Cations
Cations, Divalent
Cations, Monovalent
Organic Cation Transport Proteins
Organic Cation Transporter 1
Magnesium
TRPM Cation Channels
Calcium
Sodium
TRPC Cation Channels
Ion Channels
Potassium
Manganese
Cation Transport Proteins
Hydrogen-Ion Concentration
Membrane Potentials
Rubidium
Strontium
Lithium
TRPV Cation Channels
Cation Exchange Resins
Cesium
Metals, Alkali
Ion Transport
Cell Membrane Permeability
Cyclic Nucleotide-Gated Cation Channels
Barium
Ions
Ion Channel Gating
Patch-Clamp Techniques
Quaternary Ammonium Compounds
Edetic Acid
Biological Transport
Flufenamic Acid
Metals
Calcium Channels
Binding Sites
Lanthanum
Cobalt
Molecular Sequence Data
Adenosine Triphosphate
Cell Membrane
Zinc
Catecholamine Plasma Membrane Transport Proteins
Amino Acid Sequence
Biological Transport, Active
Osmolar Concentration
Electrophysiology
Nickel
Salts
Gadolinium
Temperature
Models, Molecular
TRPP Cation Channels
Antiporters
Sodium-Potassium-Exchanging ATPase
Substrate Specificity
Cadmium
Metals, Rare Earth
Metals, Alkaline Earth
Permeability
Ouabain
Potassium Chloride
Oocytes
Calcium Chloride
Tromethamine
Protons
Chelating Agents
Ion Exchange
Rabbits
Transient Receptor Potential Channels
Ionophores
Protein Binding
1-Methyl-4-phenylpyridinium
Gramicidin
Potassium Channels
Protein Conformation
Erythrocytes
Valinomycin
Membrane Proteins
Carrier Proteins
Amiloride
Thermodynamics
Escherichia coli
Electrochemistry
Dose-Response Relationship, Drug
Cesium Isotopes
Onium Compounds
Molecular Structure
Models, Chemical
Cells, Cultured
Kidney
Lipid Bilayers
Mutation
Water
Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels
Sodium Channels
Spermidine
Adenosine Triphosphatases
Equilibrative Nucleoside Transport Proteins
Cattle
Models, Biological
Spermine
Chromatography, Ion Exchange
Choline
Structure-Activity Relationship
Organophosphorus Compounds
Calcimycin
Base Sequence
Calcium Channel Blockers
Lasalocid
Tetraphenylborate
Extracellular Space
Receptors, Purinergic P2X7
Binding, Competitive
Bentonite
Meglumine
Potassium Isotopes
Magnetic Resonance Spectroscopy
Mathematics
Sodium Isotopes
Membrane Transport Modulators
Fluorescent Dyes
Potassium-Hydrogen Antiporters
Ion Exchange Resins
Buffers
Xenopus
Sequence Homology, Amino Acid
Nigericin
Receptors, Purinergic P2
DNA
Mutagenesis, Site-Directed
Nucleic Acid Conformation
Bromides
Guinea Pigs
Melibiose
Neurons
Free Radicals
Cloning, Molecular
Ruthenium Red
Receptors, Purinergic P2X4
Protein Structure, Tertiary
Mercury
Hydrogen
Fura-2
Acid Sensing Ion Channels
Spectrophotometry
Ion Pumps
Catalysis
Terbium
Calcium Signaling
Carnitine
Membranes, Artificial
4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid
Solutions
Sodium Radioisotopes
Sodium-Hydrogen Antiporter
Silver
Rubidium Radioisotopes
Calixarenes
Spectrophotometry, Ultraviolet
Thapsigargin
Crystallography, X-Ray
Electrolytes
Receptors, Purinergic P2X
Oxidation-Reduction
Electrophoresis, Polyacrylamide Gel
Cloning and expression of the algL gene, encoding the Azotobacter chroococcum alginate lyase: purification and characterization of the enzyme. (1/3809)
The alginate lyase-encoding gene (algL) of Azotobacter chroococcum was localized to a 3.1-kb EcoRI DNA fragment that revealed an open reading frame of 1,116 bp. This open reading frame encodes a protein of 42.98 kDa, in agreement with the value previously reported by us for this protein. The deduced protein has a potential N-terminal signal peptide that is consistent with its proposed periplasmic location. The analysis of the deduced amino acid sequence indicated that the gene sequence has a high homology (90% identity) to the Azotobacter vinelandii gene sequence, which has very recently been deposited in the GenBank database, and that it has 64% identity to the Pseudomonas aeruginosa gene sequence but that it has rather low homology (15 to 22% identity) to the gene sequences encoding alginate lyase in other bacteria. The A. chroococcum AlgL protein was overproduced in Escherichia coli and purified to electrophoretic homogeneity in a two-step chromatography procedure on hydroxyapatite and phenyl-Sepharose. The kinetic and molecular parameters of the recombinant alginate lyase are similar to those found for the native enzyme. (+info)Regulated exopolysaccharide production in Myxococcus xanthus. (2/3809)
Myxococcus xanthus fibrils are cell surface-associated structures composed of roughly equal amounts of polysaccharide and protein. The level of M. xanthus polysaccharide production under different conditions in the wild type and in several mutants known to have alterations in fibril production was investigated. Wild-type exopolysaccharide increased significantly as cells entered the stationary phase of growth or upon addition of Ca2+ to growing cells, and the polysaccharide-induced cells exhibited an enhanced capacity for cell-cell agglutination. The activity of the key gluconeogenic pathway enzyme phosphoenolpyruvate carboxykinase (Pck) also increased under these conditions. Most fibril-deficient mutants failed to produce polysaccharide in a stationary-phase- or Ca2+-dependent fashion. However, regulation of Pck activity was generally unimpaired in these mutant strains. In an stk mutant, which overproduces fibrils, polysaccharide production and Pck activity were constitutively high under the conditions tested. Polysaccharide production increased in most fibril-deficient strains when an stk mutant allele was present, indicating that these fibril-deficient mutants retained the basic cellular components required for fibril polysaccharide production. In contrast to other divalent cations tested, Sr2+ effectively replaced Ca2+ in stimulating polysaccharide production, and either Ca2+ or Sr2+ was required for fruiting-body formation by wild-type cells. By using transmission electron microscopy of freeze-substituted log-phase wild-type cells, fibril material was observed as a cell surface-associated layer of uniform thickness composed of filaments with an ordered structure. (+info)Metal-catalyzed oxidation of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli: inactivation and destabilization by oxidation of active-site cysteines. (3/3809)
The in vitro instability of the phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase [DAHPS(Phe)] from Escherichia coli has been found to be due to a metal-catalyzed oxidation mechanism. DAHPS(Phe) is one of three differentially feedback-regulated isoforms of the enzyme which catalyzes the first step of aromatic biosynthesis, the formation of DAHP from phosphoenolpyruvate and D-erythrose-4-phosphate. The activity of the apoenzyme decayed exponentially, with a half-life of about 1 day at room temperature, and the heterotetramer slowly dissociated to the monomeric state. The enzyme was stabilized by the presence of phosphoenolpyruvate or EDTA, indicating that in the absence of substrate, a trace metal(s) was the inactivating agent. Cu2+ and Fe2+, but none of the other divalent metals that activate the enzyme, greatly accelerated the rate of inactivation and subunit dissociation. Both anaerobiosis and the addition of catalase significantly reduced Cu2+-catalyzed inactivation. In the spontaneously inactivated enzyme, there was a net loss of two of the seven thiols per subunit; this value increased with increasing concentrations of added Cu2+. Dithiothreitol completely restored the enzymatic activity and the two lost thiols in the spontaneously inactivated enzyme but was only partially effective in reactivation of the Cu2+-inactivated enzyme. Mutant enzymes with conservative replacements at either of the two active-site cysteines, Cys61 or Cys328, were insensitive to the metal attack. Peptide mapping of the Cu2+-inactivated enzyme revealed a disulfide linkage between these two cysteine residues. All results indicate that DAHPS(Phe) is a metal-catalyzed oxidation system wherein bound substrate protects active-site residues from oxidative attack catalyzed by bound redox metal cofactor. A mechanism of inactivation of DAHPS is proposed that features a metal redox cycle that requires the sequential oxidation of its two active-site cysteines. (+info)Enhanced bioaccumulation of heavy metal ions by bacterial cells due to surface display of short metal binding peptides. (4/3809)
Metal binding peptides of sequences Gly-His-His-Pro-His-Gly (named HP) and Gly-Cys-Gly-Cys-Pro-Cys-Gly-Cys-Gly (named CP) were genetically engineered into LamB protein and expressed in Escherichia coli. The Cd2+-to-HP and Cd2+-to-CP stoichiometries of peptides were 1:1 and 3:1, respectively. Hybrid LamB proteins were found to be properly folded in the outer membrane of E. coli. Isolated cell envelopes of E. coli bearing newly added metal binding peptides showed an up to 1.8-fold increase in Cd2+ binding capacity. The bioaccumulation of Cd2+, Cu2+, and Zn2+ by E. coli was evaluated. Surface display of CP multiplied the ability of E. coli to bind Cd2+ from growth medium fourfold. Display of HP peptide did not contribute to an increase in the accumulation of Cu2+ and Zn2+. However, Cu2+ ceased contribution of HP for Cd2+ accumulation, probably due to the strong binding of Cu2+ to HP. Thus, considering the cooperation of cell structures with inserted peptides, the relative affinities of metal binding peptide and, for example, the cell wall to metal ion should be taken into account in the rational design of peptide sequences possessing specificity for a particular metal. (+info)Identification and characterization of ligands for L-selectin in the kidney. II. Expression of chondroitin sulfate and heparan sulfate proteoglycans reactive with L-selectin. (5/3809)
Ligands for the leukocyte adhesion molecule L-selectin are expressed not only in lymph node high endothelial venules (HEV) but also in the renal distal tubuli. Here we report that L-selectin-reactive molecules in the kidney are chondroitin sulfate and heparan sulfate proteoglycans of 500-1000 kDa, unlike those in HEV bearing sialyl Lewis X-like carbohydrates. Binding of L-selectin to these molecules was mediated by the lectin domain of L-selectin and required divalent cations. Binding was inhibited by chondroitinase and/or heparitinase but not sialidase. Thus, L-selectin can recognize chondroitin sulfate and heparan sulfate glycosaminoglycans structurally distinct from sialyl Lewis X-like carbohydrates. (+info)Eosinophil peroxidase increases membrane permeability in mammalian urinary bladder epithelium. (6/3809)
Eosinophil peroxidase (EPO), a cationic protein found in eosinophils, has been reported to be cytotoxic independent of its peroxidase activity. This study investigated with electrophysiological methods whether EPO is toxic to mammalian urinary bladder epithelium. Results indicate that EPO, when added to the mucosal solution, increases apical membrane conductance of urinary bladder epithelium only when the apical membrane potential is cell interior negative. The EPO-induced conductance was concentration dependent, with a maximum conductance of 411 microseconds/cm2 and a Michaelis-Menten constant of 113 nM. The EPO-induced conductance was nonselective for K+ and Cl-. The conductance was partially reversed using voltage but not by removal of EPO from the bulk solution. Mucosal Ca2+ reversed the EPO-induced conductance by a mechanism involving reversible block of the conductance. Prolonged exposure (up to 1 h) to EPO was toxic to the urinary bladder epithelium, as indicated by an irreversible increase in transepithelial conductance. These results suggest that EPO is indeed toxic to urinary bladder epithelium via a mechanism that involves an increase in membrane permeability. (+info)Structure of the oligonucleotide d(CGTATATACG) as a site-specific complex with nickel ions. (7/3809)
In this paper we explore the application of Ni2+to the crystallization of oligonucleotides. We have determined in this way the structure of a fully alternating (Y-R) decanucleotide d(CGTATATACG) by single crystal X-ray diffraction. This is the first oligonucleotide crystal structure with an alternating 5'-(TA)3-3' central part. Alternating oligonucleotides have a particular interest since they often have a unique structure. In this case the general conformation is B-like with an alternating twist and an end-to-end interaction which involves terminal guanines. The crystal belongs to space group P41212 with a = b = 52.46, c = 101.49 A. This packing imposes a 90 degrees crossing of the symmetry related helices. This is a new way of packing for decamers. The oligonucleotide structure is characterized by the specific association with seven nickel ions, involving the N7 atom of every guanine. One of the Ni2+ions is shared between two guanines of symmetry related molecules. Until now no oligonucleotide has been crystallized in the presence of this metal ion. A novel C.A.T triplet structure has also been tentatively identified. (+info)Heparin influence on alpha-staphylotoxin formed channel. (8/3809)
The effects of heparin on ion channels formed by Staphylococcus aureus alpha-toxin (ST channel) in lipid bilayers were studied under voltage clamp conditions. Heparin concentrations as small as 100 pM induced a sharp dose-dependent increase in channel voltage sensitivity. This was only observed when heparin was added to the negative-potential side of lipid bilayers in the presence of divalent cations. Divalent cations differ in their efficiency: Zn2+>Ca2+>Mg2+. The apparent positive gating charge increased 2-3-fold with heparin addition as well as with acidification of the bathing solution. 'Free' carboxyl groups and carboxyl groups in ion pairs of the protein moiety are hypothesized to interact with sulfated groups of heparin through divalent cation bridges. The cis mouth of the channel (that protrudes beyond the membrane plane on the side of ST addition and to which voltage was applied) is less sensitive to heparin than the trans-mouth. It is suggested that charged residues which interact with heparin at the cis mouth of ST channels and which contribute to the effective gating charge at negative voltage may be physically different from those at the trans mouth and at positive voltage. (+info)Prevalence: Anemia, hemolytic, congenital is a rare disorder, affecting approximately 1 in 100,000 to 1 in 200,000 births.
Causes: The condition is caused by mutations in genes that code for proteins involved in hemoglobin synthesis or red blood cell membrane structure. These mutations can lead to abnormal hemoglobin formation, red blood cell membrane instability, and increased susceptibility to oxidative stress, which can result in hemolytic anemia.
Symptoms: Symptoms of anemia, hemolytic, congenital may include jaundice (yellowing of the skin and eyes), fatigue, weakness, pale skin, and shortness of breath. In severe cases, the condition can lead to life-threatening complications such as anemia, infections, and kidney failure.
Diagnosis: Anemia, hemolytic, congenital is typically diagnosed through a combination of physical examination, medical history, and laboratory tests, including blood smear examination, hemoglobin electrophoresis, and mutation analysis.
Treatment: Treatment for anemia, hemolytic, congenital depends on the specific underlying genetic cause and may include blood transfusions, folic acid supplements, antibiotics, and/or surgery to remove the spleen. In some cases, bone marrow transplantation may be necessary.
Prognosis: The prognosis for anemia, hemolytic, congenital varies depending on the specific underlying genetic cause and the severity of the condition. With appropriate treatment, many individuals with this condition can lead relatively normal lives, but in severe cases, the condition can be life-threatening.
Leukocyte extravasation
Ephesite
Kinase
Microbial rhodopsin
Cell adhesion molecule
5-guanidino-2-oxopentanoate decarboxylase
Integrin
Pikachurin
Diisopropyl-fluorophosphatase
Polyphosphate
PRIM2
Nickel oxyacid salts
Undecaprenyl-diphosphatase
DNA polymerase alpha subunit 2
Adenosine triphosphate
PRIM1
TAPS (buffer)
Gitelman syndrome
Nucleic acid tertiary structure
TSE buffer
TRPV6
Calcium alginate
TBE buffer
Terminal deoxynucleotidyl transferase
Hypomagnesemia with secondary hypocalcemia
Polycystin cation channel family
Collagenase
Natural resistance-associated macrophage protein
A23187
Ionophore
Sulfide
Prokaryotic DNA replication
Europium anomaly
Guluronic acid
Extended periodic table
Sucrose-phosphate synthase
Gene delivery
Gregory S. Girolami
Lipid bilayer fusion
Hin recombinase
UTP-glucose-1-phosphate uridylyltransferase
Biotite
Calcium caseinate
Ribonuclease T
Lipid bilayer
Uranate
Serine racemase
Carrollite
Sodium cellulose phosphate
Metalloid
Chondrodite
MFAP2
Aiyu jelly
Bacterial adhesion in aquatic system
Germanium(II) hydrides
Beta-propeller phytase
C4orf36
Prostasomes
Mineral group
Adsorption of divalent cations on DNA - PubMed
Inhibition of human red cell sodium and potassium transport by divalent cations - PubMed
Influence of divalent cations on the biofouling behaviors of alginate hydrogels. | Biomed Mater;15(1): 015003, 2019 12 09. ...
Interactions between FE 90 Plus Oral and divalent-trivalent-cations-tetracyclines
Divalent cations enhance fluoride binding to Streptococcus mutans and Streptococcus sanguinis cells and subsequently inhibit...
ArboCat Virus: Simian hemorrhagic fever (SHFV)
Monovalent and Divalent Cation Standards (8) (Ethylenediamine Containing Sample) - Shodex
DailyMed - FOSAPREPITANT DIMEGLUMINE injection, powder, lyophilized, for solution
Publications - Peter Basser Lab | NICHD - Eunice Kennedy Shriver National Institute of Child Health and Human Development
All-temperature zinc batteries with high-entropy aqueous electrolyte | Nature Sustainability
Journal of Research Volume 58 | NIST
Primer designing tool
CDD Conserved Protein Domain Family: PLPDE III LS D-TA like
SLC11A2 gene: MedlinePlus Genetics
Publication Detail
Biomarkers Search
Hypermagnesemia: Overview, Renal Failure, Other Causes
NACHSHEN DA[au] - Search Results - PubMed
Hyperphosphatemia Medication: Diuretics, Phosphate Binders
NEWRECORD
A Case-Control Study on the Origin of Atypical Scrapie in Sheep, France - Volume 15, Number 5-May 2009 - Emerging Infectious...
Frontiers | Variation for Composition and Quality in a Collection of the Resilient Mediterranean 'de penjar' Long Shelf-Life...
SCOPe 2.08: Domain d2yvxa3: 2yvx A:276-448
TCDB » SEARCH
Registration Dossier - ECHA
Ions3
- The distribution of divalent ions in semidilute solutions of high-molecular-mass DNA containing both sodium chloride and strontium chloride in near-physiological conditions is studied by small-angle x-ray scattering and by small-angle neutron scattering. (nih.gov)
- In general, gramicidin channels are ideally selective for monovalent cations and the single-channel conductances for the alkali cations are ranked in the same order as the aqueous mobilities of these ions. (wikidoc.org)
- Idealized image of water softening process involving replacement of calcium ions in water with sodium ions donated by a cation-exchange resin . (wikipedia.org)
Monovalent cations3
- Gramicidin's bactericidal activity is a result of increasing the permeability of the bacterial cell wall allowing inorganic monovalent cations (e.g. (wikidoc.org)
- Cl- in particular is excluded from the channel because its hydration shell is thermodynamically stronger than that of most monovalent cations. (wikidoc.org)
- The channel is permeable to most monovalent cations, which move through the channel in single file. (wikidoc.org)
Trivalent1
- You can also try the effects of divalent or trivalent cations, such as calcium, magnesium and aluminum salts. (madsci.org)
Nucleotide2
- 5. Divalent cation-, nucleotide-, and polymerization-dependent changes in the conformation of subdomain 2 of actin. (nih.gov)
- Guanine nucleotide and divalent cation sensitivity. (aspetjournals.org)
Transporter2
- The SLC11A2 gene provides instructions for making a protein called divalent metal transporter 1 (DMT1). (medlineplus.gov)
- Divalent metal transporter 1. (medlineplus.gov)
Inorganic1
- The category consists of inorganic cobalt substances for which the toxicity is governed by the cobalt cation. (europa.eu)
CALCIUM3
- When the strontium chloride is replaced by calcium chloride, similar results are obtained, but the thickness of the sheath increases when the divalent salt concentration decreases. (nih.gov)
- It binds and transports CALCIUM and other divalent cations across membranes and uncouples oxidative phosphorylation while inhibiting ATPase of rat liver mitochondria. (nih.gov)
- Water softening is the removal of calcium , magnesium , and certain other metal cations in hard water . (wikipedia.org)
Aqueous1
- Concentrated dual-cation electrolyte strategy for aqueous zinc-ion batteries. (nature.com)
ATPase1
- Divalent cation transporting ATPase of 1207 aas and 9 putative TMSs, Catp-6. (tcdb.org)
Gene2
Cobalt2
Metal2
Increases1
- These findings suggest that exposure of oral bacteria to fluoride in the presence of divalent cations increases fluoride binding to bacterial cells and subsequently enhances fluoride-induced inhibition of bacterial acid production. (elsevier.com)
Influence6
- Influence of divalent cations on the biofouling behaviors of alginate hydrogels. (bvsalud.org)
- 1. Spectroscopic study of conformational changes in subdomain 1 of G-actin: influence of divalent cations. (nih.gov)
- 2. The influence of divalent cations on the dynamic properties of actin filaments: a spectroscopic study. (nih.gov)
- 6. Fluorescence anisotropy of labeled F-actin: influence of divalent cations on the interaction between F-actin and myosin heads. (nih.gov)
- 17. Influence of the high affinity divalent cation on actin tryptophan fluorescence. (nih.gov)
- The influence of divalent cations. (nih.gov)
Bind1
- Its ability to bind and transport cations is due to the presence of cation-binding sites in the channel. (wikidoc.org)
Inhibition1
- The enhanced inhibition of acid production in the presence of divalent cations is probably due to the improved efficiency of fluoride binding to bacterial cells being improved via these divalent cations. (elsevier.com)
Bacterial2
- Furthermore, divalent cations such as Ca 2+ and Mg 2+ increase the binding of fluoride to bacterial cells. (elsevier.com)
- Furthermore, divalent cations such as Ca2+ and Mg2+ increase the binding of fluoride to bacterial cells. (elsevier.com)
Effect1
- In addition, the effect of some divalent cations on the interaction with vesicles TRCDA/DMPC was investigated. (scielo.cl)
High5
- Both small-angle neutron scattering and small-angle x-ray scattering reveal a continuous increase in the scattering intensity at low q with increasing divalent ion concentration, while at high q the scattering curves converge. (nih.gov)
- 4. Effects of the type of divalent cation, Ca2+ or Mg2+, bound at the high-affinity site and of the ionic composition of the solution on the structure of F-actin. (nih.gov)
- 13. Divalent cation binding to the high- and low-affinity sites on G-actin. (nih.gov)
- 14. High affinity divalent cation binding to actin. (nih.gov)
- 16. Fluorescence measurements of the binding of cations to high-affinity and low-affinity sites on ATP-G-actin. (nih.gov)
Content1
- Regulation of cation content and cell volume in hemoglobin erythrocytes from patients with homozygous hemoglobin C disease. (nih.gov)
Human1
- Mg and other divalent cations should not be used as 'inert' ionic substitutes in human red cell Na and K transport studies. (nih.gov)
Channels1
- Background and Purpose P2X receptors (P2XRs) are trimeric ligand-gated ion channels (LGICs) that open a cation-selective pore in response to ATP binding to their large extracellular domain (ECD). (biorxiv.org)
DMT11
- The SLC11A2 gene provides instructions for making a protein called divalent metal transporter 1 (DMT1). (medlineplus.gov)
Calcium2
- The divalent cations calcium and magnesium and the anion phosphorus are important in several cellular processes. (medscape.com)
- It binds and transports CALCIUM and other divalent cations across membranes and uncouples oxidative phosphorylation while inhibiting ATPase of rat liver mitochondria. (nih.gov)
Complex1
- Our results provide evidence that cellular divalent cation regulation is functionally coupled to the Kell/XK system in erythrocytes and loss of this complex may contribute to acanthocytosis formation in McLeod syndrome. (nih.gov)