-
2
-
-
27644456601
-
Neuropathology of dementia in Parkinson's disease: A prospective, community-based study
-
Aarsland D, Perry R, Brown A, Larsen JP, Ballard C. Neuropathology of dementia in Parkinson's disease: a prospective, community-based study. Ann. Neurol. 2005; 58: 773-776.
-
(2005)
Ann. Neurol
, vol.58
, pp. 773-776
-
-
Aarsland, D.1
Perry, R.2
Brown, A.3
Larsen, J.P.4
Ballard, C.5
-
4
-
-
0029981197
-
Alternative conformations of amyloidogenic proteins govern their behavior
-
Kelly JW. Alternative conformations of amyloidogenic proteins govern their behavior. Curr. Opin. Struct. Biol. 1996; 6: 11-17.
-
(1996)
Curr. Opin. Struct. Biol
, vol.6
, pp. 11-17
-
-
Kelly, J.W.1
-
5
-
-
0032006678
-
The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
-
Kelly JW. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 1998; 8: 101-106.
-
(1998)
Curr. Opin. Struct. Biol
, vol.8
, pp. 101-106
-
-
Kelly, J.W.1
-
6
-
-
0347357617
-
Protein folding and misfolding
-
Dobson CM. Protein folding and misfolding. Nature 2003;426: 884-890.
-
(2003)
Nature
, vol.426
, pp. 884-890
-
-
Dobson, C.M.1
-
8
-
-
57749098600
-
Amyloid formation by globular proteins under native conditions
-
Chiti F, Dobson CM. Amyloid formation by globular proteins under native conditions. Nat. Chem. Biol. 2009; 5: 15-22.
-
(2009)
Nat. Chem. Biol
, vol.5
, pp. 15-22
-
-
Chiti, F.1
Dobson, C.M.2
-
9
-
-
77951759131
-
Lysozymes in the animal kingdom
-
Callewaert L, Michiels CW. Lysozymes in the animal kingdom. J. Biosci. 2010; 35: 127-160.
-
(2010)
J. Biosci
, vol.35
, pp. 127-160
-
-
Callewaert, L.1
Michiels, C.W.2
-
10
-
-
84900908190
-
Lysozyme
-
In: Huopalahti R, Lopez-Fandino R, Anton M, Schade R, eds., Berlin Heiderberg: Springer-Verlag
-
Lesnierowsli G, Kjowski J. Lysozyme. In: Huopalahti R, Lopez-Fandino R, Anton M, Schade R, eds. Bioactive Egg Compounds. Berlin Heiderberg: Springer-Verlag. 2007: 34-42.
-
(2007)
Bioactive Egg Compounds
, pp. 34-42
-
-
Lesnierowsli, G.1
Kjowski, J.2
-
11
-
-
33846562360
-
Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion
-
Mishra R, Sorgjerd K, Nystrom S, Nordigarden A, Yu YC, Hammarstrom P. Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion. J. Mol. Biol. 2007; 399: 1029-1044.
-
(2007)
J. Mol. Biol
, vol.399
, pp. 1029-1044
-
-
Mishra, R.1
Sorgjerd, K.2
Nystrom, S.3
Nordigarden, A.4
Yu, Y.C.5
Hammarstrom, P.6
-
12
-
-
0033849915
-
Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants
-
Morozova-Roche LA, Zurdo J, Spencer A, Noppe W, Receveur V, Archer DB, Joniau M, Dobson CM. Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants. J Struct Biol. 2000; 130: 339-3351.
-
(2000)
J Struct Biol
, vol.130
, pp. 339-3351
-
-
Morozova-Roche, L.A.1
Zurdo, J.2
Spencer, A.3
Noppe, W.4
Receveur, V.5
Archer, D.B.6
Joniau, M.7
Dobson, C.M.8
-
13
-
-
0034005357
-
Amyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution
-
Goda S, Takano K, Yamagata Y, Nagata R, Akutsu H, Maki S, Namba K, Yutani K. Amyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution. Protein Sci. 2000; 9: 369-375.
-
(2000)
Protein Sci
, vol.9
, pp. 369-375
-
-
Goda, S.1
Takano, K.2
Yamagata, Y.3
Nagata, R.4
Akutsu, H.5
Maki, S.6
Namba, K.7
Yutani, K.8
-
14
-
-
1642452936
-
Formation of amyloid fibrils from fully reduced hen egg white lysozyme
-
Cao A, Hu D, Lai L. Formation of amyloid fibrils from fully reduced hen egg white lysozyme. Protein Sci. 2004; 13: 319-324.
-
(2004)
Protein Sci
, vol.13
, pp. 319-324
-
-
Cao, A.1
Hu, D.2
Lai, L.3
-
15
-
-
80051903352
-
Lysozyme: A model protein for amyloid research
-
Swaminathan R, Ravi VK, Kumar S, Kumar MV, Chandra N. Lysozyme: a model protein for amyloid research. Adv. Protein Chem. Struct. Biol. 2011; 84: 63-111.
-
(2011)
Adv. Protein Chem. Struct. Biol
, vol.84
, pp. 63-111
-
-
Swaminathan, R.1
Ravi, V.K.2
Kumar, S.3
Kumar, M.V.4
Chandra, N.5
-
16
-
-
34247579524
-
The first step of hen egg white lysozyme fibrillation, irreversible partial unfolding, is a two-state transition
-
Xu M, Shashilov VA, Ermolenkov VV, Fredriksen L, Zagorevski D, Lednev IK. The first step of hen egg white lysozyme fibrillation, irreversible partial unfolding, is a two-state transition. Protein Sci. 2007; 16: 815-832.
-
(2007)
Protein Sci
, vol.16
, pp. 815-832
-
-
Xu, M.1
Shashilov, V.A.2
Ermolenkov, V.V.3
Fredriksen, L.4
Zagorevski, D.5
Lednev, I.K.6
-
17
-
-
3042673992
-
A highly amyloidogenic region of hen lysozyme
-
Frare E, Polverino De Laureto P, Zurdo J, Dobson CM, Fontana A. A highly amyloidogenic region of hen lysozyme. J. Mol. Biol. 2004; 340: 1153-1165.
-
(2004)
J. Mol. Biol
, vol.340
, pp. 1153-1165
-
-
Frare, E.1
De Polverino, L.P.2
Zurdo, J.3
Dobson, C.M.4
Fontana, A.5
-
18
-
-
84861149876
-
Changes in Lysozyme Flexibility upon Mutation Are Frequent, Large and Long-Ranged
-
Verma D, Jacobs DJ, Livesay DR. Changes in Lysozyme Flexibility upon Mutation Are Frequent, Large and Long-Ranged. PLoS Comput Biol. 2012; 8: 1-18.
-
(2012)
PLoS Comput Biol
, vol.8
, pp. 1-18
-
-
Verma, D.1
Jacobs, D.J.2
Livesay, D.R.3
-
19
-
-
84857339663
-
Aggregates with lysozyme and ovalbumin show features of amyloid-like fibrils
-
Sugimoto Y, Kamada Y, Tokunaga Y, Shinohara H, Matsumoto M, Kusakabe T, Ohkuri T, Ueda T. Aggregates with lysozyme and ovalbumin show features of amyloid-like fibrils. Biochem Cell Biol. 2011; 89: 533-544.
-
(2011)
Biochem Cell Biol
, vol.89
, pp. 533-544
-
-
Sugimoto, Y.1
Kamada, Y.2
Tokunaga, Y.3
Shinohara, H.4
Matsumoto, M.5
Kusakabe, T.6
Ohkuri, T.7
Ueda, T.8
-
20
-
-
8844259690
-
Modulation of compactness and long-range interactions of unfolded lysozyme by single point mutations
-
Wirmer J, Schlorb C, Klein-Seetharaman J, Hirano R, Ueda T, Imoto T, Schwalbe H. Modulation of compactness and long-range interactions of unfolded lysozyme by single point mutations. Angew. Chem. Int. Ed. Engl. 2004; 43: 5780-5785.
-
(2004)
Angew. Chem. Int. Ed. Engl
, vol.43
, pp. 5780-5785
-
-
Wirmer, J.1
Schlorb, C.2
Klein-Seetharaman, J.3
Hirano, R.4
Ueda, T.5
Imoto, T.6
Schwalbe, H.7
-
21
-
-
14144254725
-
Effect of the structure of the denatured state of lysozyme on the aggregation reaction at the early stages of folding from the reduced form
-
Ohkuri T, Shioi S, Imoto T, Ueda T. Effect of the structure of the denatured state of lysozyme on the aggregation reaction at the early stages of folding from the reduced form. J. Mol. Biol. 2009; 347: 159-168.
-
(2009)
J. Mol. Biol
, vol.347
, pp. 159-168
-
-
Ohkuri, T.1
Shioi, S.2
Imoto, T.3
Ueda, T.4
-
22
-
-
18244364614
-
Long-range interactions within a nonnative protein
-
Klein-Seetharaman J, Oikawa M, Grimshaw SB, Wirmer J, Duchardt E, Ueda T, Imoto T, Smith LJ, Dobson CM, Schwalbe H. Long-range interactions within a nonnative protein. Science. 2002; 295:1719-1722.
-
(2002)
Science
, vol.295
, pp. 1719-1722
-
-
Klein-Seetharaman, J.1
Oikawa, M.2
Grimshaw, S.B.3
Wirmer, J.4
Duchardt, E.5
Ueda, T.6
Imoto, T.7
Smith, L.J.8
Dobson, C.M.9
Schwalbe, H.10
-
24
-
-
33947658419
-
A particular hydrophobic cluster in the residual structure of reduced lysozyme drastically affects the amyloid fibrils formation
-
Mishima T, Ohkuri T, Monji A, Imoto T, Ueda T. A particular hydrophobic cluster in the residual structure of reduced lysozyme drastically affects the amyloid fibrils formation. Biochem. Biophys. Res. Commun. 2007; 356: 769-772.
-
(2007)
Biochem. Biophys. Res. Commun
, vol.356
, pp. 769-772
-
-
Mishima, T.1
Ohkuri, T.2
Monji, A.3
Imoto, T.4
Ueda, T.5
-
25
-
-
0037048671
-
Stimulation and inhibition of fibril formation by a peptide in the presence of different concentrations of SDS
-
Pertinhez TA, Bouchard M, Smith RA, Dobson CM, Smith LJ. Stimulation and inhibition of fibril formation by a peptide in the presence of different concentrations of SDS. FEBS Lett. 2002; 529: 193-197.
-
(2002)
FEBS Lett
, vol.529
, pp. 193-197
-
-
Pertinhez, T.A.1
Bouchard, M.2
Smith, R.A.3
Dobson, C.M.4
Smith, L.J.5
-
26
-
-
3343003514
-
Techniques to study amyloid fibril formation in vitro
-
Nilsson MR. Techniques to study amyloid fibril formation in vitro. Methods 2004; 34: 151-160.
-
(2004)
Methods
, vol.34
, pp. 151-160
-
-
Nilsson, M.R.1
-
27
-
-
67349237729
-
Organization and dynamics of tryptophan residues in tetrameric and monomeric soybean agglutinin: Studies by steady-state and time-resolved fluorescence, phosphorescence and chemical modification
-
Molla AR, Maity SS, Ghosh S, Mandal DK. Organization and dynamics of tryptophan residues in tetrameric and monomeric soybean agglutinin: studies by steady-state and time-resolved fluorescence, phosphorescence and chemical modification. Biochimie. 2009; 91: 857-867.
-
(2009)
Biochimie
, vol.91
, pp. 857-867
-
-
Molla, A.R.1
Maity, S.S.2
Ghosh, S.3
Mandal, D.K.4
-
28
-
-
0022503457
-
Calculation of protein conformation from circular dichroism
-
Yang JT, Wu CSC, Martinez HM. Calculation of protein conformation from circular dichroism. Methods in Enzymol. 1986; 130: 208-269.
-
(1986)
Methods In Enzymol
, vol.130
, pp. 208-269
-
-
Yang, J.T.1
Wu, C.S.C.2
Martinez, H.M.3
-
29
-
-
33746377894
-
Protein misfolding, functional amyloid, and human disease
-
Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006; 75: 333-366.
-
(2006)
Annu. Rev. Biochem
, vol.75
, pp. 333-366
-
-
Chiti, F.1
Dobson, C.M.2
-
31
-
-
39349102682
-
The formation of amyloid fibrils from proteins in the lysozyme family
-
Trexler AJ, Nilsson MR. The formation of amyloid fibrils from proteins in the lysozyme family. Curr. Protein Pept. Sci. 2007; 8: 537-557.
-
(2007)
Curr. Protein Pept. Sci
, vol.8
, pp. 537-557
-
-
Trexler, A.J.1
Nilsson, M.R.2
-
32
-
-
3242743649
-
Probing protein structure by limited proteolysis
-
Fontana A, de Laureto PP, Spolaore B, Frare E, Picotti P, Zambonin M. Probing protein structure by limited proteolysis. Acta Biochim. Pol. 2004; 51: 299-321.
-
(2004)
Acta Biochim. Pol
, vol.51
, pp. 299-321
-
-
Fontana, A.1
de Laureto, P.P.2
Spolaore, B.3
Frare, E.4
Picotti, P.5
Zambonin, M.6
-
33
-
-
0034647438
-
Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain
-
Krebs MR, Wilkins DK, Chung EW, Pitkeathly MC, Chamberlain AK, Zurdo J, Robinson CV, Dobson CM. Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain. J. Mol. Biol. 2000; 300: 541-549.
-
(2000)
J. Mol. Biol
, vol.300
, pp. 541-549
-
-
Krebs, M.R.1
Wilkins, D.K.2
Chung, E.W.3
Pitkeathly, M.C.4
Chamberlain, A.K.5
Zurdo, J.6
Robinson, C.V.7
Dobson, C.M.8
-
34
-
-
0030586945
-
Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous beta-sheet helix
-
Blake C, Serpell L. Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous beta-sheet helix. Structure 1996; 4: 989-998.
-
(1996)
Structure
, vol.4
, pp. 989-998
-
-
Blake, C.1
Serpell, L.2
-
35
-
-
70349160466
-
Cross-beta-sheet structure in amyloid fiber formation
-
Xu S. Cross-beta-sheet structure in amyloid fiber formation. J. Phys. Chem. B. 2009; 113: 12447-1255.
-
(2009)
J. Phys. Chem. B
, vol.113
, pp. 12447-12555
-
-
Xu, S.1
-
36
-
-
0032538350
-
Peptide models of local and long-range interactions in the molten globule state of human alpha-lactalbumin
-
Demarest SJ, Fairman R, Raleigh DP. Peptide models of local and long-range interactions in the molten globule state of human alpha-lactalbumin. J. Mol. Biol. 1998; 283: 279-291.
-
(1998)
J. Mol. Biol
, vol.283
, pp. 279-291
-
-
Demarest, S.J.1
Fairman, R.2
Raleigh, D.P.3
-
37
-
-
0035254984
-
A protein dissection study demonstrates that two specific hydrophobic clusters play a key role in stabilizing the core structure of the molten globule state of human alpha- lactalbumin
-
Demarest SJ, Horng JC, Raleigh DP. A protein dissection study demonstrates that two specific hydrophobic clusters play a key role in stabilizing the core structure of the molten globule state of human alpha- lactalbumin. Proteins 2001; 42: 237-242.
-
(2001)
Proteins
, vol.42
, pp. 237-242
-
-
Demarest, S.J.1
Horng, J.C.2
Raleigh, D.P.3
-
38
-
-
0019593952
-
Fluorescence quenching studies with proteins
-
Eftink MR, Ghiron CA. Fluorescence quenching studies with proteins. Anal. Biochem. 1981; 114: 199-227.
-
(1981)
Anal. Biochem
, vol.114
, pp. 199-227
-
-
Eftink, M.R.1
Ghiron, C.A.2
-
39
-
-
0031923940
-
Beta-lactamases as models for protein- folding studies
-
Vanhove M, Lejeune A, Pain RH. Beta-lactamases as models for protein- folding studies. Cell Mol. Life Sci. 1998; 54: 372-377.
-
(1998)
Cell Mol. Life Sci
, vol.54
, pp. 372-377
-
-
Vanhove, M.1
Lejeune, A.2
Pain, R.H.3
-
40
-
-
0027506498
-
Human lysozyme gene mutations cause hereditary systemic amyloidosis
-
Pepys MB, Hawkins PN, Booth DR, Vigushin DM, Tennent GA, Soutar AK, Totty N, Nguyen O, Blake CC, Terry CJ, et al. Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature 1993; 362: 553-557.
-
(1993)
Nature
, vol.362
, pp. 553-557
-
-
Pepys, M.B.1
Hawkins, P.N.2
Booth, D.R.3
Vigushin, D.M.4
Tennent, G.A.5
Soutar, A.K.6
Totty, N.7
Nguyen, O.8
Blake, C.C.9
Terry, C.J.10
-
41
-
-
0036189848
-
Hereditary renal amyloidosis caused by a new variant lysozyme W64R in a French family
-
Valleix S, Drunat S, Philit JB, Adoue D, Piette JC, Droz D, MacGregor B, Canet D, Delpech M, Grateau G. Hereditary renal amyloidosis caused by a new variant lysozyme W64R in a French family. Kidney Int. 2002; 61: 907-912.
-
(2002)
Kidney Int
, vol.61
, pp. 907-912
-
-
Valleix, S.1
Drunat, S.2
Philit, J.B.3
Adoue, D.4
Piette, J.C.5
Droz, D.6
Macgregor, B.7
Canet, D.8
Delpech, M.9
Grateau, G.10
-
42
-
-
0242500842
-
A novel lysozyme mutation Phe57Ile associated with hereditary renal amyloidosis
-
Yazaki M, Farrell SA, Benson MD. A novel lysozyme mutation Phe57Ile associated with hereditary renal amyloidosis. Kidney Int. 2003; 63: 1652-1657.
-
(2003)
Kidney Int
, vol.63
, pp. 1652-1657
-
-
Yazaki, M.1
Farrell, S.A.2
Benson, M.D.3
-
43
-
-
34548058571
-
ALys amyloidosis caused by compound heterozygosity in exon 2 (Thr70 Asn) and exon 4 (Trp112Arg) of the lysozyme gene
-
Rocken C, Becker K, Fandrich M, Schroeckh V, Stix B, Rath T, Kahne T, Dierkes J, Roessner A, Albert FW. ALys amyloidosis caused by compound heterozygosity in exon 2 (Thr70 Asn) and exon 4 (Trp112Arg) of the lysozyme gene. Hum. Mutat. 2006; 27: 119-120.
-
(2006)
Hum. Mutat
, vol.27
, pp. 119-120
-
-
Rocken, C.1
Becker, K.2
Fandrich, M.3
Schroeckh, V.4
Stix, B.5
Rath, T.6
Kahne, T.7
Dierkes, J.8
Roessner, A.9
Albert, F.W.10
-
44
-
-
33644939444
-
Impact of the native-state stability of human lysozyme variants on protein secretion by Pichia pastoris
-
Kumita JR, Johnson RJ, Alcocer MJ, Dumoulin M, Holmqvist F, McCammon MG, Robinson CV, Archer DB, Dobson CM. Impact of the native-state stability of human lysozyme variants on protein secretion by Pichia pastoris. FEBS J. 2006; 273: 711-720.
-
(2006)
FEBS J
, vol.273
, pp. 711-720
-
-
Kumita, J.R.1
Johnson, R.J.2
Alcocer, M.J.3
Dumoulin, M.4
Holmqvist, F.5
McCammon, M.G.6
Robinson, C.V.7
Archer, D.B.8
Dobson, C.M.9
-
45
-
-
33644944847
-
Lysozyme amyloidosis: Report of 4 cases and a review of the literature
-
Granel B, Valleix S, Serratrice J, Cherin P, Texeira A, Disdier P, Weiller PJ, Grateau G. Lysozyme amyloidosis: report of 4 cases and a review of the literature. Medicine (Baltimore) 2006; 85: 66-73.
-
(2006)
Medicine (Baltimore)
, vol.85
, pp. 66-73
-
-
Granel, B.1
Valleix, S.2
Serratrice, J.3
Cherin, P.4
Texeira, A.5
Disdier, P.6
Weiller, P.J.7
Grateau, G.8
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