4-nitrophenol and tyrosine

4-nitrophenol has been researched along with tyrosine in 6 studies

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19901 (16.67)18.7374
1990's0 (0.00)18.2507
2000's4 (66.67)29.6817
2010's1 (16.67)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Burgin, AB; Cheng, C; Shuman, S; Woodfield, G1
Choi, EC; Kwon, AR; Yun, HJ1
BISSET, GW1
Bourenkov, GP; Clausen, T; Fitzpatrick, TB; Kitzing, K; Macheroux, P; Sawa, J; Wilken, C1
Alzari, P; Amaya, MF; Buchini, S; Buschiazzo, A; Damager, I; Frasch, AC; Watts, A; Withers, SG1
An, X; Chang, W; Li, H; Li, M; Liu, MC; Liu, MY; Lu, J; Zhang, J1

Other Studies

6 other study(ies) available for 4-nitrophenol and tyrosine

ArticleYear
Vaccinia topoisomerase and Cre recombinase catalyze direct ligation of activated DNA substrates containing a 3'-para-nitrophenyl phosphate ester.
    Nucleic acids research, 2000, Sep-01, Volume: 28, Issue:17

    Topics: Arginine; Base Sequence; Binding Sites; Catalysis; DNA; DNA Topoisomerases, Type I; Esters; Integrases; Molecular Mimicry; Nitrophenols; Oligodeoxyribonucleotides; Organophosphorus Compounds; Substrate Specificity; Tyrosine; Vaccinia virus; Viral Proteins

2000
Kinetic mechanism and identification of the active site tyrosine residue in Enterobacter amnigenus arylsulfate sulfotransferase.
    Biochemical and biophysical research communications, 2001, Jul-13, Volume: 285, Issue:2

    Topics: Amino Acid Substitution; Arylsulfotransferase; Binding Sites; Cloning, Molecular; Enterobacter; Escherichia coli; Feedback; Kinetics; Mutagenesis, Site-Directed; Nitrophenols; Recombinant Proteins; Tyrosine

2001
Effect of tyrosinase preparations on oxytocin, vasopressin and bradykinin.
    British journal of pharmacology and chemotherapy, 1962, Volume: 18

    Topics: Arginine Vasopressin; Ascorbic Acid; Bradykinin; Catechol Oxidase; Kallikreins; Monophenol Monooxygenase; Nitrophenols; Oxidoreductases; Oxytocics; Oxytocin; Phenylalanine; Tyrosine; Vasoconstrictor Agents; Vasopressins

1962
The 1.3 A crystal structure of the flavoprotein YqjM reveals a novel class of Old Yellow Enzymes.
    The Journal of biological chemistry, 2005, Jul-29, Volume: 280, Issue:30

    Topics: Amino Acid Sequence; Arginine; Bacillus subtilis; Benzaldehydes; Binding Sites; Catalysis; Crystallography, X-Ray; Dimerization; Electrons; Escherichia coli; Flavoproteins; Kinetics; Ligands; Models, Molecular; Molecular Sequence Data; Nitrophenols; Open Reading Frames; Oxidative Stress; Oxidoreductases; Phylogeny; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Substrate Specificity; Tyrosine; X-Ray Diffraction

2005
Kinetic and mechanistic analysis of Trypanosoma cruzi trans-sialidase reveals a classical ping-pong mechanism with acid/base catalysis.
    Biochemistry, 2008, Mar-18, Volume: 47, Issue:11

    Topics: Alanine; Animals; Aspartic Acid; Azides; Catalysis; Glycoproteins; Hydrogen-Ion Concentration; Hydrolysis; Kinetics; N-Acetylneuraminic Acid; Neuraminidase; Nitrophenols; Substrate Specificity; Trypanosoma cruzi; Tyrosine

2008
Crystal structures of SULT1A2 and SULT1A1 *3: insights into the substrate inhibition and the role of Tyr149 in SULT1A2.
    Biochemical and biophysical research communications, 2010, May-28, Volume: 396, Issue:2

    Topics: Arylsulfotransferase; Catalysis; Crystallography, X-Ray; Humans; Mutagenesis, Site-Directed; Mutation; Nitrophenols; Phosphoadenosine Phosphosulfate; Protein Conformation; Substrate Specificity; Tyrosine

2010