5'-Adenylic acid, monoanhydride with imidodiphosphoric acid. An analog of ATP, in which the oxygen atom bridging the beta to the gamma phosphate is replaced by a nitrogen atom. It is a potent competitive inhibitor of soluble and membrane-bound mitochondrial ATPase and also inhibits ATP-dependent reactions of oxidative phosphorylation.
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 non-hydrolyzable analog of GTP, in which the oxygen atom bridging the beta to the gamma phosphate is replaced by a nitrogen atom. It binds tightly to G-protein in the presence of Mg2+. The nucleotide is a potent stimulator of ADENYLYL CYCLASES.
The rate dynamics in chemical or physical systems.
An enzyme of the lyase class that catalyzes the formation of CYCLIC AMP and pyrophosphate from ATP. EC 4.6.1.1.
Guanine nucleotides are cyclic or linear molecules that consist of a guanine base, a pentose sugar (ribose in the cyclic form, deoxyribose in the linear form), and one or more phosphate groups, playing crucial roles in signal transduction, protein synthesis, and regulation of enzymatic activities.
Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.
A source of inorganic fluoride which is used topically to prevent dental caries.
A family of MEMBRANE TRANSPORT PROTEINS that require ATP hydrolysis for the transport of substrates across membranes. The protein family derives its name from the ATP-binding domain found on the protein.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
A superfamily of large integral ATP-binding cassette membrane proteins whose expression pattern is consistent with a role in lipid (cholesterol) efflux. It is implicated in TANGIER DISEASE characterized by accumulation of cholesteryl ester in various tissues.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
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.
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.
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 deinsertion of SecA underlying proton motive force-dependent stimulation of protein translocation. (1/521)

The proton motive force (PMF) renders protein translocation across the Escherichia coli membrane highly efficient, although the underlying mechanism has not been clarified. The membrane insertion and deinsertion of SecA coupled to ATP binding and hydrolysis, respectively, are thought to drive the translocation. We report here that PMF significantly decreases the level of membrane-inserted SecA. The prlA4 mutation of SecY, which causes efficient protein translocation in the absence of PMF, was found to reduce the membrane-inserted SecA irrespective of the presence or absence of PMF. The PMF-dependent decrease in the membrane-inserted SecA caused an increase in the amount of SecA released into the extra-membrane milieu, indicating that PMF deinserts SecA from the membrane. The PMF-dependent deinsertion reduced the amount of SecA required for maximal translocation activity. Neither ATP hydrolysis nor exchange with external SecA was required for the PMF-dependent deinsertion of SecA. These results indicate that the SecA deinsertion is a limiting step of protein translocation and is accelerated by PMF, efficient protein translocation thereby being caused in the presence of PMF.  (+info)

Dual actions of the metabolic inhibitor, sodium azide on K(ATP) channel currents in the rat CRI-G1 insulinoma cell line. (2/521)

1. The effects of various inhibitors of the mitochondrial electron transport chain on the activity of ATP-sensitive K+ channels were examined in the Cambridge rat insulinoma G1 (CRI-G1) cell line using a combination of whole cell and single channel recording techniques. 2. Whole cell current clamp recordings, with 5 mM ATP in the pipette, demonstrate that the mitochondrial uncoupler sodium azide (3 mM) rapidly hyperpolarizes CRI-G1 cells with a concomitant increase in K+ conductance. This is due to activation of K(ATP) channels as the sulphonylurea tolbutamide (100 microM) completely reversed the actions of azide. Other inhibitors of the mitochondrial electron transport chain, rotenone (10 microM) or oligomycin (2 microM) did not hyperpolarize CRI-G1 cells or increase K+ conductance. 3. In cell-attached recordings, bath application of 3 mM sodium azide (in the absence of glucose) resulted in a rapid increase in K(ATP) channel activity, an action readily reversible by tolbutamide (100 microM). Application of sodium azide (3 mM), in the presence of Mg-ATP, to the intracellular surface of excised inside-out patches also increased K(ATP) channel activity, in a reversible manner. 4. In contrast, rotenone (10 microM) or oligomycin (2 microM) did not increase K(ATP) channel activity in either cell-attached, in the absence of glucose, or inside-out membrane patch recordings. 5. Addition of sodium azide (3 mM) to the intracellular surface of inside-out membrane patches in the presence of Mg-free ATP or the non-hydrolysable analogue 5'-adenylylimidodiphosphate (AMP-PNP) inhibited, rather than increased, K(ATP) channel activity. 6. In conclusion, sodium azide, but not rotenone or oligomycin, directly activates K(ATP) channels in CRI-G1 insulin secreting cells. This action of azide is similar to that reported previously for diazoxide.  (+info)

ATP inhibition of a mouse brain large-conductance K+ (mslo) channel variant by a mechanism independent of protein phosphorylation. (3/521)

1. We investigated the effect of ATP in the regulation of two closely related cloned mouse brain large conductance calcium- and voltage-activated potassium (BK) channel alpha-subunit variants, expressed in human embryonic kidney (HEK 293) cells, using the excised inside-out configuration of the patch-clamp technique. 2. The mB2 BK channel alpha-subunit variant expressed alone was potently inhibited by application of ATP to the intracellular surface of the patch with an IC50 of 30 microM. The effect of ATP was largely independent of protein phosphorylation events as the effect of ATP was mimicked by the non-hydrolysable analogue 5'-adenylylimidodiphosphate (AMP-PNP) and the inhibitory effect of ATPgammaS was reversible. 3. In contrast, under identical conditions, direct nucleotide inhibition was not observed in the closely related mouse brain BK channel alpha-subunit variant mbr5. Furthermore, direct nucleotide regulation was not observed when mB2 was functionally coupled to regulatory beta-subunits. 4. These data suggest that the mB2 alpha-subunit splice variant could provide a dynamic link between cellular metabolism and cell excitability.  (+info)

ATP counteracts the rundown of gap junctional channels of rat ventricular myocytes by promoting protein phosphorylation. (4/521)

1. The degree of cell-to-cell coupling between ventricular myocytes of neonatal rats appeared well preserved when studied in the perforated version of the patch clamp technique or, in double whole-cell conditions, when ATP was present in the patch pipette solution. In contrast, when ATP was omitted, the amplitude of junctional current rapidly declined (rundown). 2. To examine the mechanism(s) of ATP action, an 'internal perfusion technique' was adapted to dual patch clamp conditions, and reintroduction of ATP partially reversed the rundown of junctional channels. 3. Cell-to-cell communication was not preserved by a non-hydrolysable ATP analogue (5'-adenylimidodiphosphate, AMP-PNP), indicating that the effect most probably did not involve direct interaction of ATP with the channel-forming proteins. 4. An ATP analogue supporting protein phosphorylation but not active transport processes (adenosine 5'-O-(3-thiotriphosphate), ATPgammaS) maintained normal intercellular communication, suggesting that the effect was due to kinase activity rather than to altered intracellular Ca2+. 5. A broad spectrum inhibitor of endogenous serine/threonine protein kinases (H7) reversibly reduced the intercellular coupling. A non-specific exogenous protein phosphatase (alkaline phosphatase) mimicked the effects of ATP deprivation. The non-specific inhibition of endogenous protein phosphatases resulted in the preservation of substantial cell-to-cell communication in ATP-free conditions. 6. The activity of gap junctional channels appears to require both the presence of ATP and protein kinase activity to counteract the tonic activity of endogenous phosphatase(s).  (+info)

Analysis of DNA cleavage by reverse gyrase from Sulfolobus shibatae B12. (5/521)

Reverse gyrase is a type I-5' topoisomerase, which catalyzes a positive DNA supercoiling reaction in vitro. To ascertain how this reaction takes places, we looked at the DNA sequences recognized by reverse gyrase. We used linear DNA fragments of its preferred substrate, the viral SSV1 DNA, which has been shown to be positively supercoiled in vivo. The Sulfolobus shibatae B12 strain, an SSV1 virus host, was chosen for production of reverse gyrase. This naturally occurring system (SSV1 DNA-S. shibatae reverse gyrase) allowed us to determine which SSV1 DNA sequences are bound and cleaved by the enzyme with particularly high selectivity. We show that the presence of ATP decreases the number of cleaved complexes obtained whereas the non-hydrolyzable ATP analog adenosine 5'-[beta, gamma-imido]triphosphate increases it without changing the sequence specificity.  (+info)

Motile properties of the kinesin-related Cin8p spindle motor extracted from Saccharomyces cerevisiae cells. (6/521)

We have developed microtubule binding and motility assays for Cin8p, a kinesin-related mitotic spindle motor protein from Saccharomyces cerevisiae. The methods examine Cin8p rapidly purified from crude yeast cell extracts. We created a recombinant form of CIN8 that fused the biotin carrying polypeptide from yeast pyruvate carboxylase to the carboxyl terminus of Cin8p. This form was biotinated in yeast cells and provided Cin8p activity in vivo. Avidin-coated glass surfaces were used to specifically bind biotinated Cin8p from crude extracts. Microtubules bound to the Cin8p-coated surfaces and moved at 3.4 +/- 0.5 micrometer/min in the presence of ATP. Force production by Cin8p was directed toward the plus ends of microtubules. A mutation affecting the microtubule-binding site within the motor domain (cin8-F467A) decreased Cin8p's ability to bind microtubules to the glass surface by >10-fold, but reduced gliding velocity by only 35%. The cin8-3 mutant form, affecting the alpha2 helix of the motor domain, caused a moderate defect in microtubule binding, but motility was severely affected. cin8-F467A cells, but not cin8-3 cells, were greatly impaired in bipolar spindle forming ability. We conclude that microtubule binding by Cin8p is more important than motility for proper spindle formation.  (+info)

Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. (7/521)

We have determined two different structures of PcrA DNA helicase complexed with the same single strand tailed DNA duplex, providing snapshots of different steps on the catalytic pathway. One of the structures is of a complex with a nonhydrolyzable analog of ATP and is thus a "substrate" complex. The other structure contains a bound sulphate ion that sits in a position equivalent to that occupied by the phosphate ion produced after ATP hydrolysis, thereby mimicking a "product" complex. In both complexes, the protein is monomeric. Large and distinct conformational changes occur on binding DNA and the nucleotide cofactor. Taken together, these structures provide evidence against an "active rolling" model for helicase action but are instead consistent with an "inchworm" mechanism.  (+info)

Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair. (8/521)

The MutL DNA mismatch repair protein has recently been shown to be an ATPase and to belong to an emerging ATPase superfamily that includes DNA topoisomerase II and Hsp90. We report here the crystal structures of a 40 kDa ATPase fragment of E. coli MutL (LN40) complexed with a substrate analog, ADPnP, and with product ADP. More than 60 residues that are disordered in the apoprotein structure become ordered and contribute to both ADPnP binding and dimerization of LN40. Hydrolysis of ATP, signified by subsequent release of the gamma-phosphate, releases two key loops and leads to dissociation of the LN40 dimer. Dimerization of the LN40 region is required for and is the rate-limiting step in ATP hydrolysis by MutL. The ATPase activity of MutL is stimulated by DNA and likely acts as a switch to coordinate DNA mismatch repair.  (+info)

Adenylyl Imidodiphosphate (AMP-PNP) is a non-hydrolysable analog of adenosine triphosphate (ATP). ATP is a high-energy molecule that provides energy for many cellular processes, including muscle contraction, protein synthesis, and transport of molecules across cell membranes.

AMP-PNP is used in biochemical research as an ATP substitute to study various enzymatic reactions that require ATP as a substrate. Unlike ATP, AMP-PNP cannot be hydrolyzed by most enzymes, and it remains stable during the reaction, allowing researchers to observe and analyze the reaction kinetics more accurately.

AMP-PNP is also used in structural biology studies to determine the three-dimensional structures of proteins that bind to ATP. The non-hydrolyzable property of AMP-PNP makes it an ideal molecule for co-crystallization with proteins, providing valuable insights into the molecular mechanisms of ATP-dependent enzymes.

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.

Guanylyl Imidodiphosphate (GIP) is not a medical term itself, but it is a biochemical compound that plays a crucial role in the body's signaling pathways. It is a vital intracellular second messenger involved in various physiological processes, including vasodilation and smooth muscle relaxation.

To be more specific, GIP is a nucleotide that activates a family of enzymes called guanylyl cyclases (GCs). Once activated, these enzymes convert guanosine triphosphate (GTP) to cyclic guanosine monophosphate (cGMP), another essential second messenger. The increased levels of cGMP then mediate the relaxation of smooth muscle and vasodilation by activating protein kinases and ion channels, among other mechanisms.

In summary, Guanylyl Imidodiphosphate (GIP) is a biochemical compound that plays a critical role in intracellular signaling pathways, leading to vasodilation and smooth muscle relaxation.

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.

Adenylate cyclase is an enzyme that catalyzes the conversion of adenosine triphosphate (ATP) to cyclic adenosine monophosphate (cAMP). It plays a crucial role in various cellular processes, including signal transduction and metabolism. Adenylate cyclase is activated by hormones and neurotransmitters that bind to G-protein-coupled receptors on the cell membrane, leading to the production of cAMP, which then acts as a second messenger to regulate various intracellular responses. There are several isoforms of adenylate cyclase, each with distinct regulatory properties and subcellular localization.

Guanine nucleotides are molecules that play a crucial role in intracellular signaling, cellular regulation, and various biological processes within cells. They consist of a guanine base, a sugar (ribose or deoxyribose), and one or more phosphate groups. The most common guanine nucleotides are GDP (guanosine diphosphate) and GTP (guanosine triphosphate).

GTP is hydrolyzed to GDP and inorganic phosphate by certain enzymes called GTPases, releasing energy that drives various cellular functions such as protein synthesis, signal transduction, vesicle transport, and cell division. On the other hand, GDP can be rephosphorylated back to GTP by nucleotide diphosphate kinases, allowing for the recycling of these molecules within the cell.

In addition to their role in signaling and regulation, guanine nucleotides also serve as building blocks for RNA (ribonucleic acid) synthesis during transcription, where they pair with cytosine nucleotides via hydrogen bonds to form base pairs in the resulting RNA molecule.

Guanosine triphosphate (GTP) is a nucleotide that plays a crucial role in various cellular processes, such as protein synthesis, signal transduction, and regulation of enzymatic activities. It serves as an energy currency, similar to adenosine triphosphate (ATP), and undergoes hydrolysis to guanosine diphosphate (GDP) or guanosine monophosphate (GMP) to release energy required for these processes. GTP is also a precursor for the synthesis of other essential molecules, including RNA and certain signaling proteins. Additionally, it acts as a molecular switch in many intracellular signaling pathways by binding and activating specific GTPase proteins.

Sodium fluoride is an inorganic compound with the chemical formula NaF. Medically, it is commonly used as a dental treatment to prevent tooth decay, as it is absorbed into the structure of teeth and helps to harden the enamel, making it more resistant to acid attacks from bacteria. It can also reduce the ability of bacteria to produce acid. Sodium fluoride is often found in toothpastes, mouth rinses, and various dental treatments. However, excessive consumption can lead to dental fluorosis and skeletal fluorosis, which cause changes in bone structure and might negatively affect health.

ATP-binding cassette (ABC) transporters are a family of membrane proteins that utilize the energy from ATP hydrolysis to transport various substrates across extra- and intracellular membranes. These transporters play crucial roles in several biological processes, including detoxification, drug resistance, nutrient uptake, and regulation of cellular cholesterol homeostasis.

The structure of ABC transporters consists of two nucleotide-binding domains (NBDs) that bind and hydrolyze ATP, and two transmembrane domains (TMDs) that form the substrate-translocation pathway. The NBDs are typically located adjacent to each other in the cytoplasm, while the TMDs can be either integral membrane domains or separate structures associated with the membrane.

The human genome encodes 48 distinct ABC transporters, which are classified into seven subfamilies (ABCA-ABCG) based on their sequence similarity and domain organization. Some well-known examples of ABC transporters include P-glycoprotein (ABCB1), multidrug resistance protein 1 (ABCC1), and breast cancer resistance protein (ABCG2).

Dysregulation or mutations in ABC transporters have been implicated in various diseases, such as cystic fibrosis, neurological disorders, and cancer. In cancer, overexpression of certain ABC transporters can contribute to drug resistance by actively effluxing chemotherapeutic agents from cancer cells, making them less susceptible to treatment.

An encyclopedia is a comprehensive reference work containing articles on various topics, usually arranged in alphabetical order. In the context of medicine, a medical encyclopedia is a collection of articles that provide information about a wide range of medical topics, including diseases and conditions, treatments, tests, procedures, and anatomy and physiology. Medical encyclopedias may be published in print or electronic formats and are often used as a starting point for researching medical topics. They can provide reliable and accurate information on medical subjects, making them useful resources for healthcare professionals, students, and patients alike. Some well-known examples of medical encyclopedias include the Merck Manual and the Stedman's Medical Dictionary.

ATP Binding Cassette Transporter 1 (ABC Transporter 1 or ABCB1) is a protein that belongs to the superfamily of ATP-binding cassette (ABC) transporters. These proteins utilize the energy from ATP hydrolysis to transport various substrates across membranes.

The ABCB1 gene encodes for the P-glycoprotein (P-gp), a 170 kDa protein, which is an efflux transporter primarily located in the plasma membrane of various cell types, including epithelial and endothelial cells. P-gp plays a crucial role in limiting the absorption and facilitating the excretion of many drugs by actively pumping them out of cells, thereby contributing to multidrug resistance (MDR) in cancer cells.

P-gp has a broad substrate specificity and can transport various structurally diverse compounds, including chemotherapeutic agents, antibiotics, antiviral drugs, and natural toxins. Its expression is often upregulated in cancer cells, leading to reduced intracellular drug accumulation and decreased therapeutic efficacy. In addition to its role in drug resistance, P-gp also functions in the absorption, distribution, and excretion of drugs in normal tissues, particularly in the intestine, liver, and kidney.

Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:

1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction

Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:

1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.

Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).

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.

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.

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.

The structure of MsbA-AMP-PNP (5'-adenylyl-β-γ-imidodiphosphate), obtained from S. typhimurium, is similar to Sav1866. The NBDs ... adenylyl-β-γ-imidodiphosphate (AMP-PNP), showed that ATP binding, in the absence of hydrolysis, is sufficient to reduce ...
In a closed state, the two domains of eIF4AIII form composite binding sites for the 5'-adenylyl-β,γ-imidodiphosphate (ADPNP) ...
... adenylyl-imidodiphosphate, a substrate analog of ATP, and 3-acetylpyridine adenine dinucleotide, a substrate analog of NADH. As ...
... adenylyl imidodiphosphate MeSH D13.695.667.138.236.250 - ethenoadenosine triphosphate MeSH D13.695.667.138.382 - coenzyme a ... adenylyl imidodiphosphate MeSH D13.695.827.068.236.250 - ethenoadenosine triphosphate MeSH D13.695.827.068.382 - coenzyme a ... guanylyl imidodiphosphate MeSH D13.695.667.454.525 - 5'-guanylic acid MeSH D13.695.667.454.700 - rna caps MeSH D13.695.667.454. ... guanylyl imidodiphosphate MeSH D13.695.827.426.525 - 5'-guanylic acid MeSH D13.695.827.426.700 - rna caps MeSH D13.695.827.426. ...
The structure of MsbA-AMP-PNP (5-adenylyl-β-γ-imidodiphosphate), obtained from S. typhimurium, is similar to Sav1866. The NBDs ... adenylyl-β-γ-imidodiphosphate (AMP-PNP), showed that ATP binding, in the absence of hydrolysis, is sufficient to reduce ...
Adenylyl Imidodiphosphate Medicin och livsvetenskap 18% * AAA Domain Medicin och livsvetenskap 17% ...
... adenylyl-imidodiphosphate (AMPPNP). Furthermore, the structure is compared with the ADP-bound form of the CENP-E motor domain ...
Adenylyl Imidodiphosphate D3.438.759.646.138.236.50 D3.633.100.759.646.138.236.50 Adhesiveness G2.842.850.139 G2.860.139 ... Guanylyl Imidodiphosphate D3.438.759.646.454.504.400 D3.633.100.759.646.454.504.400 Guernsey Z1.639.280.161.500 Gymnastics ...
Adenylyl Imidodiphosphate D3.438.759.646.138.236.50 D3.633.100.759.646.138.236.50 Adhesiveness G2.842.850.139 G2.860.139 ... Guanylyl Imidodiphosphate D3.438.759.646.454.504.400 D3.633.100.759.646.454.504.400 Guernsey Z1.639.280.161.500 Gymnastics ...
MeSH Terms: Adenosine Diphosphate/metabolism; Adenosine Triphosphate/metabolism; Adenylyl Imidodiphosphate/metabolism; Animals ...
Adenylyl Imidodiphosphate / chemistry Actions. * Search in PubMed * Search in MeSH * Add to Search ...
Adenylyl Imidodiphosphate / metabolism* Actions. * Search in PubMed * Search in MeSH * Add to Search ...
Adenylyl Imidodiphosphate D3.438.759.646.138.236.50 D3.633.100.759.646.138.236.50 Adhesiveness G2.842.850.139 G2.860.139 ... Guanylyl Imidodiphosphate D3.438.759.646.454.504.400 D3.633.100.759.646.454.504.400 Guernsey Z1.639.280.161.500 Gymnastics ...
Adenylyl Imidodiphosphate / metabolism Actions. * Search in PubMed * Search in MeSH * Add to Search ...
Adenyl Imidodiphosphate Adenylimidodiphosphate Adenylylimidodiphosphate Mg AMP-PNP Mg-5-Adenylylimidodiphosphate beta,gamma- ... Adenylyl Imidodiphosphate Preferred Term Term UI T000835. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1976). ... Adenylyl Imidodiphosphate Preferred Concept UI. M0000416. Registry Number. 25612-73-1. Scope Note. 5-Adenylic acid, ... Mg-5-Adenylylimidodiphosphate Narrower Concept UI. M0000417. Registry Number. 0. Terms. Mg-5-Adenylylimidodiphosphate ...
Adenyl Imidodiphosphate Adenylimidodiphosphate Adenylylimidodiphosphate Mg AMP-PNP Mg-5-Adenylylimidodiphosphate beta,gamma- ... Adenylyl Imidodiphosphate Preferred Term Term UI T000835. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1976). ... Adenylyl Imidodiphosphate Preferred Concept UI. M0000416. Registry Number. 25612-73-1. Scope Note. 5-Adenylic acid, ... Mg-5-Adenylylimidodiphosphate Narrower Concept UI. M0000417. Registry Number. 0. Terms. Mg-5-Adenylylimidodiphosphate ...
Adenyl Imidodiphosphate Adenylimidodiphosphate Adenylylimidodiphosphate Imidodiphosphate, Adenyl Imidodiphosphate, Adenylyl ... Adenylylimidodiphosphate. Imidodiphosphate, Adenyl. Imidodiphosphate, Adenylyl. Mg 5 Adenylylimidodiphosphate. Mg AMP PNP. Mg ... Adenylyl Imidodiphosphate - Preferred Concept UI. M0000416. Scope note. 5-Adenylic acid, monoanhydride with imidodiphosphoric ... Adenylyl Imidodiphosphate Entry term(s). AMP-PNP AMPPNP ATP(beta,gamma-NH) Adenosine 5-(beta,gamma-Imino)triphosphate ...
... adenylyl-imidodiphosphate; PNP, di- phosphoimide; ADP-NH;, 5-adenylyl-phosphoamide; cyclic AMP, cyclic-3,5-AMP. 1877 1878 ... adenylyl imidodiphosphate labeled with **P at the a posi- tion (AMP-PNP-a-"*P), an analogue of ATP containing nitro- gen ...
Adenylate Kinase N0000168017 Adenylosuccinate Lyase N0000167766 Adenylosuccinate Synthase N0000170831 Adenylyl Imidodiphosphate ... Cyclase-Activating Proteins N0000168258 Guanylate Kinase N0000166459 Guanylthiourea N0000170847 Guanylyl Imidodiphosphate ...
Previously, the crystal structure of APH(4)-Ia was reported as a ternary complex with HygB and 5-adenylyl-ß,γ- ... imidodiphosphate (AMP-PNP). To investigate the differences in the substrate-recognition mechanism between APH(7)-Ia and APH(4 ...
D3.438.759.590.138.25 Adenylyl Imidodiphosphate D3.438.759.646.138.236.50 Adiposis Dolorosa C17.800.849.77 C17.800.463.249 ... D3.438.759.646.454.504 Guanylyl Imidodiphosphate D3.438.759.646.454.504.400 Guided Tissue Regeneration, Periodontal E6.645.410 ...
Pyrophosphate analogs like imidodiphosphate strongly promote reverse reaction dNTP products containing the imidodiphosphate ... The ß?-subunits of Go interact with ion channels, and the a subunit has been shown to inhibit adenylyl cyclase. However a ... This imidodiphosphate-containing dNTP was found to be a potent inhibitor of the forward RT reaction. ... Heterotrimeric G proteins couple signals between GPCRs (G protein coupled receptors) and effectors such as adenylyl cyclase, ...
Adenylyl Cyclase Inhibitors Adenylyl Cyclases Adenylyl Imidodiphosphate Adherens Junctions Adhesins, Bacterial Adhesins, ...

No FAQ available that match "adenylyl imidodiphosphate"