lapachol has been researched along with plumbagin in 5 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (20.00) | 18.2507 |
| 2000's | 1 (20.00) | 29.6817 |
| 2010's | 3 (60.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Abdeen, S; Chapman, E; Chitre, S; Hoang, QQ; Johnson, SM; Park, Y; Ray, AM; Salim, N; Sivinski, J; Stevens, M; Washburn, A | 1 |
| Danilenko, NV; Karpenko, AS; Khlebnikov, AI; Kirpotina, LN; Levandovskiy, IA; Quinn, MT; Schepetkin, IA; Shibinska, MO | 1 |
| Chatterjee, I; Kiema, G; McDermott, MT; Rothery, RA; Weiner, JH | 1 |
| de Vries, S; Heering, HA | 1 |
| Bao, JL; Chen, XP; Huang, MQ; Lu, JJ; Wang, YT; Wu, GS; Xu, WS | 1 |
1 review(s) available for lapachol and plumbagin
| Article | Year |
|---|---|
Quinones derived from plant secondary metabolites as anti-cancer agents.
Topics: Anthraquinones; Antineoplastic Agents, Phytogenic; Benzoquinones; Cell Line, Tumor; Cell Survival; Humans; Naphthoquinones; Neoplasms; Plant Extracts | 2013 |
4 other study(ies) available for lapachol and plumbagin
| Article | Year |
|---|---|
HSP60/10 chaperonin systems are inhibited by a variety of approved drugs, natural products, and known bioactive molecules.
Topics: Biological Products; Chaperonin 10; Chaperonin 60; Escherichia coli; Humans; Inhibitory Concentration 50; Protein Folding; Rafoxanide; Salicylanilides; Suramin | 2019 |
Synthesis, anticancer activity, and molecular modeling of 1,4-naphthoquinones that inhibit MKK7 and Cdc25.
Topics: Antineoplastic Agents; cdc25 Phosphatases; Cell Line, Tumor; Cell Survival; Enzyme Inhibitors; Humans; MAP Kinase Kinase 7; Models, Molecular; Molecular Docking Simulation; Naphthoquinones | 2019 |
Hydroxylated naphthoquinones as substrates for Escherichia coli anaerobic reductases.
Topics: Anaerobiosis; Binding Sites; Electrochemistry; Electron Transport Complex IV; Enzyme Inhibitors; Escherichia coli; Hydroxyquinolines; Kinetics; Molecular Structure; Naphthoquinones; Oxidoreductases; Spectrophotometry; Substrate Specificity | 1998 |
NO reductase from Bacillus azotoformans is a bifunctional enzyme accepting electrons from menaquinol and a specific endogenous membrane-bound cytochrome c551.
Topics: Amino Acid Sequence; Bacillus; Bacterial Proteins; Cytochrome c Group; Electrochemistry; Electron Transport; Intracellular Membranes; Kinetics; Membrane Proteins; Molecular Sequence Data; Multienzyme Complexes; Naphthoquinones; Nitric Oxide; Oxidation-Reduction; Oxidoreductases; Protein Subunits | 2004 |