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December 2023

Juvenile hormone epoxide hydrolase (JHEH) is an enzyme that inactivates insect juvenile hormones. This inactivation is accomplished through hydrolysis of the epoxide functional group contained within these hormones into diols. JHEH is one of two enzymes involved in the termination of signaling properties of the various juvenile

The enzyme juvenile hormone esterase (EC 3.1.1.59, systematic name methyl-(2E,6E,10R)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate acylhydrolase, JH esterase) catalyzes the hydrolysis of juvenile hormone: (1) juvenile hormone I + H2O = juvenile hormone I acid + methanol (2) juvenile hormone III + H2O = juvenile hormone III acid + methanol Nomenclature and function This enzyme belongs to the

The conjugate (10S,11S) JH diol phosphate is the product of a two-step enzymatic process: conversion of JH to JH diol and then addition of a phosphate group to C10. Halarnkar, P.P., Jackson, G.P., Straub, K.M., Schooley, D.A., 1993. Juvenile hormone catabolism in Manduca sexta - homologue selectivity of catabolism

Food allergies are potentially fatal immune-mediated disorders that are growing globally. The relationship between sex and food allergy remains incompletely understood. Here we tested the hypothesis that, should sex influence the clinical response to food allergens, this would be reflected

The receptor is a non-covalent heterodimer of two proteins, the EcR protein and ultraspiracle protein (USP). These nuclear hormone receptor proteins are the insect orthologs of the mammalian farnesoid X receptor (FXR) and retinoid X receptor (RXR) proteins, respectively. It binds to and is activated by ecdysteroids. Insect ecdysone receptors are currently better characterized

Juvenile hormones (JHs) are a group of acyclic sesquiterpenoids that regulate many aspects of insect physiology. The first discovery of a JH was by Vincent Wigglesworth. JHs regulate development, reproduction, diapause, and polyphenisms. The chemical formula for juvenile hormone is C18H30O3. Riddiford, L. M. (1994). "Cellular and molecular actions

In embryology, cleavage is the division of cells in the early development of the embryo, following fertilization. The zygotes of many species undergo rapid cell cycles with no significant overall growth, producing a cluster of cells the same size as the original zygote. The different cells derived from cleavage are called blastomeres and form

Diagram of vitellogenesis in the digenean Crepidostomum metoecus. GER: granular endoplasmic reticulum; L: lipid droplet; M: mitochondrion; N: nucleus; Nl: nucleolus; SG: shell globule; SGC: shell globule cluster. Greani S, Quilichini Y, Marchand B (2016). "Ultrastructural study of vitellogenesis and oogenesis of Crepidostomum metoecus

Hold onto your hypothalamus, folks! We're about to dive into the wild world of the Paraventricular Nucleus (PVN), where tiny cells pack a mighty hormonal punch! Picture this: deep in the brain's control center, the hypothalamus, sits the PVN - a

Vitellogenin (VTG or less popularly known as VG) (from Latin vitellus, yolk, and genero, I produce) is a precursor of egg yolk that transports protein and some lipid from the liver through the blood to the growing oocytes where it becomes part of the yolk. Normally,

Vitellin is a protein found in the egg yolk. It is a phosphoprotein. Vitellin is a generic name for major of many yolk proteins. Vitellins at the U.S. National Library of Medicine Medical Subject Headings (MeSH) KUNKEL, JOSEPH G.; JOHN H. NORDIN (1985). "Yolk Proteins. 2.2 Vitellin, the major

Protein phosphorylation is a reversible post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or otherwise modifying its function. Approximately 13,000 human proteins have

In biochemistry, phosphorylation is the attachment of a phosphate group to a molecule or an ion.[1] This process and its inverse, dephosphorylation, are common in biology.[2] Protein phosphorylation often activates (or deactivates) many enzymes.[3][4] During respiration and photosynthesis Phosphorylation is essential to the processes of both anaerobic and aerobic respiration, which involve the production of adenosine triphosphate (ATP),