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  2. Tyrosine - Wikipedia

    en.wikipedia.org/wiki/Tyrosine

    Tyrosine ball and stick model spinning. L-Tyrosine or tyrosine (symbol Tyr or Y) [2] or 4-hydroxyphenylalanine is one of the 20 standard amino acids that are used by cells to synthesize proteins. It is a conditionally essential amino acid with a polar side group.

  3. Everything You Need To Know about Tyrosine - AOL

    www.aol.com/lifestyle/everything-know-tyrosine...

    Tyrosine is an amino acid made by the body. It may boost cognitive function, especially during periods of stress. Many foods contain tyrosine. Tyrosine is an amino acid made by the body. It may ...

  4. Tyrosinemia type I - Wikipedia

    en.wikipedia.org/wiki/Tyrosinemia_type_I

    Patients received amino acid supplements lacking tyrosine and phenylalanine, most often by drinking a specially engineered formula, in order to acquire sufficient protein. It is recommended that tyrosine levels remain below 500 μmol/L. [5] Phenylalnine is the precursor to tyrosine. The ideology behind maintaining low tyrosine levels is two-fold.

  5. Bruton's tyrosine kinase - Wikipedia

    en.wikipedia.org/wiki/Bruton's_tyrosine_kinase

    Bruton's+tyrosine+kinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Human BTK genome location and BTK gene details page in the UCSC Genome Browser. Overview of all the structural information available in the PDB for UniProt: Q06187 (Tyrosine-protein kinase BTK) at the PDBe-KB

  6. Thyroid hormones - Wikipedia

    en.wikipedia.org/wiki/Thyroid_hormones

    The thyroid system of the thyroid hormones T 3 and T 4 [1] Thyroid hormones are two hormones produced and released by the thyroid gland, triiodothyronine (T 3) and thyroxine (T 4). They are tyrosine-based hormones that are primarily responsible for regulation of metabolism. T 3 and T 4 are partially composed of iodine, derived from food. [2]

  7. Non-receptor tyrosine kinase - Wikipedia

    en.wikipedia.org/wiki/Non-receptor_tyrosine_kinase

    There are two tyrosine phosphorylation sites within the activation loop. It is known that the autophosphorylation of the first of these tyrosines is important for stimulation of tyrosine kinase activity and biological function, [19] but the role of the second tyrosine is not clear.

  8. Tyrosine aminotransferase - Wikipedia

    en.wikipedia.org/wiki/Tyrosine_aminotransferase

    In humans, the tyrosine aminotransferase protein is encoded by the TAT gene. [7] A deficiency of the enzyme in humans can result in what is known as type II tyrosinemia, wherein there is an abundance of tyrosine as a result of tyrosine failing to undergo an aminotransferase reaction to form 4-hydroxyphenylpyruvate. [8]

  9. Immunoreceptor tyrosine-based activation motif - Wikipedia

    en.wikipedia.org/wiki/Immunoreceptor_tyrosine...

    Other non-catalytic tyrosine-phosphorylated receptors carry a conserved inhibitory motif that, when phosphorylated, results in the inhibition of the signaling pathway via recruitment of phosphatases, namely SHP-1, SHP-2 and SHIP1. This serves not only for inhibition and regulation of signalling pathways related to ITAM-based signalling, but ...