4-aminobenzoic acid and benzyloxycarbonylleucyl-leucyl-leucine aldehyde

4-aminobenzoic acid has been researched along with benzyloxycarbonylleucyl-leucyl-leucine aldehyde in 1 studies

Research

Studies (1)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Arulpragasam, A; Butcher, NJ; Minchin, RF	1

Other Studies

1 other study(ies) available for 4-aminobenzoic acid and benzyloxycarbonylleucyl-leucyl-leucine aldehyde

Article	Year
Proteasomal degradation of N-acetyltransferase 1 is prevented by acetylation of the active site cysteine: a mechanism for the slow acetylator phenotype and substrate-dependent down-regulation. The Journal of biological chemistry, 2004, May-21, Volume: 279, Issue:21 Topics: 4-Aminobenzoic Acid; Alleles; Arylamine N-Acetyltransferase; Binding Sites; Blotting, Western; Cell Line, Tumor; Cloning, Molecular; Cycloheximide; Cysteine; Cysteine Endopeptidases; Cysteine Proteinase Inhibitors; DNA, Complementary; Down-Regulation; Escherichia coli; Genotype; Glutathione Transferase; Humans; Isoenzymes; Leukocytes, Mononuclear; Leupeptins; Models, Biological; Multienzyme Complexes; Mutagenesis, Site-Directed; Mutation; Oxidative Stress; Peptide Hydrolases; Phenotype; Precipitin Tests; Proteasome Endopeptidase Complex; Protein Binding; Protein Synthesis Inhibitors; Recombinant Proteins; Time Factors; Ubiquitin	2004

Article

Year

Proteasomal degradation of N-acetyltransferase 1 is prevented by acetylation of the active site cysteine: a mechanism for the slow acetylator phenotype and substrate-dependent down-regulation.

The Journal of biological chemistry, 2004, May-21, Volume: 279, Issue:21

Topics: 4-Aminobenzoic Acid; Alleles; Arylamine N-Acetyltransferase; Binding Sites; Blotting, Western; Cell Line, Tumor; Cloning, Molecular; Cycloheximide; Cysteine; Cysteine Endopeptidases; Cysteine Proteinase Inhibitors; DNA, Complementary; Down-Regulation; Escherichia coli; Genotype; Glutathione Transferase; Humans; Isoenzymes; Leukocytes, Mononuclear; Leupeptins; Models, Biological; Multienzyme Complexes; Mutagenesis, Site-Directed; Mutation; Oxidative Stress; Peptide Hydrolases; Phenotype; Precipitin Tests; Proteasome Endopeptidase Complex; Protein Binding; Protein Synthesis Inhibitors; Recombinant Proteins; Time Factors; Ubiquitin

2004