erythrosine and tetramethylrhodamine iodoacetamide

erythrosine has been researched along with tetramethylrhodamine iodoacetamide in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's4 (80.00)18.2507
2000's1 (20.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Burridge, K; Nuckolls, GH; Turner, CE1
Ajtai, K; Burghardt, TP1
Abe, H; Nagaoka, R; Obinata, T1
Ajtai, K; Burghardt, TP; Garamszegi, SP; Park, S1
Schepartz, A; Schneider, TL1

Other Studies

5 other study(ies) available for erythrosine and tetramethylrhodamine iodoacetamide

ArticleYear
Functional studies of the domains of talin.
    The Journal of cell biology, 1990, Volume: 110, Issue:5

    Topics: Actins; Animals; Blotting, Western; Cadherins; Cell Adhesion; Cells, Cultured; Cytoskeletal Proteins; Fluorescein-5-isothiocyanate; Fluoresceins; Fluorescent Antibody Technique; Fluorescent Dyes; Humans; Iodine Radioisotopes; Kidney; Membrane Proteins; Microinjections; Microscopy, Fluorescence; Peptides; Rhodamines; Structure-Activity Relationship; Talin; Thiocyanates; Vinculin

1990
Conformation of xanthene dyes in the sulfhydryl 1 binding site of myosin. 2.
    Biochemistry, 1995, Dec-12, Volume: 34, Issue:49

    Topics: Animals; Binding Sites; Circular Dichroism; Fluoresceins; Fluorescence Polarization; Fluorescent Dyes; Models, Molecular; Molecular Conformation; Myosin Subfragments; Myosins; Protein Conformation; Protein Structure, Secondary; Rabbits; Rhodamines; Tryptophan; Xanthenes

1995
Site-directed mutagenesis of the phosphorylation site of cofilin: its role in cofilin-actin interaction and cytoplasmic localization.
    Cell motility and the cytoskeleton, 1996, Volume: 35, Issue:3

    Topics: Actin Depolymerizing Factors; Actins; Binding Sites; Cell Line; Cytoplasm; Fluoresceins; Fluorescent Dyes; Microfilament Proteins; Microinjections; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Phosphorylation; Rhodamines

1996
Tertiary structural changes in the cleft containing the ATP sensitive tryptophan and reactive thiol are consistent with pivoting of the myosin heavy chain at Gly699.
    Biochemistry, 1998, Jun-02, Volume: 37, Issue:22

    Topics: Adenosine Triphosphate; Animals; Circular Dichroism; Fluoresceins; Glycine; Muscle Fibers, Skeletal; Myosin Heavy Chains; Myosin Subfragments; Protein Structure, Tertiary; Rabbits; Rhodamines; Spectrometry, Fluorescence; Sulfhydryl Compounds; Tryptophan

1998
Hepatitis B virus protein pX enhances the monomer assembly pathway of bZIP.DNA complexes.
    Biochemistry, 2001, Mar-06, Volume: 40, Issue:9

    Topics: Amino Acid Sequence; Basic-Leucine Zipper Transcription Factors; Dimerization; DNA-Binding Proteins; Electrophoresis, Polyacrylamide Gel; Energy Transfer; Fluoresceins; Fluorescence Polarization; Fluorescent Dyes; G-Box Binding Factors; Hepatitis B virus; Humans; Kinetics; Molecular Sequence Data; Oligonucleotides; Protein Binding; Rhodamines; Sequence Deletion; Spectrometry, Fluorescence; Trans-Activators; Transcription Factors; Viral Regulatory and Accessory Proteins

2001