Übersetzung für 'tyrosine residue' von Englisch nach Deutsch

tyrosine residue

Tyrosinrest {m}biochem.

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tyrosine nitration

Tyrosin-Nitrierung {f} [auch: Tyrosinnitrierung]biochem.

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tyrosine kinase

Tyrosinkinase {f}biochem.

tyrosine phosphorylation

Tyrosinphosphorylierung {f}biochem.

tyrosine metabolism

Tyrosinstoffwechsel {m} [auch: Tyrosin-Stoffwechsel]chem.

Tyrosinmetabolismus {m} [auch: Tyrosin-Metabolismus]chem.

tyrosine synthesis

Tyrosinsynthese {f}biochem.

tyrosine radical

Tyrosinradikal {n} [auch: Tyrosin-Radikal]biochem.

cytosolic tyrosine kinase

zytosolische Tyrosinkinase {f}biochem.

receptor tyrosine kinase

Rezeptortyrosinkinase {f}biochem.

tyrosine kinase activity

Tyrosinkinase-Aktivität {f}med.

tyrosine hydroxylase <TYH>

Tyrosinhydroxylase {f} <TYH>biochem.

tyrosine kinase receptor

Tyrosinkinaserezeptor {m} [auch: Tyrosinkinase-Rezeptor]biochem.

tubulin-tyrosine ligase

Tubulin-Tyrosin-Ligase {f}biochem.

tyrosine kinase inhibitor

Tyrosinkinase-Hemmer {m}pharm.

receptor tyrosine kinase <RTK>

Rezeptor-Tyrosinkinase {f} <RTK>biochem.

tyrosine kinase inhibitor <TKI>

Tyrosinkinase-Inhibitor {m} <TKI> [auch: Tyrosinkinaseinhibitor]pharm.

tyrosine kinase inhibitors <TKIs>

Tyrosinkinase-Inhibitoren {pl} <TKI> [Tyrosinkinaseinhibitoren]pharm.

protein tyrosine phosphatase <PTP>

Proteintyrosinphosphatase {f} <PTP>biochem.

tyrosine-kinase inhibitor <TKI>

Tyrosinkinasehemmer {m} <TKI>pharm.

tyrosine <Tyr, Y> [C9H11NO3]

Tyrosin {n} <Tyr, Y>biochem.

• The relatively unstructured and unconserved SR region (amino acids 86-638) contains a focal adhesion targeting (FAT) domain, including a tyrosine residue at position 442, which interacts with SH2 domains of tensin1 Rho-GTPases are involved in regulating cell morphology (through cytoskeletal organization) and migration (through focal adhesion formation).
• A tyrosine residue within the kinase domain of Tec kinase is then phosphorylated by Src family kinases.
• IRAK-1 also contains a tyrosine residue (Tyr262) that conformationally changes the active site of the IRAK-1 by inhibiting the hydrophilic pocket behind the binding site and thereby allows the IRAK-1 to remain in an active state.
• This inner part of the pocket contains several amino acids with nonpolar side chains necessary for stabilization of the hydrophobic phenyl ring in addition to a tyrosine residue important for hydrogen bond formation with the ring's 4-hydroxyl group.
• The AMPylation on a tyrosine residue of the switch 1 region blocks the interaction of the GTPases with downstream substrates such as PAK.

• L-DOPA is a tyrosine residue that bears an additional hydroxyl group.
• A catalytic cycle has been proposed that involves this di-iron center and at least one transient protein-derived free radical, which is probably formed on a tyrosine residue.
• This pocket has a tyrosine residue that is able to form van der Waals interactions with the correctly paired nucleotide.
• Tyrosine sulfation is a posttranslational modification in which a tyrosine residue of a protein is sulfated by a tyrosylprotein sulfotransferase (TPST) typically in the Golgi apparatus.
• In conjunction with dimerization and kinase activation, the receptor molecules undergo conformational changes, which allow a basal kinase activity to phosphorylate a critical tyrosine residue, thereby "unlocking" the kinase, leading to full enzymatic activity directed toward other tyrosine residues in the receptor molecules as well as other substrates for the kinase.

• SH2 domains typically bind a phosphorylated tyrosine residue in the context of a longer peptide motif within a target protein, and SH2 domains represent the largest class of known pTyr-recognition domains.
• Tyrosine sulfation is a posttranslational modification where a sulfate group is added to a tyrosine residue of a protein molecule.
• Here, SHP-1 binds directly to a tyrosine residue (at position 429) on EpoR and removes phosphate groups from the receptor-associated JAK2.
• Next, a nearby tyrosine residue deprotonates the ε-amino group of the lysine residue.
• Gastrin II has identical amino acid composition to Gastrin I, the only difference is that the single tyrosine residue is sulfated in Gastrin II.

• A reddish-brown coloration or precipitate indicates the presence of tyrosine residue which occur in nearly all proteins.
• At both of the DNA duplexes, the bonding of the phosphate group to tyrosine residues leave a 3’ OH group free in the DNA backbone.
• A non-receptor tyrosine kinase (nRTK) is a cytosolic enzyme that is responsible for catalysing the transfer of a phosphate group from a nucleoside triphosphate donor, such as ATP, to tyrosine residues in proteins.