-
1
-
-
0033849738
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
14
-
-
34247862247
-
A three-stage kinetic model of amyloid fibrillation
-
Lee C.-C., Nayak A., Sethuraman A., Belfort G., and McRae G.J. A three-stage kinetic model of amyloid fibrillation. Biophys. J. 92 (2007) 3448-3458
-
(2007)
Biophys. J.
, vol.92
, pp. 3448-3458
-
-
Lee, C.-C.1
Nayak, A.2
Sethuraman, A.3
Belfort, G.4
McRae, G.J.5
-
16
-
-
36749056299
-
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
-
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
-
18
-
-
0242668337
-
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
-
Kayed R., Head E., Thompson J.L., McIntire T.M., Milton S.C., Cotman C.W., and Glabe C.G. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300 (2003) 486-489
-
(2003)
Science
, vol.300
, 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
Glabe, C.G.7
-
19
-
-
0034657130
-
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
-
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
-
21
-
-
40649125572
-
Mechanisms of prion protein assembly into amyloid
-
Stöhr J., Weinmann N., Wille H., Kaimann T., Nagel-Steger L., Birkmann E., et al. Mechanisms of prion protein assembly into amyloid. Proc. Natl Acad. Sci. USA 105 (2008) 2409-2414
-
(2008)
Proc. Natl Acad. Sci. USA
, vol.105
, pp. 2409-2414
-
-
Stöhr, J.1
Weinmann, N.2
Wille, H.3
Kaimann, T.4
Nagel-Steger, L.5
Birkmann, E.6
-
22
-
-
34250834054
-
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
-
23
-
-
0033534397
-
Watching amyloid fibrils grow by time-lapse atomic force microscopy
-
Goldsbury C., Kistler J., Aebi U., Arvinte T., and Cooper G.J.S. Watching amyloid fibrils grow by time-lapse atomic force microscopy. J. Mol. Biol. 285 (1999) 33-39
-
(1999)
J. Mol. Biol.
, vol.285
, pp. 33-39
-
-
Goldsbury, C.1
Kistler, J.2
Aebi, U.3
Arvinte, T.4
Cooper, G.J.S.5
-
24
-
-
0033767765
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
35
-
-
0033616575
-
Designing conditions for in vitro formation of amyloid protofilaments and fibrils
-
Chiti F., Webster P., Taddei N., Clark A., Stefani M., Ramponi G., and Dobson C.M. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc. Natl Acad. Sci. USA 96 (1999) 3590-3594
-
(1999)
Proc. Natl Acad. Sci. USA
, vol.96
, pp. 3590-3594
-
-
Chiti, F.1
Webster, P.2
Taddei, N.3
Clark, A.4
Stefani, M.5
Ramponi, G.6
Dobson, C.M.7
-
36
-
-
0037262743
-
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
-
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
-
38
-
-
0037077234
-
Pathway complexity of prion protein assembly into amyloid
-
Baskakov I.V., Legname G., Baldwin M.A., Prusiner S.B., and Cohen F.E. Pathway complexity of prion protein assembly into amyloid. J. Biol. Chem. 277 (2002) 21140-21148
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 21140-21148
-
-
Baskakov, I.V.1
Legname, G.2
Baldwin, M.A.3
Prusiner, S.B.4
Cohen, F.E.5
-
39
-
-
0032725562
-
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
-
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
-
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
-
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
-
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
-
44
-
-
25144517646
-
Integrated modeling program, applied chemical theory (IMPACT)
-
Banks J.L., Beard H.S., Cao Y., Cho A.E., Damm W., Farid R., et al. Integrated modeling program, applied chemical theory (IMPACT). J. Comput. Chem. 26 (2005) 1752-1780
-
(2005)
J. Comput. Chem.
, vol.26
, pp. 1752-1780
-
-
Banks, J.L.1
Beard, H.S.2
Cao, Y.3
Cho, A.E.4
Damm, W.5
Farid, R.6
-
45
-
-
0039842514
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
56
-
-
0035150938
-
Structural and kinetic characterization of early folding events in β-lactoglobulin
-
Kuwata K., Shastry R., Cheng H., Hoshino M., Batt C.A., Goto Y., and Roder H. Structural and kinetic characterization of early folding events in β-lactoglobulin. Nat. Struct. Biol. 8 (2001) 151-155
-
(2001)
Nat. Struct. Biol.
, vol.8
, pp. 151-155
-
-
Kuwata, K.1
Shastry, R.2
Cheng, H.3
Hoshino, M.4
Batt, C.A.5
Goto, Y.6
Roder, H.7
-
57
-
-
0024121181
-
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
-
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
-
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
-
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
-
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
-
62
-
-
0035957228
-
Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates
-
Khurana R., Gillespie J.R., Talapatra A., Minert L.J., Ionescu-Zanetti C., Millett I., and Fink A.L. Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. Biochemistry 40 (2001) 3525-3535
-
(2001)
Biochemistry
, vol.40
, pp. 3525-3535
-
-
Khurana, R.1
Gillespie, J.R.2
Talapatra, A.3
Minert, L.J.4
Ionescu-Zanetti, C.5
Millett, I.6
Fink, A.L.7
-
63
-
-
22244456042
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
73
-
-
34248670403
-
Study on the binding of thioflavin T to β-sheet-rich and non-β-sheet cavities
-
Groenning M., Olsen L., van de Weert M., Flink J.M., Frokjaer S., and Jørgensen F.S. Study on the binding of thioflavin T to β-sheet-rich and non-β-sheet cavities. J. Struct. Biol. 158 (2007) 358-369
-
(2007)
J. Struct. Biol.
, vol.158
, pp. 358-369
-
-
Groenning, M.1
Olsen, L.2
van de Weert, M.3
Flink, J.M.4
Frokjaer, S.5
Jørgensen, F.S.6
-
74
-
-
37349050368
-
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
-
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
83
-
-
0003476369
-
-
Prentice-Hall, Inc., Englewood Cliffs, NJ
-
Lawson C.L., and Hanson R.J. Solving Least Squares Problems (1974), Prentice-Hall, Inc., Englewood Cliffs, NJ
-
(1974)
Solving Least Squares Problems
-
-
Lawson, C.L.1
Hanson, R.J.2
-
84
-
-
0020176542
-
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
|