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 SourceID
PubMed CID3632
CHEMBL ID143812
SCHEMBL ID7115053
MeSH IDM0357891

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.

ExcerptReferenceRelevance
"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

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
CholinesteraseHomo sapiens (human)Ki0.06000.00001.51739.7300AID1796481
AcetylcholinesteraseMus musculus (house mouse)Ki0.00000.00001.42829.3000AID1800423
AcetylcholinesteraseHomo sapiens (human)IC50 (µMol)0.00030.00000.933210.0000AID243154
AcetylcholinesteraseHomo sapiens (human)Ki0.04000.00001.27869.7300AID1796481; AID1800423
Acetylcholinesterase Bos taurus (cattle)IC50 (µMol)0.00200.00000.61068.7000AID243153; AID272365
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (25)

Processvia Protein(s)Taxonomy
xenobiotic metabolic processCholinesteraseHomo sapiens (human)
learningCholinesteraseHomo sapiens (human)
negative regulation of cell population proliferationCholinesteraseHomo sapiens (human)
neuroblast differentiationCholinesteraseHomo sapiens (human)
peptide hormone processingCholinesteraseHomo sapiens (human)
response to alkaloidCholinesteraseHomo sapiens (human)
cocaine metabolic processCholinesteraseHomo sapiens (human)
negative regulation of synaptic transmissionCholinesteraseHomo sapiens (human)
response to glucocorticoidCholinesteraseHomo sapiens (human)
response to folic acidCholinesteraseHomo sapiens (human)
choline metabolic processCholinesteraseHomo sapiens (human)
acetylcholine catabolic processCholinesteraseHomo sapiens (human)
acetylcholine catabolic process in synaptic cleftAcetylcholinesteraseHomo sapiens (human)
regulation of receptor recyclingAcetylcholinesteraseHomo sapiens (human)
osteoblast developmentAcetylcholinesteraseHomo sapiens (human)
acetylcholine catabolic processAcetylcholinesteraseHomo sapiens (human)
cell adhesionAcetylcholinesteraseHomo sapiens (human)
nervous system developmentAcetylcholinesteraseHomo sapiens (human)
synapse assemblyAcetylcholinesteraseHomo sapiens (human)
receptor internalizationAcetylcholinesteraseHomo sapiens (human)
negative regulation of synaptic transmission, cholinergicAcetylcholinesteraseHomo sapiens (human)
amyloid precursor protein metabolic processAcetylcholinesteraseHomo sapiens (human)
positive regulation of protein secretionAcetylcholinesteraseHomo sapiens (human)
retina development in camera-type eyeAcetylcholinesteraseHomo sapiens (human)
acetylcholine receptor signaling pathwayAcetylcholinesteraseHomo sapiens (human)
positive regulation of cold-induced thermogenesisAcetylcholinesteraseHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (15)

Processvia Protein(s)Taxonomy
amyloid-beta bindingCholinesteraseHomo sapiens (human)
catalytic activityCholinesteraseHomo sapiens (human)
acetylcholinesterase activityCholinesteraseHomo sapiens (human)
cholinesterase activityCholinesteraseHomo sapiens (human)
protein bindingCholinesteraseHomo sapiens (human)
hydrolase activity, acting on ester bondsCholinesteraseHomo sapiens (human)
enzyme bindingCholinesteraseHomo sapiens (human)
choline bindingCholinesteraseHomo sapiens (human)
identical protein bindingCholinesteraseHomo sapiens (human)
amyloid-beta bindingAcetylcholinesteraseHomo sapiens (human)
acetylcholinesterase activityAcetylcholinesteraseHomo sapiens (human)
cholinesterase activityAcetylcholinesteraseHomo sapiens (human)
protein bindingAcetylcholinesteraseHomo sapiens (human)
collagen bindingAcetylcholinesteraseHomo sapiens (human)
hydrolase activityAcetylcholinesteraseHomo sapiens (human)
serine hydrolase activityAcetylcholinesteraseHomo sapiens (human)
acetylcholine bindingAcetylcholinesteraseHomo sapiens (human)
protein homodimerization activityAcetylcholinesteraseHomo sapiens (human)
laminin bindingAcetylcholinesteraseHomo sapiens (human)
amyloid-beta bindingAcetylcholinesterase Bos taurus (cattle)
protein bindingAcetylcholinesterase Bos taurus (cattle)
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (16)

Processvia Protein(s)Taxonomy
extracellular regionCholinesteraseHomo sapiens (human)
nuclear envelope lumenCholinesteraseHomo sapiens (human)
endoplasmic reticulum lumenCholinesteraseHomo sapiens (human)
blood microparticleCholinesteraseHomo sapiens (human)
plasma membraneCholinesteraseHomo sapiens (human)
extracellular spaceCholinesteraseHomo sapiens (human)
extracellular regionAcetylcholinesteraseHomo sapiens (human)
basement membraneAcetylcholinesteraseHomo sapiens (human)
extracellular spaceAcetylcholinesteraseHomo sapiens (human)
nucleusAcetylcholinesteraseHomo sapiens (human)
Golgi apparatusAcetylcholinesteraseHomo sapiens (human)
plasma membraneAcetylcholinesteraseHomo sapiens (human)
cell surfaceAcetylcholinesteraseHomo sapiens (human)
membraneAcetylcholinesteraseHomo sapiens (human)
neuromuscular junctionAcetylcholinesteraseHomo sapiens (human)
synaptic cleftAcetylcholinesteraseHomo sapiens (human)
synapseAcetylcholinesteraseHomo sapiens (human)
perinuclear region of cytoplasmAcetylcholinesteraseHomo sapiens (human)
side of membraneAcetylcholinesteraseHomo sapiens (human)
synapseAcetylcholinesterase Bos taurus (cattle)
side of membraneAcetylcholinesterase Bos taurus (cattle)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (5)

Assay IDTitleYearJournalArticle
AID1796481Enzyme Inhibition Assay from Article 10.1021/jm060257t: \\Discovery of huperzine A-tacrine hybrids as potent inhibitors of human cholinesterases targeting their midgorge recognition sites.\\2006Journal 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.
AID1800423Assay 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.\\2013Biochemistry, 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.
AID243154Inhibitory activity against human erythrocyte acetylcholinesterase2004Journal 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.
AID243153In vitro inhibitory activity against bovine acetylcholinesterase2004Journal 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.
AID272365Inhibition of bovine erythrocyte AChE2006Journal 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)

TimeframeStudies, This Drug (%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's12 (52.17)29.6817
2010's11 (47.83)24.3611
2020's0 (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.

MetricThis Compound (vs All)
Research Demand Index17.64 (24.57)
Research Supply Index3.18 (2.92)
Research Growth Index5.64 (4.65)
Search Engine Demand Index10.37 (26.88)
Search Engine Supply Index2.00 (0.95)

This Compound (17.64)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials0 (0.00%)5.53%
Reviews1 (4.35%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other22 (95.65%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]