نتایج جستجو برای: Ferritins

تعداد نتایج: 281  

Journal: :Accounts of chemical research 2005
Xiaofeng Liu Elizabeth C Theil

Ferritins are spherical, cage-like proteins with nanocavities formed by multiple polypeptide subunits (four-helix bundles) that manage iron/oxygen chemistry. Catalytic coupling yields diferric oxo/hydroxo complexes at ferroxidase sites in maxi-ferritin subunits (24 subunits, 480 kDa; plants, animals, microorganisms). Oxidation occurs at the cavity surface of mini-ferritins/Dps proteins (12 subu...

Journal: :The Biochemical journal 1992
S Lobreaux S J Yewdall J F Briat P M Harrison

The iron storage protein, ferritin, is widely distributed in the living kingdom. Here the complete cDNA and derived amino-acid sequence of pea seed ferritin are described, together with its predicted secondary structure, namely a four-helix-bundle fold similar to those of mammalian ferritins, with a fifth short helix at the C-terminus. An N-terminal extension of 71 residues contains a transit p...

2004
Jae-Woo Kim Sang H. Choi Peter T. Lillehei Glen C. King James R. Elliott Sang-Hyon Chu Yeonjoon Park Gerald D. Watt

ABSRACT Nanoparticle arrays biologically derived from an electrochemicallycontrolled site-specific biomineralization were fabricated on a gold substrate through the immobilization process of biomolecules. The work reported herein includes the immobilization of ferritin with various surface modifications, the electrochemical biomineralization of ferritins with different inorganic cores, the fabr...

2008
Jae-Woo Kim Sang H. Choi Peter T. Lillehei Sang-Hyon Chu Glen C. King Gerald D. Watt

Site-specific reconstituted nanoparticles were fabricated via electrochemicallycontrolled biomineralization through the immobilization of biomolecules. The work reported herein includes the immobilization of ferritin with various surface modifications, the electrochemical biomineralization of ferritins with different inorganic cores, and the electrocatalytic reduction of oxygen on the reconstit...

Journal: :Blood 1994
K Morikawa F Oseko S Morikawa

The effect of human spleen(L-rich) and heart(H-rich) ferritins on the proliferation and differentiation of human B lymphocytes was studied in comparison with that of holo- and apo-transferrins. Ferritins rich in H and L chain, as well as the transferrins, did not inhibit the proliferative response of resting and activated B cells stimulated with polyclonal B-cell mitogen, Staphylococcus aureus ...

Journal: :The Biochemical journal 1994
L R Harris M H Cake D J Macey

The influence of the superoxide-generating system, xanthine oxidase, on the release of iron from various vertebrate ferritins was determined both in the presence and absence of superoxide dismutase. The initial rate of iron release in the presence of this system was higher for ferritins from human, trout and rat liver than for those from lamprey liver and horse spleen. The proportion of this ir...

Journal: :Cancer research 1984
H L Hann M W Stahlhut I Millman

Fifteen nude mice were inoculated with a human neuroblastoma cell line and 14 with a human primary hepatocellular carcinoma cell line. Human ferritins were detected in the sera of the mice which developed tumors. Of 14 mice bearing human neuroblastoma, 12 had human liver-type ferritin (8 to 52 ng/ml) in their sera, and three of these also had HeLa-type ferritin (acidic ferritin) (29 to 40 ng/ml...

Journal: :Gene 2004
Jean-Pierre Durand Françoise Goudard Jacques Pieri Jean-Michel Escoubas Nathalie Schreiber Jean-Paul Cadoret

Ferritin has been shown as being the principal iron storage in the majority of living organisms. In marine species, ferritin is also involved in high-level accumulation of (210)Po. As part of our work on the investigation of these radionuclides' concentration in natural environment, ferritin was searched at the gene and protein level. Ferritin was purified from the visceral mass of the oyster C...

Journal: :The Biochemical journal 1992
J P Laulhère A M Labouré O Van Wuytswinkel J Gagnon J F Briat

Storage and buffering of iron is achieved by a class of proteins, the ferritins, widely distributed throughout the living kingdoms. All ferritins have in common their three-dimensional structure and their ability to store large amounts of iron in their central cavity. However, eukaryotic ferritins from plants and animals and bacterioferritins have no sequence similarity, and besides non-haem ir...

2011
Yu Zhang Brendan P. Orner

Protein self-assembly, through specific, high affinity, and geometrically constraining protein-protein interactions, can control and lead to complex cellular nano-structures. Establishing an understanding of the underlying principles that govern protein self-assembly is not only essential to appreciate the fundamental biological functions of these structures, but could also provide a basis for ...

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