Results 1 to 10 of about 79,952 (154)

Recombinant ferritins for multimodal nanomedicine

Journal of Enzyme Inhibition and Medicinal Chemistry, 2023
In all living organisms, ferritins are a group of proteins important for maintaining iron homeostasis. Increasing amount of studies has shown that recombinant ferritins can be widely used in multimodal nanomedicine, especially for anticancer treatment ...
Yihao Li, Haoyu Gao, Eugenie Nepovimova, Qinghua Wu, Vojtech Adam, Kamil Kuca   +5 more
doaj   +2 more sources

Structural comparison of two ferritins from the marine invertebrate Phascolosoma esculenta

FEBS Open Bio, 2021
For marine invertebrates with no adaptive immune system, ferritin is a major intracellular iron‐storage protein with a critical role in innate immunity.
Tinghong Ming, Hengshang Huan, Chang Su, Chunheng Huo, Yan Wu, Qinqin Jiang, Xiaoting Qiu, Chenyang Lu, Jun Zhou, Ye Li, Xiurong Su   +10 more
doaj   +2 more sources

Effective charge saturation in ferritin cages [PDF]

Scientific Reports
Ferritins are proteins consisting of 24 subunits that make a spherical cage structure. We prepared a series of net-charge mutants of Escherichia coli and Pseudo-nitzschia multiseries ferritins (EcFtn and PmFtn, respectively) in which glutamate (Glu) and ...
Takumi Kuwata, Yuusuke Murakami, Daisuke Sato, Kazuo Fujiwara, Masamichi Ikeguchi   +4 more
doaj   +2 more sources

A Novel Approach for the Synthesis of Human Heteropolymer Ferritins of Different H to L Subunit Ratios

Journal of Molecular Biology, 2021
Mammalian ferritins are predominantly heteropolymeric species consisting of 24 structurally similar, but functionally different subunit types, named H and L, that co-assemble in different proportions.
Maura Poli, Paolo Arosio, Fadi Bou-Abdallah   +2 more
exaly   +2 more sources

Ferritins as natural and artificial nanozymes for theranostics

Theranostics, 2020
Nanozymes are a class of nanomaterials with intrinsic enzyme-like characteristics which overcome the limitations of natural enzymes such as high cost, low stability and difficulty to large scale preparation.
Bing Jiang, Kelong Fan, Xiyun Yan
exaly   +2 more sources

Heterologous Expression of Either Human or Soya Bean Ferritins in Budding Yeast Reveals Common Functions Protecting Against Oxidative Agents and Counteracting Double-Strand Break Accumulation [PDF]

Biomolecules
Ferritins are globular proteins that, upon self-assembly in nanocages, are capable of bio-safely storing huge concentrations of bioavailable iron. They are present in most cell types and organisms; one of the exceptions is yeast.
Nuria Pujol Carrión, Maria Ángeles de la Torre-Ruiz   +1 more
doaj   +2 more sources

The importance of eukaryotic ferritins in iron handling and cytoprotection

Biochemical Journal, 2015
Ferritins, the main intracellular iron storage proteins, have been studied for over 60 years, mainly focusing on the mammalian ones. This allowed the elucidation of the structure of these proteins and the mechanisms regulating their iron incorporation ...
Maura Poli, Federica Maccarinelli, Raffaella Gozzelino   +2 more
exaly   +2 more sources

Diversity of Fe2+ entry and oxidation in ferritins

Current Opinion in Chemical Biology, 2017
Nick le Brun, Justin Bradley
exaly   +2 more sources

Effect of Phosphate and Ferritin Subunit Composition on the Kinetics, Structure, and Reactivity of the Iron Core in Human Homo- and Heteropolymer Ferritins

Biochemistry, 2022
Ferritins are highly conserved supramolecular protein nanostructures that play a key role in iron homeostasis. Thousands of iron atoms can be stored inside their hollow cavity as a hydrated ferric oxyhydroxide mineral.
Aliaksandra A Reutovich, A. Srivastava, Gideon L Smith, Alexandre C. Foucher, D. Yates, E. Stach, G. Papaefthymiou, P. Arosio, Fadi Bou-Abdallah   +8 more
semanticscholar   +1 more source

Conservative and Atypical Ferritins of Sponges

International Journal of Molecular Sciences, 2021
Ferritins comprise a conservative family of proteins found in all species and play an essential role in resistance to redox stress, immune response, and cell differentiation.
K. I. Adameyko, A. Burakov, A. Finoshin, K. Mikhailov, O. Kravchuk, O. Kozlova, N. G. Gornostaev, A. Cherkasov, P. Erokhov, M. Indeykina, A. Bugrova, A. Kononikhin, A. Moiseenko, O. Sokolova, A. N. Bonchuk, I. Zhegalova, A. A. Georgiev, V. Mikhailov, N. Gogoleva, G. Gazizova, E. Shagimardanova, O. Gusev, Y. Lyupina   +22 more
semanticscholar   +1 more source