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tyrosine

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(biochemistry) A nonessential amino acid C <sub>9</sub> H <sub>11</sub> NO <sub>3</sub> found in most animal proteins, especially casein.

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Among the regulators of p130Cas/BCAR1 tyrosine phosphorylation, receptor tyrosine kinases (RTKs) and integrins play a prominent role.
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It does so by the covalent modification of histidine (most strongly), lysine, cysteine, and tyrosine residues.
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Another reaction is tyrosine nitration; however peroxynitrite does not react directly with tyrosine.
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The presence of a tyrosine-phosphorylated ITIM (immunoreceptor tyrosine-based inhibitory motif) sequence in the B2 receptor is necessary to mediate this interaction and subsequently the antiproliferative effect of bradykinin.
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Both RTKs and integrin activation affect p130Cas/BCAR1 tyrosine phosphorylation and represent an efficient means by which cells utilize signals coming from growth factors and integrin activation to coordinate cell responses.
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Upon this activation, the TCR co-receptor CD4 or CD8 binds to the MHC, activating the co-receptor associated tyrosine kinase Lck.
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At any point in this process, the β-arrestins may also recruit other proteins—such as the non-receptor tyrosine kinase (nRTK), c-SRC—which may activate ERK1/2, or other mitogen-activated protein kinase (MAPK) signaling through, for example, phosphorylation of the small GTPase, Ras, or recruit the proteins of the ERK cascade directly (i.e., Raf-1, MEK, ERK-1/2) at which point signaling is initiated due to their close proximity to one another.
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There is evidence for roles as signal transducers in nearly all other types of receptor-mediated signaling, including integrins, receptor tyrosine kinases (RTKs), cytokine receptors (JAK/STATs), as well as modulation of various other "accessory" proteins such as GEFs, guanine-nucleotide dissociation inhibitors (GDIs) and protein phosphatases.
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Pepsin is most efficient in cleaving peptide bonds between hydrophobic and preferably aromatic amino acids such as phenylalanine, tryptophan, and tyrosine.
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Tyrosine kinases are either receptor molecules, which contain transmembrane and extracellular domains, or nonreceptor proteins, which are located intracellularly.
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At Salk, he worked in Walter Eckhart's laboratory alongside Tony Hunter and witnessed Hunter's discovery of tyrosine phosphorylation.
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As of 2009, there are 6 known types of enzyme-linked receptors: Receptor tyrosine kinases; Tyrosine kinase associated receptors; Receptor-like tyrosine phosphatases; Receptor serine/threonine kinases; Receptor guanylyl cyclases and histidine kinase associated receptors.
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In hepatitis B, lamivudine resistance was first described in the YMDD (tyrosine-methionine-aspartate-aspartate) locus of the HBV reverse transcriptase gene.
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RTK-dependent p130Cas/BCAR1 tyrosine phosphorylation and the subsequent binding with specific downstream signaling molecule modulate cell processes such as actin cytoskeleton remodeling, cell adhesion, proliferation, migration, invasion and survival.
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U A U = tyrosine
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