-
1
-
-
37349062690
-
Micrometer-sized fibrillar protein aggregates from soy glycinin and soy protein isolate
-
Akkermans C., van der Goot A.J., Venema P., Gruppen H., Vereijken J.M., van der Linden E., et al. Micrometer-sized fibrillar protein aggregates from soy glycinin and soy protein isolate. Journal of Agricultural and Food Chemistry 2007, 55:9877-9882.
-
(2007)
Journal of Agricultural and Food Chemistry
, vol.55
, pp. 9877-9882
-
-
Akkermans, C.1
van der Goot, A.J.2
Venema, P.3
Gruppen, H.4
Vereijken, J.M.5
van der Linden, E.6
-
2
-
-
44449138916
-
Peptides are building blocks of heat-induced fibrillar protein aggregates of β-lactoglobulin formed at pH 2
-
Akkermans C., Venema P., van der Goot A.J., Gruppen H., Bakx E.J., Boom R.M., et al. Peptides are building blocks of heat-induced fibrillar protein aggregates of β-lactoglobulin formed at pH 2. Biomacromolecules 2008, 9:1474-1479.
-
(2008)
Biomacromolecules
, vol.9
, pp. 1474-1479
-
-
Akkermans, C.1
Venema, P.2
van der Goot, A.J.3
Gruppen, H.4
Bakx, E.J.5
Boom, R.M.6
-
3
-
-
11244340520
-
Thermally induced fibrillar aggregation of hen egg white lysozyme
-
Arnaudov L.N., de Vries R. Thermally induced fibrillar aggregation of hen egg white lysozyme. Biophysical Journal 2005, 88:515-526.
-
(2005)
Biophysical Journal
, vol.88
, pp. 515-526
-
-
Arnaudov, L.N.1
de Vries, R.2
-
4
-
-
33846274983
-
Strong impact of ionic strength on the kinetics of fibrillar aggregation of bovine β-lactoglobulin
-
Arnaudov L.N., de Vries R. Strong impact of ionic strength on the kinetics of fibrillar aggregation of bovine β-lactoglobulin. Biomacromolecules 2006, 7:3490-3498.
-
(2006)
Biomacromolecules
, vol.7
, pp. 3490-3498
-
-
Arnaudov, L.N.1
de Vries, R.2
-
5
-
-
34247257911
-
Theoretical modeling of the kinetics of fibrillar aggregation of bovine β-lactoglobulin at pH 2
-
Arnaudov L.N., de Vries R. Theoretical modeling of the kinetics of fibrillar aggregation of bovine β-lactoglobulin at pH 2. Journal of Chemistry and Physics 2007, 126.
-
(2007)
Journal of Chemistry and Physics
, vol.126
-
-
Arnaudov, L.N.1
de Vries, R.2
-
6
-
-
0001417865
-
Static and dynamic scattering of β-lactoglobulin aggregates formed after heat-induced denaturation at pH 2
-
Aymard P., Nicolai T., Durand D., Clark A. Static and dynamic scattering of β-lactoglobulin aggregates formed after heat-induced denaturation at pH 2. Macromolecules 1999, 32:2542-2552.
-
(1999)
Macromolecules
, vol.32
, pp. 2542-2552
-
-
Aymard, P.1
Nicolai, T.2
Durand, D.3
Clark, A.4
-
7
-
-
0034623193
-
Electrostatic potential profiles may guide cation-pi interaction in antimalarials chloroquine and mefloquine: an ab initio quantum chemical study
-
Bhattacharjee A.K. Electrostatic potential profiles may guide cation-pi interaction in antimalarials chloroquine and mefloquine: an ab initio quantum chemical study. Journal of Molecular Structure: THEOCHEM 2000, 529:193-201.
-
(2000)
Journal of Molecular Structure: THEOCHEM
, vol.529
, pp. 193-201
-
-
Bhattacharjee, A.K.1
-
8
-
-
34447640541
-
Effect of stirring and seeding on whey protein fibril formation
-
Bolder S.G., Sagis L.M.C., Venema P., van der Linden E. Effect of stirring and seeding on whey protein fibril formation. Journal of Agricultural and Food Chemistry 2007, 55:5661-5669.
-
(2007)
Journal of Agricultural and Food Chemistry
, vol.55
, pp. 5661-5669
-
-
Bolder, S.G.1
Sagis, L.M.C.2
Venema, P.3
van der Linden, E.4
-
9
-
-
33947694371
-
Heat-induced whey protein isolate fibrils: conversion, hydrolysis, and disulphide bond formation
-
Bolder S.G., Vasbinder A.J., Sagis L.M.C., van der Linden E. Heat-induced whey protein isolate fibrils: conversion, hydrolysis, and disulphide bond formation. International Dairy Journal 2007, 17:846-853.
-
(2007)
International Dairy Journal
, vol.17
, pp. 846-853
-
-
Bolder, S.G.1
Vasbinder, A.J.2
Sagis, L.M.C.3
van der Linden, E.4
-
11
-
-
3343005633
-
Differences and limits in estimates of persistence length for semi-flexible macromolecules
-
Cifra P. Differences and limits in estimates of persistence length for semi-flexible macromolecules. Polymer 2004, 45:5995-6002.
-
(2004)
Polymer
, vol.45
, pp. 5995-6002
-
-
Cifra, P.1
-
12
-
-
0030033588
-
Cation-pi interactions in chemistry and biology: a new view of Benzene, Phe, Tyr, and Trp
-
Dougherty D.A. Cation-pi interactions in chemistry and biology: a new view of Benzene, Phe, Tyr, and Trp. Science 1996, 271:163-168.
-
(1996)
Science
, vol.271
, pp. 163-168
-
-
Dougherty, D.A.1
-
13
-
-
0036468090
-
Aggregation, gelation and phase separation of heat denatured globular proteins
-
Durand D., Gimel J.C., Nicolai T. Aggregation, gelation and phase separation of heat denatured globular proteins. Physica A: Statistical Mechanics and its Applications 2002, 304:253-265.
-
(2002)
Physica A: Statistical Mechanics and its Applications
, vol.304
, pp. 253-265
-
-
Durand, D.1
Gimel, J.C.2
Nicolai, T.3
-
14
-
-
34047132881
-
Denaturation and aggregation of β-lactoglobulin-a preliminary molecular dynamics study
-
Euston S.R., Ur-Rehman S., Costello G. Denaturation and aggregation of β-lactoglobulin-a preliminary molecular dynamics study. Food Hydrocolloids 2007, 21:1081-1091.
-
(2007)
Food Hydrocolloids
, vol.21
, pp. 1081-1091
-
-
Euston, S.R.1
Ur-Rehman, S.2
Costello, G.3
-
15
-
-
35148865232
-
On the structural definition of amyloid fibrils and other polypeptide aggregates
-
Fändrich M. On the structural definition of amyloid fibrils and other polypeptide aggregates. Cellular and Molecular Life Sciences 2007, 64:2066-2078.
-
(2007)
Cellular and Molecular Life Sciences
, vol.64
, pp. 2066-2078
-
-
Fändrich, M.1
-
16
-
-
9744228666
-
Fibrillar β-lactoglobulin gels: part 1. Fibril formation and structure
-
Gosal W.S., Clark A.H., Ross-Murphy S.B. Fibrillar β-lactoglobulin gels: part 1. Fibril formation and structure. Biomacromolecules 2004, 5:2408-2419.
-
(2004)
Biomacromolecules
, vol.5
, pp. 2408-2419
-
-
Gosal, W.S.1
Clark, A.H.2
Ross-Murphy, S.B.3
-
17
-
-
4043078473
-
Influence of calcium on the self-assembly of partially hydrolyzed alpha-lactalbumin
-
Graveland-Bikker J.F., Ipsen R., Otte J., de Kruif C.G. Influence of calcium on the self-assembly of partially hydrolyzed alpha-lactalbumin. Langmuir 2004, 20:6841-6846.
-
(2004)
Langmuir
, vol.20
, pp. 6841-6846
-
-
Graveland-Bikker, J.F.1
Ipsen, R.2
Otte, J.3
de Kruif, C.G.4
-
19
-
-
59749090968
-
Competition between folding, native-state dimerisation and amyloid aggregation in β-lactoglobulin
-
Hamada D., Tanaka T., Tartaglia G.G., Pawar A., Vendruscolo M., Kawamura M., et al. Competition between folding, native-state dimerisation and amyloid aggregation in β-lactoglobulin. Journal of Molecular Biology 2009, 386:878-890.
-
(2009)
Journal of Molecular Biology
, vol.386
, pp. 878-890
-
-
Hamada, D.1
Tanaka, T.2
Tartaglia, G.G.3
Pawar, A.4
Vendruscolo, M.5
Kawamura, M.6
-
20
-
-
73649116661
-
Liquid crystalline phase behavior of protein fibers in water: experiments versus theory
-
Jung J.M., Mezzenga R. Liquid crystalline phase behavior of protein fibers in water: experiments versus theory. Langmuir 2010, 26:504-514.
-
(2010)
Langmuir
, vol.26
, pp. 504-514
-
-
Jung, J.M.1
Mezzenga, R.2
-
22
-
-
0035955555
-
2-Microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro
-
2-Microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro. Journal of Molecular Biology 2001, 313:559-571.
-
(2001)
Journal of Molecular Biology
, vol.313
, pp. 559-571
-
-
Kad, N.M.1
Thomson, N.H.2
Smith, D.P.3
Smith, D.A.4
Radford, S.E.5
-
23
-
-
0034318911
-
Heat-induced gelation of globular proteins: 4. Gelation kinetics of low pH β-lactoglobulin gels
-
Kavanagh G.M., Clark A.H., Ross-Murphy S.B. Heat-induced gelation of globular proteins: 4. Gelation kinetics of low pH β-lactoglobulin gels. Langmuir 2000, 16:9584-9594.
-
(2000)
Langmuir
, vol.16
, pp. 9584-9594
-
-
Kavanagh, G.M.1
Clark, A.H.2
Ross-Murphy, S.B.3
-
25
-
-
85025567869
-
Fine-stranded and particulate gels of β-lactoglobulin and whey-protein at varying pH
-
Langton M., Hermansson A.M. Fine-stranded and particulate gels of β-lactoglobulin and whey-protein at varying pH. Food Hydrocolloids 1992, 5:523-539.
-
(1992)
Food Hydrocolloids
, vol.5
, pp. 523-539
-
-
Langton, M.1
Hermansson, A.M.2
-
26
-
-
18444375570
-
Protein dissection enhances the amyloidogenic properties of alpha-lactalbumin
-
de Laureto P.P., Frare E., Battaglia F., Mossuto M.F., Uversky V.N., Fontana A. Protein dissection enhances the amyloidogenic properties of alpha-lactalbumin. FEBS Journal 2005, 272:2176-2188.
-
(2005)
FEBS Journal
, vol.272
, pp. 2176-2188
-
-
de Laureto, P.P.1
Frare, E.2
Battaglia, F.3
Mossuto, M.F.4
Uversky, V.N.5
Fontana, A.6
-
27
-
-
0031823022
-
Theoretical models of viscoelasticity of actin solutions and the actin cortex
-
Mackintosh F.C. Theoretical models of viscoelasticity of actin solutions and the actin cortex. Biological Bulletin 1998, 194:351-353.
-
(1998)
Biological Bulletin
, vol.194
, pp. 351-353
-
-
Mackintosh, F.C.1
-
28
-
-
33846562360
-
Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion
-
Mishra R., Sörgjerd K., Nyström S., Nordigården A., Yu Y.-C., Hammarström P. Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion. Journal of Molecular Biology 2007, 366:1029-1044.
-
(2007)
Journal of Molecular Biology
, vol.366
, pp. 1029-1044
-
-
Mishra, R.1
Sörgjerd, K.2
Nyström, S.3
Nordigården, A.4
Yu, Y.-C.5
Hammarström, P.6
-
29
-
-
39749112546
-
Fitting neurological protein aggregation kinetic data via a 2-step, Minimal/" Ockham's Razor" model: the Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth
-
Morris A.M., Watzky M.A., Agar J.N., Finke R.G. Fitting neurological protein aggregation kinetic data via a 2-step, Minimal/" Ockham's Razor" model: the Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth. Biochemistry 2008, 47:2413-2427.
-
(2008)
Biochemistry
, vol.47
, pp. 2413-2427
-
-
Morris, A.M.1
Watzky, M.A.2
Agar, J.N.3
Finke, R.G.4
-
30
-
-
67349276424
-
Cold-set thickening mechanism of β-lactoglobulin at low pH: concentration effects
-
Mudgal P., Daubert C.R., Foegeding E.A. Cold-set thickening mechanism of β-lactoglobulin at low pH: concentration effects. Food Hydrocolloids 2009, 23:1762-1770.
-
(2009)
Food Hydrocolloids
, vol.23
, pp. 1762-1770
-
-
Mudgal, P.1
Daubert, C.R.2
Foegeding, E.A.3
-
31
-
-
0030030956
-
First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro
-
Naiki H., Nakakuki K. First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro. Laboratory Investigation 1996, 74:374-383.
-
(1996)
Laboratory Investigation
, vol.74
, pp. 374-383
-
-
Naiki, H.1
Nakakuki, K.2
-
32
-
-
0035158241
-
Studies of the structure of insulin fibrils by Fourier transform infrared (FTIR) spectroscopy and electron microscopy
-
Nielsen L., Frokjaer S., Carpenter J.F., Brange J. Studies of the structure of insulin fibrils by Fourier transform infrared (FTIR) spectroscopy and electron microscopy. Journal of Pharmaceutical Sciences 2001, 90:29-37.
-
(2001)
Journal of Pharmaceutical Sciences
, vol.90
, pp. 29-37
-
-
Nielsen, L.1
Frokjaer, S.2
Carpenter, J.F.3
Brange, J.4
-
33
-
-
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., Vyas S., et al. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 2001, 40:6036-6046.
-
(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
-
34
-
-
19544375553
-
Sequence dependence of amyloid fibril formation: insights from molecular dynamics simulations
-
de la Paz M.L., de Mori G.M.S., Serrano L., Colombo G. Sequence dependence of amyloid fibril formation: insights from molecular dynamics simulations. Journal of Molecular Biology 2005, 349:583-596.
-
(2005)
Journal of Molecular Biology
, vol.349
, pp. 583-596
-
-
de la Paz, M.L.1
de Mori, G.M.S.2
Serrano, L.3
Colombo, G.4
-
35
-
-
8644266740
-
X-ray and light scattering study of the structure of large protein aggregates at neutral pH
-
Pouzot M., Nicolai T., Visschers R.W., Weijers M. X-ray and light scattering study of the structure of large protein aggregates at neutral pH. Food Hydrocolloids 2005, 19:231-238.
-
(2005)
Food Hydrocolloids
, vol.19
, pp. 231-238
-
-
Pouzot, M.1
Nicolai, T.2
Visschers, R.W.3
Weijers, M.4
-
36
-
-
26844482366
-
+] interactions with the aromatic
-
+] interactions with the aromatic motifs of naturally occurring amino acids: a theoretical study. Journal of Physical Chemistry 2005, 109:8893-8903.
-
(2005)
Journal of Physical Chemistry
, vol.109
, pp. 8893-8903
-
-
Reddy, A.S.1
Sastry, G.N.2
-
37
-
-
0036182892
-
Mesoscopic structure and viscoelastic properties of β-lactoglobulin gels at low pH and low ionic strength
-
Sagis L.M.C., Veerman C., Ganzevles R., Ramaekers M., Bolder S.G., van der Linden E. Mesoscopic structure and viscoelastic properties of β-lactoglobulin gels at low pH and low ionic strength. Food Hydrocolloids 2002, 16:207-213.
-
(2002)
Food Hydrocolloids
, vol.16
, pp. 207-213
-
-
Sagis, L.M.C.1
Veerman, C.2
Ganzevles, R.3
Ramaekers, M.4
Bolder, S.G.5
van der Linden, E.6
-
38
-
-
1242310516
-
Mesoscopic properties of semiflexible amyloid fibrils
-
Sagis L.M.C., Veerman C., van der Linden E. Mesoscopic properties of semiflexible amyloid fibrils. Langmuir 2004, 20:924-927.
-
(2004)
Langmuir
, vol.20
, pp. 924-927
-
-
Sagis, L.M.C.1
Veerman, C.2
van der Linden, E.3
-
39
-
-
0033846408
-
Heat-induced aggregation of β-lactoglobulin AB at pH 2.5 as influenced by ionic strength and protein concentration
-
Schokker E.P., Singh H., Pinder D.N., Creamer L.K. Heat-induced aggregation of β-lactoglobulin AB at pH 2.5 as influenced by ionic strength and protein concentration. International Dairy Journal 2000, 10:233-240.
-
(2000)
International Dairy Journal
, vol.10
, pp. 233-240
-
-
Schokker, E.P.1
Singh, H.2
Pinder, D.N.3
Creamer, L.K.4
|