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Cleavage (embryology)
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 a compact mass called the morula. Cleavage ends with the formation of the blastula, or of the blastocyst in
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The Yolk’s On Us: Unraveling the Secrets of Vitellogenesis
Hold onto your ovaries, folks. We’re about to dive into the wild world of Vitellogenesis – the cellular rave where eggs get their groove on. Picture this: You’re a lonely liver cell, minding your own business, when suddenly – BAM! – you’re hit with a tsunami of estradiol. It’s like Mother Nature’s Red Bull, and
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The PVN Powerhouse: How the Paraventricular Nucleus Rules Hormone Secretion
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 cluster of cells that’s like the body’s own hormone factory. But we’re not talking
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Vitellogenin 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, it is only found in the blood or hemolymph of females…
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, it is only found in the blood or hemolymph of females, and can therefore be
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Vitellin is essential in the fertilization process, and embryonic development in egg-laying organisms
Vitellin is a protein found in the egg yolk. It is a phosphoprotein. Vitellin is a generic name for major of many yolk proteins. Vitellin has been known since the 1900s. The periodic acid-Schiff method and Sudan black B dye was used to help determine that Vitellin is a glycolipoprotein because it stained positive when tested. This protein was
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Protein Phosphorylation Was First Reported in 1906
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 sites that are phosphorylated. The reverse reaction of phosphorylation is called dephosphorylation, and is catalyzed by
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Phosphorylation
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), the “high-energy” exchange medium in the cell. During aerobic respiration, ATP is synthesized
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Human cells contain a DNA-activated protein kinase that phosphorylates simian virus 40 T antigen, mouse p53, and the human Ku autoantigen
Abstract HeLa cells contain a serine/threonine protein kinase (DNA-PK) that is strongly activated in vitro by low concentrations of double-stranded DNA (dsDNA). Activation was specific for dsDNA; both natural DNAs and synthetic oligonucleotides functioned as kinase activators. The fact that DNA-PK activity was rapidly inhibited by incubation with dsDNA and ATP suggests that DNA-PK activity
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Non-homologous end joining (NHEJ) is a pathway that repairs double-strand breaks in DNA. NHEJ is active in both non-dividing and proliferating cells.
Non-homologous end joining (NHEJ) is a pathway that repairs double-strand breaks in DNA. It is called “non-homologous” because the break ends are directly ligated without the need for a homologous template, in contrast to homology directed repair (HDR), which requires a homologous sequence to guide repair. NHEJ is active in both non-dividing and proliferating cells, while HDR is not readily
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Ku is a dimeric protein complex that binds to DNA double-strand break ends and is required for the non-homologous end joining (NHEJ) pathway of DNA repair
Ku is evolutionarily conserved from bacteria to humans. The ancestral bacterial Ku is a homodimer (two copies of the same protein bound to each other).[2] Eukaryotic Ku is a heterodimer of two polypeptides, Ku70 (XRCC6) and Ku80 (XRCC5), so named because the molecular weight of the human Ku proteins is around 70 kDa and 80 kDa. The two Ku subunits form a basket-shaped structure that threads onto
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