| Nome |
# |
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Protein misfolding, amyloid formation, and human disease: A summary of progress over the last decade, file e398c381-5047-179a-e053-3705fe0a4cff
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511
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A causative link between the structure of aberrant protein oligomers and their toxicity, file e398c378-b3de-179a-e053-3705fe0a4cff
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451
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Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers, file e398c381-2859-179a-e053-3705fe0a4cff
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366
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Soluble Oligomers Require a Ganglioside to Trigger Neuronal Calcium Overload, file e398c37c-38cf-179a-e053-3705fe0a4cff
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327
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Patterns of cell death triggered in two different cell lines by HypF-N prefibrillar aggregates., file e398c378-955b-179a-e053-3705fe0a4cff
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207
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The contribution of acidic residues to the conformational stability of common-type acylphosphatase, file e398c378-9199-179a-e053-3705fe0a4cff
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182
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The Folding process of Human Profilin-1, a novel protein associated with familial amyotrophic lateral sclerosis, file e398c379-5353-179a-e053-3705fe0a4cff
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159
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Destabilisation, aggregation, toxicity and cytosolic mislocalisation of nucleophosmin regions associated with acute myeloid leukemia, file e398c37b-d25c-179a-e053-3705fe0a4cff
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151
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A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity, file e398c37b-a4f1-179a-e053-3705fe0a4cff
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146
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Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions, file e398c37b-e1f9-179a-e053-3705fe0a4cff
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146
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Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases, file e398c37b-9ff3-179a-e053-3705fe0a4cff
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137
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Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes, file e398c37d-de56-179a-e053-3705fe0a4cff
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136
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Probing the origin of the toxicity of oligomeric aggregates of α-synuclein with antibodies, file e398c37e-624e-179a-e053-3705fe0a4cff
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136
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Insight into the structure of amyloid fibrils from the analysis of globular proteins, file e398c37a-405e-179a-e053-3705fe0a4cff
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135
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TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells, file e398c37b-a4b0-179a-e053-3705fe0a4cff
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134
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Effect of molecular chaperones on aberrant protein oligomers in vitro: super- versus sub-stoichiometric chaperone concentrations, file e398c37b-db9c-179a-e053-3705fe0a4cff
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130
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Identification of Novel 1,3,5-Triphenylbenzene Derivative Compounds as Inhibitors of Hen Lysozyme Amyloid Fibril Formation, file e398c37e-944e-179a-e053-3705fe0a4cff
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129
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TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells, file e398c378-f70d-179a-e053-3705fe0a4cff
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121
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Capturing Aβ42 aggregation in the cell, file e398c37d-fee9-179a-e053-3705fe0a4cff
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121
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Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrils, file e398c37a-4b72-179a-e053-3705fe0a4cff
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119
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Interaction of toxic and non-toxic HypF-N oligomers with lipid bilayers investigated at high resolution with atomic force microscopy, file e398c37b-dfe1-179a-e053-3705fe0a4cff
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114
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Chaperones in Neurodegeneration, file e398c37a-701d-179a-e053-3705fe0a4cff
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111
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A computational approach for identifying the chemical factors involved in the glycosaminoglycans-mediated acceleration of amyloid fibril formation, file e398c37a-42d6-179a-e053-3705fe0a4cff
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108
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TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells, file e398c37b-d4e5-179a-e053-3705fe0a4cff
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103
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The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain., file e398c37a-5643-179a-e053-3705fe0a4cff
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98
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Partial Failure of Proteostasis Systems Counteracting TDP-43 Aggregates in Neurodegenerative Diseases, file e398c37e-9cdd-179a-e053-3705fe0a4cff
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98
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Quantification of the Relative Contributions of Loss-of function and Gain-of-function Mechanisms in TAR DNA-binding Protein 43 (TDP-43) Proteinopathies, file e398c37b-a4ab-179a-e053-3705fe0a4cff
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94
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Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers, file e398c37d-a842-179a-e053-3705fe0a4cff
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94
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Aggregation propensity of the human proteome, file e398c37a-3f88-179a-e053-3705fe0a4cff
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91
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Systematic in vivo analysis of the intrinsic determinants of amyloid Beta pathogenicity, file e398c37a-3ffb-179a-e053-3705fe0a4cff
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84
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Toxic HypF-N oligomers selectively bind the plasma membrane to impair cell adhesion capability, file e398c37e-99f9-179a-e053-3705fe0a4cff
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78
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Nanoscopic insights into the surface conformation of neurotoxic amyloid b oligomers, file e398c37f-83ec-179a-e053-3705fe0a4cff
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62
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The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells, file e398c381-6775-179a-e053-3705fe0a4cff
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60
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Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism, file e398c380-3498-179a-e053-3705fe0a4cff
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58
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Chaperones as Suppressors of Protein Misfolded Oligomer Toxicity, file e398c37f-015a-179a-e053-3705fe0a4cff
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57
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Probing conformational changes of monomeric transthyretin with second derivative fluorescence, file e398c37f-e67b-179a-e053-3705fe0a4cff
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54
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Soluble Prion peptide 107–120 protects neuroblastoma SH-SY5Y cells against oligomers associated with Alzheimer’s disease, file e398c380-1e71-179a-e053-3705fe0a4cff
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54
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Stability of an aggregation-prone partially folded state of human profilin-1 correlates with aggregation propensity, file e398c37d-a844-179a-e053-3705fe0a4cff
|
51
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Thermodynamics and kinetics of folding of common type acylphosphatase, file e398c378-8b7d-179a-e053-3705fe0a4cff
|
48
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Homage to Chris Dobson, file e398c380-1538-179a-e053-3705fe0a4cff
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41
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Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers, file e398c37c-aeff-179a-e053-3705fe0a4cff
|
37
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Amyloid fibrils act as a reservoir of soluble oligomers, the main culprits in protein deposition diseases, file b874e5ce-3aa3-4310-99d2-e82ed99c889b
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36
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Small molecule protein binding to correct cellular folding or stabilize the native state against misfolding and aggregation, file ab1d5478-d4c6-40c5-9842-a7b546304310
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34
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Cloning, expression and characterization of a new human LMW-PTP isoform originating by alternative splicing, file e398c378-950c-179a-e053-3705fe0a4cff
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34
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Molecular links between aberrant protein oligomers and neurodegeneration in Alzheimer’s disease, file e398c37b-a5d6-179a-e053-3705fe0a4cff
|
31
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Sphingosine 1-phosphate attenuates neuronal dysfunction induced by amyloid-β oligomers through endocytic internalization of NMDA receptors, file 469d176f-7b4a-40b4-b914-7dd8103eb913
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30
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Making biological membrane resistant to the toxicity of misfolded protein oligomers: a lesson from trodusquemine, file 96185b7c-60c4-427b-aad6-d7dd27eeff43
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29
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Squalamine and its derivatives modulate the aggregation of amyloid-β and α-synuclein and suppress the toxicity of their oligomers, file e398c381-814f-179a-e053-3705fe0a4cff
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29
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Single particle tracking to study the binding of protein misfolded oligomer to membrane ganglioside GM1, file e398c37b-9f1f-179a-e053-3705fe0a4cff
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28
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Looking for residues involved in the muscle acylphosphatase catalytic mechanism and structural stabilization: role of Asn41, Ther42 and Thr46, file e398c378-b2ce-179a-e053-3705fe0a4cff
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24
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A quantitative biology approach correlates neuronal toxicity with the largest inclusions of TDP-43, file 3c046775-2499-4dfb-8ac3-79be4811ffad
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23
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Urea titration of a lipase from Pseudomonas sp. reveals four different conformational states, with a stable partially folded state explaining its high aggregation propensity, file 6e45af78-546e-4636-8ec4-1687ea0ee4b3
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18
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Multistep Inhibition of α‑Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine, file e398c37d-7b95-179a-e053-3705fe0a4cff
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18
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Misfolded protein oligomers induce an increase of intracellular Ca2+ causing an escalation of reactive oxidative species, file 37ec0f86-dbc8-4919-8ac7-b0287cffde83
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9
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Quantitative Measurement of the Affinity of Toxic and Nontoxic Misfolded Protein Oligomers for Lipid Bilayers and of its Modulation by Lipid Composition and Trodusquemine, file 51e5654f-4b60-4086-9db0-2a4a10f8bdbb
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7
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Multistep Inhibition of α‑Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine, file e398c381-7c02-179a-e053-3705fe0a4cff
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6
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Distinct responses of human peripheral blood cells to different misfolded protein oligomers, file 1220483e-e090-4118-8b42-d3cbf0349667
|
5
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Conversion of the Native N-Terminal Domain of TDP-43 into a Monomeric Alternative Fold with Lower Aggregation Propensity, file 71778391-8e07-4058-9703-be2b1cc33e0b
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5
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Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans, file 7cbac64d-4a11-41d1-a2ca-8dba546ab1ff
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5
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Biophysical characterization of full length TAR DNA-Binding Protein (TDP-43) phase separation, file e4e41f7c-7fab-442f-974b-ef0ca3b6aeff
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5
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Full-length TDP-43 and its C-terminal domain form filaments in vitro having non-amyloid properties, file 7dbd0e4b-007c-492d-8f12-adff1379560d
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4
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Squalamine and trodusquemine: two natural products for neurodegenerative diseases, from physical chemistry to the clinic, file 935afeee-5831-47a3-b6fb-4bdce5d92630
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4
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Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers, file e398c378-bf91-179a-e053-3705fe0a4cff
|
2
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Glycosaminoglycans (GAGs) Suppress the Toxicity of
HypF-N Prefibrillar Aggregates, file e398c378-db1b-179a-e053-3705fe0a4cff
|
2
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Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers, file e398c378-db1c-179a-e053-3705fe0a4cff
|
2
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|
The polyphenol Oleuropein aglycone hinders the growth of toxic transthyretin amyloid assemblies, file e398c37b-1be1-179a-e053-3705fe0a4cff
|
2
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A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells, file e398c378-b3fe-179a-e053-3705fe0a4cff
|
1
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|
Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro, file e398c378-df1b-179a-e053-3705fe0a4cff
|
1
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|
Extracellular chaperones prevent Aβ42-induced toxicity in rat brains, file e398c378-e3a1-179a-e053-3705fe0a4cff
|
1
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Toxicity of Protein Oligomers Is Rationalized by a Function
Combining Size and Surface Hydrophobicity, file e398c378-f3b2-179a-e053-3705fe0a4cff
|
1
|
|
A Complex Equilibrium among Partially Unfolded
Conformations in Monomeric Transthyretin, file e398c378-fb29-179a-e053-3705fe0a4cff
|
1
|
|
Protein misfolding, amyloid formation, and human disease: A summary of progress over the last decade, file e398c37c-8be3-179a-e053-3705fe0a4cff
|
1
|
| Totale |
5937 |