Page last updated: 2024-11-12

tolserine

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

Description

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

Cross-References

ID SourceID
PubMed CID9928397
CHEMBL ID130458
SCHEMBL ID8920175
MeSH IDM0368037

Synonyms (8)

Synonym
2-methylphenserine
tolserine.tartaric acid
tolserine
(3as,8ar)-1,3a,8-trimethyl-1h,2h,3h,3ah,8h,8ah-pyrrolo[2,3-b]indol-5-yl n-(2-methylphenyl)carbamate
bdbm10959
CHEMBL130458
SCHEMBL8920175
[(3ar,8bs)-3,4,8b-trimethyl-2,3a-dihydro-1h-pyrrolo[2,3-b]indol-7-yl] n-(2-methylphenyl)carbamate

Research Excerpts

Overview

Tolserine proved to be a highly potent inhibitor of human AChE compared to its structural analogues physostigmine and phenserine.

ExcerptReferenceRelevance
"Tolserine proved to be a highly potent inhibitor of human AChE compared to its structural analogues physostigmine and phenserine."( Kinetics of human acetylcholinesterase inhibition by the novel experimental Alzheimer therapeutic agent, tolserine.
Al-Jafari, AA; Alhomida, AS; Greig, NH; Kamal, MA, 2000
)
1.24
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Protein Targets (2)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
CholinesteraseHomo sapiens (human)IC50 (µMol)1.17400.00001.559910.0000AID1796572; AID1796574; AID1916842
AcetylcholinesteraseHomo sapiens (human)IC50 (µMol)0.49880.00000.933210.0000AID1796572; AID1796574; AID1916841; AID262754; AID31501; AID511766
[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 (11)

Assay IDTitleYearJournalArticle
AID511766Inhibition of human AChE by Ellmans test2010Journal of medicinal chemistry, Sep-09, Volume: 53, Issue:17
Novel carbamates as orally active acetylcholinesterase inhibitors found to improve scopolamine-induced cognition impairment: pharmacophore-based virtual screening, synthesis, and pharmacology.
AID262756Selectivity for AChE over BChE2006Journal of medicinal chemistry, Apr-06, Volume: 49, Issue:7
Inhibition of human acetyl- and butyrylcholinesterase by novel carbamates of (-)- and (+)-tetrahydrofurobenzofuran and methanobenzodioxepine.
AID1916842Inhibition of human plasma BChE using S-butyrylthiocholine as substrate by enzymatic assay2022European journal of medicinal chemistry, Oct-05, Volume: 240Recent advance on carbamate-based cholinesterase inhibitors as potential multifunctional agents against Alzheimer's disease.
AID44293In vitro inhibition of human plasma butyrylcholinesterase.2001Journal of medicinal chemistry, Nov-22, Volume: 44, Issue:24
Methyl analogues of the experimental Alzheimer drug phenserine: synthesis and structure/activity relationships for acetyl- and butyrylcholinesterase inhibitory action.
AID262754Anticholinesterase activity against human erythrocyte AChE2006Journal of medicinal chemistry, Apr-06, Volume: 49, Issue:7
Inhibition of human acetyl- and butyrylcholinesterase by novel carbamates of (-)- and (+)-tetrahydrofurobenzofuran and methanobenzodioxepine.
AID262755Anticholinesterase activity against human plasma BChE2006Journal of medicinal chemistry, Apr-06, Volume: 49, Issue:7
Inhibition of human acetyl- and butyrylcholinesterase by novel carbamates of (-)- and (+)-tetrahydrofurobenzofuran and methanobenzodioxepine.
AID1916843Selectivity index, ratio of IC50 for human plasma BChE to IC50 for human erythrocyte AChE2022European journal of medicinal chemistry, Oct-05, Volume: 240Recent advance on carbamate-based cholinesterase inhibitors as potential multifunctional agents against Alzheimer's disease.
AID31501In vitro inhibition of human erythrocyte acetylcholinesterase.2001Journal of medicinal chemistry, Nov-22, Volume: 44, Issue:24
Methyl analogues of the experimental Alzheimer drug phenserine: synthesis and structure/activity relationships for acetyl- and butyrylcholinesterase inhibitory action.
AID1916841Inhibition of human erythrocyte AChE using acetyl-(beta-methyl)thiocholine as substrate by enzymatic assay2022European journal of medicinal chemistry, Oct-05, Volume: 240Recent advance on carbamate-based cholinesterase inhibitors as potential multifunctional agents against Alzheimer's disease.
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.
AID1796574Cholinesterase Inhibition Assay from Article 10.1021/jm010080x: \\Methyl analogues of the experimental Alzheimer drug phenserine: synthesis and structure/activity relationships for acetyl- and butyrylcholinesterase inhibitory action.\\2001Journal of medicinal chemistry, Nov-22, Volume: 44, Issue:24
Methyl analogues of the experimental Alzheimer drug phenserine: synthesis and structure/activity relationships for acetyl- and butyrylcholinesterase inhibitory action.
[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's4 (57.14)29.6817
2010's2 (28.57)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%
Reviews1 (14.29%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other6 (85.71%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]