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1-naphthylamine and adenosine diphosphate

1-naphthylamine has been researched along with adenosine diphosphate in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Armstrong, S; Merrill, AR	1
Lee, AM; Ross, CT; Singleton, SF; Zeng, BB	1

Other Studies

2 other study(ies) available for 1-naphthylamine and adenosine diphosphate

Article	Year
Toward the elucidation of the catalytic mechanism of the mono-ADP-ribosyltransferase activity of Pseudomonas aeruginosa exotoxin A. Biochemistry, 2004, Jan-13, Volume: 43, Issue:1 Topics: 1-Naphthylamine; Adenosine Diphosphate; Adenosine Diphosphate Ribose; Adenosine Monophosphate; ADP Ribose Transferases; Bacterial Toxins; Binding, Competitive; Catalysis; Enzyme Activation; Exotoxins; Fluorescence Resonance Energy Transfer; Kinetics; Mutagenesis, Site-Directed; NAD; Naphthalimides; Niacinamide; Peptide Elongation Factor 2; Protein Binding; Pseudomonas aeruginosa; Pseudomonas aeruginosa Exotoxin A; Quinolones; Recombinant Proteins; Substrate Specificity; Virulence Factors	2004
A molecular target for suppression of the evolution of antibiotic resistance: inhibition of the Escherichia coli RecA protein by N(6)-(1-naphthyl)-ADP. Journal of medicinal chemistry, 2005, Aug-25, Volume: 48, Issue:17 Topics: 1-Naphthylamine; Adenosine Diphosphate; Adenosine Triphosphate; DNA, Single-Stranded; Drug Resistance, Bacterial; Escherichia coli Proteins; Hydrolysis; Kinetics; Models, Molecular; Protein Binding; Rec A Recombinases; Structure-Activity Relationship	2005

Article

Year

Toward the elucidation of the catalytic mechanism of the mono-ADP-ribosyltransferase activity of Pseudomonas aeruginosa exotoxin A.

Biochemistry, 2004, Jan-13, Volume: 43, Issue:1

Topics: 1-Naphthylamine; Adenosine Diphosphate; Adenosine Diphosphate Ribose; Adenosine Monophosphate; ADP Ribose Transferases; Bacterial Toxins; Binding, Competitive; Catalysis; Enzyme Activation; Exotoxins; Fluorescence Resonance Energy Transfer; Kinetics; Mutagenesis, Site-Directed; NAD; Naphthalimides; Niacinamide; Peptide Elongation Factor 2; Protein Binding; Pseudomonas aeruginosa; Pseudomonas aeruginosa Exotoxin A; Quinolones; Recombinant Proteins; Substrate Specificity; Virulence Factors

2004

A molecular target for suppression of the evolution of antibiotic resistance: inhibition of the Escherichia coli RecA protein by N(6)-(1-naphthyl)-ADP.

Journal of medicinal chemistry, 2005, Aug-25, Volume: 48, Issue:17

Topics: 1-Naphthylamine; Adenosine Diphosphate; Adenosine Triphosphate; DNA, Single-Stranded; Drug Resistance, Bacterial; Escherichia coli Proteins; Hydrolysis; Kinetics; Models, Molecular; Protein Binding; Rec A Recombinases; Structure-Activity Relationship

2005