tyrosine and retinaldehyde

tyrosine has been researched along with retinaldehyde in 15 studies

Research

Studies (15)

TimeframeStudies, this research(%)All Research%
pre-19904 (26.67)18.7374
1990's3 (20.00)18.2507
2000's6 (40.00)29.6817
2010's1 (6.67)24.3611
2020's1 (6.67)2.80

Authors

AuthorsStudies
Duñach, M; Khorana, HG; Marti, T; Rothschild, KJ1
el-Sayed, MA; Jang, DJ; Khorana, HG; Mogi, T; Stern, LJ1
Mandel, P; Trayhurn, P; Virmaux, N1
Engelhard, M; Hess, B; Kuschmitz, D1
Herz, JM; Hrabeta, E; Packer, L1
Eyring, H; Hays, TR; Lin, SH1
Balashov, S; Ebrey, T; Govindjee, R; Oesterhelt, D; Sheves, M; Steinberg, G1
Lanyi, JK; Luecke, H; Schobert, B; Spudich, EN; Spudich, JL1
Mostafa, HI1
Creemers, AF; de Groot, HJ; Kiihne, SR; Lugtenburg, J1
Kawamura, I; Kihara, N; Naito, A; Nishimura, K; Ohmine, M; Saitô, H; Tuzi, S1
Borhan, B; Geiger, JH; Jia, X; Lee, KS; Vasileiou, C; Wang, W; Watson, CT1
Kandori, H; Mizuno, M; Mizutani, Y; Shibata, M; Yamada, J1
Bartl, FJ; Elgeti, M; Ernst, OP; Heck, M; Hofmann, KP; Kazmin, R; Morizumi, T; Ritter, E; Scheerer, P; Siebert, F1
Chen, S; Ding, X; He, X; Sun, C; Watts, A; Zhao, X1

Other Studies

15 other study(ies) available for tyrosine and retinaldehyde

ArticleYear
Uv-visible spectroscopy of bacteriorhodopsin mutants: substitution of Arg-82, Asp-85, Tyr-185, and Asp-212 results in abnormal light-dark adaptation.
    Proceedings of the National Academy of Sciences of the United States of America, 1990, Volume: 87, Issue:24

    Topics: Arginine; Aspartic Acid; Bacteriorhodopsins; Darkness; Halobacterium; Light; Mutagenesis, Site-Directed; Retinaldehyde; Spectrophotometry; Tyrosine

1990
Effect of genetic modification of tyrosine-185 on the proton pump and the blue-to-purple transition in bacteriorhodopsin.
    Proceedings of the National Academy of Sciences of the United States of America, 1990, Volume: 87, Issue:11

    Topics: Bacteriorhodopsins; Biological Transport, Active; Hydrogen-Ion Concentration; Light; Mutation; Pigments, Biological; Retinaldehyde; Spectrum Analysis; Structure-Activity Relationship; Tyrosine

1990
Composition of the rhodopsin-core obtained by proteolysis of retinal rod outer segments with papain, and its regenerability after photobleaching.
    Experimental eye research, 1974, Volume: 19, Issue:3

    Topics: Alanine; Animals; Arginine; Carbohydrates; Cattle; Chromatography, Thin Layer; Electrophoresis; Glutamates; Glycine; Histidine; Leucine; Light; Lysine; Papain; Photoreceptor Cells; Retinal Pigments; Retinaldehyde; Rhodopsin; Threonine; Tryptophan; Tyrosine

1974
Synoptic views on the photochemical reaction cycle in bacteriorhodopsin.
    Progress in clinical and biological research, 1984, Volume: 164

    Topics: Aspartic Acid; Bacteriorhodopsins; Biological Transport, Active; Carotenoids; Halobacterium; Isomerism; Light; Photochemistry; Protons; Retinaldehyde; Structure-Activity Relationship; Tyrosine

1984
Evidence for a carboxyl group in the vicinity of the retinal chromophore of bacteriorhodopsin.
    Biochemical and biophysical research communications, 1983, Jul-29, Volume: 114, Issue:2

    Topics: Bacteriorhodopsins; Carotenoids; Circular Dichroism; Halobacterium; Kinetics; Protein Conformation; Retinaldehyde; Spectrophotometry; Tyrosine; Vitamin A

1983
Wavelength regulation in rhodopsin: effects of dipoles and amino acid side chains.
    Proceedings of the National Academy of Sciences of the United States of America, 1980, Volume: 77, Issue:11

    Topics: Chemical Phenomena; Chemistry, Physical; Light; Models, Theoretical; Motion; Protein Conformation; Retinal Pigments; Retinaldehyde; Rhodopsin; Tryptophan; Tyrosine; Vitamin A

1980
Lowering the intrinsic pKa of the chromophore's Schiff base can restore its light-induced deprotonation in the inactive Tyr-57-->Asn mutant of bacteriorhodopsin.
    The Journal of biological chemistry, 1994, May-20, Volume: 269, Issue:20

    Topics: Amino Acid Sequence; Asparagine; Bacteriorhodopsins; Halobacterium; Hydrogen-Ion Concentration; Kinetics; Light; Point Mutation; Retinaldehyde; Schiff Bases; Spectrophotometry; Tyrosine

1994
Crystal structure of sensory rhodopsin II at 2.4 angstroms: insights into color tuning and transducer interaction.
    Science (New York, N.Y.), 2001, Aug-24, Volume: 293, Issue:5534

    Topics: Archaeal Proteins; Arginine; Bacteriorhodopsins; Binding Sites; Carotenoids; Color; Crystallography, X-Ray; Electron Spin Resonance Spectroscopy; Hydrogen Bonding; Ion Transport; Light; Models, Molecular; Natronobacterium; Protein Conformation; Protein Structure, Secondary; Protons; Retinaldehyde; Schiff Bases; Signal Transduction; Tyrosine

2001
Effect of beta-particles on the retinal chromophore in bacteriorhodopsin of Halobacterium salinarium.
    Radiation measurements, 2004, Volume: 38, Issue:2

    Topics: Bacteriorhodopsins; Beta Particles; Biotechnology; Dose-Response Relationship, Radiation; Halobacterium salinarum; Mathematics; Photochemistry; Proton Pumps; Purple Membrane; Radiation Monitoring; Retinaldehyde; Schiff Bases; Tryptophan; Tyrosine

2004
Accurate CSA measurements from uniformly isotopically labeled biomolecules at high magnetic field.
    Journal of magnetic resonance (San Diego, Calif. : 1997), 2005, Volume: 172, Issue:1

    Topics: Anisotropy; Carbon Isotopes; Computer Simulation; Histidine; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Quantum Theory; Retinaldehyde; Signal Processing, Computer-Assisted; Tyrosine

2005
Solid-state NMR studies of two backbone conformations at Tyr185 as a function of retinal configurations in the dark, light, and pressure adapted bacteriorhodopsins.
    Journal of the American Chemical Society, 2007, Feb-07, Volume: 129, Issue:5

    Topics: Bacteriorhodopsins; Darkness; Halobacterium salinarum; Isomerism; Light; Magnetic Resonance Spectroscopy; Molecular Conformation; Retinaldehyde; Stress, Mechanical; Tyrosine

2007
Elucidating the exact role of engineered CRABPII residues for the formation of a retinal protonated Schiff base.
    Proteins, 2009, Volume: 77, Issue:4

    Topics: Amino Acid Substitution; Arginine; Base Sequence; Binding Sites; Crystallography, X-Ray; DNA Primers; Models, Molecular; Mutagenesis, Site-Directed; Protein Engineering; Protons; Receptors, Retinoic Acid; Recombinant Proteins; Retinaldehyde; Schiff Bases; Spectrometry, Fluorescence; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Static Electricity; Tryptophan; Tyrosine

2009
Picosecond time-resolved ultraviolet resonance Raman spectroscopy of bacteriorhodopsin: primary protein response to the photoisomerization of retinal.
    The journal of physical chemistry. B, 2009, Sep-03, Volume: 113, Issue:35

    Topics: Bacteriorhodopsins; Catalytic Domain; Hydrogen Bonding; Light; Photochemistry; Photoreceptors, Microbial; Retinaldehyde; Spectrum Analysis, Raman; Time Factors; Tryptophan; Tyrosine

2009
Conserved Tyr223(5.58) plays different roles in the activation and G-protein interaction of rhodopsin.
    Journal of the American Chemical Society, 2011, May-11, Volume: 133, Issue:18

    Topics: Amino Acid Sequence; Conserved Sequence; Protein Interaction Domains and Motifs; Protein Structure, Secondary; Retinaldehyde; Rhodopsin; Spectroscopy, Fourier Transform Infrared; Transducin; Tyrosine

2011
Dynamic Coupling of Tyrosine 185 with the Bacteriorhodopsin Photocycle, as Revealed by Chemical Shifts, Assisted AF-QM/MM Calculations and Molecular Dynamic Simulations.
    International journal of molecular sciences, 2021, Dec-18, Volume: 22, Issue:24

    Topics: Bacteriorhodopsins; Binding Sites; Halobacterium salinarum; Hydrogen Bonding; Light; Molecular Dynamics Simulation; Protein Conformation; Quantum Theory; Retinaldehyde; Tyrosine

2021