Page last updated: 2024-08-22

dithiothreitol and 11-cis-retinal

dithiothreitol has been researched along with 11-cis-retinal in 9 studies

Research

Studies (9)

TimeframeStudies, this research(%)All Research%
pre-19904 (44.44)18.7374
1990's3 (33.33)18.2507
2000's2 (22.22)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Bownds, D; Brodie, AE1
Bitensky, MW; Keirns, JJ; Keirns, M; Miki, N1
Buzney, SM; Frank, RN1
Fung, BK; Hubbell, WL1
Khorana, HG; Sakamoto, T1
Boelens, R; Crielaard, W; Devreese, B; Düx, P; Hård, K; Hellingwerf, KJ; Hoff, WD; Kaptein, R; Nugteren-Roodzant, IM; van Beeumen, J1
Heckelmann, M; Hofmann, KP; Maretzki, D; Sachs, K; Schmidt, MF; Veit, M1
Cai, K; Itoh, Y; Khorana, HG1
Gross, AK; Oprian, DD; Xie, G1

Other Studies

9 other study(ies) available for dithiothreitol and 11-cis-retinal

ArticleYear
Light-sensitive swelling of isolated frog rod outer segments as an in vitro assay for visual transduction and dark adaptation.
    The Journal of general physiology, 1975, Volume: 66, Issue:4

    Topics: Animals; Anti-Bacterial Agents; Anura; Calcimycin; Calcium; Carbonyl Cyanide m-Chlorophenyl Hydrazone; Dark Adaptation; Dithiothreitol; Egtazic Acid; Gramicidin; Hydrogen-Ion Concentration; In Vitro Techniques; Light; Magnesium; Papaverine; Photoreceptor Cells; Rhodopsin; Rotenone; Sodium Chloride; Sulfhydryl Reagents; Valinomycin

1975
A link between rhodopsin and disc membrane cyclic nucleotide phosphodiesterase. Action spectrum and sensitivity to illumination.
    Biochemistry, 1975, Jun-17, Volume: 14, Issue:12

    Topics: Adenosine Triphosphate; Animals; Cattle; Cell Membrane; Cyclic GMP; Dithiothreitol; Enzyme Activation; Kinetics; Light; Phosphoric Diester Hydrolases; Photoreceptor Cells; Rana pipiens; Retinal Pigments; Rhodopsin; Spectrophotometry; Time Factors

1975
Rhodopsin phosphorylation and retinal outer segment cyclic nucleotide phosphodiesterase: lack of a causal relationship.
    Experimental eye research, 1977, Volume: 25, Issue:5

    Topics: 3',5'-Cyclic-GMP Phosphodiesterases; Adenosine Triphosphate; Animals; Cattle; Dithiothreitol; Guanosine Triphosphate; In Vitro Techniques; Protein Kinases; Retina; Retinal Pigments; Rhodopsin; Stimulation, Chemical

1977
Organization of rhodopsin in photoreceptor membranes. 1. Proteolysis of bovine rhodopsin in native membranes and the distribution of sulfhydryl groups in the fragments.
    Biochemistry, 1978, Oct-17, Volume: 17, Issue:21

    Topics: Animals; Cattle; Cell Membrane; Darkness; Dithiothreitol; Kinetics; Light; Molecular Weight; Papain; Peptide Fragments; Photoreceptor Cells; Retinal Pigments; Rhodopsin; Thermolysin

1978
Structure and function in rhodopsin: the fate of opsin formed upon the decay of light-activated metarhodopsin II in vitro.
    Proceedings of the National Academy of Sciences of the United States of America, 1995, Jan-03, Volume: 92, Issue:1

    Topics: Animals; Cattle; Cell Membrane; Dithiothreitol; Glutathione; Glutathione Disulfide; Hydroxylamine; Hydroxylamines; Kinetics; Light; Oxidation-Reduction; Phospholipids; Protein Binding; Protein Folding; Retinaldehyde; Rhodopsin; Rod Cell Outer Segment; Rod Opsins; Spectrophotometry

1995
Thiol ester-linked p-coumaric acid as a new photoactive prosthetic group in a protein with rhodopsin-like photochemistry.
    Biochemistry, 1994, Nov-29, Volume: 33, Issue:47

    Topics: Chromatiaceae; Chromatography, High Pressure Liquid; Coumaric Acids; Cysteine; Disulfides; Dithiothreitol; Esters; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Photochemistry; Propionates; Rhodopsin; Sodium Hydroxide; Sulfhydryl Compounds

1994
Palmitoylation of rhodopsin with S-protein acyltransferase: enzyme catalyzed reaction versus autocatalytic acylation.
    Biochimica et biophysica acta, 1998, Oct-02, Volume: 1394, Issue:1

    Topics: Acetyltransferases; Acylation; Animals; Catalysis; Cattle; Dithiothreitol; Octoxynol; Palmitic Acid; Protein Conformation; Rhodopsin

1998
Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: use of a photoactivatable reagent.
    Proceedings of the National Academy of Sciences of the United States of America, 2001, Apr-24, Volume: 98, Issue:9

    Topics: Amino Acid Sequence; Animals; Azides; Binding Sites; Cattle; COS Cells; Cross-Linking Reagents; Cysteine; Disulfides; Dithiothreitol; Ethylmaleimide; Guanosine Diphosphate; Light; Lysine; Maleimides; Models, Molecular; Molecular Sequence Data; Mutation; Photolysis; Protein Binding; Protein Structure, Secondary; Pyridines; Rhodopsin; Sepharose; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Transducin; Trypsin; Ultraviolet Rays

2001
An opsin mutant with increased thermal stability.
    Biochemistry, 2003, Feb-25, Volume: 42, Issue:7

    Topics: Amino Acid Sequence; Animals; Asparagine; Aspartic Acid; Cattle; COS Cells; Cross-Linking Reagents; Cysteine; Disulfides; Dithiothreitol; Light; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Denaturation; Recombinant Proteins; Retinaldehyde; Rhodopsin; Thermodynamics; Transducin; Transfection

2003