Results 331 to 340 of about 1,534,933 (399)
Some of the next articles are maybe not open access.
The discovery of receptor tyrosine kinases: targets for cancer therapy
Nature Reviews Cancer, 2004A. Gschwind, O. Fischer, A. Ullrich
exaly +2 more sources
Effect of the phosphonic analogue of tyrosine on tyrosine iodination
Amino Acids, 1994Depositing ofDL-1-amino-2-(p-hydroxyphenyl)-ethylphosphonic acid (Tyr-P) on the chicken embryo induced a dose dependent decrease of the iodine uptake by the embryonic thyroid. Tyr-P interfered on iodination of tyrosine when tested with hog thyroid peroxidase (TPO) and with bovine lactoperoxidase (LPO); the analogue was recognized by the two enzymes but
A, Iron, E, Neuzil, A, Cassaigne
openaire +2 more sources
Radiation Physics and Chemistry (1977), 1982
Abstract Blue fluorescence characteristics of dityrosine appeared in y -irradiated solutions of tyrosine, glycyl- L -tyrosine or polytyrosine (MW 110,000). The intensity of fluorescence was used for the determination of the dityrosine concentration in hydrolysed samples.
Grzegorz Boguta, Antoni M. Dancewicz
openaire +1 more source
Abstract Blue fluorescence characteristics of dityrosine appeared in y -irradiated solutions of tyrosine, glycyl- L -tyrosine or polytyrosine (MW 110,000). The intensity of fluorescence was used for the determination of the dityrosine concentration in hydrolysed samples.
Grzegorz Boguta, Antoni M. Dancewicz
openaire +1 more source
Inhibition of tyrosine phenol-lyase by tyrosine homologues
Amino Acids, 2016We have designed, synthesized, and evaluated tyrosine homologues and their O-methyl derivatives as potential inhibitors for tyrosine phenol lyase (TPL, E.C. 4.1.99.2). Recently, we reported that homologues of tryptophan are potent inhibitors of tryptophan indole-lyase (tryptophanase, TIL, E.C.
Quang, Do +2 more
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +3 more sources
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
openaire +3 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources