n-acetylhistidine has been researched along with tryptophan in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 2 (40.00) | 18.7374 |
1990's | 1 (20.00) | 18.2507 |
2000's | 1 (20.00) | 29.6817 |
2010's | 1 (20.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Muszkat, KA; Wismontski-Knittel, T | 1 |
Endo, Y | 1 |
Barkley, MD; Chen, Y | 1 |
Nagaraj, RH; Staniszewska, MM | 1 |
Ivanov, KL; Pravdivtsev, AN; Vieth, HM; Yurkovskaya, AV | 1 |
5 other study(ies) available for n-acetylhistidine and tryptophan
Article | Year |
---|---|
Reactivities of tyrosine, histidine, tryptophan, and methionine in radical pair formation in flavin triplet induced protein nuclear magnetic polarization.
Topics: Flavins; Histidine; Kinetics; Magnetic Resonance Spectroscopy; Methionine; Oligopeptides; Photolysis; Proteins; Tryptophan; Tyrosine | 1985 |
In vivo deacetylation of N-acetyl amino acids by kidney acylases in mice and rats. A possible role of acylase system in mammalian kidneys.
Topics: Aging; Amidohydrolases; Animals; Histidine; Kidney; Kinetics; Liver; Mice; Rats; Tissue Distribution; Tryptophan | 1980 |
Toward understanding tryptophan fluorescence in proteins.
Topics: Acetylcysteine; Energy Transfer; Fluorescence Polarization; Glycine; Histidine; Photolysis; Proteins; Protons; Skatole; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Tryptophan | 1998 |
3-hydroxykynurenine-mediated modification of human lens proteins: structure determination of a major modification using a monoclonal antibody.
Topics: Acetylcysteine; Antibodies, Monoclonal; Antigens; Arginine; Binding, Competitive; Blotting, Western; Cell Membrane; Chromatography, High Pressure Liquid; Cross-Linking Reagents; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Histidine; Humans; Immunohistochemistry; Kynurenine; Lens, Crystalline; Lysine; Magnetic Resonance Spectroscopy; Models, Chemical; Ninhydrin; Oxygen; Protein Conformation; Spectrophotometry; Time Factors; Tryptophan; Water | 2005 |
Importance of polarization transfer in reaction products for interpreting and analyzing CIDNP at low magnetic fields.
Topics: Amino Acids; Electromagnetic Fields; Histidine; Indicators and Reagents; Lasers; Magnetic Resonance Spectroscopy; Spin Labels; Tryptophan; Tyrosine | 2015 |