• Sre1p specifically bound DNA containing the 5'-(G/A)ATC(T/A)GATAA-3' sequence, and that binding was both iron- and zinc-dependent. (nih.gov)
  • Reliable and robust methods for determining iron, zinc and copper status in the general population are needed. (europa.eu)
  • This study will investigate the isotopic fractionation of iron, copper and zinc on binding with proteins in simple to complex biological systems, and how this relates to metal cell metabolism, with the key aim of establishing a robust reference frame for future investigations of isotope biochemistry. (europa.eu)
  • The toxic effects of lead result from its interference with the physiologic actions of calcium, zinc, and iron, through the inhibition of certain enzymes, and through binding to ion channels and regulatory proteins. (cdc.gov)
  • Absence of a binding ligand needed to transport zinc may further contribute to zinc malabsorption. (medscape.com)
  • The etiopathogenesis of the zinc deficiency occurs as a result of loss-of-function mutations of the zinc-ligand binding protein ZIP4 encoded by the SLC39A4 ( solute carrier 39A) gene located on band 8q24.3. (medscape.com)
  • ZIP4 is a member of the Zrt-/Irt-like protein (ZIP) family, and it is a histidine-rich transmembrane protein that is specifically expressed on the apical side of enterocytes in the small intestine, as well as in the kidney, and is responsible for zinc absorption. (medscape.com)
  • An example of this is in hemoglobin, where the porphyrin works together with a histidine side chain and a bound O2 molecule, forming an octahedral complex. (wikipedia.org)
  • Hemoglobin is an oxygen-transport protein found in virtually all vertebrates. (wikipedia.org)
  • Hemoglobin has a binding affinity for carbon monoxide that is 250 times greater than for oxygen. (wikipedia.org)
  • In adults, hemoglobin normally contains two subunits of beta-globin and two subunits of another protein called alpha-globin. (medlineplus.gov)
  • For hemoglobin to bind to oxygen, the iron within the heme molecule needs to be in a form called ferrous iron (Fe 2+ ). (medlineplus.gov)
  • Hemoglobin that contains ferric iron is known as methemoglobin. (medlineplus.gov)
  • Carbon monoxide binds to hemoglobin, which has a 210-fold greater affinity for carbon monoxide than for oxygen. (medscape.com)
  • [ 7 ] This binding results in a left-shift of the oxygen-hemoglobin dissociation curve, leading to tissue hypoxia. (medscape.com)
  • Hemoglobin is a protein found in red blood cells that transports oxygen from the lungs to your whole body. (superkidsnutrition.com)
  • During the growing years both males and females require iron to produce hemoglobin for the production of red blood cells. (curezone.com)
  • Heme proteins like hemoglobin (Hb) and myoglobin (Mb) contain redox-active transition metal iron that makes them susceptible to causing oxidative damage. (scialert.net)
  • Most of the body's iron (about 60%) is contained in hemoglobin, which is the essential oxygen carrying protein of the blood. (irondisorders.org)
  • The body requires iron to make hemoglobin for blood and myoglobin for muscles. (irondisorders.org)
  • The body uses iron to make important compounds, such as hemoglobin and myoglobin. (medicalnewstoday.com)
  • Beta-globin is a component (subunit) of a larger protein called hemoglobin, which is located inside red blood cells. (medlineplus.gov)
  • In adults, hemoglobin consists of four protein subunits: usually two subunits of beta-globin and two subunits of a protein called alpha-globin, which is produced from another gene called HBA . (medlineplus.gov)
  • Hemoglobin that contains ferric iron is known as methemoglobin and is unable to efficiently deliver oxygen to the body's tissues. (medlineplus.gov)
  • The variant that causes hemoglobin S changes a single protein building block (amino acid) in beta-globin. (medlineplus.gov)
  • Finally, iron is necessary to form myoglobin-a type of protein that carries and stores oxygen in the muscle tissue. (superkidsnutrition.com)
  • Another 30% is stored in ferritin, a protein found throughout the body (although this percentage can be significantly higher or lower in cases of iron overload or deficiency), and a few percent in myoglobin, a protein specifically utilized by muscle cells. (irondisorders.org)
  • Transferrin can bind two Fe(III) ions, along with an anion (usually carbonate). (wikipedia.org)
  • Besides shielding bacterial DNA through binding and condensation, Dps proteins protect the cell from reactive oxygen species by oxidizing and storing ferrous ions within their cavity, using either hydrogen peroxide or molecular oxygen as the co-substrate, thus reducing the toxic effects of Fenton reactions. (unl.pt)
  • Results obtained using electron paramagnetic resonance (EPR), Mössbauer and UV/Visible spectroscopies revealed that Cu 2+ ions bind to specific binding sites in Dps, exerting a rate-enhancing effect on the ferroxidation reaction in the presence of molecular oxygen and directly oxidizing ferrous ions when no other co-substrate is present, in a yet uncharacterized redox reaction. (unl.pt)
  • Additionally, there are a few other soluble components such as ions, proteins, and trace cells. (medscape.com)
  • Iron-binding proteins are carrier proteins and metalloproteins that are important in iron metabolism and the immune response. (wikipedia.org)
  • Research on Fe-S cluster biosynthesis in the Johnson group currently involves investigating the molecular mechanisms of Fe-S cluster assembly on scaffold proteins and the subsequent intact cluster transfer to acceptor or carrier proteins. (uga.edu)
  • Some of the iron will then bind to other molecules not have transferrin's ability to protect its host from iron catalyzed lipid peroxidation and the formation of reactive oxygen species. (irondisorders.org)
  • Dps proteins (DNA-binding proteins from starved cells) are multifunctional stress defense proteins from the Ferritin family expressed in Prokarya during starvation and/or acute oxidative stress. (unl.pt)
  • Ferritin is a protein in the body that binds to iron. (anylabtestnow.com)
  • The level of ferritin correlates with the total amount of iron stored in the body. (anylabtestnow.com)
  • Ferritin is low in those with iron deficiency anemia and high when levels of iron are raised. (anylabtestnow.com)
  • When body iron stores increase above these relatively normal ratios, proportionally greater amounts of iron are stored in non-blood tissue in ferritin molecules or a complex called hemosiderin. (irondisorders.org)
  • Very low or very high ferritin in combination with low or high TS % can help a physician confirm a diagnosis of either iron deficiency or iron overload. (irondisorders.org)
  • Ferritin is a protein synthesized by the body that is mainly utilized to store iron for future use. (irondisorders.org)
  • Iron in excess of daily needs is stored in ferritin molecules, which hold up to 4,500 iron atoms each. (irondisorders.org)
  • Ferritin is an iron-containing protein in the blood. (medicalnewstoday.com)
  • Levels of ferritin can help doctors understand how much iron is in the body's stores. (medicalnewstoday.com)
  • Low ferritin levels indicate low iron stores and iron deficiency. (medicalnewstoday.com)
  • Combined measurement of ferritin, soluble transferrin receptor, retinol binding protein, and C-reactive protein by an inexpensive, sensitive, and simple sandwich enzyme-linked immunosorbent assay technique. (who.int)
  • Full blood count, serum ferritin, soluble transferring receptor, C-reactive protein, serum iron and total iron binding capacity were measured in the patients and healthy controls. (bvsalud.org)
  • Oxygen binding is fully cooperative for each of the subunits because as the first oxygen binds to one of the four heme groups, the protein undergoes a drastic conformational change that sharply increases the oxygen affinity of the other three subunits. (wikipedia.org)
  • The essential ATP-binding cassette protein ABCE1 splits 80S ribosomes into 60S and 40S subunits after canonical termination or quality-control-based mRNA surveillance processes. (nature.com)
  • If the membrane-anchor is missing or defective, Fp and Ip subunits accumulate as soluble proteins in the cytoplasm. (lu.se)
  • Typically, OMVs are dominated by outer membrane proteins, while the cytoplasmic membrane proteins and cytoplasmic proteins are the primary contents of MVs. (nature.com)
  • Autophagy is a process of engulfing one's own cytoplasmic proteins or organelles and coating them into vesicles, fusing with lysosomes to form autophagic lysosomes, and degrading the contents it encapsulates. (hindawi.com)
  • The hallmark of autophagy is the formation of autophagosomes, where lysosomes wrap cytoplasmic proteins or organelles and achieve self-renewal [ 4 ]. (hindawi.com)
  • Four nitrogen atoms in the porphyrin ring act as a ligand for the iron in the center. (wikipedia.org)
  • Li C, Sato K, Monari S, Salard I, Sola M, Banfield MJ, Dennison C. Metal-Binding Loop Length Is a Determinant of the pK(a) of a Histidine Ligand at a Type 1 Copper Site . (ncl.ac.uk)
  • The tight energy controls in biological systems mean that the isotope effect is seen in different metal-protein environments, depending on the ligand coordination and, if relevant, the oxidation state of the metal. (europa.eu)
  • Lactoferrin is a member of the transferrin family and is the predominant protein found in mammal exocrine secretions, such as tears, milk, and saliva. (wikipedia.org)
  • Washington, May 1 (ANI): Researchers have shed light on the several health benefits associated with lactoferrin, an important iron-binding protein. (newstrackindia.com)
  • Lactoferrin, a protein found in whey proteins, helps in binding iron, reducing the formation of free-radicals and thereby preventing cell damage and reducing the risk of cancer. (nutraingredients.com)
  • The results of recently conducted clinical trials suggest that lactoferrin, an iron-binding protein that is abundant in mammalian colostrum and milk, may be an effective agent in preventing sepsis in newborns. (springer.com)
  • However, despite numerous basic studies on lactoferrin, very little is known about how metal saturation of this protein affects a host's health. (springer.com)
  • Therefore, the main objective of this study was to elucidate how iron-depleted, iron-saturated, and manganese-saturated forms of lactoferrin regulate intestinal barrier function via interactions with epithelial cells and macrophages. (springer.com)
  • There was also no change in the production of tight junction proteins regardless of lactoferrin metal saturation status. (springer.com)
  • Lactoferrin that was not bound to its cognate receptor was able to bind and neutralize lipopolysaccharide. (springer.com)
  • The N-terminal part of lactoferrin possesses a serine protease which functions to inactivate the TYPE III SECRETION SYSTEM used by bacteria to export virulence proteins for host cell invasion. (bvsalud.org)
  • In response to excess iron, H. capsulatum represses transcription of genes involved in iron uptake. (nih.gov)
  • We report here that SRE1, a gene encoding a GATA-type protein, bound to promoter sequences of genes involved in siderophore biosynthesis. (nih.gov)
  • Expression of SRE1 was reduced under iron-starving conditions, underscoring its role as a negative regulator of genes involved in iron uptake. (nih.gov)
  • The loss of iron led to a approximately 2.5-fold decrease in DNA-binding affinity, indicating that iron was directly involved in SRE1 regulation of iron-uptake genes. (nih.gov)
  • Matthew Barber and Nels Elde from the University of Utah School of Medicine compared transferrin-encoding genes from 21 primate species, and found remarkable variation at sites known to interact with a bacterial transferrin binding protein, TbpA. (the-scientist.com)
  • 11 Million Americans or more have the genes that can result in too much iron. (irondisorders.org)
  • Each of the four monomeric units contain a heme prosthetic group in which a ferric cation is bound between four nitrogen atoms of a porphyrin ring. (wikipedia.org)
  • These proteins act as electron shuttles by switching the oxidation state of the heme iron atom between ferrous (Fe2+) and ferric (Fe3+). (wikipedia.org)
  • Metal nanoclusters bound to the Ferric Binding Protein from Neisseria gonorrhoeae. (expasy.org)
  • The iron within the heme can change to another form of iron called ferric iron (Fe 3+ ), which cannot bind oxygen. (medlineplus.gov)
  • HBB gene mutations that cause methemoglobinemia, beta-globin type change the structure of beta-globin and promote the heme iron to change from ferrous to ferric. (medlineplus.gov)
  • The ferric iron cannot bind oxygen and causes cyanosis and the brown appearance of blood. (medlineplus.gov)
  • 1, 2 However, at least in vitro, AA also has pro-oxidant activity, principally by reducing ferric iron to the ferrous form, which converts hydrogen peroxide into the more toxic hydroxyl radical (Fenton reaction). (bmj.com)
  • In methemoglobinemia, beta-globin type, variants in the HBB gene alter the beta-globin protein and promote the heme iron to change from ferrous to ferric. (medlineplus.gov)
  • Meningitis-causing bacteria exerted strong evolutionary pressure on an iron-binding protein in primates, a study shows. (the-scientist.com)
  • In primates, the iron-carrying protein transferrin likely evolved to inhibit meningitis-causing bacteria from scavenging iron, an essential but limited nutrient, researchers reported last week (December 11) in Science . (the-scientist.com)
  • Bacteria are able to compete effectively for iron bound to host proteins because of the secretion of high-affinity, low molecular weight iron chelators known as siderophores. (medscape.com)
  • In order to deprive bacteria of iron, the host also secretes iron-binding proteins. (medscape.com)
  • Group 1 (Dur-19, PF00477, LEA_5) Late Embryogenesis Abundant (LEA) proteins are present in organisms from all three domains of life, Archaea, Bacteria, and Eukarya. (researchgate.net)
  • One of the reasons it remains under-studied is because there are inherent problems with working with iron-oxidizing bacteria (FeOB), including low biomass yields and interference from the iron oxides in the samples. (darkenergybiosphere.org)
  • This is necessary because most host iron is bound to intracellular and extracellular proteins. (medscape.com)
  • We highlight proteins involved in angiogenesis, iron homeostasis, and the extracellular matrix, many of which are novel, including training-induced increases in fibroblast activation. (lu.se)
  • We highlight proteins involved in angiogenesis, iron homeostasis, and the extracellular matrix, many of which are novel, including training-induced increases in fibroblast activation protein (FAP), a membrane-bound and circulating protein relevant in body-composition homeostasis. (lu.se)
  • When TIBC is at or below the low end of a laboratory range, it is an indication that there is limited capacity for transferrin molecules to accept additional iron. (irondisorders.org)
  • Transferrin saturation percentage (TS %) is calculated by dividing serum iron by TIBC, then multiplying by 100. (irondisorders.org)
  • If TIBC levels are high, it may indicate low iron in the blood due to iron deficiency anemia. (medicalnewstoday.com)
  • TIBC must not be confused with unsaturated binding capacity (UIBC), which represents the residual after subtraction of serum iron from TIBC. (medscape.com)
  • The relationship of TIBC and transferrin is disrupted in individuals with conditions that affect transferrin-binding capacity or other iron-binding proteins. (medscape.com)
  • The UIBC and TIBC are usually increased in patients with iron-deficiency anemia, in whom a transferrin saturation of 15% or less is noted. (medscape.com)
  • This group is composed of Mycobacterium tuberculosis putative mycofactocin radical SAM maturase MftC and similar proteins. (nih.gov)
  • In this study, we address the issue of the interactions of plasma proteins with polymer coated surfaces. (unict.it)
  • Host defense against bacterial invasion depends on phagocytosis by polymorphonuclear granulocytes and the bactericidal effect of serum, mediated in large part by complement proteins. (medscape.com)
  • Lipopolysaccharide-binding protein facilitates transfer of bacterial cell wall components to inflammatory cells. (medscape.com)
  • For example, MVs from E. coli under envelope stress contain multiple misfolded proteins, whose release enhances bacterial survival [ 9 ]. (nature.com)
  • Neutrophilic, bacterial iron-oxidation remains one of the least understood energy-generating biological reactions to date. (darkenergybiosphere.org)
  • Clusters are often associated with cysteine residues in the protein chain. (wikipedia.org)
  • Iron-oxo clusters biomineralizing on protein surfaces. (berkeley.edu)
  • Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1. (nature.com)
  • Fe-S clusters are present in more than 300 different types of enzymes or proteins and play crucial roles in fundamental life processes such as respiration, photosynthesis and nitrogen fixation. (uga.edu)
  • The flavin together with the iron-sulfur clusters function to mediate electron transfer from the dicarboxylate binding site on the Fp subunit to the membrane-anchor domain where quinone is reduced to quinol. (lu.se)
  • Exceptions to this rule detract considerably from the diagnostic value of measuring transferrin saturation in patients with suspected iron deficiency. (medscape.com)
  • [ 1 , 7 ] A low serum iron concentration is typically present along with a normal transferrin saturation in individuals with anemia of chronic inflammation. (medscape.com)
  • It is this specific combination that makes lactoferrin's iron affinity 300 times greater than transferrin. (wikipedia.org)
  • however, conventional anti-PD-1 mAbs are not suitable as therapeutic agents because of their low binding affinity to antigen. (bvsalud.org)
  • To address these issues, we established two anti-bovine PD-1 rabbit mAbs (1F10F1 and 4F5F2) and its chimeric form using bovine IgG1 (Boch1D10F1), which exhibit high binding affinity. (bvsalud.org)
  • Boch1D10F1 exhibited a similar binding affinity to bovine PD-1 and the inhibitory activity on PD-1/PD-L1 binding compared with 1D10F1. (bvsalud.org)
  • He says while we have sophisticated our systems in the use of iron, it can still be very damaging to cells because it can cause oxidative stress. (northwestern.edu)
  • A major goal of his research is to find ways to reduce iron in chronic diseases and therefore reduce the oxidative stress that iron can cause. (northwestern.edu)
  • Ardehali says too much iron can lead to significant damage to the cells through oxidative stress. (northwestern.edu)
  • 1994). High-res- belongs to the family of intracellular lipid bind- olution crystal structures (Sacchetti ni et al. (lu.se)
  • Frataxin is a highly conserved protein encoded by the frataxin (FXN) gene. (nih.gov)
  • Iron-dependent enzymes catalyze a variety of biochemical reactions and can be divided into three broad classes depending on the structure of their active site: non-heme mono-iron, non-heme diiron , or heme centers. (wikipedia.org)
  • A well-known family of iron-dependent enzymes include oxygenases that facilitate hydroxyl group addition of one or both atoms from o2. (wikipedia.org)
  • Radical SAM enzymes are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster that is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical, which in turn abstracts a hydrogen from the appropriately positioned carbon atom of the substrate. (nih.gov)
  • Radical SAM enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster. (nih.gov)
  • Their logic was that all proteins are broken down by strong digestive enzymes. (drgreene.com)
  • Leghemoglobin is chemically bound to a non-protein molecule called heme, an iron-containing molecule that gives red meat its color. (singularityhub.com)
  • Only a small proportion of anemia in North East Thai school children is associated with iron deficiency. (who.int)
  • Instead of binding and expelling radionuclides from the body, we could maybe block the uptake. (sciencedaily.com)
  • However, whether MVs are also responsible for efficient iron uptake and therefore involved in microbial interaction remains to be elucidated. (nature.com)
  • Iron is an element that is crucial for the growth of most microorganisms which have developed efficient mechanisms for uptake of this metal. (springer.com)
  • We relate protein changes to training-induced maximal oxygen uptake adaptations and validate our top findings in an external exercise cohort. (lu.se)
  • Peroxide, rather than superoxide, is shown to be the product of O 2 reduction, implying that ferroxidase centers function in pairs via long-range electron transfer through the protein resulting in reduction of O 2 bound at only one of the centers. (rcsb.org)
  • We also collaborate with other groups for Mossbauer, electron-nuclear double resonance (ENDOR), X-ray absorption and X-ray crystallography studies of proteins prepared in our laboratory. (uga.edu)
  • Iron-O 2 chemistry of this type is currently unknown among the growing family of proteins that bind a diiron site within a four α-helical bundle in general and ferritins in particular. (rcsb.org)
  • MitoNEET belongs to the CDGSH Iron-Sulfur Domain (cisd)-gene family of proteins and is a [2Fe-2S] cluster-containing protein found on the outer membrane of mitochondria. (researchgate.net)
  • Mature frataxin (81-210) is a critically important protein because it facilitates the assembly of mitochondrial iron-sulfur cluster protein complexes such as aconitase, lipoate synthase, and succinate dehydrogenases. (nih.gov)
  • Compared to the pre-splitting state, we observe repositioning of ABCE1's iron-sulfur cluster domain, which rotates 150° into a binding pocket on the 40S subunit. (nature.com)
  • Moreover, a molecular-level understanding of iron-sulfur cluster biogenesis is crucial for understanding a variety of human diseases involving anemias, myopathies and ataxias that arise from defects in Fe-S cluster biogenesis proteins. (uga.edu)
  • Iron-sulfur protein maturation in Helicobacter pylori:Identifying a Nfu-type cluster carrier protein and its iron-sulfur protein targets. (uga.edu)
  • It is unexpected that B. subtilis SQR without covalently bound FAD is not assembled in the E. coli membrane provided that all other aspects of assembly, including iron-sulfur cluster biogenesis, are functional in the heterologous system. (lu.se)
  • The covalent bond to FAD in SQR is essential for enzyme activity and the main reason for this is that the bond raises the midpoint redox potential of the flavin by more than 80 mV compared to non-covalently bound flavin. (lu.se)
  • Mutations in the conserved cysteine residues in the cysteine-rich region led to a decrease in bound iron. (nih.gov)
  • 32303) chromosome segregation and condensation protein%2C ScpB CP001857 CDS Arcpr_0039 complement(32287. (go.jp)
  • 32898) chromosome segregation and condensation protein ScpA CP001857 CDS Arcpr_0040 complement(32907. (go.jp)
  • This gene provides instructions for making a protein called beta-globin. (medlineplus.gov)
  • Normally, our intestines stop absorbing iron when we have enough in our blood but due to a faulty gene, those with haemochromatosis take on so much from their diet that it reaches toxic levels. (dailymail.co.uk)
  • 9766 conserved hypothetical protein CP001857 CDS Arcpr_0009 complement(9767. (go.jp)
  • 10378) hypothetical protein CP001857 CDS Arcpr_0010 complement(10422. (go.jp)
  • 13428) hypothetical protein CP001857 CDS Arcpr_0013 complement(13425. (go.jp)
  • 13751) hypothetical protein CP001857 CDS Arcpr_0014 complement(13789. (go.jp)
  • 19702 hypothetical protein CP001857 CDS Arcpr_0022 complement(19723. (go.jp)
  • 21298 hypothetical protein CP001857 CDS Arcpr_0025 complement(21287. (go.jp)
  • 23242 hypothetical protein CP001857 CDS Arcpr_0028 23232. (go.jp)
  • 29158) hypothetical protein CP001857 CDS Arcpr_0035 complement(29143. (go.jp)
  • 29526) hypothetical protein CP001857 CDS Arcpr_0036 29596. (go.jp)
  • 36678) hypothetical protein CP001857 CDS Arcpr_0042 complement(36769. (go.jp)
  • 42520) hypothetical protein CP001857 tRNA Arcpr_R0002 complement(42639. (go.jp)
  • 43572) hypothetical protein CP001857 CDS Arcpr_0052 43655. (go.jp)
  • 47353) hypothetical protein CP001857 CDS Arcpr_0058 complement(47350. (go.jp)
  • 52977 conserved hypothetical protein CP001857 CDS Arcpr_0062 complement(52960. (go.jp)
  • 53727) hypothetical protein CP001857 CDS Arcpr_0063 complement(53793. (go.jp)
  • The current focus is copper-containing proteins and we use a multi-disciplinary approach to study the relationship between their structure and function. (ncl.ac.uk)
  • Allen S, Badarau A, Dennison C. The influence of protein folding on the copper affinities of trafficking and target sites . (ncl.ac.uk)
  • El Ghazouani A, Basle A, Firbank SJ, Knapp CW, Gray J, Graham DW, Dennison C. Copper-Binding Properties and Structures of Methanobactins from Methylosinus trichosporium OB3b . (ncl.ac.uk)
  • Badarau A, Firbank SJ, McCarthy AA, Banfield MJ, Dennison C. Visualizing the Metal-Binding Versatility of Copper Trafficking Sites . (ncl.ac.uk)
  • Flavinylation of Fp in B. subtilis does not require the Ip subunit or the membrane anchor but depends on folding of the Fp polypeptide into a state that can bind FAD and subsequent mediate covalent binding of the FAD [3, 4]. (lu.se)
  • Each pocket contributes four amino acids (two tyrosines, one histidine, and one aspartate) and, along with two carbonate or bicarbonate anions, forms a six-membered coordinate around the iron cation. (wikipedia.org)
  • The specific functions of mitoNEET/CISD1 remain to be fully elucidated, but the protein is involved in regulating mitochondrial bioenergetics in several metabolic diseases. (researchgate.net)
  • mRNA-binding protein tristetraprolin is essential for cardiac response to iron deficiency by regulating mitochondrial function. (northwestern.edu)
  • Dean, M. & Annilo, T. Evolution of the ATP-binding cassette (ABC) transporter superfamily in vertebrates. (nature.com)
  • Because iron is toxic at high levels, iron acquisition in pathogenic organisms, including H. capsulatum, is a highly regulated process. (nih.gov)
  • As well as demonstrating an expansion of the iron-O 2 chemistry known to occur in nature, these data are also highly relevant to the question of whether all ferritins mineralize iron via a common mechanism, providing unequivocal proof that they do not. (rcsb.org)
  • Recent data from preclinical studies suggest a role for neutrophil myeloperoxidase and lipopolysaccharide-binding protein in host defense against K pneumoniae infection. (medscape.com)