Page last updated: 2024-11-12

s-benzyl phenylmethanethiosulfinate

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

Description

S-benzyl phenylmethanethiosulfinate: an antioxidant; structure in first source [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

Cross-References

ID SourceID
PubMed CID10244468
CHEMBL ID1224167
SCHEMBL ID10391146
MeSH IDM0522614

Synonyms (13)

Synonym
s-benzyl phenylmethanesulfinothioate
CHEMBL1224167 ,
benzenemethanesulfinothioic acid, s-(phenylmethyl) ester
benzylsulfinylsulfanylmethylbenzene
petivericin
s-benzyl phenylmethanethiosulfinate
bdbm50325648
16302-98-0
SCHEMBL10391146
DTXSID90437280
phenylmethanethiosulfinic acid s-benzyl ester
SY359041
mfcd00443820
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Pathways (1)

PathwayProteinsCompounds
(Z)-phenylmethanethial S-oxide biosynthesis18
(Z)-phenylmethanethial S-oxide biosynthesis09

Protein Targets (3)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
Procathepsin LHomo sapiens (human)Ki31.70000.00001.10139.3000AID502278
Cathepsin BHomo sapiens (human)Ki7.80000.00001.21808.6000AID502276
Cysteine protease Trypanosoma brucei rhodesienseKi2.31000.03502.55175.3100AID502282
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (25)

Processvia Protein(s)Taxonomy
adaptive immune responseProcathepsin LHomo sapiens (human)
proteolysisProcathepsin LHomo sapiens (human)
protein autoprocessingProcathepsin LHomo sapiens (human)
fusion of virus membrane with host plasma membraneProcathepsin LHomo sapiens (human)
receptor-mediated endocytosis of virus by host cellProcathepsin LHomo sapiens (human)
antigen processing and presentationProcathepsin LHomo sapiens (human)
antigen processing and presentation of exogenous peptide antigen via MHC class IIProcathepsin LHomo sapiens (human)
collagen catabolic processProcathepsin LHomo sapiens (human)
zymogen activationProcathepsin LHomo sapiens (human)
enkephalin processingProcathepsin LHomo sapiens (human)
fusion of virus membrane with host endosome membraneProcathepsin LHomo sapiens (human)
CD4-positive, alpha-beta T cell lineage commitmentProcathepsin LHomo sapiens (human)
symbiont entry into host cellProcathepsin LHomo sapiens (human)
antigen processing and presentation of peptide antigenProcathepsin LHomo sapiens (human)
proteolysis involved in protein catabolic processProcathepsin LHomo sapiens (human)
elastin catabolic processProcathepsin LHomo sapiens (human)
macrophage apoptotic processProcathepsin LHomo sapiens (human)
cellular response to thyroid hormone stimulusProcathepsin LHomo sapiens (human)
positive regulation of apoptotic signaling pathwayProcathepsin LHomo sapiens (human)
positive regulation of peptidase activityProcathepsin LHomo sapiens (human)
immune responseProcathepsin LHomo sapiens (human)
proteolysisCathepsin BHomo sapiens (human)
thyroid hormone generationCathepsin BHomo sapiens (human)
collagen catabolic processCathepsin BHomo sapiens (human)
epithelial cell differentiationCathepsin BHomo sapiens (human)
regulation of apoptotic processCathepsin BHomo sapiens (human)
decidualizationCathepsin BHomo sapiens (human)
symbiont entry into host cellCathepsin BHomo sapiens (human)
proteolysis involved in protein catabolic processCathepsin BHomo sapiens (human)
cellular response to thyroid hormone stimulusCathepsin BHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (10)

Processvia Protein(s)Taxonomy
fibronectin bindingProcathepsin LHomo sapiens (human)
cysteine-type endopeptidase activityProcathepsin LHomo sapiens (human)
protein bindingProcathepsin LHomo sapiens (human)
collagen bindingProcathepsin LHomo sapiens (human)
cysteine-type peptidase activityProcathepsin LHomo sapiens (human)
histone bindingProcathepsin LHomo sapiens (human)
proteoglycan bindingProcathepsin LHomo sapiens (human)
serpin family protein bindingProcathepsin LHomo sapiens (human)
cysteine-type endopeptidase activator activity involved in apoptotic processProcathepsin LHomo sapiens (human)
cysteine-type endopeptidase activityCathepsin BHomo sapiens (human)
protein bindingCathepsin BHomo sapiens (human)
collagen bindingCathepsin BHomo sapiens (human)
peptidase activityCathepsin BHomo sapiens (human)
cysteine-type peptidase activityCathepsin BHomo sapiens (human)
proteoglycan bindingCathepsin BHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (20)

Processvia Protein(s)Taxonomy
extracellular regionProcathepsin LHomo sapiens (human)
extracellular spaceProcathepsin LHomo sapiens (human)
nucleusProcathepsin LHomo sapiens (human)
lysosomeProcathepsin LHomo sapiens (human)
multivesicular bodyProcathepsin LHomo sapiens (human)
Golgi apparatusProcathepsin LHomo sapiens (human)
plasma membraneProcathepsin LHomo sapiens (human)
apical plasma membraneProcathepsin LHomo sapiens (human)
endolysosome lumenProcathepsin LHomo sapiens (human)
chromaffin granuleProcathepsin LHomo sapiens (human)
lysosomal lumenProcathepsin LHomo sapiens (human)
intracellular membrane-bounded organelleProcathepsin LHomo sapiens (human)
collagen-containing extracellular matrixProcathepsin LHomo sapiens (human)
extracellular exosomeProcathepsin LHomo sapiens (human)
endocytic vesicle lumenProcathepsin LHomo sapiens (human)
extracellular spaceProcathepsin LHomo sapiens (human)
lysosomeProcathepsin LHomo sapiens (human)
collagen-containing extracellular matrixCathepsin BHomo sapiens (human)
extracellular regionCathepsin BHomo sapiens (human)
extracellular spaceCathepsin BHomo sapiens (human)
lysosomeCathepsin BHomo sapiens (human)
external side of plasma membraneCathepsin BHomo sapiens (human)
apical plasma membraneCathepsin BHomo sapiens (human)
endolysosome lumenCathepsin BHomo sapiens (human)
melanosomeCathepsin BHomo sapiens (human)
perinuclear region of cytoplasmCathepsin BHomo sapiens (human)
collagen-containing extracellular matrixCathepsin BHomo sapiens (human)
extracellular exosomeCathepsin BHomo sapiens (human)
peptidase inhibitor complexCathepsin BHomo sapiens (human)
ficolin-1-rich granule lumenCathepsin BHomo sapiens (human)
extracellular spaceCathepsin BHomo sapiens (human)
lysosomeCathepsin BHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (8)

Assay IDTitleYearJournalArticle
AID502276Inhibition of cathepsin B2010Bioorganic & medicinal chemistry letters, Sep-15, Volume: 20, Issue:18
Allicin and derivates are cysteine protease inhibitors with antiparasitic activity.
AID502287Time dependent inhibition of Trypanosoma brucei rhodesiense rhodesain by Dixon plot analysis2010Bioorganic & medicinal chemistry letters, Sep-15, Volume: 20, Issue:18
Allicin and derivates are cysteine protease inhibitors with antiparasitic activity.
AID502278Inhibition of cathepsin L2010Bioorganic & medicinal chemistry letters, Sep-15, Volume: 20, Issue:18
Allicin and derivates are cysteine protease inhibitors with antiparasitic activity.
AID502284Antiparasitic activity against Trypanosoma brucei brucei2010Bioorganic & medicinal chemistry letters, Sep-15, Volume: 20, Issue:18
Allicin and derivates are cysteine protease inhibitors with antiparasitic activity.
AID502283Antiparasitic activity against Plasmodium falciparum2010Bioorganic & medicinal chemistry letters, Sep-15, Volume: 20, Issue:18
Allicin and derivates are cysteine protease inhibitors with antiparasitic activity.
AID502281Inhibition of Plasmodium falciparum falcipain-22010Bioorganic & medicinal chemistry letters, Sep-15, Volume: 20, Issue:18
Allicin and derivates are cysteine protease inhibitors with antiparasitic activity.
AID502286Time dependent inhibition of Plasmodium falciparum falcipain-2 by Dixon plot analysis2010Bioorganic & medicinal chemistry letters, Sep-15, Volume: 20, Issue:18
Allicin and derivates are cysteine protease inhibitors with antiparasitic activity.
AID502282Inhibition of Trypanosoma brucei rhodesiense rhodesain2010Bioorganic & medicinal chemistry letters, Sep-15, Volume: 20, Issue:18
Allicin and derivates are cysteine protease inhibitors with antiparasitic activity.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (6)

TimeframeStudies, This Drug (%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's3 (50.00)29.6817
2010's3 (50.00)24.3611
2020's0 (0.00)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Market Indicators

Research Demand Index: 12.43

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 weak demand-to-supply ratio for research on this compound.

MetricThis Compound (vs All)
Research Demand Index12.43 (24.57)
Research Supply Index1.95 (2.92)
Research Growth Index4.37 (4.65)
Search Engine Demand Index0.00 (26.88)
Search Engine Supply Index0.00 (0.95)

This Compound (12.43)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials0 (0.00%)5.53%
Reviews0 (0.00%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other6 (100.00%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]