Page last updated: 2024-11-11

ganstigmine

Description Research Excerpts Clinical Trials Roles Classes Pathways Study Profile Bioassays Related Drugs Related Conditions Protein Interactions Research Growth

Description

ganstigmine: structure in first source [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

Cross-References

ID SourceID
PubMed CID9823294
CHEMBL ID121810
MeSH IDM0414809

Synonyms (14)

Synonym
ganstigmine
2-ethylphenylgeneserine oxazine
bdbm10970
(4as,9as)-2,4a,9-trimethyl-2h,3h,4h,4ah,9h,9ah-indolo[3,2-e][1,2]oxazin-6-yl n-(2-ethylphenyl)carbamate
CHEMBL121810
unii-qrr9sv89xi
ganstigmine [inn]
457075-21-7
qrr9sv89xi ,
(4as,9as)-2,3,4,4a,9,9a-hexahydro-2,4a,9-trimethyl-1,2-oxazino(6,5-b)indol-6-yl o-ethylcarbanilate
DTXSID30196607
DB06525
Q27287464
[(4as,9as)-2,4a,9-trimethyl-4,9a-dihydro-3h-oxazino[6,5-b]indol-6-yl] n-(2-ethylphenyl)carbamate

Research Excerpts

Overview

Ganstigmine (CHF2819) is an orally active, geneserine derived, carbamate-based acetylcholinesterase inhibitor developed for the treatment of Alzheimer's disease.

ExcerptReferenceRelevance
"Ganstigmine (CHF2819) is an acetylcholinesterase inhibitor that increases acetylcholine in rat hippocampus and ameliorates scopolamine-induced amnesia. "( Ganstigmine and donepezil improve neurodegeneration in AD11 antinerve growth factor transgenic mice.
Capsoni, S; Cattaneo, A; De Rosa, R; Garcia, AA; Giannotta, S; Imbimbo, BP; Pietra, C; Stebel, M; Villetti, G,
)
3.02
"Ganstigmine is an orally active, geneserine derived, carbamate-based acetylcholinesterase inhibitor developed for the treatment of Alzheimer's disease. "( Structural determinants of Torpedo californica acetylcholinesterase inhibition by the novel and orally active carbamate based anti-alzheimer drug ganstigmine (CHF-2819).
Amari, G; Bartolucci, C; Bolzoni, PT; Delcanale, M; Ghidini, E; Lamba, D; Racchi, M; Siotto, M; Villetti, G, 2006
)
1.98
"Ganstigmine (CHF2819) is a novel, orally active acetylcholinesterase inhibitor that induces a stimulation of brain cholinergic transmission. "( Neurochemical and neurobehavioral effects of ganstigmine (CHF2819), a novel acetylcholinesterase inhibitor, in rat prefrontal cortex: an in vivo study.
Amoroso, S; Cassano, T; Castrignanò, S; Colaianna, M; Cuomo, V; Giustino, A; Steardo, L; Trabace, L, 2007
)
2.04

Dosage Studied

ExcerptRelevanceReference
" Ganstigmine, a novel cholinesterase inhibitor, was well tolerated within a dosing range of 5 to 10 mg."( First clinical evaluation of ganstigmine in patients with probable Alzheimer's disease.
Fabbri, L; Frackiewicz, EJ; Jhee, SS; Monici, P; Moran, S; Piccinno, A; Shiovitz, T; Tan, EY; Zarotsky, V,
)
1.33
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Protein Targets (3)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
AcetylcholinesteraseTetronarce californica (Pacific electric ray)IC50 (µMol)5.12000.00570.42855.1200AID404434
CholinesteraseHomo sapiens (human)IC50 (µMol)0.18750.00001.559910.0000AID1796572
AcetylcholinesteraseHomo sapiens (human)IC50 (µMol)0.14670.00000.933210.0000AID1796572; AID31163
[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)
[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)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (5)

Assay IDTitleYearJournalArticle
AID404434Inhibition of Torpedo californica AChE2008Journal of medicinal chemistry, Jun-12, Volume: 51, Issue:11
Exploiting protein fluctuations at the active-site gorge of human cholinesterases: further optimization of the design strategy to develop extremely potent inhibitors.
AID234643Selectivity at AChE and BChE2002Journal of medicinal chemistry, Aug-15, Volume: 45, Issue:17
Anticholinesterase activity of compounds related to geneserine tautomers. N-Oxides and 1,2-oxazines.
AID44285Ex vivo inhibition of human plasma Butyrylcholinesterase.2002Journal of medicinal chemistry, Aug-15, Volume: 45, Issue:17
Anticholinesterase activity of compounds related to geneserine tautomers. N-Oxides and 1,2-oxazines.
AID31163Ex vivo inhibition of human erythrocyte Acetylcholinesterase.2002Journal of medicinal chemistry, Aug-15, Volume: 45, Issue:17
Anticholinesterase activity of compounds related to geneserine tautomers. N-Oxides and 1,2-oxazines.
AID1796572Cholinesterase Inhibition Assay from Article 10.1021/jm010491d: \\Anticholinesterase activity of compounds related to geneserine tautomers. N-Oxides and 1,2-oxazines.\\2002Journal of medicinal chemistry, Aug-15, Volume: 45, Issue:17
Anticholinesterase activity of compounds related to geneserine tautomers. N-Oxides and 1,2-oxazines.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (10)

TimeframeStudies, This Drug (%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's10 (100.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials1 (8.33%)5.53%
Reviews2 (16.67%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other9 (75.00%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]