Compounds > 4-aminophenylphosphate
Page last updated: 2024-09-03

4-aminophenylphosphate and cysteine

4-aminophenylphosphate has been researched along with cysteine in 3 studies

Compound Research Comparison

Studies
(4-aminophenylphosphate)		Trials
(4-aminophenylphosphate)		Recent Studies (post-2010)
(4-aminophenylphosphate)		Studies
(cysteine)		Trials
(cysteine)		Recent Studies (post-2010) (cysteine)
7701940,13241811,457

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (33.33)18.2507
2000's2 (66.67)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Bose, SK; Roknabadi, SM; Taneja, V1
Bennett, MS; Guan, Z; Laurberg, M; Su, XD1
Ge, BX; Hu, JH; Kong, L; Sun, L; Yu, MC; Zhuang, ZH1

Other Studies

3 other study(ies) available for 4-aminophenylphosphate and cysteine

ArticleYear
A histidine thiol 100 kDa, tetrameric acid phosphatase from lentil, Lens esculenta, seeds with the characteristics of protein tyrosine phosphatases.
    Biochimica et biophysica acta, 1999, Aug-17, Volume: 1433, Issue:1-2

    Topics: Adenosine Monophosphate; Aniline Compounds; Binding Sites; Chromatography, Liquid; Cysteine; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors; Fabaceae; Histidine; Kinetics; Molecular Weight; Organophosphorus Compounds; Plants, Medicinal; Protein Conformation; Protein Tyrosine Phosphatases; Seeds; Substrate Specificity

1999
Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases.
    Proceedings of the National Academy of Sciences of the United States of America, 2001, Nov-20, Volume: 98, Issue:24

    Topics: Amino Acid Sequence; Aniline Compounds; Animals; Arsenate Reductases; Bacillus subtilis; Binding Sites; Catalysis; Cysteine; Hydrolysis; Models, Molecular; Molecular Sequence Data; Molecular Weight; Organophosphorus Compounds; Oxidation-Reduction; Oxidoreductases; Protein Structure, Secondary; Protein Tyrosine Phosphatases; Sequence Homology, Amino Acid; Substrate Specificity

2001
Molecular identification and functional characterization of a Drosophila dual-specificity phosphatase DMKP-4 which is involved in PGN-induced activation of the JNK pathway.
    Cellular signalling, 2008, Volume: 20, Issue:7

    Topics: Amino Acid Sequence; Aniline Compounds; Animals; Base Sequence; Cell Line; Cysteine; Drosophila melanogaster; Drosophila Proteins; Dual-Specificity Phosphatases; Enzyme Activation; HeLa Cells; Humans; JNK Mitogen-Activated Protein Kinases; Models, Biological; Molecular Sequence Data; Mutation; Organophosphorus Compounds; Phosphorylation; Protein Binding; Protein Structure, Tertiary; Signal Transduction; Transfection

2008