-
1
-
-
34250330794
-
Oligomerization of the human prion protein proceeds via a molten globule intermediate
-
DOI 10.1074/jbc.M608926200
-
R. Gerber, A. Tahiri-Alaoui, P.J. Hore, and W. James Oligomerization of the human prion protein proceeds via a molten globule intermediate J. Biol. Chem. 282 2007 6300 6307 (Pubitemid 47100833)
-
(2007)
Journal of Biological Chemistry
, vol.282
, Issue.9
, pp. 6300-6307
-
-
Gerber, R.1
Tahiri-Alaoui, A.2
Hore, P.J.3
James, W.4
-
2
-
-
22244456042
-
Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy
-
DOI 10.1529/biophysj.104.049700
-
M. Lindgren, K. Sorgjerd, and P. Hammarstrom Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy Biophys. J. 88 2005 4200 4212 (Pubitemid 40991131)
-
(2005)
Biophysical Journal
, vol.88
, Issue.6
, pp. 4200-4212
-
-
Lindgren, M.1
Sorgjerd, K.2
Hammarstrom, P.3
-
3
-
-
38049005587
-
Similar toxicity of the oligomeric molten globule state and the prefibrillar oligomers
-
S. Ceru, and E. Zerovnik Similar toxicity of the oligomeric molten globule state and the prefibrillar oligomers FEBS Lett. 582 2008 203 209
-
(2008)
FEBS Lett.
, vol.582
, pp. 203-209
-
-
Ceru, S.1
Zerovnik, E.2
-
4
-
-
0033538015
-
Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro
-
DOI 10.1006/jmbi.1999.2646
-
R. Kayed, J.È. Bernhagen, N. Greenfield, K. Sweimeh, H. Brunner, W. Voelter, and A. Kapurniotu Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro J. Mol. Biol. 287 1999 781 796 (Pubitemid 29176513)
-
(1999)
Journal of Molecular Biology
, vol.287
, Issue.4
, pp. 781-796
-
-
Kayed, R.1
Bernhagen, J.2
Greenfield, N.3
Sweimeh, K.4
Brunner, H.5
Voelter, W.6
Kapurniotu, A.7
-
5
-
-
0036652217
-
Protein folding in the post-genomic era
-
M.Y. Jeannine Protein folding in the post-genomic era J. Cell Mol. Med. 6 2002 307 327
-
(2002)
J. Cell Mol. Med.
, vol.6
, pp. 307-327
-
-
Jeannine, M.Y.1
-
6
-
-
0029124248
-
Molten globule and protein folding
-
O.B. Ptitsyn Molten globule and protein folding Adv. Protein Chem. 47 1995 83 229
-
(1995)
Adv. Protein Chem.
, vol.47
, pp. 83-229
-
-
Ptitsyn, O.B.1
-
7
-
-
0027749370
-
Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
-
P.A. Jennings, and P.E. Wright Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin Science 262 1993 892 896 (Pubitemid 24014075)
-
(1993)
Science
, vol.262
, Issue.5135
, pp. 892-896
-
-
Jennings, P.A.1
Wright, P.E.2
-
8
-
-
84855833470
-
Structural and dynamical insights into the molten-globule form of ovalbumin
-
M. Bhattacharya, and S. Mukhopadhyay Structural and dynamical insights into the molten-globule form of ovalbumin J. Phys. Chem. B 116 2012 520 531
-
(2012)
J. Phys. Chem. B
, vol.116
, pp. 520-531
-
-
Bhattacharya, M.1
Mukhopadhyay, S.2
-
9
-
-
84866649525
-
Illuminating the off-pathway nature of the molten globule folding intermediate of an α-β Parallel protein
-
S. Lindhoud, A.H. Westphal, J.W. Borst, and C.P. van Mierlo Illuminating the off-pathway nature of the molten globule folding intermediate of an α-β parallel protein PLoS ONE 7 2012 e45746
-
(2012)
PLoS ONE
, vol.7
, pp. 45746
-
-
Lindhoud, S.1
Westphal, A.H.2
Borst, J.W.3
Van Mierlo, C.P.4
-
10
-
-
78649728415
-
Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution
-
A. Dhulesia, N. Cremades, J.R. Kumita, S.T. Hsu, M.F. Mossuto, M. Dumoulin, D. Nietlispach, M. Akke, X. Salvatella, and C.M. Dobson Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution J. Am. Chem. Soc. 132 2010 15580 15588
-
(2010)
J. Am. Chem. Soc.
, vol.132
, pp. 15580-15588
-
-
Dhulesia, A.1
Cremades, N.2
Kumita, J.R.3
Hsu, S.T.4
Mossuto, M.F.5
Dumoulin, M.6
Nietlispach, D.7
Akke, M.8
Salvatella, X.9
Dobson, C.M.10
-
11
-
-
2342569618
-
Conformational constraints for amyloid fibrillation: The importance of being unfolded
-
DOI 10.1016/j.bbapap.2003.12.008, PII S1570963904000020
-
V.N. Uversky, and A.L. Fink Conformational constraints for amyloid fibrillation: the importance of being unfolded Biochim. Biophys. Acta 1698 2004 131 153 (Pubitemid 38591469)
-
(2004)
Biochimica et Biophysica Acta - Proteins and Proteomics
, vol.1698
, Issue.2
, pp. 131-153
-
-
Uversky, V.N.1
Fink, A.L.2
-
12
-
-
70349333845
-
Effect of curcumin on amyloidogenic property of molten globule-like intermediate state of 2,5-diketo-D-gluconate reductase A
-
N. Sarkar, A.N. Singh, and V.K. Dubey Effect of curcumin on amyloidogenic property of molten globule-like intermediate state of 2,5-diketo-D-gluconate reductase A Biol. Chem. 390 2009 1057 1061
-
(2009)
Biol. Chem.
, vol.390
, pp. 1057-1061
-
-
Sarkar, N.1
Singh, A.N.2
Dubey, V.K.3
-
13
-
-
78649778065
-
Differences in the pathways of proteins unfolding induced by urea and guanidine hydrochloride: Molten globule state and aggregates
-
O.I. Povarova, I.M. Kuznetsova, and K.K. Turoverov Differences in the pathways of proteins unfolding induced by urea and guanidine hydrochloride: molten globule state and aggregates PLoS ONE 5 2010 e15035
-
(2010)
PLoS ONE
, vol.5
, pp. 15035
-
-
Povarova, O.I.1
Kuznetsova, I.M.2
Turoverov, K.K.3
-
14
-
-
77956418467
-
Off-pathway status for the alkali molten globule of horse ferricytochrome c
-
A.K. Bhuyan Off-pathway status for the alkali molten globule of horse ferricytochrome c Biochemistry 49 2010 7764 7773
-
(2010)
Biochemistry
, vol.49
, pp. 7764-7773
-
-
Bhuyan, A.K.1
-
15
-
-
77953692444
-
Specific molten globule conformation of stem bromelain at alkaline pH
-
S. Dave, S. Mahajan, V. Chandra, H.K. Dkhar, Sambhavi, and P. Gupta Specific molten globule conformation of stem bromelain at alkaline pH Arch. Biochem. Biophys. 499 2010 26 31
-
(2010)
Arch. Biochem. Biophys.
, vol.499
, pp. 26-31
-
-
Dave, S.1
Mahajan, S.2
Chandra, V.3
Dkhar, H.K.4
Sambhavi5
Gupta, P.6
-
16
-
-
2342663171
-
Molten-globule like partially folded states of human serum albumin induced by fluoro and alkyl alcohols at low pH
-
DOI 10.1016/j.abb.2004.03.025, PII S0003986104001651
-
Y. Kumar, S. Tayyab, and S. Muzammil Molten-globule like partially folded states of human serum albumin induced by fluoro and alkyl alcohols at low pH Arch. Biochem. Biophys. 426 2004 3 10 (Pubitemid 38595125)
-
(2004)
Archives of Biochemistry and Biophysics
, vol.426
, Issue.1
, pp. 3-10
-
-
Kumar, Y.1
Tayyab, S.2
Muzammil, S.3
-
17
-
-
0033200063
-
Protein misfolding, evolution and disease
-
DOI 10.1016/S0968-0004(99)01445-0, PII S0968000499014450
-
C.M. Dobson Protein misfolding, evolution and disease Trends Biochem. Sci. 24 1999 329 332 (Pubitemid 29421804)
-
(1999)
Trends in Biochemical Sciences
, vol.24
, Issue.9
, pp. 329-332
-
-
Dobson, C.M.1
-
18
-
-
0020184671
-
How crowded is the cytoplasm?
-
A.B. Fulton How crowded is the cytoplasm? Cell 30 1982 345 347
-
(1982)
Cell
, vol.30
, pp. 345-347
-
-
Fulton, A.B.1
-
20
-
-
0032079008
-
Biophysical compensation mechanisms buffering E coli protein-nucleic acid interactions against changing environments
-
DOI 10.1016/S0968-0004(98)01207-9
-
M.T. Record Jr., E.S. Courtenay, S. Cayley, and H.J. Guttman Biophysical compensation mechanisms buffering E. coli protein-nucleic acid interactions against changing environments Trends Biochem. Sci. 23 1998 190 194 (Pubitemid 28261038)
-
(1998)
Trends in Biochemical Sciences
, vol.23
, Issue.5
, pp. 190-194
-
-
Record Jr., T.M.1
Courtenay, E.S.2
Cayley, S.3
Guttman, H.J.4
-
21
-
-
0035253217
-
Macromolecular crowding: An important but neglected aspect of the intracellular environment
-
DOI 10.1016/S0959-440X(00)00172-X
-
R.J. Ellis Macromolecular crowding: an important but neglected aspect of the intracellular environment Curr. Opin. Struct. Biol. 11 2001 114 119 (Pubitemid 32155560)
-
(2001)
Current Opinion in Structural Biology
, vol.11
, Issue.1
, pp. 114-119
-
-
Ellis, R.J.1
-
22
-
-
0035478585
-
Macromolecular crowding: Obvious but underappreciated
-
DOI 10.1016/S0968-0004(01)01938-7, PII S0968000401019387
-
R.J. Ellis Macromolecular crowding: obvious but underappreciated Trends Biochem. Sci. 26 2001 597 604 (Pubitemid 32925190)
-
(2001)
Trends in Biochemical Sciences
, vol.26
, Issue.10
, pp. 597-604
-
-
Ellis R.John1
-
23
-
-
41049090929
-
Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences
-
H.X. Zhou, G. Rivas, and A.P. Minton Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences Ann. Rev. Biophys. 37 2008 375 397
-
(2008)
Ann. Rev. Biophys.
, vol.37
, pp. 375-397
-
-
Zhou, H.X.1
Rivas, G.2
Minton, A.P.3
-
24
-
-
0035815743
-
The Influence of Macromolecular Crowding and Macromolecular Confinement on Biochemical Reactions in Physiological Media
-
DOI 10.1074/jbc.R100005200
-
A.P. Minton The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media J. Biol. Chem. 276 2001 10577 10580 (Pubitemid 38089223)
-
(2001)
Journal of Biological Chemistry
, vol.276
, Issue.14
, pp. 10577-10580
-
-
Minton, A.P.1
-
25
-
-
16344364032
-
Models for excluded volume interaction between an unfolded protein and rigid macromolecular cosolutes: Macromolecular crowding and protein stability revisited
-
DOI 10.1529/biophysj.104.050351
-
A.P. Minton Models for excluded volume interaction between an unfolded protein and rigid macromolecular cosolutes: macromolecular crowding and protein stability revisited Biophys. J. 88 2005 971 985 (Pubitemid 40975932)
-
(2005)
Biophysical Journal
, vol.88
, Issue.2
, pp. 971-985
-
-
Minton, A.P.1
-
26
-
-
33746099650
-
Protein aggregation in crowded environments
-
DOI 10.1515/BC.2006.064, PII BCHM3875485
-
R.J. Ellis, and A.P. Minton Protein aggregation in crowded environments Biol. Chem. 387 2006 485 497 (Pubitemid 44071450)
-
(2006)
Biological Chemistry
, vol.387
, Issue.5
, pp. 485-497
-
-
Ellis, R.J.1
Minton, A.P.2
-
27
-
-
4544252011
-
The effect of macromolecular crowding on protein aggregation and amyloid fibril formation
-
DOI 10.1002/jmr.699, EMBO Workshop on Biological Implications of Macromolecular Crowding
-
L.A. Munishkina, E.M. Cooper, V.N. Uversky, and A.L. Fink The effect of macromolecular crowding on protein aggregation and amyloid fibril formation J. Mol. Recognit. 17 2004 456 464 (Pubitemid 39218989)
-
(2004)
Journal of Molecular Recognition
, vol.17
, Issue.5
, pp. 456-464
-
-
Munishkina, L.A.1
Cooper, E.M.2
Uversky, V.N.3
Fink, A.L.4
-
28
-
-
0037040878
-
Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II
-
DOI 10.1074/jbc.M110429200
-
D.M. Hatters, A.P. Minton, and G.J. Howlett Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II J. Biol. Chem. 277 2002 7824 7830 (Pubitemid 34968230)
-
(2002)
Journal of Biological Chemistry
, vol.277
, Issue.10
, pp. 7824-7830
-
-
Hatters, D.M.1
Minton, A.P.2
Howlett, G.J.3
-
29
-
-
21744444004
-
Forcing nonamyloidogenic beta-synuclein to fibrillate
-
G. Yamin, L.A. Munishkina, M.A. Karymov, Y.L. Lyubchenko, V.N. Uversky, and A.L. Fink Forcing nonamyloidogenic beta-synuclein to fibrillate Biochemistry 44 2005 9096 9107
-
(2005)
Biochemistry
, vol.44
, pp. 9096-9107
-
-
Yamin, G.1
Munishkina, L.A.2
Karymov, M.A.3
Lyubchenko, Y.L.4
Uversky, V.N.5
Fink, A.L.6
-
30
-
-
43049096368
-
Mixed macromolecular crowding inhibits amyloid formation of hen egg white lysozyme
-
B.R. Zhou, Z. Zhou, Q.L. Hu, J. Chen, and Y. Liang Mixed macromolecular crowding inhibits amyloid formation of hen egg white lysozyme Biochim. Biophys. Acta 1784 2008 472 480
-
(2008)
Biochim. Biophys. Acta
, vol.1784
, pp. 472-480
-
-
Zhou, B.R.1
Zhou, Z.2
Hu, Q.L.3
Chen, J.4
Liang, Y.5
-
32
-
-
0033572725
-
Effects of macromolecular crowding on protein folding and aggregation
-
B. van den Berg, R.J. Ellis, and C.M. Dobson Effects of macromolecular crowding on protein folding and aggregation EMBO J. 18 1999 6927 6933 (Pubitemid 30000446)
-
(1999)
EMBO Journal
, vol.18
, Issue.24
, pp. 6927-6933
-
-
Van Den Berg, B.1
Ellis, R.J.2
Dobson, C.M.3
-
33
-
-
0013852463
-
Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution
-
C.C.F. Blake, D.F. Koenig, G.A. Mair, A.C.T. North, D.C. Phillips, and V.R. Sarma Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution Nature 206 1965 757 761
-
(1965)
Nature
, vol.206
, pp. 757-761
-
-
Blake, C.C.F.1
Koenig, D.F.2
Mair, G.A.3
North, A.C.T.4
Phillips, D.C.5
Sarma, V.R.6
-
34
-
-
0028053187
-
Understanding how proteins fold: The lysozyme story so far
-
DOI 10.1016/0968-0004(94)90171-6
-
C.M. Dobson, P.A. Evans, and S.E. Radford Understanding how proteins fold: the lysozyme story so far Trends Biochem. Sci. 19 1994 31 37 (Pubitemid 24028729)
-
(1994)
Trends in Biochemical Sciences
, vol.19
, Issue.1
, pp. 31-37
-
-
Dobson, C.M.1
Evans, P.A.2
Radford, S.E.3
-
35
-
-
11244340520
-
Thermally induced fibrillar aggregation of hen egg white lysozyme
-
DOI 10.1529/biophysj.104.048819
-
L.N. Arnaudov, and R. de Vries Thermally induced fibrillar aggregation of hen egg white lysozyme Biophys. J. 88 2005 515 526 (Pubitemid 40070697)
-
(2005)
Biophysical Journal
, vol.88
, Issue.1
, pp. 515-526
-
-
Arnaudov, L.N.1
De Vries, R.2
-
36
-
-
33846562360
-
Lysozyme Amyloidogenesis Is Accelerated by Specific Nicking and Fragmentation but Decelerated by Intact Protein Binding and Conversion
-
DOI 10.1016/j.jmb.2006.11.084, PII S0022283606016433
-
R. Mishra, K. Sörgjerd, S. Nyström, A. Nordigården, Y.C. Yu, and P. Hammarström Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion J. Mol. Biol. 366 2007 1029 1044 (Pubitemid 46175878)
-
(2007)
Journal of Molecular Biology
, vol.366
, Issue.3
, pp. 1029-1044
-
-
Mishra, R.1
Sorgjerd, K.2
Nystrom, S.3
Nordigarden, A.4
Yu, Y.-C.5
Hammarstrom, P.6
-
37
-
-
70149093400
-
Effects of glutathione on amyloid fibrillation of hen egg-white lysozyme
-
S.S. Wang, S.W. Chou, K.N. Liu, and C.H. Wu Effects of glutathione on amyloid fibrillation of hen egg-white lysozyme Int. J. Biol. Macromol. 45 2009 321 329
-
(2009)
Int. J. Biol. Macromol.
, vol.45
, pp. 321-329
-
-
Wang, S.S.1
Chou, S.W.2
Liu, K.N.3
Wu, C.H.4
-
38
-
-
84867200449
-
Photoinduced fibrils formation of chicken egg white lysozyme under native conditions
-
J.B. Xie, Y. Cao, H. Pan, M. Qin, Z.Q. Yan, X. Xiong, and W. Wang Photoinduced fibrils formation of chicken egg white lysozyme under native conditions Proteins 80 2012 2501 2513
-
(2012)
Proteins
, vol.80
, pp. 2501-2513
-
-
Xie, J.B.1
Cao, Y.2
Pan, H.3
Qin, M.4
Yan, Z.Q.5
Xiong, X.6
Wang, W.7
-
39
-
-
77955665370
-
Effects of dithiothreitol on the amyloid fibrillogenesis of hen egg-white lysozyme
-
S.S. Wang, K.N. Liu, and B.W. Wang Effects of dithiothreitol on the amyloid fibrillogenesis of hen egg-white lysozyme Eur. Biophys. J. 39 2010 1229 1242
-
(2010)
Eur. Biophys. J.
, vol.39
, pp. 1229-1242
-
-
Wang, S.S.1
Liu, K.N.2
Wang, B.W.3
-
40
-
-
70249114002
-
Investigating the influences of redox buffer compositions on the amyloid fibrillogenesis of hen egg-white lysozyme
-
S.S. Wang, K.N. Liu, C.H. Wu, and J.K. Lai Investigating the influences of redox buffer compositions on the amyloid fibrillogenesis of hen egg-white lysozyme Biochim. Biophys. Acta 1794 2009 1663 1672
-
(2009)
Biochim. Biophys. Acta
, vol.1794
, pp. 1663-1672
-
-
Wang, S.S.1
Liu, K.N.2
Wu, C.H.3
Lai, J.K.4
-
41
-
-
79953875355
-
Effect of sodium tetrathionate on amyloid fibril: Insight into the role of disulfide bond in amyloid progression
-
N. Sarkar, M. Kumar, and V.K. Dubey Effect of sodium tetrathionate on amyloid fibril: insight into the role of disulfide bond in amyloid progression Biochimie 93 2011 962 968
-
(2011)
Biochimie
, vol.93
, pp. 962-968
-
-
Sarkar, N.1
Kumar, M.2
Dubey, V.K.3
-
42
-
-
61549119795
-
Tertiary butanol induced amyloidogenesis of hen egg white lysozyme (HEWL) is facilitated by aggregation-prone alkali-induced molten globule like conformational state
-
M. Hameed, B. Ahmad, R.H. Khan, K.I. Andrabi, and K.M. Fazili Tertiary butanol induced amyloidogenesis of hen egg white lysozyme (HEWL) is facilitated by aggregation-prone alkali-induced molten globule like conformational state Protein Pept. Lett. 16 2009 56 60
-
(2009)
Protein Pept. Lett.
, vol.16
, pp. 56-60
-
-
Hameed, M.1
Ahmad, B.2
Khan, R.H.3
Andrabi, K.I.4
Fazili, K.M.5
-
44
-
-
0027506498
-
Human lysozyme gene mutations cause hereditary systemic amyloidosis
-
DOI 10.1038/362553a0
-
M.B. Pepys, P.N. Hawkins, D.R. Booth, D.M. Vigushin, G.A. Tennent, A.K. Soutar, N. Totty, O. Nguyen, C.C.F. Blake, and C.J. Terry Human lysozyme gene mutations cause hereditary systemic amyloidosis Nature 362 1993 553 557 (Pubitemid 23113032)
-
(1993)
Nature
, vol.362
, Issue.6420
, 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.F.9
Terry, C.J.10
Feest, T.G.11
Zalin, A.M.12
Hsuan, J.J.13
-
45
-
-
0033849915
-
Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants
-
L.A. Morozova-Roche, J. Zurdo, A. Spencer, W. Noppe, V. Receveur, D.B. Archer, M. Joniau, and C.M. Dobson Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants J. Struct. Biol. 130 2000 339 351
-
(2000)
J. Struct. Biol.
, vol.130
, pp. 339-351
-
-
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
-
46
-
-
67650233979
-
Hen lysozyme amyloid fibrils induce aggregation of erythrocytes and lipid vesicles
-
N. Chaudhary, and R. Nagaraj Hen lysozyme amyloid fibrils induce aggregation of erythrocytes and lipid vesicles Mol. Cell. Biochem. 328 2009 209 215
-
(2009)
Mol. Cell. Biochem.
, vol.328
, pp. 209-215
-
-
Chaudhary, N.1
Nagaraj, R.2
-
47
-
-
33846023647
-
Lysozyme Amyloid Oligomers and Fibrils Induce Cellular Death via Different Apoptotic/Necrotic Pathways
-
DOI 10.1016/j.jmb.2006.10.101, PII S0022283606015294
-
A.L. Gharibyan, V. Zamotin, K. Yanamandra, O.S. Moskaleva, B.A. Margulis, I.A. Kostanyan, and L.A. Morozova-Roche Lysozyme amyloid oligomers and fibrils induce cellular death via different apoptotic/necrotic pathways J. Mol. Biol. 365 2007 1337 1349 (Pubitemid 46048842)
-
(2007)
Journal of Molecular Biology
, vol.365
, Issue.5
, pp. 1337-1349
-
-
Gharibyan, A.L.1
Zamotin, V.2
Yanamandra, K.3
Moskaleva, O.S.4
Margulis, B.A.5
Kostanyan, I.A.6
Morozova-Roche, L.A.7
-
48
-
-
0031056829
-
Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
-
DOI 10.1038/385787a0
-
D.R. Booth, M. Sunde, V. Bellotti, C.V. Robinson, W.L. Hutchinson, P.E. Fraser, P.N. Hawkins, C.M. Dobson, S.E. Radford, C.C. Blake, and M.B. Pepys Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis Nature 385 1997 787 793 (Pubitemid 27106061)
-
(1997)
Nature
, vol.385
, Issue.6619
, pp. 787-793
-
-
Booth, D.R.1
Sunde, M.2
Bellotti, V.3
Robinson, C.V.4
Hutchinson, W.L.5
Fraser, P.E.6
Hawkins, P.N.7
Dobson, C.M.8
Radford, S.E.9
Blake, C.C.F.10
Pepys, M.B.11
-
49
-
-
33749831531
-
Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants
-
M. Dumoulin, J.R. Kumita, and C.M. Dobson Normal and aberrant biological self-assembly: insights from studies of human lysozyme and its amyloidogenic variants Acc. Chem. Res. 39 2006 603 610
-
(2006)
Acc. Chem. Res.
, vol.39
, pp. 603-610
-
-
Dumoulin, M.1
Kumita, J.R.2
Dobson, C.M.3
-
50
-
-
0033580657
-
Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants
-
D. Canet, M. Sunde, A.M. Last, A. Miranker, A. Spencer, C.V. Robinson, and C.M. Dobson Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants Biochemistry 38 1999 6419 6427
-
(1999)
Biochemistry
, vol.38
, pp. 6419-6427
-
-
Canet, D.1
Sunde, M.2
Last, A.M.3
Miranker, A.4
Spencer, A.5
Robinson, C.V.6
Dobson, C.M.7
-
51
-
-
38449094348
-
Different molten globule-like folding intermediates of hen egg white lysozyme induced by high pH and tertiary butanol
-
DOI 10.1093/jb/mvm057
-
M. Hameed, B. Ahmad, K.M. Fazili, K.I. Andrabi, and R.H. Khan Different molten globule-like folding intermediates of hen egg white lysozyme induced by high pH and tertiary butanol J. Biochem. 141 2007 573 583 (Pubitemid 351455304)
-
(2007)
Journal of Biochemistry
, vol.141
, Issue.4
, pp. 573-583
-
-
Hameed, M.1
Ahmad, B.2
Fazili, K.M.3
Andrabi, K.4
Khan, R.H.5
-
52
-
-
54049088134
-
How do surfactants and DTT affect the size, dynamics, activity and growth of soluble lysozyme aggregates?
-
S. Kumar, V.K. Ravi, and R. Swaminathan How do surfactants and DTT affect the size, dynamics, activity and growth of soluble lysozyme aggregates? Biochem. J. 415 2008 275 288
-
(2008)
Biochem. J.
, vol.415
, pp. 275-288
-
-
Kumar, S.1
Ravi, V.K.2
Swaminathan, R.3
-
53
-
-
84900300867
-
On the characterization of intermediates in the isodesmic aggregation pathway of hen lysozyme at alkaline pH
-
V.K. Ravi, T. Swain, N. Chandra, and R. Swaminathan On the characterization of intermediates in the isodesmic aggregation pathway of hen lysozyme at alkaline pH PLoS ONE 9 2014 e87256
-
(2014)
PLoS ONE
, vol.9
, pp. 87256
-
-
Ravi, V.K.1
Swain, T.2
Chandra, N.3
Swaminathan, R.4
-
54
-
-
77949990336
-
Identification and characterization of molten globule state of hen egg white lysozyme in presence of salts under alkaline conditions
-
M.A. Ansari, S. Zubair, S.M. Atif, M. Kashif, N. Khan, M. Rehan, T. Anwar, A. Iqbal, and M. Owais Identification and characterization of molten globule state of hen egg white lysozyme in presence of salts under alkaline conditions Protein Pept. Lett. 17 2010 11 17
-
(2010)
Protein Pept. Lett.
, vol.17
, pp. 11-17
-
-
Ansari, M.A.1
Zubair, S.2
Atif, S.M.3
Kashif, M.4
Khan, N.5
Rehan, M.6
Anwar, T.7
Iqbal, A.8
Owais, M.9
-
55
-
-
79251538929
-
Crowding alone cannot account for cosolute effect on amyloid aggregation
-
S. Sukenik, R. Politi, L. Ziserman, D. Danino, A. Friedler, and D. Harries Crowding alone cannot account for cosolute effect on amyloid aggregation PLoS ONE 6 2011 e15608
-
(2011)
PLoS ONE
, vol.6
, pp. 15608
-
-
Sukenik, S.1
Politi, R.2
Ziserman, L.3
Danino, D.4
Friedler, A.5
Harries, D.6
-
56
-
-
84860446148
-
The contrasting effect of macromolecular crowding on amyloid fibril formation
-
Q. Ma, J.B. Fan, Z. Zhou, B.R. Zhou, S.R. Meng, J.Y. Hu, J. Chen, and Y. Liang The contrasting effect of macromolecular crowding on amyloid fibril formation PLoS One 7 2012 e36288
-
(2012)
PLoS One
, vol.7
, pp. 36288
-
-
Ma, Q.1
Fan, J.B.2
Zhou, Z.3
Zhou, B.R.4
Meng, S.R.5
Hu, J.Y.6
Chen, J.7
Liang, Y.8
-
58
-
-
0033969150
-
Implications of macromolecular crowding for protein assembly
-
DOI 10.1016/S0959-440X(99)00045-7
-
A.P. Minton Implications of macromolecular crowding for protein assembly Curr. Opin. Struct. Biol. 10 2000 34 39 (Pubitemid 30099324)
-
(2000)
Current Opinion in Structural Biology
, vol.10
, Issue.1
, pp. 34-39
-
-
Minton, A.P.1
-
59
-
-
84872370305
-
Macromolecular crowding modulates the kinetics and morphology of amyloid self-assembly by β-lactoglobulin
-
B. Ma, J. Xie, L. Wei, and W. Li Macromolecular crowding modulates the kinetics and morphology of amyloid self-assembly by β-lactoglobulin Int. J. Biol. Macromol. 53 2013 82 87
-
(2013)
Int. J. Biol. Macromol.
, vol.53
, pp. 82-87
-
-
Ma, B.1
Xie, J.2
Wei, L.3
Li, W.4
-
60
-
-
84861998164
-
Effect of polyethylene glycols on the alkaline-induced molten globule intermediate of bovine serum albumin
-
P. Qu, Y. Wang, G. Wu, Z. Lu, and M. Xu Effect of polyethylene glycols on the alkaline-induced molten globule intermediate of bovine serum albumin Int. J. Biol. Macromol. 51 2012 97 104
-
(2012)
Int. J. Biol. Macromol.
, vol.51
, pp. 97-104
-
-
Qu, P.1
Wang, Y.2
Wu, G.3
Lu, Z.4
Xu, M.5
-
61
-
-
84861965219
-
Fibrillation of hen egg white lysozyme triggers reduction of Copper(II)
-
S. Ghosh, N.K. Pandey, S. Bhattacharya, A. Roy, and S. Dasgupta Fibrillation of hen egg white lysozyme triggers reduction of Copper(II) Int. J. Biol. Macromol. 51 2012 1 6
-
(2012)
Int. J. Biol. Macromol.
, vol.51
, pp. 1-6
-
-
Ghosh, S.1
Pandey, N.K.2
Bhattacharya, S.3
Roy, A.4
Dasgupta, S.5
-
62
-
-
84871664742
-
(-)-Epicatechin gallate prevents alkali-salt mediated fibrillogenesis of hen egg white lysozyme
-
S. Ghosh, N.K. Pandey, and S. Dasgupta (-)-Epicatechin gallate prevents alkali-salt mediated fibrillogenesis of hen egg white lysozyme Int. J. Biol. Macromol. 54 2013 90 98
-
(2013)
Int. J. Biol. Macromol.
, vol.54
, pp. 90-98
-
-
Ghosh, S.1
Pandey, N.K.2
Dasgupta, S.3
-
63
-
-
0028871804
-
How to measure and predict the molar absorption coefficient of a protein
-
C.N. Pace, F. Vajdos, L. Fee, G. Grimsley, and T. Gray How to measure and predict the molar absorption coefficient of a protein Protein Sci. 4 1995 2411 2423
-
(1995)
Protein Sci.
, vol.4
, pp. 2411-2423
-
-
Pace, C.N.1
Vajdos, F.2
Fee, L.3
Grimsley, G.4
Gray, T.5
-
64
-
-
0024509805
-
Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T
-
DOI 10.1016/0003-2697(89)90046-8
-
H. Naiki, K. Higuchi, M. Hosokawa, and T. Takeda Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1 Anal. Biochem. 177 1989 244 249 (Pubitemid 19088253)
-
(1989)
Analytical Biochemistry
, vol.177
, Issue.2
, pp. 244-249
-
-
Naiki, H.1
Higuchi, K.2
Hosokawa, M.3
Takeda, T.4
-
65
-
-
58149326746
-
Molecular mechanism of thioflavin-T binding to the surface of beta-rich peptide self-assemblies
-
M. Biancalana, K. Makabe, A. Koide, and S. Koide Molecular mechanism of thioflavin-T binding to the surface of beta-rich peptide self-assemblies J. Mol. Biol. 385 2009 1052 1063
-
(2009)
J. Mol. Biol.
, vol.385
, pp. 1052-1063
-
-
Biancalana, M.1
Makabe, K.2
Koide, A.3
Koide, S.4
-
66
-
-
77449100085
-
Formation of amyloid fibrils in vitro from partially unfolded intermediates of human gammaC-crystallin
-
Y. Wang, S. Petty, A. Trojanowski, K. Knee, D. Goulet, I. Mukerji, and J. King Formation of amyloid fibrils in vitro from partially unfolded intermediates of human gammaC-crystallin Invest. Ophthalmol. Vis. Sci. 51 2010 672 678
-
(2010)
Invest. Ophthalmol. Vis. Sci.
, vol.51
, pp. 672-678
-
-
Wang, Y.1
Petty, S.2
Trojanowski, A.3
Knee, K.4
Goulet, D.5
Mukerji, I.6
King, J.7
-
67
-
-
3242877618
-
DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
-
L. Whitmore, and B.A. Wallace DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data Nucleic Acids Res. 32 2004 W668 W673
-
(2004)
Nucleic Acids Res.
, vol.32
-
-
Whitmore, L.1
Wallace, B.A.2
-
68
-
-
0022691315
-
Examination of the secondary structure of proteins by deconvolved FTIR spectra
-
D.M. Byler, and H. Susi Examination of the secondary structure of proteins by deconvolved FTIR spectra Biopolymers 25 1986 469 487
-
(1986)
Biopolymers
, vol.25
, pp. 469-487
-
-
Byler, D.M.1
Susi, H.2
-
69
-
-
34247124903
-
The measurement of lysozyme activity and the ultra-violet inactivation of lysozyme
-
D. Shugar The measurement of lysozyme activity and the ultra-violet inactivation of lysozyme Biochim. Biophys. Acta 8 1952 302 309
-
(1952)
Biochim. Biophys. Acta
, vol.8
, pp. 302-309
-
-
Shugar, D.1
-
70
-
-
34548417549
-
Transition of a compact intermediate state of pea lectin under the influence of different molecular weight polyethylene glycols
-
DOI 10.1007/s10930-007-9081-4
-
F. Naseem, and R.H. Khan Transition of a compact intermediate state of pea lectin under the influence of different molecular weight polyethylene glycols Protein J. 26 2007 415 421 (Pubitemid 47351810)
-
(2007)
Protein Journal
, vol.26
, Issue.6
, pp. 415-421
-
-
Naseem, F.1
Khan, R.H.2
-
72
-
-
0347994108
-
Protein folding by the effects of macromolecular crowding
-
DOI 10.1110/ps.03288104
-
N. Tokuriki, M. Kinjo, S. Negi, M. Hoshino, Y. Goto, I. Urabe, and T. Yomo Protein folding by the effects of macromolecular crowding Protein Sci. 13 2004 125 133 (Pubitemid 38021147)
-
(2004)
Protein Science
, vol.13
, Issue.1
, pp. 125-133
-
-
Tokuriki, N.1
Kinjo, M.2
Negi, S.3
Hoshino, M.4
Goto, Y.5
Urabe, I.6
Yomo, T.7
-
73
-
-
1842426531
-
Effects of polyethylene glycol on stability of α-chymotrypsin in aqueous ethanol solvent
-
DOI 10.1016/j.bbrc.2004.03.087, PII S0006291X04005807
-
L.M. Simon, M. Kotorman, A. Szabo, G. Garab, and I. Laczko Effects of polyethylene glycol on stability of alpha-chymotrypsin in aqueous ethanol solvent Biochem. Biophys. Res. Commun. 317 2004 610 613 (Pubitemid 38452526)
-
(2004)
Biochemical and Biophysical Research Communications
, vol.317
, Issue.2
, pp. 610-613
-
-
Simon, L.M.1
Kotorman, M.2
Szabo, A.3
Garab, G.4
Laczko, I.5
-
74
-
-
11144248639
-
Biochemical effects of molecular crowding
-
DOI 10.1007/s10541-005-0070-y
-
N.A. Chebotareva, B.I. Kurganov, and N.B. Livanova Biochemical effects of molecular crowding Biochemistry (Mosc). 69 2004 1239 1251 (Pubitemid 40050043)
-
(2004)
Biochemistry (Moscow)
, vol.69
, Issue.11
, pp. 1239-1251
-
-
Chebotareva, N.A.1
Kurganov, B.I.2
Livanova, N.B.3
-
75
-
-
84868325436
-
Combined effects of agitation, macromolecular crowding, and interfaces on amyloidogenesis
-
C.F. Lee, S. Bird, M. Shaw, L. Jean, and D.J. Vaux Combined effects of agitation, macromolecular crowding, and interfaces on amyloidogenesis J. Biol. Chem. 287 2012 38006 38019
-
(2012)
J. Biol. Chem.
, vol.287
, pp. 38006-38019
-
-
Lee, C.F.1
Bird, S.2
Shaw, M.3
Jean, L.4
Vaux, D.J.5
-
76
-
-
0344665699
-
Relationship between the protein surface hydrophobicity and its partitioning behaviour in aqueous two-phase systems of polyethyleneglycol- dextran
-
DOI 10.1016/j.jchromb.2003.10.060
-
G. Tubio, B. Nerli, and G. Picó Relationship between the protein surface hydrophobicity and its partitioning behaviour in aqueous two-phase, systems of polyethyleneglycol-dextran J. Chromatogr. B 799 2004 293 301 (Pubitemid 37510232)
-
(2004)
Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
, vol.799
, Issue.2
, pp. 293-301
-
-
Tubio, G.1
Nerli, B.2
Pico, G.3
-
77
-
-
0026096545
-
Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe
-
G.V. Semisotnov, N.A. Rodionova, O.I. Razgulyaev, V.N. Uversky, A.F. Gripas, and R.I. Gilmanshin Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe Biopolymers 31 1991 119 128
-
(1991)
Biopolymers
, vol.31
, pp. 119-128
-
-
Semisotnov, G.V.1
Rodionova, N.A.2
Razgulyaev, O.I.3
Uversky, V.N.4
Gripas, A.F.5
Gilmanshin, R.I.6
-
78
-
-
0035812658
-
Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis
-
DOI 10.1006/jmbi.2001.4970
-
M.D. Kirkitadze, M.M. Condron, and D.B. Teplow Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis J. Mol. Biol. 312 2001 1103 1119 (Pubitemid 32980329)
-
(2001)
Journal of Molecular Biology
, vol.312
, Issue.5
, pp. 1103-1119
-
-
Kirkitadze, M.D.1
Condron, M.M.2
Teplow, D.B.3
-
79
-
-
84876491523
-
Parallel β-sheet fibril and antiparallel β-sheet oligomer: New insights into amyloid formation of hen egg white lysozyme under heat and acidic condition from FTIR spectroscopy
-
Y. Zou, Y. Li, W. Hao, X. Hu, and G. Ma Parallel β-sheet fibril and antiparallel β-sheet oligomer: new insights into amyloid formation of hen egg white lysozyme under heat and acidic condition from FTIR spectroscopy J. Phys. Chem. B. 117 2013 4003 4013
-
(2013)
J. Phys. Chem. B.
, vol.117
, pp. 4003-4013
-
-
Zou, Y.1
Li, Y.2
Hao, W.3
Hu, X.4
Ma, G.5
-
80
-
-
61849106912
-
Formation and dissolution of hen egg white lysozyme amyloid fibrils in protic ionic liquids
-
N. Byrne, and C.A. Angell Formation and dissolution of hen egg white lysozyme amyloid fibrils in protic ionic liquids Chem. Commun. 2009 1046 1048
-
(2009)
Chem. Commun.
, pp. 1046-1048
-
-
Byrne, N.1
Angell, C.A.2
-
81
-
-
33646154457
-
Modulation of protein aggregation by polyethylene glycol conjugation: GCSF as a case study
-
R.S. Rajan, T. Li, M. Aras, C. Sloey, W. Sutherland, H. Arai, R. Briddell, O. Kinstler, A.M. Lueras, Y. Zhang, H. Yeghnazar, M. Treuheit, and D.N. Brems Modulation of protein aggregation by polyethylene glycol conjugation: GCSF as a case study Protein Sci. 15 2006 1063 1075
-
(2006)
Protein Sci.
, vol.15
, pp. 1063-1075
-
-
Rajan, R.S.1
Li, T.2
Aras, M.3
Sloey, C.4
Sutherland, W.5
Arai, H.6
Briddell, R.7
Kinstler, O.8
Lueras, A.M.9
Zhang, Y.10
Yeghnazar, H.11
Treuheit, M.12
Brems, D.N.13
-
82
-
-
84859608007
-
Light scattering studies of hydration and structural transformations of lysozyme
-
A. Szymanska, and G. Slosarek Light scattering studies of hydration and structural transformations of lysozyme Acta Phys. Pol., A 121 2012 694 698
-
(2012)
Acta Phys. Pol., A
, vol.121
, pp. 694-698
-
-
Szymanska, A.1
Slosarek, G.2
-
83
-
-
79955922159
-
Comparative analysis of viscosity of complex liquids and cytoplasmof mammalian cells at the nanoscale
-
T. Kalwarczyk, N. Ziebacz, A. Bielejewska, E. Zaboklicka, K. Koynov, J. Szymanski, A. Wilk, A. Patkowski, J. Gapinski, H.J. Butt, and R. Holyst Comparative analysis of viscosity of complex liquids and cytoplasmof mammalian cells at the nanoscale Nano Lett. 11 2011 2157 2163
-
(2011)
Nano Lett.
, vol.11
, pp. 2157-2163
-
-
Kalwarczyk, T.1
Ziebacz, N.2
Bielejewska, A.3
Zaboklicka, E.4
Koynov, K.5
Szymanski, J.6
Wilk, A.7
Patkowski, A.8
Gapinski, J.9
Butt, H.J.10
Holyst, R.11
-
84
-
-
84880844306
-
Macromolecular crowding as a suppressor of human IAPP fibril formation and cytotoxicity
-
J. Seeliger, A. Werkmüller, and R. Winter Macromolecular crowding as a suppressor of human IAPP fibril formation and cytotoxicity PLoS ONE 8 2013 e69652
-
(2013)
PLoS ONE
, vol.8
, pp. 69652
-
-
Seeliger, J.1
Werkmüller, A.2
Winter, R.3
-
85
-
-
67651098677
-
Aggregation of amyloidogenic peptides near hydrophobic and hydrophilic surfaces
-
I. Brovchenko, G. Singh, and R. Winter Aggregation of amyloidogenic peptides near hydrophobic and hydrophilic surfaces Langmuir 25 2009 8111 8116
-
(2009)
Langmuir
, vol.25
, pp. 8111-8116
-
-
Brovchenko, I.1
Singh, G.2
Winter, R.3
|