asparagine has been researched along with retinaldehyde in 12 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (8.33) | 18.7374 |
| 1990's | 6 (50.00) | 18.2507 |
| 2000's | 4 (33.33) | 29.6817 |
| 2010's | 1 (8.33) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Betlach, MC; Kliger, DS; Miercke, LJ; Milder, SJ; Shand, RF; Stroud, RM; Thorgeirsson, TE | 1 |
| Nathans, J | 1 |
| Maeda, A | 1 |
| Beck, M; Fahmy, K; Jäger, F; Sakmar, TP; Siebert, F; Zvyaga, TA | 1 |
| Balashov, S; Ebrey, T; Govindjee, R; Oesterhelt, D; Sheves, M; Steinberg, G | 1 |
| Brown, LS; Dioumaev, AK; Lanyi, JK; Needleman, R | 2 |
| Kamo, N; Kandori, H; Shichida, Y; Shimono, K | 1 |
| Gross, AK; Oprian, DD; Xie, G | 1 |
| Balashov, SP; Dioumaev, AK; Imasheva, ES; Lanyi, JK; Wang, JM | 1 |
| Brown, LS; Fan, Y; Furutani, Y; Kandori, H; Shi, L; Sumii, M; Waschuk, SA | 1 |
| Ding, J; Huang, W; Ma, D; Wang, Y; Wu, J; Zhao, Y | 1 |
12 other study(ies) available for asparagine and retinaldehyde
| Article | Year |
|---|---|
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 |
[Mechanism of energy conversion in retinal proteins].
Topics: Asparagine; Bacteriorhodopsins; Energy Transfer; Protons; Retinaldehyde; 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 |
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.
Topics: Amino Acid Sequence; Asparagine; Bacteriorhodopsins; Halobacterium; Hydrogen-Ion Concentration; Kinetics; Light; Point Mutation; Retinaldehyde; Schiff Bases; Spectrophotometry; Tyrosine | 1994 |
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 |
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 |
Interaction of Asn105 with the retinal chromophore during photoisomerization of pharaonis phoborhodopsin.
Topics: Amino Acid Substitution; Archaeal Proteins; Asparagine; Binding Sites; Carotenoids; Escherichia coli; Halobacterium salinarum; Halorhodopsins; Mutagenesis, Site-Directed; Recombinant Proteins; Retinaldehyde; Sensory Rhodopsins; Spectrophotometry, Infrared | 2002 |
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 |
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 |
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 |
Effects of mutations of Lys41 and Asp102 of bacteriorhodopsin.
Topics: Amino Acid Sequence; Asparagine; Bacteriorhodopsins; Halobacterium salinarum; Hydrogen-Ion Concentration; Kinetics; Light; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Proton Pumps; Retinaldehyde | 2011 |