Page last updated: 2024-09-05

4-nitrophenyl anthranilate and tyrosine

4-nitrophenyl anthranilate has been researched along with tyrosine in 3 studies

Compound Research Comparison

Studies
(4-nitrophenyl anthranilate)
Trials
(4-nitrophenyl anthranilate)
Recent Studies (post-2010)
(4-nitrophenyl anthranilate)
Studies
(tyrosine)
Trials
(tyrosine)
Recent Studies (post-2010) (tyrosine)
60044,2738468,225

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19902 (66.67)18.7374
1990's0 (0.00)18.2507
2000's1 (33.33)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Birnbaum, ER; Darnall, DW; Hagag, N; McPherson, RA1
Birnbaum, ER; Darnall, DW; Hagag, N1
Banerjee, A; Panda, D; Rahaman, O; Santra, MK1

Other Studies

3 other study(ies) available for 4-nitrophenyl anthranilate and tyrosine

ArticleYear
Anthraniloyl-tyrosine 411 as a spectroscopic probe of fatty acid binding to human serum albumin.
    The Journal of biological chemistry, 1984, May-10, Volume: 259, Issue:9

    Topics: Fatty Acids; Humans; Kinetics; ortho-Aminobenzoates; Palmitic Acid; Palmitic Acids; Protease Inhibitors; Protein Binding; Serum Albumin; Spectrophotometry; Tyrosine

1984
Resonance energy transfer between cysteine-34, tryptophan-214, and tyrosine-411 of human serum albumin.
    Biochemistry, 1983, May-10, Volume: 22, Issue:10

    Topics: Circular Dichroism; Cysteine; Energy Transfer; Humans; Hydrogen-Ion Concentration; Kinetics; ortho-Aminobenzoates; Protease Inhibitors; Protein Conformation; Serum Albumin; Spectrophotometry; Tryptophan; Tyrosine

1983
Unfolding pathways of human serum albumin: evidence for sequential unfolding and folding of its three domains.
    International journal of biological macromolecules, 2005, Dec-15, Volume: 37, Issue:4

    Topics: Circular Dichroism; Cysteine; Fluorescence; Fluorescent Dyes; Humans; Kinetics; Maleimides; ortho-Aminobenzoates; Protein Folding; Protein Structure, Tertiary; Serum Albumin; Tryptophan; Tyrosine

2005