ethylmaleimide and 11-cis-retinal

ethylmaleimide has been researched along with 11-cis-retinal in 11 studies

Research

Studies (11)

TimeframeStudies, this research(%)All Research%
pre-19906 (54.55)18.7374
1990's4 (36.36)18.2507
2000's1 (9.09)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Akhtar, M; Sale, GJ; Towner, P1
Bonting, SL; Daemen, FJ; De Grip, WJ1
Downer, NW1
Hofmann, KP; Reichert, J2
Zorn, M1
Khorana, HG; Ridge, KD; Zhang, C1
Bovee-Geurts, PH; DeGrip, WJ; Rath, P; Rothschild, KJ1
Farrens, DL; Hubbell, WL; Khorana, HG; Yang, K1
Kono, M; Oprian, DD; Yu, H1
Cai, K; Itoh, Y; Khorana, HG1

Other Studies

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

ArticleYear
Functional rhodopsin complex consisting of three noncovalently linked fragments.
    Biochemistry, 1977, Dec-13, Volume: 16, Issue:25

    Topics: Amino Acids; Animals; Cattle; Drug Stability; Ethylmaleimide; Kinetics; Molecular Weight; Papain; Peptide Fragments; Photoreceptor Cells; Protein Binding; Retinal Pigments; Retinaldehyde; Rhodopsin; Spectrophotometry; Tritium

1977
Biochemical aspects of the visual process. XXVIII. Classification of sulfhydryl groups in phodopsin and other photoreceptor membrane proteins.
    Biochimica et biophysica acta, 1975, Jul-08, Volume: 396, Issue:1

    Topics: Animals; Binding Sites; Cattle; Cell Membrane; Chloromercuribenzoates; Dithionitrobenzoic Acid; Electrophoresis, Polyacrylamide Gel; Ethylmaleimide; Kinetics; Nerve Tissue Proteins; Photoreceptor Cells; Protein Binding; Retinal Pigments; Rhodopsin; Sulfhydryl Compounds; Time Factors; Ultracentrifugation; Vision, Ocular

1975
Cross-linking of dark-adapted frog photoreceptor disk membranes. Evidence for monomeric rhodopsin.
    Biophysical journal, 1985, Volume: 47, Issue:3

    Topics: Animals; Cell Membrane; Darkness; Electrophoresis, Polyacrylamide Gel; Ethylmaleimide; Glutaral; Photoreceptor Cells; Rana catesbeiana; Retina; Retinal Pigments; Rhodopsin; Rod Cell Outer Segment

1985
Chemical probing of the light-induced interaction between rhodopsin and G-protein. Near-infrared light-scattering and sulfhydryl modifications.
    The Journal of biological chemistry, 1985, Jul-05, Volume: 260, Issue:13

    Topics: Animals; Cattle; Dithionitrobenzoic Acid; Electrophoresis, Polyacrylamide Gel; Ethylmaleimide; GTP-Binding Proteins; Guanosine Diphosphate; Guanosine Triphosphate; Infrared Rays; Light; Photoreceptor Cells; Retinal Pigments; Rhodopsin; Rod Cell Outer Segment; Scattering, Radiation

1985
The effect of blocked sulfhydryl groups on the regenerability of bleached rhodopsin.
    Experimental eye research, 1974, Volume: 19, Issue:3

    Topics: Animals; Carbon Radioisotopes; Cattle; Darkness; Digitonin; Ethylmaleimide; Hydroxymercuribenzoates; Light; Molecular Conformation; Retinal Pigments; Rhodopsin; Spectrophotometry; Sulfhydryl Compounds; Sulfhydryl Reagents; Vitamin A

1974
Sulfhydryl group modification of photoreceptor G-protein prevents its light-induced binding to rhodopsin.
    FEBS letters, 1984, Mar-12, Volume: 168, Issue:1

    Topics: Alkylation; Animals; Cattle; Ethylmaleimide; Eye Proteins; Heterotrimeric GTP-Binding Proteins; Light; Photoreceptor Cells; Protein Binding; Retinal Pigments; Rhodopsin; Rod Cell Outer Segment; Spectrophotometry, Infrared; Transducin

1984
Mapping of the amino acids in the cytoplasmic loop connecting helices C and D in rhodopsin. Chemical reactivity in the dark state following single cysteine replacements.
    Biochemistry, 1995, Jul-11, Volume: 34, Issue:27

    Topics: Amino Acid Sequence; Animals; Cattle; Cysteine; Cytoplasm; Darkness; Ethylmaleimide; GTP-Binding Proteins; Molecular Sequence Data; Mutation; Protein Structure, Secondary; Rhodopsin

1995
Photoactivation of rhodopsin involves alterations in cysteine side chains: detection of an S-H band in the Meta I-->Meta II FTIR difference spectrum.
    Biophysical journal, 1994, Volume: 66, Issue:6

    Topics: Amino Acid Sequence; Animals; Cattle; Cysteine; Disulfides; Ethylmaleimide; Rhodopsin; Rod Cell Outer Segment; Spectroscopy, Fourier Transform Infrared

1994
Structure and function in rhodopsin. Single cysteine substitution mutants in the cytoplasmic interhelical E-F loop region show position-specific effects in transducin activation.
    Biochemistry, 1996, Sep-24, Volume: 35, Issue:38

    Topics: Amino Acid Sequence; Animals; Cattle; COS Cells; Cysteine; Ethylmaleimide; Fluorescence; Gene Expression; Guanosine Triphosphate; Light; Molecular Sequence Data; Mutagenesis; Recombinant Proteins; Rhodopsin; Rod Opsins; Spectrophotometry; Transducin

1996
Disulfide bond exchange in rhodopsin.
    Biochemistry, 1998, Feb-03, Volume: 37, Issue:5

    Topics: Animals; Cattle; Cysteine; Disulfides; Electrophoresis, Polyacrylamide Gel; Ethylmaleimide; Mutagenesis; Photolysis; Protein Denaturation; Rhodopsin; Spectrophotometry; Transducin

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