Page last updated: 2024-12-05
huprine x
Description
Research Excerpts
Clinical Trials
Roles
Classes
Pathways
Study Profile
Bioassays
Related Drugs
Related Conditions
Protein Interactions
Research Growth
Market Indicators
Description
huprine X: structure in first source [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]
Cross-References
| ID Source | ID |
|---|---|
| PubMed CID | 3632 |
| CHEMBL ID | 143812 |
| SCHEMBL ID | 7115053 |
| MeSH ID | M0357891 |
Synonyms (9)
| Synonym |
|---|
| NCI60_041180 |
| rac-huprine h7 |
| (1s)-7-chloro-15-ethyl-10-azatetracyclo[11.3.1.0^{2,11}.0^{4,9}]heptadeca-2(11),3,5,7,9,14-hexaen-3-amine |
| 7-chloro-15-ethyl-(1r,13s)-10-azoniatetracyclo[11.3.1.02,11.04,9]heptadeca-2,4,6,8,10,14-hexaen-3-amine |
| chembl143812 , |
| huprine x |
| bdbm10597 |
| SCHEMBL7115053 |
| DTXSID901336714 |
Research Excerpts
Overview
Huprine X (HX) is a synthetic anticholinesterasic compound. exerts a potent inhibitory action on acetylcholinestersase (AChE) It also has an agonist effect on cholinergic receptors.
| Excerpt | Reference | Relevance |
|---|---|---|
| "Huprine X (HX) is a synthetic anticholinesterasic compound that exerts a potent inhibitory action on acetylcholinesterase (AChE) activity, an agonist effect on cholinergic receptors, neuroprotective activity in different neurotoxicity models in vivo and in vitro and cognition enhancing effects in non-transgenic (C57BL/6) and transgenic (3xTg-AD, APPswe) mice. " | ( Huprine X Attenuates The Neurotoxicity Induced by Kainic Acid, Especially Brain Inflammation. Badia, A; Camps, P; Muñoz-Torrero, D; Pérez, B; Relat, J; Victòria Clos, M, 2018) | 3.37 |
| "Huprine X is a novel acetylcholinesterase (AChE) inhibitor, with one of the highest affinities reported for a reversible inhibitor. " | ( 3D structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 A resolution: kinetic and molecular dynamic correlates. Barril, X; Camps, P; Dvir, H; Harel, M; Luque, FJ; Muñoz-Torrero, D; Orozco, M; Rosenberry, TL; Silman, I; Sussman, JL; Wong, DM, 2002) | 1.99 |
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]
Protein Targets (4)
Inhibition Measurements
| Protein | Taxonomy | Measurement | Average | Min (ref.) | Avg (ref.) | Max (ref.) | Bioassay(s) |
|---|---|---|---|---|---|---|---|
| Cholinesterase | Homo sapiens (human) | Ki | 0.0600 | 0.0000 | 1.5173 | 9.7300 | AID1796481 |
| Acetylcholinesterase | Mus musculus (house mouse) | Ki | 0.0000 | 0.0000 | 1.4282 | 9.3000 | AID1800423 |
| Acetylcholinesterase | Homo sapiens (human) | IC50 (µMol) | 0.0003 | 0.0000 | 0.9332 | 10.0000 | AID243154 |
| Acetylcholinesterase | Homo sapiens (human) | Ki | 0.0400 | 0.0000 | 1.2786 | 9.7300 | AID1796481; AID1800423 |
| Acetylcholinesterase | Bos taurus (cattle) | IC50 (µMol) | 0.0020 | 0.0000 | 0.6106 | 8.7000 | AID243153; AID272365 |
| [prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023] | |||||||
Biological Processes (25)
Molecular Functions (15)
Ceullar Components (16)
Bioassays (5)
| Assay ID | Title | Year | Journal | Article |
|---|---|---|---|---|
| AID1796481 | Enzyme Inhibition Assay from Article 10.1021/jm060257t: \\Discovery of huperzine A-tacrine hybrids as potent inhibitors of human cholinesterases targeting their midgorge recognition sites.\\ | 2006 | Journal of medicinal chemistry, Jun-01, Volume: 49, Issue:11 | Discovery of huperzine A-tacrine hybrids as potent inhibitors of human cholinesterases targeting their midgorge recognition sites. |
| AID1800423 | Assay of Substrate Hydrolysis from Article 10.1021/bi401043w: \\The natural product dihydrotanshinone I provides a prototype for uncharged inhibitors that bind specifically to the acetylcholinesterase peripheral site with nanomolar affinity.\\ | 2013 | Biochemistry, Oct-22, Volume: 52, Issue:42 | The natural product dihydrotanshinone I provides a prototype for uncharged inhibitors that bind specifically to the acetylcholinesterase peripheral site with nanomolar affinity. |
| AID243154 | Inhibitory activity against human erythrocyte acetylcholinesterase | 2004 | Journal of medicinal chemistry, Aug-26, Volume: 47, Issue:18 | Modulation of binding strength in several classes of active site inhibitors of acetylcholinesterase studied by comparative binding energy analysis. |
| AID243153 | In vitro inhibitory activity against bovine acetylcholinesterase | 2004 | Journal of medicinal chemistry, Aug-26, Volume: 47, Issue:18 | Modulation of binding strength in several classes of active site inhibitors of acetylcholinesterase studied by comparative binding energy analysis. |
| AID272365 | Inhibition of bovine erythrocyte AChE | 2006 | Journal of medicinal chemistry, Nov-16, Volume: 49, Issue:23 | Binding of 13-amidohuprines to acetylcholinesterase: exploring the ligand-induced conformational change of the gly117-gly118 peptide bond in the oxyanion hole. |
| [information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023] | ||||
Research
Studies (23)
| Timeframe | Studies, This Drug (%) | All Drugs % |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 12 (52.17) | 29.6817 |
| 2010's | 11 (47.83) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| [information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023] | ||
Market Indicators
Research Demand Index: 17.64
According to the monthly volume, diversity, and competition of internet searches for this compound, as well the volume and growth of publications, there is estimated to be moderate demand-to-supply ratio for research on this compound.
| This Compound (17.64) All Compounds (24.57) |
Study Types
| Publication Type | This drug (%) | All Drugs (%) |
|---|---|---|
| Trials | 0 (0.00%) | 5.53% |
| Reviews | 1 (4.35%) | 6.00% |
| Case Studies | 0 (0.00%) | 4.05% |
| Observational | 0 (0.00%) | 0.25% |
| Other | 22 (95.65%) | 84.16% |
| [information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023] | ||