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Tyrosinase-catalyzed reactions for the conjugation of a tyrosine-containing peptide to chitosan

Tyrosinase-like activity by a synthetic dicopper dioxygen complex.

Tyrosine and iodotyrosines.

Tyrosine and phenylalanine residues can undergo oxidation to modify their phenyl side-chain groups. Tyrosine can form covalent dimers that link two side chains together via a radical reaction. Both tyrosine and phenylalanine can be modified by oxidation to add oxygen-containing groups directly to their aromatic ring.

Tyrosine and tyrosinate fluorescence and phosphorescence emission spectra with 280-nm excitation. Curve 1

Tyrosine as a precursor for thyroid and medullary hormones

Tyrosine coordination modes in galactose oxidase-copper complex. Tyrosine phenolate bond angles

Tyrosine degradation pathway.

Tyrosine degradation pathway. Metabolic markers are framed. Possible metabolic disorders are marked with boxes, 4.1, fumarylacetoacetase 4.2, tyrosine aminotransferase 4.3, 4-hydroxyphenylpyruvate dioxygenase 4.5, homogentisate dioxygenase. Inhibition by succinylacetone and NTBC are indicated by crosses. 5-ALA, 5-aminolevulinate

Tyrosine hydroxylase immunoreactivity .

Tyrosine hydroxylase immunostaining in representative brain sections of mice in the post-MPTP protocol.

Tyrosine hydroxylase is characterized by high mRNA expression levels of these dopaminergic markers.

Tyrosine hydroxylase mRNA expression in a whole hemisphere horizontal human brain section . Note the lack of TH mRNA expression in the forebrain regions, but widespread expression throughout the mesencephalon.

Tyrosine inhibitory prenylated flavonoids from Sophora flavescens and kojic acid as a control of tyrosine inhibition

Tyrosine is hydroxylated in a rate-limiting step by tyrosine hydroxylase . Newly synthesized DA is stored in vesicles, from which release occurs into the synaptic

Tyrosine is hydroxylated to dihydroxyphenylalanine.

Tyrosine is oxidized to DOPA and then to DOPA quinone.

Tyrosine kinase structure

Tyrosine kinase-linked receptors those with inherentTK activity insulin receptor. The intracellular tail and cytoplasmic proteins become phosphoryLated following hormone engagement with the ligand-binding domain

Tyrosine modification using a when proteins are treated alone with either three component Mannich-type reaction. component, Aldehydes and anilines condense to listed for a number of anilines and aliphatic form imines in situ, which react with tyrosine amines using a-chymotrypsinogen A as the residues through an electrophilic aromatic substrate and formaldehyde as the aldehyde substitution reaction. No reaction occurs component.

Tyrosine modification using commercially available lysine-reactive probes, Modification of

Tyrosine modification using palladium jr-allyl chemistry, in aqueous solution to yield electrophilic 7r-allyl complexes. These species alkylate tyrosine residues with high

Tyrosine oxidation by hydroxyl radicals

Tyrosine oxidation reduction pathways in photosystem II

Tyrosine reactive probes. Nitration of tyrosine by reaction with tetranitromethane, followed by reduction with sodium dithionite, to yield an o-aminotyrosine.



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