threonine has been researched along with phalloidine in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (25.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (75.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Faulstich, H; Heber, H; Wieland, T | 1 |
| Bagheri-Yarmand, R; Barnes, CJ; Kumar, R; Li, F; Vadlamudi, RK | 1 |
| Hunter, T; Wang, JY; Woodring, PJ | 1 |
| Egelman, EH; Galkin, VE; Kudryashov, DS; Orlova, A; Phan, M; Reisler, E | 1 |
4 other study(ies) available for threonine and phalloidine
| Article | Year |
|---|---|
Syntheses of further analogues of norphalloin. Gly1-, L-val1- and D-Abu2-norphalloin and (beta-trideutero)-Ala5- norphalloin.
Topics: Alanine; Aminobutyrates; Anhydrides; Animals; Chromatography, Thin Layer; Cyclization; Deuterium; Lethal Dose 50; Mice; Mycotoxins; Oligopeptides; Peptides, Cyclic; Phalloidine; Polarography; Temperature; Threonine; Valine | 1974 |
p41-Arc subunit of human Arp2/3 complex is a p21-activated kinase-1-interacting substrate.
Topics: Actin Cytoskeleton; Actin-Related Protein 2-3 Complex; Actins; Cell Movement; Epidermal Growth Factor; Gene Library; Glutathione Transferase; Humans; Immunoprecipitation; Mutation; p21-Activated Kinases; Phalloidine; Phosphorylation; Protein Binding; Protein Serine-Threonine Kinases; Protein Subunits; RNA, Small Interfering; Threonine; Wound Healing | 2004 |
Mitotic phosphorylation rescues Abl from F-actin-mediated inhibition.
Topics: Actins; Allosteric Site; Amino Acid Sequence; Animals; Aspartic Acid; Cell Line; Enzyme Inhibitors; Fibroblasts; Glutathione Transferase; Immunoprecipitation; Mice; Mitosis; Molecular Sequence Data; Mutation; NIH 3T3 Cells; Okadaic Acid; Peptides; Phalloidine; Phosphorylation; Polymers; Proline; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Proto-Oncogene Proteins c-abl; Recombinant Fusion Proteins; RNA Polymerase II; src Homology Domains; Threonine; Transfection; Trypsin | 2005 |
Cofilin cross-bridges adjacent actin protomers and replaces part of the longitudinal F-actin interface.
Topics: Actin Depolymerizing Factors; Actins; Adenosine Diphosphate; Animals; Cysteine; Humans; Microscopy, Electron; Models, Molecular; Mutation; Phalloidine; Promoter Regions, Genetic; Protein Binding; Protein Structure, Quaternary; Rabbits; Rhodamines; Saccharomyces cerevisiae; Threonine; Time Factors | 2006 |