-
2
-
-
66949117423
-
The scientific and clinical basis for the treatment of Parkinson disease
-
C.W. Olanow, M.D. Stern, and K. Sethi The scientific and clinical basis for the treatment of Parkinson disease Neurology 72 2009 S65 S73
-
(2009)
Neurology
, vol.72
-
-
Olanow, C.W.1
Stern, M.D.2
Sethi, K.3
-
3
-
-
33749841522
-
The aggregation and fibrillation of α-synuclein
-
A.L. Fink The aggregation and fibrillation of α-synuclein Acc. Chem. Res. 39 2006 628 634
-
(2006)
Acc. Chem. Res.
, vol.39
, pp. 628-634
-
-
Fink, A.L.1
-
4
-
-
0037551741
-
Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
-
B. Caughey, and P.T. Lansbury Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders Annu. Rev. Neurosci. 26 2003 267 298
-
(2003)
Annu. Rev. Neurosci.
, vol.26
, pp. 267-298
-
-
Caughey, B.1
Lansbury, P.T.2
-
5
-
-
0033771793
-
Is there a cause-and-effect relationship between α-synuclein fibrillization and Parkinson's disease?
-
M.S. Goldberg, and P.T. Lansbury Jr. Is there a cause-and-effect relationship between α-synuclein fibrillization and Parkinson's disease? Nat. Cell Biol. 2 2000 E115 E119
-
(2000)
Nat. Cell Biol.
, vol.2
-
-
Goldberg, M.S.1
Lansbury, Jr.P.T.2
-
6
-
-
3142514201
-
Protein aggregation and neurodegenerative disease
-
C.A. Ross, and M.A. Poirier Protein aggregation and neurodegenerative disease Nat. Med. 10 Suppl 2004 S10 S17
-
(2004)
Nat. Med.
, vol.10
, Issue.SUPPL.
-
-
Ross, C.A.1
Poirier, M.A.2
-
7
-
-
33746377894
-
Protein misfolding, functional amyloid, and human disease
-
F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366
-
(2006)
Annu. Rev. Biochem.
, vol.75
, pp. 333-366
-
-
Chiti, F.1
Dobson, C.M.2
-
8
-
-
78649894243
-
Mechanistic study of self-assembling peptide RADA16-I in formation of nanofibers and hydrogels
-
011007-011006
-
H. Zhang, H. Luo, and X. Zhao Mechanistic study of self-assembling peptide RADA16-I in formation of nanofibers and hydrogels J.Nanotechnol. Eng. Med 1 2010 011007-011006
-
(2010)
J.Nanotechnol. Eng. Med
, vol.1
-
-
Zhang, H.1
Luo, H.2
Zhao, X.3
-
9
-
-
65249179551
-
Designed amphiphilic peptide forms stable nanoweb, slowly releases encapsulated hydrophobic drug, and accelerates animal hemostasis
-
L.P. Ruan, and H.Y. Zhang X. Zhao Designed amphiphilic peptide forms stable nanoweb, slowly releases encapsulated hydrophobic drug, and accelerates animal hemostasis Proc. Natl. Acad. Sci. USA 106 2009 5105 5110
-
(2009)
Proc. Natl. Acad. Sci. USA
, vol.106
, pp. 5105-5110
-
-
Ruan, L.P.1
Zhang, H.Y.2
Zhao, X.3
-
10
-
-
0037041420
-
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
-
M. Bucciantini, and E. Giannoni M. Stefani Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases Nature 416 2002 507 511
-
(2002)
Nature
, vol.416
, pp. 507-511
-
-
Bucciantini, M.1
Giannoni, E.2
Stefani, M.3
-
11
-
-
39649085356
-
Temperature and pH effects on biophysical and morphological properties of self-assembling peptide RADA16-I
-
Z. Ye, and H. Zhang X. Zhao Temperature and pH effects on biophysical and morphological properties of self-assembling peptide RADA16-I J. Pept. Sci. 14 2008 152 162
-
(2008)
J. Pept. Sci.
, vol.14
, pp. 152-162
-
-
Ye, Z.1
Zhang, H.2
Zhao, X.3
-
12
-
-
0242668337
-
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
-
R. Kayed, and E. Head C.G. Glabe Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis Science 300 2003 486 489
-
(2003)
Science
, vol.300
, pp. 486-489
-
-
Kayed, R.1
Head, E.2
Glabe, C.G.3
-
13
-
-
78650763561
-
Membrane permeabilization by oligomeric α-synuclein: In search of the mechanism
-
B.D. van Rooijen, M.M. Claessens, and V. Subramaniam Membrane permeabilization by oligomeric α-synuclein: in search of the mechanism PLoS ONE 5 2010 e14292
-
(2010)
PLoS ONE
, vol.5
, pp. 14292
-
-
Van Rooijen, B.D.1
Claessens, M.M.2
Subramaniam, V.3
-
14
-
-
0034681163
-
Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
-
K.A. Conway, and S.J. Lee P.T. Lansbury Jr. Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy Proc. Natl. Acad. Sci. USA 97 2000 571 576
-
(2000)
Proc. Natl. Acad. Sci. USA
, vol.97
, pp. 571-576
-
-
Conway, K.A.1
Lee, S.J.2
Lansbury, Jr.P.T.3
-
15
-
-
0034646391
-
Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid
-
K.A. Conway, J.D. Harper, and P.T. Lansbury Jr. Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid Biochemistry 39 2000 2552 2563
-
(2000)
Biochemistry
, vol.39
, pp. 2552-2563
-
-
Conway, K.A.1
Harper, J.D.2
Lansbury, Jr.P.T.3
-
16
-
-
0037072284
-
Annular α-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes
-
T.T. Ding, and S.J. Lee P.T. Lansbury Jr. Annular α-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes Biochemistry 41 2002 10209 10217
-
(2002)
Biochemistry
, vol.41
, pp. 10209-10217
-
-
Ding, T.T.1
Lee, S.J.2
Lansbury, Jr.P.T.3
-
17
-
-
0036415838
-
Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils
-
H.A. Lashuel, and B.M. Petre P.T. Lansbury Jr. Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils J. Mol. Biol. 322 2002 1089 1102
-
(2002)
J. Mol. Biol.
, vol.322
, pp. 1089-1102
-
-
Lashuel, H.A.1
Petre, B.M.2
Lansbury, Jr.P.T.3
-
18
-
-
0037130174
-
Neurodegenerative disease: Amyloid pores from pathogenic mutations
-
H.A. Lashuel, and D. Hartley P.T. Lansbury Jr. Neurodegenerative disease: amyloid pores from pathogenic mutations Nature 418 2002 291
-
(2002)
Nature
, vol.418
, pp. 291
-
-
Lashuel, H.A.1
Hartley, D.2
Lansbury, Jr.P.T.3
-
19
-
-
63249103989
-
Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer
-
R. Kayed, and A. Pensalfini C. Glabe Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer J. Biol. Chem. 284 2009 4230 4237
-
(2009)
J. Biol. Chem.
, vol.284
, pp. 4230-4237
-
-
Kayed, R.1
Pensalfini, A.2
Glabe, C.3
-
20
-
-
0041825430
-
Mixtures of wild-type and a pathogenic (E22G) form of Aβ40 in vitro accumulate protofibrils, including amyloid pores
-
H.A. Lashuel, and D.M. Hartley P.T. Lansbury Jr. Mixtures of wild-type and a pathogenic (E22G) form of Aβ40 in vitro accumulate protofibrils, including amyloid pores J. Mol. Biol. 332 2003 795 808
-
(2003)
J. Mol. Biol.
, vol.332
, pp. 795-808
-
-
Lashuel, H.A.1
Hartley, D.M.2
Lansbury, Jr.P.T.3
-
21
-
-
0035159553
-
Amyloid β protein forms ion channels: Implications for Alzheimer's disease pathophysiology
-
H. Lin, R. Bhatia, and R. Lal Amyloid β protein forms ion channels: implications for Alzheimer's disease pathophysiology FASEB J. 15 2001 2433 2444
-
(2001)
FASEB J.
, vol.15
, pp. 2433-2444
-
-
Lin, H.1
Bhatia, R.2
Lal, R.3
-
22
-
-
0142040121
-
Formation of critical oligomers is a key event during conformational transition of recombinant Syrian hamster prion protein
-
F. Sokolowski, and A.J. Modler D. Naumann Formation of critical oligomers is a key event during conformational transition of recombinant Syrian hamster prion protein J. Biol. Chem. 278 2003 40481 40492
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 40481-40492
-
-
Sokolowski, F.1
Modler, A.J.2
Naumann, D.3
-
23
-
-
0141653970
-
The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies
-
Y. Porat, and S. Kolusheva E. Gazit The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies Biochemistry 42 2003 10971 10977
-
(2003)
Biochemistry
, vol.42
, pp. 10971-10977
-
-
Porat, Y.1
Kolusheva, S.2
Gazit, E.3
-
24
-
-
33750365052
-
Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
-
H.A. Lashuel, and P.T. Lansbury Jr. Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? Q. Rev. Biophys. 39 2006 167 201
-
(2006)
Q. Rev. Biophys.
, vol.39
, pp. 167-201
-
-
Lashuel, H.A.1
Lansbury, Jr.P.T.2
-
25
-
-
23044449398
-
Amyloid ion channels: A common structural link for protein-misfolding disease
-
A. Quist, and I. Doudevski R. Lal Amyloid ion channels: a common structural link for protein-misfolding disease Proc. Natl. Acad. Sci. USA 102 2005 10427 10432
-
(2005)
Proc. Natl. Acad. Sci. USA
, vol.102
, pp. 10427-10432
-
-
Quist, A.1
Doudevski, I.2
Lal, R.3
-
26
-
-
72549099399
-
Misfolded amyloid ion channels present mobile β-sheet subunits in contrast to conventional ion channels
-
H. Jang, and F.T. Arce R. Nussinov Misfolded amyloid ion channels present mobile β-sheet subunits in contrast to conventional ion channels Biophys. J. 97 2009 3029 3037
-
(2009)
Biophys. J.
, vol.97
, pp. 3029-3037
-
-
Jang, H.1
Arce, F.T.2
Nussinov, R.3
-
27
-
-
52049098478
-
Structural characteristics of α-synuclein oligomers stabilized by the flavonoid baicalein
-
D.-P. Hong, A.L. Fink, and V.N. Uversky Structural characteristics of α-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
-
28
-
-
33644527256
-
Characterization of oligomers during α-synuclein aggregation using intrinsic tryptophan fluorescence
-
A. Dusa, and J. Kaylor A.L. Fink Characterization of oligomers during α-synuclein aggregation using intrinsic tryptophan fluorescence Biochemistry 45 2006 2752 2760
-
(2006)
Biochemistry
, vol.45
, pp. 2752-2760
-
-
Dusa, A.1
Kaylor, J.2
Fink, A.L.3
-
29
-
-
34548094323
-
Fourier transform infrared spectroscopic analysis of protein secondary structures
-
J. Kong, and S. Yu Fourier transform infrared spectroscopic analysis of protein secondary structures Acta Biochim. Biophys. Sin. (Shanghai) 39 2007 549 559
-
(2007)
Acta Biochim. Biophys. Sin. (Shanghai)
, vol.39
, pp. 549-559
-
-
Kong, J.1
Yu, S.2
-
30
-
-
78649808726
-
Negative staining and cryo-negative staining of macromolecules and viruses for TEM
-
S. De Carlo, and J.R. Harris Negative staining and cryo-negative staining of macromolecules and viruses for TEM Micron 42 2011 117 131
-
(2011)
Micron
, vol.42
, pp. 117-131
-
-
De Carlo, S.1
Harris, J.R.2
-
32
-
-
38949167084
-
New structures help the modeling of toxic amyloidβ ion channels
-
H.B. Jang, and J. Zheng R. Nussinov New structures help the modeling of toxic amyloidβ ion channels Trends Biochem. Sci. 33 2008 91 100
-
(2008)
Trends Biochem. Sci.
, vol.33
, pp. 91-100
-
-
Jang, H.B.1
Zheng, J.2
Nussinov, R.3
-
33
-
-
0031444010
-
Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein
-
J.D. Harper, C.M. Lieber, and P.T. Lansbury Jr. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein Chem. Biol. 4 1997 951 959
-
(1997)
Chem. Biol.
, vol.4
, pp. 951-959
-
-
Harper, J.D.1
Lieber, C.M.2
Lansbury, Jr.P.T.3
-
34
-
-
11544279355
-
Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins
-
M.P. Lambert, and A.K. Barlow W.L. Klein Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins Proc. Natl. Acad. Sci. USA 95 1998 6448 6453
-
(1998)
Proc. Natl. Acad. Sci. USA
, vol.95
, pp. 6448-6453
-
-
Lambert, M.P.1
Barlow, A.K.2
Klein, W.L.3
-
35
-
-
0030799122
-
Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate
-
D.M. Walsh, and A. Lomakin D.B. Teplow Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate J. Biol. Chem. 272 1997 22364 22372
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 22364-22372
-
-
Walsh, D.M.1
Lomakin, A.2
Teplow, D.B.3
-
37
-
-
15444373250
-
Structural characterization of copper(II) binding to α-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease
-
R.M. Rasia, and C.W. Bertoncini C.O. Fernández Structural characterization of copper(II) binding to α-synuclein: insights into the bioinorganic chemistry of Parkinson's disease Proc. Natl. Acad. Sci. USA 102 2005 4294 4299
-
(2005)
Proc. Natl. Acad. Sci. USA
, vol.102
, pp. 4294-4299
-
-
Rasia, R.M.1
Bertoncini, C.W.2
Fernández, C.O.3
-
38
-
-
0035941201
-
Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure
-
V.N. Uversky, J. Li, and A.L. Fink Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure J. Biol. Chem. 276 2001 44284 44296
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 44284-44296
-
-
Uversky, V.N.1
Li, J.2
Fink, A.L.3
|