Angel Orte

TL;DR: A conformational change from the initially formed oligomers to stable, more compact proteinase-K-resistant oligomers is identified as the key step that leads ultimately to fibril formation, indicating a significant period of time for the cellular protective machinery to operate and potentially for therapeutic intervention, prior to the onset of cellular damage.

TL;DR: This review focuses on the developments and analytical applications of fluorescent nanoparticles in chemical and biological sensing within the intracellular environment, and points out the great potential of fluorescent NPs for fluorescence lifetime imaging microscopy (FLIM).

TL;DR: In this paper, the interactions between human clusterin and the Alzheimer's disease-associated amyloid-β(1-40) peptide (Aβ( 1-40)), which is prone to aggregate into an ensemble of oligomeric intermediates implicated in both the proliferation of amylid fibrils and in neuronal toxicity, were examined.

TL;DR: The application of a two-color single-molecule fluorescence technique to examine the assembly of oligomeric species formed during the aggregation of the SH3 domain of PI3 kinase provides direct evidence for a general mechanism of amyloid aggregation in which the stable cross-β structure emerges via internal reorganization of disordered oligomers form during the lag phase of the self-assembly reaction.

TL;DR: Conformational equilibria in ubiquitin chains provide an additional layer of regulation in the ubiquitIn system, and distinct conformations observed in differently linked polyubiquitin may contribute to the specificity of ubiquit in-interacting proteins.