Nature is a great source of inspiration in solving extremely complex problems, and it is every
day more common to use its strategies for the development of new materials, methods, and …

Ferritin is a vital protein complex responsible for storing iron in almost all living organisms. It
plays a crucial role in various metabolic pathways, inflammation processes, stress response …

This Handbook on Metalloproteins focuses on the available structural information of proteins
and their metal ion coordination spheres. It centers on the metal ions indispensable for life …

Ferritins, the cellular iron repositories, are self-assembled, hollow spherical nanocage
proteins composed of 24 subunits. The self-assembly process in ferritin generates the …

Protein self-assembly, through specific, high affinity, and geometrically constraining protein-
protein interactions, can control and lead to complex cellular nano-structures. Establishing …

Ferritin is a ubiquitous iron storage protein responsible for maintaining the iron homeostasis
in living organism and thereby protects the cell from oxidative damage. The ferritin protein …

Listeria innocua Dps (D NA binding p rotein from s tarved cells) affords protection to DNA
against oxidative damage and can accumulate about 500 iron atoms within its central cavity …

The subject of this review article was first reported approximately three decades ago upon
the discovery of a starvation-inducible protein found tightly bound to chromosomal DNA in 3 …

Dps (DNA-binding proteins from starved cells) proteins belong to a widespread bacterial
family of proteins expressed under nutritional and oxidative stress conditions. In particular …

Elucidating pore function at the 3-fold channels of 12-subunit, microbial Dps proteins is
important in understanding their role in the management of iron/hydrogen peroxide. The Dps …