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  2. Protein phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Protein_phosphorylation

    Model of a phosphorylated serine residue Serine in an amino acid chain, before and after phosphorylation.. 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.

  3. Arachidonic acid - Wikipedia

    en.wikipedia.org/wiki/Arachidonic_acid

    Arachidonic acid (AA, sometimes ARA) is a polyunsaturated omega−6 fatty acid 20:4(ω−6), or 20:4(5,8,11,14). [2] [3] If its precursors or diet contains linoleic acid it is formed by biosynthesis and can be deposited in animal fats. It is a precursor in the formation of leukotrienes, prostaglandins, and thromboxanes. [4]

  4. Phosphomimetics - Wikipedia

    en.wikipedia.org/wiki/Phosphomimetics

    However some non-phosphorylated amino acids appear chemically similar to phosphorylated amino acids. Therefore, by replacing an amino acid, the protein may maintain a higher level of activity. For example, aspartic acid can be considered chemically similar to phospho-serine, due to it also carrying a negative charge. Therefore, when an aspartic ...

  5. Phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Phosphorylation

    However, due to the chemical lability of these phosphorylated residues, and in marked contrast to Ser, Thr and Tyr phosphorylation, the analysis of phosphorylated histidine (and other non-canonical amino acids) using standard biochemical and mass spectrometric approaches is much more challenging [16] [17] [18] and special procedures and ...

  6. Glycogen phosphorylase - Wikipedia

    en.wikipedia.org/wiki/Glycogen_phosphorylase

    The glycogen phosphorylase monomer is a large protein, composed of 842 amino acids with a mass of 97.434 kDa in muscle cells. While the enzyme can exist as an inactive monomer or tetramer, it is biologically active as a dimer of two identical subunits.

  7. Tyrosine phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Tyrosine_phosphorylation

    In the late G2 phase, it is present as an inactive complex of tyrosine-phosphorylated p34cdc2 and unphosphorylated cyclin Bcdc13. In M phase, its activation as an active MPF displaying histone H1 kinase (H1K) originates from the concomitant tyrosine dephosphorylation of the p34cdc2 subunit and the phosphorylation of the cylin Bcdc13 subunit.

  8. Red dye No. 3 has been banned, but what about other ...

    lite.aol.com/.../ef5af10b3aca66d0033d3f239546f1aa

    Makers of ingested drugs like cough syrups have until January 2028. Who is concerned about these dyes and why? Consumer advocates, including the Center for Science in the Public Interest, had long lobbied to ban Red 3 from food because of the rat-cancer link. The dye was prohibited for decades in cosmetics, but not in food or ingested medications.

  9. CYP3A4 - Wikipedia

    en.wikipedia.org/wiki/CYP3A4

    1576 n/a Ensembl ENSG00000160868 n/a UniProt P08684 n/a RefSeq (mRNA) NM_001202855 NM_001202856 NM_001202857 NM_017460 n/a RefSeq (protein) NP_001189784 NP_059488 n/a Location (UCSC) Chr 7: 99.76 – 99.78 Mb n/a PubMed search n/a Wikidata View/Edit Human Cytochrome P450 3A4 (abbreviated CYP3A4) (EC 1.14.13.97) is an important enzyme in the body, mainly found in the liver and in the intestine ...