The protein components of ferritins. Apoferritins are shell-like structures containing nanocavities and ferroxidase activities. Apoferritin shells are composed of 24 subunits, heteropolymers in vertebrates and homopolymers in bacteria. In vertebrates, there are two types of subunits, light chain and heavy chain. The heavy chain contains the ferroxidase activity.
Iron-containing proteins that are widely distributed in animals, plants, and microorganisms. Their major function is to store IRON in a nontoxic bioavailable form. Each ferritin molecule consists of ferric iron in a hollow protein shell (APOFERRITINS) made of 24 subunits of various sequences depending on the species and tissue types.

Overexpression of the hereditary hemochromatosis protein, HFE, in HeLa cells induces and iron-deficient phenotype. (1/232)

A transfectant HeLa cell clone expressing HFE under the control of a tetracycline-repressible promoter was generated. HFE expression was fully repressed by the presence of doxycycline, while it was strongly induced by growth in the absence of doxycycline. HFE accumulation was accompanied by a large (approximately 10-fold) decrease in H- and L-ferritin levels, by a approximately 3-4-fold increase in transferrin receptor, and a approximately 2-fold increase in iron regulatory protein activity. These indices of cellular iron deficiency were reversed by iron supplementation complexes. The overexpressed HFE immunoprecipitated together with transferrin receptor, indicating a physical association which is the likely cause for the observed approximately 30% decrease in 55Fe-transferrin incorporation after 18 h incubation. In the HFE-expressing cells the reduction in transferrin-mediated iron incorporation was partially compensated by a approximately 30% increase in non-transferrin iron incorporation from 55Fe-NTA, evident after prolonged, 18 h, incubations. The findings indicate that HFE binding to transferrin receptor reduces cellular iron availability and regulates the balance between transferrin-mediated and non-transferrin-mediated cellular iron incorporation.  (+info)

Iron primes hepatic macrophages for NF-kappaB activation in alcoholic liver injury. (2/232)

NF-kappaB activation induced by lipopolysaccharide (LPS) in cultured hepatic macrophages (HM) may be abrogated by pretreatment of cells with a lipophilic iron chelator, 1,2-dimethyl-3-hydroxypyrid-4-one (L1, deferiprone), suggesting a role for iron in this molecular event [M. Lin, M., R. A. Rippe, O. Niemela, G. Brittenham, and H. Tsukamoto, Am. J. Physiol. 272 (Gastrointest. Liver Physiol. 35): G1355-G1364, 1997]. To ascertain the relevance in vivo of this hypothesis, HM from an experimental model of alcoholic liver injury were examined for the relationship between nuclear factor (NF)-kappaB activation and iron storage. HM showed a significant increase in nonheme iron concentration (+70%), accompanied by enhanced generation of electron paramagnetic resonance-detected radicals (+200%), NF-kappaB activation (+100%), and tumor necrosis factor-alpha (+150%) and macrophage inflammatory protein-1 (+280%) mRNA induction. Treatment of the cells ex vivo with L1 normalized all these parameters. HM content of ferritin protein, ferritin L chain mRNA, and hemeoxygenase-1 mRNA and splenic content of nonheme iron were increased, suggesting enhanced heme turnover as a cause of the increased iron storage and NF-kappaB activation. To test this possibility, increased iron content in HM was reproduced in vitro by phagocytosis of heat-treated red blood cells. Treatment caused a 40% increase in nonheme iron concentration and accentuated LPS-induced NF-kappaB activation twofold. Both effects could be abolished by pretreatment of cells with zinc protoporphyrin, a hemeoxygenase inhibitor. To extend this observation, animals were splenectomized before 9-wk alcohol feeding. Splenectomy resulted in further increments in HM nonheme iron storage (+60%) and NF-kappaB activation (+90%) and mononuclear cell infiltration (+450%), particularly around the iron-loaded HM in alcohol-fed animals. These results support the pivotal role of heme-derived iron in priming HM for NF-kappaB activation and expression of proinflammatory genes in alcoholic liver injury.  (+info)

Interactions and aggregation of apoferritin molecules in solution: effects of added electrolytes. (3/232)

We have studied the structure of the protein species and the protein-protein interactions in solutions containing two apoferritin molecular forms, monomers and dimers, in the presence of Na(+) and Cd(2+) ions. We used chromatographic, and static and dynamic light scattering techniques, and atomic force microscopy (AFM). Size-exclusion chromatography was used to isolate these two protein fractions. The sizes and shapes of the monomers and dimers were determined by dynamic light scattering and AFM. Although the monomer is an apparent sphere with a diameter corresponding to previous x-ray crystallography determinations, the dimer shape corresponds to two, bound monomer spheres. Static light scattering was applied to characterize the interactions between solute molecules of monomers and dimers in terms of the second osmotic virial coefficients. The results for the monomers indicate that Na(+) ions cause strong intermolecular repulsion even at concentrations higher than 0.15 M, contrary to the predictions of the commonly applied Derjaguin-Landau-Verwey-Overbeek theory. We argue that the reason for such behavior is hydration force due to the formation of a water shell around the protein molecules with the help of the sodium ions. The addition of even small amounts of Cd(2+) changes the repulsive interactions to attractive but does not lead to oligomer formation, at least at the protein concentrations used. Thus, the two ions provide examples of strong specificity of their interactions with the protein molecules. In solutions of the apoferritin dimer, the molecules attract even in the presence of Na(+) only, indicating a change in the surface of the apoferritin molecule. In view of the strong repulsion between the monomers, this indicates that the dimers and higher oligomers form only after partial denaturation of some of the apoferritin monomers. These observations suggest that aggregation and self-assembly of protein molecules or molecular subunits may be driven by forces other than those responsible for crystallization and other phase transitions in the protein solution.  (+info)

The role of lactoferrin in the bactericidal function of polymorphonuclear leucocytes. (4/232)

Rabbit polymorphonuclear leucocytes contain the iron-binding protein lactoferrin, and can rapidly phagocytose and destroy Pseudomonas aeruginosa. The lactoferrin normally has a large unsaturated iron-binding capacity. If the cells are exposed to a ferritin-antibody complex, large amounts of this are phagocytosed and appear in the cytoplasmic granules and phagosomes. This leads to saturation of the cellular iron-binding protein with Fe. In these circumstances, the bactericidal power of the cells is greatly reduced with the result that some phagocytosed bacteria survive and eventually grow and destroy the cells. An apoferritin-antibody complex used as a control is also phagocytosed but has no effect on the bactericidal power of the cell. The results support the view that lactoferrin plays an essential role in the bactericidal power of the cell.  (+info)

Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: in vivo role of ferritin ferroxidase activity. (5/232)

Transfectant HeLa cells were generated that expressed human ferritin H-chain wild type and an H-chain mutant with inactivated ferroxidase activity under the control of the tetracycline-responsive promoter (Tet-off). The clones accumulated exogenous ferritins up to levels 14-16-fold over background, half of which were as H-chain homopolymers. This had no evident effect in the mutant ferritin clone, whereas it induced an iron-deficient phenotype in the H-ferritin wild type clone, manifested by approximately 5-fold increase of IRPs activity, approximately 2.5-fold increase of transferrin receptor, approximately 1.8-fold increase in iron-transferrin iron uptake, and approximately 50% reduction of labile iron pool. Overexpression of the H-ferritin, but not of the mutant ferritin, strongly reduced cell growth and increased resistance to H(2)O(2) toxicity, effects that were reverted by prolonged incubation in iron-supplemented medium. The results show that in HeLa cells H-ferritin regulates the metabolic iron pool with a mechanism dependent on the functionality of the ferroxidase centers, and this affects, in opposite directions, cellular growth and resistance to oxidative damage. This, and the finding that also in vivo H-chain homopolymers are much less efficient than the H/L heteropolymers in taking up iron, indicate that functional activity of H-ferritin in HeLa cells is that predicted from the in vitro data.  (+info)

Hydrogen ion interactions of horse spleen ferritin and apoferritin. (6/232)

The interactions of horse spleen ferritin and its derivative apoferritin with H+ ions were studied by potentiometric and spectrophotometric titration; to aid in data analysis, heats of ionization over a limited pH range and amide content were also determined. Per apoferritin subunit, all tyrosine and cysteine side chains, two of the nine lysine side chains and at least three of the six histidine side chains were found not to titrate; a preliminary but self-consistent analysis of the titration data is proposed. The titration curve of ferritin was identical with that of apoferritin in the pH range 5.5 to 3. In addition, under the conditions used, the reactivities of ferritin histidines to bromoacetate and of ferritin lysines to formaldehyde were identical with those in apoferritin. Above pH 8, a time-dependent titration of the ferritin core occurs which prevents comparison of the titration curves of the two proteins in this region. However, in the pH regions 5.5 to 7.5, two extra groups per subunit titrate reversibly in ferritin relative to apoferritin. Moreover, although the isoionic points of ferritin and apoferritin are identical in water, the isoionic point of ferritin is 0.5 pH unit lower than that of apoferritin in 0.16 to 1 M KCl. The different effects of KCl and NaCl on the two proteins indicate the presence of cation binding sites in ferritin that are absent in apoferritin and possibly also the presence of anion binding sites in apoferritin that are occupied in ferritin by anions of the core. The difference between the isoionic points of the two proteins in KCl has been interpreted to indicate the presence of approximately 2 phosphate residues per ferritin subunit which serve as cation binding sites and which are negatively charged at the isoionic point in KCl. These phosphates may also represent the additional residues that titrate in ferritin between pH 5.5 and 7.5, or may interact with positively charged residues on the inner surface of the ferritin shell, or both.  (+info)

Expression and characterization of the chemokine receptors CCR2 and CCR5 in mice. (7/232)

The chemokine receptors CCR2 and CCR5 play important roles in the recruitment of monocytes/macrophages and T cells. To better understand the role of both receptors in murine models of inflammatory diseases and to recognize potential problems when correlating these data to humans, we have generated mAbs against murine CCR2 and CCR5. In mice CCR2 is homogeneously expressed on monocytes and on 2--15% of T cells, closely resembling the expression pattern in humans. In contrast to humans, murine NK cells are highly CCR5 positive. In addition, CCR5 is expressed on 3--10% of CD4 and 10--40% of CD8-positive T cells and is weakly detectable on monocytes. Using a model of immune complex nephritis, we examined the effects of inflammation on chemokine receptor expression and found a 10-fold enrichment of CCR5(+) and CCR2(+) T cells in the inflamed kidneys. The activity of various chemokines and the antagonistic properties of the mAbs were measured by ligand-induced internalization of CCR2 and CCR5 on primary leukocytes. The Ab MC-21 (anti-CCR2) reduced the activity of murine monocyte chemotactic protein 1 by 95%, whereas the Ab MC-68 (anti-CCR5) blocked over 99% of the macrophage-inflammatory protein 1alpha and RANTES activity. MC-21 and MC-68 efficiently blocked the ligand binding to CCR2 and CCR5 with an IC(50) of 0.09 and 0.6--1.0 microg/ml, respectively. In good correlation to these in vitro data, MC-21 almost completely prevented the influx of monocytes in thioglycollate-induced peritonitis. Therefore, both Abs appear as useful reagents to further study the role of CCR2 and CCR5 in murine disease models.  (+info)

Chemokine and chemokine receptor expression during initiation and resolution of immune complex glomerulonephritis. (8/232)

Chemokines participate in leukocyte infiltration, which plays a major role in glomerular injury during immune complex glomerulonephritis (IC-GN). Because target cell expression of chemokine receptors (CCR) is thought to mediate leukocyte migration, the expression pattern of chemokines and CCR in a model of IC-GN was examined. The transient course and predominant glomerular pathology of this model allows the examination of both the induction and resolution phases of IC-GN. GN was induced in mice by daily apoferritin injection for 2 wk. Urine samples and kidneys were obtained at 1, 2, and 4 wk. Albuminuria was noted at 2 wk, but resolved after 4 wk. This was associated with glomerular IC deposits and mesangial proliferation. Glomerular macrophage infiltration was prominent at 1 and 2 wk, which resolved at 4 wk. Expression of monocyte chemoattractant protein-1 (MCP-1) and RANTES mRNA was upregulated at week 1 and decreased to control levels at weeks 2 and 4. The expression was localized to glomeruli by in situ hybridization and immunohistochemistry. The mRNA of CCR1, CCR2, and CCR5 but not CCR3 or CCR4 were upregulated at week 1 and decreased at weeks 2 and 4. Expression of CCR5 was located to the glomerulus by in situ hybridization and quantitative reverse transcription-PCR of isolated glomeruli. In summary, in a model of transient IC-GN, MCP-1 and RANTES and their receptors CCR1, CCR2, and CCR5 are expressed early and are already downregulated at the peak of proteinuria and leukocyte infiltration. Resolution of glomerulonephritis is associated with a return to baseline of chemokine and CCR expression. Therefore, it is concluded that glomerular MCP-1 and RANTES production directs circulating leukocytes that express CCR1, CCR2, and CCR5 into the glomerulus. After initiating GN, MCP-1 and RANTES and their receptors are readily downregulated.  (+info)

Apoferritins are the protein shells or apoproteins of ferritin molecules that are devoid of iron. Ferritin is a protein in cells that stores iron and releases it in a form that can be used by the body. Apoferritin can bind with iron ions to form ferritin. It has a hollow, spherical structure and is often used as a model for studying protein folding and assembly.

Ferritin is a protein in iron-metabolizing cells that stores iron in a water-soluble form. It is found inside the cells (intracellular) and is released into the bloodstream when the cells break down or die. Measuring the level of ferritin in the blood can help determine the amount of iron stored in the body. High levels of ferritin may indicate hemochromatosis, inflammation, liver disease, or other conditions. Low levels of ferritin may indicate anemia, iron deficiency, or other conditions.

Apoferritin of horse spleen". J. Biol. Chem. 147 (1): 91-97. Granick, S. (1938). "Chloroplast nitrogen of some higher plants". ... A second paper, by Granick and Michaelis, showed that iron could be removed from ferritin to produce apoferritin. Granick went ... Kresge, Nicole; Robert D. Simoni; Robert L. Hill (2004-12-03). "The Characterization of Ferritin and Apoferritin by Leonor ...
Addison JM, Fitton JE, Lewis WG, May K, Harrison PM (November 1983). "The amino acid sequence of human liver apoferritin". FEBS ... "Cloning and sequencing of a full length cDNA coding for a human apoferritin H chain: evidence for a multigene family". The EMBO ... "Structure of gene and pseudogenes of human apoferritin H". Nucleic Acids Research. 14 (2): 721-36. doi:10.1093/nar/14.2.721. ...
Addison JM, Fitton JE, Lewis WG, May K, Harrison PM (November 1983). "The amino acid sequence of human liver apoferritin". FEBS ... A study conducted with different apoferritins with distinct compositions of heavy and light subunits revealed that both ... "Cloning of the gene coding for human L apoferritin". Nucleic Acids Res. 14 (7): 2863-76. doi:10.1093/nar/14.7.2863. PMC 339708 ... "Negative and positive elements in the promoter region of the human apoferritin L gene". Biochem. Biophys. Res. Commun. 215 (1 ...
"Helix packing and subunit conformation in horse spleen apoferritin". Nature. 288 (5788): 298-300. Bibcode:1980Natur.288..298C. ...
Apoferritin binds to free ferrous iron and stores it in the ferric state. As ferritin accumulates within cells of the ... "Ferritin - Homo sapiens (Human)". Look up ferritin or apoferritin in Wiktionary, the free dictionary. Ferritins at the U.S. ... Ferritin that is not combined with iron is called apoferritin.[citation needed] Ferritin genes are highly conserved between ... "Size-Selective Olefin Hydrogenation by a Pd Nanocluster Provided in an Apo-Ferritin Cage". Angewandte Chemie. 43 (19): 2527-30 ...
Ho, Ru-Hung; Chen, Yu-Hung; Wang, Chong Mou (June 2012). "Surface differentiation of ferritin and apoferritin with atomic force ...
Luo, Yanan; Wang, Xuenv; Du, Dan; Lin, Yuehe (2015-09-15). "Hyaluronic acid-conjugated apoferritin nanocages for lung cancer ...
This is an alternative to the apoferritin cage technique currently used to synthesize uniform CdSe nanoparticles. Such ... Apoferritin". Chemistry Letters. 33 (9): 1158-1159. doi:10.1246/cl.2004.1158. Benyus, J. M. (2001). Along Came a Spider. Sierra ...
Chavan SG, Yagati AK, Mohammadniaei M, Min J, Lee MH (May 2019). "Robust Bioengineered Apoferritin Nanoprobes for ...
In 2020, Scheres and collaborators used RELION to reach atomic resolution for a cryo-EM reconstruction of apo-Ferritin. Besides ...
... apoferritin MeSH D12.776.556.579.374.187 - hemerythrin MeSH D12.776.556.579.374.281 - inositol oxygenase MeSH D12.776.556.579. ...
... which is accomplished by Fe2+ binding to apoferritin (in which case the iron will leave the body when the cell dies and is ...
... apoferritin MeSH D12.776.157.427.374.187 - hemerythrin MeSH D12.776.157.427.374.375 - iron-sulfur proteins MeSH D12.776.157.427 ...
... which is accomplished by Fe2+ binding to apoferritin (in which case the iron will leave the body when the cell dies and is ...
Harrison, Pauline M. (1959), "The structures of ferritin and apoferritin: Some preliminary X-ray data", Journal of Molecular ...
1.55 A structure of human apoferritin obtained from data subset of Titan Mono-BCOR microscope ... Our apoferritin structure has almost twice the 3D information content of the current world record reconstruction (at 1.54 Å ... Here we report a 1.25 Å-resolution structure of apoferritin obtained by cryo-EM with a newly developed electron microscope that ... 1.55 A structure of human apoferritin obtained from data subset of Titan Mono-BCOR microscope. *PDB DOI: https://doi.org/ ...
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updated apoferritin tutorial for 2.0.0 alpha When can we expect an updated tutorial for version 2.0.0? I can only achieve an 8A ...
The present study is the first report of a Y-sutural congenital cataract mapping to 19q13.3. The mutation observed in FTL in this family highlights the phenotypic heterogeneity of the disorder in relation to the genotype as the identical mutation (32 G|A) has previously been reported in two Itali …
Apoferritin of horse spleen". J. Biol. Chem. 147 (1): 91-97. Granick, S. (1938). "Chloroplast nitrogen of some higher plants". ... A second paper, by Granick and Michaelis, showed that iron could be removed from ferritin to produce apoferritin. Granick went ... Kresge, Nicole; Robert D. Simoni; Robert L. Hill (2004-12-03). "The Characterization of Ferritin and Apoferritin by Leonor ...
L apoferritin. *MGC71996. *NBIA3. Additional Information & Resources. Tests Listed in the Genetic Testing Registry. *Tests of ...
... apoferritin; APT, abnormal prothrombin; ATLP, apoferritin templated lead phosphates; AU, uric acid; Bax, Bcl-2 associated X ... Abbreviations: AA, ascorbic acid; AA-P, ascorbic acid 2-phosphate; ACTP, apoferritin templated cadmium phosphates; AFP, alpha ... Ge, X.; Zhang, A.; Lin, Y.; Du, D. Simultaneous immunoassay of phosphorylated proteins based on apoferritin templated metallic ... or Cd and Pb apoferritins for the stripping voltammetric detection of AFP and CEA by SWV [58], and metal ions-doped chitosan ...
Apoferritin-encapsulation of cysteine protease inhibitors for cathepsin L inhibition in cancer cells. RSC Advances. 9, 36699- ... An Apoferritin-based Drug Delivery System for the Tyrosine Kinase Inhibitor Gefitinib ADVANCED HEALTHCARE MATERIALS. 4(18), ... TARGETING BRAIN TUMOURS: APOFERRITIN NANOCAGE FOR DELIVERY OF NOVEL ANALOGUES OF TEMOZOLOMIDE NEURO-ONCOLOGY. 21, 4-4 ... Development of novel apoferritin formulations for antitumour benzothiazoles. Cancer Reports. 2, e1155 ...
The AAV-DJ structure has been determined to 1.56 Å resolution through cryo-electron microscopy (cryo-EM). Only apoferritin is ... The AAV-DJ structure has been determined to 1.56 Å resolution through cryo-electron microscopy (cryo-EM). Only apoferritin is ...
Supercharged Fluorescent Protein-Apoferritin Cocrystals for Lighting Applications. Marta Patrian, Ahmed Shaukat, Mattia Nieddu ... Supercharged Fluorescent Protein-Apoferritin Cocrystals for Lighting Applications. Marta Patrian, Ahmed Shaukat, Mattia Nieddu ... Supercharged Fluorescent Protein-Apoferritin Cocrystals for Lighting Applications. Marta Patrian, Ahmed Shaukat, Mattia Nieddu ...
Categories: Apoferritin Image Types: Photo, Illustrations, Video, Color, Black&White, PublicDomain, CopyrightRestricted 1 ...
Different apoferritin templated metal phosphates were used as distinguishable signal reporters (apoferritin templated cadmium ... Simultaneous immunoassay of phosphorylated proteins based on apoferritin templated metallic phosphates as voltammetrically ... Apoferritin templated metallic phosphates; Phoaphorylated protein; Electrochemical detection ... phosphates (ATCP) and apoferritin templated lead phosphates (ATLP)) to enhance the detection sensitivity. Here, magnetic Fe3O4 ...
Apo)ferritin [47246] (3 species). *. Species Bullfrog (Rana catesbeiana) [TaxId:8400] [47249] (7 PDB entries). ...
How does it work? The teams used as their "test bed" a protein called apoferritin, measuring resolution with metric units ... called ångströms (1 Å is one ten-billion of a meter); the previous resolution record for imaging apoferritin was 1.54 ångströms ...
apoferritin. Fe2+. ferroportin. Fe3+. Ceruloplasmin-Cu2+ Ceruloplasmin-Cu1+. Other (not well understood). • Immune system, ...
The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins ( ...
Zhen, Z. ; Tang, W. ; Chen, H. ; Lin, X. ; Todd, T. ; Wang, G. ; Cowger, T. ; Chen, X. ; Xie, J. RGD-modified apoferritin ...
A part of the apoferritin protein (yellow) with a tyrosine side chain highlighted in grey. The amino acid tyrosine consists of ... Using the new microscope, the scientists have taken more than one million images of the protein apoferritin to map the ...
Figure: An Apoferritin reconstruction at 1.9 Angstrom resolution collected on our Titan Krios using our Gatan K2 detector. The ... The FEI Titan Krios performance has been validated to 1.9 Angstrom structural resolution using Apoferritin as a well-studied ...
Electrochemical detection of DNA hybridization based on signal DNA probe modified with Au and apoferritin nanoparticles. Pages ...
Investigations on Differently Sized Monodisperse Iron Oxide Nanoparticles Synthesized by Remineralization of Apoferritin ...
The researchers used human apoferritin, a protein found naturally in humans and which is biologically inactive, as a scaffold ...
Its formed in the intestine when iron unites with a special protein called apoferritin. It is then stored in the bodys ...
Hereditary hyperferritinaemia-cataract syndrome (HHCS) is a rare disorder usually caused by heterozygous mutations in the iron-responsive element (IRE) in the 5 untranslated region (5UTR) of the L-ferritin gene (FTL), disturbing the binding of iron regulatory proteins (IRPs) and the post-transcrip …
Suitability for high resolution structure determination is confirmed by SPA of apoferritin. Prevention of protein denaturation ...
Fractionation of subunits of horse apoferritin by gel filtration. 1969, Vol. 34, Issue 3, pp. 1067-1075 [Abstract] ... V. The preparation of apoferritin by alcohol precipitation. 1951, Vol. 16, pp. 204-206 [Abstract] ...
Thyroglobulin bovine (669 kDa), Horse apoferritin (443 kDa), Sweet potato β-Amylase (200 kDa), BSA (66 kDa), Bovine carbonic ...
L-CHAIN HORSE APOFERRITIN. div#help { text-align: right; } div#help a { text-decoration: none; } Help ...
Journal Article] In Vitro synthesis of calcium nanoparticles using the protein cage of apoferritin2008. *. Author(s). H.Fukano ... Journal Article] In Vitro synthesis of calcium nanoparticles using the protein cage of apoferritin2008. *. Author(s). Fukano, H ... Presentation] In Vitro Synthesis of Calcium Nanoparticles Using the Protein Cage of Apoferritin2007. *. Author(s). Fukano, H., ...
Development of high sensitive MRI contrast agent encapsulating CEST agent into apoferritin cavityPrincipal Investigator. *. ... Journal Article] Effective encapsulation of a new cationic gadolinium chelate into apoferritin and its evaluation as an MRI ...
  • A second paper, by Granick and Michaelis, showed that iron could be removed from ferritin to produce apoferritin. (wikipedia.org)
  • The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins (APOLIPOPROTEINS). (harvard.edu)
  • A part of the apoferritin protein (yellow) with a tyrosine side chain highlighted in grey. (phys.org)
  • Using the new microscope, the scientists have taken more than one million images of the protein apoferritin to map the molecular structure with a resolution of 1.25 angstroms. (phys.org)
  • Simultaneous immunoassay of phosphorylated proteins based on apoferritin templated metallic phosphates as voltammetrically distinguishable signal reporters. (cdc.gov)
  • Here we report a 1.25 Å-resolution structure of apoferritin obtained by cryo-EM with a newly developed electron microscope that provides, to our knowledge, unprecedented structural detail. (rcsb.org)
  • The FEI Titan Krios performance has been validated to 1.9 Angstrom structural resolution using Apoferritin as a well-studied target structure utilizing our Gatan K2 detector and Gatan Energy Filter combination. (edu.au)
  • Ullrich, A. and Horn, S. (2013) Structural Investigations on Differently Sized Monodisperse Iron Oxide Nanoparticles Synthesized by Remineralization of Apoferritin Molecules. (scirp.org)
  • Heavy or light, actions: Carbon monoxide combines with apoferritin to form magnesium carbonate. (riversideortho.com)
  • Our apoferritin structure has almost twice the 3D information content of the current world record reconstruction (at 1.54 Å resolution 3 ). (rcsb.org)
  • Figure: An Apoferritin reconstruction at 1.9 Angstrom resolution collected on our Titan Krios using our Gatan K2 detector. (edu.au)
  • Suitability for high resolution structure determination is confirmed by SPA of apoferritin. (fu-berlin.de)
  • Titan reached 1.47A resolution with apoferritin on June benchmarking and is running smoothly now. (jhmi.edu)
  • In this paper, we show that collecting cryo-ET STA data using the same conditions as SPA, with both correlated double sampling (CDS) and the super-resolution mode, allowed apoferritin to be reconstructed out to the physical Nyquist frequency of the images. (ox.ac.uk)
  • Even with just two tilt series, STA yields an apoferritin map at 2.9 Å resolution. (ox.ac.uk)
  • The compounds were tested for their ability to bind a surrogate anesthetic binding protein target, apoferritin. (asahq.org)
  • However, our lab recently developed a miniaturized fluorescence assay to screen 397,939 compounds, utilizing apoferritin protein as a surrogate for GABAA. (nih.gov)
  • Herein, gold nanoparticles (AuNPs) were synthesized in the cavity of horse spleen apoferritin protein (HoSAF) and protein surface was labeled with 2-amino-2-deoxy-glucose (2DG) as a cell surface glucose transport protein specific targeting probe to study the feasibility of its usage as a computer tomography (CT) contrast agent with tumor targeting capability through in vitro experiments. (metu.edu.tr)
  • 2DG conjugated and gold-loaded apoferritin (Au-HoSAF-2DG) nanoparticles (NPs) showed selective targeting for human breast adenocarcinoma (MCF-7) cells when compared to normal breast (MCF-10A) cells. (metu.edu.tr)
  • With this improvement, we determine the structure of apoferritin, a smooth octahedral shell of α-helical subunits that is particularly difficult to solve by electron microscopy. (rcsb.org)
  • Apoferritin shells are composed of 24 subunits, heteropolymers in vertebrates and homopolymers in bacteria. (bvsalud.org)
  • Each ferritin molecule consists of ferric iron in a hollow protein shell (APOFERRITINS) made of 24 subunits of various sequences depending on the species and tissue types. (rush.edu)
  • Ferritin consists of a protein shell (apoferritin) surrounding variable amounts of iron complexed as ferric hydroxide-phosphate. (medicalalgorithms.com)
  • Simultaneous immunoassay of phosphorylated proteins based on apoferritin templated metallic phosphates as voltammetrically distinguishable signal reporters. (cdc.gov)
  • A second paper, by Granick and Michaelis, showed that iron could be removed from ferritin to produce apoferritin. (wikipedia.org)
  • Wishing to check his own method on a stable, reproducible protein, he chose apoferritin (the iron-free fraction of heme discovered by Granick). (nih.gov)
  • The researchers used human apoferritin, a protein found naturally in humans and which is biologically inactive, as a scaffold for the molecule. (viewgtalistings.com)
  • Upon iron removal, apoferritin was shown to allow the encapsulation of an artificial transfer hydrogenase (ATHase) based on the streptavidin-biotin technology. (rsc.org)
  • This study compared the effect of loading apoferritin either with ferrous ammonium sulfate in various buffers or with ceruloplasmin and chelated ferrous iron. (jostchemical.com)
  • It was shown that loading of apoferritin with ferrous ammonium sulfate was dependent on buffer and pH, and was directly related to the rate of iron autoxidation. (jostchemical.com)
  • Ferrous gluconate is a source of iron that, following administration, combines with apoferritin to form ferritin, which is stored in the liver, spleen, red bone marrow, and intestinal mucosa. (affygility.com)
  • Iron in excess of the amount needed for hemoglobin synthesis binds to a storage protein, apoferritin, forming ferritin. (hypothes.is)
  • Two data sets for recombinant mouse heavy-chain apoferritin cooled with liquid-nitrogen or liquid-helium to 85 or 17 K were collected, processed and compared. (mpg.de)
  • His values of the molecular weights of apoferritin from man, horse, and dog agreed with each other within a range of possible error of little more than 1 per cent. (nih.gov)
  • Apoferritins are shell-like structures containing nanocavities and ferroxidase activities. (bvsalud.org)
  • Apoferritin reconstruction at 1.2 Å resolution created from 3,600 images of 297k particles acquired in 6 hours (EPU data acquisition on the Thermo Scientific Krios G4 Cryo-TEM). (thermofisher.com)
  • 2020 ) 2.7 Å cryo-EM structure of vitrified M. musculus H-chain apoferritin from a compact 200 keV cryo-microscope. (neurotree.org)
  • Apoferritin: a potential nanocarrier for cancer imaging and drug delivery. (medscape.com)
  • Benches, omitting generic farxiga withdrawal next the agrestic apoferritin purchase precose purchase generic because of tenesmic, extrapolate inconsequential Halotex clippingly regardless of found. (mercedessosa.org)