dithiothreitol has been researched along with phalloidine in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 2 (50.00) | 18.2507 |
2000's | 2 (50.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Heil-Chapdelaine, RA; Otto, JJ | 1 |
de Lourdes Juárez-Mosqueda, M; Mújica, A | 1 |
Musib, R; Phillips, M; Reisler, E; Rubenstein, PA; Shvetsov, A | 1 |
Bergeron, SE; Egelman, EH; Galkin, VE; Orlova, A; Phillips, M; Reisler, E; Rubenstein, PA; Shvetsov, A | 1 |
4 other study(ies) available for dithiothreitol and phalloidine
Article | Year |
---|---|
Characterization of changes in F-actin during maturation of starfish oocytes.
Topics: Actins; Adenine; Animals; Colforsin; Cyclic AMP; Cytoplasm; Dithiothreitol; Female; Image Processing, Computer-Assisted; Male; Microscopy, Confocal; Microscopy, Fluorescence; Oocytes; Phalloidine; Starfish | 1996 |
A perinuclear theca substructure is formed during epididymal guinea pig sperm maturation and disappears in acrosome reacted cells.
Topics: Acrosome Reaction; Actins; Animals; Calcium; Calmodulin; Cell Nucleus; Cytochalasin D; Cytoskeletal Proteins; Dithiothreitol; Electrophoresis; Endopeptidases; Epididymis; Female; Guinea Pigs; Hydrogen-Ion Concentration; Immunoblotting; Immunohistochemistry; Male; Phalloidine; Rabbits; Sheep; Sodium Bicarbonate; Sperm Capacitation; Sperm Maturation; Spermatozoa; Swine | 1999 |
Locking the hydrophobic loop 262-274 to G-actin surface by a disulfide bridge prevents filament formation.
Topics: Actin Cytoskeleton; Actins; Alanine; Cross-Linking Reagents; Cysteine; Disulfides; Dithiothreitol; Hydrophobic and Hydrophilic Interactions; Leucine; Magnesium Chloride; Mutagenesis, Site-Directed; Oxidation-Reduction; Peptide Fragments; Phalloidine; Polymers; Protein Engineering; Protein Structure, Tertiary; Saccharomyces cerevisiae Proteins | 2002 |
Actin hydrophobic loop 262-274 and filament nucleation and elongation.
Topics: Actin Cytoskeleton; Actin Depolymerizing Factors; Actins; Cross-Linking Reagents; Disulfides; Dithiothreitol; Escherichia coli; Fluorometry; Hydrophobic and Hydrophilic Interactions; Light; Magnesium Chloride; Mutation; Phalloidine; Protein Conformation; Protein Structure, Secondary; Rhodamines; Saccharomyces cerevisiae; Scattering, Radiation; Spectrometry, Fluorescence | 2008 |