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4-phenyl-1-(1h-1,2,4-triazol-1-yl)-2-butanone

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Description

4-phenyl-1-(1H-1,2,4-triazol-1-yl)-2-butanone: inhibits heme oxidase; structure in first source [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

Cross-References

ID SourceID
PubMed CID25141500
CHEMBL ID1235557
SCHEMBL ID10247229
MeSH IDM0550602

Synonyms (12)

Synonym
4-phenyl-1-(1h-1,2,4-triazol-1-yl)butan-2-one
CHEMBL1235557
bdbm84805
1-azolyl-4-phenyl-2-butanone, 7
SCHEMBL10247229
1092851-29-0
A1-03045
4-phenyl-1-[1,2,4]triazol-1-yl-butan-2-one
1093058-26-4
4-phenyl-1-(1h-1,2,4-triazol-1-yl)-2-butanone
Q27464692
4-phenyl-1-(1,2,4-triazol-1-yl)butan-2-one
[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)
Heme oxygenase 1 Rattus norvegicus (Norway rat)IC50 (µMol)1,259.00001.10004.320010.0000AID1799633
Heme oxygenase 2Rattus norvegicus (Norway rat)IC50 (µMol)850.66671.10004.483310.0000AID1799633; AID764734
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Bioassays (8)

Assay IDTitleYearJournalArticle
AID1353892Inhibition of HO-2 in Sprague-Dawley albino rat brain microsomes assessed as reduction in bilirubin formation using hemin as substrate after 60 mins in presence of NADPH by biliverdin reductase enzyme coupled spectrophotometric assay2018European journal of medicinal chemistry, Mar-25, Volume: 148Potholing of the hydrophobic heme oxygenase-1 western region for the search of potent and selective imidazole-based inhibitors.
AID764734Inhibition of Sprague-Dawley rat brain HO-2 assessed as bilirubin formation after 60 mins by spectrophotometric analysis2013Bioorganic & medicinal chemistry, Sep-01, Volume: 21, Issue:17
Evaluation of novel aryloxyalkyl derivatives of imidazole and 1,2,4-triazole as heme oxygenase-1 (HO-1) inhibitors and their antitumor properties.
AID764735Inhibition of Sprague-Dawley rat spleen microsomal HO-1 assessed as bilirubin formation after 60 mins by spectrophotometric analysis2013Bioorganic & medicinal chemistry, Sep-01, Volume: 21, Issue:17
Evaluation of novel aryloxyalkyl derivatives of imidazole and 1,2,4-triazole as heme oxygenase-1 (HO-1) inhibitors and their antitumor properties.
AID1353891Inhibition of HO-1 in Sprague-Dawley albino rat spleen microsomes assessed as reduction in bilirubin formation using hemin as substrate after 60 mins in presence of NADPH by biliverdin reductase enzyme coupled spectrophotometric assay2018European journal of medicinal chemistry, Mar-25, Volume: 148Potholing of the hydrophobic heme oxygenase-1 western region for the search of potent and selective imidazole-based inhibitors.
AID1353893Selectivity index, ratio of IC50 for HO-2 in Sprague-Dawley albino rat brain microsomes to IC50 for HO-1 in Sprague-Dawley albino rat spleen microsomes2018European journal of medicinal chemistry, Mar-25, Volume: 148Potholing of the hydrophobic heme oxygenase-1 western region for the search of potent and selective imidazole-based inhibitors.
AID1633156Inhibition of HO-2 in Sprague-Dawley rat brain microsomes using NADPH as substrate preincubated for 10 mins followed by substrate addition and measured after 15 mins by GC analysis2019European journal of medicinal chemistry, Apr-01, Volume: 167Progress in the development of selective heme oxygenase-1 inhibitors and their potential therapeutic application.
AID1633155Inhibition of HO-1 in Sprague-Dawley rat spleen microsomes using NADPH as substrate preincubated for 10 mins followed by substrate addition and measured after 15 mins by GC analysis2019European journal of medicinal chemistry, Apr-01, Volume: 167Progress in the development of selective heme oxygenase-1 inhibitors and their potential therapeutic application.
AID1799633Heme Oxygenase from Article 10.1111/j.1747-0285.2009.00909.x: \\Heme oxygenase inhibition by 2-oxy-substituted 1-azolyl-4-phenylbutanes: effect of variation of the azole moiety. X-ray crystal structure of human heme oxygenase-1 in complex with 4-phenyl-1-(2010Chemical biology & drug design, Jan, Volume: 75, Issue:1
Heme oxygenase inhibition by 2-oxy-substituted 1-azolyl-4-phenylbutanes: effect of variation of the azole moiety. X-ray crystal structure of human heme oxygenase-1 in complex with 4-phenyl-1-(1H-1,2,4-triazol-1-yl)-2-butanone.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (5)

TimeframeStudies, This Drug (%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's5 (100.00)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 (%)
Trials0 (0.00%)5.53%
Reviews1 (20.00%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other4 (80.00%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]