glutamic acid has been researched along with retinaldehyde in 19 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (5.26) | 18.7374 |
| 1990's | 9 (47.37) | 18.2507 |
| 2000's | 7 (36.84) | 29.6817 |
| 2010's | 2 (10.53) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Cohen, GB; Oprian, DD; Robinson, PR; Zhukovsky, EA | 1 |
| De Caluwé, GL; De Grip, WJ; Jansen, JJ; Mulder, WR; Vlak, JM | 1 |
| Nathans, J | 1 |
| Oprian, DD; Zhukovsky, EA | 1 |
| Beck, M; Fahmy, K; Jäger, F; Sakmar, TP; Siebert, F; Zvyaga, TA | 1 |
| DeDecker, BS; Han, M; Smith, SO | 1 |
| Honig, B; Sampogna, RV | 1 |
| Brown, LS; Dioumaev, AK; Kimura, Y; Lanyi, JK; Needleman, R; Richter, HT; Saito, H; Tanio, M; Tuzi, S | 1 |
| Aalten, DM; Findlay, JB; Sivaprasadarao, A; Sundaram, M | 1 |
| Baker, EN; Baker, HM; Blythe, TJ; Kitson, KE; Kitson, TM; Moore, SA | 1 |
| Balashov, SP; Ebrey, TG; Gennis, RB; Kandori, H; Maeda, A; Tomson, FL | 1 |
| Farrens, DL; Janz, JM | 1 |
| Babu, KR; Birge, RR; Dukkipati, A; Knox, BE | 1 |
| Guidoni, L; Röhrig, UF; Rothlisberger, U | 1 |
| Gross, AK; Oprian, DD; Xie, G | 1 |
| Asato, AE; Sheves, M; Zadok, U | 1 |
| Brown, LS; Fan, Y; Furutani, Y; Kandori, H; Shi, L; Sumii, M; Waschuk, SA | 1 |
| Choi, AR; Furutani, Y; Hashimoto, K; Jung, KH; Kandori, H | 1 |
| Heberle, J; Lórenz-Fonfría, VA | 1 |
1 review(s) available for glutamic acid and retinaldehyde
| Article | Year |
|---|---|
Channelrhodopsin unchained: structure and mechanism of a light-gated cation channel.
Topics: Aspartic Acid; Chlamydomonas reinhardtii; Glutamic Acid; Hydrogen-Ion Concentration; Ion Channel Gating; Ion Transport; Kinetics; Light; Models, Molecular; Protein Conformation; Protons; Retinaldehyde; Rhodopsin; Thermodynamics; Time Factors | 2014 |
18 other study(ies) available for glutamic acid and retinaldehyde
| Article | Year |
|---|---|
Constitutively active mutants of rhodopsin.
Topics: Amino Acid Sequence; Animals; Cell Line; Glutamates; Glutamic Acid; Kinetics; Lysine; Mutagenesis, Site-Directed; Retinaldehyde; Rhodopsin; Rod Cell Outer Segment; Rod Opsins; Schiff Bases; Transducin; Transfection | 1992 |
In vitro expression of bovine opsin using recombinant baculovirus: the role of glutamic acid (134) in opsin biosynthesis and glycosylation.
Topics: Animals; Baculoviridae; Cell Line; Chromatography, Affinity; Eye Proteins; Gene Expression; Genetic Vectors; Glutamates; Glutamic Acid; Glycosylation; Immunoblotting; Mutagenesis, Site-Directed; Protein Processing, Post-Translational; Recombinant Proteins; Retinaldehyde; Rhodopsin; Rod Opsins | 1991 |
Determinants of visual pigment absorbance: identification of the retinylidene Schiff's base counterion in bovine rhodopsin.
Topics: Animals; Asparagine; Aspartic Acid; Cattle; Glutamates; Glutamic Acid; Glutamine; Kinetics; Membranes; Models, Molecular; Mutagenesis, Site-Directed; Plasmids; Protein Conformation; Recombinant Proteins; Retinaldehyde; Rhodopsin; Schiff Bases; Spectrophotometry | 1990 |
Effect of carboxylic acid side chains on the absorption maximum of visual pigments.
Topics: Aspartic Acid; Glutamates; Glutamic Acid; Hydrogen-Ion Concentration; Hydroxylamine; Hydroxylamines; Models, Molecular; Mutation; Protein Conformation; Retinal Pigments; Retinaldehyde; Retinoids; Rhodopsin; Schiff Bases; Spectrophotometry | 1989 |
Protonation states of membrane-embedded carboxylic acid groups in rhodopsin and metarhodopsin II: a Fourier-transform infrared spectroscopy study of site-directed mutants.
Topics: Amino Acid Sequence; Animals; Asparagine; Aspartic Acid; Cell Line; Glutamates; Glutamic Acid; Glutamine; Kinetics; Light; Mutagenesis, Site-Directed; Protein Conformation; Recombinant Proteins; Retinaldehyde; Rhodopsin; Spectrophotometry; Spectroscopy, Fourier Transform Infrared; Time Factors; Transfection | 1993 |
Localization of the retinal protonated Schiff base counterion in rhodopsin.
Topics: Amino Acid Sequence; Binding Sites; Carbon Isotopes; Glutamates; Glutamic Acid; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Conformation; Protein Conformation; Retinaldehyde; Rhodopsin; Schiff Bases | 1993 |
Electrostatic coupling between retinal isomerization and the ionization state of Glu-204: a general mechanism for proton release in bacteriorhodopsin.
Topics: Bacteriorhodopsins; Binding Sites; Biophysical Phenomena; Biophysics; Glutamic Acid; Hydrogen-Ion Concentration; Ions; Isomerism; Models, Molecular; Molecular Structure; Protein Conformation; Protons; Retinaldehyde; Static Electricity | 1996 |
Existence of a proton transfer chain in bacteriorhodopsin: participation of Glu-194 in the release of protons to the extracellular surface.
Topics: Bacteriorhodopsins; Binding Sites; Cell Membrane; Glutamic Acid; Halobacterium salinarum; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Photochemistry; Point Mutation; Protein Conformation; Protons; Retinaldehyde; Schiff Bases; Spectroscopy, Fourier Transform Infrared | 1998 |
Expression, characterization and engineered specificity of rat epididymal retinoic acid-binding protein.
Topics: Animals; Arginine; Binding Sites; Cloning, Molecular; Epididymis; Escherichia coli; Glutamic Acid; Isoleucine; Male; Models, Molecular; Mutagenesis, Site-Directed; Point Mutation; Polymerase Chain Reaction; Rats; Receptors, Retinoic Acid; Recombinant Proteins; Restriction Mapping; Retinaldehyde; Retinoids; Retinol-Binding Proteins, Plasma; Substrate Specificity; Tretinoin; Vitamin A | 1998 |
A structural explanation for the retinal specificity of class 1 ALDH enzymes.
Topics: Aldehyde Dehydrogenase; Aldehyde Dehydrogenase 1 Family; Aldehyde Dehydrogenase, Mitochondrial; Animals; Binding Sites; Cattle; Crystallography, X-Ray; Glutamic Acid; Isoenzymes; NAD; Protein Conformation; Retinal Dehydrogenase; Retinaldehyde; Sheep; Structure-Activity Relationship; Substrate Specificity | 1999 |
Relocation of internal bound water in bacteriorhodopsin during the photoreaction of M at low temperatures: an FTIR study.
Topics: Aspartic Acid; Bacteriorhodopsins; Cell Polarity; Glutamic Acid; Halobacterium; Mutation; Proton Pumps; Retinaldehyde; Schiff Bases; Spectroscopy, Fourier Transform Infrared; Threonine; Valine; Water | 2000 |
Engineering a functional blue-wavelength-shifted rhodopsin mutant.
Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Animals; Aspartic Acid; Cattle; COS Cells; Glutamic Acid; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Photochemistry; Retinaldehyde; Rhodopsin; Serine; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Thermodynamics; Threonine; Transducin | 2001 |
Regulation of phototransduction in short-wavelength cone visual pigments via the retinylidene Schiff base counterion.
Topics: Animals; Aspartic Acid; Cattle; COS Cells; Glutamic Acid; Glutamine; Mutagenesis, Site-Directed; Protons; Retinal Cone Photoreceptor Cells; Retinaldehyde; Retinoids; Rod Opsins; Schiff Bases; Spectrophotometry, Ultraviolet; Static Electricity; Vision, Ocular; Xenopus | 2001 |
Early steps of the intramolecular signal transduction in rhodopsin explored by molecular dynamics simulations.
Topics: Animals; Cattle; Computational Biology; Computer Simulation; Crystallography, X-Ray; Glutamic Acid; Hydrogen-Ion Concentration; Isomerism; Membrane Proteins; Models, Molecular; Molecular Mimicry; Protein Conformation; Protons; Retinaldehyde; Retinoids; Rhodopsin; Signal Transduction; Software; Thermodynamics | 2002 |
Slow binding of retinal to rhodopsin mutants G90D and T94D.
Topics: Alanine; Amino Acid Sequence; Animals; Aspartic Acid; Glutamic Acid; Glutamine; Glycine; Humans; Molecular Sequence Data; Mutagenesis, Insertional; Night Blindness; Protein Binding; Protein Denaturation; Retinaldehyde; Rhodopsin; Schiff Bases; Spectrophotometry, Ultraviolet; Threonine | 2003 |
Titration of the bacteriorhodopsin Schiff base involves titration of an additional protein residue.
Topics: Amino Acid Substitution; Aspartic Acid; Bacteriorhodopsins; Deuterium Exchange Measurement; Glutamic Acid; Glutamine; Halobacterium salinarum; Hydrogen-Ion Concentration; Photochemistry; Protons; Retinaldehyde; Schiff Bases; Titrimetry | 2005 |
Conformational coupling between the cytoplasmic carboxylic acid and the retinal in a fungal light-driven proton pump.
Topics: Amino Acid Substitution; Ascomycota; Asparagine; Aspartic Acid; Carboxylic Acids; Cytoplasm; Glutamic Acid; Lasers; Neurospora; Protein Conformation; Proton Pumps; Retinaldehyde; Rhodopsin | 2006 |
Low-temperature FTIR study of Gloeobacter rhodopsin: presence of strongly hydrogen-bonded water and long-range structural protein perturbation upon retinal photoisomerization.
Topics: Amino Acid Sequence; Amino Acids; Carboxylic Acids; Cyanobacteria; Glutamic Acid; Hydrogen Bonding; Isomerism; Models, Molecular; Molecular Sequence Data; Photochemistry; Protein Conformation; Retinaldehyde; Rhodopsins, Microbial; Spectroscopy, Fourier Transform Infrared; Water | 2010 |