Self-assembling systems play a significant role in physiological functions and have therefore
attracted tremendous attention due to their great potential for applications in energy …

The aggregation of a polypeptide chain into amyloid fibrils and their accumulation and
deposition into insoluble plaques and intracellular inclusions is the hallmark of several …

Protein-folding intermediates have been implicated in amyloid fibril formation involved in
neurodegenerative disorders. However, the structural mechanisms by which intermediates …

Abstract Src homology 3 (SH3) domains are involved in the regulation of important cellular
pathways, such as cell proliferation, migration and cytoskeletal modifications. Recognition of …

The abnormal misfolding and aggregation of amyloid-β (Aβ) peptides into β-sheet enriched
insoluble deposits initiates a cascade of events leading to pathological processes and …

SRC homology 3 (SH3) domains are fundamental modules that enable the assembly of
protein complexes through physical interactions with a pool of proline-rich/noncanonical …

Liquid–liquid phase separation (LLPS) is an emerging phenomenon in cell physiology and
diseases. The weak multivalent interaction prerequisite for LLPS is believed to be facilitated …

Protein aggregation presents one of the key challenges in the development of protein
biotherapeutics. It affects not only product quality but also potentially impacts safety, as …

Protein aggregation is a topic of immense interest to the scientific community due to its role
in several neurodegenerative diseases/disorders and industrial importance. Several in silico …

Amyloid fibrillar assemblies, originally identified as pathological entities in
neurodegenerative diseases, have been widely adopted by various proteins to fulfill diverse …