-
1
-
-
84901355639
-
The amyloid state and its association with protein misfolding diseases
-
Knowles T.P.J., et al. The amyloid state and its association with protein misfolding diseases. Nat. Rev. Mol. Cell Biol. 2014, 15:384-396.
-
(2014)
Nat. Rev. Mol. Cell Biol.
, vol.15
, pp. 384-396
-
-
Knowles, T.P.J.1
-
2
-
-
73649140576
-
The common architecture of cross-beta amyloid
-
Jahn T.R., et al. The common architecture of cross-beta amyloid. J. Mol. Biol. 2010, 395:717-727.
-
(2010)
J. Mol. Biol.
, vol.395
, pp. 717-727
-
-
Jahn, T.R.1
-
3
-
-
84868374880
-
Amyloid fibril protein nomenclature: 2012 recommendations from the Nomenclature Committee of the International Society of Amyloidosis
-
Sipe J., et al. Amyloid fibril protein nomenclature: 2012 recommendations from the Nomenclature Committee of the International Society of Amyloidosis. Amyloid 2012, 19:167-170.
-
(2012)
Amyloid
, vol.19
, pp. 167-170
-
-
Sipe, J.1
-
4
-
-
77956362155
-
Protein homeostasis and aging in neurodegeneration
-
Douglas P.M., Dillin A. Protein homeostasis and aging in neurodegeneration. J. Cell Biol. 2010, 190:719-729.
-
(2010)
J. Cell Biol.
, vol.190
, pp. 719-729
-
-
Douglas, P.M.1
Dillin, A.2
-
5
-
-
44849094781
-
Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
-
Morimoto R. Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev. 2008, 22:1427-1438.
-
(2008)
Genes Dev.
, vol.22
, pp. 1427-1438
-
-
Morimoto, R.1
-
6
-
-
0015219685
-
Amyloid fibril proteins: proof of homology with immunoglobulin light chains by sequence analyses
-
Glenner C., et al. Amyloid fibril proteins: proof of homology with immunoglobulin light chains by sequence analyses. Science 1971, 172:1150-1151.
-
(1971)
Science
, vol.172
, pp. 1150-1151
-
-
Glenner, C.1
-
7
-
-
0242668337
-
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
-
Kayed R., et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003, 300:486-489.
-
(2003)
Science
, vol.300
, pp. 486-489
-
-
Kayed, R.1
-
8
-
-
84856671147
-
Diversity, biogenesis and function of microbial amyloids
-
Blanco L.P., et al. Diversity, biogenesis and function of microbial amyloids. Trends Microbiol. 2012, 20:66-73.
-
(2012)
Trends Microbiol.
, vol.20
, pp. 66-73
-
-
Blanco, L.P.1
-
9
-
-
67650809307
-
Functional amyloids as natural storage of peptide hormones in pituitary secretory granules
-
Maji S.K., et al. Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 2009, 325:328-332.
-
(2009)
Science
, vol.325
, pp. 328-332
-
-
Maji, S.K.1
-
10
-
-
37549063068
-
Role of intermolecular forces in protein nanofibrils
-
Knowles T.P., et al. Role of intermolecular forces in protein nanofibrils. Science 2007, 318:1900-1903.
-
(2007)
Science
, vol.318
, pp. 1900-1903
-
-
Knowles, T.P.1
-
11
-
-
78049285236
-
Prion-like aggregates: infectious agents in human disease
-
Westermark G.T., Westermark P. Prion-like aggregates: infectious agents in human disease. Trends Mol. Med. 2010, 16:501-507.
-
(2010)
Trends Mol. Med.
, vol.16
, pp. 501-507
-
-
Westermark, G.T.1
Westermark, P.2
-
12
-
-
84939506533
-
Alzheimer's and Parkinson's diseases: the prion concept in relation to assembled amyloid-β, tau, and α-synuclein
-
Goedert M. Alzheimer's and Parkinson's diseases: the prion concept in relation to assembled amyloid-β, tau, and α-synuclein. Science 2015, 349:12555.
-
(2015)
Science
, vol.349
, pp. 12555
-
-
Goedert, M.1
-
13
-
-
84941198850
-
Evidence for human transmission of amyloid-β pathology and cerebral amyloid angiopathy
-
Jaunmuktane Z., et al. Evidence for human transmission of amyloid-β pathology and cerebral amyloid angiopathy. Nature 2015, 525:247-250.
-
(2015)
Nature
, vol.525
, pp. 247-250
-
-
Jaunmuktane, Z.1
-
14
-
-
84942860108
-
Evidence for α-synuclein prions causing multiple system atrophy in humans with parkinsonism
-
Prusiner S.B., et al. Evidence for α-synuclein prions causing multiple system atrophy in humans with parkinsonism. Proc. Natl. Acad. Sci. U.S.A. 2015, 112:E5308-E5317.
-
(2015)
Proc. Natl. Acad. Sci. U.S.A.
, vol.112
, pp. E5308-E5317
-
-
Prusiner, S.B.1
-
15
-
-
84926175712
-
An animal model of glomerular light-chain-associated amyloidogenesis depicts the crucial role of lysosomes
-
Teng J., et al. An animal model of glomerular light-chain-associated amyloidogenesis depicts the crucial role of lysosomes. Kidney Int. 2014, 86:738-746.
-
(2014)
Kidney Int.
, vol.86
, pp. 738-746
-
-
Teng, J.1
-
16
-
-
84901660540
-
Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation
-
Buell A.K., et al. Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation. Proc. Natl. Acad. Sci. U.S.A. 2014, 111:7671-7676.
-
(2014)
Proc. Natl. Acad. Sci. U.S.A.
, vol.111
, pp. 7671-7676
-
-
Buell, A.K.1
-
17
-
-
0034255027
-
A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro
-
Ramirez-Alvarado M., et al. A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:8979-8984.
-
(2000)
Proc. Natl. Acad. Sci. U.S.A.
, vol.97
, pp. 8979-8984
-
-
Ramirez-Alvarado, M.1
-
18
-
-
79957674907
-
Population of nonnative states of lysozyme variants drives amyloid fibril formation
-
Buell A.K., et al. Population of nonnative states of lysozyme variants drives amyloid fibril formation. J. Am. Chem. Soc. 2011, 133:7737-7743.
-
(2011)
J. Am. Chem. Soc.
, vol.133
, pp. 7737-7743
-
-
Buell, A.K.1
-
19
-
-
79959887638
-
A diversity of assembly mechanisms of a generic amyloid fold
-
Eichner T., Radford S.E. A diversity of assembly mechanisms of a generic amyloid fold. Mol. Cell 2011, 43:8-18.
-
(2011)
Mol. Cell
, vol.43
, pp. 8-18
-
-
Eichner, T.1
Radford, S.E.2
-
20
-
-
79952742454
-
In vivo demonstration that α-synuclein oligomers are toxic
-
Winner B., et al. In vivo demonstration that α-synuclein oligomers are toxic. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:4194-4199.
-
(2011)
Proc. Natl. Acad. Sci. U.S.A.
, vol.108
, pp. 4194-4199
-
-
Winner, B.1
-
21
-
-
0037041420
-
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
-
Bucciantini M., et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 2002, 416:507-511.
-
(2002)
Nature
, vol.416
, pp. 507-511
-
-
Bucciantini, M.1
-
22
-
-
0025992417
-
In vitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity
-
Pike C.J., et al. In vitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res. 1991, 563:311-314.
-
(1991)
Brain Res.
, vol.563
, pp. 311-314
-
-
Pike, C.J.1
-
23
-
-
84862701723
-
Fibrillar α-synuclein and huntingtin exon 1 assemblies are toxic to the cells
-
Pieri L., et al. Fibrillar α-synuclein and huntingtin exon 1 assemblies are toxic to the cells. Biophys. J. 2012, 102:2894-2905.
-
(2012)
Biophys. J.
, vol.102
, pp. 2894-2905
-
-
Pieri, L.1
-
24
-
-
71749089460
-
Fibril fragmentation enhances amyloid cytotoxicity
-
Xue W.F., et al. Fibril fragmentation enhances amyloid cytotoxicity. J. Biol. Chem. 2009, 284:34272-34282.
-
(2009)
J. Biol. Chem.
, vol.284
, pp. 34272-34282
-
-
Xue, W.F.1
-
25
-
-
84870947924
-
Direct three-dimensional visualization of membrane disruption by amyloid fibrils
-
Milanesi L., et al. Direct three-dimensional visualization of membrane disruption by amyloid fibrils. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:20455-20460.
-
(2012)
Proc. Natl. Acad. Sci. U.S.A.
, vol.109
, pp. 20455-20460
-
-
Milanesi, L.1
-
26
-
-
84881457232
-
2-microglobulin fibrils
-
2-microglobulin fibrils. Biophys. J. 2013, 105:745-755.
-
(2013)
Biophys. J.
, vol.105
, pp. 745-755
-
-
Sheynis, T.1
-
27
-
-
84905457722
-
2-microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH
-
2-microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH. PLoS ONE 2014, 9:e104492.
-
(2014)
PLoS ONE
, vol.9
-
-
Goodchild, S.C.1
-
28
-
-
84919799070
-
2-microglobulin amyloid fibrils are nanoparticles that disrupt lysosomal membrane protein trafficking and inhibit protein degradation by lysosomes
-
2-microglobulin amyloid fibrils are nanoparticles that disrupt lysosomal membrane protein trafficking and inhibit protein degradation by lysosomes. J. Biol. Chem. 2014, 289:35781-35794.
-
(2014)
J. Biol. Chem.
, vol.289
, pp. 35781-35794
-
-
Jakhria, T.1
-
29
-
-
84887851652
-
Amyloid-β nanotubes are associated with prion protein-dependent synaptotoxicity
-
Nicoll A.J., et al. Amyloid-β nanotubes are associated with prion protein-dependent synaptotoxicity. Nat. Commun. 2013, 4:e2416.
-
(2013)
Nat. Commun.
, vol.4
, pp. e2416
-
-
Nicoll, A.J.1
-
30
-
-
38049056730
-
Lipids revert inert Abeta amyloid fibrils to neurotoxic protofibrils that affect learning in mice
-
Martins I.C., et al. Lipids revert inert Abeta amyloid fibrils to neurotoxic protofibrils that affect learning in mice. EMBO J. 2008, 27:224-233.
-
(2008)
EMBO J.
, vol.27
, pp. 224-233
-
-
Martins, I.C.1
-
31
-
-
84863289390
-
How type II diabetes-related islet amyloid polypeptide damages lipid bilayers
-
Lee C.C., et al. How type II diabetes-related islet amyloid polypeptide damages lipid bilayers. Biophys. J. 2012, 102:1059-1068.
-
(2012)
Biophys. J.
, vol.102
, pp. 1059-1068
-
-
Lee, C.C.1
-
32
-
-
43149118349
-
Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane
-
Engel M.F.M., et al. Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:6033-6038.
-
(2008)
Proc. Natl. Acad. Sci. U.S.A.
, vol.105
, pp. 6033-6038
-
-
Engel, M.F.M.1
-
33
-
-
84923362547
-
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
-
Galvagnion C., et al. Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation. Nat. Chem. Biol. 2015, 11:229-234.
-
(2015)
Nat. Chem. Biol.
, vol.11
, pp. 229-234
-
-
Galvagnion, C.1
-
34
-
-
84924196173
-
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers
-
Cohen S.I.A., et al. A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers. Nat. Struct. Mol. Biol. 2015, 22:208-213.
-
(2015)
Nat. Struct. Mol. Biol.
, vol.22
, pp. 208-213
-
-
Cohen, S.I.A.1
-
35
-
-
84878994873
-
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
-
Cohen S.I., et al. Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:9758-9763.
-
(2013)
Proc. Natl. Acad. Sci. U.S.A.
, vol.110
, pp. 9758-9763
-
-
Cohen, S.I.1
-
36
-
-
34547638452
-
Fiber-dependent amyloid formation as catalysis of an existing reaction pathway
-
Ruschak A.M., Miranker A.D. Fiber-dependent amyloid formation as catalysis of an existing reaction pathway. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:12341-12346.
-
(2007)
Proc. Natl. Acad. Sci. U.S.A.
, vol.104
, pp. 12341-12346
-
-
Ruschak, A.M.1
Miranker, A.D.2
-
37
-
-
48249092311
-
Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly
-
Xue W-F., et al. Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:8926-8931.
-
(2008)
Proc. Natl. Acad. Sci. U.S.A.
, vol.105
, pp. 8926-8931
-
-
Xue, W.-F.1
-
38
-
-
72149118250
-
An analytical solution to the kinetics of breakable filament assembly
-
Knowles T.P.J., et al. An analytical solution to the kinetics of breakable filament assembly. Science 2009, 326:1533-1537.
-
(2009)
Science
, vol.326
, pp. 1533-1537
-
-
Knowles, T.P.J.1
-
39
-
-
84857034922
-
The presence of Abeta seeds, and not age per se, is critical to the initiation of Abeta deposition in the brain
-
Hamaguchi T., et al. The presence of Abeta seeds, and not age per se, is critical to the initiation of Abeta deposition in the brain. Acta Neuropathol. 2012, 123:31-37.
-
(2012)
Acta Neuropathol.
, vol.123
, pp. 31-37
-
-
Hamaguchi, T.1
-
40
-
-
79955522862
-
Transmission of prion strains in a transgenic mouse model overexpressing human A53T mutated α-synuclein
-
Mougenot A.L.J., et al. Transmission of prion strains in a transgenic mouse model overexpressing human A53T mutated α-synuclein. J. Neuropathol. Exp. Neurol. 2011, 70:377-385.
-
(2011)
J. Neuropathol. Exp. Neurol.
, vol.70
, pp. 377-385
-
-
Mougenot, A.L.J.1
-
41
-
-
84934983329
-
α-Synuclein strains cause distinct synucleinopathies after local and systemic administration
-
Peelaerts W., et al. α-Synuclein strains cause distinct synucleinopathies after local and systemic administration. Nature 2015, 522:340-344.
-
(2015)
Nature
, vol.522
, pp. 340-344
-
-
Peelaerts, W.1
-
42
-
-
84876000270
-
Spreading of a prion domain from cell-to-cell by vesicular transport in Caenorhabditis elegans
-
Nussbaum-Krammer C.I., et al. Spreading of a prion domain from cell-to-cell by vesicular transport in Caenorhabditis elegans. PLoS Genet. 2013, 9:e1003351.
-
(2013)
PLoS Genet.
, vol.9
-
-
Nussbaum-Krammer, C.I.1
-
43
-
-
35748986138
-
2-microglobulin amyloid fibrils
-
2-microglobulin amyloid fibrils. J. Biol. Chem. 2007, 282:29691-29700.
-
(2007)
J. Biol. Chem.
, vol.282
, pp. 29691-29700
-
-
Morten, I.J.1
-
44
-
-
84904742860
-
Defined α-synuclein prion-like molecular assemblies spreading in cell culture
-
Aulić S., et al. Defined α-synuclein prion-like molecular assemblies spreading in cell culture. BMC Neurosci. 2014, 15:69.
-
(2014)
BMC Neurosci.
, vol.15
, pp. 69
-
-
Aulić, S.1
-
45
-
-
59649095699
-
Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
-
Ren P-H., et al. Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat. Cell Biol. 2009, 11:219-225.
-
(2009)
Nat. Cell Biol.
, vol.11
, pp. 219-225
-
-
Ren, P.-H.1
-
46
-
-
69149089854
-
Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein
-
Desplats P., et al. Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:13010-13015.
-
(2009)
Proc. Natl. Acad. Sci. U.S.A.
, vol.106
, pp. 13010-13015
-
-
Desplats, P.1
-
47
-
-
84865307818
-
Exosomal cell-to-cell transmission of α-synuclein oligomers
-
Danzer K.M., et al. Exosomal cell-to-cell transmission of α-synuclein oligomers. Mol. Neurodegener. 2012, 7:42.
-
(2012)
Mol. Neurodegener.
, vol.7
, pp. 42
-
-
Danzer, K.M.1
-
48
-
-
84927949614
-
Prion-like transmission of neuronal huntingtin aggregates to phagocytic glia in the Drosophila brain
-
Pearce M.M.P., et al. Prion-like transmission of neuronal huntingtin aggregates to phagocytic glia in the Drosophila brain. Nat. Commun. 2015, 6:6768.
-
(2015)
Nat. Commun.
, vol.6
, pp. 6768
-
-
Pearce, M.M.P.1
-
49
-
-
84866679781
-
Antibody-aided clearance of extracellular α-synuclein prevents cell-to-cell aggregate transmission
-
Bae E.J., et al. Antibody-aided clearance of extracellular α-synuclein prevents cell-to-cell aggregate transmission. J. Neurosci. 2012, 32:13454-13469.
-
(2012)
J. Neurosci.
, vol.32
, pp. 13454-13469
-
-
Bae, E.J.1
-
50
-
-
84872144291
-
A plaque-specific antibody clears existing β-amyloid plaques in Alzheimer's disease mice
-
DeMattos R.B., et al. A plaque-specific antibody clears existing β-amyloid plaques in Alzheimer's disease mice. Neuron 2012, 76:908-920.
-
(2012)
Neuron
, vol.76
, pp. 908-920
-
-
DeMattos, R.B.1
-
51
-
-
23144459082
-
Molecular recycling within amyloid fibrils
-
Carulla N., et al. Molecular recycling within amyloid fibrils. Nature 2005, 436:554-558.
-
(2005)
Nature
, vol.436
, pp. 554-558
-
-
Carulla, N.1
-
52
-
-
84861563520
-
Direct observation of the interconversion of normal and toxic forms of α-synuclein
-
Cremades N., et al. Direct observation of the interconversion of normal and toxic forms of α-synuclein. Cell 2012, 149:1048-1059.
-
(2012)
Cell
, vol.149
, pp. 1048-1059
-
-
Cremades, N.1
-
53
-
-
84855450514
-
The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide
-
Narayan P., et al. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. Nat. Struct. Mol. Biol. 2012, 19:79-83.
-
(2012)
Nat. Struct. Mol. Biol.
, vol.19
, pp. 79-83
-
-
Narayan, P.1
-
54
-
-
62649174753
-
Oligomeric amyloid beta associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques
-
Koffie R.M., et al. Oligomeric amyloid beta associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:4012-4017.
-
(2009)
Proc. Natl. Acad. Sci. U.S.A.
, vol.106
, pp. 4012-4017
-
-
Koffie, R.M.1
-
55
-
-
84928963185
-
PH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers
-
Tipping K.W., et al. pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers. Proc. Natl. Acad. Sci. U.S.A. 2015, 112:5691-5696.
-
(2015)
Proc. Natl. Acad. Sci. U.S.A.
, vol.112
, pp. 5691-5696
-
-
Tipping, K.W.1
-
56
-
-
77951081386
-
2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry
-
2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:6794-6798.
-
(2010)
Proc. Natl. Acad. Sci. U.S.A.
, vol.107
, pp. 6794-6798
-
-
Smith, D.P.1
-
57
-
-
79955406741
-
Aβ40 and Aβ42 amyloid fibrils exhibit distinct molecular recycling properties
-
Sánchez L., et al. Aβ40 and Aβ42 amyloid fibrils exhibit distinct molecular recycling properties. J. Am. Chem. Soc. 2011, 133:6505-6508.
-
(2011)
J. Am. Chem. Soc.
, vol.133
, pp. 6505-6508
-
-
Sánchez, L.1
-
58
-
-
84869392249
-
Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones
-
Narayan P., et al. Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones. Biochemistry 2012, 51:9270-9276.
-
(2012)
Biochemistry
, vol.51
, pp. 9270-9276
-
-
Narayan, P.1
-
59
-
-
80053408422
-
Hsc70 protein interaction with soluble and fibrillar alpha-synuclein
-
Pemberton S., et al. Hsc70 protein interaction with soluble and fibrillar alpha-synuclein. J. Biol. Chem. 2011, 286:34690-34699.
-
(2011)
J. Biol. Chem.
, vol.286
, pp. 34690-34699
-
-
Pemberton, S.1
-
60
-
-
84880638556
-
Structure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta
-
Jiang L., et al. Structure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta. Elife 2013, 2:e00857.
-
(2013)
Elife
, vol.2
, pp. e00857
-
-
Jiang, L.1
-
61
-
-
33750873994
-
Heat shock protein 70 inhibits alpha-synuclein fibril formation via interactions with diverse intermediates
-
Huang C., et al. Heat shock protein 70 inhibits alpha-synuclein fibril formation via interactions with diverse intermediates. J. Mol. Biol. 2006, 364:323-336.
-
(2006)
J. Mol. Biol.
, vol.364
, pp. 323-336
-
-
Huang, C.1
-
62
-
-
84884217594
-
Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue
-
Lu J.X., et al. Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue. Cell 2013, 154:1257-1268.
-
(2013)
Cell
, vol.154
, pp. 1257-1268
-
-
Lu, J.X.1
-
63
-
-
84892150877
-
Structural and functional characterization of two alpha-synuclein strains
-
Bousset L., et al. Structural and functional characterization of two alpha-synuclein strains. Nat. Commun. 2013, 4:2575.
-
(2013)
Nat. Commun.
, vol.4
, pp. 2575
-
-
Bousset, L.1
-
64
-
-
12244249201
-
Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
-
Petkova A.T., et al. Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils. Science 2005, 307:262-265.
-
(2005)
Science
, vol.307
, pp. 262-265
-
-
Petkova, A.T.1
-
65
-
-
78650963274
-
Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions
-
Olzscha H., et al. Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell 2011, 144:67-78.
-
(2011)
Cell
, vol.144
, pp. 67-78
-
-
Olzscha, H.1
-
66
-
-
71449108913
-
Reduced IGF-1 signaling delays age-associated proteotoxicity in mice
-
Cohen E., et al. Reduced IGF-1 signaling delays age-associated proteotoxicity in mice. Cell 2009, 139:1157-1169.
-
(2009)
Cell
, vol.139
, pp. 1157-1169
-
-
Cohen, E.1
-
67
-
-
84879920420
-
PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone
-
Park S.H., et al. PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone. Cell 2013, 154:134-145.
-
(2013)
Cell
, vol.154
, pp. 134-145
-
-
Park, S.H.1
-
68
-
-
84904360470
-
Organismal proteostasis: role of cell-nonautonomous regulation and transcellular chaperone signaling
-
van Oosten-Hawle P., Morimoto R. Organismal proteostasis: role of cell-nonautonomous regulation and transcellular chaperone signaling. Genes Dev. 2014, 28:1533-1543.
-
(2014)
Genes Dev.
, vol.28
, pp. 1533-1543
-
-
van Oosten-Hawle, P.1
Morimoto, R.2
|