The ferritins: molecular properties, iron storage function and cellular regulation

PM Harrison, P Arosio - Biochimica et biophysica acta (BBA)-bioenergetics, 1996 - Elsevier
The iron storage protein, ferritin, plays a key role in iron metabolism. Its ability to sequester
the element gives ferritin the dual functions of iron detoxification and iron reserve. The …

Unity in the biochemistry of the iron-storage proteins ferritin and bacterioferritin

K Honarmand Ebrahimi, PL Hagedoorn… - Chemical …, 2015 - ACS Publications
Life on earth is dependent on the catalytic activity of a number of different metal ions in their
polypeptide scaffold. Of these metals iron is widely used for catalysis of many reactions by …

Rapid protein-folding assay using green fluorescent protein

GS Waldo, BM Standish, J Berendzen… - Nature …, 1999 - nature.com
Formation of the chromophore of green fluorescent protein (GFP) depends on the correct
folding of the protein. We constructed a" folding reporter" vector, in which a test protein is …

Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts

DM Lawson, PJ Artymiuk, SJ Yewdall, JMA Smith… - Nature, 1991 - nature.com
FERRITINis important in iron homeostasis. Its twenty-four chains of two types, H and L,
assemble as a hollow shell providing an iron-storage cavity1–3. Ferritin molecules in cells …

Identification of the iron-responsive element for the translational regulation of human ferritin mRNA

MW Hentze, SW Caughman, TA Rouault… - Science, 1987 - science.org
Regulated translation of messenger RNA offers an important mechanism for the control of
gene expression. The biosynthesis of the intracellular iron storage protein ferritin is …

Ferritins: dynamic management of biological iron and oxygen chemistry

X Liu, EC Theil - Accounts of chemical research, 2005 - ACS Publications
Ferritins are spherical, cage-like proteins with nanocavities formed by multiple polypeptide
subunits (four-helix bundles) that manage iron/oxygen chemistry. Catalytic coupling yields …

Sequence patterns indicate an enzymatic involvement in integration of mammalian retroposons

J Jurka - Proceedings of the National Academy of Sciences, 1997 - National Acad Sciences
It is commonly accepted that the reverse-transcribed cellular RNA molecules, called
retroposons, integrate at staggered breaks in mammalian chromosomes. However, unlike …

Ferritin self-assembly, structure, function, and biotechnological applications

VV Sudarev, SM Dolotova, SM Bukhalovich… - International journal of …, 2023 - Elsevier
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 …

Ferritin nanocage: a versatile nanocarrier utilized in the field of food, nutrition, and medicine

C Zhang, X Zhang, G Zhao - Nanomaterials, 2020 - mdpi.com
Compared with other nanocarriers such as liposomes, mesoporous silica, and cyclodextrin,
ferritin as a typical protein nanocage has received considerable attention in the field of food …

Structure, function, and evolution of ferritins

SC Andrews, PM Harrison, SJ Yewdall, P Arosio… - Journal of inorganic …, 1992 - Elsevier
The ferritins of animals and plants and the bacterioferritins (BFRs) have a common iron-
storage function in spite of differences in cytological location and biosynthetic regulation …