arsenic trioxide has been researched along with lysine in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 3 (100.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Anania, VG; Fasci, D; Lill, JR; Salvesen, GS | 1 |
| Cai, Y; Ding, J; Dong, L; Hu, L; Jin, J; Liu, D; Wang, F; Wu, D; Yang, Y; Zhao, L; Zhao, X | 1 |
| Bott, AJ; Catanzaro, JM; Chen, JS; Diaz-Meco, MT; Ding, WX; Dou, Z; Du, C; Jaber, N; Jiang, YP; Lin, RZ; Moscat, J; Ozato, K; Pan, JA; Sun, Y; Yang, B; Zong, WX | 1 |
3 other study(ies) available for arsenic trioxide and lysine
| Article | Year |
|---|---|
SUMO deconjugation is required for arsenic-triggered ubiquitylation of PML.
Topics: Amino Acid Sequence; Animals; Arsenic Trioxide; Arsenicals; Blotting, Western; Chlorocebus aethiops; CHO Cells; COS Cells; Cricetinae; Cricetulus; Cysteine Endopeptidases; Endopeptidases; HEK293 Cells; Humans; Lysine; Microscopy, Confocal; Molecular Sequence Data; Mutation; Nuclear Proteins; Oxides; Promyelocytic Leukemia Protein; RNA Interference; Signal Transduction; Small Ubiquitin-Related Modifier Proteins; SUMO-1 Protein; Transcription Factors; Tumor Suppressor Proteins; Ubiquitination | 2015 |
Arsenic Trioxide Reduces Global Histone H4 Acetylation at Lysine 16 through Direct Binding to Histone Acetyltransferase hMOF in Human Cells.
Topics: Acetylation; Arsenic Trioxide; Arsenicals; Cell Death; Environmental Pollutants; HEK293 Cells; HeLa Cells; Histone Acetyltransferases; Histones; Humans; Lysine; Oxides; Protein Binding; Zinc Fingers | 2015 |
TRIM21 Ubiquitylates SQSTM1/p62 and Suppresses Protein Sequestration to Regulate Redox Homeostasis.
Topics: Adaptor Proteins, Signal Transducing; Animals; Arsenic Trioxide; Arsenicals; Cell Death; Chemical and Drug Induced Liver Injury; Cytoskeletal Proteins; Disease Models, Animal; Heart Failure; Heat-Shock Proteins; HEK293 Cells; Homeostasis; Humans; Intracellular Signaling Peptides and Proteins; Kelch-Like ECH-Associated Protein 1; Liver; Lysine; Mice; Mice, Inbred C57BL; Mice, Knockout; Myocardium; Oxidation-Reduction; Oxidative Stress; Oxides; Protein Binding; Protein Interaction Domains and Motifs; Protein Multimerization; Ribonucleoproteins; RNA Interference; Sequestosome-1 Protein; Signal Transduction; Time Factors; Transfection; Ubiquitination | 2016 |