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.
The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
An encapsulated lymphatic organ through which venous blood filters.
Large, hoofed mammals of the family EQUIDAE. Horses are active day and night with most of the day spent seeking and consuming food. Feeding peaks occur in the early morning and late afternoon, and there are several daily periods of rest.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A colorless to white crystalline compound with a camphoraceous odor and taste. It is a widely used preservative in various pharmaceutical solutions, especially injectables. Also, it is an active ingredient in certain oral sedatives and topical anesthetics.
Compounds consisting of glucosamine and lactate joined by an ether linkage. They occur naturally as N-acetyl derivatives in peptidoglycan, the characteristic polysaccharide composing bacterial cell walls. (From Dorland, 28th ed)
The diversion of RADIATION (thermal, electromagnetic, or nuclear) from its original path as a result of interactions or collisions with atoms, molecules, or larger particles in the atmosphere or other media. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
That portion of the electromagnetic spectrum in the visible, ultraviolet, and infrared range.
Relating to the size of solids.
Scattering of a beam of electromagnetic or acoustic RADIATION, or particles, at small angles by particles or cavities whose dimensions are many times as large as the wavelength of the radiation or the de Broglie wavelength of the scattered particles. Also know as low angle scattering. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed) Small angle scattering (SAS) techniques, small angle neutron (SANS), X-ray (SAXS), and light (SALS, or just LS) scattering, are used to characterize objects on a nanoscale.
Treatment using irradiation with LASER light of low power intensity so that the effects are not due to heat, as they are in LASER THERAPY.
An optical source that emits photons in a coherent beam. Light Amplification by Stimulated Emission of Radiation (LASER) is brought about using devices that transform light of varying frequencies into a single intense, nearly nondivergent beam of monochromatic radiation. Lasers operate in the infrared, visible, ultraviolet, or X-ray regions of the spectrum.
Particles consisting of aggregates of molecules held loosely together by secondary bonds. The surface of micelles are usually comprised of amphiphatic compounds that are oriented in a way that minimizes the energy of interaction between the micelle and its environment. Liquids that contain large numbers of suspended micelles are referred to as EMULSIONS.
A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN.
The study and practice of medicine by direct examination of the patient.
An excessive accumulation of iron in the body due to a greater than normal absorption of iron from the gastrointestinal tract or from parenteral injection. This may arise from idiopathic hemochromatosis, excessive iron intake, chronic alcoholism, certain types of refractory anemia, or transfusional hemosiderosis. (From Churchill's Illustrated Medical Dictionary, 1989)
A disorder of iron metabolism characterized by a triad of HEMOSIDEROSIS; LIVER CIRRHOSIS; and DIABETES MELLITUS. It is caused by massive iron deposits in parenchymal cells that may develop after a prolonged increase of iron absorption. (Jablonski's Dictionary of Syndromes & Eponymic Diseases, 2d ed)
An iron-binding beta1-globulin that is synthesized in the LIVER and secreted into the blood. It plays a central role in the transport of IRON throughout the circulation. A variety of transferrin isoforms exist in humans, including some that are considered markers for specific disease states.
A series of steps taken in order to conduct research.
A procedure consisting of a sequence of algebraic formulas and/or logical steps to calculate or determine a given task.
Computer-based representation of physical systems and phenomena such as chemical processes.
The homogeneous mixtures formed by the mixing of a solid, liquid, or gaseous substance (solute) with a liquid (the solvent), from which the dissolved substances can be recovered by physical processes. (From Grant & Hackh's Chemical Dictionary, 5th ed)
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
A federal area located between Maryland and Virginia on the Potomac river; it is coextensive with Washington, D.C., which is the capital of the United States.
A rare autosomal recessive disease characterized by the deposition of copper in the BRAIN; LIVER; CORNEA; and other organs. It is caused by defects in the ATP7B gene encoding copper-transporting ATPase 2 (EC 3.6.3.4), also known as the Wilson disease protein. The overload of copper inevitably leads to progressive liver and neurological dysfunction such as LIVER CIRRHOSIS; TREMOR; ATAXIA and intellectual deterioration. Hepatic dysfunction may precede neurologic dysfunction by several years.
Complex sets of enzymatic reactions connected to each other via their product and substrate metabolites.
The addition of descriptive information about the function or structure of a molecular sequence to its MOLECULAR SEQUENCE DATA record.
Occasions to commemorate an event or occasions designated for a specific purpose.
Anastomosis of splenic vein to renal vein to relieve portal hypertension.
Sets of structured vocabularies used for describing and categorizing genes, and gene products by their molecular function, involvement in biological processes, and cellular location. These vocabularies and their associations to genes and gene products (Gene Ontology annotations) are generated and curated by the Gene Ontology Consortium.
Ruminant mammals of South America. They are related to camels.
An immunoglobulin fragment composed of one variable domain from an IMMUNOGLOBULIN HEAVY CHAIN or IMMUNOGLOBULIN LIGHT CHAIN.
The largest of polypeptide chains comprising immunoglobulins. They contain 450 to 600 amino acid residues per chain, and have molecular weights of 51-72 kDa.
A form of antibodies consisting only of the variable regions of the heavy and light chains (FV FRAGMENTS), connected by a small linker peptide. They are less immunogenic than complete immunoglobulin and thus have potential therapeutic use.
A primitive form of digestive gland found in marine ARTHROPODS, that contains cells similar to those found in the mammalian liver (HEPATOCYTES), and the PANCREAS.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
Hereditary and sporadic conditions which are characterized by progressive nervous system dysfunction. These disorders are often associated with atrophy of the affected central or peripheral nervous system structures.
Genes bearing close resemblance to known genes at different loci, but rendered non-functional by additions or deletions in structure that prevent normal transcription or translation. When lacking introns and containing a poly-A segment near the downstream end (as a result of reverse copying from processed nuclear RNA into double-stranded DNA), they are called processed genes.

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)

Mouse Ferritin light chain 1, Ftl1 ELISA KIT allows for the in vitro quantitative determination of Mouse Ftl1 concentrations in serum, plasma, tissue homogenates, cell culture supernates or other biological fluids.
Ferritin heavy chain is a ferroxidase enzyme that in humans is encoded by the FTH1 gene. This gene encodes the heavy subunit of ferritin, the major intracellular iron storage protein in prokaryotes and eukaryotes. It is composed of 24 subunits of the heavy and light ferritin chains. Variation in ferritin subunit composition may affect the rates of iron uptake and release in different tissues. A major function of ferritin is the storage of iron in a soluble and nontoxic state. Defects in ferritin proteins are associated with several neurodegenerative diseases. This gene has multiple pseudogenes. Several alternatively spliced transcript variants have been observed, but their biological validity has not been determined. FTH1 has been shown to interact with Ferritin light chain. Ferritin GRCh38: Ensembl release 89: ENSG00000167996 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000024661 - Ensembl, May 2017 Human PubMed Reference:. Mouse PubMed Reference:. Hentze MW, Keim S, ...
1. Mumbauer S, Pascual J, Kolotuev I, Hamaratoglu F (2019) Ferritin heavy chain protects the developing wing from reactive oxygen species and ferroptosis. PLoS Genet 15(9): e1008396. https://doi.org/10.1371/journal.pgen.1008396 31568497. ...
Mutations in the coding sequence of the ferritin light chain (FTL) gene cause a neurodegenerative disease known as neuroferritinopathy or hereditary ferritinopathy, which is characterized by the presence of intracellular inclusion bodies containing the mutant FTL polypeptide and by abnormal accumulation of iron in the brain. Here, we describe the x-ray crystallographic structure and report functional studies of ferritin homopolymers formed from the mutant FTL polypeptide p.Phe167SerfsX26, which has a C terminus that is altered in amino acid sequence and length. The structure was determined and refined to 2.85 A resolution and was very similar to the wild type between residues Ile-5 and Arg-154. However, instead of the E-helices normally present in wild type ferritin, the C-terminal sequences of all 24 mutant subunits showed substantial amounts of disorder, leading to multiple C-terminal polypeptide conformations and a large disruption of the normally tiny 4-fold axis pores. Functional studies ...
Long-lived lens proteins undergo little turnover but show a high degree of enzymatic and non-enzymatic posttranslational modification. These modifications start early in life and continue as the lens ages, resulting in the accumulation of modified proteins [11]. Changes in lens protein structure lead to formation of high molecular weight aggregates with decreased solubility, a factor that contributes to the increase in the light-scattering characteristic of older lenses [12]. Lens proteins can also be modified by partial or complete proteolytic degradation, which is particularly dramatic during the transformation of epithelial cells into fiber cells [13]. Furthermore, proteosomal and non-proteosomal degradation systems are present in lens fiber cells. The activity of both systems declines with age, but is still detectable in mature fiber cells [14]. Analysis of the distribution pattern and characteristics of ferritin chains in lens fiber cells revealed similar changes to those described for lens ...
Fig. 8. Accumulation of CD8+ T-lymphocytes in tumor regions with expression of cFTH1. A, IHC staining of FTH1, CD3, CD4 and CD8 in TNBC whole tissue sections (yellow arrows: CD4+ T-lymphocytes; red arrows: CD8+ T-lymphocytes); B, Box plots summarize the observation in (A). CD4+/CD8+ ratio was significantly increased in TNBC samples with high expression of cFTH1. Data are presented as the median ± interquartile range (Mann-Whitney U test, n = 15 per group); C, A proposed functional model of cFTH1 in the context of the antigen processing and presentation pathway: Ferritin complex captures intracellular Fe2+ ions (green dots) and converts them into Fe3+ ions (yellow dots). Accumulation of Fe3+ iron in tumor cells increases in response to inflammation, and IFN γ (red dots) can enhance the inflammatory response of tumor cells. Together, inflammatory signals can enhance processing of cytosolic antigens through the proteasome, heat shock proteins (HSP), and antigen peptide transporters (TAP), ...
Crichton R. R., Millar J. A., Cumming R. L. C., Bryce C. F. A., The organ-specificity of ferritin in human and horse liver and spleen, 10.1042/bj1310051 ...
Complete information for FTLP17 gene (Pseudogene), Ferritin Light Chain Pseudogene 17, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
SED021Mu, FTH1; FTHL6; PIG15; PLIF; Ferritin Heavy Chain; Apoferritin; Placenta Immunoregulatory Factor; Proliferation-Inducing Protein 15; Cell proliferation-inducing gene 15 protein | Products for research use only!
1DAT: X-ray structure of recombinant horse L-chain apoferritin at 2.0 angstrom resolution: Implications for stability and function.
Biochemistry CRP1.50|5.0mg/L Ferritin78.320 - 150ug/L Thyroid Function TSH1.050.27 - 4.20mIU/L T4 Total87.464.5 - 142.0nmol/L Free T415.5512 - 22pmol/L Free T34.623.1 - 6.8pmol/L Immunology Anti...
While trying to buy 500 shares of a preferred stock this morning, Principal Financial Group Inc. series B (NYSE:PFG-B), PreMarketInfos Dennis Dick encountered the algos heads on. As he notes It is such a challenge to trade any type of illiquid issue as the execution of orders is nearly impossible in this HFT world. Here is the sequence of events. Some serious issues are highlighted in these few minutes of activity: 1) Inability for market participants to access a quote; 2) Excessive quote pollution as HFT algorithms battle each other; 3) Market fragmentation can lead to inferior execution; and 4) HFT penny jumping can discourage market liquidity. The bottom line is that all of these issues discourage participants from trading illiquid securities - making these securities even more illiquid.
Read reviews, compare customer ratings, see screenshots and learn more about FTL: Faster Than Light. Download FTL: Faster Than Light and enjoy it on your Apple TV.
The tags customers have most frequently applied to FTL: Faster Than Light + Soundtrack have also been applied to these products ...
And so my FTL campaign, the flight of the starship Moggy, limps to the games penultimate sector. It seems impossible that were still alive at this point - let
Chord diagram. The backbone chain is represented by a circle. Chords (arcs) connect those residues that are in contact. Structure elements can be removed from the above chord diagram by clicking on their symbols. In case of proteins for which it is possible to identify the secondary structure, symbols are given in the Stride classification (e.g. AH stands for alpha-helix). {{ pdb }} {{ chain }} ...
Here I am again, THIS time I have a little more time on my hands. I was able to actually sit down, do some crafting AND make a card! WOO HOO!! YAY, me!! LOL This time, when I did the cleanandsimplestamping.blogspot.com layout for THIS week, I didnt really have a stamp set, color scheme or…
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Hereditary hyperferritinemia cataract syndrome is characterized by an excess buildup of ferritin in the blood and tissues which can lead to cataracts at an early age, often starting in infancy.
Hereditary hyperferritinemia cataract syndrome is characterized by an excess buildup of ferritin in the blood and tissues which can lead to cataracts at an early age, often starting in infancy.
The +51G,C mutation has already been described in 2 father-child pairs with moderate hyperferritinemia and clinically silent bilateral cataract.6,7 The first father-daughter pair (50 and 15 years old, respectively) were Canadians, like our proband. Both had serum ferritin levels below 1000 μg/L and only fine bilateral lenticular changes were observed by slit lamp examination.6 The second father-son pair (46 and 19 years old, respectively) was of Caucasian origin. They displayed serum ferritin levels of 1291 and 1251 μg/L, respectively. Slit-lamp and dilated funduscopic examinations revealed bilateral white breadcrumb-like nuclear and cortical lens opacity, whereas visual acuity was not affected.7 In our case, the proband displayed higher ferritin levels (roughly twice the levels observed in heterozygotes) but as for heterozygous affected patients, visual symptoms were mild and ophthalmological examination revealed bilateral cataract in the third decade only. However, it is noteworthy that ...
Ferritins (MW: ~ 450 kD) are polymeric proteins composed of 2 subunits a heavy chain and a light chain polypeptide, that reversibly bind and store iron in liver, spleen and bone marrow. The ferritin molecule consists of 24 self-assembling polypeptide subunits composed of the heavy and light chains. Ferritin light chain is the main intracellular iron storage protein. The proportion of heavy and light chain composing the ferritin molecule varies from tissue to tissue. This variation accounts for the differences in the rate of iron uptake and release in different tissues or organs. Recombinant Human Ferritin Light Chain is produced in E.coli as a single non-glycosylated polypeptide having a molecular weight of 19 kDa. Clinically, the monitoring of serum ferritin levels aides in the diagnosis and management of iron metabolic disorders. Serum levels increase in hepatic diseases, various malignancies, inflammation and late stage hemochromatosis. Ferritin levels are also indicative of the ero
Ferritin is a major iron storage protein and essential for iron homeostasis. It has a wide range of functions in the body including iron delivery, immunosuppression, angiogenesis, and cell proliferation. Ferritin is overexpressed in many cancer cells, but its precise role in cancer is unclear. In the present study, we examined the functional roles of ferritin in protecting the MCF-7 breast cancer cell line against treatment with the chemotherapeutic agent doxorubicin. The effects of ferritin (human liver ferritin) and doxorubicin on the human MCF-7 breast cancer cell line were evaluated using the cell viability assay. The impact of decreasing ferritin light chain (FTL) and ferritin heavy chain (FTH) expression on doxorubicin sensitivity was assessed using siRNA. Reactive oxygen species (ROS) was also measured using the fluorescence probe CM-H2DCFDA. The mechanism of modulated chemosensitivity was evaluated by western blot analysis. Ferritin treatment activated MCF-7 cell proliferation in a ...
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Cadmium atom in PDB 1ier: Cubic Crystal Structure of Native Horse Spleen Ferritin
When ferritin is reconstituted from Fe and apoferritin in vitro in the presence of Pi, the product obtained differs both from native ferritin and from ferritin reconstituted in the absence of Pi. When the latter is incubated with Pi the product resembles native ferritin with respect both to the pattern of Pi incorporated per molecule or per Fe atom and to the ease of release of this Pi relative to Fe release. It is concluded that much of the Pi of native ferritin is adsorbed on surfaces of ferritin iron-core crystallites. The results also suggest that Pi is not present at the intracellular site of Fe incorporation into ferritin, but is added after Fe. ...
Ferritin is the intracellular protein responsible for the sequestration, storage and release of iron. Ferritin can accumulate up to 4500 iron atoms as a ferrihydrite mineral in a protein shell and releases these iron atoms when there is an increase in the cells need for bioavailable iron. The ferritin protein shell consists of 24 protein subunits of two types, the H-subunit and the L-subunit. These ferritin subunits perform different functions in the mineralization process of iron. The ferritin protein shell can exist as various combinations of these two subunit types, giving rise to heteropolymers or isoferritins. Isoferritins are functionally distinct and characteristic populations of isoferritins are found depending on the type of cell, the proliferation status of the cell and the presence of disease. The synthesis of ferritin is regulated both transcriptionally and translationally. Translation of ferritin subunit mRNA is increased or decreased, depending on the labile iron pool and is ...
Goat anti human ferritin antibody recognizes Human Ferritin, a large globular protein found in the liver, intestines and spleen that funct
Ferritin- The ferritins are a class of iron storage proteins found widely distributed among the animal, plant and microbial kingdoms. These proteins consist of 24 subunits assembled into hollow spherical structure within which iron is stored as a hydrous ferric oxide mineral core. Our research focuses on understanding the redox and hydrolysis-mineralization mechanisms by which iron is acquired and released by ferritin. We seek to understand the structural attributes by which this unusual protein is capable of reversibly storing such large quantities of iron (4500 Fe/protein). A variety of spectroscopic, kinetic and thermochemical techniques and site-directed mutagenesis are employed in this research (see Methodologies and Major Instrumentation ...
2. As we discussed yesterday, ferritin is an iron storage protein. Basically, it functions as a giant ball that sequesters Fe3+ by polymerizing it with oxygen-rich anions (sulfate, phosphate, hydroxide). In the PDB, look at file 1AEW. If you download it directly into RasMol, you will see just one chain, but ferritin is made up of a bunch of identical chains. So, when you have pulled up 1AEW in the PDB, look to the left-hand margin. Under other resources go to the EBI MSD Macromolecule File Server, which will give you the quarternary structure version of 1AEW. Save it on the desktop, change the filename to .pdb and open it in RasMol.. ...
1. Measurements of T-lymphocyte surface ferritin using flow cytometry show that phytohaemagglutinin (PHA) stimulation causes a marked increase in the number of cells bearing spleen-type (S) and heart-type (H) ferritin on their membrane, whereas no such change occurs in non-stimulated cells. This coincides with increases in interleukin-2 receptors, transferrin receptors and HLA-DR antigen.. 2. There is an increase in the intracellular concentration of both S- and H-ferritin in lymphocytes after PHA stimulation: H-ferritin increases five- to seven-fold, but S-ferritin only two- to three-fold. The maximum H/S ratio is about 15/1. However, these increases also occur in cells cultured in the absence of PHA.. 3. Small amounts of both S- and H-ferritin are released into the medium, especially from stimulated cells, but the H/S ratios are lower than intracellular ratios.. 4. The present findings suggest that lymphocyte stimulation followed by ferritin synthesis is accompanied by an increase in the ...
Several novel findings on Drosophila ferritin are described in this work. We show that the absence of either Fer1HCH or Fer2LCH results in embryonic lethality and that modified Fer1HCH subunits (mutant in the ferroxidase center or GFP tagged) cannot substitute for lack of Fer1HCH. However, if the same modified subunits are expressed in the presence of wild-type subunits, they can be integrated into ferritin holomers without inducing dominant-negative effects. Analysis of heterozygous loss-of-function ferritin fly mutants or flies overexpressing ferritin subunits revealed that a constant ratio of Fer1HCH and Fer2LCH is maintained, independent of their internal transcriptional expression levels. The structural cooperation of the two subunits that is secured via disulfide bonds (Hamburger et al. 2005) likely explains these observations. A post-transcriptional mechanism, possibly involving the degradation of subunits that are present in excess, ensures the presence of equal amounts of the two ...
Discussion:. Energetics in animals is based on the availability of reducing equivalents, specifically hydrogen (H+) which is replenished byconsumed as carbohydrates and fats, that react with oxygen to generate water and hydrogen via mitochondrial oxidative phosphorylation.. The older evolutionary pathways makes far less energy than complex animals need for chronic living. Glucose is cleaved into pyruvate via glycolysis within the cytosol, reducing cytosolic NAD+ to NADH (reduced nicotinamide adenine nucleotide). The pyruvate then enters the mitochondrion via pyruvate dehydrogenase (PDH), resulting in mitochondrial acetyl-CoA (main electron provider for ECT), NADH + H+, and CO2. The acetyl-CoA then enters the tricarboxylic acid (TCA) cycle, which strips the hydrogens from the organic acids, thereby generating NADH + H+.. The new pathways (beta oxidation) are required for complex life because they provide a lot more electrons for tunneling. The more electrons the more life you live.. Fatty acids ...
Mouse monoclonal antibody raised against a full length native FTL. Native purified human FTL. (H00002512-M04) - Products - Abnova
Mouse monoclonal antibody raised against a full length native FTL. Native purified human FTL. (H00002512-M09) - Products - Abnova
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Human ferritins have been extensively studied to be used as nanocarriers for diverse applications and could represent a convenient alternative for targeted delivery of anticancer drugs and imaging agents. However, the most relevant limitation to their applications is the need for highly acidic experimental c
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Load balancers are the point of entrance to the datacenter. They are on the critical path to access anything and everything. That give them some interesting characteristics. First, they are the most important thing to monitor in an infrastructure. Second, they are in a unique position to give insights not only about themselves but also…
Load balancers are the point of entrance to the datacenter. They are on the critical path to access anything and everything. That give them some interesting characteristics. First, they are the most important thing to monitor in an infrastructure. Second, they are in a unique position to give insights not only about themselves but also…
Using bond futures data, we test whether high-frequency trading (HFT) is engaging in back running, a trading strategy that can create costs for financial institutions. We reject the hypothesis of back running and find instead that HFT mildly improves trading costs for institutions. ...
Gentaur molecular products has all kinds of products like :search , BioBasic \ Ferritin \ FB0457 for more molecular products just contact us
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TY - JOUR. T1 - H and L ferritins in myocardium in iron overload. AU - Arbustini, Eloisa. AU - Grasso, Maurizia. AU - Rindi, Guido. AU - Arosio, Paolo. AU - Gavazzi, Antonello. AU - Diegoli, Marta. AU - Bramerio, Manuela. AU - Levi, Sonia. AU - Barosi, Giovanni. PY - 1991/11/1. Y1 - 1991/11/1. N2 - Ferritin is an iron-containing protein composed of 2 subunits (H and L) with largely different primary structures and immunochemical properties. 1 The normal L-subunit-rich, basic isoferritin is prevalent in the liver and spleen, whereas the H-subunit-rich, acidic isoferritin predominates in the heart, pancreas and kidneys.2 A variation in heart isoferritin was reported in iron-overloaded patients,2 and the absence of the more acidic isoferritin was hypothesized to be specific for hereditary hemochromatosis.3 These observations prompted us to perform immunohistochemical investigations on H and L ferritins in endomyocardial biopsy samples of patients with primary or secondary iron overload, using ...
Reactions and interactions of iron and oxygen can be both beneficial and detrimental to cells and tissues. Iron is mainly found in our blood where it functions as a mediator in the transport of oxygen to the cells and is further vital for the cellular respiration reducing the oxygen to water. The flexible redox state of iron makes it ideal to contribute in single electron transfers, but may also catalyze reactions with oxygen resulting in cell damaging reactive oxygen species (ROS). Normally the cells are protected against iron toxicity by controlling iron uptake and storage. When the intracellular demand for iron increases; the iron uptake is promoted by increasing the expression of transferrin receptor (TfR) and by decreasing the expression of the iron storage protein ferritin. Ferritin has a central role in the cellular iron detoxification by keeping it in a non reactive but still bioavailable form. However, in neurodegenerative diseases like in Alzheimers and Parkinsons disease the iron ...
TY - JOUR. T1 - Do oligodendrocytes mediate iron regulation in the human brain?. AU - Gerber, Megan R.. AU - Connor, James R.. PY - 1989/7. Y1 - 1989/7. N2 - We used immunohistochemical studies to demonstrate that transferrin (the iron mobilization protein) and ferritin (the iron storage protein) are specifically localized in oligodendrocytes in gray and white matter of the human central nervous system. In addition, iron is also localized predominantly in oligodendrocytes. Oligodendrocytes have been well established as the cells responsible for myelin production in the central nervous system. The results of this study suggest that oligodendrocytes (or a subpopulation of oligodendrocytes) might have the additional function of mediating iron mobilization and storage in the central nervous system.. AB - We used immunohistochemical studies to demonstrate that transferrin (the iron mobilization protein) and ferritin (the iron storage protein) are specifically localized in oligodendrocytes in gray and ...
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Fluothane (halothane) is a small molecule pharmaceutical. Halothane was first approved as Fluothane on 1982-01-01. It is used to treat status asthmaticus in the USA. The pharmaceutical is active against potassium channel subfamily K member 9 and potassium channel subfamily K member 10. In addition, it is known to target potassium channel subfamily K member 2, potassium channel subfamily K member 12, potassium channel subfamily K member 3, potassium channel subfamily K member 5, potassium channel subfamily K member 13, potassium voltage-gated channel subfamily B member 1, G protein-activated inward rectifier potassium channel 2, and ferritin light chain.
Recombinant ferritin is an excellent template for the synthesis of magnetic nanoparticles. This paper describes carefully performed experiments both to identify ironoxides within nanoparticles and to measure the number of iron atoms in the cores of recombinant human H-chain ferritin (HFn), based on spectroscopy techniques. Using electron energy-loss spectroscopy (EELS) analysis, magnetite (Fe3O4) has been unequivocally identified as the ironoxide formed within HFn cores under special preparation conditions. Atom counting analysis by EELS and high-angle annular dark-field imaging further allowed the correlation of the particle sizes to the real Fe atom numbers in a quantitative manner. These results help clarify some structural confusion between magnetite and maghemite (γ-Fe2O3), and also provide standard data for the number of Fe atoms within Fe3O4 particles of a given size, whose use is not limited to cases of magnetite synthesized in the cores of recombinant human ferritin.
Iron is required for normal cell growth and proliferation. However, excess iron is potentially harmful, as it can catalyse the formation of toxic reactive oxygen species (ROS) via Fenton chemistry. For this reason, cells have evolved highly regulated mechanisms for controlling intracellular iron levels. Chief among these is the sequestration of iron in ferritin. Ferritin is a 24 subunit protein composed of two subunit types, termed H and L. The ferritin H subunit has a potent ferroxidase activity that catalyses the oxidation of ferrous iron, whereas ferritin L plays a role in iron nucleation and protein stability. In the present study we report that increased synthesis of both subunits of ferritin occurs in HeLa cells exposed to oxidative stress. An increase in the activity of iron responsive element binding proteins in response to oxidative stress was also observed. However, this activation was transient, allowing ferritin protein induction to subsequently proceed. To assess whether ferritin ...
Ferritins are ubiquitous and can be found in practically all organisms that utilize Fe. They are composed of 24 subunits forming a hollow sphere with an inner cavity of ~80 A in diameter. The main function of ferritin is to oxidize the cytotoxic Fe(2+) ions and store the oxidized Fe in the inner cavity. It has been established that the initial step of rapid oxidation of Fe(2+) (ferroxidation) by H-type ferritins, found in vertebrates, occurs at a diiron binding center, termed the ferroxidase center. In bacterial ferritins, however, X-ray crystallographic evidence and amino acid sequence analysis revealed a trinuclear Fe binding center comprising a binuclear Fe binding center (sites A and B), homologous to the ferroxidase center of H-type ferritin, and an adjacent mononuclear Fe binding site (site C). In an effort to obtain further evidence supporting the presence of a trinuclear Fe binding center in bacterial ferritins and to gain information on the states of the iron bound to the trinuclear ...
Ferritin, a major iron storage protein, is essential to iron homeostasis and is involved in a wide range of physiologic and pathologic processes. In clinical medicine, ferritin is predominantly utilized as a serum marker of total body iron stores. In cases of iron deficiency and overload, serum ferr …
Looking for online definition of H-chain in the Medical Dictionary? H-chain explanation free. What is H-chain? Meaning of H-chain medical term. What does H-chain mean?
Over time, some gene copies mutate to lose their function entirely. Such so-called pseudogenes may arise through accumulation of mutations that A gene family is descended from a common ancestral gene. prevent translation of the gene, such as an insertion or deletion that stops translation at the beginning of the gene sequence. Pseudogenes also arise from mutation in a genes promoter region. The promoter is the site at the beginning of the gene that attracts the enzyme called RNA polymerase. Without a functional promoter, the gene cannot be transcribed effectively, and so cannot lead to protein production.. Retroposition is a very common source of pseudogenes. Pseudogenes have been discovered because their sequences are similar to functional genes. In humans, pseudogenes are known to exist for topoisomerase (a gene that cuts DNA to prevent twisting), ferritin (an iron storage protein), two different forms of actin, and many other genes.. ...
Iron is an essential nutrient for the human body. Too little can compromise many important functions and lead to various diseases. Similarly, too much can cause severe damage to organs and tissues, leading to disease and early death.. A normal diet provides between 10-20 mg of iron daily, of which the body absorbs only 1.0 to 1.5 mg through the intestinal tract. The rest of the iron not absorbed during digestion is excreted in the stool. Iron metabolism is a complex process. The body responds to increased or decreased demand by adjusting the amount it absorbs. Once iron is absorbed into the body, it is difficult to eliminate, and can only be lost in small amounts through blood loss, sweat, urine and the sloughing of skin and gut cells. Therefore, our body maintains a strict regulation of iron absorption.. Normally, the body has about 4,000 mg of iron, of which about 3,000 mg is contained in hemoglobin in the red blood cells. About 500 mg is bound to the storage protein ferritin, and 300 mg is ...
Homologs from the ferric uptake regulator Hair as well as the iron storage space proteins ferritin play a central function in maintaining iron homeostasis in bacterias. out by various other metals. The gram-negative microaerophilic bacterial pathogen colonizes the mucus level of the individual tummy (12, 20). Its hostile ecological specific niche market provides necessitated the […]. ...
Nobody has yet worked out how to make a good nanobattery, so nanoscale devices are typically driven by power sources many times their own size. A key problem is how to assemble a battery on such a tiny scale and a number of research groups have been working on exploiting the way biological molecules self-assemble for this task.. NASA says one promising avenue is exploiting the ability of the protein ferritin to carry either a positive or negative charge. Ferritin also self assembles relatively easily into a uniform nanolayer. So, the agency says, it is straightforward to create a layer of ferritin and then cover it with another layer of the opposite charge. The result is a capacitor just a few nanometres thick that can store charge between its layers - in other words a battery. Adding more layers of alternately charged ferritin increases the capacitance of this bio-nanobattery. NASA reckons its battery is not only stable and robust but can be produced easily and quickly too.. Justin ...
Okay, Im new and feeling a little overwhelmed. I was just told today that my hematocrit, hemoglobin, and ferritin are low. Also Low D, elevated bad cholesterol and tested positive for thyroid antibodies. I was excited to have answers and be able to start feeling better and now everything in here is completely contradictory to the intended plan. I actually got a magnesium shot last week when they drew my blood for the tests because theyre big believers in everyone needing magnesium and I didnt feel it made me any better. Someone give me some cliff notes info. My brain is foggy and Im not sure what I should be doing. ...
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Definition : Immunoassay reagents intended to perform qualitative and/or quantitative analyses on a body fluid sample (typically serum) to determine the level of ferritin, an iron-apoferritin complex, one of the main forms of iron storage in the body. Ferritin is present in the blood in very low concentrations, but it usually reflects the variation in the total iron body stores. Decreased levels of ferritin are found very early in the development of iron deficiency in otherwise healthy patients; increased levels of ferritin are associated with chronic infections, rheumatoid arthritis, renal diseases, a variety of malignancies , viral hepatitis, and other diseases.. Entry Terms : Ferritin Determination Reagents , Reagents, Ferritin , Reagents, Immunoassay, Anemia Test, Ferritin. UMDC code : 17342 ...
After installation, FTL may fail to run due to a Text file busy error (characterised in Steam by your portrait border going green then blue again). The easiest way to mend this is to just reboot your system. Upon logging back in FTL should run. The Steam overlay in FTL does not function as it is not a 3D accelerated game. Because of this the desktop notifications will be visible. If playing in fullscreen, therefore, these notifications in some systems may steal focus and revert you back to windowed mode with no way of going back to fullscreen without relaunching. The binaries for FTL on Steam have no DRM and it is possible to run the game without Steam running, so in some cases that may be optimum - just ensure that you launch FTL via the launcher script in ...
Iron is a metal that is essential for all living things as it is heavily involved in cell redox reactions and the electron transport chain (a major part of aerobic respiration). However it is strongly reactive with oxygen - outside of living organisms this leads to rust, inside it can lead to the production of dangerous reactive oxygen species - and therefore needs to be controlled and contained within the cell. In order to provide this control, all living organisms (apart from yeast, weirdly enough) use a protein called ferritin. Multiple subunits of ferritin proteins (usually 24, although occasionally only 12) form an outer shell, with a central cavity that can contain around 2000-400 individual ferric ions (iron ions) keeping them safely out of harms way ...
Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. Modulates the RNA-binding activity of ACO1 ...
First, let me say what you read here is going to be wrong in several ways. HFT covers such a wide path of trading that different parties participate or are impacted in different ways. I wanted to put this out there as a starting point . Hopefully the comments will help further educate us all. 1. Electronic trading is part of HFT, but not all electronic trading is high frequency trading.. Trading equities and other financial instruments has been around for a long time. it is Electronic Trading that has lead to far smaller spreads and lower actual trading costs from your broker. Very often HFT companies take credit for reducing spreads. They did not. Electronic trading did.. We all trade electronically now. Its no big deal. 2. Speed is not a problem. People like to look at the speed of trading as the problem. It is not. We have had a need for speed since the first stock quotes were communicated cross country via telegraph. The search for speed has been never ending. While i dont think co location ...
Bad puns and video games since 1999.. This site © 2020 Gamer Network. All Rights Reserved. No part of this site or its content may be reproduced without the permission of the copyright holder.. ...
The FTL then decides if the find is anything important. For instance, a 20 year old soda bottle with moss inside it is not a clue, nor is a deer footprint. The FTL tells the navigator to plot the exact location of the team, (which should be easy if theyve been keeping track all along) and asks the radio operator to contact base. Everybody else on the team stays put, so you know where to begin if base tells you to continue on the task. Nows a good time to have a snack or drink some water ...
In seltenen Fällen können Mutationen im FTH1-Gen, das für die schwere Kette von Ferritin kodiert, zu Hämochromatose ähnlichen Erkrankungen führen, die mit einer Hyperferritinämie einhergehen.
Ferritin is a protein in the bodys cells that is responsible for the storage of iron, according to Healthline. Cells irelease ferritin when they receive a signal that the body needs more red blood...
Ferritin is a protein found inside the body that aids in storing iron in the body. A blood test is used to measure the amount of ferritin in the body,...
Addison JM, Fitton JE, Lewis WG, May K, Harrison PM (Nov 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. doi:10.1038/288298a0. PMID ...
Apoferritin binds to free ferrous iron and stores it in the ferric state. As ferritin accumulates within cells of the ... Ferritin that is not combined with iron is called apoferritin. Ferritin genes are highly conserved between species. All ... "Size-Selective Olefin Hydrogenation by a Pd Nanocluster Provided in an Apo-Ferritin Cage". Angewandte Chemie. 43 (19): 2527-30 ...
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 ...
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 ...
This is an alternative to the apoferritin cage technique currently used to synthesize uniform CdSe nanoparticles.[88] Such ... "Bio-template Synthesis of Uniform CdSe Nanoparticles Using Cage-shaped Protein, Apoferritin." Chemistry Letters (2004). Volume ...
... apoferritin MeSH D12.776.556.579.374.187 - hemerythrin MeSH D12.776.556.579.374.281 - inositol oxygenase MeSH D12.776.556.579. ...
... 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 ...
X-ray structure of recombinant horse L-chain apoferritin at 2.0 angstrom resolution: Implications for stability and function. ...
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 ... 1.33 A structure of human apoferritin obtained from Titan Mono- BCOR microscope. *DOI: 10.2210/pdb7A6B/pdb ...
Herein, we evaluated the long-term stability of the naturally found protein nanocarrier apoferritin (Apo) with encapsulated ... Keywords: anticancer therapy, doxorubicin-loaded apoferritin, encapsulation, long-term stability, protein nanocarriers ... Apoferritin as an ubiquitous nanocarrier with excellent shelf life Simona Dostalova,1,2 Katerina Vasickova,1 David Hynek,1,2 ... Apoferritin modified magnetic particles as doxorubicin carriers for anticancer drug delivery. Int J Mol Sci. 2013;14(7):13391- ...
The spherical structure of apoferritin remained intact after loading Pt particles in its cavit ... were bio-mimetically prepared by an in situreduction method in the unique 8 nm spherical cage of apoferritin. The average size ... apoferritin. . The average size of AFt-Pt was 4.3 ± 0.9 nm. The spherical structure of apoferritin. remained intact after ... Apoferritin. -camouflaged Pt nanoparticles. : surface effects on cellular uptake and cytotoxicity Xiangyou Liu,abe Wei Wei,c ...
Page contains details about apoferritin encapsulated catalytic nanoparticles . It has composition images, properties, ...
Iron(III) complexation of Desferrioxamine B encapsulated in apoferritin Dominguez-Vera, Jose M. Journal of Inorganic ... Apoferritin as a nanoreactor for preparing metallic nanoparticles Galvez, Natividad; Fernandez, Belen; Valero, Elsa; Sanchez, ... Apoferritin-encapsulated Ni and Co superparamagnetic nanoparticles Galvez, Natividad; Sanchez, Purificacion; Dominguez-Vera, ... Permanentmagnetism in apoferritin-encapsulated Pd nanoparticles. Clemente-Leon, Miguel; Coronado, Eugenio; Soriano-Portillo, ...
The Amino-acid-sequence of Human Spleen Apoferritin. In: FEBS Letters, Vol. 150, no. 1, p. 43-48 (1982). ... The Amino-acid-sequence of Human Spleen Apoferritin Primary tabs. *Détail(active tab) ... Heusterspreute Michel, Crichton Robert R., Amino acid sequence of horse spleen apoferritin, 10.1016/0014-5793(81)80193-7 ... Fish Wayne W., Bjork Ingemar, Native and subunit molecular weights of apoferritin, 10.1021/bi00791a007 ...
Expression of CCR2/CCR5 on T cells in apoferritin-induced glomerulonephritis. A detailed knowledge of chemokine receptor ... Thioglycollate-induced peritonitis and apoferritin-induced glomerulonephritis. For the induction of peritonitis in BALB/c mice ... the apoferritin-induced glomerulonephritis. Previously we have shown by RT-PCR and in situ hybridization that both receptors ... injections of 4 mg of horse spleen apoferritin (Aldrich Chemical, Steinheim, Germany) in 80 μl of 0.1 M of sodium chloride as ...
Apoferritin. Bacteria. Fibrinogen. Microsomes. Protein Macromolecules. 6 Support Films. Introduction. Plastic Support Films. ...
Polymerization of phenylacetylene by rhodium complexes within a discrete space of apo-ferritin. In: Journal of the American ... Polymerization of phenylacetylene by rhodium complexes within a discrete space of apo-ferritin. Journal of the American ... Polymerization of phenylacetylene by rhodium complexes within a discrete space of apo-ferritin. / Abe, Satoshi; Hirata, Kunio; ... N2 - Polymerization reactions of phenylacetylene derivatives are promoted by rhodium complexes within the discrete space of apo ...
L apoferritin. *MGC71996. *NBIA3. Additional Information & Resources. Tests Listed in the Genetic Testing Registry. *Tests of ...
Examples are the pH-dependent dissociation and hydrolysis of Apoferritin (Jaenicke 1987), human prion protein (PrP) aggregation ...
Apoferritins * Iron Grant support * R37 DK42421/DK/NIDDK NIH HHS/United States ...
Mutant R59M Recombinant Horse Spleen Apoferritin Cocrystallized With Haemin in Acidic Conditions ... The binding sites of Cadmium atom in the structure of Mutant R59M Recombinant Horse Spleen Apoferritin Cocrystallized With ... Cadmium in the structure of Mutant R59M Recombinant Horse Spleen Apoferritin Cocrystallized With Haemin in Acidic Conditions ( ...
Apoferritin. F432. 171. SAD, 8 Cd. 2.0. -m20 -h8 -s0.61 -a3 -q -t13 -m20 -h8 -s0.61 -a3 -q14 -t18 ... Three examples of tracing evolution: (a, b) apoferritin, (c, d) autophagy-related protein 38 and (e, f) titin A168-A169. (a), ( ... Apoferritin†. -s0.61 -h8. F432. 2.00. 29.0. 4. 77/7. 47.6. 91.2. 29.8. ... SAD data for apoferritin and titin protein A168-A169 are from Mueller-Dieckmann et al. (2007. ) and those for fibronectin are ...
FPN expression was induced after apoferritin administration at the mRNA and protein levels (Figure 6, C and D). As apoferritin ... C) FtHPT+/+ proximal tubular epithelial cells were treated in vitro with apoferritin for 8 hours and analyzed for FPN ... Apoferritin and FtH treatment. Primary proximal tubular cells were isolated from wild-type mice as described previously (59) ... To clarify whether FPN expression is mediated by iron and/or ferritin, we used apoferritin and recombinant FtH and FtH-M, the ...
Process of Accumulation of Metal Ions on the Interior Surface of apo-Ferritin: Crystal Structures of a Series of apo-Ferritins ... Process of Accumulation of Metal Ions on the Interior Surface of apo-Ferritin: Crystal Structures of a Series of apo-Ferritins ... Process of Accumulation of Metal Ions on the Interior Surface of apo-Ferritin: Crystal Structures of a Series of apo-Ferritins ... ions demonstrated by a series of X-ray crystal structural analyses of apo-ferritin (apo-Fr), an iron storage protein, ...
IgM Pentamer (900 Kda), 2. Thyroglobulin (667 KDa), 3. Apoferritin (443KDa), 4. β-Amylase (200 Kda), 5. IgG (150 KDa), 6. BSA ( ... USP resolution values (half-height measurement) calculated for the separation between the apoferritin monomer (MW=443 KDa) and ... IgM Pentamer (900 Kda), 2. Thyroglobulin (667 KDa), 3. Apoferritin (443KDa), 4. β-Amylase (200 KDa), 5. IgG (150 KDa). Sample ... for the separation of apoferritin (443 KDa). Sample injection volumes and flow rate were normalized for column geometry. UV ...
Horse spleen apoferritin. LN. Lupus nephritis. MC. Mesangial cell. PBS. Phosphate-buffered saline ...
Deery E, Schroeder S, Lawrence AD, Taylor SL, Seyedarabi A, Waterman J, Wilson KS, Brown D, Geeves MA, Howard MJ, Pickersgill RW, Warren ...
Apoferritin. *Cell proliferation inducing gene 15 protein. *Cell proliferation-inducing gene 15 protein ...
2013) RGD-modified apoferritin nanoparticles for efficient drug delivery to tumors. ACS Nano 7(6):4830-4837. ... 2004) Iron(III) complexation of Desferrioxamine B encapsulated in apoferritin. J Inorg Biochem 98(3):469-472. ... 2009) Characterization and cellular uptake of platinum anticancer drugs encapsulated in apoferritin. J Inorg Biochem 103(7): ... 2011) pH-dependent structures of ferritin and apoferritin in solution: Disassembly and reassembly. Biomacromolecules 12(5):1629 ...
Iron incorporation into apoferritin. The role of apoferritin as a ferroxidase. J Biol Chem (1986) 261(28):13182-5. ...
Beyond the detergent effect: a binding site for sodium do-decyl sulfate (SDS) in mammalian apoferritin. ... binds specifically to a pre-formed internal cavity in horse-spleen apoferritin. ...
Apoferritin antibody. *Cell proliferation inducing gene 15 protein antibody. *Cell proliferation-inducing gene 15 protein ...
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Processing Apoferritin with the Appion Pipeline. Scott M. Stagg, Joshua H. Mendez. Journal of Structural Biology, Volume 204, ...
Apoferritin (the protein) + iron. Ferritin increased in . . . any condition that leads to increased protein: hepatic necrosis; ...
ApoferritinsIBA 12/2011. 1. ProteomeIBA 12/2011. 1. Serine (L-Serine)FDA Link 08/2011. ...
Discovery of Novel General Anesthetics Using Apoferritin as a Surrogate System.. Rai G, Bu W, Lea WA, Liang D, Weiser B, Setola ...

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