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Volumn 932, Issue , 2013, Pages 237-257

Cross-β-sheet supersecondary structure in amyloid folds: Techniques for detection and characterization

Author keywords

Amyloid; Beta fold; Cross beta sheet; Fibril; Protein aggregation

Indexed keywords

AMYLOID; CONGO RED; THIOFLAVINE;

EID: 84934436437     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-62703-65-6_15     Document Type: Article
Times cited : (27)

References (39)
  • 2
    • 36749078792 scopus 로고    scopus 로고
    • Folding versus aggregation: Polypeptide conformations on competing pathways
    • Jahn TR, Radford SE (2008) Folding versus aggregation: polypeptide conformations on competing pathways. Arch Biochem Biophys 469(1):100-117
    • (2008) Arch Biochem Biophys , vol.469 , Issue.1 , pp. 100-117
    • Jahn, T.R.1    Radford, S.E.2
  • 3
    • 79551595773 scopus 로고    scopus 로고
    • Bacterial inclusion bodies of Alzheimer's disease beta-amyloid peptides can be employed to study native-like aggregation intermediate states
    • Dasari M, Espargaro A, Sabate R et al (2011) Bacterial inclusion bodies of Alzheimer's disease beta-amyloid peptides can be employed to study native-like aggregation intermediate states. Chembiochem 12(3):407-423
    • (2011) Chembiochem , vol.12 , Issue.3 , pp. 407-423
    • Dasari, M.1    Espargaro, A.2    Sabate, R.3
  • 4
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with sitedirected spin labeling
    • doi: 10.1038/78956
    • Hubbell WL, Ca fi so DS, Altenbach C (2000) Identifying conformational changes with sitedirected spin labeling. Nat Struct Biol 7(9):735-739. doi: 10.1038/78956
    • (2000) Nat Struct Biol , vol.7 , Issue.9 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 5
    • 0030623866 scopus 로고    scopus 로고
    • Data processing in multidimensional NMR
    • Pelczer I, Carter BG (1997) Data processing in multidimensional NMR. Methods Mol Biol 60:71-155
    • (1997) Methods Mol Biol , vol.60 , pp. 71-155
    • Pelczer, I.1    Carter, B.G.2
  • 6
    • 34249290108 scopus 로고    scopus 로고
    • Atomic structures of amyloid crossbeta spines reveal varied steric zippers
    • Sawaya MR, Sambashivan S, Nelson R et al (2007) Atomic structures of amyloid crossbeta spines reveal varied steric zippers. Nature 447(7143):453-457
    • (2007) Nature , vol.447 , Issue.7143 , pp. 453-457
    • Sawaya, M.R.1    Sambashivan, S.2    Nelson, R.3
  • 7
    • 33750017513 scopus 로고    scopus 로고
    • Molecular structure of amyloid fi brils: Insights from solid-state NMR
    • Tycko R (2006) Molecular structure of amyloid fi brils: insights from solid-state NMR. Q Rev Biophys 39(1):1-55
    • (2006) Q Rev Biophys , vol.39 , Issue.1 , pp. 1-55
    • Tycko, R.1
  • 8
    • 79953765150 scopus 로고    scopus 로고
    • Solid-state NMR studies of amyloid fi bril structure
    • Tycko R (2011) Solid-state NMR studies of amyloid fi bril structure. Annu Rev Phys Chem 62:279-299
    • (2011) Annu Rev Phys Chem , vol.62 , pp. 279-299
    • Tycko, R.1
  • 9
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fi brils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core
    • Wasmer C, Lange A, Van Melckebeke H et al (2008) Amyloid fi brils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core. Science 319(5869):1523-1526
    • (2008) Science , vol.319 , Issue.5869 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    Van Melckebeke, H.3
  • 10
    • 34248670403 scopus 로고    scopus 로고
    • Study on the binding of Thio fl avin T to beta-sheet-rich and non-beta-sheet cavities
    • Groenning M, Olsen L, van de Weert M et al (2007) Study on the binding of Thio fl avin T to beta-sheet-rich and non-beta-sheet cavities. J Struct Biol 158(3):358-369
    • (2007) J Struct Biol , vol.158 , Issue.3 , pp. 358-369
    • Groenning, M.1    Olsen, L.2    Van De Weert, M.3
  • 11
    • 22144484114 scopus 로고    scopus 로고
    • Microfocus Cu K(alpha) source for femtosecond X-ray science
    • Zhavoronkov N, Gritsai Y, Bargheer M et al (2005) Microfocus Cu K(alpha) source for femtosecond X-ray science. Opt Lett 30(13):1737-1739
    • (2005) Opt Lett , vol.30 , Issue.13 , pp. 1737-1739
    • Zhavoronkov, N.1    Gritsai, Y.2    Bargheer, M.3
  • 12
    • 34548599694 scopus 로고    scopus 로고
    • CLEARER: A new tool for the analysis of X-ray fi bre diffraction patterns and diffraction simulation from atomic structural models
    • Makin O, Sikorski P, Serpell L (2007) CLEARER: a new tool for the analysis of X-ray fi bre diffraction patterns and diffraction simulation from atomic structural models. J Appl Crystallogr 40:966-972
    • (2007) J Appl Crystallogr , vol.40 , pp. 966-972
    • Makin, O.1    Sikorski, P.2    Serpell, L.3
  • 13
    • 0035257136 scopus 로고    scopus 로고
    • "Congo" red: Out of Africa?
    • Steensma DP (2001) "Congo" red: out of Africa? Arch Pathol Lab Med 125(2):250-252
    • (2001) Arch Pathol Lab Med , vol.125 , Issue.2 , pp. 250-252
    • Steensma, D.P.1
  • 14
    • 0024363054 scopus 로고
    • Two simple methods for quantifying lowaf fi nity dye-substrate binding
    • Klunk WE, Pettegrew JW, Abraham DJ (1989) Two simple methods for quantifying lowaf fi nity dye-substrate binding. J Histochem Cytochem 37(8):1293-1297
    • (1989) J Histochem Cytochem , vol.37 , Issue.8 , pp. 1293-1297
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 15
    • 0024352110 scopus 로고
    • Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation
    • Klunk WE, Pettegrew JW, Abraham DJ (1989) Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J Histochem Cytochem 37(8):1273-1281
    • (1989) J Histochem Cytochem , vol.37 , Issue.8 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 16
    • 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
  • 17
    • 0032855483 scopus 로고    scopus 로고
    • Quantifying amyloid by Congo red spectral shift assay
    • Klunk WE, Jacob RF, Mason RP (1999) Quantifying amyloid by Congo red spectral shift assay. Methods Enzymol 309: 285-305
    • (1999) Methods Enzymol , vol.309 , pp. 285-305
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 18
    • 0032899322 scopus 로고    scopus 로고
    • Quantifying amyloid beta-peptide (Abeta) aggregation using the Congo red-Abeta (CR-abeta) spectrophotometric assay
    • Klunk WE, Jacob RF, Mason RP (1999) Quantifying amyloid beta-peptide (Abeta) aggregation using the Congo red-Abeta (CR-abeta) spectrophotometric assay. Anal Biochem 266(1):66-76
    • (1999) Anal Biochem , vol.266 , Issue.1 , pp. 66-76
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 19
    • 0033798946 scopus 로고    scopus 로고
    • Histidine residues underlie Congo red binding to A beta analogs
    • Inouye H, Nguyen JT, Fraser PE et al (2000) Histidine residues underlie Congo red binding to A beta analogs. Amyloid 7(3):179-188
    • (2000) Amyloid , vol.7 , Issue.3 , pp. 179-188
    • Inouye, H.1    Nguyen, J.T.2    Fraser, P.E.3
  • 20
    • 0242611913 scopus 로고    scopus 로고
    • Pinacyanol as effective probe of fi brillar beta-amyloid peptide: Comparative study with Congo red
    • Sabate R, Estelrich J (2003) Pinacyanol as effective probe of fi brillar beta-amyloid peptide: comparative study with Congo red. Biopolymers 72(6):455-463
    • (2003) Biopolymers , vol.72 , Issue.6 , pp. 455-463
    • Sabate, R.1    Estelrich, J.2
  • 21
    • 79959218074 scopus 로고    scopus 로고
    • The amyloid-Congo red interface at atomic resolution
    • doi: 10.1002/anie.201008276
    • Schutz AK, Soragni A, Hornemann S et al (2011) The amyloid-Congo red interface at atomic resolution. Angew Chem Int Ed Engl. doi: 10.1002/anie.201008276
    • (2011) Angew Chem Int Ed Engl
    • Schutz, A.K.1    Soragni, A.2    Hornemann, S.3
  • 22
    • 71149094496 scopus 로고    scopus 로고
    • Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion
    • Sabate R, Espargaro A, Saupe SJ et al (2009) Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion. Microb Cell Fact 8:56
    • (2009) Microb Cell Fact , vol.8 , pp. 56
    • Sabate, R.1    Espargaro, A.2    Saupe, S.J.3
  • 23
    • 0013812532 scopus 로고
    • Congo red as a stain for fl uorescence microscopy of amyloid
    • Puchtler H, Sweat F (1965) Congo red as a stain for fl uorescence microscopy of amyloid. J Histochem Cytochem 13(8):693-694
    • (1965) J Histochem Cytochem , vol.13 , Issue.8 , pp. 693-694
    • Puchtler, H.1    Sweat, F.2
  • 24
    • 7444243704 scopus 로고    scopus 로고
    • Improved detection of amyloid in fat pad aspiration: An evaluation of Congo red stain by fl uorescent microscopy
    • Giorgadze TA, Shiina N, Baloch ZW et al (2004) Improved detection of amyloid in fat pad aspiration: an evaluation of Congo red stain by fl uorescent microscopy. Diagn Cytopathol 31(5):300-306
    • (2004) Diagn Cytopathol , vol.31 , Issue.5 , pp. 300-306
    • Giorgadze, T.A.1    Shiina, N.2    Baloch, Z.W.3
  • 25
    • 0032849874 scopus 로고    scopus 로고
    • Quanti fi cation of betasheet amyloid fi bril structures with thio fl avin T
    • LeVine H 3rd (1999) Quanti fi cation of betasheet amyloid fi bril structures with thio fl avin T. Methods Enzymol 309:274-284
    • (1999) Methods Enzymol , vol.309 , pp. 274-284
    • Levine III, H.1
  • 26
    • 0032855484 scopus 로고    scopus 로고
    • Kinetic analysis of amyloid fi bril formation
    • Naiki H, Gejyo F (1999) Kinetic analysis of amyloid fi bril formation. Methods Enzymol 309:305-318
    • (1999) Methods Enzymol , vol.309 , pp. 305-318
    • Naiki, H.1    Gejyo, F.2
  • 27
    • 44549084117 scopus 로고    scopus 로고
    • On the binding of Thio fl avin-T to HET-s amyloid fi brils assembled at pH 2
    • Sabate R, Lascu I, Saupe SJ (2008) On the binding of Thio fl avin-T to HET-s amyloid fi brils assembled at pH 2. J Struct Biol 162(3):387-396
    • (2008) J Struct Biol , vol.162 , Issue.3 , pp. 387-396
    • Sabate, R.1    Lascu, I.2    Saupe, S.J.3
  • 28
    • 27944455577 scopus 로고    scopus 로고
    • Chiral bias of amyloid fi brils revealed by the twisted conformation of Thio fl avin T: An induced circular dichroism/DFT study
    • Dzwolak W, Pecul M (2005) Chiral bias of amyloid fi brils revealed by the twisted conformation of Thio fl avin T: an induced circular dichroism/DFT study. FEBS Lett 579(29):6601-6603
    • (2005) FEBS Lett , vol.579 , Issue.29 , pp. 6601-6603
    • Dzwolak, W.1    Pecul, M.2
  • 29
    • 34250890734 scopus 로고    scopus 로고
    • Thio fl avin T fl uorescence anisotropy: An alternative technique for the study of amyloid aggregation
    • Sabate R, Saupe SJ (2007) Thio fl avin T fl uorescence anisotropy: an alternative technique for the study of amyloid aggregation. Biochem Biophys Res Commun 360(1):135-138
    • (2007) Biochem Biophys Res Commun , vol.360 , Issue.1 , pp. 135-138
    • Sabate, R.1    Saupe, S.J.2
  • 30
    • 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
  • 31
    • 0033777523 scopus 로고    scopus 로고
    • Formation of insulin amyloid fi brils followed by FTIR simultaneously with CD and electron microscopy
    • Bouchard M, Zurdo J, Nettleton EJ et al (2000) Formation of insulin amyloid fi brils followed by FTIR simultaneously with CD and electron microscopy. Protein Sci 9(10):1960-1967
    • (2000) Protein Sci , vol.9 , Issue.10 , pp. 1960-1967
    • Bouchard, M.1    Zurdo, J.2    Nettleton, E.J.3
  • 32
    • 33847772827 scopus 로고    scopus 로고
    • Ile-phe dipeptide self-assembly: Clues to amyloid formation
    • de Groot NS, Parella T, Aviles FX et al (2007) Ile-phe dipeptide self-assembly: clues to amyloid formation. Biophys J 92(5):1732-1741
    • (2007) Biophys J , vol.92 , Issue.5 , pp. 1732-1741
    • De Groot, N.S.1    Parella, T.2    Aviles, F.X.3
  • 33
    • 78349308081 scopus 로고    scopus 로고
    • The role of protein sequence and amino acid composition in amyloid formation: Scrambling and backward reading of IAPP amyloid fi brils
    • Sabate R, Espargaro A, de Groot NS et al (2010) The role of protein sequence and amino acid composition in amyloid formation: scrambling and backward reading of IAPP amyloid fi brils. J Mol Biol 404(2):337-352
    • (2010) J Mol Biol , vol.404 , Issue.2 , pp. 337-352
    • Sabate, R.1    Espargaro, A.2    De Groot, N.S.3
  • 34
    • 57349120654 scopus 로고    scopus 로고
    • Structural insights into the polymorphism of amyloid-like fi brils formed by region 20-29 of amylin revealed by solid-state NMR and X-ray fi ber diffraction
    • Madine J, Jack E, Stockley PG et al (2008) Structural insights into the polymorphism of amyloid-like fi brils formed by region 20-29 of amylin revealed by solid-state NMR and X-ray fi ber diffraction. J Am Chem Soc 130(45): 14990-15001
    • (2008) J Am Chem Soc , vol.130 , Issue.45 , pp. 14990-15001
    • Madine, J.1    Jack, E.2    Stockley, P.G.3
  • 35
    • 77955838718 scopus 로고    scopus 로고
    • From natural to designer self-assembling biopolymers, the structural characterisation of fi brous proteins & peptides using fi bre diffraction
    • Morris K, Serpell L (2010) From natural to designer self-assembling biopolymers, the structural characterisation of fi brous proteins & peptides using fi bre diffraction. Chem Soc Rev 39(9):3445-3453
    • (2010) Chem Soc Rev , vol.39 , Issue.9 , pp. 3445-3453
    • Morris, K.1    Serpell, L.2
  • 36
    • 0032539578 scopus 로고    scopus 로고
    • The structural aspects of limited proteolysis of native proteins
    • Hubbard SJ (1998) The structural aspects of limited proteolysis of native proteins. Biochim Biophys Acta 1382(2):191-206
    • (1998) Biochim Biophys Acta , vol.1382 , Issue.2 , pp. 191-206
    • Hubbard, S.J.1
  • 37
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: Amyloid growth occurs by monomer addition
    • Collins SR, Douglass A, Vale RD et al (2004) Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol 2(10):e321
    • (2004) PLoS Biol , vol.2 , Issue.10
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3
  • 38
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett JT, Lansbury PT Jr (1993) Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73(6):1055-1058
    • (1993) Cell , vol.73 , Issue.6 , pp. 1055-1058
    • Jarrett, J.T.1
  • 39
    • 0038795608 scopus 로고    scopus 로고
    • An autocatalytic reaction as a model for the kinetics of the aggregation of beta-amyloid
    • Sabate R, Gallardo M, Estelrich J (2003) An autocatalytic reaction as a model for the kinetics of the aggregation of beta-amyloid. Biopolymers 71(2):190-195
    • (2003) Biopolymers , vol.71 , Issue.2 , pp. 190-195
    • Sabate, R.1    Gallardo, M.2    Estelrich, J.3


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