Page last updated: 2024-08-23

azides and 11-cis-retinal

azides has been researched along with 11-cis-retinal in 17 studies

Research

Studies (17)

TimeframeStudies, this research(%)All Research%
pre-19906 (35.29)18.7374
1990's0 (0.00)18.2507
2000's6 (35.29)29.6817
2010's5 (29.41)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Darszon, A; Klip, A; Montal, M1
Ross, EM; Ruoho, AE; Slaughter, C; Wong, SK1
Farber, DB; Nagy, AK; Shuster, TA1
Bercovici, T; Gitler, C; Raviv, Y; Salomon, Y1
Kohnken, RE; Mc Connell, DG1
Haley, BE; Hansen, J; Pinkett, O; Takemoto, DJ; Takemoto, LJ1
Bamberg, E; Becker, A; Chizhov, I; Engelhard, M; Lüttenberg, B; Schmies, G1
Cai, K; Itoh, Y; Khorana, HG2
Ebrey, TG; Govindjee, R; Kuwata, O; Misra, S; Yuan, C1
Bustamante, C; Greenfield, D; Liphardt, J; Walter, JM1
Huber, T; Sakmar, TP; Vogel, R; Ye, S1
Caltabiano, G; Deupi, X; Sakmar, TP; Schertler, GF; Vogel, R; Ye, S; Zaitseva, E1
Hoffmann, C1
Huber, T; Sakmar, TP; Tian, H3

Other Studies

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

ArticleYear
Labelling of rhodopsin moieties confined to the membrane lipid bilayer.
    Biochemical and biophysical research communications, 1976, Oct-18, Volume: 72, Issue:4

    Topics: Animals; Azides; Carbohydrates; Cattle; Chymotrypsin; Coloring Agents; Membrane Lipids; Molecular Weight; Naphthalenes; Peptide Fragments; Photoreceptor Cells; Polyethylene Glycols; Retinal Pigments; Rhodopsin

1976
The catecholamine binding site of the beta-adrenergic receptor is formed by juxtaposed membrane-spanning domains.
    The Journal of biological chemistry, 1988, Jun-15, Volume: 263, Issue:17

    Topics: Affinity Labels; Animals; Azides; Binding Sites; Catecholamines; Cell Membrane; Diazomethane; Iodocyanopindolol; Peptide Mapping; Photochemistry; Pindolol; Receptors, Adrenergic, beta; Rhodopsin; Turkeys

1988
8-Azido-ATP (alpha 32P) binding to rod outer segment proteins.
    Experimental eye research, 1988, Volume: 46, Issue:4

    Topics: Adenosine Triphosphate; Animals; Azides; Binding, Competitive; Electrophoresis, Polyacrylamide Gel; Eye Proteins; GTP-Binding Proteins; Heterotrimeric GTP-Binding Proteins; Manganese; Membrane Proteins; Phosphodiesterase Inhibitors; Photoreceptor Cells; Protein Binding; Rats; Rhodopsin; Rod Cell Outer Segment; Zinc

1988
Selective labeling of proteins in biological systems by photosensitization of 5-iodonaphthalene-1-azide.
    Proceedings of the National Academy of Sciences of the United States of America, 1987, Volume: 84, Issue:17

    Topics: Adenylyl Cyclases; Animals; Azides; In Vitro Techniques; Lipid Bilayers; Membrane Proteins; Photolysis; Rhodopsin; Rod Cell Outer Segment

1987
Use of 8-azidoguanosine 5'-[gamma-32P]triphosphate as a probe of the guanosine 5'-triphosphate binding protein subunits in bovine rod outer segments.
    Biochemistry, 1985, Jul-02, Volume: 24, Issue:14

    Topics: Animals; Azides; Binding Sites; Cattle; GTP-Binding Proteins; Guanosine Triphosphate; Kinetics; Macromolecular Substances; Molecular Weight; Phosphorus Radioisotopes; Photolysis; Photoreceptor Cells; Retinal Pigments; Rhodopsin; Rod Cell Outer Segment; Ultraviolet Rays

1985
GTPase from rod outer segments: characterization by photoaffinity labeling and tryptic peptide mapping.
    Biochemical and biophysical research communications, 1981, Sep-16, Volume: 102, Issue:1

    Topics: Adenosine Triphosphate; Affinity Labels; Animals; Azides; Cattle; GTP Phosphohydrolases; Macromolecular Substances; Molecular Weight; Peptide Fragments; Phosphoric Monoester Hydrolases; Photoreceptor Cells; Rhodopsin; Rod Cell Outer Segment; Trypsin

1981
Sensory rhodopsin II from the haloalkaliphilic natronobacterium pharaonis: light-activated proton transfer reactions.
    Biophysical journal, 2000, Volume: 78, Issue:2

    Topics: Archaeal Proteins; Azides; Electrophysiology; Hydrogen-Ion Concentration; Imidazoles; Kinetics; Light; Mutation; Natronobacterium; Photolysis; Proton Pumps; Recombinant Proteins; Rhodopsin; Spectrophotometry

2000
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
Mapping of contact sites in complex formation between light-activated rhodopsin and transducin by covalent crosslinking: use of a chemically preactivated 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; Amino Acid Substitution; Animals; Azides; Binding Sites; Blotting, Western; Cattle; Cross-Linking Reagents; Cysteine; Hydrogen-Ion Concentration; Light; Models, Molecular; Molecular Sequence Data; Mutation; Peptide Fragments; Protein Binding; Protein Structure, Secondary; Protein Subunits; Pyridines; Rhodopsin; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Succinimides; Transducin

2001
Kinetics and pH dependence of light-induced deprotonation of the Schiff base of rhodopsin: possible coupling to proton uptake and formation of the active form of Meta II.
    Biochemistry. Biokhimiia, 2001, Volume: 66, Issue:11

    Topics: Azides; Hydrogen-Ion Concentration; Kinetics; Light; Protons; Rhodopsin; Schiff Bases

2001
Light-powering Escherichia coli with proteorhodopsin.
    Proceedings of the National Academy of Sciences of the United States of America, 2007, Feb-13, Volume: 104, Issue:7

    Topics: Anaerobiosis; Azides; Energy Metabolism; Escherichia coli; Flagella; Kinetics; Light; Oceans and Seas; Proton Pumps; Rhodopsin; Rhodopsins, Microbial

2007
FTIR analysis of GPCR activation using azido probes.
    Nature chemical biology, 2009, Volume: 5, Issue:6

    Topics: Azides; Electron Spin Resonance Spectroscopy; Models, Structural; Molecular Probes; Phenylalanine; Receptors, G-Protein-Coupled; Rhodopsin; Spectroscopy, Fourier Transform Infrared; Static Electricity

2009
Tracking G-protein-coupled receptor activation using genetically encoded infrared probes.
    Nature, 2010, Apr-29, Volume: 464, Issue:7293

    Topics: Azides; Cell Line; Humans; Infrared Rays; Models, Molecular; Movement; Phenylalanine; Protein Conformation; Rhodopsin; Spectroscopy, Fourier Transform Infrared; Static Electricity; Vibration

2010
G protein-coupled receptor activation: amino acid movements caught infra-red-handed.
    Chembiochem : a European journal of chemical biology, 2010, Nov-02, Volume: 11, Issue:16

    Topics: Azides; Codon, Terminator; HEK293 Cells; Humans; Phenylalanine; Protein Structure, Tertiary; Receptors, G-Protein-Coupled; Rhodopsin; RNA, Transfer; Spectroscopy, Fourier Transform Infrared

2010
Site-specific labeling of genetically encoded azido groups for multicolor, single-molecule fluorescence imaging of GPCRs.
    Methods in cell biology, 2013, Volume: 117

    Topics: Azides; Codon, Nonsense; Cycloaddition Reaction; Fluorescent Dyes; Gene Expression; HEK293 Cells; Humans; Hydrazines; Immunoprecipitation; Kinetics; Molecular Imaging; Opsins; Protein Multimerization; Retinaldehyde; Rhodopsin; Signal Transduction; Spectrometry, Fluorescence; Staining and Labeling; Transfection

2013
Micelle-Enhanced Bioorthogonal Labeling of Genetically Encoded Azido Groups on the Lipid-Embedded Surface of a GPCR.
    Chembiochem : a European journal of chemical biology, 2015, Jun-15, Volume: 16, Issue:9

    Topics: Alkynes; Animals; Azides; Cattle; Cell Line; Cell Membrane; Cycloaddition Reaction; Detergents; Fluorescent Dyes; Gene Expression; Lipids; Micelles; Models, Molecular; Phenylalanine; Protein Conformation; Receptors, G-Protein-Coupled; Rhodopsin

2015
A simple method for enhancing the bioorthogonality of cyclooctyne reagent.
    Chemical communications (Cambridge, England), 2016, Apr-07, Volume: 52, Issue:31

    Topics: Alkynes; Animals; Azides; Cattle; Cycloaddition Reaction; Cyclooctanes; Cysteine; Mercaptoethanol; Models, Molecular; Rhodopsin; Sulfhydryl Compounds

2016