aspartic acid has been researched along with retinaldehyde in 38 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 3 (7.89) | 18.7374 |
| 1990's | 15 (39.47) | 18.2507 |
| 2000's | 15 (39.47) | 29.6817 |
| 2010's | 5 (13.16) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Masland, RH; Pepperberg, DR | 1 |
| Betlach, MC; Kliger, DS; Miercke, LJ; Milder, SJ; Shand, RF; Stroud, RM; Thorgeirsson, TE | 1 |
| Nathans, J | 2 |
| Duñach, M; Khorana, HG; Marti, T; Rothschild, KJ | 1 |
| Oprian, DD; Zhukovsky, EA | 1 |
| Engelhard, M; Hess, B; Kuschmitz, D | 1 |
| Friedman, N; Ottolenghi, M; Rousso, I; Sheves, M | 1 |
| Beck, M; Fahmy, K; Jäger, F; Sakmar, TP; Siebert, F; Zvyaga, TA | 1 |
| Schulten, K; Sheves, M; Xu, D | 1 |
| Kandori, H; Lanyi, JK; Maeda, A; Needleman, R; Richter, HT | 1 |
| Friedman, N; Gat, Y; Ottolenghi, M; Sheves, M | 1 |
| Friedman, N; Hatanaka, M; Kandori, H; Kashima, R; Lanyi, JK; Maeda, A; Needleman, R; Sheves, M | 1 |
| Bressler, S; Eliash, T; Friedman, N; Fu, X; Ottolenghi, M; Sheves, M | 1 |
| Brown, LS; Dioumaev, AK; Lanyi, JK; Needleman, R | 4 |
| Lanyi, JK; Luecke, H; Richter, HT | 1 |
| Bennett, AE; Engelhard, M; Griffin, RG; Griffiths, JM; Herzfeld, J; Lugtenburg, J; Raap, J; Siebert, F | 1 |
| Bergo, V; Rothschild, KJ; Scott, KL; Spudich, EN; Spudich, JL | 1 |
| Balashov, SP; Ebrey, TG; Gennis, RB; Kandori, H; Maeda, A; Tomson, FL | 1 |
| Farrens, DL; Janz, JM | 1 |
| Aharoni, A; Ottolenghi, M; Sheves, M | 1 |
| Babu, KR; Birge, RR; Dukkipati, A; Knox, BE | 1 |
| Gross, AK; Oprian, DD; Xie, G | 2 |
| Brown, LS; Lanyi, JK; Schobert, B | 1 |
| Balashov, SP; Dioumaev, AK; Imasheva, ES; Lanyi, JK; Wang, JM | 1 |
| Gerwert, K; Kandt, C; Schlitter, J | 1 |
| Asato, AE; Sheves, M; Zadok, U | 1 |
| Brown, LS; Fan, Y; Furutani, Y; Kandori, H; Shi, L; Sumii, M; Waschuk, SA | 1 |
| Cilluffo, MC; Cornwall, MC; Dizhoor, AM; Fain, GL; Olshevskaya, EV; Sieving, PA; Woodruff, ML | 1 |
| Homma, M; Irieda, H; Kandori, H; Kawanabe, A; Reissig, L; Sudo, Y | 1 |
| Bamann, C; Glaubitz, C; Herz, J; Verhoefen, MK; Wachtveitl, J; Weber, I | 1 |
| Alvarez, S; Bourdelande, JL; de Lera, AR; Domínguez, M; Lórenz-Fonfría, VA; Padrós, E; Perálvarez-Marín, A; Simón-Vázquez, R | 1 |
| Heberle, J; Lórenz-Fonfría, VA | 1 |
| Barty, A; Båth, P; Borin, V; Bosman, R; Brünle, S; Carbajo, S; Furrer, A; Gashi, D; Hunter, M; Iwata, S; Jaeger, K; James, D; Kekilli, D; Koglin, J; Lane, T; Milne, C; Nango, E; Nass, K; Neutze, R; Nogly, P; Ozerov, D; Panneels, V; Schapiro, I; Schertler, G; Seaberg, M; Skopintsev, P; Standfuss, J; Tanaka, T; Weierstall, U; Weinert, T; White, T; Wu, W | 1 |
1 review(s) available for aspartic 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 |
37 other study(ies) available for aspartic acid and retinaldehyde
| Article | Year |
|---|---|
Retinal-induced sensitization of light-adapted rabbit photoreceptors.
Topics: Animals; Aspartic Acid; Dark Adaptation; Photic Stimulation; Photoreceptor Cells; Rabbits; Retina; Retinaldehyde; Synaptic Transmission; Vitamin A | 1978 |
Effects of Asp-96----Asn, Asp-85----Asn, and Arg-82----Gln single-site substitutions on the photocycle of bacteriorhodopsin.
Topics: Arginine; Asparagine; Aspartic Acid; Bacteriorhodopsins; Biological Transport, Active; Glutamine; Halobacterium; In Vitro Techniques; Kinetics; Light; Photosynthesis; Recombinant Proteins; Retinaldehyde; Schiff Bases; Spectrum Analysis; Structure-Activity Relationship | 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 |
Determinants of visual pigment absorbance: role of charged amino acids in the putative transmembrane segments.
Topics: Amino Acid Sequence; Animals; Arginine; Aspartic Acid; Cattle; Gene Expression; Glutamates; Histidine; Lysine; Membrane Proteins; Molecular Sequence Data; Molecular Structure; Mutation; Retinal Pigments; Retinaldehyde; Rhodopsin; Spectrophotometry | 1990 |
Uv-visible spectroscopy of bacteriorhodopsin mutants: substitution of Arg-82, Asp-85, Tyr-185, and Asp-212 results in abnormal light-dark adaptation.
Topics: Arginine; Aspartic Acid; Bacteriorhodopsins; Darkness; Halobacterium; Light; Mutagenesis, Site-Directed; Retinaldehyde; Spectrophotometry; Tyrosine | 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 |
Synoptic views on the photochemical reaction cycle in bacteriorhodopsin.
Topics: Aspartic Acid; Bacteriorhodopsins; Biological Transport, Active; Carotenoids; Halobacterium; Isomerism; Light; Photochemistry; Protons; Retinaldehyde; Structure-Activity Relationship; Tyrosine | 1984 |
pKa of the protonated Schiff base and aspartic 85 in the bacteriorhodopsin binding site is controlled by a specific geometry between the two residues.
Topics: Aspartic Acid; Bacteriorhodopsins; Binding Sites; Hydrogen-Ion Concentration; Light; Molecular Structure; Proton Pumps; Protons; Retinaldehyde; Schiff Bases; Spectrophotometry | 1995 |
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 |
Molecular dynamics study of the M412 intermediate of bacteriorhodopsin.
Topics: Amino Acid Sequence; Aspartic Acid; Bacteriorhodopsins; Calorimetry; Computer Simulation; Kinetics; Light; Models, Molecular; Models, Structural; Protein Conformation; Protein Structure, Secondary; Retinaldehyde; Schiff Bases; Software | 1995 |
Relationship of retinal configuration and internal proton transfer at the end of the bacteriorhodopsin photocycle.
Topics: Aspartic Acid; Bacteriorhodopsins; Chemical Phenomena; Chemistry, Physical; Kinetics; Protons; Retinaldehyde; Spectroscopy, Fourier Transform Infrared | 1996 |
Interaction between Asp-85 and the proton-releasing group in bacteriorhodopsin. A study of an O-like photocycle intermediate.
Topics: Arylsulfonates; Aspartic Acid; Bacteriorhodopsins; Bromphenol Blue; Halobacterium; Hydrogen-Ion Concentration; Kinetics; Lasers; Molecular Structure; Photolysis; Protons; Retinaldehyde; Spectrophotometry; Titrimetry | 1997 |
Trp86 --> Phe replacement in bacteriorhodopsin affects a water molecule near Asp85 and light adaptation.
Topics: Aspartic Acid; Bacteriorhodopsins; Halobacterium; Light; Mutation; Phenylalanine; Photochemistry; Protein Binding; Retinaldehyde; Spectroscopy, Fourier Transform Infrared; Tryptophan; Water | 1997 |
Titration kinetics of Asp-85 in bacteriorhodopsin: exclusion of the retinal pocket as the color-controlling cation binding site.
Topics: Aspartic Acid; Bacteriorhodopsins; Binding Sites; Calcium; Cations, Divalent; Kinetics; Magnesium; Quaternary Ammonium Compounds; Retinaldehyde; Spectrophotometry; Time Factors | 1997 |
Local-access model for proton transfer in bacteriorhodopsin.
Topics: Amino Acid Substitution; Asparagine; Aspartic Acid; Bacteriorhodopsins; Electron Transport; Halobacterium salinarum; Hydrogen-Ion Concentration; Isomerism; Kinetics; Models, Biological; Mutagenesis, Site-Directed; Photochemistry; Protons; Retinaldehyde; Schiff Bases | 1998 |
Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution.
Topics: Aspartic Acid; Bacteriorhodopsins; Binding Sites; Crystallography, X-Ray; Hydrogen Bonding; Hydrogen-Ion Concentration; Ligands; Light; Models, Molecular; Photochemistry; Protein Conformation; Protein Structure, Secondary; Protons; Retinaldehyde; Schiff Bases; Water | 1998 |
Partitioning of free energy gain between the photoisomerized retinal and the protein in bacteriorhodopsin.
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 |
Connectivity of the retinal Schiff base to Asp85 and Asp96 during the bacteriorhodopsin photocycle: the local-access model.
Topics: Aspartic Acid; Bacteriorhodopsins; Biophysical Phenomena; Biophysics; Halobacterium salinarum; Hydrogen-Ion Concentration; Kinetics; Light; Models, Chemical; Mutagenesis, Site-Directed; Photochemistry; Protein Conformation; Protons; Retinaldehyde; Schiff Bases; Spectroscopy, Fourier Transform Infrared | 1998 |
Structural investigation of the active site in bacteriorhodopsin: geometric constraints on the roles of Asp-85 and Asp-212 in the proton-pumping mechanism from solid state NMR.
Topics: Anisotropy; Aspartic Acid; Bacteriorhodopsins; Binding Sites; Magnetic Resonance Spectroscopy; Retinaldehyde; Spectroscopy, Fourier Transform Infrared | 2000 |
FTIR analysis of the SII540 intermediate of sensory rhodopsin II: Asp73 is the Schiff base proton acceptor.
Topics: Archaeal Proteins; Aspartic Acid; Bacteriorhodopsins; Carotenoids; Cold Temperature; Halobacterium salinarum; Halorhodopsins; Mutagenesis, Site-Directed; Oxygen; Peptides; Photochemistry; Protein Conformation; Protons; Retinaldehyde; Schiff Bases; Sensory Rhodopsins; Spectroscopy, Fourier Transform Infrared | 2000 |
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 |
Coupling of the reisomerization of the retinal, proton uptake, and reprotonation of Asp-96 in the N photointermediate of bacteriorhodopsin.
Topics: Amino Acid Sequence; Amino Acid Substitution; Aspartic Acid; Bacteriorhodopsins; Binding Sites; Crystallography, X-Ray; Halobacterium salinarum; Hydrogen-Ion Concentration; Kinetics; Light; Models, Molecular; Molecular Conformation; Mutagenesis, Site-Directed; Protein Structure, Secondary; Recombinant Proteins; Retinaldehyde; Spectroscopy, Fourier Transform Infrared; Stereoisomerism | 2001 |
Retinal isomerization in bacteriorhodopsin is controlled by specific chromophore-protein interactions. A study with noncovalent artificial pigments.
Topics: Aspartic Acid; Bacteriorhodopsins; Binding Sites; Circular Dichroism; Halobacterium salinarum; Hydrogen-Ion Concentration; Isomerism; Light; Molecular Structure; Pigments, Biological; Protein Binding; Retinaldehyde; Schiff Bases | 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 |
An opsin mutant with increased thermal stability.
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 |
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 |
Crystallographic structures of the M and N intermediates of bacteriorhodopsin: assembly of a hydrogen-bonded chain of water molecules between Asp-96 and the retinal Schiff base.
Topics: Aspartic Acid; Bacteriorhodopsins; Crystallography, X-Ray; Hydrogen Bonding; Models, Molecular; Point Mutation; Protein Conformation; Retinaldehyde; Schiff Bases; Spectroscopy, Fourier Transform Infrared; Valine; Water | 2003 |
Selectivity of retinal photoisomerization in proteorhodopsin is controlled by aspartic acid 227.
Topics: Amino Acid Substitution; Asparagine; Aspartic Acid; Bacteriorhodopsins; Binding Sites; Darkness; Gammaproteobacteria; Hydrogen-Ion Concentration; Isomerism; Light; Retinaldehyde; Rhodopsin; Rhodopsins, Microbial; Solubility; Spectroscopy, Fourier Transform Infrared; Temperature | 2004 |
Water dynamics simulation as a tool for probing proton transfer pathways in a heptahelical membrane protein.
Topics: Aspartic Acid; Bacteriorhodopsins; Binding Sites; Cell Membrane; Computer Simulation; Cytoplasm; Halobacterium salinarum; Hydrogen Bonding; Hydrogen-Ion Concentration; Light; Membrane Proteins; Models, Chemical; Models, Molecular; Protein Conformation; Proteins; Protons; Retinaldehyde; Schiff Bases; Thermodynamics; Water | 2005 |
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 |
Night blindness and the mechanism of constitutive signaling of mutant G90D rhodopsin.
Topics: Animals; Aspartic Acid; Calcium; Carrier Proteins; cis-trans-Isomerases; Dark Adaptation; Disease Models, Animal; Dose-Response Relationship, Radiation; Eye Proteins; Glycine; Kinetics; Light Signal Transduction; Membrane Potentials; Mice; Mice, Transgenic; Mutation; Night Blindness; Opsins; Photic Stimulation; Retinal Rod Photoreceptor Cells; Retinaldehyde; Rhodopsin; Spectrum Analysis; Time Factors | 2008 |
Structural characteristics around the β-ionone ring of the retinal chromophore in Salinibacter sensory rhodopsin I.
Topics: Aspartic Acid; Bacteroidetes; Hydroxylamine; Norisoprenoids; Retinaldehyde; Sensory Rhodopsins; Signal Transduction; Spectroscopy, Fourier Transform Infrared; Structure-Activity Relationship | 2011 |
Critical role of Asp227 in the photocycle of proteorhodopsin.
Topics: Aspartic Acid; Deuterium Oxide; Hydrogen-Ion Concentration; Isomerism; Models, Molecular; Mutation; Photochemical Processes; Retinaldehyde; Rhodopsin; Rhodopsins, Microbial; Spectrophotometry; Water | 2012 |
Probing a polar cluster in the retinal binding pocket of bacteriorhodopsin by a chemical design approach.
Topics: Adaptation, Ocular; Aspartic Acid; Bacteriorhodopsins; Binding Sites; Biochemistry; Biological Transport; Halobacterium salinarum; Models, Molecular; Mutant Proteins; Protein Denaturation; Protein Stability; Retinaldehyde; Temperature | 2012 |
Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser.
Topics: Aspartic Acid; Bacteriorhodopsins; Ion Transport; Isomerism; Protein Conformation; Retinaldehyde; Schiff Bases; Time Factors; Water; X-Rays | 2018 |