A lipoprotein-associated PHOSPHOLIPASE A2 which modulates the action of PLATELET ACTIVATING FACTOR by hydrolyzing the SN-2 ester bond to yield the biologically inactive lyso-platelet-activating factor. It has specificity for phospholipid substrates with short-chain residues at the SN-2 position, but inactive against long-chain phospholipids. Deficiency in this enzyme is associated with many diseases including ASTHMA, and HYPERCHOLESTEROLEMIA.
Esterases are hydrolase enzymes that catalyze the hydrolysis of ester bonds, converting esters into alcohols and acids, playing crucial roles in various biological processes including metabolism and detoxification.
Enzymes which catalyze the hydrolysis of carboxylic acid esters with the formation of an alcohol and a carboxylic acid anion.
Hydrolytic enzyme activity used as a histocytochemical test for the presence of esterases in tissue. Substrate used is 3-hydroxy-4'-nitro-2-naphthanilide chloroacetate (naphthol AS-D).
An enzyme that catalyzes the hydrolysis of CHOLESTEROL ESTERS and some other sterol esters, to liberate cholesterol plus a fatty acid anion.
An enzyme that catalyzes the conversion of acetate esters and water to alcohols and acetate. EC 3.1.1.6.
Carboxylesterase is a serine-dependent esterase with wide substrate specificity. The enzyme is involved in the detoxification of XENOBIOTICS and the activation of ester and of amide PRODRUGS.
"Esters are organic compounds that result from the reaction between an alcohol and a carboxylic acid, playing significant roles in various biological processes and often used in pharmaceutical synthesis."
A di-isopropyl-fluorophosphate which is an irreversible cholinesterase inhibitor used to investigate the NERVOUS SYSTEM.
The covalent bonding of an alkyl group to an organic compound. It can occur by a simple addition reaction or by substitution of another functional group.

Lipoprotein-associated phospholipase A2, platelet-activating factor acetylhydrolase, generates two bioactive products during the oxidation of low-density lipoprotein: use of a novel inhibitor. (1/562)

A novel and potent azetidinone inhibitor of the lipoprotein-associated phospholipase A2 (Lp-PLA2), i.e. platelet-activating factor acetylhydrolase, is described for the first time. This inhibitor, SB-222657 (Ki=40+/-3 nM, kobs/[I]=6. 6x10(5) M-1.s-1), is inactive against paraoxonase, is a poor inhibitor of lecithin:cholesterol acyltransferase and has been used to investigate the role of Lp-PLA2 in the oxidative modification of lipoproteins. Although pretreatment with SB-222657 did not affect the kinetics of low-density lipoprotein (LDL) oxidation by Cu2+ or an azo free-radical generator as determined by assay of lipid hydroperoxides (LOOHs), conjugated dienes and thiobarbituric acid-reacting substances, in both cases it inhibited the elevation in lysophosphatidylcholine content. Moreover, the significantly increased monocyte chemoattractant activity found in a non-esterified fatty acid fraction from LDL oxidized by Cu2+ was also prevented by pretreatment with SB-222657, with an IC50 value of 5.0+/-0.4 nM. The less potent diastereoisomer of SB-222657, SB-223777 (Ki=6.3+/-0.5 microM, kobs/[I]=1.6x10(4) M-1.s-1), was found to be significantly less active in both assays. Thus, in addition to generating lysophosphatidylcholine, a known biologically active lipid, these results demonstrate that Lp-PLA2 is capable of generating oxidized non-esterified fatty acid moieties that are also bioactive. These findings are consistent with our proposal that Lp-PLA2 has a predominantly pro-inflammatory role in atherogenesis. Finally, similar studies have demonstrated that a different situation exists during the oxidation of high-density lipoprotein, with enzyme(s) other than Lp-PLA2 apparently being responsible for generating lysophosphatidylcholine.  (+info)

Association of the inflammatory state in active juvenile rheumatoid arthritis with hypo-high-density lipoproteinemia and reduced lipoprotein-associated platelet-activating factor acetylhydrolase activity. (2/562)

OBJECTIVE: To investigate the relationship between the quantitative and qualitative abnormalities of apolipoprotein B (Apo B)- and Apo A-I-containing lipoproteins and between lipoprotein-associated platelet-activating factor acetylhydrolase (PAF-AH) activity in patients with juvenile rheumatoid arthritis (JRA) as a function of the inflammatory state. METHODS: Twenty-six JRA patients and 22 age- and sex-matched control subjects with normal lipid levels participated in the study. Fourteen patients had active disease, and 12 had inactive disease. Plasma lipoproteins were fractionated by gradient ultracentrifugation into 9 subfractions, and their chemical composition and mass were determined. The PAF-AH activity associated with lipoprotein subfractions and the activity in plasma were also measured. RESULTS: Patients with active JRA had significantly lower plasma total cholesterol and high-density lipoprotein (HDL) cholesterol levels as compared with controls, due to the decrease in the mass of both the HDL2 and HDL3 subfractions. Patients with active JRA also had higher plasma triglyceride levels, mainly due to the higher triglyceride content of the very low-density lipoprotein plus the intermediate-density lipoprotein subfraction. The plasma PAF-AH activity in patients with active JRA was lower than that in controls, mainly due to the decrease in PAF-AH activity associated with the intermediate and dense low-density lipoprotein subclasses. The lipid abnormalities and the reduction in plasma PAF-AH activity were significantly correlated with plasma C-reactive protein levels and were not observed in patients with inactive JRA. CONCLUSION: This is the first study to show that patients with active JRA exhibit low levels of HDL2 and HDL3 and are deficient in plasma PAF-AH activity. These alterations suggest that active JRA is associated with partial loss of the antiinflammatory activity of plasma Apo B- and Apo A-I-containing lipoproteins.  (+info)

Glutamate receptor signaling interplay modulates stress-sensitive mitogen-activated protein kinases and neuronal cell death. (3/562)

Glutamate receptors modulate multiple signaling pathways, several of which involve mitogen-activated protein (MAP) kinases, with subsequent physiological or pathological consequences. Here we report that stimulation of the N-methyl-D-aspartate (NMDA) receptor, using platelet-activating factor (PAF) as a messenger, activates MAP kinases, including c-Jun NH2-terminal kinase, p38, and extracellular signal-regulated kinase, in primary cultures of hippocampal neurons. Activation of the metabotropic glutamate receptor (mGluR) blocks this NMDA-signaling through PAF and MAP kinases, and the resultant cell death. Recombinant PAF-acetylhydrolase degrades PAF generated by NMDA-receptor activation; the hetrazepine BN50730 (an intracellular PAF receptor antagonist) also inhibits both NMDA-stimulated MAP kinases and neuronal cell death. The finding that the NMDA receptor-PAF-MAP kinase signaling pathway is attenuated by mGluR activation highlights the exquisite interplay between glutamate receptors in the decision making process between neuronal survival and death.  (+info)

Molecular basis of the interaction between plasma platelet-activating factor acetylhydrolase and low density lipoprotein. (4/562)

The platelet-activating factor acetylhydrolases are enzymes that were initially characterized by their ability to hydrolyze platelet-activating factor (PAF). In human plasma, PAF acetylhydrolase (EC 3.1.1.47) circulates in a complex with low density lipoproteins (LDL) and high density lipoproteins (HDL). This association defines the physical state of PAF acetylhydrolase, confers a long half-life, and is a major determinant of its catalytic efficiency in vivo. The lipoprotein-associated enzyme accounts for all of the PAF hydrolysis in plasma but only two-thirds of the protein mass. To characterize the enzyme-lipoprotein interaction, we employed site-directed mutagenesis techniques. Two domains within the primary sequence of human PAF acetylhydrolase, tyrosine 205 and residues 115 and 116, were important for its binding to LDL. Mutation or deletion of those sequences prevented the association of the enzyme with lipoproteins. When residues 115 and 116 from human PAF acetylhydrolase were introduced into mouse PAF acetylhydrolase (which normally does not associate with LDL), the mutant mouse PAF acetylhydrolase associated with lipoproteins. To analyze the role of apolipoprotein (apo) B100 in the formation of the PAF acetylhydrolase-LDL complex, we tested the ability of PAF acetylhydrolase to bind to lipoproteins containing truncated forms of apoB. These studies indicated that the carboxyl terminus of apoB plays a key role in the association of PAF acetylhydrolase with LDL. These data on the molecular basis of the PAF acetylhydrolase-LDL association provide a new level of understanding regarding the pathway for the catabolism of PAF in human blood.  (+info)

Deficiency of platelet-activating factor acetylhydrolase is a severity factor for asthma. (5/562)

Asthma, a family of airway disorders characterized by airway inflammation, has an increasing incidence worldwide. Platelet-activating factor (PAF) may play a role in the pathophysiology of asthma. Its proinflammatory actions are antagonized by PAF acetylhydrolase. A missense mutation (V279F) in the PAF acetylhydrolase gene results in the complete loss of activity, which occurs in 4% of the Japanese population. We asked if PAF acetylhydrolase deficiency correlates with the incidence and severity of asthma in Japan. We found that the prevalence of PAF acetylhydrolase deficiency is higher in Japanese asthmatics than healthy subjects and that the severity of this syndrome is highest in homozygous-deficient subjects. We conclude that the PAF acetylhydrolase gene is a modulating locus for the severity of asthma.  (+info)

Platelet-activating factor may act as an endogenous pulse generator for sheep of luteolytic PGF2alpha release. (6/562)

Pulsatile release of uterine prostaglandin F2alpha (PGF2alpha) induces luteolysis in ruminants. However, the mechanism(s) that initiates and maintains luteolysis has not been defined. The present study tested the hypothesis that the endogenous PGF2alpha pulse generator is uterine-derived platelet-activating factor (PAF). Ovariectomized ewes were given exogenous progesterone (P), estradiol (E), or both (P+E, mimicking the normal luteal phase). Only ewes treated with steroids released PAF into the uterine lumen and had increased PAF:acetylhydrolase activity in the uterine lumen. Steroid treatment also influenced the capacity of the uterus to release PGF2alpha in response to exogenous PAF. PAF infusion did not affect plasma PGF2alpha metabolite (PGFM) levels in control (no steroid treatment) ewes but increased plasma PGFM levels in P+E ewes (P < 0.001) and ewes treated with P or E alone (P < 0.05). Infusion of PAF followed by or coincident with oxytocin (OT) acted in a synergistic manner to increase plasma PGFM levels. Repeated infusion of PAF into the uterus at 1-h intervals induced tachyphylaxis of the PGFM response to PAF; however, sensitivity of the uterus to PAF returned spontaneously by the 6th h. Interferon-tau (IFN-tau) inhibits pulsatile release of PGF2alpha during pregnancy to prevent luteolysis. Exogenous recombinant ovine IFN-tau (50 microgram) inhibited the uterine response to PAF alone or the combined effects of PAF and OT. These results indicate that uterine PAF fulfills many of the criteria for an endogenous PGF2alpha pulse-generator: steroid induction of PAF production and uterine responsiveness to PAF-induced release of PGF; synergistic stimulation of PAF-induced PGF release by OT; inhibition of PAF effects by IFN-tau; and PAF's ability to induce pulses of PGF with a periodicity during a period of chronic exposure of the uterus to PAF.  (+info)

Molecular analysis of an unstable genomic region at chromosome band 11q23 reveals a disruption of the gene encoding the alpha2 subunit of platelet-activating factor acetylhydrolase (Pafah1a2) in human lymphoma. (7/562)

A region of 150 kb has been analysed around a previously isolated, lymphoma associated, translocation breakpoint located at chromosome band 11q23. This balanced and reciprocal translocation, t(11;14)(q32;q23), has been shown to result in the fusion between chromosome 11 specific sequence and the switch gamma4 region of the IGH locus. The LPC gene, encoding a novel proprotein convertase belonging to the furin family, has been identified in this region. In order to characterize further the region surrounding the translocation, we have determined the detailed structure of LPC. Here we show that LPC consists of at least 16 exons covering 25 kb, and that there is a partial duplication, involving mobile genetic elements and containing LPC exons 13-17 in a tail-tail configuration at 65 kb downstream. Since the chromosomal breakpoint lay between these two structures, the intervening region was further analysed and shown to contain at least two unrelated genes. The previously known SM22 gene was localized close to the 3' tail of LPC. Furthermore, we identified the gene encoding the alpha2 subunit of platelet-activating factor acetylhydrolase (Pafah1a2) at the chromosomal breakpoint. The position of another previously identified breakpoint was also located to within the first intron of this gene. Altogether, our results give evidence of a genomic instability of this area of 11q23 and show that Pafah1a2 and not LPC is the gene disrupted by the translocation, suggesting that deregulated Pafah1a2 may have a role in lymphomagenesis.  (+info)

All ApoB-containing lipoproteins induce monocyte chemotaxis and adhesion when minimally modified. Modulation of lipoprotein bioactivity by platelet-activating factor acetylhydrolase. (8/562)

Mildly oxidized LDL has many proinflammatory properties, including the stimulation of monocyte chemotaxis and adhesion, that are important in the development of atherosclerosis. Although ApoB-containing lipoproteins other than LDL may enter the artery wall and undergo oxidation, very little is known regarding their proinflammatory potential. LDL, IDL, VLDL, postprandial remnant particles, and chylomicrons were mildly oxidized by fibroblasts overexpressing 15-lipoxygenase (15-LO) and tested for their ability to stimulate monocyte chemotaxis and adhesion to endothelial cells. When conditioned on 15-LO cells, LDL, IDL, but not VLDL increased monocyte chemotaxis and adhesion approximately 4-fold. Chylomicrons and postprandial remnant particles were also bioactive. Although chylomicrons had a high 18:1/18:2 ratio, similar to that of VLDL, and should presumably be less susceptible to oxidation, they contained (in contrast to VLDL) essentially no platelet-activating factor acetylhydrolase (PAF-AH) activity. Because PAF-AH activity of lipoproteins may be reduced in vivo by oxidation or glycation, LDL, IDL, and VLDL were treated in vitro to reduce PAF-AH activity and then conditioned on 15-lipoxygenase cells. All 3 PAF-AH-depleted lipoproteins, including VLDL, exhibited increased stimulation of monocyte chemotaxis and adhesion. In a similar manner, lipoproteins from Japanese subjects with a deficiency of plasma PAF-AH activity were also markedly more bioactive, and stimulated monocyte adhesion nearly 2-fold compared with lipoproteins from Japanese control subjects with normal plasma PAF-AH. For each lipoprotein, bioactivity resided in the lipid fraction and monocyte adhesion could be blocked by PAF-receptor antagonists. These data suggest that the susceptibility of plasma lipoproteins to develop proinflammatory activity is in part related to their 18:1/18:2 ratio and PAF-AH activity, and that bioactive phospholipids similar to PAF are generated during oxidation of each lipoprotein. Moreover, LDL, IDL, postprandial remnant particles, and chylomicrons and PAF-AH-depleted VLDL all give rise to proinflammatory lipids when mildly oxidized.  (+info)

1-Alkyl-2-acetylglycerophosphocholine esterase is an enzyme that hydrolyzes the ester bond in 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine (also known as platelet-activating factor, PAF), resulting in the production of 1-alkyl-2-lyso-sn-glycero-3-phosphocholine and acetate. This enzyme is involved in the regulation of PAF levels and thus plays a role in the modulation of various physiological processes, including inflammation and allergic responses.

Esterases are a group of enzymes that catalyze the hydrolysis of ester bonds in esters, producing alcohols and carboxylic acids. They are widely distributed in plants, animals, and microorganisms and play important roles in various biological processes, such as metabolism, digestion, and detoxification.

Esterases can be classified into several types based on their substrate specificity, including carboxylesterases, cholinesterases, lipases, and phosphatases. These enzymes have different structures and mechanisms of action but all share the ability to hydrolyze esters.

Carboxylesterases are the most abundant and diverse group of esterases, with a wide range of substrate specificity. They play important roles in the metabolism of drugs, xenobiotics, and lipids. Cholinesterases, on the other hand, specifically hydrolyze choline esters, such as acetylcholine, which is an important neurotransmitter in the nervous system. Lipases are a type of esterase that preferentially hydrolyzes triglycerides and plays a crucial role in fat digestion and metabolism. Phosphatases are enzymes that remove phosphate groups from various molecules, including esters, and have important functions in signal transduction and other cellular processes.

Esterases can also be used in industrial applications, such as in the production of biodiesel, detergents, and food additives. They are often produced by microbial fermentation or extracted from plants and animals. The use of esterases in biotechnology is an active area of research, with potential applications in biofuel production, bioremediation, and medical diagnostics.

Carboxylic ester hydrolases are a class of enzymes that catalyze the hydrolysis of ester bonds in carboxylic acid esters, producing alcohols and carboxylates. This group includes several subclasses of enzymes such as esterases, lipases, and thioesterases. These enzymes play important roles in various biological processes, including metabolism, detoxification, and signal transduction. They are widely used in industrial applications, such as the production of biodiesel, pharmaceuticals, and food ingredients.

Naphthol AS-D esterase is an enzyme that catalyzes the hydrolysis of Naphthol AS-D esters to produce phenol and naphthoic acids. It is commonly found in various tissues, including the liver, kidney, and intestine, and is used as a marker for neutrophil activation in diagnostic tests.

In medical terms, Naphthol AS-D esterase is often referred to as a "non-specific esterase" because it can hydrolyze various types of esters, not just those containing the Naphthol AS-D group. It is also known as "alkaline phosphatase" because it has optimal activity at alkaline pH levels and contains phosphate groups in its active site.

Naphthol AS-D esterase is often used in histological staining techniques to identify and differentiate various types of cells, such as neutrophils, monocytes, and macrophages, based on their enzymatic activity. The presence and intensity of the enzyme activity can provide valuable information about the type, location, and severity of inflammation or tissue damage in various pathological conditions.

A sterol esterase is an enzyme that catalyzes the hydrolysis of sterol esters, which are fatty acid esters of sterols (such as cholesterol) that are commonly found in lipoproteins and cell membranes. Sterol esterases play a crucial role in the metabolism of lipids by breaking down sterol esters into free sterols and free fatty acids, which can then be used in various biochemical processes.

There are several types of sterol esterases that have been identified, including:

1. Cholesteryl esterase (CE): This enzyme is responsible for hydrolyzing cholesteryl esters in the intestine and liver. It plays a critical role in the absorption and metabolism of dietary cholesterol.
2. Hormone-sensitive lipase (HSL): This enzyme is involved in the hydrolysis of sterol esters in adipose tissue, as well as other lipids such as triacylglycerols. It is regulated by hormones such as insulin and catecholamines.
3. Carboxylesterase (CES): This enzyme is a broad-specificity esterase that can hydrolyze various types of esters, including sterol esters. It is found in many tissues throughout the body.

Sterol esterases are important targets for drug development, as inhibiting these enzymes can have therapeutic effects in a variety of diseases, such as obesity, diabetes, and cardiovascular disease.

Acetylesterase is an enzyme that catalyzes the hydrolysis of acetyl esters into alcohol and acetic acid. This enzyme plays a role in the metabolism of various xenobiotics, including drugs and environmental toxins, by removing acetyl groups from these compounds. Acetylesterase is found in many tissues, including the liver, intestine, and blood. It belongs to the class of enzymes known as hydrolases, which act on ester bonds.

Carboxylesterase is a type of enzyme that catalyzes the hydrolysis of ester bonds in carboxylic acid esters, producing alcohol and carboxylate products. These enzymes are widely distributed in various tissues, including the liver, intestines, and plasma. They play important roles in detoxification, metabolism, and the breakdown of xenobiotics (foreign substances) in the body.

Carboxylesterases can also catalyze the reverse reaction, forming esters from alcohols and carboxylates, which is known as transesterification or esterification. This activity has applications in industrial processes and biotechnology.

There are several families of carboxylesterases, with different substrate specificities, kinetic properties, and tissue distributions. These enzymes have been studied for their potential use in therapeutics, diagnostics, and drug delivery systems.

Esters are organic compounds that are formed by the reaction between an alcohol and a carboxylic acid. They are widely found in nature and are used in various industries, including the production of perfumes, flavors, and pharmaceuticals. In the context of medical definitions, esters may be mentioned in relation to their use as excipients in medications or in discussions of organic chemistry and biochemistry. Esters can also be found in various natural substances such as fats and oils, which are triesters of glycerol and fatty acids.

I'm sorry for any confusion, but "Isoflurophate" does not appear to be a recognized term in medical or scientific literature. It is possible that there may be a spelling error or typo in the term you are looking for. If you meant "Isoflurane," which is a commonly used anesthetic in medical and surgical procedures, I can provide a definition for that.

Isoflurane: A volatile halogenated ether liquid used as an inhalational general anesthetic agent. It has a rapid onset and offset of action, making it useful for both induction and maintenance of anesthesia. Isoflurane is also known to have bronchodilatory properties, which can be beneficial in patients with reactive airway disease or asthma.

Alkylation, in the context of medical chemistry and toxicology, refers to the process of introducing an alkyl group (a chemical moiety made up of a carbon atom bonded to one or more hydrogen atoms) into a molecule, typically a biomolecule such as a protein or DNA. This process can occur through various mechanisms, including chemical reactions with alkylating agents.

In the context of cancer therapy, alkylation is used to describe a class of chemotherapeutic drugs known as alkylating agents, which work by introducing alkyl groups onto DNA molecules in rapidly dividing cells. This can lead to cross-linking of DNA strands and other forms of DNA damage, ultimately inhibiting cell division and leading to the death of cancer cells. However, these agents can also affect normal cells, leading to side effects such as nausea, hair loss, and increased risk of infection.

It's worth noting that alkylation can also occur through non-chemical means, such as in certain types of radiation therapy where high-energy particles can transfer energy to electrons in biological molecules, leading to the formation of reactive radicals that can react with and alkylate DNA.

256 (1): 175-8. PMID 7451433. PAF+acetylhydrolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) EC ... The enzyme 1-alkyl-2-acetylglycerophosphocholine esterase (EC 3.1.1.47) catalyzes the reaction 1-alkyl-2-acetyl-sn-glycero-3- ... The systematic name of this enzyme class is 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetohydrolase. Other names in common ... Blank ML, Lee T, Fitzgerald V, Snyder F (1981). "A specific acetylhydrolase for 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine (a ...
... naphthol as d esterase MeSH D08.811.277.352.100.680 - phospholipases MeSH D08.811.277.352.100.680.510 - lysophospholipase MeSH ... cholesterol esterase MeSH D08.811.277.352.100.170 - cholinesterases MeSH D08.811.277.352.100.170.176 - acetylcholinesterase ... endo-1,4-beta xylanases MeSH D08.811.277.450.950.500 - xylan endo-1,3-beta-xylosidase MeSH D08.811.277.656.149 - atp-dependent ... glucan 1,4-beta-glucosidase MeSH D08.811.277.450.420.200.600 - glucan endo-1,3-beta-d-glucosidase MeSH D08.811.277.450.420.375 ...
... apo-salmochelin esterase * EC 3.1.1.108: iron(III)-enterobactin esterase * EC 3.1.1.109: iron(III)-salmochelin esterase * EC ... acetylxylan esterase EC 3.1.1.73: feruloyl esterase EC 3.1.1.74: cutinase EC 3.1.1.75: poly(3-hydroxybutyrate) depolymerase EC ... polyneuridine-aldehyde esterase EC 3.1.1.79: hormone-sensitive lipase EC 3.1.1.80: acetylajmaline esterase EC 3.1.1.81: quorum- ... methyl ester esterase EC 3.1.1.86: rhamnogalacturonan acetylesterase EC 3.1.1.87: fumonisin B1 esterase EC 3.1.1.88: pyrethroid ...
256 (1): 175-8. PMID 7451433. PAF+acetylhydrolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) EC ... The enzyme 1-alkyl-2-acetylglycerophosphocholine esterase (EC 3.1.1.47) catalyzes the reaction 1-alkyl-2-acetyl-sn-glycero-3- ... The systematic name of this enzyme class is 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetohydrolase. Other names in common ... Blank ML, Lee T, Fitzgerald V, Snyder F (1981). "A specific acetylhydrolase for 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine (a ...
Cholesterol Esterase D8.811.277.352.100.150 D8.811.277.352.100.700. (Replaced for 2008 by Sterol Esterase). Chorea C10.228. ... Fura-2 D3.383.312.225.250. gamma-Endorphin D6.472.699.631.525.475.505 D6.472.699.631.525.600.505. gamma-Lipotropin D6.472. ... 1-Deoxynojirimycin D9.477.500.33 D3.132.14. D9.546.412.500.33. 3,5-Cyclic-GMP Phosphodiesterase D8.811.277.352.640.125 D8.811 ... Replaced for 2008 by Shiga Toxin 1). Shiga-Like Toxin II D8.811.277.450.430.700.750.750.124. D12.776.97.275.879. (Replaced for ...
Cholesterol Esterase D8.811.277.352.100.150 D8.811.277.352.100.700. (Replaced for 2008 by Sterol Esterase). Chorea C10.228. ... Fura-2 D3.383.312.225.250. gamma-Endorphin D6.472.699.631.525.475.505 D6.472.699.631.525.600.505. gamma-Lipotropin D6.472. ... 1-Deoxynojirimycin D9.477.500.33 D3.132.14. D9.546.412.500.33. 3,5-Cyclic-GMP Phosphodiesterase D8.811.277.352.640.125 D8.811 ... Replaced for 2008 by Shiga Toxin 1). Shiga-Like Toxin II D8.811.277.450.430.700.750.750.124. D12.776.97.275.879. (Replaced for ...
Cholesterol Esterase D8.811.277.352.100.150 D8.811.277.352.100.700. (Replaced for 2008 by Sterol Esterase). Chorea C10.228. ... Fura-2 D3.383.312.225.250. gamma-Endorphin D6.472.699.631.525.475.505 D6.472.699.631.525.600.505. gamma-Lipotropin D6.472. ... 1-Deoxynojirimycin D9.477.500.33 D3.132.14. D9.546.412.500.33. 3,5-Cyclic-GMP Phosphodiesterase D8.811.277.352.640.125 D8.811 ... Replaced for 2008 by Shiga Toxin 1). Shiga-Like Toxin II D8.811.277.450.430.700.750.750.124. D12.776.97.275.879. (Replaced for ...
Cholesterol Esterase D8.811.277.352.100.150 D8.811.277.352.100.700. (Replaced for 2008 by Sterol Esterase). Chorea C10.228. ... Fura-2 D3.383.312.225.250. gamma-Endorphin D6.472.699.631.525.475.505 D6.472.699.631.525.600.505. gamma-Lipotropin D6.472. ... 1-Deoxynojirimycin D9.477.500.33 D3.132.14. D9.546.412.500.33. 3,5-Cyclic-GMP Phosphodiesterase D8.811.277.352.640.125 D8.811 ... Replaced for 2008 by Shiga Toxin 1). Shiga-Like Toxin II D8.811.277.450.430.700.750.750.124. D12.776.97.275.879. (Replaced for ...
Cholesterol Esterase D8.811.277.352.100.150 D8.811.277.352.100.700. (Replaced for 2008 by Sterol Esterase). Chorea C10.228. ... Fura-2 D3.383.312.225.250. gamma-Endorphin D6.472.699.631.525.475.505 D6.472.699.631.525.600.505. gamma-Lipotropin D6.472. ... 1-Deoxynojirimycin D9.477.500.33 D3.132.14. D9.546.412.500.33. 3,5-Cyclic-GMP Phosphodiesterase D8.811.277.352.640.125 D8.811 ... Replaced for 2008 by Shiga Toxin 1). Shiga-Like Toxin II D8.811.277.450.430.700.750.750.124. D12.776.97.275.879. (Replaced for ...
Cholesterol Esterase D8.811.277.352.100.150 D8.811.277.352.100.700. (Replaced for 2008 by Sterol Esterase). Chorea C10.228. ... Fura-2 D3.383.312.225.250. gamma-Endorphin D6.472.699.631.525.475.505 D6.472.699.631.525.600.505. gamma-Lipotropin D6.472. ... 1-Deoxynojirimycin D9.477.500.33 D3.132.14. D9.546.412.500.33. 3,5-Cyclic-GMP Phosphodiesterase D8.811.277.352.640.125 D8.811 ... Replaced for 2008 by Shiga Toxin 1). Shiga-Like Toxin II D8.811.277.450.430.700.750.750.124. D12.776.97.275.879. (Replaced for ...
Cholesterol Esterase D8.811.277.352.100.150 D8.811.277.352.100.700. (Replaced for 2008 by Sterol Esterase). Chorea C10.228. ... Fura-2 D3.383.312.225.250. gamma-Endorphin D6.472.699.631.525.475.505 D6.472.699.631.525.600.505. gamma-Lipotropin D6.472. ... 1-Deoxynojirimycin D9.477.500.33 D3.132.14. D9.546.412.500.33. 3,5-Cyclic-GMP Phosphodiesterase D8.811.277.352.640.125 D8.811 ... Replaced for 2008 by Shiga Toxin 1). Shiga-Like Toxin II D8.811.277.450.430.700.750.750.124. D12.776.97.275.879. (Replaced for ...
Cholesterol Esterase D8.811.277.352.100.150 D8.811.277.352.100.700. (Replaced for 2008 by Sterol Esterase). Chorea C10.228. ... Fura-2 D3.383.312.225.250. gamma-Endorphin D6.472.699.631.525.475.505 D6.472.699.631.525.600.505. gamma-Lipotropin D6.472. ... 1-Deoxynojirimycin D9.477.500.33 D3.132.14. D9.546.412.500.33. 3,5-Cyclic-GMP Phosphodiesterase D8.811.277.352.640.125 D8.811 ... Replaced for 2008 by Shiga Toxin 1). Shiga-Like Toxin II D8.811.277.450.430.700.750.750.124. D12.776.97.275.879. (Replaced for ...
Cholesterol Esterase D8.811.277.352.100.150 D8.811.277.352.100.700. (Replaced for 2008 by Sterol Esterase). Chorea C10.228. ... Fura-2 D3.383.312.225.250. gamma-Endorphin D6.472.699.631.525.475.505 D6.472.699.631.525.600.505. gamma-Lipotropin D6.472. ... 1-Deoxynojirimycin D9.477.500.33 D3.132.14. D9.546.412.500.33. 3,5-Cyclic-GMP Phosphodiesterase D8.811.277.352.640.125 D8.811 ... Replaced for 2008 by Shiga Toxin 1). Shiga-Like Toxin II D8.811.277.450.430.700.750.750.124. D12.776.97.275.879. (Replaced for ...
Cholesterol Esterase D8.811.277.352.100.150 D8.811.277.352.100.700. (Replaced for 2008 by Sterol Esterase). Chorea C10.228. ... Fura-2 D3.383.312.225.250. gamma-Endorphin D6.472.699.631.525.475.505 D6.472.699.631.525.600.505. gamma-Lipotropin D6.472. ... 1-Deoxynojirimycin D9.477.500.33 D3.132.14. D9.546.412.500.33. 3,5-Cyclic-GMP Phosphodiesterase D8.811.277.352.640.125 D8.811 ... Replaced for 2008 by Shiga Toxin 1). Shiga-Like Toxin II D8.811.277.450.430.700.750.750.124. D12.776.97.275.879. (Replaced for ...
Cholesterol Esterase D8.811.277.352.100.150 D8.811.277.352.100.700. (Replaced for 2008 by Sterol Esterase). Chorea C10.228. ... Fura-2 D3.383.312.225.250. gamma-Endorphin D6.472.699.631.525.475.505 D6.472.699.631.525.600.505. gamma-Lipotropin D6.472. ... 1-Deoxynojirimycin D9.477.500.33 D3.132.14. D9.546.412.500.33. 3,5-Cyclic-GMP Phosphodiesterase D8.811.277.352.640.125 D8.811 ... Replaced for 2008 by Shiga Toxin 1). Shiga-Like Toxin II D8.811.277.450.430.700.750.750.124. D12.776.97.275.879. (Replaced for ...
1-alkyl-2-acetylglycerophosphocholine esterase activity. IEP. Enrichment. MF. GO:0003989. acetyl-CoA carboxylase activity. IEP ...
Zhang, W., Dong, C., Hutchinson, S. M., Ge, C., Wang, F. & Feng, H., 1 Mar 2018, In: Current Pollution Reports. 4, 1. Research ... Dombkowski, A. A., Sultana, K. Z. & Craig, D. B., 21 Jan 2014, In: FEBS Letters. 588, 2, p. 206-212 7 p.. Research output: ... Miles, D. B., Sinervo, B., Hazard, L. C., Svensson, E. I. & Costa, D., 1 Aug 2007, In: Functional Ecology. 21, 4, p. 653-665 13 ... Li, Y., Guo, L. & Feng, H., 1 Dec 2015, In: Current Pollution Reports. 1, 4, p. 191-202 12 p.. Research output: Contribution to ...
2.82% (2/71). 7.5. 5e-05. 0.000604. GO:0009070. serine family amino acid biosynthetic process. 2.82% (2/71). 7.5. 5e-05. ... 2.82% (2/71). 7.08. 9.3e-05. 0.00103. GO:0009069. serine family amino acid metabolic process. 2.82% (2/71). 6.18. 0.000346. ... 2.82% (2/71). 4.25. 0.004999. 0.025569. GO:0003755. peptidyl-prolyl cis-trans isomerase activity. 4.23% (3/71). 3.08. 0.00542. ... 2.82% (2/71). 5.69. 0.000686. 0.00537. GO:1901607. alpha-amino acid biosynthetic process. 2.82% (2/71). 5.5. 0.000899. 0.006642 ...
English, C. J., Mayr, H. L., Lohning, A. E. & Reidlinger, D. P., 1 Jun 2022, In: Nutrition Reviews. 80, 6, p. 1371-1391 21 p., ... Milne, N., Longeri, L., Patel, A., Pool, J., Olson, K., Basson, A. & Gross, A. R., Dec 2022, In: BMC Pediatrics. 22, 1, 721.. ... Reid, M. A. & Forrest, K. A. T., 4 Apr 2022, In: The Asia Pacific Scholar. 7, 2, p. 1-5 5 p.. Research output: Contribution to ... Wallis, K. A., Zwar, N. A. & Glasziou, P. P., 15 Aug 2022, In: Medical Journal of Australia. 217, 4, p. 218 1 p.. Research ...
Here, we show that cadherin 2 (CDH2) and CDH4 cooperate to regulate radial migration in mouse brain via the protein tyrosine ... Cadherin 2/4 signaling via PTP1B and catenins is crucial for nucleokinesis during radial neuronal migration in the neocortex. ... Cadherin 2/4 signaling via PTP1B and catenins is crucial for nucleokinesis during radial neuronal migration in the neocortex. ... Here, we show that cadherin 2 (CDH2) and CDH4 cooperate to regulate radial migration in mouse brain via the protein tyrosine ...
2-Fluoro-2-deoxyglucose use Fluorodeoxyglucose F18 2H-Benzo(a)quinolizin-2-ol, 2-Ethyl-1,3,4,6,7,11b-hexahydro-3-isobutyl-9,10- ... 2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ... 2-Chloroethyl Alcohol use Ethylene Chlorohydrin 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate ...
Receptor Tipo 1 de Galanina. Receptor de Galanina Tipo 1. Receptor, Galanin, Type 2. Receptor Tipo 2 de Galanina. Receptor de ... Glucano 1,3-beta-Glucosidase. Glucano 1,3-beta-Glucosidasa. Glucan 1,4-beta-Glucosidase. Glucano 1,4-beta-Glucosidase. Glucano ... Receptor PAR-2. Receptor PAR-2. Receptor, Parathyroid Hormone, Type 1. Receptor Tipo 1 de Hormônio Paratireóideo. Receptor de ... Receptor Tipo 2 de Angiotensina. Receptor de Angiotensina Tipo 2. Receptor, Bradykinin B1. Receptor B1 de Bradicinina. Receptor ...
2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-glucose use ... 2,6-Dichlorophenolindophenol use 2,6-Dichloroindophenol 3 beta-Hydroxy-delta-5-Steroid Dehydrogenase use Progesterone Reductase ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
Phospholipase A2 Activity (consuming 1,2-dipalmitoylphosphatidylcholine). *Phospholipase A2 Activity Consuming 1,2- ...
Polyneuridine-aldehyde esterase [3.1.1.78]. (0,0). (0,0,0). - 1: Protein phosphatase methylesterase-1 [3.1.1.89]. (1,0). (1,0,0 ... INHERITED FROM: Acetylxylan esterase. beta-lactamase/transpeptidase-like. 0.9483. INHERITED FROM: Teichoic acid D-alanine ... INHERITED FROM: Acetylxylan esterase. beta-lactamase/transpeptidase-like. 0.8771. INHERITED FROM: Teichoic acid D-alanine ... Pimeloyl-[acyl-carrier protein] methyl ester esterase [3.1.1.85]. (1,1). (1,0,0). ...
1. Quality of life and factors associated among public university employees retired due to disabilities / Qualidade de vida e ... 2. Análise das gestações ectópicas íntegras tratadas com o protocolo de dose única de metotrexato / Analysis of unruptured ... Adult , Aged , Humans , Male , Female , Middle Aged , Aged, 80 and over , Blood Pressure/physiology , Diabetes Mellitus, Type 2 ... The distribution of blood pressure and associated factors of the elderly with type 2 diabetes in Jiangsu Province / 中华预防医学杂志 ...
... diphosphatase activityserine-type endopeptidase activityepoxide hydrolase activityhelicase activityjuvenile-hormone esterase ... reproductionSNARE bindingnucleotide bindingtRNA 2-phosphotransferase activitynuclear chromosomecytoplasmic chromosomemitotic ... transcription factor activityRNA bindingmRNA bindingstructural constituent of ribosomeantigen bindingcatalytic activity1-alkyl- ... 2-acetylglycerophosphocholine esterase activity2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activityGTPase ...
1. Terminal deletion of the short arm of chromosome 6 (6P25 3P 243): a literature review and case report of a Brazilian child ... 2. Investigação Citogenômica de Crianças com Doença Cardíaca Congênita: Experiência de um Centro no Brasil / Cytogenomics ... Copy number variations (CNV) were detected by CNV-seq and validated by real-time PCR.@*RESULTS@#Proband 1 was found to carry a ... Child , Humans , Male , Chromosome Deletion , Chromosomes , Chromosomes, Human, Pair 2 , In Situ Hybridization, Fluorescence , ...
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  • Predicted to enable 1-alkyl-2-acetylglycerophosphocholine esterase activity. (wormbase.org)
  • and Protein Her-1. (wormbase.org)
  • Here, we show that cadherin 2 (CDH2) and CDH4 cooperate to regulate radial migration in mouse brain via the protein tyrosine phosphatase 1B (PTP1B) and α- and β-catenins. (ox.ac.uk)
  • In C. elegans, blos-1 is involved in endosomal transport. (wormbase.org)
  • There are multiple enzymes with this function: Lipoprotein-associated phospholipase A2 Platelet-activating factor acetylhydrolase 2, cytoplasmic Platelet-activating factor acetylhydrolase 1b: regulatory subunit 1, catalytic subunit 2, catalytic subunit 3 This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. (wikipedia.org)
  • There are multiple enzymes with this function: Lipoprotein-associated phospholipase A2 Platelet-activating factor acetylhydrolase 2, cytoplasmic Platelet-activating factor acetylhydrolase 1b: regulatory subunit 1, catalytic subunit 2, catalytic subunit 3 This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. (wikipedia.org)
  • Other names in common use include 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetylhydrolase, and alkylacetyl-GPC:acetylhydrolase. (wikipedia.org)
  • A lipoprotein-associated PHOSPHOLIPASE A2 which modulates the action of PLATELET ACTIVATING FACTOR by hydrolyzing the SN-2 ester bond to yield the biologically inactive lyso-platelet-activating factor. (nih.gov)
  • Molecular basis of unique specificity and regulation of group VIA calcium-independent phospholipase A(2) (PNPLA9) and its role in neurodegenerative diseases. (beds.ac.uk)
  • Lipoprotein-associated phospholipase A(2) and risk of coronary disease, stroke, and mortality: collaborative analysis of 32 prospective studies. (nih.gov)
  • BACKGROUND: Lipoprotein-associated phospholipase A(2) (Lp-PLA(2)), an inflammatory enzyme expressed in atherosclerotic plaques, is a therapeutic target being assessed in trials of vascular disease prevention. (nih.gov)

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