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Volumn 6, Issue 1, 2009, Pages

A role for helical intermediates in amyloid formation by natively unfolded polypeptides?

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; POLYPEPTIDE; PEPTIDE;

EID: 62449226332     PISSN: 14783967     EISSN: 14783975     Source Type: Journal    
DOI: 10.1088/1478-3975/6/1/015005     Document Type: Article
Times cited : (171)

References (53)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F and Dobson C M 2006 Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 333-6
    • (2006) Annu. Rev. Biochem. , vol.75 , Issue.1 , pp. 333-336
    • Chiti, F.1    And Dobson, C.M.2
  • 3
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • DOI 10.1038/nature02264
    • Selkoe D 2003 Folding proteins in fatal ways Nature 426 900-4 (Pubitemid 38056883)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 900-904
    • Selkoe, D.J.1
  • 5
    • 1342324027 scopus 로고    scopus 로고
    • Progress towards a molecular-level structural understanding of amyloid fibrils
    • DOI 10.1016/j.sbi.2003.12.002
    • Tycko R 2004 Progress towards a molecular level understanding of amyloid fibrils Curr. Opin. Struct. Biol. 14 96-103 (Pubitemid 38249598)
    • (2004) Current Opinion in Structural Biology , vol.14 , Issue.1 , pp. 96-103
    • Tycko, R.1
  • 8
    • 36749033116 scopus 로고    scopus 로고
    • Peptide conformation and supramolecular organization in amylin fibrils: Constraints from solid-state NMR
    • DOI 10.1021/bi701427q
    • Luca S, Yau W-M, Leapman R and Tycko R 2007 Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR Biochemistry 46 13505-22 (Pubitemid 350209947)
    • (2007) Biochemistry , vol.46 , Issue.47 , pp. 13505-13522
    • Luca, S.1    Yau, W.-M.2    Leapman, R.3    Tycko, R.4
  • 9
    • 0036708168 scopus 로고    scopus 로고
    • Paradigm shifts in Alzheimer's disease and other neuro degenerative disorders: The emerging role of oligomeric assemblies
    • Kirkitadze M D, Bitan G and Teplow D B 2002 Paradigm shifts in Alzheimer's disease and other neuro degenerative disorders: the emerging role of oligomeric assemblies J. Neurosci. Res. 69 567-77
    • (2002) J. Neurosci. Res. , vol.69 , Issue.5 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 10
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • DOI 10.1146/annurev.neuro.26.010302.081142
    • Caughey B and Lansbury P T Jr 2003 Protofibrils, pores, fibrils and neurodegeneration: separating responsible protein aggregates from the innocent bystanders Annu. Rev. Neurosci. 26 267-98 (Pubitemid 37064935)
    • (2003) Annual Review of Neuroscience , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury Jr., P.T.2
  • 11
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • DOI 10.1126/science.1079469
    • Kayed R, Head E, Thompson J L, McIntire T M, Milton S C, Cotman C W and Glable C G 2003 Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis Science 300 486-9 (Pubitemid 36444329)
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabel, C.G.7
  • 12
    • 33750361540 scopus 로고    scopus 로고
    • A century-old debate on protein aggregation and neurodegeneration enters the clinic
    • DOI 10.1038/nature05290, PII NATURE05290
    • Lansbury P T and Lashuel H A 2006 A century-old debate on protein aggregation and neurodegeneration enters the clinic Nature 443 774-9 (Pubitemid 44622681)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, H.A.2
  • 13
    • 2542427690 scopus 로고    scopus 로고
    • Oligomers in the brain: The emerging role of soluble protein aggregates in neurodegeneration
    • DOI 10.2174/0929866043407174
    • Walsh D M and Selkoe D J 2004 Oligomers in the brain: the emerging role of soluble protein aggregates in neurodegeneration Protein Peptide Lett. 11 213-28 (Pubitemid 38689025)
    • (2004) Protein and Peptide Letters , vol.11 , Issue.3 , pp. 213-228
    • Walsh, D.M.1    Selkoe, D.J.2
  • 15
    • 33749597429 scopus 로고    scopus 로고
    • Nucleation: The Connections between Equilibrium and Kinetic Behavior
    • DOI 10.1016/S0076-6879(06)12017-0, PII S0076687906120170
    • Ferrone F 2006 Nucleation: the connections between equilibrium and kinetic behavior Method. Enzymol. 412 285-99 (Pubitemid 44548586)
    • (2006) Methods in Enzymology , vol.412 , pp. 285-299
    • Ferrone, F.A.1
  • 16
    • 0037046151 scopus 로고    scopus 로고
    • Islet amyloid: Phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis
    • DOI 10.1021/bi0160462
    • Padrick S B and Miranker A D 2002 Islet amyloid: phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis Biochemistry 41 4694-703 (Pubitemid 34275671)
    • (2002) Biochemistry , vol.41 , Issue.14 , pp. 4694-4703
    • Padrick, S.B.1    Miranker, A.D.2
  • 17
    • 33749824175 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of amyloid fibril assembly
    • Wetzel R 2006 Kinetics and thermodynamics of amyloid fibril assembly Acc. Chem. Res. 39 671-9
    • (2006) Acc. Chem. Res. , vol.39 , Issue.9 , pp. 671-679
    • Wetzel, R.1
  • 18
    • 1842686289 scopus 로고    scopus 로고
    • Kinetic analysis of beta-amyloid fibril elongation
    • DOI 10.1016/j.ab.2004.01.014, PII S0003269704000922
    • Cannon M J, Williams A D, Wetzel R and Myszka D G 2004 Kinetic analysis of beta-amyloid fibril elongation Anal. Biochem. 328 67-75 (Pubitemid 38479619)
    • (2004) Analytical Biochemistry , vol.328 , Issue.1 , pp. 67-75
    • Cannon, M.J.1    Williams, A.D.2    Wetzel, R.3    Myszka, D.G.4
  • 19
    • 0024387388 scopus 로고
    • Proteoglycans in the pathogenesis of Alzheimer's disease and other amyloidoses
    • DOI 10.1016/0197-4580(89)90108-5
    • Snow A D and Wight T N 1989 Proteoglycans in the pathogenesis of Alzheimer's disease and other amyloidosis Neurobiol. Aging 10 481-97 (Pubitemid 19245453)
    • (1989) Neurobiology of Aging , vol.10 , Issue.5 , pp. 481-497
    • Snow, A.D.1    Wight, T.N.2
  • 20
    • 0034828025 scopus 로고    scopus 로고
    • Basement membrane and beta amyloid fibrillogenesis in Alzheimer's disease
    • DOI 10.1016/S0074-7696(01)10005-7
    • Inoue S 2001 Basement membrane and β amyloid fibrillogenesis in Alzheimer's disease Int. Rev. Cytol. 210 121-61 (Pubitemid 32888802)
    • (2001) International Review of Cytology , vol.210 , pp. 121-161
    • Inoue, S.1
  • 21
    • 0042703654 scopus 로고    scopus 로고
    • Amyloidogenesis: Historical and modern observations point to heparan sulfate proteoglycans as a major culprit
    • Ancsin J B 2003 Amyloidogenesis: historical and modern observations point to heparan sulfate proteoglycans as a major culprit Amyloid: J. Protein Folding Disord 10 67-79 (Pubitemid 36936537)
    • (2003) Amyloid , vol.10 , Issue.2 , pp. 67-79
    • Ancsin, J.B.1
  • 22
    • 4143094106 scopus 로고    scopus 로고
    • Phospholipid catalysis of diabetic amyloid assembly
    • DOI 10.1016/j.jmb.2004.06.086, PII S0022283604007983
    • Knight J D and Miranker A D 2004 Phospholipid catalysis of diabetic amyloid assembly J. Mol. Biol 341 1175-87 (Pubitemid 39099208)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.5 , pp. 1175-1187
    • Knight, J.D.1    Miranker, A.D.2
  • 23
    • 33750365052 scopus 로고    scopus 로고
    • Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
    • Lashuel H A and Lansbury P T Jr 2006 Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? Quart. Rev. Biophys 39 167-201
    • (2006) Quart. Rev. Biophys , vol.39 , Issue.2 , pp. 167-201
    • Lashuel, H.A.1    And Lansbury, P.T.2
  • 25
    • 34547174917 scopus 로고    scopus 로고
    • Fluorescence as a method to reveal structures and membrane-interactions of amyloidogenic proteins
    • DOI 10.1016/j.bbamem.2007.03.015, PII S0005273607000806
    • Munishkina L A and Fink A L 2007 Fluorescence as a method to reveal structures and membrane-interactions of amyloidogenic proteins BBCA Biomembr. 1768 1862-85 (Pubitemid 47125851)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.8 , pp. 1862-1885
    • Munishkina, L.A.1    Fink, A.L.2
  • 26
    • 0035812658 scopus 로고    scopus 로고
    • Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis
    • DOI 10.1006/jmbi.2001.4970
    • Kirkitadze M D, Condron M M and Teplow D B 2001 Identification and characterization of key kinetic intermediates in amyloid b-protein fibrillogenesis J. Mol. Biol. 312 1103-19 (Pubitemid 32980329)
    • (2001) Journal of Molecular Biology , vol.312 , Issue.5 , pp. 1103-1119
    • Kirkitadze, M.D.1    Condron, M.M.2    Teplow, D.B.3
  • 27
    • 33749832945 scopus 로고    scopus 로고
    • Elucidating amyloid β-protein folding and assembly: A multidisciplinary approach
    • Teplow D B et al 2006 Elucidating amyloid β-protein folding and assembly: a multidisciplinary approach Acc. Chem. Res. 39 635-45
    • (2006) Acc. Chem. Res. , vol.39 , Issue.9 , pp. 635-645
    • Teplow, D.B.1    Al, E.2
  • 29
    • 0030864812 scopus 로고    scopus 로고
    • Engineering peptides and proteins that undergo α-to-beta transitions
    • DOI 10.1016/S0959-440X(97)80113-3
    • Mihara H and Takahashi Y 1997 Engineering peptides and proteins that undergo α to b transition Curr. Opin. Struct. Biol. 7 501-8 (Pubitemid 27371294)
    • (1997) Current Opinion in Structural Biology , vol.7 , Issue.4 , pp. 501-508
    • Mihara, H.1    Takahashi, Y.2
  • 30
    • 0034729680 scopus 로고    scopus 로고
    • Solid-state NMR determination of the secondary structure of Samia cynthia ricini silk
    • DOI 10.1038/35016625
    • van Beek J D, Beaulieu L, Schafer H, Demura M, Aaskura T and Meier B H 2000 Solid state NMR determination of the secondary structure of Samia Cynthia silk Nature 405 1077-9 (Pubitemid 30447795)
    • (2000) Nature , vol.405 , Issue.6790 , pp. 1077-1079
    • Van Beek, J.D.1    Beaulleu, L.2    Schafer, H.3    Demura, M.4    Asakura, T.5    Meler, B.H.6
  • 32
    • 33845960266 scopus 로고    scopus 로고
    • Direct detection of transient α-helical states in islet amyloid polypeptide
    • DOI 10.1110/ps.062486907
    • Williamson J and Miranker A 2007 Direct detection of transient α-helical states in islet amyloid polypeptide Protein Sci 16 110-17 (Pubitemid 46036503)
    • (2007) Protein Science , vol.16 , Issue.1 , pp. 110-117
    • Williamson, J.A.1    Miranker, A.D.2
  • 33
    • 0025981260 scopus 로고
    • Solution structure of human calcitonin gene-related peptide by 1 H-NMR and distance geometry with restrained molecular dynamics
    • Breeze A L, Harvey T S, Bazzo R and Campbell I D 1991 Solution structure of human calcitonin gene-related peptide by 1 H-NMR and distance geometry with restrained molecular dynamics Biochemistry 30 575-82
    • (1991) Biochemistry , vol.30 , Issue.2 , pp. 575-582
    • Breeze, A.L.1    Harvey, T.S.2    Bazzo, R.3    Campbell, I.D.4
  • 35
    • 24644502612 scopus 로고    scopus 로고
    • Lipid membranes modulate the structure of islet amyloid polypeptide
    • DOI 10.1021/bi050840w
    • Jayasinghe S A and Langen R 2005 Lipid membranes modulate the structure of islet amyloid polypeptide Biochemistry 44 12113-9 (Pubitemid 41285709)
    • (2005) Biochemistry , vol.44 , Issue.36 , pp. 12113-12119
    • Jayasinghe, S.A.1    Langen, R.2
  • 36
    • 33747119677 scopus 로고    scopus 로고
    • Conserved and cooperative assembly of membrane-bound α-helical states of islet amyloid polypeptide
    • DOI 10.1021/bi060579z
    • Knight J D, Hebda J A and Miranker A D 2006 Conserved and cooperative assembly of membrane bound α-helical states of islet amyloid polypeptide Biochemistry 45 9496-508 (Pubitemid 44223253)
    • (2006) Biochemistry , vol.45 , Issue.31 , pp. 9496-9508
    • Knight, J.D.1    Hebda, J.A.2    Miranker, A.D.3
  • 37
    • 34547152267 scopus 로고    scopus 로고
    • Membrane interaction of islet amyloid polypeptide
    • DOI 10.1016/j.bbamem.2007.01.022, PII S0005273607000351
    • Jayasinghe S A and Langen R 2007 Membrane interaction of islet amyloid polypeptide BBCA Biomembr. 1768 2002-9 (Pubitemid 47125849)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.8 , pp. 2002-2009
    • Jayasinghe, S.A.1    Langen, R.2
  • 38
    • 47749117154 scopus 로고    scopus 로고
    • Structure of α-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding
    • Apostolidou M, Jayasinghe S A and Langen R 2008 Structure of α-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding J. Biol. Chem 283 17205-10
    • (2008) J. Biol. Chem , vol.283 , Issue.25 , pp. 17205-17210
    • Apostolidou, M.1    Jayasinghe, S.A.2    Langen, R.3
  • 39
    • 35349002742 scopus 로고    scopus 로고
    • Negatively Charged Phospholipid Membranes Induce Amyloid Formation of Medin via an α-Helical Intermediate
    • DOI 10.1016/j.jmb.2007.08.064, PII S0022283607011461
    • Olofsson A, Borowik T, Grobner G and Sauer-Eriksson A E 2007 Negatively charged phospholipids membranes induce amyloid formation of Medin via an α-helical intermediate J. Mol. Biol. 374 186194 (Pubitemid 47600226)
    • (2007) Journal of Molecular Biology , vol.374 , Issue.1 , pp. 186-194
    • Olofsson, A.1    Borowik, T.2    Grobner, G.3    Sauer-Eriksson, A.E.4
  • 40
    • 0034602271 scopus 로고    scopus 로고
    • Interaction of human α-Synuclein and Parkinson's diseases variants with phospholipids
    • Perrin R J, Woods W S, Clayton D F and George J M 2000 Interaction of human α-Synuclein and Parkinson's diseases variants with phospholipids J. Biol. Chem 275 34393-8
    • (2000) J. Biol. Chem , vol.275 , Issue.44 , pp. 34393-34398
    • Perrin, R.J.1    Woods, W.S.2    Clayton, D.F.3    George, J.M.4
  • 41
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of α-synuclein in its free and lipid-associated states
    • DOI 10.1006/jmbi.2001.4538
    • Eliezer D, Kutluay E, Bussell R Jr and Brown G 2001 Conformational properties of alpha-synuclein in its free and lipid associated states J. Mol. Biol. 307 799-807 (Pubitemid 33029953)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.4 , pp. 1061-1073
    • Eliezer, D.1    Kutluay, E.2    Bussell Jr., R.3    Browne, G.4
  • 42
    • 0037930855 scopus 로고    scopus 로고
    • Lipid binding inhibits α-synuclein fibril formation
    • DOI 10.1074/jbc.M210136200
    • Zhu M, Li J and Fink A L 2003 Lipid binding inhibits α-Synuclein fibril formation J. Biol. Chem. 278 16873-7 (Pubitemid 36799558)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.19 , pp. 16873-16877
    • Zhu, M.1    Fink, A.L.2
  • 43
    • 0037016741 scopus 로고    scopus 로고
    • Membrane bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form
    • Lee H J, Choi C and Lee S J 2002 Membrane bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form J. Biol. Chem. 277 671-8
    • (2002) J. Biol. Chem. , vol.277 , Issue.1 , pp. 671-678
    • Lee, H.J.1    Choi, C.2    Lee, S.J.3
  • 44
    • 35648975218 scopus 로고    scopus 로고
    • Amyloid formation by pro-islet amyloid polypeptide processing intermediates: Examination of the role of protein heparan sulfate interactions and implications for islet amyloid formation in type 2 diabetes
    • DOI 10.1021/bi7004834
    • Meng F, Abedini A and Raleigh D P 2007 Amyloid formation by pro-islet amyloid polypeptide processing intermediates: examination of the role of protein heparan sulfate interactions and implications for islet amyloid formation in type 2 diabetes Biochemistry 46 12091-9 (Pubitemid 350022365)
    • (2007) Biochemistry , vol.46 , Issue.43 , pp. 12091-12099
    • Meng, F.1    Abedini, A.2    Song, B.3    Raleigh, D.P.4
  • 45
    • 4143094106 scopus 로고    scopus 로고
    • Phospholipid catalysis of diabetic amyloid assembly
    • DOI 10.1016/j.jmb.2004.06.086, PII S0022283604007983
    • Knight J D and Miranker A D 2004 Phospholipid catalysis of diabetic amyloid assembly J. Mol. Biol. 341 1175-87 (Pubitemid 39099208)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.5 , pp. 1175-1187
    • Knight, J.D.1    Miranker, A.D.2
  • 46
    • 0033579545 scopus 로고    scopus 로고
    • Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin
    • DOI 10.1006/jmbi.1999.3286
    • Nilsson M R and Raleigh D P 1999 Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin J. Mol. Biol. 294 1375-85 (Pubitemid 30008807)
    • (1999) Journal of Molecular Biology , vol.294 , Issue.5 , pp. 1375-1385
    • Nilsson, M.R.1    Raleigh, D.P.2
  • 47
    • 0035907265 scopus 로고    scopus 로고
    • Identification of a heparin binding domain in the N-terminal cleavage site of pro-islet amyloid polypeptide
    • Park K and Verchere C B 2001 Identification of a heparin binding domain in the N-terminal cleavage site of pro-islet amyloid polypeptide J. Biol. Chem 276 16611-6
    • (2001) J. Biol. Chem , vol.276 , Issue.20 , pp. 16611-16616
    • Park, K.1    And Verchere, C.B.2
  • 48
    • 33746614282 scopus 로고    scopus 로고
    • Characterization of the heparin binding site in the N-terminus of human pro-islet amyloid polypeptide: Implications for amyloid formation
    • DOI 10.1021/bi0510936
    • Abedini A, Tracz S M, Cho J and Raleigh D 2006 Characterization of the heparin binding site in the N-terminus of human pro-islet amyloid polypeptide: implications for amyloid formation Biochemistry 45 9228-37 (Pubitemid 44156386)
    • (2006) Biochemistry , vol.45 , Issue.30 , pp. 9228-9237
    • Abedini, A.1    Tracz, S.M.2    Cho, J.-H.3    Raleigh, D.P.4
  • 49
    • 0035443168 scopus 로고    scopus 로고
    • Two-dimensional infrared spectroscopy: A promising new method for the time resolution of structures
    • DOI 10.1016/S0959-440X(00)00243-8
    • Zanni M T and Hochstrasser R M 2001 Two-dimensional infrared spectroscopy: a promising new method for the time resolution of structures Curr. Opin. Struct. Bio. 11 516-22 (Pubitemid 32972011)
    • (2001) Current Opinion in Structural Biology , vol.11 , Issue.5 , pp. 516-522
    • Zanni, M.T.1    Hochstrasser, R.M.2
  • 52
    • 45549085028 scopus 로고    scopus 로고
    • Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Aβ40
    • Kim Y S, Liu L, Axelsen P H and Hochstrasser R M 2008 Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Aβ40 Proc. Natl. Acad. Sci. 105 7720-5
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , Issue.22 , pp. 7720-7725
    • Kim, Y.S.1    Liu, L.2    Axelsen, P.H.3    Hochstrasser, R.M.4
  • 53
    • 35048898903 scopus 로고    scopus 로고
    • A single-point mutation converts the highly amyloidogenic human islet amyloid polypeptide into a potent fibrillization inhibitor
    • DOI 10.1021/ja072157y
    • Abedini A, Meng F and Raleigh D A 2007 Single-point mutation converts the highly amyloidogenic human islet amyloid polypeptide into a potent fibrillization inhibitor J. Am. Chem. Soc. 129 11300-1 (Pubitemid 47555526)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.37 , pp. 11300-11301
    • Abedini, A.1    Meng, F.2    Raleigh, D.P.3


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