Page last updated: 2024-11-06

prolinal

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

Cross-References

ID SourceID
PubMed CID77372
CHEMBL ID4745604
CHEBI ID178202
MeSH IDM0133536

Synonyms (36)

Synonym
CHEBI:178202
nsc 42516
unii-lo74gwe7wd
lo74gwe7wd ,
einecs 223-175-7
nsc-42516
nsc42516
1-formylpyrrolidine
n-formylpyrrolidine
pyrrolidine-1-carbaldehyde
inchi=1/c5h9no/c7-5-6-3-1-2-4-6/h5h,1-4h
1-pyrrolidinecarboxaldehyde
3760-54-1
1-formylpyrrolidine, 97%
prolinal
AKOS009156885
FT-0635008
pyrrolidine-1-carboxaldehyde
(pyrrolidin-1-yl)methanone
pyrrolidin-1-yl-methanone
1-pyrrolidinecarbaldehyde #
F8884-0102
mfcd00003169
DTXSID40191042
1-pyrrolidinecarboxaldehyde (8ci)(9ci)
1-pyrrolidinecarbaldehyde
AMY24174
Q27283089
D83491
AS-57240
SY252984
chembl4745604 ,
bdbm50546258
CS-0155290
EN300-1265854
Z1255394997
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Drug Classes (1)

ClassDescription
pyrrolidinesAny of a class of heterocyclic amines having a saturated five-membered ring.
[compound class information is derived from Chemical Entities of Biological Interest (ChEBI), Hastings J, Owen G, Dekker A, Ennis M, Kale N, Muthukrishnan V, Turner S, Swainston N, Mendes P, Steinbeck C. (2016). ChEBI in 2016: Improved services and an expanding collection of metabolites. Nucleic Acids Res]

Protein Targets (2)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
Peptidyl-prolyl cis-trans isomerase BHomo sapiens (human)IC50 (µMol)5,000.00000.00880.00950.0103AID1674212
Peptidyl-prolyl cis-trans isomerase A Homo sapiens (human)IC50 (µMol)5,000.00000.00200.14381.5490AID1674211
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (35)

Processvia Protein(s)Taxonomy
chaperone-mediated protein foldingPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
regulation of post-translational protein modificationPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
protein peptidyl-prolyl isomerizationPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
neutrophil chemotaxisPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
positive regulation of multicellular organism growthPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
positive regulation by host of viral processPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
positive regulation by host of viral genome replicationPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
protein stabilizationPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
bone developmentPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
chaperone-mediated protein foldingPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
protein foldingPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
protein peptidyl-prolyl isomerizationPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
negative regulation of protein phosphorylationPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
positive regulation of protein phosphorylationPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
protein foldingPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
negative regulation of protein kinase activityPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
apoptotic processPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
viral release from host cellPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
platelet activationPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
neuron differentiationPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
neutrophil chemotaxisPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
leukocyte chemotaxisPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
activation of protein kinase B activityPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
negative regulation of stress-activated MAPK cascadePeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
lipid droplet organizationPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
cellular response to oxidative stressPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
positive regulation of protein dephosphorylationPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
endothelial cell activationPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
positive regulation of MAPK cascadePeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
regulation of viral genome replicationPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
positive regulation of viral genome replicationPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
positive regulation of protein secretionPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
positive regulation of NF-kappaB transcription factor activityPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
cell adhesion molecule productionPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
negative regulation of protein K48-linked ubiquitinationPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
platelet aggregationPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathwayPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
negative regulation of viral life cyclePeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
regulation of apoptotic signaling pathwayPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (10)

Processvia Protein(s)Taxonomy
collagen bindingPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
RNA bindingPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
peptidyl-prolyl cis-trans isomerase activityPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
protein bindingPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
cyclosporin A bindingPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
unfolded protein bindingPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
RNA polymerase bindingPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
RNA bindingPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
peptidyl-prolyl cis-trans isomerase activityPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
integrin bindingPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
protein bindingPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
cyclosporin A bindingPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
virion bindingPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
unfolded protein bindingPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
heparan sulfate bindingPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (20)

Processvia Protein(s)Taxonomy
nucleusPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
nucleoplasmPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
endoplasmic reticulumPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
endoplasmic reticulum lumenPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
smooth endoplasmic reticulumPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
cytosolPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
focal adhesionPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
membranePeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
melanosomePeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
perinuclear region of cytoplasmPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
extracellular exosomePeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
protein-containing complexPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
endoplasmic reticulum chaperone complexPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
intracellular membrane-bounded organellePeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
cytoplasmPeptidyl-prolyl cis-trans isomerase BHomo sapiens (human)
extracellular regionPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
extracellular spacePeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
nucleusPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
cytoplasmPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
cytosolPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
focal adhesionPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
membranePeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
vesiclePeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
secretory granule lumenPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
extracellular exosomePeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
ficolin-1-rich granule lumenPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
protein-containing complexPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
cytoplasmPeptidyl-prolyl cis-trans isomerase A Homo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (3)

Assay IDTitleYearJournalArticle
AID1674212Inhibition of C-terminal His6-tagged CypB (unknown origin) expressed in Escherichia coli C41(DE3) using Suc-Ala-Ala-Cis-Pro-Phe-pNA as substrate by spectrophotometric analysis2020Journal of medicinal chemistry, 10-22, Volume: 63, Issue:20
Fragment Linking Strategies for Structure-Based Drug Design.
AID1674213Inhibition of C-terminal His6-tagged human CypD K133I mutant expressed in Escherichia coli BL21(DE3) using Suc-Ala-Ala-Cis-Pro-Phe-pNA as substrate by spectrophotometric analysis2020Journal of medicinal chemistry, 10-22, Volume: 63, Issue:20
Fragment Linking Strategies for Structure-Based Drug Design.
AID1674211Inhibition of C-terminal His6-tagged CypA (unknown origin) expressed in Escherichia coli C41(DE3) using Suc-Ala-Ala-Cis-Pro-Phe-pNA as substrate by spectrophotometric analysis2020Journal of medicinal chemistry, 10-22, Volume: 63, Issue:20
Fragment Linking Strategies for Structure-Based Drug Design.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (13)

TimeframeStudies, This Drug (%)All Drugs %
pre-19903 (23.08)18.7374
1990's2 (15.38)18.2507
2000's3 (23.08)29.6817
2010's3 (23.08)24.3611
2020's2 (15.38)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Market Indicators

Research Demand Index: 22.66

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

MetricThis Compound (vs All)
Research Demand Index22.66 (24.57)
Research Supply Index2.64 (2.92)
Research Growth Index4.62 (4.65)
Search Engine Demand Index24.72 (26.88)
Search Engine Supply Index2.83 (0.95)

This Compound (22.66)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials0 (0.00%)5.53%
Reviews1 (7.69%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other12 (92.31%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]