threonine has been researched along with uridine triphosphate in 5 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (40.00) | 18.2507 |
| 2000's | 3 (60.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Communi, D; Erneux, C; Vanweyenberg, V | 1 |
| Kantrowitz, ER; Williams, MK | 1 |
| Assairi, L; Barzu, O; Briozzo, P; Evrin, C; Gilles, AM; Joly, N; Meyer, P | 1 |
| Dihazi, H; Eschrich, K; Flehmig, G; Fürst, S; Gerevich, Z; Illes, P; Nörenberg, W; Stanchev, D; Wirkner, K | 1 |
| Khan, S; Nandicoori, VK; Parikh, A; Prakash, B; Verma, SK | 1 |
5 other study(ies) available for threonine and uridine triphosphate
| Article | Year |
|---|---|
D-myo-inositol 1,4,5-trisphosphate 3-kinase A is activated by receptor activation through a calcium:calmodulin-dependent protein kinase II phosphorylation mechanism.
Topics: Animals; Calcium; Calcium-Calmodulin-Dependent Protein Kinase Type 2; Calcium-Calmodulin-Dependent Protein Kinases; Carbachol; Cerebral Cortex; CHO Cells; Cricetinae; Enzyme Activation; Enzyme Inhibitors; Humans; Male; Muscarinic Agonists; Okadaic Acid; Phosphorylation; Phosphotransferases (Alcohol Group Acceptor); Rats; Rats, Sprague-Dawley; Receptors, Purinergic P2; Receptors, Purinergic P2Y2; Threonine; Uridine Triphosphate | 1997 |
Threonine 82 in the regulatory chain is important for nucleotide affinity and for the allosteric stabilization of Escherichia coli aspartate transcarbamoylase.
Topics: Adenosine Triphosphate; Alanine; Allosteric Regulation; Aspartate Carbamoyltransferase; Cytidine Triphosphate; Escherichia coli; Gene Expression Regulation; Kinetics; Mutagenesis, Site-Directed; Regulatory Sequences, Nucleic Acid; Threonine; Uridine Triphosphate | 1998 |
Structure of Escherichia coli UMP kinase differs from that of other nucleoside monophosphate kinases and sheds new light on enzyme regulation.
Topics: Allosteric Regulation; Amino Acid Sequence; Amino Acid Substitution; Asparagine; Binding Sites; Crystallography; Enzyme Activation; Escherichia coli; Guanosine Triphosphate; Ligands; Molecular Sequence Data; Mutagenesis, Site-Directed; Nucleoside-Phosphate Kinase; Phosphates; Protein Folding; Protein Structure, Quaternary; Threonine; Uridine Diphosphate; Uridine Monophosphate; Uridine Triphosphate | 2005 |
Decrease of current responses at human recombinant P2X3 receptors after substitution by Asp of Ser/Thr residues in protein kinase C phosphorylation sites of their ecto-domains.
Topics: Adenosine Triphosphate; Aspartic Acid; Cell Line; Dose-Response Relationship, Drug; Electric Stimulation; Humans; Membrane Potentials; Mutagenesis; Patch-Clamp Techniques; Phosphorylation; Protein Kinase C; Purinergic P2 Receptor Agonists; Purinergic P2 Receptor Antagonists; Receptors, Purinergic P2; Receptors, Purinergic P2X2; Recombinant Proteins; Serine; Threonine; Transfection; Uridine Triphosphate | 2006 |
PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity.
Topics: Acetyl Coenzyme A; Acetylglucosamine; Bacterial Proteins; Crystallography, X-Ray; DNA Mutational Analysis; Glucosamine; Glucosephosphates; Models, Molecular; Multienzyme Complexes; Mycobacterium tuberculosis; Phosphorylation; Protein Folding; Protein Serine-Threonine Kinases; Protein Structure, Secondary; Protein Structure, Tertiary; Threonine; Uridine Diphosphate N-Acetylglucosamine; Uridine Triphosphate | 2009 |