1-naphthylacetylspermine has been researched along with acetazolamide in 1 studies
Studies (1-naphthylacetylspermine) | Trials (1-naphthylacetylspermine) | Recent Studies (post-2010) (1-naphthylacetylspermine) | Studies (acetazolamide) | Trials (acetazolamide) | Recent Studies (post-2010) (acetazolamide) |
---|---|---|---|---|---|
51 | 0 | 22 | 7,604 | 495 | 1,521 |
Protein | Taxonomy | 1-naphthylacetylspermine (IC50) | acetazolamide (IC50) |
---|---|---|---|
Chain A, Class Iii Chitinase Chia1 | Aspergillus fumigatus A1163 | 164 | |
Carbonic anhydrase 12 | Homo sapiens (human) | 0.3178 | |
Renin | Homo sapiens (human) | 8.2 | |
Carbonic anhydrase 1 | Homo sapiens (human) | 2.3173 | |
Carbonic anhydrase 2 | Homo sapiens (human) | 1.2619 | |
Carbonic anhydrase 2 | Bos taurus (cattle) | 0.7 | |
Carbonic anhydrase 3 | Homo sapiens (human) | 1.95 | |
Cathepsin B | Bos taurus (cattle) | 0.02 | |
Steryl-sulfatase | Homo sapiens (human) | 0.025 | |
Carbonic anhydrase 4 | Homo sapiens (human) | 0.1216 | |
Carbonic anhydrase 6 | Homo sapiens (human) | 0.2925 | |
Carbonic anhydrase 5A, mitochondrial | Homo sapiens (human) | 0.1763 | |
Carbonic anhydrase 7 | Homo sapiens (human) | 1.1737 | |
Carbonic anhydrase 9 | Homo sapiens (human) | 0.464 | |
Renin | Macaca mulatta (Rhesus monkey) | 8.2 | |
Carbonic anhydrase 13 | Homo sapiens (human) | 0.23 | |
Carbonic anhydrase 4 | Bos taurus (cattle) | 0.07 | |
Carbonic anhydrase 13 | Mus musculus (house mouse) | 0.77 | |
Carbonic anhydrase 14 | Homo sapiens (human) | 0.183 | |
Carbonic anhydrase 5B, mitochondrial | Homo sapiens (human) | 0.23 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 1 (100.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Carta, F; Innocenti, A; Kaila, K; Scozzafava, A; Supuran, CT; Temperini, C | 1 |
1 other study(ies) available for 1-naphthylacetylspermine and acetazolamide
Article | Year |
---|---|
Polyamines inhibit carbonic anhydrases by anchoring to the zinc-coordinated water molecule.
Topics: Carbonic Anhydrase Inhibitors; Crystallography, X-Ray; Humans; Isoenzymes; Models, Molecular; Polyamines; Spermine; Structure-Activity Relationship; Water; Zinc | 2010 |