Disrupted protein folding or decreased protein stability can lead to the accumulation of
(partially) un‐or misfolded proteins, which ultimately cause the formation of protein …

Antibody-based biotherapeutics have emerged as a successful class of pharmaceuticals
despite significant challenges and risks to their discovery and development. This review …

Transition of soluble proteins into insoluble amyloid fibrils is driven by self-propagating short
sequence stretches. However, accurate prediction of aggregation determinants remains …

The tendency for proteins to form aggregates is an inherent part of every proteome and
arises from the self-assembly of short protein segments called aggregation-prone regions …

The light chain (AL) amyloidosis is caused by the aggregation of light chain of antibodies
into amyloid fibrils. There are plenty of computational resources available for the prediction …

Short aggregation prone sequence motifs can trigger aggregation in peptide and protein
sequences. Most algorithms developed so far to identify potential aggregation prone regions …

Highlights•Computational methods identify aggregation-prone regions in protein sequences
as a guide for protein engineering.•Rational methods can reveal genotype-phenotype …

Cardiac amyloidosis is an uncommon restrictive cardiomyopathy featuring an unregulated
amyloid protein deposition that impairs organic function. Early cardiac amyloidosis …

Amyloids are fibrous cross-β protein aggregates that are capable of proliferation via
nucleated polymerization. Amyloid conformation likely represents an ancient protein fold …

Abstract The Curated Protein Aggregation Database (CPAD) is a manually curated and
open-access database dedicated to providing comprehensive information related to …