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Volumn 7, Issue 9, 2012, Pages

Distinct Annular Oligomers Captured along the Assembly and Disassembly Pathways of Transthyretin Amyloid Protofibrils

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; OLIGOMER; PREALBUMIN;

EID: 84866318129     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0044992     Document Type: Article
Times cited : (44)

References (54)
  • 1
    • 84869887960 scopus 로고    scopus 로고
    • Structural features and cytotoxicity of amyloid oligomers: Implications in Alzheimer's disease and other diseases with amyloid deposits
    • 10.1016/j.pneurobio.2012.1003.1002
    • Stefani M (2012) Structural features and cytotoxicity of amyloid oligomers: Implications in Alzheimer's disease and other diseases with amyloid deposits. Prog Neurobiol: 10.1016/j.pneurobio.2012.1003.1002.
    • (2012) Prog Neurobiol
    • Stefani, M.1
  • 2
    • 66549106850 scopus 로고    scopus 로고
    • Serial PIB and MRI in normal, mild cognitive impairment and Alzheimer's disease: implications for sequence of pathological events in Alzheimer's disease
    • Jack CR Jr, Lowe VJ, Weigand SD, Wiste HJ, Senjem ML, et al. (2009) Serial PIB and MRI in normal, mild cognitive impairment and Alzheimer's disease: implications for sequence of pathological events in Alzheimer's disease. Brain 132: 1355-1365.
    • (2009) Brain , vol.132 , pp. 1355-1365
    • Jack Jr., C.R.1    Lowe, V.J.2    Weigand, S.D.3    Wiste, H.J.4    Senjem, M.L.5
  • 3
    • 84855750207 scopus 로고    scopus 로고
    • Single-channel Ca(2+) imaging implicates Abeta1-42 amyloid pores in Alzheimer's disease pathology
    • Demuro A, Smith M, Parker I, (2011) Single-channel Ca(2+) imaging implicates Abeta1-42 amyloid pores in Alzheimer's disease pathology. J Cell Biol 195: 515-524.
    • (2011) J Cell Biol , vol.195 , pp. 515-524
    • Demuro, A.1    Smith, M.2    Parker, I.3
  • 4
    • 63649147251 scopus 로고    scopus 로고
    • Amyloid-beta-induced ion flux in artificial lipid bilayers and neuronal cells: resolving a controversy
    • Capone R, Quiroz FG, Prangkio P, Saluja I, Sauer AM, et al. (2009) Amyloid-beta-induced ion flux in artificial lipid bilayers and neuronal cells: resolving a controversy. Neurotox Res 16: 1-13.
    • (2009) Neurotox Res , vol.16 , pp. 1-13
    • Capone, R.1    Quiroz, F.G.2    Prangkio, P.3    Saluja, I.4    Sauer, A.M.5
  • 5
    • 79959342196 scopus 로고    scopus 로고
    • Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity
    • Last NB, Rhoades E, Miranker AD, (2011) Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity. Proc Natl Acad Sci U S A 108: 9460-9465.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 9460-9465
    • Last, N.B.1    Rhoades, E.2    Miranker, A.D.3
  • 6
    • 23044449398 scopus 로고    scopus 로고
    • Amyloid ion channels: a common structural link for protein-misfolding disease
    • Quist A, Doudevski I, Lin H, Azimova R, Ng D, et al. (2005) Amyloid ion channels: a common structural link for protein-misfolding disease. Proc Natl Acad Sci U S A 102: 10427-10432.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 10427-10432
    • Quist, A.1    Doudevski, I.2    Lin, H.3    Azimova, R.4    Ng, D.5
  • 7
    • 3142664614 scopus 로고    scopus 로고
    • Annular alpha-synuclein species from purified multiple system atrophy inclusions
    • Pountney DL, Lowe R, Quilty M, Vickers JC, Voelcker NH, et al. (2004) Annular alpha-synuclein species from purified multiple system atrophy inclusions. J Neurochem 90: 502-512.
    • (2004) J Neurochem , vol.90 , pp. 502-512
    • Pountney, D.L.1    Lowe, R.2    Quilty, M.3    Vickers, J.C.4    Voelcker, N.H.5
  • 8
    • 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: 48-57.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 48-57
    • Kodali, R.1    Wetzel, R.2
  • 9
    • 0033857583 scopus 로고    scopus 로고
    • Review: TTR amyloidosis-structural features leading to protein aggregation and their implications on therapeutic strategies
    • Damas AM, Saraiva MJ, (2000) Review: TTR amyloidosis-structural features leading to protein aggregation and their implications on therapeutic strategies. J Struct Biol 130: 290-299.
    • (2000) J Struct Biol , vol.130 , pp. 290-299
    • Damas, A.M.1    Saraiva, M.J.2
  • 10
    • 0028969996 scopus 로고
    • Transthyretin mutations in health and disease
    • Saraiva MJ, (1995) Transthyretin mutations in health and disease. Hum Mutat 5: 191-196.
    • (1995) Hum Mutat , vol.5 , pp. 191-196
    • Saraiva, M.J.1
  • 11
    • 23044470902 scopus 로고    scopus 로고
    • Hereditary transthyretin amyloidosis: molecular basis and therapeutical strategies
    • Saraiva MJ, (2002) Hereditary transthyretin amyloidosis: molecular basis and therapeutical strategies. Expert Rev Mol Med 4: 1-11.
    • (2002) Expert Rev Mol Med , vol.4 , pp. 1-11
    • Saraiva, M.J.1
  • 13
    • 0035018450 scopus 로고    scopus 로고
    • Transthyretin mutations in hyperthyroxinemia and amyloid diseases
    • Saraiva MJ, (2001) Transthyretin mutations in hyperthyroxinemia and amyloid diseases. Hum Mutat 17: 493-503.
    • (2001) Hum Mutat , vol.17 , pp. 493-503
    • Saraiva, M.J.1
  • 14
    • 0030004644 scopus 로고    scopus 로고
    • The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid
    • Lai Z, Colon W, Kelly JW, (1996) The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. Biochemistry 35: 6470-6482.
    • (1996) Biochemistry , vol.35 , pp. 6470-6482
    • Lai, Z.1    Colon, W.2    Kelly, J.W.3
  • 15
    • 79955124353 scopus 로고    scopus 로고
    • Structure and assembly-disassembly properties of wild-type transthyretin amyloid protofibrils observed with atomic force microscopy
    • Pires RH, Saraiva MJ, Damas AM, Kellermayer MS, (2011) Structure and assembly-disassembly properties of wild-type transthyretin amyloid protofibrils observed with atomic force microscopy. J Mol Recognit 24: 467-476.
    • (2011) J Mol Recognit , vol.24 , pp. 467-476
    • Pires, R.H.1    Saraiva, M.J.2    Damas, A.M.3    Kellermayer, M.S.4
  • 16
    • 0026675307 scopus 로고
    • Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
    • Colon W, Kelly JW, (1992) Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 31: 8654-8660.
    • (1992) Biochemistry , vol.31 , pp. 8654-8660
    • Colon, W.1    Kelly, J.W.2
  • 17
    • 0030694782 scopus 로고    scopus 로고
    • The amyloidogenic potential of transthyretin variants correlates with their tendency to aggregate in solution
    • Quintas A, Saraiva MJ, Brito RM, (1997) The amyloidogenic potential of transthyretin variants correlates with their tendency to aggregate in solution. FEBS Lett 418: 297-300.
    • (1997) FEBS Lett , vol.418 , pp. 297-300
    • Quintas, A.1    Saraiva, M.J.2    Brito, R.M.3
  • 18
    • 15444372454 scopus 로고    scopus 로고
    • Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize
    • Barrera NP, Ormond SJ, Henderson RM, Murrell-Lagnado RD, Edwardson JM, (2005) Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize. J Biol Chem 280: 10759-10765.
    • (2005) J Biol Chem , vol.280 , pp. 10759-10765
    • Barrera, N.P.1    Ormond, S.J.2    Henderson, R.M.3    Murrell-Lagnado, R.D.4    Edwardson, J.M.5
  • 20
    • 72149113587 scopus 로고    scopus 로고
    • The transient receptor potential channels TRPP2 and TRPC1 form a heterotetramer with a 2:2 stoichiometry and an alternating subunit arrangement
    • Kobori T, Smith GD, Sandford R, Edwardson JM, (2009) The transient receptor potential channels TRPP2 and TRPC1 form a heterotetramer with a 2:2 stoichiometry and an alternating subunit arrangement. J Biol Chem 284: 35507-35513.
    • (2009) J Biol Chem , vol.284 , pp. 35507-35513
    • Kobori, T.1    Smith, G.D.2    Sandford, R.3    Edwardson, J.M.4
  • 21
    • 0017824077 scopus 로고
    • Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A
    • Blake CC, Geisow MJ, Oatley SJ, Rerat B, Rerat C, (1978) Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A. J Mol Biol. 121: 339-356.
    • (1978) J Mol Biol , vol.121 , pp. 339-356
    • Blake, C.C.1    Geisow, M.J.2    Oatley, S.J.3    Rerat, B.4    Rerat, C.5
  • 22
    • 33750365052 scopus 로고    scopus 로고
    • Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins
    • Lashuel HA, Lansbury PT Jr, (2006) Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? Q Rev Biophys 39: 167-201.
    • (2006) Q Rev Biophys , vol.39 , pp. 167-201
    • Lashuel, H.A.1    Lansbury Jr., P.T.2
  • 25
    • 0142040121 scopus 로고    scopus 로고
    • Formation of critical oligomers is a key event during conformational transition of recombinant syrian hamster prion protein
    • Sokolowski F, Modler AJ, Masuch R, Zirwer D, Baier M, et al. (2003) Formation of critical oligomers is a key event during conformational transition of recombinant syrian hamster prion protein. J Biol Chem 278: 40481-40492.
    • (2003) J Biol Chem , vol.278 , pp. 40481-40492
    • Sokolowski, F.1    Modler, A.J.2    Masuch, R.3    Zirwer, D.4    Baier, M.5
  • 26
    • 36049044748 scopus 로고    scopus 로고
    • Atomic force microscopy images suggest aggregation mechanism in cerato-platanin
    • Sbrana F, Bongini L, Cappugi G, Fanelli D, Guarino A, et al. (2007) Atomic force microscopy images suggest aggregation mechanism in cerato-platanin. Eur Biophys J 36: 727-732.
    • (2007) Eur Biophys J , vol.36 , pp. 727-732
    • Sbrana, F.1    Bongini, L.2    Cappugi, G.3    Fanelli, D.4    Guarino, A.5
  • 27
    • 0037072284 scopus 로고    scopus 로고
    • Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes
    • Ding TT, Lee SJ, Rochet JC, Lansbury PT, (2002) Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes. Biochemistry 41: 10209-10217.
    • (2002) Biochemistry , vol.41 , pp. 10209-10217
    • Ding, T.T.1    Lee, S.J.2    Rochet, J.C.3    Lansbury, P.T.4
  • 29
    • 0041825430 scopus 로고    scopus 로고
    • Mixtures of wild-type and a pathogenic (E22G) form of A beta 40 in vitro accumulate protofibrils, including amyloid pores
    • Lashuel HA, Hartley DM, Petre BM, Wall JS, Simon MN, et al. (2003) Mixtures of wild-type and a pathogenic (E22G) form of A beta 40 in vitro accumulate protofibrils, including amyloid pores. Journal of Molecular Biology 332: 795-808.
    • (2003) Journal of Molecular Biology , vol.332 , pp. 795-808
    • Lashuel, H.A.1    Hartley, D.M.2    Petre, B.M.3    Wall, J.S.4    Simon, M.N.5
  • 30
    • 2542483823 scopus 로고    scopus 로고
    • ABri peptide associated with familial British dementia forms annular and ring-like protofibrillar structures
    • Srinivasan R, Marchant RE, Zagorski MG, (2004) ABri peptide associated with familial British dementia forms annular and ring-like protofibrillar structures. Amyloid-Journal of Protein Folding Disorders 11: 10-13.
    • (2004) Amyloid-Journal of Protein Folding Disorders , vol.11 , pp. 10-13
    • Srinivasan, R.1    Marchant, R.E.2    Zagorski, M.G.3
  • 31
    • 0042744699 scopus 로고    scopus 로고
    • Amyloid protofilaments from the calcium-binding protein equine lysozyme: Formation of ring and linear structures depends on pH and metal ion concentration
    • Malisauskas M, Zamotin V, Jass J, Noppe W, Dobson CM, et al. (2003) Amyloid protofilaments from the calcium-binding protein equine lysozyme: Formation of ring and linear structures depends on pH and metal ion concentration. Journal of Molecular Biology 330: 879-890.
    • (2003) Journal of Molecular Biology , vol.330 , pp. 879-890
    • Malisauskas, M.1    Zamotin, V.2    Jass, J.3    Noppe, W.4    Dobson, C.M.5
  • 32
    • 23144463784 scopus 로고    scopus 로고
    • Assembly of the full-length recombinant mouse prion protein I. Formation of soluble oligomers
    • Vendrely C, Valadie H, Bednarova L, Cardin L, Pasdeloup M, et al. (2005) Assembly of the full-length recombinant mouse prion protein I. Formation of soluble oligomers. Biochim Biophys Acta 1724: 355-366.
    • (2005) Biochim Biophys Acta , vol.1724 , pp. 355-366
    • Vendrely, C.1    Valadie, H.2    Bednarova, L.3    Cardin, L.4    Pasdeloup, M.5
  • 34
    • 58149400915 scopus 로고    scopus 로고
    • Conformational conversion may precede or follow aggregate elongation on alternative pathways of amyloid protofibril formation
    • Kumar S, Udgaonkar JB, (2009) Conformational conversion may precede or follow aggregate elongation on alternative pathways of amyloid protofibril formation. J Mol Biol 385: 1266-1276.
    • (2009) J Mol Biol , vol.385 , pp. 1266-1276
    • Kumar, S.1    Udgaonkar, J.B.2
  • 35
    • 55749087363 scopus 로고    scopus 로고
    • Direct characterization of amyloidogenic oligomers by single-molecule fluorescence
    • Orte A, Birkett NR, Clarke RW, Devlin GL, Dobson CM, et al. (2008) Direct characterization of amyloidogenic oligomers by single-molecule fluorescence. Proc Natl Acad Sci U S A 105: 14424-14429.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 14424-14429
    • Orte, A.1    Birkett, N.R.2    Clarke, R.W.3    Devlin, G.L.4    Dobson, C.M.5
  • 36
    • 77951975748 scopus 로고    scopus 로고
    • Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils
    • Ahmed M, Davis J, Aucoin D, Sato T, Ahuja S,et al. Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils. Nat Struct Mol Biol 17: 561-567.
    • Nat Struct Mol Biol , vol.17 , pp. 561-567
    • Ahmed, M.1    Davis, J.2    Aucoin, D.3    Sato, T.4    Ahuja, S.5
  • 37
    • 24044518189 scopus 로고    scopus 로고
    • Protofibril formation of amyloid beta-protein at low pH via a non-cooperative elongation mechanism
    • Carrotta R, Manno M, Bulone D, Martorana V, San Biagio PL, (2005) Protofibril formation of amyloid beta-protein at low pH via a non-cooperative elongation mechanism. J Biol Chem 280: 30001-30008.
    • (2005) J Biol Chem , vol.280 , pp. 30001-30008
    • Carrotta, R.1    Manno, M.2    Bulone, D.3    Martorana, V.4    San Biagio, P.L.5
  • 38
    • 67650403403 scopus 로고    scopus 로고
    • Amyloid protofibrils of lysozyme nucleate and grow via oligomer fusion
    • Hill SE, Robinson J, Matthews G, Muschol M, (2009) Amyloid protofibrils of lysozyme nucleate and grow via oligomer fusion. Biophys J 96: 3781-3790.
    • (2009) Biophys J , vol.96 , pp. 3781-3790
    • Hill, S.E.1    Robinson, J.2    Matthews, G.3    Muschol, M.4
  • 39
    • 34250808419 scopus 로고    scopus 로고
    • Formation of amyloid fibrils via longitudinal growth of oligomers
    • Shahi P, Sharma R, Sanger S, Kumar I, Jolly RS, (2007) Formation of amyloid fibrils via longitudinal growth of oligomers. Biochemistry 46: 7365-7373.
    • (2007) Biochemistry , vol.46 , pp. 7365-7373
    • Shahi, P.1    Sharma, R.2    Sanger, S.3    Kumar, I.4    Jolly, R.S.5
  • 40
    • 12244255795 scopus 로고    scopus 로고
    • Polymerization of proteins into amyloid protofibrils shares common critical oligomeric states but differs in the mechanisms of their formation
    • Modler AJ, Fabian H, Sokolowski F, Lutsch G, Gast K, et al. (2004) Polymerization of proteins into amyloid protofibrils shares common critical oligomeric states but differs in the mechanisms of their formation. Amyloid 11: 215-231.
    • (2004) Amyloid , vol.11 , pp. 215-231
    • Modler, A.J.1    Fabian, H.2    Sokolowski, F.3    Lutsch, G.4    Gast, K.5
  • 41
    • 0037255361 scopus 로고    scopus 로고
    • Assembly of amyloid protofibrils via critical oligomers-a novel pathway of amyloid formation
    • Modler AJ, Gast K, Lutsch G, Damaschun G, (2003) Assembly of amyloid protofibrils via critical oligomers-a novel pathway of amyloid formation. J Mol Biol 325: 135-148.
    • (2003) J Mol Biol , vol.325 , pp. 135-148
    • Modler, A.J.1    Gast, K.2    Lutsch, G.3    Damaschun, G.4
  • 42
    • 33745039756 scopus 로고    scopus 로고
    • Characterization of the formation of amyloid protofibrils from barstar by mapping residue-specific fluorescence dynamics
    • Mukhopadhyay S, Nayak PK, Udgaonkar JB, Krishnamoorthy G, (2006) Characterization of the formation of amyloid protofibrils from barstar by mapping residue-specific fluorescence dynamics. J Mol Biol 358: 935-942.
    • (2006) J Mol Biol , vol.358 , pp. 935-942
    • Mukhopadhyay, S.1    Nayak, P.K.2    Udgaonkar, J.B.3    Krishnamoorthy, G.4
  • 43
    • 0035942986 scopus 로고    scopus 로고
    • Apolipoprotein E inhibits the depolymerization of beta 2-microglobulin-related amyloid fibrils at a neutral pH
    • Yamaguchi I, Hasegawa K, Takahashi N, Gejyo F, Naiki H, (2001) Apolipoprotein E inhibits the depolymerization of beta 2-microglobulin-related amyloid fibrils at a neutral pH. Biochemistry 40: 8499-8507.
    • (2001) Biochemistry , vol.40 , pp. 8499-8507
    • Yamaguchi, I.1    Hasegawa, K.2    Takahashi, N.3    Gejyo, F.4    Naiki, H.5
  • 44
    • 0030586945 scopus 로고    scopus 로고
    • Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous beta-sheet helix
    • Blake C, Serpell L, (1996) Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous beta-sheet helix. Structure 4: 989-998.
    • (1996) Structure , vol.4 , pp. 989-998
    • Blake, C.1    Serpell, L.2
  • 46
    • 0036295080 scopus 로고    scopus 로고
    • Transthyretin fibrillogenesis entails the assembly of monomers: a molecular model for in vitro assembled transthyretin amyloid-like fibrils
    • Cardoso I, Goldsbury CS, Muller SA, Olivieri V, Wirtz S, et al. (2002) Transthyretin fibrillogenesis entails the assembly of monomers: a molecular model for in vitro assembled transthyretin amyloid-like fibrils. J Mol Biol 317: 683-695.
    • (2002) J Mol Biol , vol.317 , pp. 683-695
    • Cardoso, I.1    Goldsbury, C.S.2    Muller, S.A.3    Olivieri, V.4    Wirtz, S.5
  • 47
    • 0030830019 scopus 로고    scopus 로고
    • Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid
    • Kelly JW, Colon W, Lai Z, Lashuel HA, McCulloch J, et al. (1997) Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid. Adv Protein Chem 50: 161-181.
    • (1997) Adv Protein Chem , vol.50 , pp. 161-181
    • Kelly, J.W.1    Colon, W.2    Lai, Z.3    Lashuel, H.A.4    McCulloch, J.5
  • 48
    • 63249103989 scopus 로고    scopus 로고
    • Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer
    • Kayed R, Pensalfini A, Margol L, Sokolov Y, Sarsoza F, et al. (2009) Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer. J Biol Chem 284: 4230-4237.
    • (2009) J Biol Chem , vol.284 , pp. 4230-4237
    • Kayed, R.1    Pensalfini, A.2    Margol, L.3    Sokolov, Y.4    Sarsoza, F.5
  • 49
    • 79959351077 scopus 로고    scopus 로고
    • Amyloid-{beta} Annular Protofibrils Evade Fibrillar Fate in Alzheimer Disease Brain
    • Lasagna-Reeves CA, Glabe CG, Kayed R, (2011) Amyloid-{beta} Annular Protofibrils Evade Fibrillar Fate in Alzheimer Disease Brain. J Biol Chem 286: 22122-22130.
    • (2011) J Biol Chem , vol.286 , pp. 22122-22130
    • Lasagna-Reeves, C.A.1    Glabe, C.G.2    Kayed, R.3
  • 50
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution
    • Stefani M, Dobson CM, (2003) Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J Mol Med (Berl) 81: 678-699.
    • (2003) J Mol Med (Berl) , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 51
    • 46749113483 scopus 로고    scopus 로고
    • Annular structures as intermediates in fibril formation of Alzheimer Abeta17-42
    • Zheng J, Jang H, Ma B, Nussinov R, (2008) Annular structures as intermediates in fibril formation of Alzheimer Abeta17-42. J Phys Chem B 112: 6856-6865.
    • (2008) J Phys Chem B , vol.112 , pp. 6856-6865
    • Zheng, J.1    Jang, H.2    Ma, B.3    Nussinov, R.4
  • 52
    • 2642544056 scopus 로고    scopus 로고
    • Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy
    • Zhu M, Han S, Zhou F, Carter SA, Fink AL, (2004) Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy. J Biol Chem 279: 24452-24459.
    • (2004) J Biol Chem , vol.279 , pp. 24452-24459
    • Zhu, M.1    Han, S.2    Zhou, F.3    Carter, S.A.4    Fink, A.L.5
  • 53
    • 0030885583 scopus 로고    scopus 로고
    • Thyroxine binding to transthyretin Met 119. Comparative studies of different heterozygotic carriers and structural analysis
    • Almeida MR, Damas AM, Lans MC, Brouwer A, Saraiva MJ, (1997) Thyroxine binding to transthyretin Met 119. Comparative studies of different heterozygotic carriers and structural analysis. Endocrine 6: 309-315.
    • (1997) Endocrine , vol.6 , pp. 309-315
    • Almeida, M.R.1    Damas, A.M.2    Lans, M.C.3    Brouwer, A.4    Saraiva, M.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.