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Showing 1 to 4 of 4 for “"human thymidylate synthase"”.

  1. Molecular Dissection of the Ubiquitin-Independent Degradation Signal At the Unstructured Amino Terminal End of Human Thymidylate Synthase

    … of these ubiquitin-independent substrates is the human DNA metabolic enzyme thymidylate synthase (TS). Previous studies showed that the degradation of TS is mediated by an intrinsically disordered 27-residue region at the N-terminal end of the protein, and that this region, in cooperation with an …

    south-carolina Repository record for Molecular Dissection of the Ubiquitin-Independent Degradation Signal At the Unstructured Amino Terminal End of Human Thymidylate Synthase (opens in a new tab)

  2. The Mechanism of N10-Formyltetrahydrofolate Synthetase. Use of Human Thymidylate Synthase Variants to Characterize Asymmetric Ligand Binding and to Identify Novel Allosteric Inhibitors.

    … fixation, and purinolysis, through the glycine synthase/reductase pathway. The formation of fTHF occurs via a two-step process, which involves the formation of a formylphosphate (XPO) intermediate. The XPO intermediate has been proposed based on kinetic and spectroscopic experiments and …

    south-carolina Repository record for The Mechanism of N10-Formyltetrahydrofolate Synthetase. Use of Human Thymidylate Synthase Variants to Characterize Asymmetric Ligand Binding and to Identify Novel Allosteric Inhibitors. (opens in a new tab)

  3. Interactions between Folate Deficiency and β-Nicotinamide Adenine Dinucleotide Deficiency and Conformational Study of Thymidylate Synthase and its Physiological Relevance

    … <p><strong>Part II:</strong></p> <p>Thymidylate synthase (TS) catalyzes the reaction that forms dTMP from dUMP. Previous data suggested that human thymidylate synthase (hTS) exists in two major conformations, active and inactive. Two hTS mutants were created to mimic the active and …

    south-carolina Repository record for Interactions between Folate Deficiency and β-Nicotinamide Adenine Dinucleotide Deficiency and Conformational Study of Thymidylate Synthase and its Physiological Relevance (opens in a new tab)