Despite advances in machine learning-based protein structure prediction, we are still far
from fully understanding how proteins fold into their native conformation. The conventional …

It is now well established that the blood-clotting protein fibrinogen can polymerise into an
anomalous form of fibrin that is amyloid in character; the resultant clots and microclots entrap …

ABSTRACT p53 (also known as TP53) mutation and amyloid formation are long associated
with cancer pathogenesis; however, the direct demonstration of the link between p53 …

The secretory granules from the mammalian endocrine system are functional amyloids that
act as dynamic depots to store and release protein hormones into the bloodstream. The …

Enzyme‐instructed self‐assembly of bioactive molecules into nanobundles inside cells is
conceived to potentially disrupt plasma membrane and subcellular structure. Herein, an …

Hexahistidine-tagged proteins can be clustered by divalent cations into self-containing,
dynamic protein depots at the microscale, which under physiological conditions leak …

Nattokinase, from the Japanese fermented food natto, is a protease with fibrinolytic activity
that can thus degrade conventional blood clots. In some cases, however, including in Long …

In acidic secretory granules of mammalian cells, peptide hormones including the parathyroid
hormone are presumably stored in the form of functional amyloid fibrils. Mature PTH …

In nature, nontoxic protein amyloids serve as dynamic, protein-specific depots, exemplified
by both bacterial inclusion bodies and secretory granules from the endocrine system …

Among bio-inspired protein materials, secretory protein microparticles are of clinical interest
as self-contained, slow protein delivery platforms that mimic secretory granules of the human …