-
1
-
-
0347357617
-
Protein folding and misfolding
-
DOI 10.1038/nature02261
-
C.M. Dobson Protein folding and misfolding Nature 426 2003 884 890 (Pubitemid 38056880)
-
(2003)
Nature
, vol.426
, Issue.6968
, pp. 884-890
-
-
Dobson, C.M.1
-
2
-
-
84867680187
-
A calorimetric approach with structure-based thermodynamics for molecular interactions
-
Y.H. Lee, S. Kume, T. Inui, and Y. Goto A calorimetric approach with structure-based thermodynamics for molecular interactions Netsu Sokutei 38 2011 165 173
-
(2011)
Netsu Sokutei
, vol.38
, pp. 165-173
-
-
Lee, Y.H.1
Kume, S.2
Inui, T.3
Goto, Y.4
-
3
-
-
65849165676
-
Competition between intramolecular and intermolecular interactions in an amyloid-forming protein
-
K.E. Routledge, G.G. Tartaglia, G.W. Platt, M. Vendruscolo, and S.E. Radford Competition between intramolecular and intermolecular interactions in an amyloid-forming protein J. Mol. Biol. 389 2009 776 786
-
(2009)
J. Mol. Biol.
, vol.389
, pp. 776-786
-
-
Routledge, K.E.1
Tartaglia, G.G.2
Platt, G.W.3
Vendruscolo, M.4
Radford, S.E.5
-
4
-
-
34547378641
-
Dimethylsulfoxide-quenched hydrogen/deuterium exchange method to study amyloid fibril structure
-
DOI 10.1016/j.bbamem.2007.03.001, PII S0005273607000703
-
M. Hoshino, H. Katou, K. Yamaguchi, and Y. Goto Dimethylsulfoxide- quenched hydrogen/deuterium exchange method to study amyloid fibril structure Biochim. Biophys. Acta 1768 2007 1886 1899 (Pubitemid 47135569)
-
(2007)
Biochimica et Biophysica Acta - Biomembranes
, vol.1768
, Issue.8
, pp. 1886-1899
-
-
Hoshino, M.1
Katou, H.2
Yamaguchi, K.-i.3
Goto, Y.4
-
5
-
-
27744505831
-
2- microglobulin in comparison with its native fold
-
DOI 10.1016/j.bbapap.2005.08.002, PII S1570963905002530, Dialysis-related Amyloidosis: from Molecular Mechanisms to Therapies
-
E. Chatani, and Y. Goto Structural stability of amyloid fibrils of beta(2)-microglobulin in comparison with its native fold Biochim. Biophys. Acta 1753 2005 64 75 (Pubitemid 41597432)
-
(2005)
Biochimica et Biophysica Acta - Proteins and Proteomics
, vol.1753
, Issue.1
, pp. 64-75
-
-
Chatani, E.1
Goto, Y.2
-
6
-
-
59649087258
-
Structure, formation and propagation of amyloid fibrils
-
Y. Goto, H. Yagi, K. Yamaguchi, E. Chatani, and T. Ban Structure, formation and propagation of amyloid fibrils Curr. Pharm. Des. 14 2008 3205 3218
-
(2008)
Curr. Pharm. Des.
, vol.14
, pp. 3205-3218
-
-
Goto, Y.1
Yagi, H.2
Yamaguchi, K.3
Chatani, E.4
Ban, T.5
-
7
-
-
34247882072
-
Life on the edge: A link between gene expression levels and aggregation rates of human proteins
-
DOI 10.1016/j.tibs.2007.03.005, PII S0968000407000618
-
G.G. Tartaglia, S. Pechmann, C.M. Dobson, and M. Vendruscolo Life on the edge: a link between gene expression levels and aggregation rates of human proteins Trends Biochem. Sci. 32 2007 204 206 (Pubitemid 46694330)
-
(2007)
Trends in Biochemical Sciences
, vol.32
, Issue.5
, pp. 204-206
-
-
Tartaglia, G.G.1
Pechmann, S.2
Dobson, C.M.3
Vendruscolo, M.4
-
8
-
-
77951887037
-
Low-level expression of a folding-incompetent protein in Escherichia coli: Search for the molecular determinants of protein aggregation in vivo
-
J. Winkelmann, G. Calloni, S. Campioni, B. Mannini, N. Taddei, and F. Chiti Low-level expression of a folding-incompetent protein in Escherichia coli: search for the molecular determinants of protein aggregation in vivo J. Mol. Biol. 398 2010 600 613
-
(2010)
J. Mol. Biol.
, vol.398
, pp. 600-613
-
-
Winkelmann, J.1
Calloni, G.2
Campioni, S.3
Mannini, B.4
Taddei, N.5
Chiti, F.6
-
9
-
-
79959865248
-
Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions
-
K. Yanagi, M. Ashizaki, H. Yagi, K. Sakurai, Y.H. Lee, and Y. Goto Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions J. Biol. Chem. 286 2011 23959 23966
-
(2011)
J. Biol. Chem.
, vol.286
, pp. 23959-23966
-
-
Yanagi, K.1
Ashizaki, M.2
Yagi, H.3
Sakurai, K.4
Lee, Y.H.5
Goto, Y.6
-
10
-
-
33746377894
-
Protein misfolding, functional amyloid, and human disease
-
DOI 10.1146/annurev.biochem.75.101304.123901
-
F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366 (Pubitemid 44118036)
-
(2006)
Annual Review of Biochemistry
, vol.75
, pp. 333-366
-
-
Chiti, F.1
Dobson, C.M.2
-
11
-
-
55249087467
-
Immunological features of alpha-synuclein in Parkinson's disease
-
C. Roodveldt, J. Christodoulou, and C.M. Dobson Immunological features of alpha-synuclein in Parkinson's disease J. Cell. Mol. Med. 12 2008 1820 1829
-
(2008)
J. Cell. Mol. Med.
, vol.12
, pp. 1820-1829
-
-
Roodveldt, C.1
Christodoulou, J.2
Dobson, C.M.3
-
12
-
-
83055176454
-
Atomic-resolution dynamics on the surface of amyloid-beta protofibrils probed by solution NMR
-
N.L. Fawzi, J. Ying, R. Ghirlando, D.A. Torchia, and G.M. Clore Atomic-resolution dynamics on the surface of amyloid-beta protofibrils probed by solution NMR Nature 480 2011 268 272
-
(2011)
Nature
, vol.480
, pp. 268-272
-
-
Fawzi, N.L.1
Ying, J.2
Ghirlando, R.3
Torchia, D.A.4
Clore, G.M.5
-
13
-
-
77749308383
-
Amyloid oligomers: Spectroscopic characterization of amyloidogenic protein states
-
M. Lindgren, and P. Hammarstrom Amyloid oligomers: spectroscopic characterization of amyloidogenic protein states FEBS J. 277 2010 1380 1388
-
(2010)
FEBS J.
, vol.277
, pp. 1380-1388
-
-
Lindgren, M.1
Hammarstrom, P.2
-
14
-
-
77954358960
-
Mysterious oligomerization of the amyloidogenic proteins
-
V.N. Uversky Mysterious oligomerization of the amyloidogenic proteins FEBS J. 277 2010 2940 2953
-
(2010)
FEBS J.
, vol.277
, pp. 2940-2953
-
-
Uversky, V.N.1
-
15
-
-
84863229747
-
Atomic view of a toxic amyloid small oligomer
-
A. Laganowsky, C. Liu, M.R. Sawaya, J.P. Whitelegge, J. Park, M. Zhao, A. Pensalfini, A.B. Soriaga, M. Landau, P.K. Teng, D. Cascio, C. Glabe, and D. Eisenberg Atomic view of a toxic amyloid small oligomer Science 335 2012 1228 1231
-
(2012)
Science
, vol.335
, pp. 1228-1231
-
-
Laganowsky, A.1
Liu, C.2
Sawaya, M.R.3
Whitelegge, J.P.4
Park, J.5
Zhao, M.6
Pensalfini, A.7
Soriaga, A.B.8
Landau, M.9
Teng, P.K.10
Cascio, D.11
Glabe, C.12
Eisenberg, D.13
-
16
-
-
79251631002
-
Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to beta-sheet in amyloid fibril formation
-
C. Bleiholder, N.F. Dupuis, T. Wyttenbach, and M.T. Bowers Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to beta-sheet in amyloid fibril formation Nat. Chem. 3 2010 172 177
-
(2010)
Nat. Chem.
, vol.3
, pp. 172-177
-
-
Bleiholder, C.1
Dupuis, N.F.2
Wyttenbach, T.3
Bowers, M.T.4
-
17
-
-
57749098600
-
Amyloid formation by globular proteins under native conditions
-
F. Chiti, and C.M. Dobson Amyloid formation by globular proteins under native conditions Nat. Chem. Biol. 5 2009 15 22
-
(2009)
Nat. Chem. Biol.
, vol.5
, pp. 15-22
-
-
Chiti, F.1
Dobson, C.M.2
-
18
-
-
68649110959
-
Bridging the gap: From protein misfolding to protein misfolding diseases
-
L.M. Luheshi, and C.M. Dobson Bridging the gap: from protein misfolding to protein misfolding diseases FEBS Lett. 583 2009 2581 2586
-
(2009)
FEBS Lett.
, vol.583
, pp. 2581-2586
-
-
Luheshi, L.M.1
Dobson, C.M.2
-
19
-
-
77955682352
-
Structure and intermolecular dynamics of aggregates populated during amyloid fibril formation studied by hydrogen/deuterium exchange
-
N. Carulla, M. Zhou, E. Giralt, C.V. Robinson, and C.M. Dobson Structure and intermolecular dynamics of aggregates populated during amyloid fibril formation studied by hydrogen/deuterium exchange Acc. Chem. Res. 43 2010 1072 1079
-
(2010)
Acc. Chem. Res.
, vol.43
, pp. 1072-1079
-
-
Carulla, N.1
Zhou, M.2
Giralt, E.3
Robinson, C.V.4
Dobson, C.M.5
-
20
-
-
3342906956
-
Fibrillation of carrier protein albebetin and its biologically active constructs. Multiple oligomeric intermediates and pathways
-
DOI 10.1021/bi0494121
-
L.A. Morozova-Roche, V. Zamotin, M. Malisauskas, A. Ohman, R. Chertkova, M.A. Lavrikova, I.A. Kostanyan, D.A. Dolgikh, and M.P. Kirpichnikov Fibrillation of carrier protein albebetin and its biologically active constructs. Multiple oligomeric intermediates and pathways Biochemistry 43 2004 9610 9619 (Pubitemid 38993811)
-
(2004)
Biochemistry
, vol.43
, Issue.30
, pp. 9610-9619
-
-
Morozova-Roche, L.A.1
Zamotin, V.2
Malisauskas, M.3
Ohman, A.4
Chertkova, R.5
Lavrikova, M.A.6
Kostanyan, I.A.7
Dolgikh, D.A.8
Kirpichnikov, M.P.9
-
21
-
-
77957782470
-
Biology of amyloid: Structure, function, and regulation
-
J. Greenwald, and R. Riek Biology of amyloid: structure, function, and regulation Structure 18 2010 1244 1260
-
(2010)
Structure
, vol.18
, pp. 1244-1260
-
-
Greenwald, J.1
Riek, R.2
-
22
-
-
67650809307
-
Functional amyloids as natural storage of peptide hormones in pituitary secretory granules
-
S.K. Maji, M.H. Perrin, M.R. Sawaya, S. Jessberger, K. Vadodaria, R.A. Rissman, P.S. Singru, K.P. Nilsson, R. Simon, D. Schubert, D. Eisenberg, J. Rivier, P. Sawchenko, W. Vale, and R. Riek Functional amyloids as natural storage of peptide hormones in pituitary secretory granules Science 325 2009 328 332
-
(2009)
Science
, vol.325
, pp. 328-332
-
-
Maji, S.K.1
Perrin, M.H.2
Sawaya, M.R.3
Jessberger, S.4
Vadodaria, K.5
Rissman, R.A.6
Singru, P.S.7
Nilsson, K.P.8
Simon, R.9
Schubert, D.10
Eisenberg, D.11
Rivier, J.12
Sawchenko, P.13
Vale, W.14
Riek, R.15
-
23
-
-
31144460030
-
Functional amyloid formation within mammalian tissue
-
D.M. Fowler, A.V. Koulov, C. Alory-Jost, M.S. Marks, W.E. Balch, and J.W. Kelly Functional amyloid formation within mammalian tissue PLoS Biol. 4 2006 e6
-
(2006)
PLoS Biol.
, vol.4
, pp. 6
-
-
Fowler, D.M.1
Koulov, A.V.2
Alory-Jost, C.3
Marks, M.S.4
Balch, W.E.5
Kelly, J.W.6
-
24
-
-
34250305540
-
Amyloidogenesis of type III-dependent harpins from plant pathogenic bacteria
-
DOI 10.1074/jbc.M602576200
-
J. Oh, J.G. Kim, E. Jeon, C.H. Yoo, J.S. Moon, S. Rhee, and I. Hwang Amyloidogenesis of type III-dependent harpins from plant pathogenic bacteria J. Biol. Chem. 282 2007 13601 13609 (Pubitemid 47100514)
-
(2007)
Journal of Biological Chemistry
, vol.282
, Issue.18
, pp. 13601-13609
-
-
Oh, J.1
Kim, J.-G.2
Jeon, E.3
Yoo, C.-H.4
Jae, S.M.5
Rhee, S.6
Hwang, I.7
-
25
-
-
40149111861
-
Amyloid as a depot for the formulation of long-acting drugs
-
S.K. Maji, D. Schubert, C. Rivier, S. Lee, J.E. Rivier, and R. Riek Amyloid as a depot for the formulation of long-acting drugs PLoS Biol. 6 2008 e17
-
(2008)
PLoS Biol.
, vol.6
, pp. 17
-
-
Maji, S.K.1
Schubert, D.2
Rivier, C.3
Lee, S.4
Rivier, J.E.5
Riek, R.6
-
26
-
-
38749119393
-
Functionalised amyloid fibrils for roles in cell adhesion
-
S.L. Gras, A.K. Tickler, A.M. Squires, G.L. Devlin, M.A. Horton, C.M. Dobson, and C.E. MacPhee Functionalised amyloid fibrils for roles in cell adhesion Biomaterials 29 2008 1553 1562
-
(2008)
Biomaterials
, vol.29
, pp. 1553-1562
-
-
Gras, S.L.1
Tickler, A.K.2
Squires, A.M.3
Devlin, G.L.4
Horton, M.A.5
Dobson, C.M.6
MacPhee, C.E.7
-
27
-
-
84858074134
-
Short self-assembling peptides as building blocks for modern nanodevices
-
A. Lakshmanan, S. Zhang, and C.A. Hauser Short self-assembling peptides as building blocks for modern nanodevices Trends Biotechnol. 30 2012 155 165
-
(2012)
Trends Biotechnol.
, vol.30
, pp. 155-165
-
-
Lakshmanan, A.1
Zhang, S.2
Hauser, C.A.3
-
28
-
-
51349143098
-
Label-free detection of amyloid growth with microcantilever sensors
-
T.P. Knowles, W. Shu, F. Huber, H.P. Lang, C. Gerber, C.M. Dobson, and M.E. Welland Label-free detection of amyloid growth with microcantilever sensors Nanotechnology 19 2008 384007
-
(2008)
Nanotechnology
, vol.19
, pp. 384007
-
-
Knowles, T.P.1
Shu, W.2
Huber, F.3
Lang, H.P.4
Gerber, C.5
Dobson, C.M.6
Welland, M.E.7
-
29
-
-
77649240855
-
Identifying the amylome, proteins capable of forming amyloid-like fibrils
-
L. Goldschmidt, P.K. Teng, R. Riek, and D. Eisenberg Identifying the amylome, proteins capable of forming amyloid-like fibrils Proc. Natl. Acad. Sci. U. S. A. 107 2010 3487 3492
-
(2010)
Proc. Natl. Acad. Sci. U. S. A.
, vol.107
, pp. 3487-3492
-
-
Goldschmidt, L.1
Teng, P.K.2
Riek, R.3
Eisenberg, D.4
-
30
-
-
78651468727
-
Conformational conversion during amyloid formation at atomic resolution
-
T. Eichner, A.P. Kalverda, G.S. Thompson, S.W. Homans, and S.E. Radford Conformational conversion during amyloid formation at atomic resolution Mol. Cell 41 2011 161 172
-
(2011)
Mol. Cell
, vol.41
, pp. 161-172
-
-
Eichner, T.1
Kalverda, A.P.2
Thompson, G.S.3
Homans, S.W.4
Radford, S.E.5
-
31
-
-
79959887638
-
A diversity of assembly mechanisms of a generic amyloid fold
-
T. Eichner, and S.E. Radford A diversity of assembly mechanisms of a generic amyloid fold Mol. Cell 43 2011 8 18
-
(2011)
Mol. Cell
, vol.43
, pp. 8-18
-
-
Eichner, T.1
Radford, S.E.2
-
32
-
-
80053596817
-
Understanding the complex mechanisms of beta2-microglobulin amyloid assembly
-
T. Eichner, and S.E. Radford Understanding the complex mechanisms of beta2-microglobulin amyloid assembly FEBS J. 278 2011 3868 3883
-
(2011)
FEBS J.
, vol.278
, pp. 3868-3883
-
-
Eichner, T.1
Radford, S.E.2
-
33
-
-
16244398884
-
2-microglobulin trapped by non-native prolyl peptide bond
-
DOI 10.1016/j.jmb.2005.02.050
-
A. Kameda, M. Hoshino, T. Higurashi, S. Takahashi, H. Naiki, and Y. Goto Nuclear magnetic resonance characterization of the refolding intermediate of beta2-microglobulin trapped by non-native prolyl peptide bond J. Mol. Biol. 348 2005 383 397 (Pubitemid 40462103)
-
(2005)
Journal of Molecular Biology
, vol.348
, Issue.2
, pp. 383-397
-
-
Kameda, A.1
Hoshino, M.2
Higurashi, T.3
Takahashi, S.4
Naiki, H.5
Goto, Y.6
-
34
-
-
67749124075
-
NMR-based characterization of a refolding intermediate of beta2-microglobulin labeled using a wheat germ cell-free system
-
A. Kameda, E.H. Morita, K. Sakurai, H. Naiki, and Y. Goto NMR-based characterization of a refolding intermediate of beta2-microglobulin labeled using a wheat germ cell-free system Protein Sci. 18 2009 1592 1601
-
(2009)
Protein Sci.
, vol.18
, pp. 1592-1601
-
-
Kameda, A.1
Morita, E.H.2
Sakurai, K.3
Naiki, H.4
Goto, Y.5
-
35
-
-
51549116627
-
Kinetic coupling of folding and prolyl isomerization of beta2-microglobulin studied by mutational analysis
-
M. Sakata, E. Chatani, A. Kameda, K. Sakurai, H. Naiki, and Y. Goto Kinetic coupling of folding and prolyl isomerization of beta2-microglobulin studied by mutational analysis J. Mol. Biol. 382 2008 1242 1255
-
(2008)
J. Mol. Biol.
, vol.382
, pp. 1242-1255
-
-
Sakata, M.1
Chatani, E.2
Kameda, A.3
Sakurai, K.4
Naiki, H.5
Goto, Y.6
-
36
-
-
33644813233
-
A native to amyloidogenic transition regulated by a backbone trigger
-
DOI 10.1038/nsmb1068, PII N1068
-
C.M. Eakin, A.J. Berman, and A.D. Miranker A native to amyloidogenic transition regulated by a backbone trigger Nat. Struct. Mol. Biol. 13 2006 202 208 (Pubitemid 43348505)
-
(2006)
Nature Structural and Molecular Biology
, vol.13
, Issue.3
, pp. 202-208
-
-
Eakin, C.M.1
Berman, A.J.2
Miranker, A.D.3
-
37
-
-
0035861649
-
A partially structured species of beta 2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis
-
F. Chiti, E. De Lorenzi, S. Grossi, P. Mangione, S. Giorgetti, G. Caccialanza, C.M. Dobson, G. Merlini, G. Ramponi, and V. Bellotti A partially structured species of beta 2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis J. Biol. Chem. 276 2001 46714 46721
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 46714-46721
-
-
Chiti, F.1
De Lorenzi, E.2
Grossi, S.3
Mangione, P.4
Giorgetti, S.5
Caccialanza, G.6
Dobson, C.M.7
Merlini, G.8
Ramponi, G.9
Bellotti, V.10
-
38
-
-
33144467755
-
Amyloid formation under physiological conditions proceeds via a native-like folding intermediate
-
DOI 10.1038/nsmb1058, PII N1058
-
T.R. Jahn, M.J. Parker, S.W. Homans, and S.E. Radford Amyloid formation under physiological conditions proceeds via a native-like folding intermediate Nat. Struct. Mol. Biol. 13 2006 195 201 (Pubitemid 43348504)
-
(2006)
Nature Structural and Molecular Biology
, vol.13
, Issue.3
, pp. 195-201
-
-
Jahn, T.R.1
Parker, M.J.2
Homans, S.W.3
Radford, S.E.4
-
39
-
-
27744437192
-
From chance to frequent encounters: Origins of β2-microglobulin fibrillogenesis
-
DOI 10.1016/j.bbapap.2005.09.002, PII S1570963905003286, Dialysis-related Amyloidosis: from Molecular Mechanisms to Therapies
-
C.M. Eakin, and A.D. Miranker From chance to frequent encounters: origins of beta2-microglobulin fibrillogenesis Biochim. Biophys. Acta 1753 2005 92 99 (Pubitemid 41597435)
-
(2005)
Biochimica et Biophysica Acta - Proteins and Proteomics
, vol.1753
, Issue.1
, pp. 92-99
-
-
Eakin, C.M.1
Miranker, A.D.2
-
41
-
-
1342289275
-
2- microglobulin upon copper binding: A possible role for copper in dialysis-related amyloidosis
-
DOI 10.1110/ps.03445704
-
J. Villanueva, M. Hoshino, H. Katou, J. Kardos, K. Hasegawa, H. Naiki, and Y. Goto Increase in the conformational flexibility of beta 2-microglobulin upon copper binding: a possible role for copper in dialysis-related amyloidosis Protein Sci. 13 2004 797 809 (Pubitemid 38252576)
-
(2004)
Protein Science
, vol.13
, Issue.3
, pp. 797-809
-
-
Villanueva, J.1
Hoshino, M.2
Katou, H.3
Kardos, J.4
Hasegawa, K.5
Naiki, H.6
Goto, Y.7
-
42
-
-
0034254241
-
Partially unfolded states of β-microglobulin and amyloid formation in vitro
-
DOI 10.1021/bi000276j
-
V.J. McParland, N.M. Kad, A.P. Kalverda, A. Brown, P. Kirwin-Jones, M.G. Hunter, M. Sunde, and S.E. Radford Partially unfolded states of beta(2)-microglobulin and amyloid formation in vitro Biochemistry 39 2000 8735 8746 (Pubitemid 30602783)
-
(2000)
Biochemistry
, vol.39
, Issue.30
, pp. 8735-8746
-
-
McParland, V.J.1
Kad, N.M.2
Kalverda, A.P.3
Brown, A.4
Kirwin-Jones, P.5
Hunter, M.G.6
Sunde, M.7
Radford, S.E.8
-
43
-
-
0035896018
-
Detection of two partially structured species in the folding process of the amyloidogenic protein β2-microglobulin
-
DOI 10.1006/jmbi.2000.4478
-
F. Chiti, P. Mangione, A. Andreola, S. Giorgetti, M. Stefani, C.M. Dobson, V. Bellotti, and N. Taddei Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin J. Mol. Biol. 307 2001 379 391 (Pubitemid 33029988)
-
(2001)
Journal of Molecular Biology
, vol.307
, Issue.1
, pp. 379-391
-
-
Chiti, F.1
Mangione, P.2
Andreola, A.3
Giorgetti, S.4
Stefani, M.5
Dobson, C.M.6
Bellotti, V.7
Taddei, N.8
-
44
-
-
52049098478
-
Structural characteristics of alpha-synuclein oligomers stabilized by the flavonoid baicalein
-
D.P. Hong, A.L. Fink, and V.N. Uversky Structural characteristics of alpha-synuclein oligomers stabilized by the flavonoid baicalein J. Mol. Biol. 383 2008 214 223
-
(2008)
J. Mol. Biol.
, vol.383
, pp. 214-223
-
-
Hong, D.P.1
Fink, A.L.2
Uversky, V.N.3
-
45
-
-
68749092581
-
The binding of pullulan modified cholesteryl nanogels to Abeta oligomers and their suppression of cytotoxicity
-
S. Boridy, H. Takahashi, K. Akiyoshi, and D. Maysinger The binding of pullulan modified cholesteryl nanogels to Abeta oligomers and their suppression of cytotoxicity Biomaterials 30 2009 5583 5591
-
(2009)
Biomaterials
, vol.30
, pp. 5583-5591
-
-
Boridy, S.1
Takahashi, H.2
Akiyoshi, K.3
Maysinger, D.4
-
46
-
-
79960501434
-
Polyphenolic glycosides and aglycones utilize opposing pathways to selectively remodel and inactivate toxic oligomers of amyloid beta
-
A.R. Ladiwala, M. Mora-Pale, J.C. Lin, S.S. Bale, Z.S. Fishman, J.S. Dordick, and P.M. Tessier Polyphenolic glycosides and aglycones utilize opposing pathways to selectively remodel and inactivate toxic oligomers of amyloid beta Chembiochem 12 2011 1749 1758
-
(2011)
Chembiochem
, vol.12
, pp. 1749-1758
-
-
Ladiwala, A.R.1
Mora-Pale, M.2
Lin, J.C.3
Bale, S.S.4
Fishman, Z.S.5
Dordick, J.S.6
Tessier, P.M.7
-
47
-
-
79952796718
-
Aromatic small molecules remodel toxic soluble oligomers of amyloid beta through three independent pathways
-
A.R. Ladiwala, J.S. Dordick, and P.M. Tessier Aromatic small molecules remodel toxic soluble oligomers of amyloid beta through three independent pathways J. Biol. Chem. 286 2011 3209 3218
-
(2011)
J. Biol. Chem.
, vol.286
, pp. 3209-3218
-
-
Ladiwala, A.R.1
Dordick, J.S.2
Tessier, P.M.3
-
48
-
-
77954907699
-
Resveratrol selectively remodels soluble oligomers and fibrils of amyloid Abeta into off-pathway conformers
-
A.R. Ladiwala, J.C. Lin, S.S. Bale, A.M. Marcelino-Cruz, M. Bhattacharya, J.S. Dordick, and P.M. Tessier Resveratrol selectively remodels soluble oligomers and fibrils of amyloid Abeta into off-pathway conformers J. Biol. Chem. 285 2010 24228 24237
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 24228-24237
-
-
Ladiwala, A.R.1
Lin, J.C.2
Bale, S.S.3
Marcelino-Cruz, A.M.4
Bhattacharya, M.5
Dordick, J.S.6
Tessier, P.M.7
-
49
-
-
84863799510
-
Conformational differences between two amyloid beta oligomers of similar size and dissimilar toxicity
-
A.R. Ladiwala, J. Litt, R.S. Kane, D.S. Aucoin, S.O. Smith, S. Ranjan, J. Davis, W.E. Vannostrand, and P.M. Tessier Conformational differences between two amyloid beta oligomers of similar size and dissimilar toxicity J. Biol. Chem. 287 2012 24765 24773
-
(2012)
J. Biol. Chem.
, vol.287
, pp. 24765-24773
-
-
Ladiwala, A.R.1
Litt, J.2
Kane, R.S.3
Aucoin, D.S.4
Smith, S.O.5
Ranjan, S.6
Davis, J.7
Vannostrand, W.E.8
Tessier, P.M.9
-
50
-
-
79953199374
-
Biflavonoids are superior to monoflavonoids in inhibiting amyloid-beta toxicity and fibrillogenesis via accumulation of nontoxic oligomer-like structures
-
A. Thapa, E.R. Woo, E.Y. Chi, M.G. Sharoar, H.G. Jin, S.Y. Shin, and I.S. Park Biflavonoids are superior to monoflavonoids in inhibiting amyloid-beta toxicity and fibrillogenesis via accumulation of nontoxic oligomer-like structures Biochemistry 50 2011 2445 2455
-
(2011)
Biochemistry
, vol.50
, pp. 2445-2455
-
-
Thapa, A.1
Woo, E.R.2
Chi, E.Y.3
Sharoar, M.G.4
Jin, H.G.5
Shin, S.Y.6
Park, I.S.7
-
51
-
-
33646570598
-
Small molecule inhibitors of α-synuclein filament assembly
-
DOI 10.1021/bi0600749
-
M. Masuda, N. Suzuki, S. Taniguchi, T. Oikawa, T. Nonaka, T. Iwatsubo, S. Hisanaga, M. Goedert, and M. Hasegawa Small molecule inhibitors of alpha-synuclein filament assembly Biochemistry 45 2006 6085 6094 (Pubitemid 43727101)
-
(2006)
Biochemistry
, vol.45
, Issue.19
, pp. 6085-6094
-
-
Masuda, M.1
Suzuki, N.2
Taniguchi, S.3
Oikawa, T.4
Nonaka, T.5
Iwatsubo, T.6
Hisanaga, S.-I.7
Goedert, M.8
Hasegawa, M.9
-
52
-
-
84856415710
-
Copper inducing Abeta42 rather than Abeta40 nanoscale oligomer formation is the key process for Abeta neurotoxicity
-
L. Jin, W.H. Wu, Q.Y. Li, Y.F. Zhao, and Y.M. Li Copper inducing Abeta42 rather than Abeta40 nanoscale oligomer formation is the key process for Abeta neurotoxicity Nanoscale 3 2011 4746 4751
-
(2011)
Nanoscale
, vol.3
, pp. 4746-4751
-
-
Jin, L.1
Wu, W.H.2
Li, Q.Y.3
Zhao, Y.F.4
Li, Y.M.5
-
53
-
-
80053289958
-
A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells
-
M. Zampagni, R. Cascella, F. Casamenti, C. Grossi, E. Evangelisti, D. Wright, M. Becatti, G. Liguri, B. Mannini, S. Campioni, F. Chiti, and C. Cecchi A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells J. Cell. Mol. Med. 15 2011 2106 2116
-
(2011)
J. Cell. Mol. Med.
, vol.15
, pp. 2106-2116
-
-
Zampagni, M.1
Cascella, R.2
Casamenti, F.3
Grossi, C.4
Evangelisti, E.5
Wright, D.6
Becatti, M.7
Liguri, G.8
Mannini, B.9
Campioni, S.10
Chiti, F.11
Cecchi, C.12
-
54
-
-
75349097530
-
A causative link between the structure of aberrant protein oligomers and their toxicity
-
S. Campioni, B. Mannini, M. Zampagni, A. Pensalfini, C. Parrini, E. Evangelisti, A. Relini, M. Stefani, C.M. Dobson, C. Cecchi, and F. Chiti A causative link between the structure of aberrant protein oligomers and their toxicity Nat. Chem. Biol. 6 2010 140 147
-
(2010)
Nat. Chem. Biol.
, vol.6
, pp. 140-147
-
-
Campioni, S.1
Mannini, B.2
Zampagni, M.3
Pensalfini, A.4
Parrini, C.5
Evangelisti, E.6
Relini, A.7
Stefani, M.8
Dobson, C.M.9
Cecchi, C.10
Chiti, F.11
-
55
-
-
74849125564
-
Methionine oxidation stabilizes non-toxic oligomers of alpha-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions
-
W. Zhou, C. Long, S.H. Reaney, D.A. Di Monte, A.L. Fink, and V.N. Uversky Methionine oxidation stabilizes non-toxic oligomers of alpha-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions Biochim. Biophys. Acta 1802 2010 322 330
-
(2010)
Biochim. Biophys. Acta
, vol.1802
, pp. 322-330
-
-
Zhou, W.1
Long, C.2
Reaney, S.H.3
Di Monte, D.A.4
Fink, A.L.5
Uversky, V.N.6
-
56
-
-
78650909852
-
Kinetic intermediates of beta(2)-microglobulin fibril elongation probed by pulse-labeling H/D exchange combined with NMR analysis
-
T. Konuma, E. Chatani, M. Yagi, K. Sakurai, T. Ikegami, H. Naiki, and Y. Goto Kinetic intermediates of beta(2)-microglobulin fibril elongation probed by pulse-labeling H/D exchange combined with NMR analysis J. Mol. Biol. 405 2011 851 862
-
(2011)
J. Mol. Biol.
, vol.405
, pp. 851-862
-
-
Konuma, T.1
Chatani, E.2
Yagi, M.3
Sakurai, K.4
Ikegami, T.5
Naiki, H.6
Goto, Y.7
-
57
-
-
77954620268
-
Pre-steady-state kinetic analysis of the elongation of amyloid fibrils of beta(2)-microglobulin with tryptophan mutagenesis
-
E. Chatani, R. Ohnishi, T. Konuma, K. Sakurai, H. Naiki, and Y. Goto Pre-steady-state kinetic analysis of the elongation of amyloid fibrils of beta(2)-microglobulin with tryptophan mutagenesis J. Mol. Biol. 400 2010 1057 1066
-
(2010)
J. Mol. Biol.
, vol.400
, pp. 1057-1066
-
-
Chatani, E.1
Ohnishi, R.2
Konuma, T.3
Sakurai, K.4
Naiki, H.5
Goto, Y.6
-
58
-
-
34547174917
-
Fluorescence as a method to reveal structures and membrane-interactions of amyloidogenic proteins
-
DOI 10.1016/j.bbamem.2007.03.015, PII S0005273607000806
-
L.A. Munishkina, and A.L. Fink Fluorescence as a method to reveal structures and membrane-interactions of amyloidogenic proteins Biochim. Biophys. Acta 1768 2007 1862 1885 (Pubitemid 47125851)
-
(2007)
Biochimica et Biophysica Acta - Biomembranes
, vol.1768
, Issue.8
, pp. 1862-1885
-
-
Munishkina, L.A.1
Fink, A.L.2
-
59
-
-
79959208754
-
Seed-dependent deposition behavior of Abeta peptides studied with wireless quartz-crystal-microbalance biosensor
-
H. Ogi, Y. Fukunishi, T. Yanagida, H. Yagi, Y. Goto, M. Fukushima, K. Uesugi, and M. Hirao Seed-dependent deposition behavior of Abeta peptides studied with wireless quartz-crystal-microbalance biosensor Anal. Chem. 83 2011 4982 4988
-
(2011)
Anal. Chem.
, vol.83
, pp. 4982-4988
-
-
Ogi, H.1
Fukunishi, Y.2
Yanagida, T.3
Yagi, H.4
Goto, Y.5
Fukushima, M.6
Uesugi, K.7
Hirao, M.8
-
60
-
-
68649123057
-
Biosensor-based label-free assays of amyloid growth
-
D.A. White, A.K. Buell, C.M. Dobson, M.E. Welland, and T.P. Knowles Biosensor-based label-free assays of amyloid growth FEBS Lett. 583 2009 2587 2592
-
(2009)
FEBS Lett.
, vol.583
, pp. 2587-2592
-
-
White, D.A.1
Buell, A.K.2
Dobson, C.M.3
Welland, M.E.4
Knowles, T.P.5
-
61
-
-
59049099079
-
A comprehensive model for packing and hydration for amyloid fibrils of beta2-microglobulin
-
Y.H. Lee, E. Chatani, K. Sasahara, H. Naiki, and Y. Goto A comprehensive model for packing and hydration for amyloid fibrils of beta2-microglobulin J. Biol. Chem. 284 2009 2169 2175
-
(2009)
J. Biol. Chem.
, vol.284
, pp. 2169-2175
-
-
Lee, Y.H.1
Chatani, E.2
Sasahara, K.3
Naiki, H.4
Goto, Y.5
-
62
-
-
37649000487
-
Molecular architecture of human prion protein amyloid: A parallel, in-register beta-structure
-
N.J. Cobb, F.D. Sonnichsen, H. McHaourab, and W.K. Surewicz Molecular architecture of human prion protein amyloid: a parallel, in-register beta-structure Proc. Natl. Acad. Sci. U. S. A. 104 2007 18946 18951
-
(2007)
Proc. Natl. Acad. Sci. U. S. A.
, vol.104
, pp. 18946-18951
-
-
Cobb, N.J.1
Sonnichsen, F.D.2
McHaourab, H.3
Surewicz, W.K.4
-
63
-
-
33749508090
-
Direct Observation of Amyloid Growth Monitored by Total Internal Reflection Fluorescence Microscopy
-
DOI 10.1016/S0076-6879(06)13005-0, PII S0076687906130050, Amyloid, Prions, and Other Protein Aggregates, Part C
-
T. Ban, and Y. Goto Direct observation of amyloid growth monitored by total internal reflection fluorescence microscopy Methods Enzymol. 413 2006 91 102 (Pubitemid 44528686)
-
(2006)
Methods in Enzymology
, vol.413
, pp. 91-102
-
-
Ban, T.1
Goto, Y.2
-
64
-
-
59449106971
-
Destruction of amyloid fibrils of a beta2-microglobulin fragment by laser beam irradiation
-
D. Ozawa, H. Yagi, T. Ban, A. Kameda, T. Kawakami, H. Naiki, and Y. Goto Destruction of amyloid fibrils of a beta2-microglobulin fragment by laser beam irradiation J. Biol. Chem. 284 2009 1009 1017
-
(2009)
J. Biol. Chem.
, vol.284
, pp. 1009-1017
-
-
Ozawa, D.1
Yagi, H.2
Ban, T.3
Kameda, A.4
Kawakami, T.5
Naiki, H.6
Goto, Y.7
-
65
-
-
50049095633
-
Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin)
-
J.J. Wiltzius, S.A. Sievers, M.R. Sawaya, D. Cascio, D. Popov, C. Riekel, and D. Eisenberg Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin) Protein Sci. 17 2008 1467 1474
-
(2008)
Protein Sci.
, vol.17
, pp. 1467-1474
-
-
Wiltzius, J.J.1
Sievers, S.A.2
Sawaya, M.R.3
Cascio, D.4
Popov, D.5
Riekel, C.6
Eisenberg, D.7
-
66
-
-
20444440728
-
Structure of the cross-β spine of amyloid-like fibrils
-
DOI 10.1038/nature03680
-
R. Nelson, M.R. Sawaya, M. Balbirnie, A.O. Madsen, C. Riekel, R. Grothe, and D. Eisenberg Structure of the cross-beta spine of amyloid-like fibrils Nature 435 2005 773 778 (Pubitemid 40839722)
-
(2005)
Nature
, vol.435
, Issue.7043
, pp. 773-778
-
-
Nelson, R.1
Sawaya, M.R.2
Balbirnie, M.3
Madsen, A.O.4
Riekel, C.5
Grothe, R.6
Eisenberg, D.7
-
67
-
-
34249290108
-
Atomic structures of amyloid cross-β spines reveal varied steric zippers
-
DOI 10.1038/nature05695, PII NATURE05695
-
M.R. Sawaya, S. Sambashivan, R. Nelson, M.I. Ivanova, S.A. Sievers, M.I. Apostol, M.J. Thompson, M. Balbirnie, J.J. Wiltzius, H.T. McFarlane, A.O. Madsen, C. Riekel, and D. Eisenberg Atomic structures of amyloid cross-beta spines reveal varied steric zippers Nature 447 2007 453 457 (Pubitemid 46816731)
-
(2007)
Nature
, vol.447
, Issue.7143
, pp. 453-457
-
-
Sawaya, M.R.1
Sambashivan, S.2
Nelson, R.3
Ivanova, M.I.4
Sievers, S.A.5
Apostol, M.I.6
Thompson, M.J.7
Balbirnie, M.8
Wiltzius, J.J.W.9
McFarlane, H.T.10
Madsen, A.O.11
Riekel, C.12
Eisenberg, D.13
-
68
-
-
69949187643
-
Molecular mechanisms for protein-encoded inheritance
-
J.J. Wiltzius, M. Landau, R. Nelson, M.R. Sawaya, M.I. Apostol, L. Goldschmidt, A.B. Soriaga, D. Cascio, K. Rajashankar, and D. Eisenberg Molecular mechanisms for protein-encoded inheritance Nat. Struct. Mol. Biol. 16 2009 973 978
-
(2009)
Nat. Struct. Mol. Biol.
, vol.16
, pp. 973-978
-
-
Wiltzius, J.J.1
Landau, M.2
Nelson, R.3
Sawaya, M.R.4
Apostol, M.I.5
Goldschmidt, L.6
Soriaga, A.B.7
Cascio, D.8
Rajashankar, K.9
Eisenberg, D.10
-
69
-
-
78650159249
-
Intermolecular alignment in beta(2)-microglobulin amyloid fibrils
-
G.T. Debelouchina, G.W. Platt, M.J. Bayro, S.E. Radford, and R.G. Griffin Intermolecular alignment in beta(2)-microglobulin amyloid fibrils J. Am. Chem. Soc. 132 2010 17077 17079
-
(2010)
J. Am. Chem. Soc.
, vol.132
, pp. 17077-17079
-
-
Debelouchina, G.T.1
Platt, G.W.2
Bayro, M.J.3
Radford, S.E.4
Griffin, R.G.5
-
70
-
-
77955045091
-
Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies
-
G.T. Debelouchina, G.W. Platt, M.J. Bayro, S.E. Radford, and R.G. Griffin Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies J. Am. Chem. Soc. 132 2010 10414 10423
-
(2010)
J. Am. Chem. Soc.
, vol.132
, pp. 10414-10423
-
-
Debelouchina, G.T.1
Platt, G.W.2
Bayro, M.J.3
Radford, S.E.4
Griffin, R.G.5
-
71
-
-
77952759080
-
Stacked sets of parallel, in-register beta-strands of beta2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling
-
C.L. Ladner, M. Chen, D.P. Smith, G.W. Platt, S.E. Radford, and R. Langen Stacked sets of parallel, in-register beta-strands of beta2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling J. Biol. Chem. 285 2010 17137 17147
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 17137-17147
-
-
Ladner, C.L.1
Chen, M.2
Smith, D.P.3
Platt, G.W.4
Radford, S.E.5
Langen, R.6
-
72
-
-
67349152747
-
Globular tetramers of beta(2)-microglobulin assemble into elaborate amyloid fibrils
-
H.E. White, J.L. Hodgkinson, T.R. Jahn, S. Cohen-Krausz, W.S. Gosal, S. Muller, E.V. Orlova, S.E. Radford, and H.R. Saibil Globular tetramers of beta(2)-microglobulin assemble into elaborate amyloid fibrils J. Mol. Biol. 389 2009 48 57
-
(2009)
J. Mol. Biol.
, vol.389
, pp. 48-57
-
-
White, H.E.1
Hodgkinson, J.L.2
Jahn, T.R.3
Cohen-Krausz, S.4
Gosal, W.S.5
Muller, S.6
Orlova, E.V.7
Radford, S.E.8
Saibil, H.R.9
-
73
-
-
57649128935
-
Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: Molecular insights from electron paramagnetic resonance spectroscopy
-
M. Margittai, and R. Langen Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy Q. Rev. Biophys. 41 2008 265 297
-
(2008)
Q. Rev. Biophys.
, vol.41
, pp. 265-297
-
-
Margittai, M.1
Langen, R.2
-
74
-
-
58249094358
-
HDX-ESI-MS reveals enhanced conformational dynamics of the amyloidogenic protein beta(2)-microglobulin upon release from the MHC-1
-
J.P. Hodkinson, T.R. Jahn, S.E. Radford, and A.E. Ashcroft HDX-ESI-MS reveals enhanced conformational dynamics of the amyloidogenic protein beta(2)-microglobulin upon release from the MHC-1 J. Am. Soc. Mass Spectrom. 20 2009 278 286
-
(2009)
J. Am. Soc. Mass Spectrom.
, vol.20
, pp. 278-286
-
-
Hodkinson, J.P.1
Jahn, T.R.2
Radford, S.E.3
Ashcroft, A.E.4
-
75
-
-
78649664464
-
Direct observation of minimum-sized amyloid fibrils using solution NMR spectroscopy
-
Y. Yoshimura, K. Sakurai, Y.H. Lee, T. Ikegami, E. Chatani, H. Naiki, and Y. Goto Direct observation of minimum-sized amyloid fibrils using solution NMR spectroscopy Protein Sci. 19 2010 2347 2355
-
(2010)
Protein Sci.
, vol.19
, pp. 2347-2355
-
-
Yoshimura, Y.1
Sakurai, K.2
Lee, Y.H.3
Ikegami, T.4
Chatani, E.5
Naiki, H.6
Goto, Y.7
-
77
-
-
34247103661
-
+ reductase revealed by hydrogen/deuterium exchange
-
DOI 10.1074/jbc.M608417200
-
+ reductase revealed by hydrogen/deuterium exchange J. Biol. Chem. 282 2007 5959 5967 (Pubitemid 47093743)
-
(2007)
Journal of Biological Chemistry
, vol.282
, Issue.8
, pp. 5959-5967
-
-
Lee, Y.-H.1
Tamura, K.2
Maeda, M.3
Hoshino, M.4
Sakurai, K.5
Takahashi, S.6
Ikegami, T.7
Hase, T.8
Goto, Y.9
-
79
-
-
0033871781
-
Protein folding intermediates and pathways studied by hydrogen exchange
-
DOI 10.1146/annurev.biophys.29.1.213
-
S.W. Englander Protein folding intermediates and pathways studied by hydrogen exchange Annu. Rev. Biophys. Biomol. Struct. 29 2000 213 238 (Pubitemid 30599593)
-
(2000)
Annual Review of Biophysics and Biomolecular Structure
, vol.29
, pp. 213-238
-
-
Englander, S.W.1
-
80
-
-
42449151176
-
Protein folding and misfolding: Mechanism and principles
-
DOI 10.1017/S0033583508004654, PII S0033583508004654
-
S.W. Englander, L. Mayne, and M.M. Krishna Protein folding and misfolding: mechanism and principles Q. Rev. Biophys. 40 2007 287 326 (Pubitemid 351569384)
-
(2007)
Quarterly Reviews of Biophysics
, vol.40
, Issue.4
, pp. 287-326
-
-
Englander, S.W.1
Mayne, L.2
Krishna, M.M.G.3
-
81
-
-
58849151382
-
Equilibrium unfolding thermodynamics of beta2-microglobulin analyzed through native-state H/D exchange
-
E. Rennella, A. Corazza, F. Fogolari, P. Viglino, S. Giorgetti, M. Stoppini, V. Bellotti, and G. Esposito Equilibrium unfolding thermodynamics of beta2-microglobulin analyzed through native-state H/D exchange Biophys. J. 96 2009 169 179
-
(2009)
Biophys. J.
, vol.96
, pp. 169-179
-
-
Rennella, E.1
Corazza, A.2
Fogolari, F.3
Viglino, P.4
Giorgetti, S.5
Stoppini, M.6
Bellotti, V.7
Esposito, G.8
-
82
-
-
84858228154
-
Determining the energy landscape of proteins by a fast isotope exchange NMR approach
-
E. Rennella, A. Corazza, L. Codutti, V. Bellotti, M. Stoppini, P. Viglino, F. Fogolari, and G. Esposito Determining the energy landscape of proteins by a fast isotope exchange NMR approach J. Am. Chem. Soc. 134 2012 4457 4460
-
(2012)
J. Am. Chem. Soc.
, vol.134
, pp. 4457-4460
-
-
Rennella, E.1
Corazza, A.2
Codutti, L.3
Bellotti, V.4
Stoppini, M.5
Viglino, P.6
Fogolari, F.7
Esposito, G.8
-
83
-
-
84860361268
-
Single-shot NMR measurement of protein unfolding landscapes
-
E. Rennella, A. Corazza, L. Codutti, A. Causero, V. Bellotti, M. Stoppini, P. Viglino, F. Fogolari, and G. Esposito Single-shot NMR measurement of protein unfolding landscapes Biochim. Biophys. Acta 1824 2012 842 849
-
(2012)
Biochim. Biophys. Acta
, vol.1824
, pp. 842-849
-
-
Rennella, E.1
Corazza, A.2
Codutti, L.3
Causero, A.4
Bellotti, V.5
Stoppini, M.6
Viglino, P.7
Fogolari, F.8
Esposito, G.9
-
84
-
-
0036242430
-
2-microglobulin amyloid fibril by H/D exchange
-
DOI 10.1038/nsb792
-
M. Hoshino, H. Katou, Y. Hagihara, K. Hasegawa, H. Naiki, and Y. Goto Mapping the core of the beta(2)-microglobulin amyloid fibril by H/D exchange Nat. Struct. Biol. 9 2002 332 336 (Pubitemid 34462549)
-
(2002)
Nature Structural Biology
, vol.9
, Issue.5
, pp. 332-336
-
-
Hoshino, M.1
Katou, H.2
Hagihara, Y.3
Hasegawa, K.4
Naiki, H.5
Goto, Y.6
-
85
-
-
1842786897
-
2-microglobulin amyloid fibrils as revealed by H/D exchange
-
DOI 10.1016/j.jmb.2004.02.067, PII S0022283604002621
-
K. Yamaguchi, H. Katou, M. Hoshino, K. Hasegawa, H. Naiki, and Y. Goto Core and heterogeneity of beta2-microglobulin amyloid fibrils as revealed by H/D exchange J. Mol. Biol. 338 2004 559 571 (Pubitemid 38479650)
-
(2004)
Journal of Molecular Biology
, vol.338
, Issue.3
, pp. 559-571
-
-
Yamaguchi, K.-I.1
Katou, H.2
Hoshino, M.3
Hasegawa, K.4
Naiki, H.5
Goto, Y.6
-
86
-
-
47249110199
-
The fold of alpha-synuclein fibrils
-
M. Vilar, H.T. Chou, T. Luhrs, S.K. Maji, D. Riek-Loher, R. Verel, G. Manning, H. Stahlberg, and R. Riek The fold of alpha-synuclein fibrils Proc. Natl. Acad. Sci. U. S. A. 105 2008 8637 8642
-
(2008)
Proc. Natl. Acad. Sci. U. S. A.
, vol.105
, pp. 8637-8642
-
-
Vilar, M.1
Chou, H.T.2
Luhrs, T.3
Maji, S.K.4
Riek-Loher, D.5
Verel, R.6
Manning, G.7
Stahlberg, H.8
Riek, R.9
-
87
-
-
1242316998
-
Probing Solvent Accessibility of Transthyretin Amyloid by Solution NMR Spectroscopy
-
DOI 10.1074/jbc.M310605200
-
A. Olofsson, J.H. Ippel, S.S. Wijmenga, E. Lundgren, and A. Ohman Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy J. Biol. Chem. 279 2004 5699 5707 (Pubitemid 38220599)
-
(2004)
Journal of Biological Chemistry
, vol.279
, Issue.7
, pp. 5699-5707
-
-
Olofsson, A.1
Ippel, J.H.2
Wijmenga, S.S.3
Lundgren, E.4
Ohman, A.5
-
88
-
-
34249051698
-
Amide solvent protection analysis demonstrates that amyloid-β(1-40) and amyloid-β(1-42) form different fibrillar structures under identical conditions
-
DOI 10.1042/BJ20061561
-
A. Olofsson, M. Lindhagen-Persson, A.E. Sauer-Eriksson, and A. Ohman Amide solvent protection analysis demonstrates that amyloid-beta(1-40) and amyloid-beta(1-42) form different fibrillar structures under identical conditions Biochem. J. 404 2007 63 70 (Pubitemid 46788085)
-
(2007)
Biochemical Journal
, vol.404
, Issue.1
, pp. 63-70
-
-
Olofsson, A.1
Lindhagen-Persson, M.2
Sauer-Eriksson, A.E.3
Ohman, A.4
-
90
-
-
33644851439
-
The solvent protection of alzheimer amyloid-β-(1- 42) fibrils as determined by solution NMR spectroscopy
-
DOI 10.1074/jbc.M508962200
-
A. Olofsson, A.E. Sauer-Eriksson, and A. Ohman The solvent protection of alzheimer amyloid-beta-(1-42) fibrils as determined by solution NMR spectroscopy J. Biol. Chem. 281 2006 477 483 (Pubitemid 43671210)
-
(2006)
Journal of Biological Chemistry
, vol.281
, Issue.1
, pp. 477-483
-
-
Olofsson, A.1
Sauer-Eriksson, A.E.2
Ohman, A.3
-
91
-
-
40849120669
-
Amyloid fibrils of the HET-s(218-289) prion form a β solenoid with a triangular hydrophobic core
-
DOI 10.1126/science.1151839
-
C. Wasmer, A. Lange, H. Van Melckebeke, A.B. Siemer, R. Riek, and B.H. Meier Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core Science 319 2008 1523 1526 (Pubitemid 351398180)
-
(2008)
Science
, vol.319
, Issue.5869
, pp. 1523-1526
-
-
Wasmer, C.1
Lange, A.2
Van Melckebeke, H.3
Siemer, A.B.4
Riek, R.5
Meier, B.H.6
-
92
-
-
23144459082
-
Molecular recycling within amyloid fibrils
-
DOI 10.1038/nature03986
-
N. Carulla, G.L. Caddy, D.R. Hall, J. Zurdo, M. Gairi, M. Feliz, E. Giralt, C.V. Robinson, and C.M. Dobson Molecular recycling within amyloid fibrils Nature 436 2005 554 558 (Pubitemid 41112928)
-
(2005)
Nature
, vol.436
, Issue.7050
, pp. 554-558
-
-
Carulla, N.1
Caddy, G.L.2
Hall, D.R.3
Zurdo, J.4
Gairi, M.5
Feliz, M.6
Giralt, E.7
Robinson, C.V.8
Dobson, C.M.9
-
93
-
-
0035234662
-
An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed by cold shock protein A
-
A.T. Alexandrescu An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed by cold shock protein A Pac. Symp. Biocomput. 2001 67 78
-
(2001)
Pac. Symp. Biocomput.
, pp. 67-78
-
-
Alexandrescu, A.T.1
-
94
-
-
67849106670
-
Amyloid-beta protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
-
S.L. Bernstein, N.F. Dupuis, N.D. Lazo, T. Wyttenbach, M.M. Condron, G. Bitan, D.B. Teplow, J.E. Shea, B.T. Ruotolo, C.V. Robinson, and M.T. Bowers Amyloid-beta protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease Nat. Chem. 1 2009 326 331
-
(2009)
Nat. Chem.
, vol.1
, pp. 326-331
-
-
Bernstein, S.L.1
Dupuis, N.F.2
Lazo, N.D.3
Wyttenbach, T.4
Condron, M.M.5
Bitan, G.6
Teplow, D.B.7
Shea, J.E.8
Ruotolo, B.T.9
Robinson, C.V.10
Bowers, M.T.11
-
95
-
-
84865098615
-
The monomer-seed interaction mechanism in the formation of the β2-microglobulin amyloid fibril clarified by solution NMR techniques
-
K. Yanagi, Y. Yoshimura, K. Sakurai, K. Konuma, Y. Lee, K. Sugase, T. Ikegami, H. Naiki, and Y. Goto The monomer-seed interaction mechanism in the formation of the β2-microglobulin amyloid fibril clarified by solution NMR techniques J. Mol. Biol. 422 2012 390 402
-
(2012)
J. Mol. Biol.
, vol.422
, pp. 390-402
-
-
Yanagi, K.1
Yoshimura, Y.2
Sakurai, K.3
Konuma, K.4
Lee, Y.5
Sugase, K.6
Ikegami, T.7
Naiki, H.8
Goto, Y.9
-
96
-
-
66049093067
-
Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation
-
N. Carulla, M. Zhou, M. Arimon, M. Gairi, E. Giralt, C.V. Robinson, and C.M. Dobson Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation Proc. Natl. Acad. Sci. U. S. A. 106 2009 7828 7833
-
(2009)
Proc. Natl. Acad. Sci. U. S. A.
, vol.106
, pp. 7828-7833
-
-
Carulla, N.1
Zhou, M.2
Arimon, M.3
Gairi, M.4
Giralt, E.5
Robinson, C.V.6
Dobson, C.M.7
-
97
-
-
0026611617
-
1H NMR assignments and secondary structure of human beta 2-microglobulin in solution
-
1H NMR assignments and secondary structure of human beta 2-microglobulin in solution Biochemistry 31 1992 8906 8915
-
(1992)
Biochemistry
, vol.31
, pp. 8906-8915
-
-
Okon, M.1
Bray, P.2
Vucelic, D.3
-
99
-
-
50249144570
-
Bacterial inclusion bodies contain amyloid-like structure
-
L. Wang, S.K. Maji, M.R. Sawaya, D. Eisenberg, and R. Riek Bacterial inclusion bodies contain amyloid-like structure PLoS Biol. 6 2008 e195
-
(2008)
PLoS Biol.
, vol.6
, pp. 195
-
-
Wang, L.1
Maji, S.K.2
Sawaya, M.R.3
Eisenberg, D.4
Riek, R.5
-
100
-
-
61949243261
-
High-resolution multi-dimensional NMR spectroscopy of proteins in human cells
-
K. Inomata, A. Ohno, H. Tochio, S. Isogai, T. Tenno, I. Nakase, T. Takeuchi, S. Futaki, Y. Ito, H. Hiroaki, and M. Shirakawa High-resolution multi-dimensional NMR spectroscopy of proteins in human cells Nature 458 2009 106 109
-
(2009)
Nature
, vol.458
, pp. 106-109
-
-
Inomata, K.1
Ohno, A.2
Tochio, H.3
Isogai, S.4
Tenno, T.5
Nakase, I.6
Takeuchi, T.7
Futaki, S.8
Ito, Y.9
Hiroaki, H.10
Shirakawa, M.11
-
101
-
-
77952075172
-
Structural variations in the cross-beta core of amyloid beta fibrils revealed by deep UV resonance Raman spectroscopy
-
L.A. Popova, R. Kodali, R. Wetzel, and I.K. Lednev Structural variations in the cross-beta core of amyloid beta fibrils revealed by deep UV resonance Raman spectroscopy J. Am. Chem. Soc. 132 2010 6324 6328
-
(2010)
J. Am. Chem. Soc.
, vol.132
, pp. 6324-6328
-
-
Popova, L.A.1
Kodali, R.2
Wetzel, R.3
Lednev, I.K.4
-
102
-
-
0041345995
-
Conformational transition occurring upon amyloid aggregation of the HET-s prion protein of Podospora anserina analyzed by hydrogen/deuterium exchange and mass spectrometry
-
DOI 10.1021/bi0344275
-
A. Nazabal, S. Dos Reis, M. Bonneu, S.J. Saupe, and J.M. Schmitter Conformational transition occurring upon amyloid aggregation of the HET-s prion protein of Podospora anserina analyzed by hydrogen/deuterium exchange and mass spectrometry Biochemistry 42 2003 8852 8861 (Pubitemid 36899829)
-
(2003)
Biochemistry
, vol.42
, Issue.29
, pp. 8852-8861
-
-
Nazabal, A.1
Dos Reis, S.D.2
Bonneu, M.3
Saupe, S.J.4
Schmitter, J.-M.5
-
103
-
-
34548710335
-
Probing the cross-β core structure of amyloid fibrils by hydrogen-deuterium exchange deep ultraviolet resonance Raman spectroscopy
-
DOI 10.1021/ja073798w
-
M. Xu, V. Shashilov, and I.K. Lednev Probing the cross-beta core structure of amyloid fibrils by hydrogen-deuterium exchange deep ultraviolet resonance Raman spectroscopy J. Am. Chem. Soc. 129 2007 11002 11003 (Pubitemid 47435688)
-
(2007)
Journal of the American Chemical Society
, vol.129
, Issue.36
, pp. 11002-11003
-
-
Xu, M.1
Shashilov, V.2
Lednev, I.K.3
-
104
-
-
79953245314
-
Amyloid structure: Conformational diversity and consequences
-
B.H. Toyama, and J.S. Weissman Amyloid structure: conformational diversity and consequences Annu. Rev. Biochem. 80 2011 557 585
-
(2011)
Annu. Rev. Biochem.
, vol.80
, pp. 557-585
-
-
Toyama, B.H.1
Weissman, J.S.2
-
105
-
-
33845334180
-
2- microglobulin fragment probed by solid-state NMR
-
DOI 10.1073/pnas.0607180103
-
K. Iwata, T. Fujiwara, Y. Matsuki, H. Akutsu, S. Takahashi, H. Naiki, and Y. Goto 3D structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR Proc. Natl. Acad. Sci. U. S. A. 103 2006 18119 18124 (Pubitemid 44871622)
-
(2006)
Proceedings of the National Academy of Sciences of the United States of America
, vol.103
, Issue.48
, pp. 18119-18124
-
-
Iwata, K.1
Fujiwara, T.2
Matsuki, Y.3
Akutsu, H.4
Takahashi, S.5
Naiki, H.6
Goto, Y.7
-
107
-
-
30744433878
-
Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils
-
DOI 10.1021/bi051952q
-
A.T. Petkova, W.M. Yau, and R. Tycko Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils Biochemistry 45 2006 498 512 (Pubitemid 43100415)
-
(2006)
Biochemistry
, vol.45
, Issue.2
, pp. 498-512
-
-
Petkova, A.T.1
Yau, W.-M.2
Tycko, R.3
-
108
-
-
24644447303
-
Seeding-dependent propagation and maturation of amyloid fibril conformation
-
DOI 10.1016/j.jmb.2005.07.061, PII S0022283605008740
-
K. Yamaguchi, S. Takahashi, T. Kawai, H. Naiki, and Y. Goto Seeding-dependent propagation and maturation of amyloid fibril conformation J. Mol. Biol. 352 2005 952 960 (Pubitemid 41267080)
-
(2005)
Journal of Molecular Biology
, vol.352
, Issue.4
, pp. 952-960
-
-
Yamaguchi, K.-I.1
Takahashi, S.2
Kawai, T.3
Naiki, H.4
Goto, Y.5
-
109
-
-
33748943122
-
2- Microglobulin Fragment Are Induced by Fluorine-substituted Alcohols
-
DOI 10.1016/j.jmb.2006.08.030, PII S0022283606010588
-
K. Yamaguchi, H. Naiki, and Y. Goto Mechanism by which the amyloid-like fibrils of a beta 2-microglobulin fragment are induced by fluorine-substituted alcohols J. Mol. Biol. 363 2006 279 288 (Pubitemid 44429956)
-
(2006)
Journal of Molecular Biology
, vol.363
, Issue.1
, pp. 279-288
-
-
Yamaguchi, K.-i.1
Naiki, H.2
Goto, Y.3
-
110
-
-
4644335370
-
2-microglobulin-related amyloid fibrils at a neutral pH
-
DOI 10.1021/bi049262u
-
S. Yamamoto, K. Hasegawa, I. Yamaguchi, S. Tsutsumi, J. Kardos, Y. Goto, F. Gejyo, and H. Naiki Low concentrations of sodium dodecyl sulfate induce the extension of beta 2-microglobulin-related amyloid fibrils at a neutral pH Biochemistry 43 2004 11075 11082 (Pubitemid 39433696)
-
(2004)
Biochemistry
, vol.43
, Issue.34
, pp. 11075-11082
-
-
Yamamoto, S.1
Hasegawa, K.2
Yamaguchi, I.3
Tsutsumi, S.4
Kardos, J.5
Goto, Y.6
Gejyo, F.7
Naiki, H.8
-
111
-
-
0037077209
-
2-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond
-
DOI 10.1074/jbc.M200188200
-
D.P. Hong, M. Gozu, K. Hasegawa, H. Naiki, and Y. Goto Conformation of beta 2-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond J. Biol. Chem. 277 2002 21554 21560 (Pubitemid 34952301)
-
(2002)
Journal of Biological Chemistry
, vol.277
, Issue.24
, pp. 21554-21560
-
-
Hong, D.-P.1
Hasegawa, K.2
Naiki, H.3
-
112
-
-
0036708005
-
2-microglobulin studied by heteronuclear NMR
-
DOI 10.1110/ps.0213202
-
H. Katou, T. Kanno, M. Hoshino, Y. Hagihara, H. Tanaka, T. Kawai, K. Hasegawa, H. Naiki, and Y. Goto The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR Protein Sci. 11 2002 2218 2229 (Pubitemid 34919625)
-
(2002)
Protein Science
, vol.11
, Issue.9
, pp. 2218-2229
-
-
Katou, H.1
Kanno, T.2
Hoshino, M.3
Hagihara, Y.4
Tanaka, H.5
Kawai, T.6
Hasegawa, K.7
Naiki, H.8
Goto, Y.9
-
113
-
-
33645240208
-
A systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments
-
M.I. Ivanova, M.J. Thompson, and D. Eisenberg A systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments Proc. Natl. Acad. Sci. U. S. A. 103 2006 4079 4082
-
(2006)
Proc. Natl. Acad. Sci. U. S. A.
, vol.103
, pp. 4079-4082
-
-
Ivanova, M.I.1
Thompson, M.J.2
Eisenberg, D.3
-
114
-
-
0037227173
-
2-microglobulin - Insights into the mechanism of fibril formation in vitro
-
DOI 10.1016/S0022-2836(02)01227-5
-
S. Jones, J. Manning, N.M. Kad, and S.E. Radford Amyloid-forming peptides from beta2-microglobulin-Insights into the mechanism of fibril formation in vitro J. Mol. Biol. 325 2003 249 257 (Pubitemid 36062686)
-
(2003)
Journal of Molecular Biology
, vol.325
, Issue.2
, pp. 249-257
-
-
Jones, S.1
Manning, J.2
Kad, N.M.3
Radford, S.E.4
-
115
-
-
0037059764
-
2-microglobulin by Achromobacter protease I
-
DOI 10.1074/jbc.M108753200
-
G.V. Kozhukh, Y. Hagihara, T. Kawakami, K. Hasegawa, H. Naiki, and Y. Goto Investigation of a peptide responsible for amyloid fibril formation of beta 2-microglobulin by achromobacter protease I J. Biol. Chem. 277 2002 1310 1315 (Pubitemid 34968884)
-
(2002)
Journal of Biological Chemistry
, vol.277
, Issue.2
, pp. 1310-1315
-
-
Kozhukh, G.V.1
Hagihara, Y.2
Kawakami, T.3
Hasegawa, K.4
Naiki, H.5
Goto, Y.6
-
116
-
-
0345237917
-
Amyloidogenic synthetic peptides of β2-microglobulin - A role of the disulfide bond
-
DOI 10.1016/S0006-291X(03)00543-6
-
K. Hasegawa, Y. Ohhashi, I. Yamaguchi, N. Takahashi, S. Tsutsumi, Y. Goto, F. Gejyo, and H. Naiki Amyloidogenic synthetic peptides of beta2-microglobulin - a role of the disulfide bond Biochem. Biophys. Res. Commun. 304 2003 101 106 (Pubitemid 36434201)
-
(2003)
Biochemical and Biophysical Research Communications
, vol.304
, Issue.1
, pp. 101-106
-
-
Hasegawa, K.1
Ohhashi, Y.2
Yamaguchi, I.3
Takahashi, N.4
Tsutsumi, S.5
Goto, Y.6
Gejyo, F.7
Naiki, H.8
-
117
-
-
3242878900
-
Using nuclear magnetic resonance spectroscopy to study molten globule states of proteins
-
DOI 10.1016/j.ymeth.2004.03.009, PII S104620230400057X
-
C. Redfield Using nuclear magnetic resonance spectroscopy to study molten globule states of proteins Methods 34 2004 121 132 (Pubitemid 38996781)
-
(2004)
Methods
, vol.34
, Issue.1
, pp. 121-132
-
-
Redfield, C.1
-
118
-
-
79251538912
-
Conserved core of amyloid fibrils of wild type and A30P mutant alpha-synuclein
-
M.K. Cho, H.Y. Kim, C.O. Fernandez, S. Becker, and M. Zweckstetter Conserved core of amyloid fibrils of wild type and A30P mutant alpha-synuclein Protein Sci. 20 2011 387 395
-
(2011)
Protein Sci.
, vol.20
, pp. 387-395
-
-
Cho, M.K.1
Kim, H.Y.2
Fernandez, C.O.3
Becker, S.4
Zweckstetter, M.5
-
119
-
-
34548615995
-
The structural basis of yeast prion strain variants
-
DOI 10.1038/nature06108, PII NATURE06108
-
B.H. Toyama, M.J. Kelly, J.D. Gross, and J.S. Weissman The structural basis of yeast prion strain variants Nature 449 2007 233 237 (Pubitemid 47402368)
-
(2007)
Nature
, vol.449
, Issue.7159
, pp. 233-237
-
-
Toyama, B.H.1
Kelly, M.J.S.2
Gross, J.D.3
Weissman, J.S.4
-
120
-
-
26944496813
-
Regions of tau implicated in the paired helical fragment core as defined by NMR
-
DOI 10.1002/cbic.200400452
-
A. Sillen, A. Leroy, J.M. Wieruszeski, A. Loyens, J.C. Beauvillain, L. Buee, I. Landrieu, and G. Lippens Regions of tau implicated in the paired helical fragment core as defined by NMR Chembiochem 6 2005 1849 1856 (Pubitemid 41475278)
-
(2005)
ChemBioChem
, vol.6
, Issue.10
, pp. 1849-1856
-
-
Sillen, A.1
Leroy, A.2
Wieruszeski, J.-M.3
Loyens, A.4
Beauvillain, J.-C.5
Buee, L.6
Landrieu, I.7
Lippens, G.8
-
121
-
-
33644555501
-
Cytochrome display on amyloid fibrils
-
A.J. Baldwin, R. Bader, J. Christodoulou, C.E. MacPhee, C.M. Dobson, and P.D. Barker Cytochrome display on amyloid fibrils J. Am. Chem. Soc. 128 2006 2162 2163
-
(2006)
J. Am. Chem. Soc.
, vol.128
, pp. 2162-2163
-
-
Baldwin, A.J.1
Bader, R.2
Christodoulou, J.3
MacPhee, C.E.4
Dobson, C.M.5
Barker, P.D.6
-
122
-
-
33749533047
-
Observation of highly flexible residues in amyloid fibrils of the HET-s prion
-
DOI 10.1021/ja063639x
-
A.B. Siemer, A.A. Arnold, C. Ritter, T. Westfeld, M. Ernst, R. Riek, and B.H. Meier Observation of highly flexible residues in amyloid fibrils of the HET-s prion J. Am. Chem. Soc. 128 2006 13224 13228 (Pubitemid 44527692)
-
(2006)
Journal of the American Chemical Society
, vol.128
, Issue.40
, pp. 13224-13228
-
-
Siemer, A.B.1
Arnold, A.A.2
Ritter, C.3
Westfeld, T.4
Ernst, M.5
Riek, R.6
Meier, B.H.7
-
123
-
-
34548041439
-
Characterisation of Amyloid Fibril Formation by Small Heat-shock Chaperone Proteins Human αA-, αB- and R120G αB-Crystallins
-
DOI 10.1016/j.jmb.2007.06.060, PII S0022283607008674
-
S. Meehan, T.P. Knowles, A.J. Baldwin, J.F. Smith, A.M. Squires, P. Clements, T.M. Treweek, H. Ecroyd, G.G. Tartaglia, M. Vendruscolo, C.E. Macphee, C.M. Dobson, and J.A. Carver Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallins J. Mol. Biol. 372 2007 470 484 (Pubitemid 47277407)
-
(2007)
Journal of Molecular Biology
, vol.372
, Issue.2
, pp. 470-484
-
-
Meehan, S.1
Knowles, T.P.J.2
Baldwin, A.J.3
Smith, J.F.4
Squires, A.M.5
Clements, P.6
Treweek, T.M.7
Ecroyd, H.8
Tartaglia, G.G.9
Vendruscolo, M.10
MacPhee, C.E.11
Dobson, C.M.12
Carver, J.A.13
-
124
-
-
6344277434
-
2- microglobulin probed by guanidine-hydrochloride-induced unfolding
-
DOI 10.1016/j.febslet.2004.09.024, PII S0014579304011408
-
T. Narimoto, K. Sakurai, A. Okamoto, E. Chatani, M. Hoshino, K. Hasegawa, H. Naiki, and Y. Goto Conformational stability of amyloid fibrils of beta2-microglobulin probed by guanidine-hydrochloride-induced unfolding FEBS Lett. 576 2004 313 319 (Pubitemid 39388619)
-
(2004)
FEBS Letters
, vol.576
, Issue.3
, pp. 313-319
-
-
Narimoto, T.1
Sakurai, K.2
Okamoto, A.3
Chatani, E.4
Hoshino, M.5
Hasegawa, K.6
Naiki, H.7
Goto, Y.8
-
125
-
-
0344603844
-
The hydrogen exchange core and protein folding
-
R. Li, and C. Woodward The hydrogen exchange core and protein folding Protein Sci. 8 1999 1571 1590
-
(1999)
Protein Sci.
, vol.8
, pp. 1571-1590
-
-
Li, R.1
Woodward, C.2
-
126
-
-
84860013075
-
Structure of an intermediate state in protein folding and aggregation
-
P. Neudecker, P. Robustelli, A. Cavalli, P. Walsh, P. Lundström, A. Zarrine-Afsar, S. Sharpe, M. Vendruscolo, and L.E. Kay Structure of an intermediate state in protein folding and aggregation Science 336 2012 362 366
-
(2012)
Science
, vol.336
, pp. 362-366
-
-
Neudecker, P.1
Robustelli, P.2
Cavalli, A.3
Walsh, P.4
Lundström, P.5
Zarrine-Afsar, A.6
Sharpe, S.7
Vendruscolo, M.8
Kay, L.E.9
-
127
-
-
10744219788
-
2- Microglobulin and Amyloidogenesis
-
DOI 10.1074/jbc.M310779200
-
A. Corazza, F. Pettirossi, P. Viglino, G. Verdone, J. Garcia, P. Dumy, S. Giorgetti, P. Mangione, S. Raimondi, M. Stoppini, V. Bellotti, and G. Esposito Properties of some variants of human beta2-microglobulin and amyloidogenesis J. Biol. Chem. 279 2004 9176 9189 (Pubitemid 38295981)
-
(2004)
Journal of Biological Chemistry
, vol.279
, Issue.10
, pp. 9176-9189
-
-
Corazza, A.1
Pettirossi, F.2
Viglino, P.3
Verdone, G.4
Garcia, J.5
Dumy, P.6
Giorgetti, S.7
Mangione, P.8
Raimondi, S.9
Stoppini, M.10
Bellotti, V.11
Esposito, G.12
-
128
-
-
41949130213
-
The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties
-
G. Esposito, S. Ricagno, A. Corazza, E. Rennella, D. Gumral, M.C. Mimmi, E. Betto, C.E. Pucillo, F. Fogolari, P. Viglino, S. Raimondi, S. Giorgetti, B. Bolognesi, G. Merlini, M. Stoppini, M. Bolognesi, and V. Bellotti The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties J. Mol. Biol. 378 2008 887 897
-
(2008)
J. Mol. Biol.
, vol.378
, pp. 887-897
-
-
Esposito, G.1
Ricagno, S.2
Corazza, A.3
Rennella, E.4
Gumral, D.5
Mimmi, M.C.6
Betto, E.7
Pucillo, C.E.8
Fogolari, F.9
Viglino, P.10
Raimondi, S.11
Giorgetti, S.12
Bolognesi, B.13
Merlini, G.14
Stoppini, M.15
Bolognesi, M.16
Bellotti, V.17
-
129
-
-
77955086949
-
Folding and fibrillogenesis: Clues from beta2-microglobulin
-
E. Rennella, A. Corazza, S. Giorgetti, F. Fogolari, P. Viglino, R. Porcari, L. Verga, M. Stoppini, V. Bellotti, and G. Esposito Folding and fibrillogenesis: clues from beta2-microglobulin J. Mol. Biol. 401 2010 286 297
-
(2010)
J. Mol. Biol.
, vol.401
, pp. 286-297
-
-
Rennella, E.1
Corazza, A.2
Giorgetti, S.3
Fogolari, F.4
Viglino, P.5
Porcari, R.6
Verga, L.7
Stoppini, M.8
Bellotti, V.9
Esposito, G.10
-
130
-
-
77949320904
-
Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein beta2-microglobulin revealed by real-time two-dimensional NMR
-
A. Corazza, E. Rennella, P. Schanda, M.C. Mimmi, T. Cutuil, S. Raimondi, S. Giorgetti, F. Fogolari, P. Viglino, L. Frydman, M. Gal, V. Bellotti, B. Brutscher, and G. Esposito Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein beta2-microglobulin revealed by real-time two-dimensional NMR J. Biol. Chem. 285 2010 5827 5835
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 5827-5835
-
-
Corazza, A.1
Rennella, E.2
Schanda, P.3
Mimmi, M.C.4
Cutuil, T.5
Raimondi, S.6
Giorgetti, S.7
Fogolari, F.8
Viglino, P.9
Frydman, L.10
Gal, M.11
Bellotti, V.12
Brutscher, B.13
Esposito, G.14
-
131
-
-
79953250721
-
Transient formation of intermediate conformational states of amyloid-beta peptide revealed by heteronuclear magnetic resonance spectroscopy
-
T. Yamaguchi, K. Matsuzaki, and M. Hoshino Transient formation of intermediate conformational states of amyloid-beta peptide revealed by heteronuclear magnetic resonance spectroscopy FEBS Lett. 585 2011 1097 1102
-
(2011)
FEBS Lett.
, vol.585
, pp. 1097-1102
-
-
Yamaguchi, T.1
Matsuzaki, K.2
Hoshino, M.3
-
132
-
-
84863116610
-
Aggregation of alpha-synuclein is kinetically controlled by intramolecular diffusion
-
B. Ahmad, Y. Chen, and L.J. Lapidus Aggregation of alpha-synuclein is kinetically controlled by intramolecular diffusion Proc. Natl. Acad. Sci. U. S. A. 109 2012 2336 2341
-
(2012)
Proc. Natl. Acad. Sci. U. S. A.
, vol.109
, pp. 2336-2341
-
-
Ahmad, B.1
Chen, Y.2
Lapidus, L.J.3
-
133
-
-
0035815664
-
Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation
-
DOI 10.1074/jbc.M010907200
-
V.N. Uversky, J. Li, and A.L. Fink Evidence for a partially folded intermediate in alpha-synuclein fibril formation J. Biol. Chem. 276 2001 10737 10744 (Pubitemid 38089246)
-
(2001)
Journal of Biological Chemistry
, vol.276
, Issue.14
, pp. 10737-10744
-
-
Uversky, V.N.1
Li, J.2
Fink, A.L.3
-
134
-
-
13444252277
-
Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein
-
DOI 10.1073/pnas.0407146102
-
C.W. Bertoncini, Y.S. Jung, C.O. Fernandez, W. Hoyer, C. Griesinger, T.M. Jovin, and M. Zweckstetter Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein Proc. Natl. Acad. Sci. U. S. A. 102 2005 1430 1435 (Pubitemid 40209187)
-
(2005)
Proceedings of the National Academy of Sciences of the United States of America
, vol.102
, Issue.5
, pp. 1430-1435
-
-
Bertoncini, C.W.1
Jung, Y.-S.2
Fernandez, C.O.3
Hoyer, W.4
Griesinger, C.5
Jovin, T.M.6
Zweckstetter, M.7
-
135
-
-
24744461907
-
Familial mutants of α-synuclein with increased neurotoxicity have a destabilized conformation
-
DOI 10.1074/jbc.C500288200
-
C.W. Bertoncini, C.O. Fernandez, C. Griesinger, T.M. Jovin, and M. Zweckstetter Familial mutants of alpha-synuclein with increased neurotoxicity have a destabilized conformation J. Biol. Chem. 280 2005 30649 30652 (Pubitemid 41291792)
-
(2005)
Journal of Biological Chemistry
, vol.280
, Issue.35
, pp. 30649-30652
-
-
Bertoncini, C.W.1
Fernandez, C.O.2
Griesinger, C.3
Jovin, T.M.4
Zweckstetter, M.5
-
136
-
-
12944304172
-
Mapping long-range interactions in α-synuclein using spin-label NMR and ensemble molecular dynamics simulations
-
DOI 10.1021/ja044834j
-
M.M. Dedmon, K. Lindorff-Larsen, J. Christodoulou, M. Vendruscolo, and C.M. Dobson Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations J. Am. Chem. Soc. 127 2005 476 477 (Pubitemid 40174345)
-
(2005)
Journal of the American Chemical Society
, vol.127
, Issue.2
, pp. 476-477
-
-
Dedmon, M.M.1
Lindorff-Larsen, K.2
Christodoulou, J.3
Vendruscolo, M.4
Dobson, C.M.5
-
137
-
-
33750072302
-
2-microglobulin probed by tryptophan mutagenesis
-
DOI 10.1074/jbc.M605358200
-
M. Kihara, E. Chatani, K. Iwata, K. Yamamoto, T. Matsuura, A. Nakagawa, H. Naiki, and Y. Goto Conformation of amyloid fibrils of beta2-microglobulin probed by tryptophan mutagenesis J. Biol. Chem. 281 2006 31061 31069 (Pubitemid 44582161)
-
(2006)
Journal of Biological Chemistry
, vol.281
, Issue.41
, pp. 31061-31069
-
-
Kihara, M.1
Chatani, E.2
Iwata, K.3
Yamamoto, K.4
Matsuura, T.5
Nakagawa, A.6
Naiki, H.7
Goto, Y.8
-
138
-
-
0344872503
-
A left-handed 3″1 helical conformation in the Alzheimer Aβ(12-28) peptide
-
DOI 10.1016/S0014-5793(03)01293-6
-
J. Jarvet, P. Damberg, J. Danielsson, I. Johansson, L.E. Eriksson, and A. Graslund A left-handed 3(1) helical conformation in the Alzheimer Abeta(12-28) peptide FEBS Lett. 555 2003 371 374 (Pubitemid 37486058)
-
(2003)
FEBS Letters
, vol.555
, Issue.2
, pp. 371-374
-
-
Jarvet, J.1
Damberg, P.2
Danielsson, J.3
Johansson, I.4
Eriksson, L.E.G.5
Graslund, A.6
-
139
-
-
18244412979
-
Removal of the N-terminal hexapeptide from human β2-microglobulin facilities protein aggregation and fibril formation
-
G. Esposito, R. Michelutti, G. Verdone, P. Viglino, H. Hernandez, C.V. Robinson, A. Amoresano, F. Dal Piaz, M. Monti, P. Pucci, P. Mangione, M. Stoppini, G. Merlini, G. Ferri, and V. Bellotti Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation Protein Sci. 9 2000 831 845 (Pubitemid 30353325)
-
(2000)
Protein Science
, vol.9
, Issue.5
, pp. 831-845
-
-
Esposito, G.1
Michelutti, R.2
Verdone, G.3
Viglino, P.4
Hernandez, H.5
Robinson, C.V.6
Amoresano, A.7
Dal Piaz, F.8
Monti, M.9
Pucci, P.10
Mangione, P.11
Stoppini, M.12
Merlini, G.13
Ferri, G.14
Bellotti, V.15
-
140
-
-
0037173120
-
Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy
-
DOI 10.1073/pnas.132098999
-
J.H. Ippel, A. Olofsson, J. Schleucher, E. Lundgren, and S.S. Wijmenga Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy Proc. Natl. Acad. Sci. U. S. A. 99 2002 8648 8653 (Pubitemid 34693614)
-
(2002)
Proceedings of the National Academy of Sciences of the United States of America
, vol.99
, Issue.13
, pp. 8648-8653
-
-
Ippel, J.H.1
Olofsson, A.2
Schleucher, J.3
Lundgren, E.4
Wijmenga, S.S.5
-
141
-
-
0034003742
-
Microscopic stability of cold shock protein a examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide
-
V.A. Jaravine, K. Rathgeb-Szabo, and A.T. Alexandrescu Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide Protein Sci. 9 2000 290 301 (Pubitemid 30127002)
-
(2000)
Protein Science
, vol.9
, Issue.2
, pp. 290-301
-
-
Jaravine, V.A.1
Rathgeb-Szabo, K.2
Alexandrescu, A.T.3
-
142
-
-
0032483047
-
Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: Evidence for conformational dynamics in the single-stranded RNA-binding site
-
DOI 10.1021/bi980269j, PII S0006296098002694
-
W. Feng, R. Tejero, D.E. Zimmerman, M. Inouye, and G.T. Montelione Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: evidence for conformational dynamics in the single-stranded RNA-binding site Biochemistry 37 1998 10881 10896 (Pubitemid 28368912)
-
(1998)
Biochemistry
, vol.37
, Issue.31
, pp. 10881-10896
-
-
Feng, W.1
Tejero, R.2
Zimmerman, D.E.3
Inouye, M.4
Montelione, G.T.5
-
143
-
-
0037257421
-
Hydrogen exchange studies on Alzheimer's amyloid-β peptides by mass spectrometry using matrix-assisted laser desorption/ionization and electrospray ionization
-
DOI 10.1002/rcm.901
-
M. Kraus, M. Bienert, and E. Krause Hydrogen exchange studies on Alzheimer's amyloid-beta peptides by mass spectrometry using matrix-assisted laser desorption/ionization and electrospray ionization Rapid Commun. Mass Spectrom. 17 2003 222 228 (Pubitemid 36164170)
-
(2003)
Rapid Communications in Mass Spectrometry
, vol.17
, Issue.3
, pp. 222-228
-
-
Kraus, M.1
Bienert, M.2
Krause, E.3
-
144
-
-
1942438614
-
Folding into a β-Hairpin Can Prevent Amyloid Fibril-Formation
-
DOI 10.1021/bi036248t
-
W. Hosia, N. Bark, E. Liepinsh, A. Tjernberg, B. Persson, D. Hallen, J. Thyberg, J. Johansson, and L. Tjernberg Folding into a beta-hairpin can prevent amyloid fibril formation Biochemistry 43 2004 4655 4661 (Pubitemid 38509085)
-
(2004)
Biochemistry
, vol.43
, Issue.16
, pp. 4655-4661
-
-
Hosia, W.1
Bark, N.2
Liepinsh, E.3
Tjernberg, A.4
Persson, B.5
Hallen, D.6
Thyberg, J.7
Johansson, J.8
Tjernberg, L.9
-
145
-
-
77953082435
-
A single destabilizing mutation (F9S) promotes concerted unfolding of an entire globular domain in gammaS-crystallin
-
S. Lee, B. Mahler, J. Toward, B. Jones, K. Wyatt, L. Dong, G. Wistow, and Z. Wu A single destabilizing mutation (F9S) promotes concerted unfolding of an entire globular domain in gammaS-crystallin J. Mol. Biol. 399 2010 320 330
-
(2010)
J. Mol. Biol.
, vol.399
, pp. 320-330
-
-
Lee, S.1
Mahler, B.2
Toward, J.3
Jones, B.4
Wyatt, K.5
Dong, L.6
Wistow, G.7
Wu, Z.8
-
146
-
-
78650871880
-
Characterization of a transient unfolding intermediate in a core mutant of gammaS-crystallin
-
B. Mahler, K. Doddapaneni, I. Kleckner, C. Yuan, G. Wistow, and Z. Wu Characterization of a transient unfolding intermediate in a core mutant of gammaS-crystallin J. Mol. Biol. 405 2011 840 850
-
(2011)
J. Mol. Biol.
, vol.405
, pp. 840-850
-
-
Mahler, B.1
Doddapaneni, K.2
Kleckner, I.3
Yuan, C.4
Wistow, G.5
Wu, Z.6
-
147
-
-
0033555275
-
Solution structures of micelle-bound amyloid β-(1-40) and β-(1-42) peptides of Alzheimer's disease
-
DOI 10.1006/jmbi.1998.2348
-
H. Shao, S. Jao, K. Ma, and M.G. Zagorski Solution structures of micelle-bound amyloid beta-(1-40) and beta-(1-42) peptides of Alzheimer's disease J. Mol. Biol. 285 1999 755 773 (Pubitemid 29041806)
-
(1999)
Journal of Molecular Biology
, vol.285
, Issue.2
, pp. 755-773
-
-
Shao, H.1
Jao, S.-C.2
Ma, K.3
Zagorski, M.G.4
-
148
-
-
33845665797
-
High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid β-peptide
-
DOI 10.1111/j.1742-4658.2006.05563.x
-
J. Danielsson, R. Pierattelli, L. Banci, and A. Graslund High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid beta-peptide FEBS J. 274 2007 46 59 (Pubitemid 44952897)
-
(2007)
FEBS Journal
, vol.274
, Issue.1
, pp. 46-59
-
-
Danielsson, J.1
Pierattelli, R.2
Banci, L.3
Graslund, A.4
-
149
-
-
13544249978
-
Alzheimer's Aβ40 studied by NMR at low pH reveals that sodium 4,4-dimethyl-4-silapentane-1-sulfonate (DSS) binds and promotes β-ball oligomerization
-
DOI 10.1074/jbc.M409507200
-
D.V. Laurents, P.M. Gorman, M. Guo, M. Rico, A. Chakrabartty, and M. Bruix Alzheimer's Abeta40 studied by NMR at low pH reveals that sodium 4,4-dimethyl-4-silapentane-1-sulfonate (DSS) binds and promotes beta-ball oligomerization J. Biol. Chem. 280 2005 3675 3685 (Pubitemid 40223835)
-
(2005)
Journal of Biological Chemistry
, vol.280
, Issue.5
, pp. 3675-3685
-
-
Laurents, D.V.1
Gorman, P.M.2
Guo, M.3
Rico, M.4
Chakrabartty, A.5
Bruix, M.6
-
150
-
-
79954631896
-
Hydrogen exchange mass spectrometry as an analytical tool for the analysis of amyloid fibrillogenesis
-
C. Scavenius, S. Ghodke, D.E. Otzen, and J.J. Enghild Hydrogen exchange mass spectrometry as an analytical tool for the analysis of amyloid fibrillogenesis Int. J. Mass Spectrom. 302 2011 167 173
-
(2011)
Int. J. Mass Spectrom.
, vol.302
, pp. 167-173
-
-
Scavenius, C.1
Ghodke, S.2
Otzen, D.E.3
Enghild, J.J.4
-
151
-
-
15544388942
-
1-40 amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy
-
DOI 10.1021/bi048292u
-
N.A. Whittemore, R. Mishra, I. Kheterpal, A.D. Williams, R. Wetzel, and E.H. Serpersu Hydrogen-deuterium (H/D) exchange mapping of Abeta 1-40 amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy Biochemistry 44 2005 4434 4441 (Pubitemid 40403985)
-
(2005)
Biochemistry
, vol.44
, Issue.11
, pp. 4434-4441
-
-
Whittemore, N.A.1
Mishra, R.2
Kheterpal, I.3
Williams, A.D.4
Wetzel, R.5
Serpersu, E.H.6
-
152
-
-
80053294730
-
Abeta peptide fibrillar architectures controlled by conformational constraints of the monomer
-
K. Brannstrom, A. Ohman, and A. Olofsson Abeta peptide fibrillar architectures controlled by conformational constraints of the monomer PLoS One 6 2011 e25157
-
(2011)
PLoS One
, vol.6
, pp. 25157
-
-
Brannstrom, K.1
Ohman, A.2
Olofsson, A.3
-
153
-
-
0034610180
-
Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchange
-
I. Kheterpal, S. Zhou, K.D. Cook, and R. Wetzel Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchange Proc. Natl. Acad. Sci. U. S. A. 97 2000 13597 13601
-
(2000)
Proc. Natl. Acad. Sci. U. S. A.
, vol.97
, pp. 13597-13601
-
-
Kheterpal, I.1
Zhou, S.2
Cook, K.D.3
Wetzel, R.4
-
154
-
-
0042572518
-
Hydrogen exchange-mass spectrometry analysis of β-amyloid peptide structure
-
DOI 10.1021/bi0342766
-
S.S. Wang, S.A. Tobler, T.A. Good, and E.J. Fernandez Hydrogen exchange-mass spectrometry analysis of beta-amyloid peptide structure Biochemistry 42 2003 9507 9514 (Pubitemid 36959259)
-
(2003)
Biochemistry
, vol.42
, Issue.31
, pp. 9507-9514
-
-
Wang, S.S.-S.1
Tobler, S.A.2
Good, T.A.3
Fernandez, E.J.4
-
155
-
-
0345060507
-
Aβ Protofibrils Possess a Stable Core Structure Resistant to Hydrogen Exchange
-
DOI 10.1021/bi0357816
-
I. Kheterpal, H.A. Lashuel, D.M. Hartley, T. Walz, P.T. Lansbury Jr., and R. Wetzel Abeta protofibrils possess a stable core structure resistant to hydrogen exchange Biochemistry 42 2003 14092 14098 (Pubitemid 37499405)
-
(2003)
Biochemistry
, vol.42
, Issue.48
, pp. 14092-14098
-
-
Kheterpal, I.1
Lashuel, H.A.2
Hartley, D.M.3
Walz, T.4
Lansbury Jr., P.T.5
Wetzel, R.6
-
156
-
-
48649109730
-
Simultaneous monitoring of peptide aggregate distributions, structure, and kinetics using amide hydrogen exchange: Application to Abeta(1-40) fibrillogenesis
-
W. Qi, A. Zhang, D. Patel, S. Lee, J.L. Harrington, L. Zhao, D. Schaefer, T.A. Good, and E.J. Fernandez Simultaneous monitoring of peptide aggregate distributions, structure, and kinetics using amide hydrogen exchange: application to Abeta(1-40) fibrillogenesis Biotechnol. Bioeng. 100 2008 1214 1227
-
(2008)
Biotechnol. Bioeng.
, vol.100
, pp. 1214-1227
-
-
Qi, W.1
Zhang, A.2
Patel, D.3
Lee, S.4
Harrington, J.L.5
Zhao, L.6
Schaefer, D.7
Good, T.A.8
Fernandez, E.J.9
-
157
-
-
68749115231
-
Membrane interactions of a self-assembling model peptide that mimics the self-association, structure and toxicity of Abeta(1-40)
-
L.C. Salay, W. Qi, B. Keshet, L.K. Tamm, and E.J. Fernandez Membrane interactions of a self-assembling model peptide that mimics the self-association, structure and toxicity of Abeta(1-40) Biochim. Biophys. Acta 1788 2009 1714 1721
-
(2009)
Biochim. Biophys. Acta
, vol.1788
, pp. 1714-1721
-
-
Salay, L.C.1
Qi, W.2
Keshet, B.3
Tamm, L.K.4
Fernandez, E.J.5
-
158
-
-
70349272854
-
Two disaccharides and trimethylamine N-oxide affect Abeta aggregation differently, but all attenuate oligomer-induced membrane permeability
-
W. Qi, A. Zhang, T.A. Good, and E.J. Fernandez Two disaccharides and trimethylamine N-oxide affect Abeta aggregation differently, but all attenuate oligomer-induced membrane permeability Biochemistry 48 2009 8908 8919
-
(2009)
Biochemistry
, vol.48
, pp. 8908-8919
-
-
Qi, W.1
Zhang, A.2
Good, T.A.3
Fernandez, E.J.4
-
159
-
-
61549108314
-
Structural differences between Abeta(1-40) intermediate oligomers and fibrils elucidated by proteolytic fragmentation and hydrogen/deuterium exchange
-
A. Zhang, W. Qi, T.A. Good, and E.J. Fernandez Structural differences between Abeta(1-40) intermediate oligomers and fibrils elucidated by proteolytic fragmentation and hydrogen/deuterium exchange Biophys. J. 96 2009 1091 1104
-
(2009)
Biophys. J.
, vol.96
, pp. 1091-1104
-
-
Zhang, A.1
Qi, W.2
Good, T.A.3
Fernandez, E.J.4
-
160
-
-
77956782713
-
Structural similarity between the prion domain of HET-s and a homologue can explain amyloid cross-seeding in spite of limited sequence identity
-
C. Wasmer, A. Zimmer, R. Sabate, A. Soragni, S.J. Saupe, C. Ritter, and B.H. Meier Structural similarity between the prion domain of HET-s and a homologue can explain amyloid cross-seeding in spite of limited sequence identity J. Mol. Biol. 402 2010 311 325
-
(2010)
J. Mol. Biol.
, vol.402
, pp. 311-325
-
-
Wasmer, C.1
Zimmer, A.2
Sabate, R.3
Soragni, A.4
Saupe, S.J.5
Ritter, C.6
Meier, B.H.7
-
161
-
-
0037372212
-
Enhanced correction methods for hydrogen exchange-mass spectrometric studies of amyloid fibrils
-
DOI 10.1110/ps.0225703
-
I. Kheterpal, R. Wetzel, and K.D. Cook Enhanced correction methods for hydrogen exchange-mass spectrometric studies of amyloid fibrils Protein Sci. 12 2003 635 643 (Pubitemid 36241120)
-
(2003)
Protein Science
, vol.12
, Issue.3
, pp. 635-643
-
-
Kheterpal, I.1
Wetzel, R.2
Cook, K.D.3
-
162
-
-
18844427273
-
Structural properties of Aβ protofibrils stabilized by a small molecule
-
DOI 10.1073/pnas.0408582102
-
A.D. Williams, M. Sega, M. Chen, I. Kheterpal, M. Geva, V. Berthelier, D.T. Kaleta, K.D. Cook, and R. Wetzel Structural properties of Abeta protofibrils stabilized by a small molecule Proc. Natl. Acad. Sci. U. S. A. 102 2005 7115 7120 (Pubitemid 40696343)
-
(2005)
Proceedings of the National Academy of Sciences of the United States of America
, vol.102
, Issue.20
, pp. 7115-7120
-
-
Williams, A.D.1
Sega, M.2
Chen, M.3
Kheterpal, I.4
Geva, M.5
Berthelier, V.6
Kaleta, D.T.7
Cook, K.D.8
Wetzel, R.9
-
163
-
-
33746781304
-
Structural Differences in Aβ Amyloid Protofibrils and Fibrils Mapped by Hydrogen Exchange - Mass Spectrometry with On-line Proteolytic Fragmentation
-
DOI 10.1016/j.jmb.2006.06.066, PII S0022283606008102
-
I. Kheterpal, M. Chen, K.D. Cook, and R. Wetzel Structural differences in Abeta amyloid protofibrils and fibrils mapped by hydrogen exchange-mass spectrometry with on-line proteolytic fragmentation J. Mol. Biol. 361 2006 785 795 (Pubitemid 44177742)
-
(2006)
Journal of Molecular Biology
, vol.361
, Issue.4
, pp. 785-795
-
-
Kheterpal, I.1
Chen, M.2
Cook, K.D.3
Wetzel, R.4
-
164
-
-
33846458989
-
A Triaxial Probe for On-line Proteolysis Coupled with Hydrogen/Deuterium Exchange-Electrospray Mass Spectrometry
-
DOI 10.1016/j.jasms.2006.09.011, PII S1044030506008282
-
M. Chen, K.D. Cook, I. Kheterpal, and R. Wetzel A triaxial probe for on-line proteolysis coupled with hydrogen/deuterium exchange-electrospray mass spectrometry J. Am. Soc. Mass Spectrom. 18 2007 208 217 (Pubitemid 46150090)
-
(2007)
Journal of the American Society for Mass Spectrometry
, vol.18
, Issue.2
, pp. 208-217
-
-
Chen, M.1
Cook, K.D.2
Kheterpal, I.3
Wetzel, R.4
-
165
-
-
79955406741
-
Abeta40 and Abeta42 amyloid fibrils exhibit distinct molecular recycling properties
-
L. Sanchez, S. Madurga, T. Pukala, M. Vilaseca, C. Lopez-Iglesias, C.V. Robinson, E. Giralt, and N. Carulla Abeta40 and Abeta42 amyloid fibrils exhibit distinct molecular recycling properties J. Am. Chem. Soc. 133 2011 6505 6508
-
(2011)
J. Am. Chem. Soc.
, vol.133
, pp. 6505-6508
-
-
Sanchez, L.1
Madurga, S.2
Pukala, T.3
Vilaseca, M.4
Lopez-Iglesias, C.5
Robinson, C.V.6
Giralt, E.7
Carulla, N.8
-
166
-
-
20444458341
-
Correlation of structural elements and infectivity of the HET-s prion
-
DOI 10.1038/nature03793
-
C. Ritter, M.L. Maddelein, A.B. Siemer, T. Luhrs, M. Ernst, B.H. Meier, S.J. Saupe, and R. Riek Correlation of structural elements and infectivity of the HET-s prion Nature 435 2005 844 848 (Pubitemid 40839737)
-
(2005)
Nature
, vol.435
, Issue.7043
, pp. 844-848
-
-
Ritter, C.1
Maddelein, M.-L.2
Siemer, A.B.3
Luhrs, T.4
Ernst, M.5
Meier, B.H.6
Saupe, S.J.7
Riek, R.8
-
167
-
-
78650914809
-
Probing water accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR
-
H. Van Melckebeke, P. Schanda, J. Gath, C. Wasmer, R. Verel, A. Lange, B.H. Meier, and A. Bockmann Probing water accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR J. Mol. Biol. 405 2011 765 772
-
(2011)
J. Mol. Biol.
, vol.405
, pp. 765-772
-
-
Van Melckebeke, H.1
Schanda, P.2
Gath, J.3
Wasmer, C.4
Verel, R.5
Lange, A.6
Meier, B.H.7
Bockmann, A.8
-
168
-
-
17144398382
-
Probing the structure of the infectious amyloid form of the prion-forming domain of HET-s using high resolution hydrogen/deuterium exchange monitored by mass spectrometry
-
DOI 10.1074/jbc.M413185200
-
A. Nazabal, M.L. Maddelein, M. Bonneu, S.J. Saupe, and J.M. Schmitter Probing the structure of the infectious amyloid form of the prion-forming domain of HET-s using high resolution hydrogen/deuterium exchange monitored by mass spectrometry J. Biol. Chem. 280 2005 13220 13228 (Pubitemid 40517205)
-
(2005)
Journal of Biological Chemistry
, vol.280
, Issue.14
, pp. 13220-13228
-
-
Nazabal, A.1
Maddelein, M.-L.2
Bonneu, M.3
Saupe, S.J.4
Schmitter, J.-M.5
-
169
-
-
19544372819
-
218-295 prion protein
-
DOI 10.1002/jms.819
-
A. Nazabal, M. Bonneu, S.J. Saupe, and J.M. Schmitter High-resolution H/D exchange studies on the HET-s218-295 prion protein J. Mass Spectrom. 40 2005 580 590 (Pubitemid 40733315)
-
(2005)
Journal of Mass Spectrometry
, vol.40
, Issue.5
, pp. 580-590
-
-
Nazabal, A.1
Bonneu, M.2
Saupe, S.J.3
Schmitter, J.-M.4
-
170
-
-
1542600164
-
Mapping Aβ amyloid fibril secondary structure using scanning proline mutagenesis
-
DOI 10.1016/j.jmb.2003.11.008, PII S0022283603013925
-
A.D. Williams, E. Portelius, I. Kheterpal, J.T. Guo, K.D. Cook, Y. Xu, and R. Wetzel Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis J. Mol. Biol. 335 2004 833 842 (Pubitemid 38352823)
-
(2004)
Journal of Molecular Biology
, vol.335
, Issue.3
, pp. 833-842
-
-
Williams, A.D.1
Portelius, E.2
Kheterpal, I.3
Guo, J.-T.4
Cook, K.D.5
Xu, Y.6
Wetzel, R.7
-
171
-
-
28444442999
-
3D structure of Alzheimer's amyloid-beta(1-42) fibrils
-
T. Luhrs, C. Ritter, M. Adrian, D. Riek-Loher, B. Bohrmann, H. Dobeli, D. Schubert, and R. Riek 3D structure of Alzheimer's amyloid-beta(1-42) fibrils Proc. Natl. Acad. Sci. U. S. A. 102 2005 17342 17347
-
(2005)
Proc. Natl. Acad. Sci. U. S. A.
, vol.102
, pp. 17342-17347
-
-
Luhrs, T.1
Ritter, C.2
Adrian, M.3
Riek-Loher, D.4
Bohrmann, B.5
Dobeli, H.6
Schubert, D.7
Riek, R.8
-
172
-
-
21744448854
-
Ethanol-perturbed amyloidogenic self-assembly of insulin: Looking for origins of amyloid strains
-
DOI 10.1021/bi050281t
-
W. Dzwolak, S. Grudzielanek, V. Smirnovas, R. Ravindra, C. Nicolini, R. Jansen, A. Loksztejn, S. Porowski, and R. Winter Ethanol-perturbed amyloidogenic self-assembly of insulin: looking for origins of amyloid strains Biochemistry 44 2005 8948 8958 (Pubitemid 40943212)
-
(2005)
Biochemistry
, vol.44
, Issue.25
, pp. 8948-8958
-
-
Dzwolak, W.1
Grudzielanek, S.2
Smirnovas, V.3
Ravindra, R.4
Nicolini, C.5
Jansen, R.6
Loksztejn, A.7
Porowski, S.8
Winter, R.9
-
173
-
-
33745610089
-
New insights into the self-assembly of insulin amyloid fibrils: An H-D exchange FT-IR study
-
DOI 10.1021/bi060341a
-
W. Dzwolak, A. Loksztejn, and V. Smirnovas New insights into the self-assembly of insulin amyloid fibrils: an H-D exchange FT-IR study Biochemistry 45 2006 8143 8151 (Pubitemid 43993235)
-
(2006)
Biochemistry
, vol.45
, Issue.26
, pp. 8143-8151
-
-
Dzwolak, W.1
Loksztejn, A.2
Smirnovas, V.3
-
174
-
-
76849100851
-
Online, high-pressure digestion system for protein characterization by hydrogen/deuterium exchange and mass spectrometry
-
L.M. Jones, H. Zhang, I. Vidavsky, and M.L. Gross Online, high-pressure digestion system for protein characterization by hydrogen/deuterium exchange and mass spectrometry Anal. Chem. 82 2010 1171 1174
-
(2010)
Anal. Chem.
, vol.82
, pp. 1171-1174
-
-
Jones, L.M.1
Zhang, H.2
Vidavsky, I.3
Gross, M.L.4
-
175
-
-
79960003359
-
Conformer-specific hydrogen exchange analysis of Abeta(1-42) oligomers by top-down electron capture dissociation mass spectrometry
-
J. Pan, J. Han, C.H. Borchers, and L. Konermann Conformer-specific hydrogen exchange analysis of Abeta(1-42) oligomers by top-down electron capture dissociation mass spectrometry Anal. Chem. 83 2011 5386 5393
-
(2011)
Anal. Chem.
, vol.83
, pp. 5386-5393
-
-
Pan, J.1
Han, J.2
Borchers, C.H.3
Konermann, L.4
-
176
-
-
0034692877
-
Dissecting the hydrogen exchange properties of insulin under amyloid fibril forming conditions: A site-specific investigation by mass spectrometry
-
P. Tito, E.J. Nettleton, and C.V. Robinson Dissecting the hydrogen exchange properties of insulin under amyloid fibril forming conditions: a site-specific investigation by mass spectrometry J. Mol. Biol. 303 2000 267 278
-
(2000)
J. Mol. Biol.
, vol.303
, pp. 267-278
-
-
Tito, P.1
Nettleton, E.J.2
Robinson, C.V.3
-
177
-
-
0033869084
-
Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry
-
E.J. Nettleton, P. Tito, M. Sunde, M. Bouchard, C.M. Dobson, and C.V. Robinson Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry Biophys. J. 79 2000 1053 1065 (Pubitemid 30626196)
-
(2000)
Biophysical Journal
, vol.79
, Issue.2
, pp. 1053-1065
-
-
Nettleton, E.J.1
Tito, P.2
Sunde, M.3
Bouchard, M.4
Dobson, C.M.5
Robinson, C.V.6
-
178
-
-
30044446633
-
Early in the fibrillation of monomeric insulin
-
DOI 10.1074/jbc.M504298200
-
A. Ahmad, V.N. Uversky, D. Hong, and A.L. Fink Early events in the fibrillation of monomeric insulin J. Biol. Chem. 280 2005 42669 42675 (Pubitemid 43049225)
-
(2005)
Journal of Biological Chemistry
, vol.280
, Issue.52
, pp. 42669-42675
-
-
Ahmad, A.1
Uversky, V.N.2
Hong, D.3
Fink, A.L.4
-
179
-
-
0032805423
-
Conformational stability of adsorbed insulin studied with mass spectrometry and hydrogen exchange
-
DOI 10.1021/ac9809433
-
J. Buijs, C. Costa Vera, E. Ayala, E. Steensma, P. Hakansson, and S. Oscarsson Conformational stability of adsorbed insulin studied with mass spectrometry and hydrogen exchange Anal. Chem. 71 1999 3219 3225 (Pubitemid 29372741)
-
(1999)
Analytical Chemistry
, vol.71
, Issue.15
, pp. 3219-3225
-
-
Buijs, J.1
Vera, C.C.2
Ayala, E.3
Steensma, E.4
Hakansson, P.5
Oscarsson, S.6
-
180
-
-
0031573529
-
Monitoring recombinant protein drugs: A study of insulin by H/D exchange and electrospray ionization mass spectrometry
-
R. Ramanathan, M.L. Gross, W.L. Zielinski, and T.P. Layloff Monitoring recombinant protein drugs: a study of insulin by H/D exchange and electrospray ionization mass spectrometry Anal. Chem. 69 1997 5142 5145
-
(1997)
Anal. Chem.
, vol.69
, pp. 5142-5145
-
-
Ramanathan, R.1
Gross, M.L.2
Zielinski, W.L.3
Layloff, T.P.4
-
181
-
-
84857115124
-
Proinsulin C-peptide interferes with insulin fibril formation
-
M. Landreh, J.B. Stukenborg, H. Willander, O. Soder, J. Johansson, and H. Jornvall Proinsulin C-peptide interferes with insulin fibril formation Biochem. Biophys. Res. Commun. 418 2012 489 493
-
(2012)
Biochem. Biophys. Res. Commun.
, vol.418
, pp. 489-493
-
-
Landreh, M.1
Stukenborg, J.B.2
Willander, H.3
Soder, O.4
Johansson, J.5
Jornvall, H.6
-
182
-
-
77951990084
-
Structural and dynamics characteristics of acylphosphatase from Sulfolobus solfataricus in the monomeric state and in the initial native-like aggregates
-
K. Pagano, F. Bemporad, F. Fogolari, G. Esposito, P. Viglino, F. Chiti, and A. Corazza Structural and dynamics characteristics of acylphosphatase from Sulfolobus solfataricus in the monomeric state and in the initial native-like aggregates J. Biol. Chem. 285 2010 14689 14700
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 14689-14700
-
-
Pagano, K.1
Bemporad, F.2
Fogolari, F.3
Esposito, G.4
Viglino, P.5
Chiti, F.6
Corazza, A.7
-
183
-
-
33846847762
-
A Structural Core Within Apolipoprotein C-II Amyloid Fibrils Identified Using Hydrogen Exchange and Proteolysis
-
DOI 10.1016/j.jmb.2006.12.040, PII S0022283606017153
-
L.M. Wilson, Y.F. Mok, K.J. Binger, M.D. Griffin, H.D. Mertens, F. Lin, J.D. Wade, P.R. Gooley, and G.J. Howlett A structural core within apolipoprotein C-II amyloid fibrils identified using hydrogen exchange and proteolysis J. Mol. Biol. 366 2007 1639 1651 (Pubitemid 46215613)
-
(2007)
Journal of Molecular Biology
, vol.366
, Issue.5
, pp. 1639-1651
-
-
Wilson, L.M.1
Mok, Y.-F.2
Binger, K.J.3
Griffin, M.D.W.4
Mertens, H.D.T.5
Lin, F.6
Wade, J.D.7
Gooley, P.R.8
Howlett, G.J.9
-
184
-
-
0036220131
-
Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme
-
DOI 10.1038/nsb768
-
D. Canet, A.M. Last, P. Tito, M. Sunde, A. Spencer, D.B. Archer, C. Redfield, C.V. Robinson, and C.M. Dobson Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme Nat. Struct. Biol. 9 2002 308 315 (Pubitemid 34289905)
-
(2002)
Nature Structural Biology
, vol.9
, Issue.4
, pp. 308-315
-
-
Canet, D.1
Last, A.M.2
Tito, P.3
Sunde, M.4
Spencer, A.5
Archer, D.B.6
Redfield, C.7
Robinson, C.V.8
Dobson, C.M.9
-
185
-
-
24344480244
-
Rationalising lysozyme amyloidosis: Insights from the structure and solution dynamics of T70N lysozyme
-
DOI 10.1016/j.jmb.2005.07.040, PII S0022283605008284
-
R.J. Johnson, J. Christodoulou, M. Dumoulin, G.L. Caddy, M.J. Alcocer, G.J. Murtagh, J.R. Kumita, G. Larsson, C.V. Robinson, D.B. Archer, B. Luisi, and C.M. Dobson Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme J. Mol. Biol. 352 2005 823 836 (Pubitemid 41267071)
-
(2005)
Journal of Molecular Biology
, vol.352
, Issue.4
, pp. 823-836
-
-
Johnson, R.J.K.1
Christodoulou, J.2
Dumoulin, M.3
Caddy, G.L.4
Alcocer, M.J.C.5
Murtagh, G.J.6
Kumita, J.R.7
Larsson, G.8
Robinson, C.V.9
Archer, D.B.10
Luisi, B.11
Dobson, C.M.12
-
186
-
-
13844281065
-
Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations
-
DOI 10.1016/j.jmb.2004.11.020
-
M. Dumoulin, D. Canet, A.M. Last, E. Pardon, D.B. Archer, S. Muyldermans, L. Wyns, A. Matagne, C.V. Robinson, C. Redfield, and C.M. Dobson Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations J. Mol. Biol. 346 2005 773 788 (Pubitemid 40247717)
-
(2005)
Journal of Molecular Biology
, vol.346
, Issue.3
, pp. 773-788
-
-
Dumoulin, M.1
Canet, D.2
Last, A.M.3
Pardon, E.4
Archer, D.B.5
Muyldermans, S.6
Wyns, L.7
Matagne, A.8
Robinson, C.V.9
Redfield, C.10
Dobson, C.M.11
-
187
-
-
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
-
188
-
-
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
-
189
-
-
48249099670
-
Hydrogen exchange of monomeric alpha-synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli
-
R.L. Croke, C.O. Sallum, E. Watson, E.D. Watt, and A.T. Alexandrescu Hydrogen exchange of monomeric alpha-synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli Protein Sci. 17 2008 1434 1445
-
(2008)
Protein Sci.
, vol.17
, pp. 1434-1445
-
-
Croke, R.L.1
Sallum, C.O.2
Watson, E.3
Watt, E.D.4
Alexandrescu, A.T.5
-
190
-
-
27344436619
-
Structure and properties of α-synuclein and other amyloids determined at the amino acid level
-
DOI 10.1073/pnas.0507405102
-
C. Del Mar, E.A. Greenbaum, L. Mayne, S.W. Englander, and V.L. Woods Jr. Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level Proc. Natl. Acad. Sci. U. S. A. 102 2005 15477 15482 (Pubitemid 41528082)
-
(2005)
Proceedings of the National Academy of Sciences of the United States of America
, vol.102
, Issue.43
, pp. 15477-15482
-
-
Del Mar, C.1
Greenbaum, E.A.2
Mayne, L.3
Englander, S.W.4
Woods Jr., V.L.5
-
191
-
-
54349118166
-
Engineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils
-
P.H. Chan, E. Pardon, L. Menzer, E. De Genst, J.R. Kumita, J. Christodoulou, D. Saerens, A. Brans, F. Bouillenne, D.B. Archer, C.V. Robinson, S. Muyldermans, A. Matagne, C. Redfield, L. Wyns, C.M. Dobson, and M. Dumoulin Engineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils Biochemistry 47 2008 11041 11054
-
(2008)
Biochemistry
, vol.47
, pp. 11041-11054
-
-
Chan, P.H.1
Pardon, E.2
Menzer, L.3
De Genst, E.4
Kumita, J.R.5
Christodoulou, J.6
Saerens, D.7
Brans, A.8
Bouillenne, F.9
Archer, D.B.10
Robinson, C.V.11
Muyldermans, S.12
Matagne, A.13
Redfield, C.14
Wyns, L.15
Dobson, C.M.16
Dumoulin, M.17
-
192
-
-
27744449235
-
2-microglobulin aggregates is a reflection of different molecular architectures
-
DOI 10.1016/j.bbapap.2005.08.013, PII S1570963905002803, Dialysis-related Amyloidosis: from Molecular Mechanisms to Therapies
-
J. Kardos, D. Okuno, T. Kawai, Y. Hagihara, N. Yumoto, T. Kitagawa, P. Zavodszky, H. Naiki, and Y. Goto Structural studies reveal that the diverse morphology of beta(2)-microglobulin aggregates is a reflection of different molecular architectures Biochim. Biophys. Acta 1753 2005 108 120 (Pubitemid 41597437)
-
(2005)
Biochimica et Biophysica Acta - Proteins and Proteomics
, vol.1753
, Issue.1
, pp. 108-120
-
-
Kardos, J.1
Okuno, D.2
Kawai, T.3
Hagihara, Y.4
Yumoto, N.5
Kitagawa, T.6
Zavodszky, P.7
Naiki, H.8
Goto, Y.9
-
193
-
-
77956244375
-
Characterization of amyloid fibrils of human beta-2-microglobulin by high-resolution magic-angle spinning NMR
-
L. Skora, S. Becker, and M. Zweckstetter Characterization of amyloid fibrils of human beta-2-microglobulin by high-resolution magic-angle spinning NMR Chembiochem 11 2010 1829 1832
-
(2010)
Chembiochem
, vol.11
, pp. 1829-1832
-
-
Skora, L.1
Becker, S.2
Zweckstetter, M.3
-
194
-
-
15544363358
-
2-microglobulin
-
DOI 10.1021/bi047594t
-
N.H. Heegaard, T.J. Jorgensen, N. Rozlosnik, D.B. Corlin, J.S. Pedersen, A.G. Tempesta, P. Roepstorff, R. Bauer, and M.H. Nissen Unfolding, aggregation, and seeded amyloid formation of lysine-58-cleaved beta 2-microglobulin Biochemistry 44 2005 4397 4407 (Pubitemid 40403981)
-
(2005)
Biochemistry
, vol.44
, Issue.11
, pp. 4397-4407
-
-
Heegaard, N.H.H.1
Jorgensen, T.J.D.2
Rozlosnik, N.3
Corlin, D.B.4
Pedersen, J.S.5
Tempesta, A.G.6
Roepstorff, P.7
Bauer, R.8
Nissen, M.H.9
-
195
-
-
33646685225
-
2-microglobulin cleaved at lysine-58 retain the main conformational features of the native protein but are more conformationally heterogeneous and unstable at physiological temperature
-
DOI 10.1111/j.1742-4658.2006.05254.x
-
M.C. Mimmi, T.J. Jorgensen, F. Pettirossi, A. Corazza, P. Viglino, G. Esposito, E. De Lorenzi, S. Giorgetti, M. Pries, D.B. Corlin, M.H. Nissen, and N.H. Heegaard Variants of beta-microglobulin cleaved at lysine-58 retain the main conformational features of the native protein but are more conformationally heterogeneous and unstable at physiological temperature FEBS J. 273 2006 2461 2474 (Pubitemid 43736659)
-
(2006)
FEBS Journal
, vol.273
, Issue.11
, pp. 2461-2474
-
-
Mimmi, M.C.1
Jorgensen, T.J.D.2
Pettirossi, F.3
Corazza, A.4
Viglino, P.5
Esposito, G.6
De Lorenzi, E.7
Giorgetti, S.8
Pries, M.9
Corlin, D.B.10
Nissen, M.H.11
Heegaard, N.H.H.12
-
196
-
-
77951081386
-
Elongated oligomers in beta2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry
-
D.P. Smith, S.E. Radford, and A.E. Ashcroft Elongated oligomers in beta2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry Proc. Natl. Acad. Sci. U. S. A. 107 2010 6794 6798
-
(2010)
Proc. Natl. Acad. Sci. U. S. A.
, vol.107
, pp. 6794-6798
-
-
Smith, D.P.1
Radford, S.E.2
Ashcroft, A.E.3
-
197
-
-
79961041262
-
Structural insights into the pre-amyloid tetramer of beta-2-microglobulin from covalent labeling and mass spectrometry
-
V.L. Mendoza, M.A. Baron-Rodriguez, C. Blanco, and R.W. Vachet Structural insights into the pre-amyloid tetramer of beta-2-microglobulin from covalent labeling and mass spectrometry Biochemistry 50 2011 6711 6722
-
(2011)
Biochemistry
, vol.50
, pp. 6711-6722
-
-
Mendoza, V.L.1
Baron-Rodriguez, M.A.2
Blanco, C.3
Vachet, R.W.4
-
198
-
-
0032806571
-
Structural mobility of the human prion protein probed by backbone hydrogen exchange
-
DOI 10.1038/11507
-
L.L. Hosszu, N.J. Baxter, G.S. Jackson, A. Power, A.R. Clarke, J.P. Waltho, C.J. Craven, and J. Collinge Structural mobility of the human prion protein probed by backbone hydrogen exchange Nat. Struct. Biol. 6 1999 740 743 (Pubitemid 29360233)
-
(1999)
Nature Structural Biology
, vol.6
, Issue.8
, pp. 740-743
-
-
Hosszu, L.L.P.1
Baxter, N.J.2
Jackson, G.S.3
Power, A.4
Clarke, A.R.5
Waltho, J.P.6
Craven, C.J.7
Collinge, J.8
-
199
-
-
34250681413
-
Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen/deuterium exchange and disulfide linkage
-
DOI 10.1073/pnas.0607745104
-
F. Eghiaian, T. Daubenfeld, Y. Quenet, M. van Audenhaege, A.P. Bouin, G. van der Rest, J. Grosclaude, and H. Rezaei Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen/deuterium exchange and disulfide linkage Proc. Natl. Acad. Sci. U. S. A. 104 2007 7414 7419 (Pubitemid 47185920)
-
(2007)
Proceedings of the National Academy of Sciences of the United States of America
, vol.104
, Issue.18
, pp. 7414-7419
-
-
Eghiaian, F.1
Daubenfeld, T.2
Quenet, Y.3
Van Audenhaege, M.4
Bouin, A.-P.5
Van Der Rest, G.6
Grosclaude, J.7
Rezaei, H.8
-
200
-
-
77954382827
-
Two amyloid States of the prion protein display significantly different folding patterns
-
V.G. Ostapchenko, M.R. Sawaya, N. Makarava, R. Savtchenko, K.P. Nilsson, D. Eisenberg, and I.V. Baskakov Two amyloid States of the prion protein display significantly different folding patterns J. Mol. Biol. 400 2010 908 921
-
(2010)
J. Mol. Biol.
, vol.400
, pp. 908-921
-
-
Ostapchenko, V.G.1
Sawaya, M.R.2
Makarava, N.3
Savtchenko, R.4
Nilsson, K.P.5
Eisenberg, D.6
Baskakov, I.V.7
-
201
-
-
67649204153
-
Hydrogen/deuterium exchange mass spectrometry identifies two highly protected regions in recombinant full-length prion protein amyloid fibrils
-
A. Nazabal, S. Hornemann, A. Aguzzi, and R. Zenobi Hydrogen/deuterium exchange mass spectrometry identifies two highly protected regions in recombinant full-length prion protein amyloid fibrils J. Mass Spectrom. 44 2009 965 977
-
(2009)
J. Mass Spectrom.
, vol.44
, pp. 965-977
-
-
Nazabal, A.1
Hornemann, S.2
Aguzzi, A.3
Zenobi, R.4
-
202
-
-
0032555738
-
Protein subunit interactions and structural integrity of amyloidogenic transthyretins: Evidence from electrospray mass spectrometry
-
DOI 10.1006/jmbi.1998.1937
-
E.J. Nettleton, M. Sunde, Z. Lai, J.W. Kelly, C.M. Dobson, and C.V. Robinson Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry J. Mol. Biol. 281 1998 553 564 (Pubitemid 28372131)
-
(1998)
Journal of Molecular Biology
, vol.281
, Issue.3
, pp. 553-564
-
-
Nettleton, E.J.1
Sunde, M.2
Lai, Z.3
Kelly, J.W.4
Dobson, C.M.5
Robinson, C.V.6
-
203
-
-
0034602241
-
Deuterium-proton exchange on the native wild-type transthyretin tetramer identifies the stable core of the individual subunits and indicates mobility at the subunit interface
-
K. Liu, H.S. Cho, D.W. Hoyt, T.N. Nguyen, P. Olds, J.W. Kelly, and D.E. Wemmer Deuterium-proton exchange on the native wild-type transthyretin tetramer identifies the stable core of the individual subunits and indicates mobility at the subunit interface J. Mol. Biol. 303 2000 555 565
-
(2000)
J. Mol. Biol.
, vol.303
, pp. 555-565
-
-
Liu, K.1
Cho, H.S.2
Hoyt, D.W.3
Nguyen, T.N.4
Olds, P.5
Kelly, J.W.6
Wemmer, D.E.7
-
204
-
-
0033813424
-
A glimpse of a possible amyloidogenic intermediate of transthyretin
-
K. Liu, H.S. Cho, H.A. Lashuel, J.W. Kelly, and D.E. Wemmer A glimpse of a possible amyloidogenic intermediate of transthyretin Nat. Struct. Biol. 7 2000 754 757
-
(2000)
Nat. Struct. Biol.
, vol.7
, pp. 754-757
-
-
Liu, K.1
Cho, H.S.2
Lashuel, H.A.3
Kelly, J.W.4
Wemmer, D.E.5
-
205
-
-
77957756752
-
Probing the conformation of a prion protein fibril with hydrogen exchange
-
S.M. Damo, A.H. Phillips, A.L. Young, S. Li, V.L. Woods Jr., and D.E. Wemmer Probing the conformation of a prion protein fibril with hydrogen exchange J. Biol. Chem. 285 2010 32303 32311
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 32303-32311
-
-
Damo, S.M.1
Phillips, A.H.2
Young, A.L.3
Li, S.4
Woods, Jr.V.L.5
Wemmer, D.E.6
-
207
-
-
0345598918
-
NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126
-
DOI 10.1073/pnas.2433563100
-
K. Kuwata, T. Matumoto, H. Cheng, K. Nagayama, T.L. James, and H. Roder NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126 Proc. Natl. Acad. Sci. U. S. A. 100 2003 14790 14795 (Pubitemid 37517969)
-
(2003)
Proceedings of the National Academy of Sciences of the United States of America
, vol.100
, Issue.25
, pp. 14790-14795
-
-
Kuwata, K.1
Matumoto, T.2
Cheng, H.3
Nagayama, K.4
James, T.L.5
Roder, H.6
-
208
-
-
0036306257
-
Native state hydrogen exchange study of suppressor and pathogenic variants of transthyretin
-
DOI 10.1016/S0022-2836(02)00471-0
-
K. Liu, J.W. Kelly, and D.E. Wemmer Native state hydrogen exchange study of suppressor and pathogenic variants of transthyretin J. Mol. Biol. 320 2002 821 832 (Pubitemid 34729408)
-
(2002)
Journal of Molecular Biology
, vol.320
, Issue.4
, pp. 821-832
-
-
Liu, K.1
Kelly, J.W.2
Wemmer, D.E.3
-
209
-
-
77951953249
-
Molecular structure of amyloid fibrils formed by residues 127 to 147 of the human prion protein
-
N.S. Lin, J.C. Chao, H.M. Cheng, F.C. Chou, C.F. Chang, Y.R. Chen, Y.J. Chang, S.J. Huang, and J.C. Chan Molecular structure of amyloid fibrils formed by residues 127 to 147 of the human prion protein Chemistry 16 2010 5492 5499
-
(2010)
Chemistry
, vol.16
, pp. 5492-5499
-
-
Lin, N.S.1
Chao, J.C.2
Cheng, H.M.3
Chou, F.C.4
Chang, C.F.5
Chen, Y.R.6
Chang, Y.J.7
Huang, S.J.8
Chan, J.C.9
-
210
-
-
28844483848
-
Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils
-
DOI 10.1110/ps.051622005
-
C. Galea, P. Bowman, and R.W. Kriwacki Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils Protein Sci. 14 2005 2993 3003 (Pubitemid 41770140)
-
(2005)
Protein Science
, vol.14
, Issue.12
, pp. 2993-3003
-
-
Galea, C.1
Bowman, P.2
Kriwacki, R.W.3
-
211
-
-
79151479228
-
Crowding agents and osmolytes provide insight into the formation and dissociation of RNase A oligomers
-
C. Ercole, J.P. Lopez-Alonso, J. Font, M. Ribo, M. Vilanova, D. Picone, and D.V. Laurents Crowding agents and osmolytes provide insight into the formation and dissociation of RNase A oligomers Arch. Biochem. Biophys. 506 2010 123 129
-
(2010)
Arch. Biochem. Biophys.
, vol.506
, pp. 123-129
-
-
Ercole, C.1
Lopez-Alonso, J.P.2
Font, J.3
Ribo, M.4
Vilanova, M.5
Picone, D.6
Laurents, D.V.7
-
212
-
-
0035919776
-
The palmitoyl groups of lung surfactant protein C reduce unfolding into a fibrillogenic intermediate
-
DOI 10.1006/jmbi.2001.4810
-
M. Gustafsson, W.J. Griffiths, E. Furusjo, and J. Johansson The palmitoyl groups of lung surfactant protein C reduce unfolding into a fibrillogenic intermediate J. Mol. Biol. 310 2001 937 950 (Pubitemid 32695706)
-
(2001)
Journal of Molecular Biology
, vol.310
, Issue.4
, pp. 937-950
-
-
Gustafsson, M.1
Griffiths, W.J.2
Furusjo, E.3
Johansson, J.4
-
213
-
-
2142808745
-
The N-terminal propeptide of lung surfactant protein C is necessary for biosynthesis and prevents unfolding of a metastable α-helix
-
DOI 10.1016/j.jmb.2004.03.051, PII S002228360400350X
-
J. Li, W. Hosia, A. Hamvas, J. Thyberg, H. Jornvall, T.E. Weaver, and J. Johansson The N-terminal propeptide of lung surfactant protein C is necessary for biosynthesis and prevents unfolding of a metastable alpha-helix J. Mol. Biol. 338 2004 857 862 (Pubitemid 38542818)
-
(2004)
Journal of Molecular Biology
, vol.338
, Issue.5
, pp. 857-862
-
-
Li, J.1
Hosia, W.2
Hamvas, A.3
Thyberg, J.4
Jornvall, H.5
Weaver, T.E.6
Johansson, J.7
-
214
-
-
0034695564
-
Thermodynamic modulation of light chain amyloid fibril formation
-
DOI 10.1074/jbc.275.3.1570
-
Y. Kim, J.S. Wall, J. Meyer, C. Murphy, T.W. Randolph, M.C. Manning, A. Solomon, and J.F. Carpenter Thermodynamic modulation of light chain amyloid fibril formation J. Biol. Chem. 275 2000 1570 1574 (Pubitemid 30060770)
-
(2000)
Journal of Biological Chemistry
, vol.275
, Issue.3
, pp. 1570-1574
-
-
Kim, Y.-S.1
Wall, J.S.2
Meyer, J.3
Murphy, C.4
Randolph, T.W.5
Manning, M.C.6
Solomon, A.7
Carpenter, J.F.8
-
215
-
-
0038532258
-
Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation
-
DOI 10.1074/jbc.M212540200
-
Y.S. Kim, T.W. Randolph, M.C. Manning, F.J. Stevens, and J.F. Carpenter Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation J. Biol. Chem. 278 2003 10842 10850 (Pubitemid 36800358)
-
(2003)
Journal of Biological Chemistry
, vol.278
, Issue.12
, pp. 10842-10850
-
-
Kim, Y.-S.1
Randolph, T.W.2
Manning, M.C.3
Stevens, F.J.4
Carpenter, J.F.5
-
216
-
-
0036690049
-
Hydrogen/deuterium exchange and aggregation of a polyvaline and a polyleucine alpha-helix investigated by matrix-assisted laser desorption ionization mass spectrometry
-
W. Hosia, J. Johansson, and W.J. Griffiths Hydrogen/deuterium exchange and aggregation of a polyvaline and a polyleucine alpha-helix investigated by matrix-assisted laser desorption ionization mass spectrometry Mol. Cell. Proteomics 1 2002 592 597
-
(2002)
Mol. Cell. Proteomics
, vol.1
, pp. 592-597
-
-
Hosia, W.1
Johansson, J.2
Griffiths, W.J.3
-
217
-
-
84857129641
-
High-resolution structure of a BRICHOS domain and its implications for anti-amyloid chaperone activity on lung surfactant protein C
-
H. Willander, G. Askarieh, M. Landreh, P. Westermark, K. Nordling, H. Keranen, E. Hermansson, A. Hamvas, L.M. Nogee, T. Bergman, A. Saenz, C. Casals, J. Aqvistg, H. Jornvall, H. Berglund, J. Presto, S.D. Knight, and J. Johansson High-resolution structure of a BRICHOS domain and its implications for anti-amyloid chaperone activity on lung surfactant protein C Proc. Natl. Acad. Sci. U. S. A. 109 2012 2325 2329
-
(2012)
Proc. Natl. Acad. Sci. U. S. A.
, vol.109
, pp. 2325-2329
-
-
Willander, H.1
Askarieh, G.2
Landreh, M.3
Westermark, P.4
Nordling, K.5
Keranen, H.6
Hermansson, E.7
Hamvas, A.8
Nogee, L.M.9
Bergman, T.10
Saenz, A.11
Casals, C.12
Aqvistg, J.13
Jornvall, H.14
Berglund, H.15
Presto, J.16
Knight, S.D.17
Johansson, J.18
-
218
-
-
36549003217
-
Exclusion of the Native α-Helix from the Amyloid Fibrils of a Mixed α/β Protein
-
DOI 10.1016/j.jmb.2007.10.033, PII S002228360701371X
-
G.J. Morgan, S. Giannini, A.M. Hounslow, C.J. Craven, E. Zerovnik, V. Turk, J.P. Waltho, and R.A. Staniforth Exclusion of the native alpha-helix from the amyloid fibrils of a mixed alpha/beta protein J. Mol. Biol. 375 2008 487 498 (Pubitemid 350192480)
-
(2008)
Journal of Molecular Biology
, vol.375
, Issue.2
, pp. 487-498
-
-
Morgan, G.J.1
Giannini, S.2
Hounslow, A.M.3
Craven, C.J.4
Zerovnik, E.5
Turk, V.6
Waltho, J.P.7
Staniforth, R.A.8
|