Results 161 to 170 of about 30,987 (215)
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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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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, T, 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, T, Abramsky
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Current Protocols in Protein Science, 2005
AbstractThe O‐sulfation of tyrosine residues of plasma membrane and secretory proteins that transit through the secretory pathway of eukaryotic cells is a widespread post‐translational modification. This enzymatic reaction is catalyzed by trans‐Golgi‐associated tyrosylprotein sulfotransferases, which recognize tyrosine residues located in a specific ...
Corbeil, D., Thiele, C., Huttner, W.
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AbstractThe O‐sulfation of tyrosine residues of plasma membrane and secretory proteins that transit through the secretory pathway of eukaryotic cells is a widespread post‐translational modification. This enzymatic reaction is catalyzed by trans‐Golgi‐associated tyrosylprotein sulfotransferases, which recognize tyrosine residues located in a specific ...
Corbeil, D., Thiele, C., Huttner, W.
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Regulation of Tyrosine Kinases by Tyrosine Phosphorylation
1991Protein kinases can be classified according to whether they phosphorylate phenolic (tyrosine) or aliphatic (serine and threonine) hydroxyl groups (Hunter and Cooper, 1985). Although there are now a few examples of kinases that seemingly break the rule (Howell et al., 1990), most tyrosine kinases differ from the serine/threonine kinases in their primary
Jonathan A. Cooper +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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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, E, 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, E, Neuzil, A, Cassaigne
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A Quantitative Assay for Tyrosine Sulfation and Tyrosine Phosphorylation in Peptides
Biological Chemistry Hoppe-Seyler, 1990A method was developed to measure sulfation and phosphorylation of tyrosine in proteins after alkaline hydrolysis, ion-exchange chromatography, reaction with [3H]dinitrofluorobenzene and subsequent thin-layer chromatography. The method allows the detection of 10-20 pmol of modified tyrosine and was applied to determine the content of tyrosine-phosphate
H, Blode, T, Heinrich, H, Diringer
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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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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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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
M, Civen, C, Wilson, C B, Brown
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