tetramethylrhodamine isothiocyanate has been researched along with Muscle Contraction in 2 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (50.00) | 18.2507 |
| 2000's | 1 (50.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Kamm, KE; Luby-Phelps, K; Stull, JT; Tansey, MG | 1 |
| Borovikov, IuS; Chacko, S; Rosliakova, MA; Vikhorev, PG; Vikhoreva, NN | 1 |
2 other study(ies) available for tetramethylrhodamine isothiocyanate and Muscle Contraction
| Article | Year |
|---|---|
Ca(2+)-dependent phosphorylation of myosin light chain kinase decreases the Ca2+ sensitivity of light chain phosphorylation within smooth muscle cells.
Topics: 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine; Amino Acid Sequence; Animals; Calcium; Calcium-Calmodulin-Dependent Protein Kinase Type 2; Calcium-Calmodulin-Dependent Protein Kinases; Calmodulin; Cattle; Cells, Cultured; Egtazic Acid; Fluorescein-5-isothiocyanate; Fluorescent Dyes; Isoquinolines; Kinetics; Microscopy, Fluorescence; Molecular Sequence Data; Muscle Contraction; Muscle, Smooth; Myosin-Light-Chain Kinase; Myosins; Peptide Fragments; Phosphorylation; Piperazines; Rhodamines; Trachea | 1994 |
[Caldesmon inhibits formation of strongly bound myosin cross-bridges and activates an ability of weakly bound cross-bridges to transform actin monomers to the off-conformation].
Topics: Actins; Animals; Calmodulin-Binding Proteins; Fluorescent Dyes; Muscle Contraction; Muscle, Skeletal; Muscle, Smooth; Myosins; Protein Binding; Protein Conformation; Rabbits; Rhodamines | 2000 |