Page last updated: 2024-11-11

phenethylcymserine

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

Description

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

Cross-References

ID SourceID
PubMed CID9804733
CHEMBL ID1080386
MeSH IDM0578866

Synonyms (6)

Synonym
bdbm50312803
3alpha,8-dimethyl-1-phenethyl-1,2,3,3alpha,8,8alpha-hexahydropyrrolo[2,3-b]indol-5-yl 4-isopropylphenylcarbamate
(3as,8ar)-3a,8-dimethyl-1-phenethyl-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indol-5-yl 4-isopropylphenylcarbamate
phenethylcymserine
CHEMBL1080386 ,
[(3ar,8bs)-4,8b-dimethyl-3-(2-phenylethyl)-2,3a-dihydro-1h-pyrrolo[2,3-b]indol-7-yl] n-(4-propan-2-ylphenyl)carbamate
[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)IC50 (µMol)0.00600.00001.559910.0000AID1916836
AcetylcholinesteraseMus musculus (house mouse)IC50 (µMol)100.00000.00071.11818.4000AID464986; AID465031
AcetylcholinesteraseHomo sapiens (human)IC50 (µMol)22.50150.00000.933210.0000AID1916835; AID600978; AID600980
CholinesteraseMus musculus (house mouse)IC50 (µMol)0.54000.00910.56021.9920AID464987; AID465032
[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 (15)

Assay IDTitleYearJournalArticle
AID600981Inhibition of human plasma BChE2011European journal of medicinal chemistry, Jun, Volume: 46, Issue:6
Quinolizidinyl derivatives of bi- and tricyclic systems as potent inhibitors of acetyl- and butyrylcholinesterase with potential in Alzheimer's disease.
AID600980Inhibition of human erythrocytes BChE2011European journal of medicinal chemistry, Jun, Volume: 46, Issue:6
Quinolizidinyl derivatives of bi- and tricyclic systems as potent inhibitors of acetyl- and butyrylcholinesterase with potential in Alzheimer's disease.
AID1916835Inhibition of AChE (unknown origin)2022European journal of medicinal chemistry, Oct-05, Volume: 240Recent advance on carbamate-based cholinesterase inhibitors as potential multifunctional agents against Alzheimer's disease.
AID464988Selectivity ratio of IC50 for mouse serum BChE over IC50 for mouse brain AChE2010Bioorganic & medicinal chemistry letters, Mar-01, Volume: 20, Issue:5
Design, synthesis, evaluation and QSAR analysis of N(1)-substituted norcymserine derivatives as selective butyrylcholinesterase inhibitors.
AID1470884In-vivo inhibition of BuChE in Harlan-Wistar rat brain assessed as increase in acetylcholine level at 1.25 mg/kg, ip by microdialysis method relative to control2017European journal of medicinal chemistry, May-26, Volume: 132Recent progress in the identification of selective butyrylcholinesterase inhibitors for Alzheimer's disease.
AID465033Selectivity ratio of IC50 for mouse serum BChE over IC50 for mouse brain AChE2010Bioorganic & medicinal chemistry letters, Mar-01, Volume: 20, Issue:5
Design, synthesis and evaluation of carbamate-modified (-)-N(1)-phenethylnorphysostigmine derivatives as selective butyrylcholinesterase inhibitors.
AID600979Inhibition of human plasma AChE2011European journal of medicinal chemistry, Jun, Volume: 46, Issue:6
Quinolizidinyl derivatives of bi- and tricyclic systems as potent inhibitors of acetyl- and butyrylcholinesterase with potential in Alzheimer's disease.
AID1916838Selectivity index, ratio of IC50 for AChE (unknown origin) to BChE (unknown origin)2022European journal of medicinal chemistry, Oct-05, Volume: 240Recent advance on carbamate-based cholinesterase inhibitors as potential multifunctional agents against Alzheimer's disease.
AID1470885In-vivo inhibition of BuChE in Harlan-Wistar rat brain assessed as increase in acetylcholine level at 2.5 mg/kg, ip by microdialysis method relative to control2017European journal of medicinal chemistry, May-26, Volume: 132Recent progress in the identification of selective butyrylcholinesterase inhibitors for Alzheimer's disease.
AID465032Inhibition of mouse serum BChE after 1 hr by modified Ellman's colorimetric method2010Bioorganic & medicinal chemistry letters, Mar-01, Volume: 20, Issue:5
Design, synthesis and evaluation of carbamate-modified (-)-N(1)-phenethylnorphysostigmine derivatives as selective butyrylcholinesterase inhibitors.
AID464987Inhibition of mouse serum BChE after 1 hr by modified Ellman's colorimetric method2010Bioorganic & medicinal chemistry letters, Mar-01, Volume: 20, Issue:5
Design, synthesis, evaluation and QSAR analysis of N(1)-substituted norcymserine derivatives as selective butyrylcholinesterase inhibitors.
AID464986Inhibition of mouse brain AChE after 1 hr by modified Ellman's colorimetric method2010Bioorganic & medicinal chemistry letters, Mar-01, Volume: 20, Issue:5
Design, synthesis, evaluation and QSAR analysis of N(1)-substituted norcymserine derivatives as selective butyrylcholinesterase inhibitors.
AID600978Inhibition of human erythrocytes AChE2011European journal of medicinal chemistry, Jun, Volume: 46, Issue:6
Quinolizidinyl derivatives of bi- and tricyclic systems as potent inhibitors of acetyl- and butyrylcholinesterase with potential in Alzheimer's disease.
AID1916836Inhibition of BChE (unknown origin)2022European journal of medicinal chemistry, Oct-05, Volume: 240Recent advance on carbamate-based cholinesterase inhibitors as potential multifunctional agents against Alzheimer's disease.
AID465031Inhibition of mouse brain AChE after 1 hr by modified Ellman's colorimetric method2010Bioorganic & medicinal chemistry letters, Mar-01, Volume: 20, Issue:5
Design, synthesis and evaluation of carbamate-modified (-)-N(1)-phenethylnorphysostigmine derivatives as selective butyrylcholinesterase inhibitors.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (7)

TimeframeStudies, This Drug (%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's6 (85.71)24.3611
2020's1 (14.29)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 (%)
Trials0 (0.00%)5.53%
Reviews2 (28.57%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other5 (71.43%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]