Results 271 to 280 of about 674,878 (317)
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Biochimica et Biophysica Acta (BBA) - General Subjects, 1972
Abstract 1. 1. An enzyme: tyrosine α,β-amino mutase was isolated from cells of Bacillus brevis Vm4. 2. 2. Tyrosine α,β-amino mutase forms β-tyrosine from L -α-tyrosine. 3. 3. The optimal conditions for the reaction are at pH 8.5 and 37°C. 4. 4. ATP is the only cofactor required for the enzyme activity. 5. 5.
Z. Kurylo-Borowska, Tessa Abramsky
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Abstract 1. 1. An enzyme: tyrosine α,β-amino mutase was isolated from cells of Bacillus brevis Vm4. 2. 2. Tyrosine α,β-amino mutase forms β-tyrosine from L -α-tyrosine. 3. 3. The optimal conditions for the reaction are at pH 8.5 and 37°C. 4. 4. ATP is the only cofactor required for the enzyme activity. 5. 5.
Z. Kurylo-Borowska, Tessa Abramsky
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PHOSPHORYLATION OF TYROSINE AND THE REACTIVITY OF DIALKYL PHOSPHITES WITH TYROSINE [PDF]
Phosphorus, Sulfur, and Silicon and the Related Elements, 1995 Abstract New methods of synthesizing N-phosphoryltyrosine and N,O-bisphosphoryl tyrosine ester were studied. The reactivity of dialkyl phosphites with tyrosine was also studied.
Yong Jin +3 more
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Current Cancer Drug Targets, 2010
Over the last ten years, several new and therapeutically relevant cancer drugs targeting tyrosine kinases signaling pathways have been developed. Tyrosine kinase inhibitors (TKIs) are a pharmaceutical class of small molecules, orally available, well-tolerated, worldwide approved drugs for the treatment of several neoplasms, including lung, breast ...
NATOLI, Clara +5 more
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Over the last ten years, several new and therapeutically relevant cancer drugs targeting tyrosine kinases signaling pathways have been developed. Tyrosine kinase inhibitors (TKIs) are a pharmaceutical class of small molecules, orally available, well-tolerated, worldwide approved drugs for the treatment of several neoplasms, including lung, breast ...
NATOLI, Clara +5 more
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Amino Acids, 1993
Tyrosine transamination has been investigatedin vitro with a preparation of rat liver tyrosine aminotransferase in the presence of several structural derivatives of the substrate, including the phosphonic analogue. The transamination by tyrosine aminotransferase (TAT) needs the presence in the substrate molecule of free amino and carboxylic groups, a ...
A. Iron, Eugène Neuzil, A. Cassaigne
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Tyrosine transamination has been investigatedin vitro with a preparation of rat liver tyrosine aminotransferase in the presence of several structural derivatives of the substrate, including the phosphonic analogue. The transamination by tyrosine aminotransferase (TAT) needs the presence in the substrate molecule of free amino and carboxylic groups, a ...
A. Iron, Eugène Neuzil, A. Cassaigne
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Tyrosine phosphatases and their possible interplay with tyrosine kinases.
Ciba Foundation symposium, 1992Protein tyrosine phosphatases represent a new family of intracellular and receptor-linked enzymes. They are totally specific toward tyrosyl residues in proteins, and, with specific activities 10-1000-fold greater than those of the protein tyrosine kinases, they can be expected to tightly control the level of phosphotyrosine within the cell.
Harry Charbonneau +3 more
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Targeted tyrosine iodination in a multi‐tyrosine vasopressin analog
Journal of Peptide Science, 2007AbstractIodination of the conserved 2‐tyrosine (Tyr2) residue in the pressin and tocin rings of arginine‐ or lysine‐vasopressin (AVP or LVP), and oxytocin, respectively, impairs binding to their respective receptors. Synthetic antagonists that have their Tyr2 either replaced by another amino acid or irreversibly blocked by an O‐methyl or O‐ethyl ether,
Jacques A. Durr +3 more
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Oxidation of Tyrosine Diketopiperazine to DOPA Diketopiperazine with Tyrosine Hydroxylase
Journal of Natural Products, 2004The diketopiperazine of DOPA was synthesized in high yield from the diketopiperazine of tyrosine using PC12 cell lysate, which expresses high levels of tyrosine hydroxylase. This represents the first use of this enzyme to prepare DOPA-containing peptides.
Maysoon B. Saleh, Russell G. Kerr
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Tyrosine-dependent increase of tyrosine hydroxylase in neuroblastoma cells
Nature, 1974TYROSINE hydroxylase (tyrosine-3-monooxygenase), presumably the rate-limiting enzyme in the biosynthesis of the adrenergic transmitters dopamine and noradrenaline1,2, catalyses the hydroxylation of both phenylalanine and tyrosine3,4. This property has been exploited for the selection of adrenergic-like mouse neuroblastoma cells5, which have high ...
Tom Lloyd +2 more
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Tyrosine transaminase: Inactivation by tyrosine metabolic end products
Biochimica et Biophysica Acta (BBA) - Enzymology, 1970Abstract The tyrosine metabolites, p- hydroxyphenylpyruvate , homogentisate, and fumarylacetoacetate were examined as inhibitors and inactivators of purified rat liver tyrosine α-ketoglutarate transaminase. Of these, homogentisate proved to be a very powerful inactivator when the enzyme was preincubated with it. This effect was blocked by prior
Morton Civen +2 more
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Study of Tyrosine Kinases and Protein Tyrosine Phosphorylation
2004In recent years, our increased understanding of the complex signal transduction mechanisms that regulate cellular function has fueled huge advances in all aspects of biomedical science and cell biology. Platelet and megakaryocyte function is no exception to this. In the last 10 yr our understanding of the receptor biochemistry and the systems that they
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