cysteine and retinaldehyde

cysteine has been researched along with retinaldehyde in 10 studies

Research

Studies (10)

TimeframeStudies, this research(%)All Research%
pre-19901 (10.00)18.7374
1990's4 (40.00)18.2507
2000's3 (30.00)29.6817
2010's1 (10.00)24.3611
2020's1 (10.00)2.80

Authors

AuthorsStudies
Beischel, CJ; Crouch, RK; Ebrey, TG; Feng, Y; Hazard, ES; Katz, BM; Menick, DR; Misra, S1
Brown, LS; Lanyi, JK; Needleman, R; Váró, G1
Brown, LS; Dioumaev, AK; Lanyi, JK; Needleman, R1
Crouch, RK; Datta-Gupta, N; Hazard, ES1
Gross, AK; Oprian, DD; Xie, G1
LOVE, BB; PESKIN, JC1
Bezerra, AG; Brown, LS; Furutani, Y; Kandori, H; Sumii, M; Waschuk, S1
Gentleman, S; Lu, Z; Poliakov, E; Redmond, TM; Tsai, JY; Yu, S1
Hendrickson, WA; Jin, Y; Min, KC1
Imamoto, Y; Mizuno, M; Mizutani, Y; Ohuchi, H; Sakai, K; Sato, K; Shichida, Y; Wada, A; Yamano, Y; Yamashita, T1

Other Studies

10 other study(ies) available for cysteine and retinaldehyde

ArticleYear
Probing of the retinal binding site of bacteriorhodopsin by affinity labeling.
    Biochemistry, 1994, Sep-27, Volume: 33, Issue:38

    Topics: Affinity Labels; Amino Acid Sequence; Bacteriorhodopsins; Binding Sites; Cross-Linking Reagents; Cysteine; Escherichia coli; Halobacterium salinarum; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Proton Pumps; Recombinant Proteins; Retinaldehyde; Sequence Analysis, DNA

1994
Functional significance of a protein conformation change at the cytoplasmic end of helix F during the bacteriorhodopsin photocycle.
    Biophysical journal, 1995, Volume: 69, Issue:5

    Topics: Bacteriorhodopsins; Biophysical Phenomena; Biophysics; Cross-Linking Reagents; Cysteine; Cytoplasm; Halobacterium; Hydrostatic Pressure; Kinetics; Maleimides; Models, Molecular; Mutagenesis, Site-Directed; Photochemistry; Protein Conformation; Proton Pumps; Retinaldehyde; Schiff Bases; Water

1995
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
Categorizing reactivity of bacteriorhodopsin cysteine mutants crosslinking to 4-bromoretinal.
    Biochemistry and molecular biology international, 1999, Volume: 47, Issue:5

    Topics: Bacterial Proteins; Bacteriorhodopsins; Cross-Linking Reagents; Cysteine; Models, Molecular; Mutagenesis; Retinaldehyde

1999
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
THE REACTION OF L-CYSTEINE WITH ALL-TRANS-RETINENE.
    Biochimica et biophysica acta, 1963, Dec-13, Volume: 78

    Topics: Cysteine; Research; Retinal Pigments; Retinaldehyde; Spectrum Analysis

1963
FTIR spectroscopy of the K photointermediate of Neurospora rhodopsin: structural changes of the retinal, protein, and water molecules after photoisomerization.
    Biochemistry, 2004, Aug-03, Volume: 43, Issue:30

    Topics: Amino Acid Sequence; Archaeal Proteins; Bacteriorhodopsins; Carrier Proteins; Cysteine; Freezing; Fungal Proteins; Isomerism; Light; Molecular Sequence Data; Photoreceptors, Microbial; Recombinant Proteins; Retinaldehyde; Rhodopsin; Schiff Bases; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman; Water

2004
Mutation of key residues of RPE65 abolishes its enzymatic role as isomerohydrolase in the visual cycle.
    Proceedings of the National Academy of Sciences of the United States of America, 2005, Sep-20, Volume: 102, Issue:38

    Topics: Acyltransferases; Amino Acid Substitution; Animals; Blindness; Carrier Proteins; Cattle; Cell Line; cis-trans-Isomerases; Cysteine; Dogs; Eye Proteins; Humans; Iron; Isomerases; Mice; Oxygenases; Point Mutation; Protein Processing, Post-Translational; Retina; Retinaldehyde; Transfection; Vision, Ocular

2005
Large-scale production of a disulfide-stabilized constitutively active mutant opsin.
    Protein expression and purification, 2011, Volume: 75, Issue:2

    Topics: Animals; Cattle; Cell Line; Cloning, Molecular; Cysteine; Detergents; Disulfides; Humans; Mutagenesis, Site-Directed; Opsins; Protein Stability; Recombinant Proteins; Retinaldehyde; Signal Transduction; Transducin

2011
Chromophore Structure in an Inactive State of a Novel Photosensor Protein Opn5L1: Resonance Raman Evidence for the Formation of a Deprotonated Adduct at the 11th Carbon Atom.
    The journal of physical chemistry. B, 2023, 03-16, Volume: 127, Issue:10

    Topics: Carbon; Cysteine; GTP-Binding Proteins; Opsins; Retinaldehyde

2023