversity and consequences. Annu Rev Biochem 80:557-585.
    • (2011) Annu Rev Biochem , vol.80 , pp. 557-585
    • Toyama, B.H.1    Weissman, J.S.2
  • 9
    • 67650809307 scopus 로고    scopus 로고
    • Functional amyloids as natural storage of peptide hormones in pituitary secretory granules
    • Maji SK, et al. (2009) Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938):328-332.
    • (2009) Science , vol.325 , Issue.5938 , pp. 328-332
    • Maji, S.K.1
  • 10
    • 34249290108 scopus 로고    scopus 로고
    • Atomic structures of amyloid cross-beta spines reveal varied steric zippers
    • Sawaya MR, et al. (2007) Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature 447(7143):453-457.
    • (2007) Nature , vol.447 , Issue.7143 , pp. 453-457
    • Sawaya, M.R.1
  • 11
    • 57649128935 scopus 로고    scopus 로고
    • Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: Molecular insights from electron paramagnetic resonance spectroscopy
    • Margittai M, Langen R (2008) Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: Molecular insights from electron paramagnetic resonance spectroscopy. Q Rev Biophys 41(3-4):265-297.
    • (2008) Q Rev Biophys , vol.41 , Issue.3-4 , pp. 265-297
    • Margittai, M.1    Langen, R.2
  • 12
    • 28444442999 scopus 로고    scopus 로고
    • 3D structure of Alzheimer's amyloid-beta(1-42) fibrils
    • Lührs T, et al. (2005) 3D structure of Alzheimer's amyloid-beta(1-42) fibrils. Proc Natl Acad Sci USA 102(48):17342-17347.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.48 , pp. 17342-17347
    • Lührs, T.1
  • 13
    • 0031592945 scopus 로고    scopus 로고
    • Common core structure of amyloid fi brils by synchrotron X-ray diffraction
    • Sunde M, et al. (1997) Common core structure of amyloid fi brils by synchrotron X-ray diffraction. J Mol Biol 273(3):729-739.
    • (1997) J Mol Biol , vol.273 , Issue.3 , pp. 729-739
    • Sunde, M.1
  • 14
    • 33746784978 scopus 로고    scopus 로고
    • Analysis of amyloid fibril structure by scanning cysteine mutagenesis
    • Shivaprasad S, Wetzel R (2006) Analysis of amyloid fibril structure by scanning cysteine mutagenesis. Methods Enzymol 413:182-198.
    • (2006) Methods Enzymol , vol.413 , pp. 182-198
    • Shivaprasad, S.1    Wetzel, R.2
  • 15
    • 0032506114 scopus 로고    scopus 로고
    • Propagating structure of Alzheimer's beta-amyloid(10-35) is parallel beta-sheet with residues in exact register
    • Benzinger TL, et al. (1998) Propagating structure of Alzheimer's beta-amyloid(10-35) is parallel beta-sheet with residues in exact register. Proc Natl Acad Sci USA 95(23):13407-13412.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.23 , pp. 13407-13412
    • Benzinger, T.L.1
  • 16
    • 79953765150 scopus 로고    scopus 로고
    • Solid-state NMR studies of amyloid fibril structure
    • Tycko R (2011) Solid-state NMR studies of amyloid fibril structure. Annu Rev Phys Chem 62:279-299.
    • (2011) Annu Rev Phys Chem , vol.62 , pp. 279-299
    • Tycko, R.1
  • 17
    • 77952305367 scopus 로고    scopus 로고
    • Beta arcades: Recurring motifs in naturally occurring and disease-related amyloid fibrils
    • Kajava AV, Baxa U, Steven AC (2010) Beta arcades: Recurring motifs in naturally occurring and disease-related amyloid fibrils. FASEB J 24(5):1311-1319.
    • (2010) FASEB J , vol.24 , Issue.5 , pp. 1311-1319
    • Kajava, A.V.1    Baxa, U.2    Steven, A.C.3
  • 18
    • 84858663186 scopus 로고    scopus 로고
    • Antiparallel β-sheet architecture in Iowa-mutant β-amyloid fibrils
    • Qiang W, Yau WM, Luo Y, Mattson MP, Tycko R (2012) Antiparallel β-sheet architecture in Iowa-mutant β-amyloid fibrils. Proc Natl Acad Sci USA 109(12):4443-4448.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.12 , pp. 4443-4448
    • Qiang, W.1    Yau, W.M.2    Luo, Y.3    Mattson, M.P.4    Tycko, R.5
  • 19
    • 84860390157 scopus 로고    scopus 로고
    • In vivo and in vitro analyses of toxic mutants of HET-s: FTIR antiparallel signature correlates with amyloid toxicity
    • Berthelot K, Ta HP, Géan J, Lecomte S, Cullin C (2011) In vivo and in vitro analyses of toxic mutants of HET-s: FTIR antiparallel signature correlates with amyloid toxicity. J Mol Biol 412(1):137-152.
    • (2011) J Mol Biol , vol.412 , Issue.1 , pp. 137-152
    • Berthelot, K.1    Ta, H.P.2    Géan, J.3    Lecomte, S.4    Cullin, C.5
  • 20
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation-based prion inheritance
    • Chien P, Weissman JS, DePace AH (2004) Emerging principles of conformation-based prion inheritance. Annu Rev Biochem 73:617-656.
    • (2004) Annu Rev Biochem , vol.73 , pp. 617-656
    • Chien, P.1    Weissman, J.S.2    DePace, A.H.3
  • 21
    • 75349097530 scopus 로고    scopus 로고
    • A causative link between the structure of aberrant protein oligomers and their toxicity
    • Campioni S, et al. (2010) A causative link between the structure of aberrant protein oligomers and their toxicity. Nat Chem Biol 6(2):140-147.
    • (2010) Nat Chem Biol , vol.6 , Issue.2 , pp. 140-147
    • Campioni, S.1
  • 22
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's beta amyloid fibrils
    • Petkova AT, et al. (2005) Self-propagating, molecular-level polymorphism in Alzheimer's beta amyloid fibrils. Science 307(5707):262-265.
    • (2005) Science , vol.307 , Issue.5707 , pp. 262-265
    • Petkova, A.T.1
  • 23
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 8(2):101-112.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 24
    • 33846160381 scopus 로고    scopus 로고
    • Polymorphism in the intermediates and products of amyloid assembly
    • Kodali R, Wetzel R (2007) Polymorphism in the intermediates and products of amyloid assembly. Curr Opin Struct Biol 17(1):48-57.
    • (2007) Curr Opin Struct Biol , vol.17 , Issue.1 , pp. 48-57
    • Kodali, R.1    Wetzel, R.2
  • 25
    • 77952324067 scopus 로고    scopus 로고
    • Low molecular weight oligomers of amyloid peptides display beta-barrel conformations: A replica exchange molecular dynamics study in explicit solvent
    • De Simone A, Derreumaux P (2010) Low molecular weight oligomers of amyloid peptides display beta-barrel conformations: A replica exchange molecular dynamics study in explicit solvent. J Chem Phys 132(16):165103.
    • (2010) J Chem Phys , vol.132 , Issue.16 , pp. 165103
    • De Simone, A.1    Derreumaux, P.2
  • 26
    • 78649529340 scopus 로고    scopus 로고
    • β-Barrel topology of Alzheimer's β-amyloid ion channels
    • Jang H, et al. (2010) β-Barrel topology of Alzheimer's β-amyloid ion channels. J Mol Biol 404(5):917-934.
    • (2010) J Mol Biol , vol.404 , Issue.5 , pp. 917-934
    • Jang, H.1
  • 27
    • 69249239132 scopus 로고    scopus 로고
    • Antiparallel beta-sheet: A signature structure of the oligomeric amyloid beta-peptide
    • Cerf E, et al. (2009) Antiparallel beta-sheet: A signature structure of the oligomeric amyloid beta-peptide. Biochem J 421(3):415-423.
    • (2009) Biochem J , vol.421 , Issue.3 , pp. 415-423
    • Cerf, E.1
  • 28
    • 84861206757 scopus 로고    scopus 로고
    • Toxic fibrillar oligomers of amyloid-β have cross-β structure
    • Stroud JC, Liu C, Teng PK, Eisenberg D (2012) Toxic fibrillar oligomers of amyloid-β have cross-β structure. Proc Natl Acad Sci USA 109(20):7717-7722.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.20 , pp. 7717-7722
    • Stroud, J.C.1    Liu, C.2    Teng, P.K.3    Eisenberg, D.4
  • 29
    • 67650325176 scopus 로고    scopus 로고
    • The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: Insights from type II diabetes
    • Hebda JA, Miranker AD (2009) The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: Insights from type II diabetes. Annu Rev Biophys 38:125-152.
    • (2009) Annu Rev Biophys , vol.38 , pp. 125-152
    • Hebda, J.A.1    Miranker, A.D.2
  • 30
    • 77951975748 scopus 로고    scopus 로고
    • Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils
    • Ahmed M, et al. (2010) Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils. Nat Struct Mol Biol 17(5):561-567.
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.5 , pp. 561-567
    • Ahmed, M.1
  • 31
    • 84863229747 scopus 로고    scopus 로고
    • Atomic view of a toxic amyloid small oligomer
    • Laganowsky A, et al. (2012) Atomic view of a toxic amyloid small oligomer. Science 335(6073):1228-1231.
    • (2012) Science , vol.335 , Issue.6073 , pp. 1228-1231
    • Laganowsky, A.1
  • 32
    • 78650982368 scopus 로고    scopus 로고
    • 2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages
    • 2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages. Nat Struct Mol Biol 18(1):49-55.
    • (2011) Nat Struct Mol Biol , vol.18 , Issue.1 , pp. 49-55
    • Liu, C.1    Sawaya, M.R.2    Eisenberg, D.3
  • 33
    • 67650500988 scopus 로고    scopus 로고
    • CHARMM: The biomolecular simulation program
    • Brooks BR, et al. (2009) CHARMM: The biomolecular simulation program. J Comput Chem 30(10):1545- 1614.
    • (2009) J Comput Chem , vol.30 , Issue.10 , pp. 1545-1614
    • Brooks, B.R.1
  • 34
    • 84867878408 scopus 로고    scopus 로고
    • Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity
    • Cheng PN, Liu C, Zhao ML, Eisenberg D, Nowick JS (2012) Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity. Nat Chem 4(11):927-933.
    • (2012) Nat Chem , vol.4 , Issue.11 , pp. 927-933
    • Cheng, P.N.1    Liu, C.2    Zhao, M.L.3    Eisenberg, D.4    Nowick, J.S.5
  • 35
    • 0037022563 scopus 로고    scopus 로고
    • Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation
    • Richardson JS, Richardson DC (2002) Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci USA 99(5):2754-2759.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.5 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 36
    • 34247884335 scopus 로고    scopus 로고
    • Macrocyclic beta-sheet peptides that mimic protein quaternary structure through intermolecular beta-sheet interactions
    • Khakshoor O, Demeler B, Nowick JS (2007) Macrocyclic beta-sheet peptides that mimic protein quaternary structure through intermolecular beta-sheet interactions. J Am Chem Soc 129(17):5558-5569.
    • (2007) J Am Chem Soc , vol.129 , Issue.17 , pp. 5558-5569
    • Khakshoor, O.1    Demeler, B.2    Nowick, J.S.3
  • 37
    • 79955440719 scopus 로고    scopus 로고
    • Characteristics of amyloid-related oligomers revealed by crystal structures of macrocyclic β-sheet mimics
    • Liu C, et al. (2011) Characteristics of amyloid-related oligomers revealed by crystal structures of macrocyclic β-sheet mimics. J Am Chem Soc 133(17):6736-6744.
    • (2011) J Am Chem Soc , vol.133 , Issue.17 , pp. 6736-6744
    • Liu, C.1
  • 38
    • 84861563520 scopus 로고    scopus 로고
    • Direct observation of the interconversion of normal and toxic forms of α-synuclein
    • Cremades N, et al. (2012) Direct observation of the interconversion of normal and toxic forms of α-synuclein. Cell 149(5):1048-1059.
    • (2012) Cell , vol.149 , Issue.5 , pp. 1048-1059
    • Cremades, N.1
  • 39
    • 84859489661 scopus 로고    scopus 로고
    • Microcin amyloid fibrils A are reservoir of toxic oligomeric species
    • Shahnawaz M, Soto C (2012) Microcin amyloid fibrils A are reservoir of toxic oligomeric species. J Biol Chem 287(15):11665-11676.
    • (2012) J Biol Chem , vol.287 , Issue.15 , pp. 11665-11676
    • Shahnawaz, M.1    Soto, C.2
  • 40
    • 80053596817 scopus 로고    scopus 로고
    • Understanding the complex mechanisms of β2-microglobulin amyloid assembly
    • Eichner T, Radford SE (2011) Understanding the complex mechanisms of β2-microglobulin amyloid assembly. FEBS J 278(20):3868-3883.
    • (2011) FEBS J , vol.278 , Issue.20 , pp. 3868-3883
    • Eichner, T.1    Radford, S.E.2
  • 41
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystsllogr 26:795-800.
    • (1993) J Appl Crystsllogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 42
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick GM (2008) A short history of SHELX. Acta Crystallogr A 64(Pt 1):112-122.
    • (2008) Acta Crystallogr A , vol.64 , Issue.PART 1 , pp. 112-122
    • Sheldrick, G.M.1
  • 43
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 PART 1 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 44
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 2 , pp. 213-221
    • Adams, P.D.1
  • 45
    • 0034625060 scopus 로고    scopus 로고
    • Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure
    • von Bergen M, et al. (2000) Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure. Proc Natl Acad Sci USA 97(10):5129-5134.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.10 , pp. 5129-5134
    • Von Bergen, M.1
  • 46
    • 41149162020 scopus 로고    scopus 로고
    • Fibril growth kinetics reveal a region of beta2-microglobulin important for nucleation and elongation of aggregation
    • Platt GW, Routledge KE, Homans SW, Radford SE (2008) Fibril growth kinetics reveal a region of beta2-microglobulin important for nucleation and elongation of aggregation. J Mol Biol 378(1):251-263.
    • (2008) J Mol Biol , vol.378 , Issue.1 , pp. 251-263
    • Platt, G.W.1    Routledge, K.E.2    Homans, S.W.3    Radford, S.E.4
  • 47
    • 36749033116 scopus 로고    scopus 로고
    • Peptide conformation and supramolecular organization in amylin fibrils: Constraints from solid-state NMR
    • Luca S, Yau WM, Leapman R, Tycko R (2007) Peptide conformation and supramolecular organization in amylin fibrils: Constraints from solid-state NMR. Biochemistry 46(47):13505-13522.
    • (2007) Biochemistry , vol.46 , Issue.47 , pp. 13505-13522
    • Luca, S.1    Yau, W.M.2    Leapman, R.3    Tycko, R.4
  • 48
    • 47249110199 scopus 로고    scopus 로고
    • The fold of alpha-synuclein fibrils
    • Vilar M, et al. (2008) The fold of alpha-synuclein fibrils. Proc Natl Acad Sci USA 105(25):8637-8642.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.25 , pp. 8637-8642
    • Vilar, M.1
  • 49
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy AJ, et al. (2007) Phaser crystallographic software. J Appl Cryst 40(Pt 4):658-674.
    • (2007) J Appl Cryst , vol.40 , Issue.PART 4 , pp. 658-674
    • McCoy, A.J.1
  • 50
    • 77957946297 scopus 로고    scopus 로고
    • Global Phasing Ltd, Cambridge, United Kingdom
    • Bricogne C, et al. (2009) Womack BUSTER, Version 2.8.0 (Global Phasing Ltd, Cambridge, United Kingdom).
    • (2009) Womack BUSTER, Version 2.8.0
    • Bricogne, C.1


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