Inorganic salts or organic esters of arsenious acid.
Inorganic compounds that contain sodium as an integral part of the molecule.
Efflux pumps that use the energy of ATP hydrolysis to pump arsenite across a membrane. They are primarily found in prokaryotic organisms, where they play a role in protection against excess intracellular levels of arsenite ions.
A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.
Inorganic or organic salts and esters of arsenic acid.
A shiny gray element with atomic symbol As, atomic number 33, and atomic weight 75. It occurs throughout the universe, mostly in the form of metallic arsenides. Most forms are toxic. According to the Fourth Annual Report on Carcinogens (NTP 85-002, 1985), arsenic and certain arsenic compounds have been listed as known carcinogens. (From Merck Index, 11th ed)
Multisubunit enzymes that reversibly synthesize ADENOSINE TRIPHOSPHATE. They are coupled to the transport of protons across a membrane.
Cation-transporting proteins that utilize the energy of ATP hydrolysis for the transport of CALCIUM. They differ from CALCIUM CHANNELS which allow calcium to pass through a membrane without the use of energy.
Proton-translocating ATPases that are involved in acidification of a variety of intracellular compartments.
A general class of integral membrane proteins that transport ions across a membrane against an electrochemical gradient.
A metallic element that has the atomic symbol Sb, atomic number 51, and atomic weight 121.75. It is used as a metal alloy and as medicinal and poisonous salts. It is toxic and an irritant to the skin and the mucous membranes.
An agent that causes the production of physical defects in the developing embryo.
Oxidoreductases that specifically reduce arsenate ion to arsenite ion. Reduction of arsenate is a critical step for its biotransformation into a form that can be transported by ARSENITE TRANSPORTING ATPASES or complexed by specific sulfhydryl-containing proteins for the purpose of detoxification (METABOLIC DETOXIFICATION, DRUG). Arsenate reductases require reducing equivalents such as GLUTAREDOXIN or AZURIN.
Inorganic or organic compounds that contain arsenic.
Calcium-transporting ATPases found on the PLASMA MEMBRANE that catalyze the active transport of CALCIUM from the CYTOPLASM into the extracellular space. They play a role in maintaining a CALCIUM gradient across plasma membrane.
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 adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
A subgroup of aquaporins that transport WATER; GLYCEROL; and other small solutes across CELL MEMBRANES.
A schistosomicide possibly useful against other parasites. It has irritant emetic properties and may cause lethal cardiac toxicity among other adverse effects.
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.
Membrane proteins whose primary function is to facilitate the transport of positively charged molecules (cations) across a biological membrane.
The type species of gram negative bacteria in the genus ALCALIGENES, found in soil. It is non-pathogenic, non-pigmented, and used for the production of amino acids.
A large group of bacteria including those which oxidize ammonia or nitrite, metabolize sulfur and sulfur compounds, or deposit iron and/or manganese oxides.
A family in the order Chromatiales, class GAMMAPROTEOBACTERIA. These are haloalkaliphilic, phototrophic bacteria that deposit elemental sulfur outside their cells.
An enzyme that catalyzes the active transport system of sodium and potassium ions across the cell wall. Sodium and potassium ions are closely coupled with membrane ATPase which undergoes phosphorylation and dephosphorylation, thereby providing energy for transport of these ions against concentration gradients.
A species of extremely thermophilic, sulfur-reducing archaea. It grows at a maximum temperature of 95 degrees C. in marine or deep-sea geothermal areas.
Any spaces or cavities within a cell. They may function in digestion, storage, secretion, or excretion.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Integral membrane proteins that transport protons across a membrane. This transport can be linked to the hydrolysis of ADENOSINE TRIPHOSPHATE. What is referred to as proton pump inhibitors frequently is about POTASSIUM HYDROGEN ATPASE.
A plant genus of the family PTERIDACEAE. Members contain entkaurane DITERPENES. The name is similar to bracken fern (PTERIDIUM).
Calcium-transporting ATPases that catalyze the active transport of CALCIUM into the SARCOPLASMIC RETICULUM vesicles from the CYTOPLASM. They are primarily found in MUSCLE CELLS and play a role in the relaxation of MUSCLES.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
Disorders associated with acute or chronic exposure to compounds containing ARSENIC (ARSENICALS) which may be fatal. Acute oral ingestion is associated with gastrointestinal symptoms and an encephalopathy which may manifest as SEIZURES, mental status changes, and COMA. Chronic exposure is associated with mucosal irritation, desquamating rash, myalgias, peripheral neuropathy, and white transverse (Mees) lines in the fingernails. (Adams et al., Principles of Neurology, 6th ed, p1212)
A cadmium halide in the form of colorless crystals, soluble in water, methanol, and ethanol. It is used in photography, in dyeing, and calico printing, and as a solution to precipitate sulfides. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
The rate dynamics in chemical or physical systems.
The process of cleaving a chemical compound by the addition of a molecule of water.
A genus in the family BURKHOLDERIACEAE, comprised of many species. They are associated with a variety of infections including MENINGITIS; PERITONITIS; and URINARY TRACT INFECTIONS.
The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.
Oxyvanadium ions in various states of oxidation. They act primarily as ion transport inhibitors due to their inhibition of Na(+)-, K(+)-, and Ca(+)-ATPase transport systems. They also have insulin-like action, positive inotropic action on cardiac ventricular muscle, and other metabolic effects.
A family of gram-negative bacteria in the class BETAPROTEOBACTERIA. There are at least eight genera.
A heavy metal trace element with the atomic symbol Cu, atomic number 29, and atomic weight 63.55.
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.

Expression cloning for arsenite-resistance resulted in isolation of tumor-suppressor fau cDNA: possible involvement of the ubiquitin system in arsenic carcinogenesis. (1/104)

Arsenic is a human carcinogen whose mechanism of action is unknown. Previously, this laboratory demonstrated that arsenite acts as a comutagen by interfering with DNA repair, although a specific DNA repair enzyme sensitive to arsenite has not been identified. A number of stable arsenite-sensitive and arsenite-resistant sublines of Chinese hamster V79 cells have now been isolated. In order to gain understanding of possible targets for arsenite's action, one arsenite-resistant subline, As/R28A, was chosen as a donor for a cDNA expression library. The library from arsenite-induced As/R28A cells was transfected into arsenite-sensitive As/S5 cells, and transfectants were selected for arsenite-resistance. Two cDNAs, asr1 and asr2, which confer arsenite resistance to arsenite-hypersensitive As/S5 cells as well as to wild-type cells, were isolated. asr1 shows almost complete homology with the rat fau gene, a tumor suppressor gene which contains a ubiquitin-like region fused to S30 ribosomal protein. Arsenite was previously shown to inhibit ubiquitin-dependent proteolysis. These results suggest that the tumor suppressor fau gene product or some other aspect of the ubiquitin system may be a target for arsenic toxicity and that disruption of the ubiquitin system may contribute to the genotoxicity and carcinogenicity of arsenite.  (+info)

Asp45 is a Mg2+ ligand in the ArsA ATPase. (2/104)

The ATPase activity of ArsA, the catalytic subunit of the plasmid-encoded, ATP-dependent extrusion pump for arsenicals and antimonials in Escherichia coli, is allosterically activated by arsenite or antimonite. Magnesium is essential for ATPase activity. To examine the role of Asp45, mutants were constructed in which Asp45 was changed to Glu, Asn, or Ala. Cells expressing these mutated arsA genes lost arsenite resistance to varying degrees. Purified D45A and D45N enzymes were inactive. The purified D45E enzyme exhibited approximately 5% of the wild type activity with about a 5-fold decrease in affinity for Mg2+. Intrinsic tryptophan fluorescence was used to probe Mg2+ binding. ArsA containing only Trp159 exhibited fluorescence enhancement upon the addition of MgATP, which was absent in D45N and D45A. As another measure of conformation, limited trypsin digestion was used to estimate the surface accessibility of residues in ArsA. ATP and Sb(III) synergistically protected wild type ArsA from trypsin digestion. Subsequent addition of Mg2+ increased trypsin sensitivity. D45N and D45A remained protected by ATP and Sb(III) but lost the Mg2+ effect. D45E exhibited an intermediate Mg2+ response. These results indicate that Asp45 is a Mg2+-responsive residue, consistent with its function as a Mg2+ ligand.  (+info)

The ATPase mechanism of ArsA, the catalytic subunit of the arsenite pump. (3/104)

The ArsA ATPase is the catalytic subunit of a novel arsenite pump, with two nucleotide-binding consensus sequences in the N- and C-terminal halves of the protein. The single tryptophan-containing Trp159 ArsA was used to elucidate the elementary steps of the ATPase mechanism by fluorescence stopped-flow experiments. The binding and hydrolysis of MgATP is a multistep process with a minimal kinetic mechanism (Mechanism 1). A notable feature of the reaction is that MgATP binding induces a slow transient increase in fluorescence of ArsA, which is independent of the ATP concentration, indicative of the build-up of a pre-steady state intermediate. This finding, coupled with a phosphate burst, implies that the steady-state intermediate builds up subsequent to product release. We propose that the rate-limiting step is an isomerization between different conformational forms of ArsA. kcat is faster than the phosphate burst, indicating that both nucleotide binding sites of ArsA are catalytic. Consistent with this interpretation, approximately 2 mol of phosphate are released per mole of ArsA during the phosphate burst.  (+info)

The anion-stimulated ATPase ArsA shows unisite and multisite catalytic activity. (4/104)

ArsA, an anion-stimulated ATPase, consists of two nucleotide binding domains, A1 in the N terminus and A2 in the C terminus of the protein, connected by a linker. The A1 domain contains a high affinity ATP binding site, whereas the A2 domain has low affinity and it requires the allosteric ligand antimonite for binding ATP. ArsA is known to form a UV-activated adduct with [alpha-(32)P]ATP in the linker region. This study shows that on addition of antimonite, much more adduct is formed. Characterization of the nature of the adduct suggests that it is between ArsA and ADP, instead of ATP, indicating that the adduct formation reflects hydrolysis of ATP. The present study also demonstrates that the A1 domain is capable of carrying out unisite catalysis in the absence of antimonite. On addition of antimonite, multisite catalysis involving both A1 and A2 sites occurs, resulting in a 40-fold increase in ATPase activity. Studies with mutant proteins suggest that the A2 site may be second in the sequence of events, so that its role in catalysis is dependent on a functional A1 site. It is also proposed that ArsA goes through an ATP-bound and an ADP-bound conformation, and the linker region, where ADP binds under both unisite and multisite catalytic conditions, may play an important role in the energy transduction process.  (+info)

Studies on the ADP-ribose pyrophosphatase subfamily of the nudix hydrolases and tentative identification of trgB, a gene associated with tellurite resistance. (5/104)

Four Nudix hydrolase genes, ysa1 from Saccharomyces cerevisiae, orf209 from Escherichia coli, yqkg from Bacillus subtilis, and hi0398 from Hemophilus influenzae were amplified, cloned into an expression vector, and transformed into E. coli. The expressed proteins were purified and shown to belong to a subfamily of Nudix hydrolases active on ADP-ribose. Comparison with other members of the subfamily revealed a conserved proline 16 amino acid residues downstream of the Nudix box, common to all of the ADP-ribose pyrophosphatase subfamily. In this same region, a conserved tyrosine designates another subfamily, the diadenosine polyphosphate pyrophosphatases, while an array of eight conserved amino acids is indicative of the NADH pyrophosphatases. On the basis of these classifications, the trgB gene, a tellurite resistance factor from Rhodobacter sphaeroides, was predicted to designate an ADP-ribose pyrophosphatase. In support of this hypothesis, a highly specific ADP-ribose pyrophosphatase gene from the archaebacterium, Methanococcus jannaschii, introduced into E. coli, increased the transformant's tolerance to potassium tellurite.  (+info)

Mechanism of the ArsA ATPase. (6/104)

The ArsAB ATPase confers metalloid resistance in Escherichia coli by pumping toxic anions out of the cells. This transport ATPase shares structural and perhaps mechanism features with ABC transporters. The ArsAB pump is composed of a membrane subunit that has two groups of six transmembrane segments, and the catalytic subunit, the ArsA ATPase. As is the case with many ABC transporters, ArsA has an internal repeat, each with an ATP binding domain, and is allosterically activated by substrates of the pump. The mechanism of allosteric activation of the ArsA ATPase has been elucidated at the molecular level. Binding of the activator produces a conformational change that forms a tight interface of the nucleotide binding domains. In the rate-limiting step in the overall reaction, the enzyme undergoes a slow conformational change. The allosteric activator accelerates catalysis by increasing the velocity of this rate-limiting step. We postulate that similar conformational changes may be rate-limiting in the mechanism of ABC transporters.  (+info)

Trimeric ring-like structure of ArsA ATPase. (7/104)

ArsA protein is the soluble subunit of the Ars anion pump in the Escherichia coli membrane which extrudes arsenite or antimonite from the cytoplasm. The molecular weight of the subunit is 63 kDa. In the cell it hydrolyzes ATP, and the energy released is used by the membrane-bound subunit ArsB to transport the substrates across the membrane. We have obtained two-dimensional crystals of ArsA in the presence of arsenite on negatively-charged lipid monolayer composed of DMPS and DOPC. These crystals have been studied using electron microscopy of negatively-stained specimens followed by image processing. The projection map obtained at 2.4 nm resolution reveals a ring-like structure with threefold symmetry. Many molecular assemblies with the same ring-shape and dimensions were also seen dispersed on electron microscopy grids, prepared directly from purified ArsA protein solution. Size-exclusion chromatography of the protein sample with arsenite present revealed that the majority of the protein particles in solution have a molecular weight of about 180 kDa. Based on these experiments, we conclude that in solution the ArsA ATPase with substrate bound is mainly in a trimeric form.  (+info)

The chromosomal arsenic resistance genes of Thiobacillus ferrooxidans have an unusual arrangement and confer increased arsenic and antimony resistance to Escherichia coli. (8/104)

The chromosomal arsenic resistance genes of the acidophilic, chemolithoautotrophic, biomining bacterium Thiobacillus ferrooxidans were cloned and sequenced. Homologues of four arsenic resistance genes, arsB, arsC, arsH, and a putative arsR gene, were identified. The T. ferrooxidans arsB (arsenite export) and arsC (arsenate reductase) gene products were functional when they were cloned in an Escherichia coli ars deletion mutant and conferred increased resistance to arsenite, arsenate, and antimony. Therefore, despite the fact that the ars genes originated from an obligately acidophilic bacterium, they were functional in E. coli. Although T. ferrooxidans is gram negative, its ArsC was more closely related to the ArsC molecules of gram-positive bacteria. Furthermore, a functional trxA (thioredoxin) gene was required for ArsC-mediated arsenate resistance in E. coli; this finding confirmed the gram-positive ArsC-like status of this resistance and indicated that the division of ArsC molecules based on Gram staining results is artificial. Although arsH was expressed in an E. coli-derived in vitro transcription-translation system, ArsH was not required for and did not enhance arsenic resistance in E. coli. The T. ferrooxidans ars genes were arranged in an unusual manner, and the putative arsR and arsC genes and the arsBH genes were translated in opposite directions. This divergent orientation was conserved in the four T. ferrooxidans strains investigated.  (+info)

Arsenites are inorganic compounds that contain arsenic in the trivalent state (arsenic-III). They are formed by the reaction of arsenic trioxide (As2O3) or other trivalent arsenic compounds with bases such as sodium hydroxide, potassium hydroxide, or ammonia.

The most common and well-known arsenite is sodium arsenite (NaAsO2), which has been used in the past as a wood preservative and pesticide. However, due to its high toxicity and carcinogenicity, its use has been largely discontinued. Other examples of arsenites include potassium arsenite (KAsO2) and calcium arsenite (Ca3(AsO3)2).

Arsenites are highly toxic and can cause a range of health effects, including skin irritation, nausea, vomiting, diarrhea, abdominal pain, and death in severe cases. Long-term exposure to arsenites has been linked to an increased risk of cancer, particularly lung, bladder, and skin cancer.

Sodium compounds are chemical substances that contain the element sodium (Na) combined with one or more other elements. Sodium is an alkali metal and is highly reactive, so it rarely exists in its pure form in nature. Instead, it is typically found combined with other elements in the form of various sodium compounds.

Some common examples of sodium compounds include:

* Sodium chloride (NaCl), also known as table salt, which is a compound formed from the reaction between sodium and chlorine.
* Sodium bicarbonate (NaHCO3), also known as baking soda, which is used as a leavening agent in baking and as a household cleaner.
* Sodium hydroxide (NaOH), also known as lye, which is a strong alkali used in industrial applications such as the manufacture of soap and paper.
* Sodium carbonate (Na2CO3), also known as washing soda, which is used as a water softener and cleaning agent.

Sodium compounds have a variety of uses in medicine, including as electrolytes to help maintain fluid balance in the body, as antacids to neutralize stomach acid, and as laxatives to relieve constipation. However, it is important to use sodium compounds as directed by a healthcare professional, as excessive intake can lead to high blood pressure and other health problems.

Arsenite transporting ATPases are a type of membrane-bound enzyme complexes that use the energy from ATP hydrolysis to actively transport arsenic compounds across cell membranes. They are part of the P-type ATPase family and play a crucial role in detoxifying cells by removing arsenite (AsIII) ions, which are highly toxic even at low concentrations.

These enzymes consist of two main domains: a cytoplasmic domain responsible for ATP binding and hydrolysis, and a transmembrane domain that contains the ion transport pathway. The transport process involves several conformational changes in the protein structure, driven by ATP hydrolysis, which ultimately result in the movement of arsenite ions against their concentration gradient from the cytoplasm to the extracellular space or into organelles like vacuoles and endosomes.

In humans, there are two main isoforms of arsenite transporting ATPases: ACR3 (also known as ARS-A) and ACR2 (or ARS-B). Both isoforms have been identified in various tissues, including the liver, kidney, and intestine. Mutations in these genes can lead to impaired arsenic detoxification and increased susceptibility to arsenic toxicity.

Overall, arsenite transporting ATPases are essential for maintaining cellular homeostasis and protecting organisms from the harmful effects of environmental arsenic exposure.

Adenosine triphosphatases (ATPases) are a group of enzymes that catalyze the conversion of adenosine triphosphate (ATP) into adenosine diphosphate (ADP) and inorganic phosphate. This reaction releases energy, which is used to drive various cellular processes such as muscle contraction, transport of ions across membranes, and synthesis of proteins and nucleic acids.

ATPases are classified into several types based on their structure, function, and mechanism of action. Some examples include:

1. P-type ATPases: These ATPases form a phosphorylated intermediate during the reaction cycle and are involved in the transport of ions across membranes, such as the sodium-potassium pump and calcium pumps.
2. F-type ATPases: These ATPases are found in mitochondria, chloroplasts, and bacteria, and are responsible for generating a proton gradient across the membrane, which is used to synthesize ATP.
3. V-type ATPases: These ATPases are found in vacuolar membranes and endomembranes, and are involved in acidification of intracellular compartments.
4. A-type ATPases: These ATPases are found in the plasma membrane and are involved in various functions such as cell signaling and ion transport.

Overall, ATPases play a crucial role in maintaining the energy balance of cells and regulating various physiological processes.

Arsenates are salts or esters of arsenic acid (AsO4). They contain the anion AsO4(3-), which consists of an arsenic atom bonded to four oxygen atoms in a tetrahedral arrangement. Arsenates can be found in various minerals, and they have been used in pesticides, wood preservatives, and other industrial applications. However, arsenic is highly toxic to humans and animals, so exposure to arsenates should be limited. Long-term exposure to arsenic can cause skin lesions, cancer, and damage to the nervous system, among other health problems.

Arsenic is a naturally occurring semi-metal element that can be found in the earth's crust. It has the symbol "As" and atomic number 33 on the periodic table. Arsenic can exist in several forms, including inorganic and organic compounds. In its pure form, arsenic is a steel-gray, shiny solid that is brittle and easily pulverized.

Arsenic is well known for its toxicity to living organisms, including humans. Exposure to high levels of arsenic can cause various health problems, such as skin lesions, neurological damage, and an increased risk of cancer. Arsenic can enter the body through contaminated food, water, or air, and it can also be absorbed through the skin.

In medicine, arsenic has been used historically in the treatment of various diseases, including syphilis and parasitic infections. However, its use as a therapeutic agent is limited due to its toxicity. Today, arsenic trioxide is still used as a chemotherapeutic agent for the treatment of acute promyelocytic leukemia (APL), a type of blood cancer. The drug works by inducing differentiation and apoptosis (programmed cell death) in APL cells, which contain a specific genetic abnormality. However, its use is closely monitored due to the potential for severe side effects and toxicity.

Proton-translocating ATPases are complex, multi-subunit enzymes found in the membranes of many organisms, from bacteria to humans. They play a crucial role in energy transduction processes within cells.

In simpler terms, these enzymes help convert chemical energy into a form that can be used to perform mechanical work, such as moving molecules across membranes against their concentration gradients. This is achieved through a process called chemiosmosis, where the movement of ions (in this case, protons or hydrogen ions) down their electrochemical gradient drives the synthesis of ATP, an essential energy currency for cellular functions.

Proton-translocating ATPases consist of two main domains: a catalytic domain responsible for ATP binding and hydrolysis, and a membrane domain that contains the ion transport channel. The enzyme operates in either direction depending on the energy status of the cell: it can use ATP to pump protons out of the cell when there's an excess of chemical energy or utilize the proton gradient to generate ATP during times of energy deficit.

These enzymes are essential for various biological processes, including nutrient uptake, pH regulation, and maintaining ion homeostasis across membranes. In humans, they are primarily located in the inner mitochondrial membrane (forming the F0F1-ATP synthase) and plasma membranes of certain cells (as V-type ATPases). Dysfunction of these enzymes has been linked to several diseases, including neurological disorders and cancer.

Calcium-transporting ATPases, also known as calcium pumps, are a type of enzyme that use the energy from ATP (adenosine triphosphate) hydrolysis to transport calcium ions across membranes against their concentration gradient. This process helps maintain low intracellular calcium concentrations and is essential for various cellular functions, including muscle contraction, neurotransmitter release, and gene expression.

There are two main types of calcium-transporting ATPases: the sarcoplasmic/endoplasmic reticulum Ca^2+^-ATPase (SERCA) and the plasma membrane Ca^2+^-ATPase (PMCA). SERCA is found in the sarcoplasmic reticulum of muscle cells and endoplasmic reticulum of other cell types, where it pumps calcium ions into these organelles to initiate muscle relaxation or signal transduction. PMCA, on the other hand, is located in the plasma membrane and extrudes calcium ions from the cell to maintain low cytosolic calcium concentrations.

Calcium-transporting ATPases play a crucial role in maintaining calcium homeostasis in cells and are important targets for drug development in various diseases, including heart failure, hypertension, and neurological disorders.

Vacuolar Proton-Translocating ATPases (V-ATPases) are complex enzyme systems that are found in the membranes of various intracellular organelles, such as vacuoles, endosomes, lysosomes, and Golgi apparatus. They play a crucial role in the establishment and maintenance of electrochemical gradients across these membranes by actively pumping protons (H+) from the cytosol to the lumen of the organelles.

The V-ATPases are composed of two major components: a catalytic domain, known as V1, which contains multiple subunits and is responsible for ATP hydrolysis; and a membrane-bound domain, called V0, which consists of several subunits and facilitates proton translocation. The energy generated from ATP hydrolysis in the V1 domain is used to drive conformational changes in the V0 domain, resulting in the vectorial transport of protons across the membrane.

These electrochemical gradients established by V-ATPases are essential for various cellular processes, including secondary active transport, maintenance of organellar pH, protein sorting and trafficking, and regulation of cell volume. Dysfunction in V-ATPases has been implicated in several human diseases, such as neurodegenerative disorders, renal tubular acidosis, and certain types of cancer.

Ion pumps, also known as ion transporters, are membrane-bound proteins that actively transport ions across a biological membrane against their electrochemical gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate), and allows cells to maintain resting potentials, regulate intracellular ion concentrations, and facilitate various physiological processes such as nerve impulse transmission, muscle contraction, and cell volume regulation.

Ion pumps can transport one or more types of ions, including sodium (Na+), potassium (K+), chloride (Cl-), calcium (Ca2+), and protons (H+). A well-known example of an ion pump is the Na+/K+ ATPase, which transports three sodium ions out of the cell and two potassium ions into the cell for each ATP molecule hydrolyzed. This creates a concentration gradient that drives the passive transport of Na+ and K+ ions through other channels, contributing to the resting membrane potential.

Antimony is a toxic metallic element with the symbol Sb and atomic number 51. It exists in several allotropic forms and can be found naturally as the mineral stibnite. Antimony has been used for centuries in various applications, including medicinal ones, although its use in medicine has largely fallen out of favor due to its toxicity.

In a medical context, antimony may still be encountered in certain medications used to treat parasitic infections, such as pentavalent antimony compounds (e.g., sodium stibogluconate and meglumine antimoniate) for the treatment of leishmaniasis. However, these drugs can have significant side effects and their use is typically reserved for severe cases that cannot be treated with other medications.

It's important to note that exposure to antimony in high concentrations or over prolonged periods can lead to serious health issues, including respiratory problems, skin irritation, gastrointestinal symptoms, and even neurological damage. Therefore, handling antimony-containing substances should be done with caution and appropriate safety measures.

Teratogens are substances, such as certain medications, chemicals, or infectious agents, that can cause birth defects or abnormalities in the developing fetus when a woman is exposed to them during pregnancy. They can interfere with the normal development of the fetus and lead to a range of problems, including physical deformities, intellectual disabilities, and sensory impairments. Examples of teratogens include alcohol, tobacco smoke, some prescription medications, and infections like rubella (German measles). It is important for women who are pregnant or planning to become pregnant to avoid exposure to known teratogens as much as possible.

Arsenate reductases are enzymes that catalyze the reduction of arsenate (As(V)) to arsenite (As(III)). This reaction is a critical step in the detoxification process of arsenic compounds in many organisms, including bacteria, fungi, and plants. The enzyme typically uses thioredoxin or glutaredoxin as an electron donor to reduce arsenate.

The medical significance of arsenate reductases lies in their role in arsenic detoxification and resistance. Exposure to high levels of arsenic can lead to a variety of health issues, including skin lesions, cancer, and neurological disorders. Understanding the mechanisms of arsenate reduction and detoxification may provide insights into new strategies for treating arsenic poisoning and developing environmental remediation technologies.

Arsenicals are a group of chemicals that contain arsenic, a naturally occurring element that is toxic to humans and animals. Arsenic can combine with other elements such as chlorine, sulfur, or carbon to form various inorganic and organic compounds known as arsenicals. These compounds have been used in a variety of industrial and agricultural applications, including wood preservatives, pesticides, and herbicides.

Exposure to high levels of arsenic can cause serious health effects, including skin damage, circulatory problems, and increased risk of cancer. Long-term exposure to lower levels of arsenic can also lead to chronic health issues, such as neurological damage and diabetes. Therefore, the use of arsenicals is regulated in many countries to minimize human and environmental exposure.

Plasma Membrane Calcium-Transporting ATPases (PMCA) are a type of P-type transmembrane transport proteins located in the plasma membrane of cells. They play a crucial role in maintaining calcium homeostasis within the cell by actively pumping calcium ions (Ca2+) out of the cytoplasm and into the extracellular space, using the energy derived from ATP hydrolysis. This process helps to reduce the intracellular Ca2+ concentration, which is essential for various cellular functions, including signal transduction, muscle contraction, neurotransmitter release, and gene expression. There are four different genes (ATP2B1-4) encoding PMCA isoforms (PMCA1-4), each with distinct expression patterns and biochemical properties, allowing for fine-tuning of calcium regulation in various tissues and cell types.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Adenosine Triphosphate (ATP) is a high-energy molecule that stores and transports energy within cells. It is the main source of energy for most cellular processes, including muscle contraction, nerve impulse transmission, and protein synthesis. ATP is composed of a base (adenine), a sugar (ribose), and three phosphate groups. The bonds between these phosphate groups contain a significant amount of energy, which can be released when the bond between the second and third phosphate group is broken, resulting in the formation of adenosine diphosphate (ADP) and inorganic phosphate. This process is known as hydrolysis and can be catalyzed by various enzymes to drive a wide range of cellular functions. ATP can also be regenerated from ADP through various metabolic pathways, such as oxidative phosphorylation or substrate-level phosphorylation, allowing for the continuous supply of energy to cells.

Aquaglyceroporins are a subfamily of aquaporin water channels that also transport glycerol and other small solutes across biological membranes. They play important roles in various physiological processes, including osmoregulation, skin hydration, and fat metabolism. In humans, there are three known aquaglyceroporins: AQP3, AQP7, and AQP9.

Antimony potassium tartrate is an inorganic compound with the chemical formula KSbC4H4O7. It is a white crystalline solid that is soluble in water and has been used historically in medical treatments, most notably in the treatment of leishmaniasis, a parasitic disease. However, due to its potential toxicity and the availability of safer alternatives, it is no longer commonly used in modern medicine.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Cation transport proteins are a type of membrane protein that facilitate the movement of cations (positively charged ions) across biological membranes. These proteins play a crucial role in maintaining ion balance and electrical excitability within cells, as well as in various physiological processes such as nutrient uptake, waste elimination, and signal transduction.

There are several types of cation transport proteins, including:

1. Ion channels: These are specialized protein structures that form a pore or channel through the membrane, allowing ions to pass through rapidly and selectively. They can be either voltage-gated or ligand-gated, meaning they open in response to changes in electrical potential or binding of specific molecules, respectively.

2. Ion pumps: These are active transport proteins that use energy from ATP hydrolysis to move ions against their electrochemical gradient, effectively pumping them from one side of the membrane to the other. Examples include the sodium-potassium pump (Na+/K+-ATPase) and calcium pumps (Ca2+ ATPase).

3. Ion exchangers: These are antiporter proteins that facilitate the exchange of one ion for another across the membrane, maintaining electroneutrality. For example, the sodium-proton exchanger (NHE) moves a proton into the cell in exchange for a sodium ion being moved out.

4. Symporters: These are cotransporter proteins that move two or more ions together in the same direction, often coupled with the transport of a solute molecule. An example is the sodium-glucose cotransporter (SGLT), which facilitates glucose uptake into cells by coupling its movement with that of sodium ions.

Collectively, cation transport proteins help maintain ion homeostasis and contribute to various cellular functions, including electrical signaling, enzyme regulation, and metabolic processes. Dysfunction in these proteins can lead to a range of diseases, such as neurological disorders, cardiovascular disease, and kidney dysfunction.

*Alcaligenes faecalis* is a species of gram-negative, rod-shaped bacteria that is commonly found in the environment, including soil, water, and the gastrointestinal tracts of animals. It is a facultative anaerobe, which means it can grow in both aerobic (with oxygen) and anaerobic (without oxygen) conditions.

The bacteria are generally not harmful to healthy individuals, but they have been associated with various types of infections in people with weakened immune systems or underlying medical conditions. These infections can include urinary tract infections, wound infections, pneumonia, and bacteremia (bloodstream infections).

*Alcaligenes faecalis* is resistant to many antibiotics, which can make treating infections caused by this bacteria challenging. It is important to identify the specific species of bacteria causing an infection so that appropriate antibiotic therapy can be administered.

Gram-negative chemolithotrophic bacteria are a type of bacteria that obtain energy by oxidizing inorganic substances, such as nitrogen, sulfur, or iron compounds, in a process called chemolithotrophy. They are classified as gram-negative because they do not retain the crystal violet stain used in the Gram staining method, which is a technique used to classify bacteria based on their cell wall structure.

Gram-negative bacteria have a thin peptidoglycan layer and an outer membrane containing lipopolysaccharides (LPS), which make them more resistant to certain antibiotics and chemical agents. The term "chemolithotrophic" refers to their ability to use inorganic chemicals as a source of energy, and they are often found in environments with high concentrations of these substances, such as soil, water, and waste treatment facilities.

Examples of gram-negative chemolithotrophic bacteria include species of the genera Nitrosomonas, Nitrobacter, Thiobacillus, and Sulfurimonas, among others. These bacteria play important roles in the global nitrogen and sulfur cycles, contributing to the oxidation of ammonia to nitrite (Nitrosomonas) or nitrite to nitrate (Nitrobacter), and the oxidation of sulfide or elemental sulfur to sulfuric acid (Thiobacillus).

Ectothiorhodospiraceae is a family of purple sulfur bacteria, which are characterized by their ability to perform anoxygenic photosynthesis using bacteriochlorophyll a or b. These bacteria typically contain intracytoplasmic membranes and use reduced sulfur compounds as electron donors during photosynthesis. They are often found in hypersaline environments, such as salt lakes and salt pans, where they play an important role in the biogeochemical cycling of sulfur and carbon.

The name "Ectothiorhodospiraceae" comes from the Greek words "ectos," meaning outside, and "thio," meaning sulfur, and "spirillum," meaning a spiral-shaped bacterium. This reflects the fact that these bacteria form external sulfur deposits during photosynthesis.

It's worth noting that medical professionals may not necessarily be familiar with this term, as it is more commonly used in the fields of microbiology and environmental science.

Sodium-Potassium-Exchanging ATPase (also known as Na+/K+ ATPase) is a type of active transporter found in the cell membrane of many types of cells. It plays a crucial role in maintaining the electrochemical gradient and membrane potential of animal cells by pumping sodium ions (Na+) out of the cell and potassium ions (K+) into the cell, using energy derived from ATP hydrolysis.

This transporter is composed of two main subunits: a catalytic α-subunit that contains the binding sites for Na+, K+, and ATP, and a regulatory β-subunit that helps in the proper targeting and functioning of the pump. The Na+/K+ ATPase plays a critical role in various physiological processes, including nerve impulse transmission, muscle contraction, and kidney function.

In summary, Sodium-Potassium-Exchanging ATPase is an essential membrane protein that uses energy from ATP to transport sodium and potassium ions across the cell membrane, thereby maintaining ionic gradients and membrane potentials necessary for normal cellular function.

'Archaeoglobus fulgidus' is a species of archaea, which are single-celled microorganisms that share some characteristics with bacteria but are genetically and biochemically distinct. This particular species is extremophilic, meaning it thrives in extreme environments that are hostile to most other life forms.

'Archaeoglobus fulgidus' is found in deep-sea hydrothermal vents and oil reservoirs, where it exists under high temperatures (up to 92°C) and high pressures. It is a sulfate-reducing organism, which means it obtains energy by reducing sulfates to hydrogen sulfide, using organic compounds as electron donors. This process plays a significant role in the global sulfur cycle and the anaerobic degradation of organic matter in extreme environments.

The study of 'Archaeoglobus fulgidus' and other archaea has provided valuable insights into the evolution and diversity of life on Earth, as well as the biochemical adaptations that allow organisms to survive under extreme conditions.

Vacuoles are membrane-bound organelles found in the cells of most eukaryotic organisms. They are essentially fluid-filled sacs that store various substances, such as enzymes, waste products, and nutrients. In plants, vacuoles often contain water, ions, and various organic compounds, while in fungi, they may store lipids or pigments. Vacuoles can also play a role in maintaining the turgor pressure of cells, which is critical for cell shape and function.

In animal cells, vacuoles are typically smaller and less numerous than in plant cells. Animal cells have lysosomes, which are membrane-bound organelles that contain digestive enzymes and break down waste materials, cellular debris, and foreign substances. Lysosomes can be considered a type of vacuole, but they are more specialized in their function.

Overall, vacuoles are essential for maintaining the health and functioning of cells by providing a means to store and dispose of various substances.

A cell membrane, also known as the plasma membrane, is a thin semi-permeable phospholipid bilayer that surrounds all cells in animals, plants, and microorganisms. It functions as a barrier to control the movement of substances in and out of the cell, allowing necessary molecules such as nutrients, oxygen, and signaling molecules to enter while keeping out harmful substances and waste products. The cell membrane is composed mainly of phospholipids, which have hydrophilic (water-loving) heads and hydrophobic (water-fearing) tails. This unique structure allows the membrane to be flexible and fluid, yet selectively permeable. Additionally, various proteins are embedded in the membrane that serve as channels, pumps, receptors, and enzymes, contributing to the cell's overall functionality and communication with its environment.

A proton pump is a specialized protein structure that functions as an enzyme, known as a proton pump ATPase, which actively transports hydrogen ions (protons) across a membrane. This process creates a gradient of hydrogen ions, resulting in an electrochemical potential difference, also known as a proton motive force. The main function of proton pumps is to generate and maintain this gradient, which can be used for various purposes, such as driving the synthesis of ATP (adenosine triphosphate) or transporting other molecules against their concentration gradients.

In the context of gastric physiology, the term "proton pump" often refers to the H+/K+-ATPase present in the parietal cells of the stomach. This proton pump is responsible for secreting hydrochloric acid into the stomach lumen, contributing to the digestion and sterilization of ingested food. Inhibiting this specific proton pump with medications like proton pump inhibitors (PPIs) is a common treatment strategy for gastric acid-related disorders such as gastroesophageal reflux disease (GERD), peptic ulcers, and Zollinger-Ellison syndrome.

I apologize for any confusion, but "Pteris" is not a medical term. It is the name of a genus of ferns, commonly known as brake ferns or table ferns. If you have any questions about a medical term or concept, please provide it, and I would be happy to help define it for you.

Sarcoplasmic Reticulum Calcium-Transporting ATPases (SERCA) are a type of calcium pumps that are located in the sarcoplasmic reticulum (SR) of muscle cells. They play a crucial role in excitation-contraction coupling, which is the process by which muscles contract and relax.

During muscle contraction, calcium ions (Ca2+) are released from the SR into the cytosol, triggering muscle fiber contraction. After the muscle fiber has contracted, Ca2+ must be actively transported back into the SR to allow the muscle fiber to relax. This is where SERCA comes in.

SERCA uses energy from ATP hydrolysis to transport Ca2+ against its concentration gradient from the cytosol back into the lumen of the SR. By doing so, it helps maintain low cytosolic Ca2+ concentrations and high SR Ca2+ concentrations, which are necessary for muscle relaxation and subsequent contraction.

There are several isoforms of SERCA, each with slightly different properties and tissue distributions. For example, SERCA1 is primarily found in fast-twitch skeletal muscle fibers, while SERCA2a is found in both slow-twitch and fast-twitch skeletal muscle fibers as well as cardiac muscle. Mutations in the genes encoding these pumps can lead to various muscle disorders, including certain forms of muscular dystrophy and heart failure.

"Saccharomyces cerevisiae" is not typically considered a medical term, but it is a scientific name used in the field of microbiology. It refers to a species of yeast that is commonly used in various industrial processes, such as baking and brewing. It's also widely used in scientific research due to its genetic tractability and eukaryotic cellular organization.

However, it does have some relevance to medical fields like medicine and nutrition. For example, certain strains of S. cerevisiae are used as probiotics, which can provide health benefits when consumed. They may help support gut health, enhance the immune system, and even assist in the digestion of certain nutrients.

In summary, "Saccharomyces cerevisiae" is a species of yeast with various industrial and potential medical applications.

Arsenic poisoning is a condition that occurs when a person ingests or comes into contact with a toxic amount of arsenic, a naturally occurring element found in the earth's crust. Arsenic has no smell or taste, making it difficult to detect in food, water, or air.

Acute arsenic poisoning can occur after a single large exposure to arsenic, while chronic arsenic poisoning occurs after repeated or long-term exposure to lower levels of arsenic. The symptoms of acute arsenic poisoning include vomiting, diarrhea, abdominal pain, and muscle cramps. In severe cases, it can lead to death due to heart failure or respiratory failure.

Chronic arsenic poisoning can cause a range of health problems, including skin changes such as pigmentation and hard patches on the palms and soles, weakness, peripheral neuropathy, and an increased risk of cancer, particularly skin, lung, bladder, and kidney cancer. It can also affect cognitive development in children.

Arsenic poisoning is treated by removing the source of exposure and providing supportive care to manage symptoms. Chelation therapy may be used to remove arsenic from the body in cases of severe acute poisoning or chronic poisoning with high levels of arsenic. Prevention measures include monitoring and reducing exposure to arsenic in food, water, and air, as well as proper handling and disposal of arsenic-containing products.

Cadmium chloride is an inorganic compound with the chemical formula CdCl2. It is a white crystalline solid that is highly soluble in water and has a bitter, metallic taste. Cadmium chloride is a toxic compound that can cause serious health effects, including kidney damage, respiratory problems, and bone degeneration. It is classified as a hazardous substance and should be handled with care.

Cadmium chloride is used in various industrial applications, such as electroplating, soldering, and as a stabilizer in plastics. It is also used in some research settings as a reagent in chemical reactions.

It's important to note that exposure to cadmium chloride should be avoided, and appropriate safety measures should be taken when handling this compound. This includes wearing protective clothing, such as gloves and lab coats, and working in a well-ventilated area or under a fume hood. In case of accidental ingestion or inhalation, seek medical attention immediately.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Hydrolysis is a chemical process, not a medical one. However, it is relevant to medicine and biology.

Hydrolysis is the breakdown of a chemical compound due to its reaction with water, often resulting in the formation of two or more simpler compounds. In the context of physiology and medicine, hydrolysis is a crucial process in various biological reactions, such as the digestion of food molecules like proteins, carbohydrates, and fats. Enzymes called hydrolases catalyze these hydrolysis reactions to speed up the breakdown process in the body.

"Ralstonia" is a genus of gram-negative, aerobic bacteria that are commonly found in soil and water. Some species of Ralstonia are known to cause healthcare-associated infections, particularly in patients with compromised immune systems. These infections can include pneumonia, bacteremia, and meningitis. One notable species, Ralstonia solanacearum, is a plant pathogen that causes bacterial wilt in a wide range of plants.

Ralstonia bacteria are known for their ability to form biofilms, which can make them resistant to antibiotics and disinfectants. They can also survive in harsh environments, such as those with low nutrient availability and high salt concentrations. These characteristics make Ralstonia a challenging organism to control in healthcare settings and in the environment.

It's important to note that while Ralstonia bacteria can cause serious infections, they are not typically considered highly virulent or contagious. Instead, infections are often associated with contaminated medical equipment or solutions, such as intravenous fluids, respiratory therapy equipment, and contaminated water sources. Proper infection control practices, including environmental cleaning and disinfection, can help prevent the spread of Ralstonia in healthcare settings.

Biological transport refers to the movement of molecules, ions, or solutes across biological membranes or through cells in living organisms. This process is essential for maintaining homeostasis, regulating cellular functions, and enabling communication between cells. There are two main types of biological transport: passive transport and active transport.

Passive transport does not require the input of energy and includes:

1. Diffusion: The random movement of molecules from an area of high concentration to an area of low concentration until equilibrium is reached.
2. Osmosis: The diffusion of solvent molecules (usually water) across a semi-permeable membrane from an area of lower solute concentration to an area of higher solute concentration.
3. Facilitated diffusion: The assisted passage of polar or charged substances through protein channels or carriers in the cell membrane, which increases the rate of diffusion without consuming energy.

Active transport requires the input of energy (in the form of ATP) and includes:

1. Primary active transport: The direct use of ATP to move molecules against their concentration gradient, often driven by specific transport proteins called pumps.
2. Secondary active transport: The coupling of the movement of one substance down its electrochemical gradient with the uphill transport of another substance, mediated by a shared transport protein. This process is also known as co-transport or counter-transport.

Vanadates are salts or esters of vanadic acid (HVO3), which contains the vanadium(V) ion. They contain the vanadate ion (VO3-), which consists of one vanadium atom and three oxygen atoms. Vanadates have been studied for their potential insulin-mimetic and antidiabetic effects, as well as their possible cardiovascular benefits. However, more research is needed to fully understand their mechanisms of action and potential therapeutic uses in medicine.

Oxalobacteraceae is a family of gram-negative, aerobic or facultatively anaerobic bacteria within the order Burkholderiales. The bacteria in this family are known for their ability to metabolize oxalate, a compound that is commonly found in many plant-based foods and can be harmful in large amounts. The type genus of this family is Oxalobacter, which includes species such as Oxalobacter formigenes, which is normally found in the human gut and helps to break down oxalates in the digestive system. Other genera in this family include Massilia, Janthinobacterium, and Herbaspirillum, among others.

Copper is a chemical element with the symbol Cu (from Latin: *cuprum*) and atomic number 29. It is a soft, malleable, and ductile metal with very high thermal and electrical conductivity. Copper is found as a free element in nature, and it is also a constituent of many minerals such as chalcopyrite and bornite.

In the human body, copper is an essential trace element that plays a role in various physiological processes, including iron metabolism, energy production, antioxidant defense, and connective tissue synthesis. Copper is found in a variety of foods, such as shellfish, nuts, seeds, whole grains, and organ meats. The recommended daily intake of copper for adults is 900 micrograms (mcg) per day.

Copper deficiency can lead to anemia, neutropenia, impaired immune function, and abnormal bone development. Copper toxicity, on the other hand, can cause nausea, vomiting, abdominal pain, diarrhea, and in severe cases, liver damage and neurological symptoms. Therefore, it is important to maintain a balanced copper intake through diet and supplements if necessary.

Saccharomyces cerevisiae proteins are the proteins that are produced by the budding yeast, Saccharomyces cerevisiae. This organism is a single-celled eukaryote that has been widely used as a model organism in scientific research for many years due to its relatively simple genetic makeup and its similarity to higher eukaryotic cells.

The genome of Saccharomyces cerevisiae has been fully sequenced, and it is estimated to contain approximately 6,000 genes that encode proteins. These proteins play a wide variety of roles in the cell, including catalyzing metabolic reactions, regulating gene expression, maintaining the structure of the cell, and responding to environmental stimuli.

Many Saccharomyces cerevisiae proteins have human homologs and are involved in similar biological processes, making this organism a valuable tool for studying human disease. For example, many of the proteins involved in DNA replication, repair, and recombination in yeast have human counterparts that are associated with cancer and other diseases. By studying these proteins in yeast, researchers can gain insights into their function and regulation in humans, which may lead to new treatments for disease.

Multienzyme complexes are specialized protein structures that consist of multiple enzymes closely associated or bound together, often with other cofactors and regulatory subunits. These complexes facilitate the sequential transfer of substrates along a series of enzymatic reactions, also known as a metabolic pathway. By keeping the enzymes in close proximity, multienzyme complexes enhance reaction efficiency, improve substrate specificity, and maintain proper stoichiometry between different enzymes involved in the pathway. Examples of multienzyme complexes include the pyruvate dehydrogenase complex, the citrate synthase complex, and the fatty acid synthetase complex.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

In enzymology, an arsenite-transporting ATPase (EC 3.6.3.16) is an enzyme that catalyzes the chemical reaction ATP + H2O + ... and arsenite, whereas its 3 products are ADP, phosphate, and arsenite. This enzyme belongs to the family of hydrolases, ... Arsenite-Antimonite efflux Silver S, Misra TK, Laddaga RA (1989). "DNA sequence analysis of bacterial toxic heavy metal ... The systematic name of this enzyme class is ATP phosphohydrolase (arsenite-exporting). As of late 2007, 3 structures have been ...
Arsenic toxicity Arsenite-transporting ATPase Solute carrier family Active transport ATP-binding cassette transporter Hasgekar ... Arsenite-antimonite transporters are membrane transporters that pump arsenite or antimonite out of a cell. Antimonite is the ... an ATPase, must be superimposed onto ArsB. Arsenite and antimonite can also be pumped out of the cell by members of the ARC3 ... which can participate in both secondary transport or primary active transport. Based on operon analyses, Arc3 homologues may ...
... arsenite-transporting ATPase * * No Wikipedia article EC 7.4.2.1: ABC-type polar-amino-acid transporter * EC 7.4.2.2: ABC-type ... mitochondrial protein-transporting ATPase * EC 7.4.2.4: chloroplast protein-transporting ATPase * EC 7.4.2.5: bacterial ABC- ... H+-transporting) * EC 7.1.1.4: caldariellaquinol oxidase (H+-transporting) * EC 7.1.1.5: menaquinol oxidase (H+-transporting ... Na+-transporting two-sector ATPase * EC 7.2.2.2: ABC-type Cd2+ transporter * EC 7.2.2.3: P-type Na+ transporter * EC 7.2.2.4: ...
... superfamily ARC3 family Arsenite-Antimonite efflux Arsenite-transporting ATPase Solute carrier family Active transport ATP- ... Arsenite or Antimonite (out). The overall reaction catalyzed by ArsB-ArsA is: Arsenite or Antimonite (in) + ATP ⇌ Arsenite or ... "Families of soft-metal-ion-transporting ATPases". Journal of Bacteriology. 181 (19): 5891-7. doi:10.1128/JB.181.19.5891- ... Arsenite resistance (Ars) efflux pumps of bacteria may consist of two proteins, ArsB (TC# 2.A.45.1.1; the integral membrane ...
V-type ATPase and A-type ATPase superfamily 3.A.3 The P-type ATPase Superfamily 3.A.4 The Arsenite-Antimonite efflux family 3.A ... Family 3.B.1 The Na+-transporting Carboxylic Acid Decarboxylase (NaT-DC) Family 3.C.1 The Na+ Transporting ... Family 1.D.58 The Anion Transporting Prodigiosene (Prodigiosene) Family 1.D.59 The Anion Transporting Perenosin (Perenosin) ... See electron transport chain. 3.D.1 The H+ or Na+-translocating NADH Dehydrogenase ("complex I") family 3.D.2 The Proton- ...
It is required for the detoxification of arsenate, arsenite, and antimonite. This system transports arsenite and antimonite out ... thus increasing its ATPase activity at lower concentrations of arsenite and enhancing the rate of arsenite extrusion. Carlin A ... This two-subunit enzyme produces resistance to arsenite and antimonite. Arsenate, however, must first be reduced to arsenite ... ArsA and ArsB form an anion-translocating ATPase. The ArsB protein is distinguished by its overall hydrophobic character, in ...
The Bacillus protein exports both arsenite and antimonite. The exact transport mechanism has not established. The generalized ... Homologous ATPases are found in families TC# 3.A.4, TC# 3.A.19 and TC# 3.A.21 as well as TC# 2.A.59. A region of the ABC ATPase ... In the latter case ATP hydrolysis again energizes transport. ARC3 homologues transport the same anions as ArsA/AB homologues, ... reaction catalyzed by members of the ACR3 family is: arsenite or antimonite (in) → arsenite or antimonite (out). Arsenite- ...
An underlying mechanism by which lead is able to cause harm is its ability to be transported by calcium ATPase pumps across the ... As a metabolite of arsenic, arsenite is formed after ingestion of arsenic and has shown significant toxicity to neurons within ... This is important as neurotransmitter transport can be impaired through vesicular transport inhibition, resulting in diminished ... This barrier creates a tight hydrophobic layer around the capillaries in the brain, inhibiting the transport of large or ...
Na+-transporting two-sector ATPase EC 3.6.3.16: Now EC 7.3.2.7, arsenite-transporting ATPase EC 3.6.3.17: Now covered by ... teichoic-acid-transporting ATPase EC 3.6.3.41: Now EC 7.6.2.5, heme-transporting ATPase EC 3.6.3.42: Now EC 7.5.2.3, β-glucan- ... fatty-acyl-CoA-transporting ATPase EC 3.6.3.48: Now EC 7.4.2.7 as α-factor-pheromone transporting ATPase EC 3.6.3.49: Now EC ... Na+/K+-exchanging ATPase EC 3.6.3.10: Now EC 7.2.2.19, H+/K+-exchanging ATPase EC 3.6.3.11: Cl--transporting ATPase. The ...
It has also been proposed that microtubules play a role in the formation of stress granules, perhaps by transporting granule ... Jain S, Wheeler JR, Walters RW, Agrawal A, Barsic A, Parker R (January 2016). "ATPase-Modulated Stress Granules Contain a ... June 2018). "ZFAND1 Recruits p97 and the 26S Proteasome to Promote the Clearance of Arsenite-Induced Stress Granules". ... In yeast, catalytic ded1 mutant alleles give rise to constitutive stress granules ATPase-deficient DDX3X (the mammalian homolog ...
Protons are transported across the membrane by the initial NADH reductase, quinones, and nitrous oxide reductase to produce the ... In all cases, however, a proton motive force is generated and used to drive ATP production via an ATPase. Most photosynthetic ... reduction to arsenite (AsO3− 3) Uranyl ion (UO2+ 2) reduction to uranium dioxide (UO 2) A number of organisms, instead of using ... This means that these organisms do not use an electron transport chain to oxidize NADH to NAD+ and therefore must have an ...
... metal transporting P1-type ATPases and a chemiosmotic antiporter efflux system similar to CzcCBA of Cupriavidus metallidurans. ... MM-1 isolated from a soil and identification of arsenite oxidase gene". Journal of Hazardous Materials. 262: 997-1003. doi: ... Bahar, Md Mezbaul; Megharaj, Mallavarapu; Naidu, Ravi (2013-11-15). "Kinetics of arsenite oxidation by Variovorax sp. ...
In enzymology, an arsenite-transporting ATPase (EC 3.6.3.16) is an enzyme that catalyzes the chemical reaction ATP + H2O + ... and arsenite, whereas its 3 products are ADP, phosphate, and arsenite. This enzyme belongs to the family of hydrolases, ... Arsenite-Antimonite efflux Silver S, Misra TK, Laddaga RA (1989). "DNA sequence analysis of bacterial toxic heavy metal ... The systematic name of this enzyme class is ATP phosphohydrolase (arsenite-exporting). As of late 2007, 3 structures have been ...
Arsenite-Translocating ATPase Arsenite-Transporting ATPase Registry Number. EC 3.6.3.16. Public MeSH Note. 2007; ARSENITE- ... ATPases Associated with Diverse Cellular Activities [D08.811.277.040.025.024] * Arsenite Transporting ATPases [D08.811.277.040. ... Cation Transport Proteins [D12.776.157.530.450.250] * Arsenite Transporting ATPases [D12.776.157.530.450.250.249] ... Cation Transport Proteins [D12.776.543.585.450.250] * Arsenite Transporting ATPases [D12.776.543.585.450.250.249] ...
ANION-TRANSLOCATING ATPASE * ARSENITE TRANSPORT * Biochemistry & Molecular Biology * GENES * Life Sciences & Biomedicine ...
Arsenite Transporting ATPases [D08.811.277.040.025.047] Arsenite Transporting ATPases * Ca(2+) Mg(2+)-ATPase [D08.811.277.040. ... ATPase. ATPase, DNA Dependent. ATPase, DNA-Dependent. ATPases. Adenosine Triphosphatase. Adenosinetriphosphatase. ... ATPase, DNA Dependent ATPase, DNA-Dependent Adenosinetriphosphatases, DNA-Dependent DNA Dependent ATPase DNA Dependent ... ATPases Associated with Diverse Cellular Activities [D08.811.277.040.025.024] ATPases Associated with Diverse Cellular ...
Arsenite Transporting ATPases. ATPases Transportadoras de Arsenito. ATPasas Transportadoras de Arsenitos. Caspase 10. Caspase ... Plasma Membrane Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio da Membrana Plasmática. ATPasas Transportadoras ... Sarcoplasmic Reticulum Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio do Retículo Sarcoplasmático. ATPasas ...
Arsenite Transporting ATPases. ATPases Transportadoras de Arsenito. ATPasas Transportadoras de Arsenitos. Caspase 10. Caspase ... Plasma Membrane Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio da Membrana Plasmática. ATPasas Transportadoras ... Sarcoplasmic Reticulum Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio do Retículo Sarcoplasmático. ATPasas ...
Arsenite Transporting ATPases. ATPases Transportadoras de Arsenito. ATPasas Transportadoras de Arsenitos. Caspase 10. Caspase ... Plasma Membrane Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio da Membrana Plasmática. ATPasas Transportadoras ... Sarcoplasmic Reticulum Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio do Retículo Sarcoplasmático. ATPasas ...
Arsenite Transporting ATPases. ATPases Transportadoras de Arsenito. ATPasas Transportadoras de Arsenitos. Caspase 10. Caspase ... Plasma Membrane Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio da Membrana Plasmática. ATPasas Transportadoras ... Sarcoplasmic Reticulum Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio do Retículo Sarcoplasmático. ATPasas ...
Arsenite Transporting ATPases. ATPases Transportadoras de Arsenito. ATPasas Transportadoras de Arsenitos. Caspase 10. Caspase ... Plasma Membrane Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio da Membrana Plasmática. ATPasas Transportadoras ... Sarcoplasmic Reticulum Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio do Retículo Sarcoplasmático. ATPasas ...
Arsenite Transporting ATPases. ATPases Transportadoras de Arsenito. ATPasas Transportadoras de Arsenitos. Caspase 10. Caspase ... Plasma Membrane Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio da Membrana Plasmática. ATPasas Transportadoras ... Sarcoplasmic Reticulum Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio do Retículo Sarcoplasmático. ATPasas ...
Arsenite Transporting ATPases. ATPases Transportadoras de Arsenito. ATPasas Transportadoras de Arsenitos. Caspase 10. Caspase ... Plasma Membrane Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio da Membrana Plasmática. ATPasas Transportadoras ... Sarcoplasmic Reticulum Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio do Retículo Sarcoplasmático. ATPasas ...
Arsenite Transporting ATPases. ATPases Transportadoras de Arsenito. ATPasas Transportadoras de Arsenitos. Caspase 10. Caspase ... Plasma Membrane Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio da Membrana Plasmática. ATPasas Transportadoras ... Sarcoplasmic Reticulum Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio do Retículo Sarcoplasmático. ATPasas ...
Arsenite Transporting ATPases. ATPases Transportadoras de Arsenito. ATPasas Transportadoras de Arsenitos. Caspase 10. Caspase ... Plasma Membrane Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio da Membrana Plasmática. ATPasas Transportadoras ... Sarcoplasmic Reticulum Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio do Retículo Sarcoplasmático. ATPasas ...
Arsenite Transporting ATPases. ATPases Transportadoras de Arsenito. ATPasas Transportadoras de Arsenitos. Caspase 10. Caspase ... Plasma Membrane Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio da Membrana Plasmática. ATPasas Transportadoras ... Sarcoplasmic Reticulum Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio do Retículo Sarcoplasmático. ATPasas ...
Arsenite Transporting ATPases. ATPases Transportadoras de Arsenito. ATPasas Transportadoras de Arsenitos. Caspase 10. Caspase ... Plasma Membrane Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio da Membrana Plasmática. ATPasas Transportadoras ... Sarcoplasmic Reticulum Calcium-Transporting ATPases. ATPases Transportadoras de Cálcio do Retículo Sarcoplasmático. ATPasas ...
Arsenite Transporting ATPases. *Calcium-Transporting ATPases. *Copper-transporting ATPases. *Organic Cation Transport Proteins ... "Calcium-Transporting ATPases" by people in this website by year, and whether "Calcium-Transporting ATPases" was a major or ... "Calcium-Transporting ATPases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ... The conformation of H,K-ATPase determines the nucleoside triphosphate (NTP) selectivity for active proton transport. ...
Cation Transport Proteins. *Arsenite Transporting ATPases. *Calcium-Transporting ATPases. *Organic Cation Transport Proteins ... "Cation Transport Proteins" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... This graph shows the total number of publications written about "Cation Transport Proteins" by people in this website by year, ... Membrane proteins whose primary function is to facilitate the transport of positively charged molecules (cations) across a ...
ATPases Associated with Diverse Cellular Activities [D08.811.277.040.025.024] * Arsenite Transporting ATPases [D08.811.277.040. ... They consist of a conserved N-terminal region with weak ATPase activity, an endonuclease motif, and a C-terminal domain that ... They consist of a conserved N-terminal region with weak ATPase activity, an endonuclease motif, and a C-terminal domain that ...
Arsenite Transporting ATPases [D08.811.277.040.025.047] Arsenite Transporting ATPases * Ca(2+) Mg(2+)-ATPase [D08.811.277.040. ... ATPases Associated with Diverse Cellular Activities [D08.811.277.040.025.024] ATPases Associated with Diverse Cellular ... They consist of a conserved N-terminal region with weak ATPase activity, an endonuclease motif, and a C-terminal domain that ... They consist of a conserved N-terminal region with weak ATPase activity, an endonuclease motif, and a C-terminal domain that ...
Team:Groningen/Project/Transport#GlpF,GlpF]] is an aquaglyceroporin channel that facilitates the transport of As(III). his part ... HmtA (heavy metal transporter A) from Pseudomonas aeruginosa Q9I147 is a P-type ATPase importer. This membrane protein mediates ... fMT is a metallothionein, binding Arsenite(III) and Arsenate(V), it has higher affinity for As(III). As a metallothionein it is ... Team:Groningen/Project/Transport#HmtA,HmtA]] (heavy metal transporter A) from Pseudomonas aeruginosa Q9I147 is a P-type ...
ATPases Associated with Diverse Cellular Activities [D08.811.277.040.025.024] * Arsenite Transporting ATPases [D08.811.277.040. ... F(1)F(0)-ATPase F-0-ATPase F-1-ATPase F0F1 ATPase F1 ATPase F1-ATPase F1F0 ATPase Complex H(+)-ATPase H(+)-Transporting ATP ... H(+)-Transporting ATPase H(+)ATPase Complex H+ ATPase H+ Transporting ATP Synthase H+-Translocating ATPase Proton-Translocating ... for ATPASE, F0 see ATPASE F(0) 1984-1992; for ATPASE, F1 see ATPASE F1 1983-1992; for F1F0 ATPASE COMPLEX see H(+)-TRANSPORTING ...
... amino acid transport and metabolism; F, nucleotide transport and metabolism; G, carbohydrate transport and metabolism; H, ... ferrivorans SS3 genome (Supplementary Figure S2). In addition, genes encoding the arsenite transporter ArsB and another ... Copper resistance components: CopZ, putative cytoplasmic copper chaperone, CopA1 and CopB, copper-exporting P-type ATPases; ... coenzyme transport and metabolism; I, lipid transport and metabolism; J, translation, ribosomal structure, and biogenesis; K, ...
The NIPs transports neutral solutes like glycerol, lactic acid, ammonia, boric acid, arsenite, selenite, silicic acid, and ... ATPase activity (Liag 1999) but negatively regulates the Na uptake (Tuna et al. 2008). Silicon application during drought ... 1995). CDF and MTP transport family transport heavy metals to endoplasmic reticulum or apoplast and also they act as sensors ... genes under arsenite treatment revals that these Si transporters effectively serve as major entry path for arsenite transport. ...
ATPase Trocadora de Sódio-Potássio/antagonistas & inibidores , ATPase Trocadora de Sódio-Potássio/metabolismo , Sulfonamidas/ ... Besides, paracellular transport of zinc in BKO mice was compromised. Hepcidin administration completely restored calcium ... Activation of p38MAPK, by Sodium Arsenite or Anisomycin, mimicked the inhibitory effect of Sildenafil on the exchanger. ... ATPases Transportadoras de Cálcio da Membrana Plasmática/genética , ATPases Transportadoras de Cálcio da Membrana Plasmática/ ...
ArsA arsenite transporter, ATP-binding, homolog 1 (bacterial). ATP11A. ATPase phospholipid transporting 11A. ...
proton-transporting two-sector ATPase complex. IEP. Neighborhood. BP. GO:0016487. farnesol metabolic process. IEP. Neighborhood ... arsenite transmembrane transporter activity. IEP. Neighborhood. MF. GO:0015142. tricarboxylic acid transmembrane transporter ... proton-transporting two-sector ATPase complex, catalytic domain. IEP. Neighborhood. BP. GO:0033865. nucleoside bisphosphate ... ATPase activity, coupled. IEP. Neighborhood. MF. GO:0042625. ATPase coupled ion transmembrane transporter activity. IEP. ...
nucleocytoplasmic transport. IEP. Neighborhood. MF. GO:0008094. DNA-dependent ATPase activity. IEP. Neighborhood. ...
Arsenite Transporting ATPases [D08.811.277.040.025.047] Arsenite Transporting ATPases * Ca(2+) Mg(2+)-ATPase [D08.811.277.040. ... E1 E2 ATPases E1-E2 ATPase E1-E2 ATPases P Type Atpase P type ATPase P type ATPases P type Adenosine Triphosphatase P type ... E1 E2 ATPases. E1-E2 ATPase. E1-E2 ATPases. P Type Atpase. P type ATPase. P type ATPases. P type Adenosine Triphosphatase. P ... P-type ATPases Entry term(s). ATPase, P-type ATPases, E1-E2 ATPases, P-type ATPases, Phosphorylation-type Adenosine ...
DYRK3 phosphorylates SNAPIN to regulate axonal retrograde transport and neurotransmitter release. Lee, Y. H., Suh, B. K., Lee, ...
  • Efflux pumps that use the energy of ATP hydrolysis to pump arsenite across a membrane. (nih.gov)
  • The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. (bvsalud.org)
  • Expression of the sarco/endoplasmic Ca(2+)-ATPase, SERCA1a, in fibroblasts induces the formation of organelle membrane arrays. (jefferson.edu)
  • Membrane proteins whose primary function is to facilitate the transport of positively charged molecules (cations) across a biological membrane. (wakehealth.edu)
  • They are coupled to the transport of protons across a membrane. (nih.gov)
  • A highly conserved family of ATPases that facilitate the transport of lipids and cations across the plasma membrane. (bvsalud.org)
  • Cation Transport Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (wakehealth.edu)
  • This graph shows the total number of publications written about "Cation Transport Proteins" by people in this website by year, and whether "Cation Transport Proteins" was a major or minor topic of these publications. (wakehealth.edu)
  • Below are the most recent publications written about "Cation Transport Proteins" by people in Profiles. (wakehealth.edu)
  • In enzymology, an arsenite-transporting ATPase (EC 3.6.3.16) is an enzyme that catalyzes the chemical reaction ATP + H2O + arsenitein ⇌ {\displaystyle \rightleftharpoons } ADP + phosphate + arseniteout The 3 substrates of this enzyme are ATP, H2O, and arsenite, whereas its 3 products are ADP, phosphate, and arsenite. (wikipedia.org)
  • Function of endoplasmic reticulum calcium ATPase in innate immunity-mediated programmed cell death. (jefferson.edu)
  • ATPase sarcoplasmic/endoplasmic reticulu. (gsea-msigdb.org)
  • The systematic name of this enzyme class is ATP phosphohydrolase (arsenite-exporting). (wikipedia.org)
  • fMT]] is a metallothionein, binding Arsenite(III) and Arsenate(V), it has higher affinity for As(III). (igem.org)
  • Cation-transporting proteins that utilize the energy of ATP hydrolysis for the transport of CALCIUM. (jefferson.edu)
  • Here, molecular mechanism involved in the Si uptake by root and subsequent transport to areal tissues is also illustrated. (researchsquare.com)
  • HmtA]] (heavy metal transporter A) from ''Pseudomonas aeruginosa'' Q9I147 is a P-type ATPase importer. (igem.org)
  • They are primarily found in prokaryotic organisms, where they play a role in protection against excess intracellular levels of arsenite ions. (nih.gov)
  • The conformation of H,K-ATPase determines the nucleoside triphosphate (NTP) selectivity for active proton transport. (jefferson.edu)
  • GlpF]] is an aquaglyceroporin channel that facilitates the transport of As(III). (igem.org)
  • Cystic fibrosis (CF) is a recessive inherited disease caused by mutations affecting anion transport by the epithelial ion channel cystic fibrosis transmembrane conductance regulator (CFTR). (bvsalud.org)
  • The Transporter Classification Database (or TCDB ) is an International Union of Biochemistry and Molecular Biology (IUBMB)-approved classification system for membrane transport proteins , including ion channels . (wikipedia.org)
  • Purine nucleoside phosphorylase in the presence of dihydrolipoic acid is a route for reduction of arsenate to arsenite in mammalian systems. (nih.gov)
  • Binding-protein-dependent transport system inner membrane component [Interproscan]. (ntu.edu.sg)
  • The STM 6070 genome contains 55 genes, located in 12 clusters, that encode HMR structural proteins belonging to the RND, MFS, CHR, ARC3, CDF and P-ATPase protein superfamilies. (researchsquare.com)
  • Arsenite-Antimonite efflux Silver S, Misra TK, Laddaga RA (1989). (wikipedia.org)
  • Efflux pumps that use the energy of ATP hydrolysis to pump arsenite across a membrane. (nih.gov)
  • The action of PINs in auxin efflux is distinct from PGPs, rate-limiting, specific to auxins and sensitive to auxin transport inhibitors. (or.jp)
  • The ion transporter Na+-K+-ATPase enables pathological B cell survival in the kidney microenvironment of lupus nephritis. (uchicago.edu)
  • The Bromodomains of the mammalian SWI/SNF (mSWI/SNF) ATPases Brahma (BRM) and Brahma Related Gene 1 (BRG1) promote chromatin interaction and are critical for skeletal muscle differentiation. (umassmed.edu)
  • They are primarily found in prokaryotic organisms, where they play a role in protection against excess intracellular levels of arsenite ions. (nih.gov)
  • An enzyme that catalyzes the active transport system of sodium and potassium ions across the cell wall. (uchicago.edu)
  • Sodium and potassium ions are closely coupled with membrane ATPase which undergoes phosphorylation and dephosphorylation, thereby providing energy for transport of these ions against concentration gradients. (uchicago.edu)
  • In the present study, we find that overexpression of a single rice gene, Oryza sativa plasma membrane (PM) H + -ATPase 1 ( OSA1 ), facilitates ammonium absorption and assimilation in roots and enhanced light-induced stomatal opening with higher photosynthesis rate in leaves. (nature.com)
  • Sodium-Potassium-Exchanging ATPase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (uchicago.edu)
  • This graph shows the total number of publications written about "Sodium-Potassium-Exchanging ATPase" by people in this website by year, and whether "Sodium-Potassium-Exchanging ATPase" was a major or minor topic of these publications. (uchicago.edu)
  • Below are the most recent publications written about "Sodium-Potassium-Exchanging ATPase" by people in Profiles. (uchicago.edu)
  • The results of the present study clearly indicated that aluminium sulphate has signi!cantly altered the normal levels of acetyl cholinesterase, sodium potassium ATPase and glutathione of rat brain. (bbrc.in)
  • But in contrast to this, elevated levels of acetyl cholinesterase, sodium potassium ATPase and glutathione were noticed in aloin and aluminium sul- phate co treated groups, indicating the protective role of aloin against aluminium sulphate toxicity. (bbrc.in)
  • Get3 in yeast or TRC40 in mammals is an ATPase that, in eukaryotes, is a central element of the GET or TRC pathway involved in the targeting of tail-anchored proteins. (nih.gov)
  • putative electron transport chain YkgEFG component [Ensembl]. (ntu.edu.sg)
  • The iterative modeling and experimental approach unveiled exciting, previously unknown physiological features, including an expanded range of substrates that support growth, such as cellobiose and citrate, and provided additional insights into important features such as the stoichiometry of the electron transport chain and the ability to grow via fumarate dismutation. (biomedcentral.com)
  • The arsenite production reaction of thymidine phosphorylase had approximately 5% of such PNP activity. (nih.gov)
  • In our previous study, NH 4 + nutrition was found to induce upregulation of PM H + -ATPase activity in rice roots 20 . (nature.com)
  • Recently, we determined that enhanced PM H + -ATPase activity in rice roots ensures rice growth at high NH 4 + concentrations 21 . (nature.com)
  • In this study, we examined the involvement of PM H + -ATPase in NH 4 + uptake by rice roots and stomatal opening for CO 2 uptake and photosynthesis in rice leaves, with the aim of developing a new strategy to improve rice yield and N use efficiency (NUE) via the overexpression of a single gene, Oryza sativa PM H + -ATPase 1 ( OSA1 ). (nature.com)
  • Root-specific role in the transport of auxin. (or.jp)