Stéphanie Baud

TL;DR: Using molecular simulations of monomeric and aggregated states, it is demonstrated that elastin-like and amyloid-like peptides are separable on the basis of backbone hydration and peptide-peptide hydrogen bonding, which supports a unified model of protein aggregation in which hydrations and conformational disorder are fundamental requirements for elastomeric function.

TL;DR: The primary goal of this comprehensive review is to summarize major achievements and paradigm-shifting discoveries made on the PG/GAG chemistry-biology axis, focusing on structural variability, structure-function relationships, metabolic, molecular, and epigenetic mechanisms underlying their synthesis.

TL;DR: This is the first study to demonstrate that EDPs, which mainly accumulate with aging, may be involved in the insidious development of IRES, and it is proposed that this IRES is due to interaction between the insulin receptor (IR) and the neuraminidase-1 subunit of the elastin receptor complex triggered by E DPs.

TL;DR: This work provides the first structural data concerning the interaction of the VGVAPG with its cognate receptor, and should allow the development of EBP-specific antagonists.

TL;DR: A general mechanism for the formation of β‐sheets on the surface of globular proteins and for amyloid self‐organization at hydrophobic interfaces is suggested.