767 results on '"Chiti, Fabrizio"'
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2. Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases
3. A single-domain antibody detects and neutralises toxic Aβ42 oligomers in the Alzheimer’s disease CSF
4. Alzheimer Disease Detection from Raman Spectroscopy of the Cerebrospinal Fluid via Topological Machine Learning
5. Amyloid Aggregation Is Potently Slowed Down by Osmolytes Due to Compaction of Partially Folded State
6. Reorganization of the outer layer of a model of the plasma membrane induced by a neuroprotective aminosterol
7. Structure–Toxicity Relationship in Intermediate Fibrils from α-Synuclein Condensates
8. Misfolded protein oligomers induce an increase of intracellular Ca2+ causing an escalation of reactive oxidative species
9. Putative novel CSF biomarkers of Alzheimer’s disease based on the novel concept of generic protein misfolding and proteotoxicity: the PRAMA cohort
10. Leveraging Machine Learning-Guided Molecular Simulations Coupled with Experimental Data to Decipher Membrane Binding Mechanisms of Aminosterols
11. Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans
12. The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells
13. Single domain antibodies as promising tools for the selective detection and neutralization of neurotoxic Aβ42 oligomers in the cerebrospinal fluid of Alzheimer’s disease patients
14. Alzheimer Disease Detection from Raman Spectroscopy of the Cerebrospinal Fluid via Topological Machine Learning
15. Rational Design of Aggregation-Resistant Bioactive Peptides: Reengineering Human Calcitonin
16. Short Amino Acid Stretches Can Mediate Amyloid Formation in Globular Proteins: The Src Homology 3 (SH3) Case
17. A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity
18. Quantitative Attribution of the Protective Effects of Aminosterols against Protein Aggregates to Their Chemical Structures and Ability to Modulate Biological Membranes
19. Studies of the Aggregation of Mutant Proteins in vitro Provide Insights into the Genetics of Amyloid Diseases
20. Very rapid amyloid fibril formation by a bacterial lipase in the absence of a detectable lag phase
21. Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism
22. Toxic oligomers of the amyloidogenic HypF-N protein form pores in mitochondrial membranes
23. A single-domain antibody detects and neutralises toxic Aβ42 oligomers in the Alzheimer's disease CSF.
24. Designing Conditions for in vitro Formation of Amyloid Protofilaments and Fibrils
25. Folding studies of acylphosphatase
26. Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers
27. Characterization of Pairs of Toxic and Nontoxic Misfolded Protein Oligomers Elucidates the Structural Determinants of Oligomer Toxicity in Protein Misfolding Diseases
28. Bis(indolyl)phenylmethane derivatives are effective small molecules for inhibition of amyloid fibril formation by hen lysozyme
29. Probing conformational changes of monomeric transthyretin with second derivative fluorescence
30. Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes
31. Misfolded protein oligomers induce an increase of intracellular Ca 2+ causing an escalation of reactive oxidative species
32. An in situ and in vitro investigation of cytoplasmic TDP-43 inclusions reveals the absence of a clear amyloid signature.
33. EGCG inactivates a pore-forming toxin by promoting its oligomerization and decreasing its solvent-exposed hydrophobicity
34. FRET studies of various conformational states adopted by transthyretin
35. An in situ and in vitro investigation of cytoplasmic TDP-43 inclusions reveals the absence of a clear amyloid signature
36. Biophysical characterization of full‐length TAR DNA‐binding protein ( TDP ‐43) phase separation
37. Studying the trafficking of labeled trodusquemine and its application as nerve marker for light‐sheet and expansion microscopy
38. Relative Importance of Hydrophobicity, Net Charge, and Secondary Structure Propensities in Protein Aggregation
39. The role of structural dynamics in the thermal adaptation of hyperthermophilic enzymes
40. Squalamine and trodusquemine: two natural products for neurodegenerative diseases, from physical chemistry to the clinic
41. Amyloid fibrils act as a reservoir of soluble oligomers, the main culprits in protein deposition diseases
42. Sphingosine 1‐phosphate attenuates neuronal dysfunction induced by amyloid‐β oligomers through endocytic internalization of NMDA receptors
43. A quantitative biology approach correlates neuronal toxicity with the largest inclusions of TDP-43
44. Conversion of the Native N-Terminal Domain of TDP-43 into a Monomeric Alternative Fold with Lower Aggregation Propensity
45. Amyloid-β oligomer synaptotoxicity is mimicked by oligomers of the model protein HypF-N
46. Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers
47. Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers
48. Editorial overview: Folding and binding
49. A Brain-Permeable Aminosterol Regulates Cell Membranes to Mitigate the Toxicity of Diverse Pore-Forming Agents
50. Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility
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