All Relations between Cortical amygdalar area and glycine

Reference Sentence Publish Date Extraction Date Species
Emma Ivantsova, Andrew S Wengrovitz, Christopher L Souders, Christopher J Martyniu. Developmental and behavioral toxicity assessment of glyphosate and its main metabolite aminomethylphosphonic acid (AMPA) in zebrafish embryos/larvae. Environmental toxicology and pharmacology vol issue 2022 35504511 gly increased cytochrome c oxidase subunit 4 isoform 1 and citrate synthase mrna in larvae while ampa decreased cytochrome c oxidase i and increased 3-hydroxyacyl coa dehydrogenase transcripts. 2022-05-03 2022-05-06 Not clear
Howard Horng, Leslie Z Bene. The nonenzymatic reactivity of the acyl-linked metabolites of mefenamic acid toward amino and thiol functional group bionucleophiles. Drug metabolism and disposition: the biological fate of chemicals vol 41 issue 11 2014 23975029 however, mfa-amp was more reactive toward both gly and tau, 17.5-fold more reactive toward the n-acyl-amidation of taurine than its corresponding coa thioester, while mfa-coa displayed little reactivity toward glycine. 2014-05-12 2022-01-12 Not clear
S Kocabiyik, I Erdura. The effect of valine substitution for glycine in the dimer interface of citrate synthase from Thermoplasma acidophilum on stability and activity. Biochemical and biophysical research communications vol 275 issue 2 2000 10964687 recombinant wild-type and gly 196 mutant tpcs enzymes were largely identical in terms of substrate specificities (k(m) for oxaloacetate and acetyl coa). 2000-10-03 2022-01-11 Not clear
M M Benning, T Haller, J A Gerlt, H M Holde. New reactions in the crotonase superfamily: structure of methylmalonyl CoA decarboxylase from Escherichia coli. Biochemistry vol 39 issue 16 2000 10769118 the carboxylate group of the thioether analogue of methylmalonyl coa is hydrogen bonded to the peptidic nh group of gly 110 and the imidazole ring of his 66. 2000-06-01 2022-01-11 Not clear
R S Bhatnagar, E Jackson-Machelski, C A McWherter, J I Gordo. Isothermal titration calorimetric studies of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase. Determinants of binding energy and catalytic discrimination among acyl-CoA and peptide ligands. The Journal of biological chemistry vol 269 issue 15 1994 8157630 saccharomyces cerevisiae myristoyl-coa:protein n-myristoyltransferase (nmt1p) is an essential, monomeric enzyme that catalyzes the transfer of myristate from coa to the amino-terminal gly residue of cellular proteins. 1994-05-19 2022-01-10 Not clear
T Lu, Q Li, A Katoh, J Hernandez, K Duffin, E Jackson-Machelski, L J Knoll, G W Gokel, J I Gordo. The substrate specificity of Saccharomyces cerevisiae myristoyl-CoA: protein N-myristoyltransferase. Polar probes of the enzyme's myristoyl-CoA recognition site. The Journal of biological chemistry vol 269 issue 7 1994 8106519 nmt1p catalyzes the co-translational transfer of myristate from coa to the amino-terminal gly of cellular proteins in an ordered bi bi reaction mechanism that initially involves binding of myristoyl-coa to the apoenzyme. 1994-03-22 2022-01-10 Not clear
J K Lodge, R L Johnson, R A Weinberg, J I Gordo. Comparison of myristoyl-CoA:protein N-myristoyltransferases from three pathogenic fungi: Cryptococcus neoformans, Histoplasma capsulatum, and Candida albicans. The Journal of biological chemistry vol 269 issue 4 1994 8300631 myristoyl-coa:protein n-myristoyltransferase (nmt) transfers myristate from coa to the n-terminal gly residue of cellular proteins in an ordered reaction mechanism that first involves binding of myristoyl-coa to the apoenzyme. 1994-03-04 2022-01-10 Not clear
W J Rocque, C A McWherter, D C Wood, J I Gordo. A comparative analysis of the kinetic mechanism and peptide substrate specificity of human and Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase. The Journal of biological chemistry vol 268 issue 14 1993 8486723 human myristoyl-coa:protein n-myristoyltransferase (hnmt) catalyzes the transfer of myristate from coa to the amino-terminal gly residue of a number of cellular proteins involved in signal transduction pathways, to structural and nonstructural proteins encoded by retroviruses, hepadnaviruses, picornaviruses, and reoviruses, as well as to several transforming tyrosine kinases. 1993-06-08 2022-01-10 Not clear
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