oxophenylarsine has been researched along with serine in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 3 (75.00) | 18.2507 |
| 2000's | 1 (25.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Li, J; Pickart, CM | 1 |
| Báez, I; Breithaupt, TB; Eylar, EH; Molina, C; Rivera-Quiñones, C | 1 |
| Dong, J; Ksenzenko, MY; Rosen, BP; Scott, RA; Shi, W | 1 |
| Jenkins, SM; Johnson, GV | 1 |
4 other study(ies) available for oxophenylarsine and serine
| Article | Year |
|---|---|
Binding of phenylarsenoxide to Arg-tRNA protein transferase is independent of vicinal thiols.
Topics: Acyltransferases; Alanine; Aminoacyltransferases; Arsenicals; Base Sequence; Cysteine; DNA Primers; Iodine Radioisotopes; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Binding; Saccharomyces cerevisiae; Serine; Sulfhydryl Compounds | 1995 |
Anti-CD2-induced tyrosine phosphorylation of T cell polypeptides is independent of the PMA-induced modification of p56lck.
Topics: Antibodies, Monoclonal; Antigens, Differentiation, T-Lymphocyte; Arsenicals; CD2 Antigens; Humans; Lymphocyte Specific Protein Tyrosine Kinase p56(lck); Mitosis; Peptides; Phosphorylation; Protein-Tyrosine Kinases; Receptors, Immunologic; Serine; Signal Transduction; T-Lymphocytes; Tetradecanoylphorbol Acetate; Tyrosine | 1993 |
The role of arsenic-thiol interactions in metalloregulation of the ars operon.
Topics: Amino Acid Sequence; Antimony; Arsenicals; Arsenites; Bacterial Proteins; Base Sequence; Cysteine; Drug Resistance, Microbial; Escherichia coli; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Helix-Turn-Helix Motifs; Kinetics; Models, Structural; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Operon; Protein Structure, Secondary; R Factors; Repressor Proteins; Sequence Homology, Amino Acid; Serine; Trans-Activators | 1996 |
Microtubule/MAP-affinity regulating kinase (MARK) is activated by phenylarsine oxide in situ and phosphorylates tau within its microtubule-binding domain.
Topics: Animals; Antineoplastic Agents, Phytogenic; Arsenicals; Binding Sites; Cerebral Cortex; Enzyme Activation; Enzyme Inhibitors; Humans; Microtubules; Neuroblastoma; Neurons; Paclitaxel; Phosphorylation; Protein Serine-Threonine Kinases; Protein Structure, Tertiary; Rats; Serine; tau Proteins; Tumor Cells, Cultured | 2000 |