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Ryanoid
Diamide insecticides are a class of insecticide, insecticides, active mainly against lepidoptera (Caterpillar, caterpillars), which act on the insect ryanodine receptor. They are diamides of either phthalic acid or anthranilic acid, with various appropriate further substitutions. Worldwide sales of diamides in 2018 were estimated at , which is 13% of the $18.4 billion insecticide market. History and examples The first diamide was flubendiamide. It was invented by Nihon Nohyaku and commercialised in 2007. It is a highly substituted diamide of phthalic acid and is highly active against lepidoptera (caterpillers). Later DuPont introduced chlorantraniliprole, which is more active against caterpillers and in addition active against other insect types. Cyantraniliprole, Cyanthraniliprole, introduced later, shows systemic activity and is also active against sucking pests such as Aphid, aphids and whitefly. According to one review, the first species reported to show resistance to diam ...
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Flubendiamide
Flubendiamide is the first insecticide of the Diamide insecticides, diamide class. It acts on the ryanodine receptor. Legality A environmentally persistent metabolite of flubendiamide is quite toxic to Marine invertebrates, aquatic invertebrates, causing flubendiamide to be banned by the United States United States Environmental Protection Agency, EPA. The product is still available in other jurisdictions such as Europe and India. References

{{insecticides Insecticides Benzamides Iodobenzene derivatives Organofluorides Sulfones ...
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Mechanism Of Action
In pharmacology, the term mechanism of action (MOA) refers to the specific biochemical Drug interaction, interaction through which a Medication, drug substance produces its pharmacological effect. A mechanism of action usually includes mention of the specific molecular targets to which the drug binds, such as an enzyme or receptor (biochemistry), receptor. Receptor sites have specific affinities for drugs based on the chemical structure of the drug, as well as the specific action that occurs there. Drugs that do not bind to receptors produce their corresponding therapeutic effect by simply interacting with chemical or physical properties in the body. Common examples of drugs that work in this way are antacids and laxatives. In contrast, a Mode of action, mode of action (MoA) describes functional or anatomical changes, at the cellular level, resulting from the exposure of a living organism to a substance. Importance Elucidating the mechanism of action of novel drugs and medicati ...
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Ryanodine
Ryanodine is a poisonous diterpenoid found in the South American plant ''Ryania speciosa'' (Salicaceae). It was originally used as an insecticide. The compound has extremely high affinity to the open-form ryanodine receptor, a group of calcium channels found in skeletal muscle, smooth muscle, and heart muscle cells. It binds with such high affinity to the receptor that it was used as a label for the first purification of that class of ion channels and gave its name to it. At nanomolar concentrations, ryanodine locks the receptor in a half-open state, whereas it fully closes them at micromolar concentration. The effect of the nanomolar-level binding is that ryanodine causes release of calcium from calcium stores as the sarcoplasmic reticulum in the cytoplasm, leading to massive muscle contractions. The effect of micromolar-level binding is paralysis. This is true for both mammals and insects. See also * Diamide insecticides, a class of insecticides with the same mechanism of ac ...
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Alkaloid
Alkaloids are a broad class of natural product, naturally occurring organic compounds that contain at least one nitrogen atom. Some synthetic compounds of similar structure may also be termed alkaloids. Alkaloids are produced by a large variety of organisms including bacteria, fungus, fungi, Medicinal plant, plants, and animals. They can be purified from crude extracts of these organisms by acid-base extraction, or solvent extractions followed by silica-gel column chromatography. Alkaloids have a wide range of pharmacology, pharmacological activities including antimalarial medication, antimalarial (e.g. quinine), asthma, antiasthma (e.g. ephedrine), chemotherapy, anticancer (e.g. omacetaxine mepesuccinate, homoharringtonine), cholinomimetic (e.g. galantamine), vasodilation, vasodilatory (e.g. vincamine), Antiarrhythmic agent, antiarrhythmic (e.g. quinidine), analgesic (e.g. morphine), antibacterial (e.g. chelerythrine), and anti-diabetic, antihyperglycemic activities (e.g. berb ...
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Endoplasmic Reticulum
The endoplasmic reticulum (ER) is a part of a transportation system of the eukaryote, eukaryotic cell, and has many other important functions such as protein folding. The word endoplasmic means "within the cytoplasm", and reticulum is Latin for "little net". It is a type of organelle made up of two subunits – rough endoplasmic reticulum (RER), and smooth endoplasmic reticulum (SER). The endoplasmic reticulum is found in most eukaryotic cells and forms an interconnected network of flattened, membrane-enclosed sacs known as cisternae (in the RER), and tubular structures in the SER. The membranes of the ER are continuous with the outer nuclear membrane. The endoplasmic reticulum is not found in red blood cells, or spermatozoa. There are two types of ER that share many of the same proteins and engage in certain common activities such as the synthesis of certain lipids and cholesterol. Different types of Cell (biology), cells contain different ratios of the two types of ER dependin ...
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Sarcoplasmic Reticulum
The sarcoplasmic reticulum (SR) is a membrane-bound structure found within muscle cells that is similar to the smooth endoplasmic reticulum in other cells. The main function of the SR is to store calcium ions (Ca2+). Calcium ion levels are kept relatively constant, with the concentration of calcium ions within a cell being 10,000 times smaller than the concentration of calcium ions outside the cell. This means that small increases in calcium ions within the cell are easily detected and can bring about important cellular changes (the calcium is said to be a second messenger). Calcium is used to make calcium carbonate (found in chalk) and calcium phosphate, two compounds that the body uses to make teeth and bones. This means that too much calcium within the cells can lead to hardening (calcification) of certain intracellular structures, including the mitochondria, leading to cell death. Therefore, it is vital that calcium ion levels are controlled tightly, and can be released int ...
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Calcium Channel
A calcium channel is an ion channel which shows selective permeability to calcium ions. It is sometimes synonymous with voltage-gated calcium channel, which are a type of calcium channel regulated by changes in membrane potential. Some calcium channels are regulated by the binding of a ligand.Striggow F, Ehrlich BE (August 1996). "Ligand-gated calcium channels inside and out". ''Current Opinion in Cell Biology''. 8 (4): 490–495. Doi (identifier), doi:doi:10.1016/S0955-0674(96)80025-1, 10.1016/S0955-0674(96)80025-1. PMID (identifier), PMID]8791458 Other calcium channels can also be regulated by both voltage and ligands to provide precise control over ion flow. Some cation channels allow calcium as well as other cations to pass through the membrane. Calcium channels can participate in the creation of Action potential, action potentials across cell membranes. Calcium channels can also be used to release calcium ions as Second messenger system, second messengers within the cell, affec ...
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Tetrameric Protein
A tetrameric protein is a protein with a quaternary structure of four subunits (tetrameric). Homotetramers have four identical subunits (such as glutathione S-transferase), and heterotetramers are complexes of different subunits. A tetramer can be assembled as dimer of dimers with two homodimer subunits (such as sorbitol dehydrogenase), or two heterodimer subunits (such as hemoglobin). Subunit interactions in tetramers The interactions between subunits forming a tetramer is primarily determined by non covalent interaction. Hydrophobic effects, hydrogen bonds and electrostatic interactions are the primary sources for this binding process between subunits. For homotetrameric proteins such as sorbitol dehydrogenase (SDH), the structure is believed to have evolved going from a monomeric to a dimeric and finally a tetrameric structure in evolution. The binding process in SDH and many other tetrameric enzymes can be described by the gain in free energy which can be determined ...
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Ryanodine Receptor
Ryanodine receptors (RyR) make up a class of high-conductance, intracellular calcium channels present in various forms, such as animal muscles and neurons. There are three major isoforms of the ryanodine receptor, which are found in different tissues and participate in various signaling pathways involving calcium release from intracellular organelles. Structure Ryanodine receptors are multidomain homotetramers which regulate intracellular calcium ion release from the sarcoplasmic and endoplasmic reticula. They are the largest known ion channels, with weights exceeding 2 megadaltons, and their structural complexity enables a wide variety of allosteric regulation mechanisms. RyR1 cryo-EM structure revealed a large cytosolic assembly built on an extended Alpha solenoid, α-solenoid scaffold connecting key regulatory domains to the pore. The RyR1 pore architecture shares the general structure of the six-transmembrane ion channel superfamily. A unique domain inserted between the secon ...
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Ryanodine Receptor 2
Ryanodine receptor 2 (RYR2) is one of a class of ryanodine receptors and a protein found primarily in cardiac muscle. In humans, it is encoded by the ''RYR2'' gene. In the process of cardiac calcium-induced calcium release, RYR2 is the major mediator for sarcoplasmic release of stored calcium ions. Structure The channel is composed of RYR2 homotetramers and  FK506-binding proteins found in a 1:4 stoichiometric ratio. Calcium channel function is affected by the specific type of FK506 isomer interacting with the RYR2 protein, due to binding differences and other factors. Function The RYR2 protein functions as the major component of a calcium channel located in the sarcoplasmic reticulum that supplies ions to the cardiac muscle during systole. To enable cardiac muscle contraction, calcium influx through voltage-gated L-type calcium channels in the plasma membrane allows calcium ions to bind to RYR2 located on the sarcoplasmic reticulum. This bindi ...
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