Compounds > phenylalanine

phenylalanine and retinaldehyde

phenylalanine has been researched along with retinaldehyde in 6 studies

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19901 (16.67)18.7374
1990's2 (33.33)18.2507
2000's0 (0.00)29.6817
2010's3 (50.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Khorana, HG; Marti, T; Mogi, T1
Friedman, N; Hatanaka, M; Kandori, H; Kashima, R; Lanyi, JK; Maeda, A; Needleman, R; Sheves, M1
Brown, LS; Dioumaev, AK; Lanyi, JK; Needleman, R1
Bach, A; Engelstoft, MS; Frimurer, TM; Holst, B; Nygaard, R; Petersen, PS; Schwartz, TW; Valentin-Hansen, L1
Fu, Y; Zhang, T1
Birge, RR; Knox, BE; Kuemmel, CM; Sandberg, MN1

Other Studies

6 other study(ies) available for phenylalanine and retinaldehyde

ArticleYear
Structure-function studies on bacteriorhodopsin. IX. Substitutions of tryptophan residues affect protein-retinal interactions in bacteriorhodopsin.
    The Journal of biological chemistry, 1989, Aug-25, Volume: 264, Issue:24

    Topics: Amino Acid Sequence; Bacteriorhodopsins; Cloning, Molecular; Hydrogen-Ion Concentration; Light; Molecular Sequence Data; Phenylalanine; Protein Conformation; Protons; Retinaldehyde; Retinoids; Structure-Activity Relationship; Tryptophan

1989
Trp86 --> Phe replacement in bacteriorhodopsin affects a water molecule near Asp85 and light adaptation.
    Biochemistry, 1997, May-06, Volume: 36, Issue:18

    Topics: Aspartic Acid; Bacteriorhodopsins; Halobacterium; Light; Mutation; Phenylalanine; Photochemistry; Protein Binding; Retinaldehyde; Spectroscopy, Fourier Transform Infrared; Tryptophan; Water

1997
Partitioning of free energy gain between the photoisomerized retinal and the protein in bacteriorhodopsin.
    Biochemistry, 1998, Jul-14, Volume: 37, Issue:28

    Topics: Amino Acid Substitution; Asparagine; Aspartic Acid; Bacterial Proteins; Bacteriorhodopsins; Cysteine; Energy Transfer; Halobacterium salinarum; Hydrogen-Ion Concentration; Isomerism; Mutagenesis, Site-Directed; Phenylalanine; Photochemistry; Retinaldehyde; Spectrophotometry; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman

1998
A conserved aromatic lock for the tryptophan rotameric switch in TM-VI of seven-transmembrane receptors.
    The Journal of biological chemistry, 2010, Feb-05, Volume: 285, Issue:6

    Topics: Allosteric Regulation; Amino Acid Sequence; Animals; Binding Sites; Chlorocebus aethiops; COS Cells; Humans; Models, Molecular; Molecular Dynamics Simulation; Molecular Sequence Data; Mutation; Phenylalanine; Protein Binding; Protein Conformation; Receptors, Adrenergic, beta-2; Receptors, G-Protein-Coupled; Receptors, Ghrelin; Retinaldehyde; Rhodopsin; Tryptophan

2010
A Phe-rich region in short-wavelength sensitive opsins is responsible for their aggregation in the absence of 11-cis-retinal.
    FEBS letters, 2013, Aug-02, Volume: 587, Issue:15

    Topics: Amino Acid Sequence; Animals; Chlorocebus aethiops; COS Cells; Humans; Mice; Molecular Sequence Data; Opsins; Phenylalanine; Retinaldehyde; Sequence Homology, Amino Acid

2013
A conserved aromatic residue regulating photosensitivity in short-wavelength sensitive cone visual pigments.
    Biochemistry, 2013, Jul-30, Volume: 52, Issue:30

    Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Binding Sites; Cone Opsins; Conserved Sequence; Models, Molecular; Molecular Conformation; Mutagenesis, Site-Directed; Mutant Proteins; Phenylalanine; Photobleaching; Recombinant Proteins; Retinaldehyde; Spectrophotometry; Xenopus; Xenopus Proteins

2013