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Volumn 5, Issue 3, 2014, Pages 607-614

Amyloid fibrils: Formation, polymorphism, and inhibition

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FORMATION; DIFFERENT MECHANISMS; FIBRIL FORMATION; PRIMARY NUCLEATION; RECENT RESEARCHES; SECONDARY NUCLEATION; STRUCTURAL MORPHOLOGY; STRUCTURAL POLYMORPHISMS;

EID: 84893869490     PISSN: None     EISSN: 19487185     Source Type: Journal    
DOI: 10.1021/jz4027612     Document Type: Review
Times cited : (45)

References (65)
  • 1
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • DOI 10.1016/S0968-0004(99)01445-0, PII S0968000499014450
    • Dobson, C. Protein Misfolding, Evolution and Disease Trends Biochem. Sci. 1999, 24, 329-332 (Pubitemid 29421804)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.9 , pp. 329-332
    • Dobson, C.M.1
  • 3
    • 78649315112 scopus 로고    scopus 로고
    • Amyloid Fibril Protein Nomenclature: 2010 Recommendations from the Nomenclature Committee of the International Society of Amyloidosis
    • Sipe, J.; Benson, M.; Buxbaum, J.; Ikeda, S.-I.; Merlini, G.; Saraiva, M.; Westermark, P. Amyloid Fibril Protein Nomenclature: 2010 Recommendations from the Nomenclature Committee of the International Society of Amyloidosis Amyloid 2010, 17, 101-104
    • (2010) Amyloid , vol.17 , pp. 101-104
    • Sipe, J.1    Benson, M.2    Buxbaum, J.3    Ikeda, S.-I.4    Merlini, G.5    Saraiva, M.6    Westermark, P.7
  • 4
    • 0014351967 scopus 로고
    • X-ray Diffraction Studies on Amyloid Filaments
    • Eanes, E.; Glenner, G. X-ray Diffraction Studies on Amyloid Filaments J. Histochem. Cytochem. 1968, 16, 673-677
    • (1968) J. Histochem. Cytochem. , vol.16 , pp. 673-677
    • Eanes, E.1    Glenner, G.2
  • 7
    • 84858374665 scopus 로고    scopus 로고
    • The Amyloid State of Proteins in Human Diseases
    • Eisenberg, D.; Jucker, M. The Amyloid State of Proteins in Human Diseases Cell 2012, 148, 1188-1203
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 9
    • 0026675307 scopus 로고
    • Partial Denaturation of Transthyretin is Sufficient for Amyloid Fibril Formation in Vitro
    • Colon, W.; Kelly, J. Partial Denaturation of Transthyretin is Sufficient for Amyloid Fibril Formation In Vitro Biochemistry 1992, 31, 8654-8660
    • (1992) Biochemistry , vol.31 , pp. 8654-8660
    • Colon, W.1    Kelly, J.2
  • 10
    • 0027006436 scopus 로고
    • Amyloid fibril formation requires a chemically discriminating nucleation event: Studies of an amyloidogenic sequence from the bacterial protein OsmB
    • DOI 10.1021/bi00164a008
    • Jarrett, J.; Lansbury, P. Amyloid Fibril Formation Requires a Chemically Discriminating Nucleation Event: Studies of an Amyloidogenic Sequence from the Bacterial Protein OsmB Biochemistry 1992, 31, 12345-12352 (Pubitemid 23163109)
    • (1992) Biochemistry , vol.31 , Issue.49 , pp. 12345-12352
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 11
    • 84857642949 scopus 로고    scopus 로고
    • The Toxic Aβ Oligomer and Alzheimer's Disease: An Emperor in Need of Clothes
    • Benilova, I.; Karran, E.; de Strooper, B. The Toxic Aβ Oligomer and Alzheimer's Disease: An Emperor in Need of Clothes Nat. Neurosci. 2012, 15, 349-357
    • (2012) Nat. Neurosci. , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 12
    • 80053595082 scopus 로고    scopus 로고
    • Protein Engineering to Stabilize Soluble Amyloid β-Protein Aggregates for Structural and Functional Studies
    • Härd, T. Protein Engineering to Stabilize Soluble Amyloid β-Protein Aggregates for Structural and Functional Studies FEBS J. 2011, 278, 3884-3892
    • (2011) FEBS J. , vol.278 , pp. 3884-3892
    • Härd, T.1
  • 13
    • 63849197629 scopus 로고    scopus 로고
    • Amyloid β-Protein Assembly and Alzheimer Disease
    • Roychaudhuri, R.; Yang, M.; Hoshi, M.; Teplow, D. Amyloid β-Protein Assembly and Alzheimer Disease J. Biol. Chem. 2009, 284, 4749-4753
    • (2009) J. Biol. Chem. , vol.284 , pp. 4749-4753
    • Roychaudhuri, R.1    Yang, M.2    Hoshi, M.3    Teplow, D.4
  • 15
    • 77951676986 scopus 로고    scopus 로고
    • Amyloid β-Protein Aggregation Produces Highly Reproducible Kinetic Data and Occurs by a Two-Phase Process
    • Hellstrand, E.; Boland, B.; Walsh, D. M.; Linse, S. Amyloid β-Protein Aggregation Produces Highly Reproducible Kinetic Data and Occurs by a Two-Phase Process ACS Chem. Neurosci. 2010, 1, 13-18
    • (2010) ACS Chem. Neurosci. , vol.1 , pp. 13-18
    • Hellstrand, E.1    Boland, B.2    Walsh, D.M.3    Linse, S.4
  • 17
    • 80051899060 scopus 로고    scopus 로고
    • Nucleated Polymerization with Secondary Pathways. II. Determination of Self-Consistent Solutions to Growth Processes Described by Non-Linear Master Equations
    • Cohen, S.; Vendruscolo, M.; Dobson, C.; Knowles, T. Nucleated Polymerization with Secondary Pathways. II. Determination of Self-Consistent Solutions to Growth Processes Described by Non-Linear Master Equations J. Chem. Phys. 2011, 135, 065106
    • (2011) J. Chem. Phys. , vol.135 , pp. 065106
    • Cohen, S.1    Vendruscolo, M.2    Dobson, C.3    Knowles, T.4
  • 18
    • 80051866825 scopus 로고    scopus 로고
    • Nucleated Polymerization with Secondary Pathways. I. Time Evolution of the Principal Moments
    • Cohen, S.; Vendruscolo, M.; Welland, M.; Dobson, C.; Terentjev, E.; Knowles, T. Nucleated Polymerization with Secondary Pathways. I. Time Evolution of the Principal Moments J. Chem. Phys. 2011, 135, 065105
    • (2011) J. Chem. Phys. , vol.135 , pp. 065105
    • Cohen, S.1    Vendruscolo, M.2    Welland, M.3    Dobson, C.4    Terentjev, E.5    Knowles, T.6
  • 21
    • 0021837479 scopus 로고
    • Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism
    • DOI 10.1016/0022-2836(85)90175-5
    • Ferrone, F.; Hofrichter, J.; Eaton, W. Kinetics of Sickle Hemoglobin Polymerization. II. A Double Nucleation Mechanism J. Mol. Biol. 1985, 183, 611-631 (Pubitemid 15036851)
    • (1985) Journal of Molecular Biology , vol.183 , Issue.4 , pp. 611-631
    • Ferrone, F.A.1    Hofrichter, J.2    Eaton, W.A.3
  • 23
    • 1842577741 scopus 로고    scopus 로고
    • Onset of heterogeneous crystal nucleation in colloidal suspensions
    • DOI 10.1038/nature02397
    • Cacciuto, A.; Auer, S.; Frenkel, D. Onset of Heterogeneous Crystal Nucleation in Colloidal Suspensions Nature 2004, 428, 404-406 (Pubitemid 38419681)
    • (2004) Nature , vol.428 , Issue.6981 , pp. 404-406
    • Cacciuto, A.1    Auer, S.2    Frenkei, D.3
  • 25
    • 0021527508 scopus 로고
    • Kinetics of Nucleation-Controlled Polymerization. A Perturbation Treatment for Use with a Secondary Pathway
    • Bishop, M.; Ferrone, F. Kinetics of Nucleation-Controlled Polymerization. A Perturbation Treatment for Use with a Secondary Pathway Biophys. J. 1984, 46, 631-644
    • (1984) Biophys. J. , vol.46 , pp. 631-644
    • Bishop, M.1    Ferrone, F.2
  • 26
    • 0020481585 scopus 로고
    • Fragmentation of Actin Filaments
    • Wegner, A.; Savko, P. Fragmentation of Actin Filaments Biochemistry 1982, 21, 1909-1913
    • (1982) Biochemistry , vol.21 , pp. 1909-1913
    • Wegner, A.1    Savko, P.2
  • 27
    • 84892178364 scopus 로고    scopus 로고
    • An Amyloid Chain Reaction Assay Quantifies the Concentration of Aβ42 Propagons during the Lag-Phase
    • Arosio, P.; Cukalevski, R.; Frohm, B.; Knowles, T.; Linse, S. An Amyloid Chain Reaction Assay Quantifies the Concentration of Aβ42 Propagons During the Lag-Phase J. Am. Chem. Soc. 2014, 136, 219-225
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 219-225
    • Arosio, P.1    Cukalevski, R.2    Frohm, B.3    Knowles, T.4    Linse, S.5
  • 28
    • 84879773805 scopus 로고    scopus 로고
    • Amyloid-β Protofibrils: Size, Morphology and Synaptotoxicity of an Engineered Mimic
    • Dubnovitsky, A.; Sandberg, A.; Rahman, M.; Benilova, I.; Lendel, C.; Härd, T. Amyloid-β Protofibrils: Size, Morphology and Synaptotoxicity of an Engineered Mimic PloS ONE 2013, 8, e66101
    • (2013) PloS ONE , vol.8 , pp. 66101
    • Dubnovitsky, A.1    Sandberg, A.2    Rahman, M.3    Benilova, I.4    Lendel, C.5    Härd, T.6
  • 31
    • 79958058969 scopus 로고    scopus 로고
    • Recent Progress in Understanding Alzheimer's β-Amyloid Structures
    • Fändrich, M.; Schmidt, M.; Grigorieff, N. Recent Progress in Understanding Alzheimer's β-Amyloid Structures Trends Biochem. Sci. 2011, 36, 338-345
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 338-345
    • Fändrich, M.1    Schmidt, M.2    Grigorieff, N.3
  • 32
    • 0042847751 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
    • DOI 10.1093/emboj/18.4.815
    • Jiménez, J.; Guijarro, J.; Orlova, E.; Zurdo, J.; Dobson, C.; Sunde, M.; Saibil, H. Cryo-Electron Microscopy Structure of an SH3 Amyloid Fibril and Model of the Molecular Packing EMBO J. 1999, 18, 815-821 (Pubitemid 29082261)
    • (1999) EMBO Journal , vol.18 , Issue.4 , pp. 815-821
    • Jimenez, J.L.1    Guijarro, J.I.2    Orlova, E.3    Zurdo, J.4    Dobson, C.M.5    Sunde, M.6    Saibil, H.R.7
  • 33
    • 79953245314 scopus 로고    scopus 로고
    • Amyloid Structure: Conformational Diversity and Consequences
    • Toyama, B.; Weissman, J. Amyloid Structure: Conformational Diversity and Consequences Annu. Rev. Biochem. 2011, 80, 557-585
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 557-585
    • Toyama, B.1    Weissman, J.2
  • 34
    • 84891368203 scopus 로고    scopus 로고
    • A Clear View of Polymorphism, Twist, and Chirality in Amyloid Fibril Formation
    • Volpatti, L.; Vendruscolo, M.; Dobson, C.; Knowles, T. A Clear View of Polymorphism, Twist, and Chirality in Amyloid Fibril Formation ACS Nano 2013, 7, 10443-10448
    • (2013) ACS Nano , vol.7 , pp. 10443-10448
    • Volpatti, L.1    Vendruscolo, M.2    Dobson, C.3    Knowles, T.4
  • 36
    • 67650022104 scopus 로고    scopus 로고
    • Evidence for Novel β-Sheet Structures in Iowa Mutant β-Amyloid Fibrils
    • Tycko, R.; Sciarretta, K.; Orgel, J.; Meredith, S. Evidence for Novel β-Sheet Structures in Iowa Mutant β-Amyloid Fibrils Biochemistry 2009, 48, 6072-6084
    • (2009) Biochemistry , vol.48 , pp. 6072-6084
    • Tycko, R.1    Sciarretta, K.2    Orgel, J.3    Meredith, S.4
  • 37
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
    • DOI 10.1126/science.1105850
    • Petkova, A.; Leapman, R.; Guo, Z.; Yau, W.-M.; Mattson, M.; Tycko, R. Self-Propagating, Molecular-Level Polymorphism in Alzheimer's β-Amyloid Fibrils Science 2005, 307, 262-265 (Pubitemid 40116242)
    • (2005) Science , vol.307 , Issue.5707 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.-M.4    Mattson, M.P.5    Tycko, R.6
  • 38
    • 84877258447 scopus 로고    scopus 로고
    • Polymorph-Specific Kinetics and Thermodynamics of β-Amyloid Fibril Growth
    • Qiang, W.; Kelley, K.; Tycko, R. Polymorph-Specific Kinetics and Thermodynamics of β-Amyloid Fibril Growth J. Am. Chem. Soc. 2013, 135, 6860-6871
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 6860-6871
    • Qiang, W.1    Kelley, K.2    Tycko, R.3
  • 39
    • 36049020231 scopus 로고    scopus 로고
    • A general model of prion strains and their pathogenicity
    • DOI 10.1126/science.1138718
    • Collinge, J.; Clarke, A. A General Model of Prion Strains and Their Pathogenicity Science 2007, 318, 930-936 (Pubitemid 350098981)
    • (2007) Science , vol.318 , Issue.5852 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 40
    • 84884217594 scopus 로고    scopus 로고
    • Molecular Structure of β-Amyloid Fibrils in Alzheimer's Disease Brain Tissue
    • Lu, J.-X.; Qiang, W.; Yau, W.-M.; Schwieters, C.; Meredith, S.; Tycko, R. Molecular Structure of β-Amyloid Fibrils in Alzheimer's Disease Brain Tissue Cell 2013, 154, 1257-1268
    • (2013) Cell , vol.154 , pp. 1257-1268
    • Lu, J.-X.1    Qiang, W.2    Yau, W.-M.3    Schwieters, C.4    Meredith, S.5    Tycko, R.6
  • 43
    • 0034722985 scopus 로고    scopus 로고
    • Formation of mixed fibrils demonstrates the generic nature and potential utility of amyloid nanostructures
    • DOI 10.1021/ja0029580
    • MacPhee, C.; Dobson, C. Formation of Mixed Fibrils Demonstrate the Generic Nature and Potential Utility of Amyloid Nanostructures J. Am. Chem. Soc. 2000, 122, 12707-12713 (Pubitemid 32052199)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.51 , pp. 12707-12713
    • MacPhee, C.E.1    Dobson, C.M.2
  • 44
    • 2342444028 scopus 로고    scopus 로고
    • Seeding Specificity in Amyloid Growth Induced by Heterologous Fibrils
    • DOI 10.1074/jbc.M311300200
    • O'Nuallain, B.; Williams, A.; Westermark, P.; Wetzel, R. Seeding Specificity in Amyloid Growth Induced by Heterologous Fibrils J. Biol. Chem. 2004, 279, 17490-17499 (Pubitemid 38560512)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.17 , pp. 17490-17499
    • O'Nuallain, B.1    Williams, A.D.2    Westermark, P.3    Wetzel, R.4
  • 45
    • 84870175936 scopus 로고    scopus 로고
    • Cross-Seeding of Fibrils from Two Types of Insulin Induces New Amyloid Strains
    • Surmacz-Chwedoruk, W.; Nieznańska, H.; Wójcik, S.; Dzwolak, W. Cross-Seeding of Fibrils from Two Types of Insulin Induces New Amyloid Strains Biochemistry 2012, 51, 9460-9469
    • (2012) Biochemistry , vol.51 , pp. 9460-9469
    • Surmacz-Chwedoruk, W.1    Nieznańska, H.2    Wójcik, S.3    Dzwolak, W.4
  • 46
    • 84871281215 scopus 로고    scopus 로고
    • S100A6 Amyloid Fibril Formation is Calcium-Modulated and Enhances Superoxide Dismutase-1 (SOD1) Aggregation
    • Botelho, H.; Leal, S.; Cardoso, I.; Yanamandra, K.; Morozova-Roche, L.; Fritz, G.; Gomes, C. S100A6 Amyloid Fibril Formation is Calcium-Modulated and Enhances Superoxide Dismutase-1 (SOD1) Aggregation J. Biol. Chem. 2012, 287, 42233-42242
    • (2012) J. Biol. Chem. , vol.287 , pp. 42233-42242
    • Botelho, H.1    Leal, S.2    Cardoso, I.3    Yanamandra, K.4    Morozova-Roche, L.5    Fritz, G.6    Gomes, C.7
  • 47
    • 84863987464 scopus 로고    scopus 로고
    • Inhibition of Amyloid Formation
    • Härd, T.; Lendel, C. Inhibition of Amyloid Formation J. Mol. Biol. 2012, 421, 441-465
    • (2012) J. Mol. Biol. , vol.421 , pp. 441-465
    • Härd, T.1    Lendel, C.2
  • 48
    • 0037473750 scopus 로고    scopus 로고
    • Prevention of transthyretin arnyloid disease by changing protein misfolding energetics
    • DOI 10.1126/science.1079589
    • Hammarström, P.; Wiseman, R.; Powers, E.; Kelly, J. Prevention of Transthyretin Amyloid Disease by Changing Protein Misfolding Energetics Science 2003, 299, 713-716 (Pubitemid 36159487)
    • (2003) Science , vol.299 , Issue.5607 , pp. 713-716
    • Hammarstrom, P.1    Wiseman, R.L.2    Powers, E.T.3    Kelly, J.W.4
  • 49
    • 77949272212 scopus 로고    scopus 로고
    • Structure-Based Design of Kinetic Stabilizers that Ameliorate the Transthyretin Amyloidoses
    • Connelly, S.; Choi, S.; Johnson, S.; Kelly, J.; Wilson, I. Structure-Based Design of Kinetic Stabilizers that Ameliorate the Transthyretin Amyloidoses Curr. Opin. Struct. Biol. 2010, 20, 54-62
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 54-62
    • Connelly, S.1    Choi, S.2    Johnson, S.3    Kelly, J.4    Wilson, I.5
  • 51
    • 33749522024 scopus 로고    scopus 로고
    • Peptide-Based Inhibitors of Amyloid Assembly
    • DOI 10.1016/S0076-6879(06)13015-3, PII S0076687906130153, Amyloid, Prions, and Other Protein Aggregates, Part C
    • Sciarretta, K.; Gordon, D.; Meredith, S. Peptide-Based Inhibitors of Amyloid Assembly Methods Enzymol. 2006, 413, 273-312 (Pubitemid 44528696)
    • (2006) Methods in Enzymology , vol.413 , pp. 273-312
    • Sciarretta, K.L.1    Gordon, D.J.2    Meredith, S.C.3
  • 53
    • 33845665382 scopus 로고    scopus 로고
    • Selection and characterization of Affibody ligands binding to Alzheimer amyloid β peptides
    • DOI 10.1016/j.jbiotec.2006.09.013, PII S0168165606007826
    • Grönwall, C.; Jonsson, A.; Lindstrom, S.; Gunneriusson, E.; StaÌŠhl, S.; Herne, N. Selection and Characterization of Affibody Ligands Binding to Alzheimer Amyloid β Peptides J. Biotechnol. 2007, 128, 162-183 (Pubitemid 44960520)
    • (2007) Journal of Biotechnology , vol.128 , Issue.1 , pp. 162-183
    • Gronwall, C.1    Jonsson, A.2    Lindstrom, S.3    Gunneriusson, E.4    Stahl, S.5    Herne, N.6
  • 56
    • 78651468727 scopus 로고    scopus 로고
    • Conformational Conversion during Amyloid Formation at Atomic Resolution
    • Eichner, T.; Kalverda, A.; Thompson, G.; Homans, S.; Radford, S. Conformational Conversion During Amyloid Formation at Atomic Resolution Mol. Cell 2011, 41, 161-172
    • (2011) Mol. Cell , vol.41 , pp. 161-172
    • Eichner, T.1    Kalverda, A.2    Thompson, G.3    Homans, S.4    Radford, S.5
  • 60
    • 33746698975 scopus 로고    scopus 로고
    • The physical basis of how prion conformations determine strain phenotypes
    • DOI 10.1038/nature04922, PII NATURE04922
    • Tanaka, M.; Collins, S.; Toyama, B.; Weissman, J. The Physical Basis of how Prion Conformations Determine Strain Phenotypes Nature 2006, 442, 585-589 (Pubitemid 44167919)
    • (2006) Nature , vol.442 , Issue.7102 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 62
    • 84860377014 scopus 로고    scopus 로고
    • Selective Molecular Recognition in Amyloid Growth and Transmission and Cross-Species Barriers
    • Ma, B.; Nussinov, R. Selective Molecular Recognition in Amyloid Growth and Transmission and Cross-Species Barriers J. Mol. Biol. 2012, 421, 172-184
    • (2012) J. Mol. Biol. , vol.421 , pp. 172-184
    • Ma, B.1    Nussinov, R.2
  • 63
    • 0035800087 scopus 로고    scopus 로고
    • Structure - Function relationships for inhibitors of β-Amyloid toxicity containing the recognition sequence KLVFF
    • DOI 10.1021/bi002734u
    • Lowe, T.; Strzelec, A.; Kiessling, L.; Murphy, R. Structure-Function Relationships for Inhibitors of β-Amyloid Toxicity Containing the Recognition Sequence KLVFF Biochemistry 2001, 40, 7882-7889 (Pubitemid 32622980)
    • (2001) Biochemistry , vol.40 , Issue.26 , pp. 7882-7889
    • Lowe, T.L.1    Strzelec, A.2    Kiessling, L.L.3    Murphy, R.M.4
  • 64
    • 79958694883 scopus 로고    scopus 로고
    • Dissecting the Role of Single Regions of an IAPP Mimic and IAPP in Inhibition of Aβ40 Amyloid Formation and Cytotoxicity
    • Andreetto, E.; Yan, L.-M.; Caporale, A.; Kapurniotu, A. Dissecting the Role of Single Regions of an IAPP Mimic and IAPP in Inhibition of Aβ40 Amyloid Formation and Cytotoxicity ChemBioChem 2011, 12, 1313-1322
    • (2011) ChemBioChem , vol.12 , pp. 1313-1322
    • Andreetto, E.1    Yan, L.-M.2    Caporale, A.3    Kapurniotu, A.4


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