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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. 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 ...

  4. 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 ...

  5. Autophosphorylation - Wikipedia

    en.wikipedia.org/wiki/Autophosphorylation

    Dimerization brings the two receptors into close proximity. This stimulates the kinase activity of EGFR, which leads to transautophosphorylation on multiple tyrosine residues in C-terminal end of the molecule. The phosphorylated tyrosine residue can then serve as a docking site for downstream signaling proteins. [21] (Fig. 1).

  6. 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.

  7. Protein kinase - Wikipedia

    en.wikipedia.org/wiki/Protein_kinase

    Above is a ball-and-stick model of the inorganic phosphate molecule (H PO 4 2−).Colour coding: P (orange); O (red); H (white). The chemical activity of a protein kinase involves removing a phosphate group from ATP and covalently attaching it to one of three amino acids that have a free hydroxyl group.

  8. Protein phosphatase 1 - Wikipedia

    en.wikipedia.org/wiki/Protein_phosphatase_1

    Protein kinase A (cAMP-dependent protein kinase) can reduce the activity of PP1. The glycogen binding region, GM, becomes phosphorylated, which causes its dissociation from the catalytic PP1 unit. [12] This separation of the catalytic PP1 unit, glycogen, and other substrates causes a significant decrease in dephosphorylation.

  9. TP53-inducible glycolysis and apoptosis regulator - Wikipedia

    en.wikipedia.org/wiki/TP53-inducible_glycolysis...

    TIGAR can act to prevent a cell progressing through the stages of its growth and division cycle by decreasing cellular ATP levels. [12] This is known as cell cycle arrest. [ 12 ] This function of TIGAR forms part of the p53 mediated DNA damage response where, under low levels of cellular stress, p53 initiates cell cycle arrest to allow the cell ...