메뉴 건너뛰기




Volumn 381, Issue 5, 2008, Pages 1332-1348

Erratum to "β-Lactoglobulin Assembles into Amyloid through Sequential Aggregated Intermediates" [J. Mol. Biol. 381 (2008) 1332-1348] (DOI:10.1016/j.jmb.2008.06.043);β-Lactoglobulin Assembles into Amyloid through Sequential Aggregated Intermediates

Author keywords

amyloid; dynamic light scattering; fluorescence; lipocalin; protein aggregation

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; AMYLOID; BETA LACTOGLOBULIN;

EID: 48749125392     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.11.014     Document Type: Erratum
Times cited : (57)

References (85)
  • 1
    • 0033849738 scopus 로고    scopus 로고
    • Review: history of the amyloid fibril
    • Sipe J.D., and Cohen A.S. Review: history of the amyloid fibril. J. Struct. Biol. 130 (2000) 88-98
    • (2000) J. Struct. Biol. , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 3
    • 0036052739 scopus 로고    scopus 로고
    • Ideas of order for amyloid fibril structure
    • Wetzel R. Ideas of order for amyloid fibril structure. Structure 10 (2002) 1031-1036
    • (2002) Structure , vol.10 , pp. 1031-1036
    • Wetzel, R.1
  • 4
    • 0036484536 scopus 로고    scopus 로고
    • Towards Alzheimer's disease vaccination
    • Solomon B. Towards Alzheimer's disease vaccination. Mini-Rev. Med. Chem. 2 (2002) 85-92
    • (2002) Mini-Rev. Med. Chem. , vol.2 , pp. 85-92
    • Solomon, B.1
  • 5
    • 0036708168 scopus 로고    scopus 로고
    • Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies
    • Kirkitadze M.D., Bitan G., and Teplow D.B. Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies. J. Neurosci. Res. 69 (2002) 567-577
    • (2002) J. Neurosci. Res. , vol.69 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 6
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J., and Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297 (2002) 353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 7
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., and Dobson C. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75 (2006) 333-366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.2
  • 8
    • 0032084472 scopus 로고    scopus 로고
    • Structural and kinetic features of amyloid β-protein fibrillogenesis
    • Teplow D.B. Structural and kinetic features of amyloid β-protein fibrillogenesis. Amyloid 5 (1998) 121-142
    • (1998) Amyloid , vol.5 , pp. 121-142
    • Teplow, D.B.1
  • 10
    • 0033849811 scopus 로고    scopus 로고
    • Probing the kinetics of β-amyloid self-association
    • Murphy R.M., and Pallitto M.M. Probing the kinetics of β-amyloid self-association. J. Struct. Biol. 130 (2000) 109-122
    • (2000) J. Struct. Biol. , vol.130 , pp. 109-122
    • Murphy, R.M.1    Pallitto, M.M.2
  • 11
    • 0036377156 scopus 로고    scopus 로고
    • Amyloid-fibril formation. Proposed mechanisms and relevance to conformational disease
    • Zerovnik E. Amyloid-fibril formation. Proposed mechanisms and relevance to conformational disease. Eur. J. Biochem. 269 (2002) 3362-3371
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3362-3371
    • Zerovnik, E.1
  • 12
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism
    • Nielsen L., Khurana R., Coats A., Frokjaer S., Brange J., and Vyas S. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 40 (2001) 6036-6046
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5    Vyas, S.6
  • 13
    • 0036784667 scopus 로고    scopus 로고
    • A kinetic study of β-lactoglobulin amyloid fibril formation promoted by urea
    • Hamada D., and Dobson C.M. A kinetic study of β-lactoglobulin amyloid fibril formation promoted by urea. Protein Sci. 11 (2002) 2417-2426
    • (2002) Protein Sci. , vol.11 , pp. 2417-2426
    • Hamada, D.1    Dobson, C.M.2
  • 16
    • 36749056299 scopus 로고    scopus 로고
    • A polymer physics perspective on driving forces and mechanisms for protein aggregation
    • Pappu R.V., Wang X., Vitalis A., and Crick S.L. A polymer physics perspective on driving forces and mechanisms for protein aggregation. Arch. Biochem. Biophys. 469 (2008) 132-141
    • (2008) Arch. Biochem. Biophys. , vol.469 , pp. 132-141
    • Pappu, R.V.1    Wang, X.2    Vitalis, A.3    Crick, S.L.4
  • 17
    • 0034875603 scopus 로고    scopus 로고
    • A mathematical model of the kinetics of β-amyloid fibril growth from the denatured state
    • Pallitto M.M., and Murphy R.M. A mathematical model of the kinetics of β-amyloid fibril growth from the denatured state. Biophys. J. 81 (2001) 1805-1822
    • (2001) Biophys. J. , vol.81 , pp. 1805-1822
    • Pallitto, M.M.1    Murphy, R.M.2
  • 19
    • 0034657130 scopus 로고    scopus 로고
    • Evidence for seeding of β-amyloid by intracerebral infusion of Alzheimer brain extracts in β-amyloid precursor protein-transgenic mice
    • Kane M.D., Lipinski W.J., Callahan M.J., Bian F., Durham R.A., Schwarz R.D., et al. Evidence for seeding of β-amyloid by intracerebral infusion of Alzheimer brain extracts in β-amyloid precursor protein-transgenic mice. J. Neurosci. 20 (2000) 3606-3611
    • (2000) J. Neurosci. , vol.20 , pp. 3606-3611
    • Kane, M.D.1    Lipinski, W.J.2    Callahan, M.J.3    Bian, F.4    Durham, R.A.5    Schwarz, R.D.6
  • 20
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper J.D., and Lansbury Jr. P.T. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 66 (1997) 385-407
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 22
    • 34250834054 scopus 로고    scopus 로고
    • A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. Aggregation with pre-equilibrated unfolding
    • Andrews J.M., and Roberts C.J. A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. Aggregation with pre-equilibrated unfolding. J. Phys. Chem. B 111 (2007) 7897-7913
    • (2007) J. Phys. Chem. B , vol.111 , pp. 7897-7913
    • Andrews, J.M.1    Roberts, C.J.2
  • 24
    • 0033767765 scopus 로고    scopus 로고
    • Monitoring biomolecular interactions by time-lapse atomic force microscopy
    • Stolz M., Stoffler D., Aebi U., and Goldsbury C. Monitoring biomolecular interactions by time-lapse atomic force microscopy. J. Struct. Biol. 131 (2000) 171-180
    • (2000) J. Struct. Biol. , vol.131 , pp. 171-180
    • Stolz, M.1    Stoffler, D.2    Aebi, U.3    Goldsbury, C.4
  • 25
    • 0037126101 scopus 로고    scopus 로고
    • Novel amyloid fibrillar networks derived from a globular protein: β-lactoglobulin
    • Gosal W.S., Clark A.H., Pudney P.D.A., and Ross-Murphy S.B. Novel amyloid fibrillar networks derived from a globular protein: β-lactoglobulin. Langmuir 18 (2002) 7174-7181
    • (2002) Langmuir , vol.18 , pp. 7174-7181
    • Gosal, W.S.1    Clark, A.H.2    Pudney, P.D.A.3    Ross-Murphy, S.B.4
  • 26
    • 0035997230 scopus 로고    scopus 로고
    • Imaging real-time aggregation of amyloid β protein (1-42) by atomic force microscopy
    • Parbhu A., Lin H., Thimm J., and Lal R. Imaging real-time aggregation of amyloid β protein (1-42) by atomic force microscopy. Peptides 23 (2002) 1265-1270
    • (2002) Peptides , vol.23 , pp. 1265-1270
    • Parbhu, A.1    Lin, H.2    Thimm, J.3    Lal, R.4
  • 28
    • 0345393292 scopus 로고    scopus 로고
    • Two-state folding kinetics of small proteins in the sequential collapse model: dependence of the folding rate on contact order and temperature
    • Bergasa-Caceres F., and Rabitz H.A. Two-state folding kinetics of small proteins in the sequential collapse model: dependence of the folding rate on contact order and temperature. J. Phys. Chem. B 107 (2003) 12874-12877
    • (2003) J. Phys. Chem. B , vol.107 , pp. 12874-12877
    • Bergasa-Caceres, F.1    Rabitz, H.A.2
  • 29
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science 216 (1982) 136-144
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 30
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith J.S. Self-replication and scrapie. Nature 215 (1967) 1043-1044
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 31
    • 0036780877 scopus 로고    scopus 로고
    • Opinion: amyloid-β immunotherapy for Alzheimer's disease: the end of the beginning
    • Schenk D. Opinion: amyloid-β immunotherapy for Alzheimer's disease: the end of the beginning. Nat. Rev. Neurosci. 3 (2002) 824-828
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 824-828
    • Schenk, D.1
  • 32
    • 0038650572 scopus 로고    scopus 로고
    • Conformational polymorphism of the amyloidogenic peptide homologous to residues 113-127 of the prion protein
    • Satheeshkumar K.S., and Jayakumar R. Conformational polymorphism of the amyloidogenic peptide homologous to residues 113-127 of the prion protein. Biophys. J. 85 (2003) 473-483
    • (2003) Biophys. J. , vol.85 , pp. 473-483
    • Satheeshkumar, K.S.1    Jayakumar, R.2
  • 33
    • 0033777523 scopus 로고    scopus 로고
    • Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
    • Bouchard M., Zurdo J., Nettleton E.J., Dobson C.M., and Robinson C.V. Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Sci. 9 (2000) 1960-1967
    • (2000) Protein Sci. , vol.9 , pp. 1960-1967
    • Bouchard, M.1    Zurdo, J.2    Nettleton, E.J.3    Dobson, C.M.4    Robinson, C.V.5
  • 34
    • 0028804827 scopus 로고
    • Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide
    • Lansbury J., Peter T., Costa P.R., Griffiths J.M., Simon E.J., Auger M., et al. Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide. Nat. Struct. Biol. 2 (1995) 990-998
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 990-998
    • Lansbury, J.1    Peter, T.2    Costa, P.R.3    Griffiths, J.M.4    Simon, E.J.5    Auger, M.6
  • 36
    • 0037262743 scopus 로고    scopus 로고
    • Novel observation of a circular dichroism band originating from amyloid fibril
    • Abe H., and Nakanishi H. Novel observation of a circular dichroism band originating from amyloid fibril. Anal. Sci. 19 (2003) 171-173
    • (2003) Anal. Sci. , vol.19 , pp. 171-173
    • Abe, H.1    Nakanishi, H.2
  • 37
    • 0034967751 scopus 로고    scopus 로고
    • Conformational characterization of oligomeric intermediates and aggregates in β-lactoglobulin heat aggregation
    • Carrotta R., Bauer R., Waninge R., and Rischel C. Conformational characterization of oligomeric intermediates and aggregates in β-lactoglobulin heat aggregation. Protein Sci. 10 (2001) 1312-1318
    • (2001) Protein Sci. , vol.10 , pp. 1312-1318
    • Carrotta, R.1    Bauer, R.2    Waninge, R.3    Rischel, C.4
  • 39
    • 0032725562 scopus 로고    scopus 로고
    • The tetrameric protein transthyretin dissociates to a non-native monomer in solution. A novel model for amyloidogenesis
    • Quintas A., Saraiva M.J., and Brito R.M. The tetrameric protein transthyretin dissociates to a non-native monomer in solution. A novel model for amyloidogenesis. J. Biol. Chem. 274 (1999) 32943-32949
    • (1999) J. Biol. Chem. , vol.274 , pp. 32943-32949
    • Quintas, A.1    Saraiva, M.J.2    Brito, R.M.3
  • 40
    • 0028120343 scopus 로고
    • Scrapie amyloid (prion) protein has the conformational characteristics of an aggregated molten globule folding intermediate
    • Safar J., Roller P.P., Gajdusek D.C., and Gibbs Jr. C.J. Scrapie amyloid (prion) protein has the conformational characteristics of an aggregated molten globule folding intermediate. Biochemistry 33 (1994) 8375-8383
    • (1994) Biochemistry , vol.33 , pp. 8375-8383
    • Safar, J.1    Roller, P.P.2    Gajdusek, D.C.3    Gibbs Jr., C.J.4
  • 41
    • 0038043276 scopus 로고    scopus 로고
    • Amyloid-like fibril formation in an all β-barrel protein. Partially structured intermediate state(s) is a precursor for fibril formation
    • Srisailam S., Kumar T.K., Rajalingam D., Kathir K.M., Sheu H.-S., Jan F.-J., et al. Amyloid-like fibril formation in an all β-barrel protein. Partially structured intermediate state(s) is a precursor for fibril formation. J. Biol. Chem. 278 (2003) 17701-17709
    • (2003) J. Biol. Chem. , vol.278 , pp. 17701-17709
    • Srisailam, S.1    Kumar, T.K.2    Rajalingam, D.3    Kathir, K.M.4    Sheu, H.-S.5    Jan, F.-J.6
  • 42
    • 0035745653 scopus 로고    scopus 로고
    • Alzheimer β-amyloid peptides: structures of amyloid fibrils and alternate aggregation products
    • Gorman P.M., and Chakrabartty A. Alzheimer β-amyloid peptides: structures of amyloid fibrils and alternate aggregation products. Biopolymers 60 (2001) 381-394
    • (2001) Biopolymers , vol.60 , pp. 381-394
    • Gorman, P.M.1    Chakrabartty, A.2
  • 43
    • 0034680781 scopus 로고    scopus 로고
    • Alternate aggregation pathways of the Alzheimer β-amyloid peptide. An in vitro model of preamyloid
    • Huang T.H.J., Yang D.-S., Fraser P.E., and Chakrabartty A. Alternate aggregation pathways of the Alzheimer β-amyloid peptide. An in vitro model of preamyloid. J. Biol. Chem. 275 (2000) 36436-36440
    • (2000) J. Biol. Chem. , vol.275 , pp. 36436-36440
    • Huang, T.H.J.1    Yang, D.-S.2    Fraser, P.E.3    Chakrabartty, A.4
  • 45
    • 0039842514 scopus 로고    scopus 로고
    • Structural changes accompanying pH-induced dissociation of the β-lactoglobulin dimer
    • Uhrinova S., Smith M.H., Jameson G.B., Uhrin D., Sawyer L., and Barlow P.N. Structural changes accompanying pH-induced dissociation of the β-lactoglobulin dimer. Biochemistry 39 (2000) 3565-3574
    • (2000) Biochemistry , vol.39 , pp. 3565-3574
    • Uhrinova, S.1    Smith, M.H.2    Jameson, G.B.3    Uhrin, D.4    Sawyer, L.5    Barlow, P.N.6
  • 46
    • 0034684161 scopus 로고    scopus 로고
    • The core lipocalin, bovine β-lactoglobulin
    • Sawyer L., and Kontopidis G. The core lipocalin, bovine β-lactoglobulin. Biochim. Biophys. Acta 1482 (2000) 136-148
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 136-148
    • Sawyer, L.1    Kontopidis, G.2
  • 47
    • 1242310516 scopus 로고    scopus 로고
    • Mesoscopic properties of semiflexible amyloid fibrils
    • Sagis L.M.C., Veerman C., and Van der Linden E. Mesoscopic properties of semiflexible amyloid fibrils. Langmuir 20 (2004) 924-927
    • (2004) Langmuir , vol.20 , pp. 924-927
    • Sagis, L.M.C.1    Veerman, C.2    Van der Linden, E.3
  • 48
    • 0032444658 scopus 로고    scopus 로고
    • Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins
    • Buck M. Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins. Q. Rev. Biophys. 31 (1998) 297-355
    • (1998) Q. Rev. Biophys. , vol.31 , pp. 297-355
    • Buck, M.1
  • 49
    • 0034687651 scopus 로고    scopus 로고
    • What is the role of non-native intermediates of β-lactoglobulin in protein folding?
    • Chikenji G., and Kikuchi M. What is the role of non-native intermediates of β-lactoglobulin in protein folding?. Proc. Natl Acad. Sci. USA 97 (2000) 14273-14277
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 14273-14277
    • Chikenji, G.1    Kikuchi, M.2
  • 50
    • 0034598947 scopus 로고    scopus 로고
    • Is folding of β-lactoglobulin non-hierarchic? Intermediate with native-like β-sheet and non-native α-helix
    • Forge V., Hoshino M., Kuwata K., Arai M., Kuwajima K., Batt C.A., and Goto Y. Is folding of β-lactoglobulin non-hierarchic? Intermediate with native-like β-sheet and non-native α-helix. J. Mol. Biol. 296 (2000) 1039-1051
    • (2000) J. Mol. Biol. , vol.296 , pp. 1039-1051
    • Forge, V.1    Hoshino, M.2    Kuwata, K.3    Arai, M.4    Kuwajima, K.5    Batt, C.A.6    Goto, Y.7
  • 51
    • 0031580203 scopus 로고    scopus 로고
    • The equilibrium intermediate of β-lactoglobulin with non-native α-helical structure
    • Hamada D., and Goto Y. The equilibrium intermediate of β-lactoglobulin with non-native α-helical structure. J. Mol. Biol. 269 (1997) 479-487
    • (1997) J. Mol. Biol. , vol.269 , pp. 479-487
    • Hamada, D.1    Goto, Y.2
  • 52
    • 0029740071 scopus 로고    scopus 로고
    • Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein
    • Hamada D., Segawa S.-I., and Goto Y. Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. Nat. Struct. Biol. 3 (1996) 868-873
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 868-873
    • Hamada, D.1    Segawa, S.-I.2    Goto, Y.3
  • 53
    • 0032491317 scopus 로고    scopus 로고
    • α → β transition of β-lactoglobulin as evidenced by heteronuclear NMR
    • Kuwata K., Hoshino M., Era S., Batt C.A., and Goto Y. α → β transition of β-lactoglobulin as evidenced by heteronuclear NMR. J. Mol. Biol. 283 (1998) 731-739
    • (1998) J. Mol. Biol. , vol.283 , pp. 731-739
    • Kuwata, K.1    Hoshino, M.2    Era, S.3    Batt, C.A.4    Goto, Y.5
  • 54
    • 0037451973 scopus 로고    scopus 로고
    • Sequential collapse folding pathway of β-lactoglobulin: parallel pathways and non-native secondary structure
    • Bergasa-Caceres F., and Rabitz H.A. Sequential collapse folding pathway of β-lactoglobulin: parallel pathways and non-native secondary structure. J. Phys. Chem. B 107 (2003) 3606-3612
    • (2003) J. Phys. Chem. B , vol.107 , pp. 3606-3612
    • Bergasa-Caceres, F.1    Rabitz, H.A.2
  • 55
    • 0030582679 scopus 로고    scopus 로고
    • The burst-phase intermediate in the refolding of β-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy
    • Kuwajima K., Yamaya H., and Sugai S. The burst-phase intermediate in the refolding of β-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy. J. Mol. Biol. 264 (1996) 806-822
    • (1996) J. Mol. Biol. , vol.264 , pp. 806-822
    • Kuwajima, K.1    Yamaya, H.2    Sugai, S.3
  • 57
    • 0024121181 scopus 로고
    • Structural stability of β-lactoglobulin in the presence of kosmotropic salts. A kinetic and thermodynamic study
    • Kella N.K., and Kinsella J.E. Structural stability of β-lactoglobulin in the presence of kosmotropic salts. A kinetic and thermodynamic study. Int. J. Pept. Protein Res. 32 (1988) 396-405
    • (1988) Int. J. Pept. Protein Res. , vol.32 , pp. 396-405
    • Kella, N.K.1    Kinsella, J.E.2
  • 58
    • 0028989022 scopus 로고
    • Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine β-lactoglobulin?
    • Creamer L.K. Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine β-lactoglobulin?. Biochemistry 34 (1995) 7170-7176
    • (1995) Biochemistry , vol.34 , pp. 7170-7176
    • Creamer, L.K.1
  • 59
    • 0038392577 scopus 로고    scopus 로고
    • Trehalose influence on β-lactoglobulin stability and hydration by time resolved fluorescence
    • D'Alfonso L., Collini M., and Baldini G. Trehalose influence on β-lactoglobulin stability and hydration by time resolved fluorescence. Eur. J. Biochem. 270 (2003) 2497-2504
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2497-2504
    • D'Alfonso, L.1    Collini, M.2    Baldini, G.3
  • 60
    • 33750690645 scopus 로고    scopus 로고
    • Photophysics of ANS v. decay modes of ANS in proteins: the IFABP-ANS complex
    • Kirk W., Kurian E., and Wessels W. Photophysics of ANS v. decay modes of ANS in proteins: the IFABP-ANS complex. Biophys. Chem. 125 (2007) 50-58
    • (2007) Biophys. Chem. , vol.125 , pp. 50-58
    • Kirk, W.1    Kurian, E.2    Wessels, W.3
  • 61
    • 36248995759 scopus 로고    scopus 로고
    • Characterization of fluorescence of ANS-tear lipocalin complex: evidence for multiple-binding modes
    • Gasymov O.K., Abduragimov A.R., and Glasgow B.J. Characterization of fluorescence of ANS-tear lipocalin complex: evidence for multiple-binding modes. Photochem. Photobiol. 83 (2007) 1405-1414
    • (2007) Photochem. Photobiol. , vol.83 , pp. 1405-1414
    • Gasymov, O.K.1    Abduragimov, A.R.2    Glasgow, B.J.3
  • 63
    • 22244456042 scopus 로고    scopus 로고
    • Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy
    • Lindgren M., Sorgjerd K., and Hammarstromy P. Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy. Biophys. J. 88 (2005) 4200-4212
    • (2005) Biophys. J. , vol.88 , pp. 4200-4212
    • Lindgren, M.1    Sorgjerd, K.2    Hammarstromy, P.3
  • 64
    • 41049087084 scopus 로고    scopus 로고
    • Global fitting without a global model: regularization based on the continuity of the evolution of parameter distributions
    • (1-18)
    • Giurleo J.T., and Talaga D.S. Global fitting without a global model: regularization based on the continuity of the evolution of parameter distributions. J. Chem. Phys. 128 (2008) 114114 (1-18)
    • (2008) J. Chem. Phys. , vol.128 , pp. 114114
    • Giurleo, J.T.1    Talaga, D.S.2
  • 65
    • 0032830123 scopus 로고    scopus 로고
    • Monitoring protein assembly using quasielastic light scattering spectroscopy
    • Lomakin A., Benedek G.B., and Teplow D.B. Monitoring protein assembly using quasielastic light scattering spectroscopy. Methods Enzymol. 309 (1999) 429-459
    • (1999) Methods Enzymol. , vol.309 , pp. 429-459
    • Lomakin, A.1    Benedek, G.B.2    Teplow, D.B.3
  • 66
    • 0037255361 scopus 로고    scopus 로고
    • Assembly of amyloid protofibrils via critical oligomers-a novel pathway of amyloid formation
    • Modler A.J., Gast K., Lutsch G., and Damaschun G. Assembly of amyloid protofibrils via critical oligomers-a novel pathway of amyloid formation. J. Mol. Biol. 325 (2003) 135-148
    • (2003) J. Mol. Biol. , vol.325 , pp. 135-148
    • Modler, A.J.1    Gast, K.2    Lutsch, G.3    Damaschun, G.4
  • 67
    • 0021721833 scopus 로고
    • Fluorescent thiazole stains for amyloid without differentiation
    • Waldrop F.S., Puchtler H., and Meloan S.N. Fluorescent thiazole stains for amyloid without differentiation. J. Histotechnol. 7 (1984) 123-126
    • (1984) J. Histotechnol. , vol.7 , pp. 123-126
    • Waldrop, F.S.1    Puchtler, H.2    Meloan, S.N.3
  • 68
    • 0009874643 scopus 로고
    • Spectroscopic study of Congo red and thioflavin binding to amyloid-like proteins
    • Elhaddaoui A., Delacourte A., and Turrell S. Spectroscopic study of Congo red and thioflavin binding to amyloid-like proteins. J. Mol. Struct. 294 (1993) 115-118
    • (1993) J. Mol. Struct. , vol.294 , pp. 115-118
    • Elhaddaoui, A.1    Delacourte, A.2    Turrell, S.3
  • 69
    • 0001733723 scopus 로고
    • Thioflavine T interaction with amyloid β-sheet structures
    • LeVine H. Thioflavine T interaction with amyloid β-sheet structures. Amyloid 2 (1995) 1-6
    • (1995) Amyloid , vol.2 , pp. 1-6
    • LeVine, H.1
  • 70
    • 0037592927 scopus 로고    scopus 로고
    • Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence
    • Ban T., Hamada D., Hasegawa K., Naiki H., and Goto Y. Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence. J. Biol. Chem. 278 (2003) 16462-16465
    • (2003) J. Biol. Chem. , vol.278 , pp. 16462-16465
    • Ban, T.1    Hamada, D.2    Hasegawa, K.3    Naiki, H.4    Goto, Y.5
  • 71
    • 0000225472 scopus 로고
    • Dye aggregation in freezing aqueous solutions
    • Schirra R. Dye aggregation in freezing aqueous solutions. Chem. Phys. Lett. 119 (1985) 463-466
    • (1985) Chem. Phys. Lett. , vol.119 , pp. 463-466
    • Schirra, R.1
  • 72
    • 0031577239 scopus 로고    scopus 로고
    • γ-Cyclodextrin induced intermolecular excimer formation of thioflavin T
    • Retna Raj R.R.C. γ-Cyclodextrin induced intermolecular excimer formation of thioflavin T. Chem. Phys. Lett. 273 (1997) 285-290
    • (1997) Chem. Phys. Lett. , vol.273 , pp. 285-290
    • Retna Raj, R.R.C.1
  • 74
    • 37349050368 scopus 로고    scopus 로고
    • Nonnative protein polymers: structure, morphology, and relation to nucleation and growth
    • Weiss W.F., Hodgdon T.K., Kaler E.W., Lenhoff A.M., and Roberts C.J. Nonnative protein polymers: structure, morphology, and relation to nucleation and growth. Biophys. J. 93 (2007) 4392-4403
    • (2007) Biophys. J. , vol.93 , pp. 4392-4403
    • Weiss, W.F.1    Hodgdon, T.K.2    Kaler, E.W.3    Lenhoff, A.M.4    Roberts, C.J.5
  • 75
    • 49949092086 scopus 로고    scopus 로고
    • Gaczynska, M. & Osmulski, P. A. AFM of biological complexes: what can we learn? Curr. Opin. Colloid Interface Sci. In press. doi:10.1016/j.cocis.2008.01.004.
    • Gaczynska, M. & Osmulski, P. A. AFM of biological complexes: what can we learn? Curr. Opin. Colloid Interface Sci. In press. doi:10.1016/j.cocis.2008.01.004.
  • 76
    • 0037039276 scopus 로고    scopus 로고
    • Does β-lactoglobulin denaturation occur via an intermediate state?
    • D'Alfonso L., Collini M., and Baldini G. Does β-lactoglobulin denaturation occur via an intermediate state?. Biochemistry 41 (2002) 326-333
    • (2002) Biochemistry , vol.41 , pp. 326-333
    • D'Alfonso, L.1    Collini, M.2    Baldini, G.3
  • 77
    • 36849126497 scopus 로고
    • Relationship between absorption intensity and fluorescence lifetime of molecules
    • Strickler S.J., and Berg R.A. Relationship between absorption intensity and fluorescence lifetime of molecules. J. Chem. Phys. 37 (1962) 814-822
    • (1962) J. Chem. Phys. , vol.37 , pp. 814-822
    • Strickler, S.J.1    Berg, R.A.2
  • 78
    • 0030867610 scopus 로고    scopus 로고
    • Ligand binding to proteins: the binding landscape model
    • Miller D.W., and Dill K.A. Ligand binding to proteins: the binding landscape model. Protein Sci. 6 (1997) 2166-2179
    • (1997) Protein Sci. , vol.6 , pp. 2166-2179
    • Miller, D.W.1    Dill, K.A.2
  • 79
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24 (1999) 329-332
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 80
    • 33750934185 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions
    • Crick S.L., Jayaraman M., Frieden C., Wetzel R., and Pappu R.V. Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions. Proc. Natl Acad. Sci. USA 103 (2006) 16764-16769
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 16764-16769
    • Crick, S.L.1    Jayaraman, M.2    Frieden, C.3    Wetzel, R.4    Pappu, R.V.5
  • 81
    • 34548757409 scopus 로고    scopus 로고
    • Quantitative characterization of intrinsic disorder in polyglutamine: insights from analysis based on polymer theories
    • Vitalis A., Wang X., and Pappu R.V. Quantitative characterization of intrinsic disorder in polyglutamine: insights from analysis based on polymer theories. Biophys. J. 93 (2007) 1923-1937
    • (2007) Biophys. J. , vol.93 , pp. 1923-1937
    • Vitalis, A.1    Wang, X.2    Pappu, R.V.3
  • 82
    • 33748612966 scopus 로고    scopus 로고
    • Hidden Markov model analysis of multichromophore photobleaching
    • Messina T.C., Kim H., Giurleo J.T., and Talaga D.S. Hidden Markov model analysis of multichromophore photobleaching. J. Phys. Chem. B 110 (2006) 16366-16376
    • (2006) J. Phys. Chem. B , vol.110 , pp. 16366-16376
    • Messina, T.C.1    Kim, H.2    Giurleo, J.T.3    Talaga, D.S.4
  • 84
    • 0020176542 scopus 로고
    • A constrained regularization method for inverting data represented by linear algebraic or integral equations
    • Provencher S.W. A constrained regularization method for inverting data represented by linear algebraic or integral equations. Comput. Phys. Commun. 27 (1982) 213-227
    • (1982) Comput. Phys. Commun. , vol.27 , pp. 213-227
    • Provencher, S.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.