Compounds > 4-iodine-benzo(b)thiophene-2-carboxamidine
Page last updated: 2024-12-04

4-iodine-benzo(b)thiophene-2-carboxamidine

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 CID1747
CHEMBL ID60088
SCHEMBL ID4312886
MeSH IDM0256031

Synonyms (22)

Synonym
1C5X ,
1C5Q
1C5N
1O5B
apc-6860
b-428
CHEMBL60088 ,
4-iodo-benzo[b]thiophene-2-carboxamidine
4-iodobenzo[b]thiophene-2-carboximidamide
2-amidino-4-iodobenzothiophene
bdbm50098137
SCHEMBL4312886
4-iodo-1-benzothiophene-2-carboximidamide
benzo[b]thiophene-2-carboximidamide, 4-iodo-
154628-42-9
DTXSID40274329
4-iodo benzo(b)thiophene-2-carboxamidine
AKOS030587190
QZT7G76BRK
4-iodanyl-1-benzothiophene-2-carboximidamide
HY-114015
CS-0064880
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Protein Targets (18)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
Chain H, Thrombin heavy chainHomo sapiens (human)Ki6.88330.210076.4417320.0000AID977610
Chain H, Thrombin heavy chainHomo sapiens (human)Ki6.88330.210076.4417320.0000AID977610
Chain A, PROTEIN (TRYPSIN)Bos taurus (cattle)Ki6.88330.210076.4417320.0000AID977610
Chain A, PROTEIN (TRYPSIN)Bos taurus (cattle)Ki6.88330.210076.4417320.0000AID977610
Chain A, PROTEIN (TRYPSIN)Bos taurus (cattle)Ki6.88330.210076.4417320.0000AID977610
Chain A, PROTEIN (TRYPSIN)Bos taurus (cattle)Ki6.88330.210076.4417320.0000AID977610
Chain B, PROTEIN (UROKINASE-TYPE PLASMINOGEN ACTIVATOR)Homo sapiens (human)Ki6.88330.210076.4417320.0000AID977610
Chain B, PROTEIN (UROKINASE-TYPE PLASMINOGEN ACTIVATOR)Homo sapiens (human)Ki6.88330.210076.4417320.0000AID977610
Chain B, PROTEIN (UROKINASE-TYPE PLASMINOGEN ACTIVATOR)Homo sapiens (human)Ki6.88330.210076.4417320.0000AID977610
Chain B, Urokinase-type plasminogen activatorHomo sapiens (human)Ki1.70001.70001.70001.7000AID977610
Chain B, Urokinase-type plasminogen activatorHomo sapiens (human)Ki1.70001.70001.70001.7000AID977610
Chain B, Urokinase-type plasminogen activatorHomo sapiens (human)Ki1.70001.70001.70001.7000AID977610
Chain H, Serine protease hepsinHomo sapiens (human)Ki1.70001.70001.70001.7000AID977610
Chain H, Serine protease hepsinHomo sapiens (human)Ki1.70001.70001.70001.7000AID977610
Chain H, ProthrombinHomo sapiens (human)Ki1.70001.70001.70001.7000AID977610
Coagulation factor IXHomo sapiens (human)Ki0.95000.00022.35479.0000AID459575
Coagulation factor XHomo sapiens (human)Ki22.00000.00000.47089.0000AID459576
Urokinase-type plasminogen activatorHomo sapiens (human)IC50 (µMol)0.21000.03703.385910.0000AID459577
Urokinase-type plasminogen activatorHomo sapiens (human)Ki0.23240.01702.62687.0000AID215662; AID215837; AID215988; AID419413
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (23)

Processvia Protein(s)Taxonomy
proteolysisCoagulation factor IXHomo sapiens (human)
blood coagulationCoagulation factor IXHomo sapiens (human)
zymogen activationCoagulation factor IXHomo sapiens (human)
proteolysisCoagulation factor XHomo sapiens (human)
blood coagulationCoagulation factor XHomo sapiens (human)
positive regulation of cell migrationCoagulation factor XHomo sapiens (human)
positive regulation of TOR signalingCoagulation factor XHomo sapiens (human)
positive regulation of cell migrationUrokinase-type plasminogen activatorHomo sapiens (human)
response to hypoxiaUrokinase-type plasminogen activatorHomo sapiens (human)
proteolysisUrokinase-type plasminogen activatorHomo sapiens (human)
chemotaxisUrokinase-type plasminogen activatorHomo sapiens (human)
signal transductionUrokinase-type plasminogen activatorHomo sapiens (human)
blood coagulationUrokinase-type plasminogen activatorHomo sapiens (human)
regulation of signaling receptor activityUrokinase-type plasminogen activatorHomo sapiens (human)
regulation of plasminogen activationUrokinase-type plasminogen activatorHomo sapiens (human)
negative regulation of plasminogen activationUrokinase-type plasminogen activatorHomo sapiens (human)
smooth muscle cell migrationUrokinase-type plasminogen activatorHomo sapiens (human)
regulation of smooth muscle cell migrationUrokinase-type plasminogen activatorHomo sapiens (human)
regulation of cell adhesionUrokinase-type plasminogen activatorHomo sapiens (human)
plasminogen activationUrokinase-type plasminogen activatorHomo sapiens (human)
regulation of cell adhesion mediated by integrinUrokinase-type plasminogen activatorHomo sapiens (human)
urokinase plasminogen activator signaling pathwayUrokinase-type plasminogen activatorHomo sapiens (human)
regulation of cell population proliferationUrokinase-type plasminogen activatorHomo sapiens (human)
fibrinolysisUrokinase-type plasminogen activatorHomo sapiens (human)
regulation of fibrinolysisUrokinase-type plasminogen activatorHomo sapiens (human)
negative regulation of fibrinolysisUrokinase-type plasminogen activatorHomo sapiens (human)
regulation of wound healingUrokinase-type plasminogen activatorHomo sapiens (human)
regulation of smooth muscle cell-matrix adhesionUrokinase-type plasminogen activatorHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (6)

Processvia Protein(s)Taxonomy
endopeptidase activityCoagulation factor IXHomo sapiens (human)
serine-type endopeptidase activityCoagulation factor IXHomo sapiens (human)
calcium ion bindingCoagulation factor IXHomo sapiens (human)
protein bindingCoagulation factor IXHomo sapiens (human)
metal ion bindingCoagulation factor IXHomo sapiens (human)
serine-type endopeptidase activityCoagulation factor XHomo sapiens (human)
calcium ion bindingCoagulation factor XHomo sapiens (human)
protein bindingCoagulation factor XHomo sapiens (human)
phospholipid bindingCoagulation factor XHomo sapiens (human)
serine-type endopeptidase activityUrokinase-type plasminogen activatorHomo sapiens (human)
protein bindingUrokinase-type plasminogen activatorHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (15)

Processvia Protein(s)Taxonomy
extracellular regionCoagulation factor IXHomo sapiens (human)
extracellular spaceCoagulation factor IXHomo sapiens (human)
endoplasmic reticulum lumenCoagulation factor IXHomo sapiens (human)
Golgi lumenCoagulation factor IXHomo sapiens (human)
plasma membraneCoagulation factor IXHomo sapiens (human)
collagen-containing extracellular matrixCoagulation factor IXHomo sapiens (human)
extracellular exosomeCoagulation factor IXHomo sapiens (human)
extracellular spaceCoagulation factor IXHomo sapiens (human)
extracellular regionCoagulation factor XHomo sapiens (human)
endoplasmic reticulum lumenCoagulation factor XHomo sapiens (human)
Golgi lumenCoagulation factor XHomo sapiens (human)
plasma membraneCoagulation factor XHomo sapiens (human)
external side of plasma membraneCoagulation factor XHomo sapiens (human)
extracellular spaceCoagulation factor XHomo sapiens (human)
extracellular regionUrokinase-type plasminogen activatorHomo sapiens (human)
extracellular spaceUrokinase-type plasminogen activatorHomo sapiens (human)
plasma membraneUrokinase-type plasminogen activatorHomo sapiens (human)
focal adhesionUrokinase-type plasminogen activatorHomo sapiens (human)
external side of plasma membraneUrokinase-type plasminogen activatorHomo sapiens (human)
cell surfaceUrokinase-type plasminogen activatorHomo sapiens (human)
specific granule membraneUrokinase-type plasminogen activatorHomo sapiens (human)
extracellular exosomeUrokinase-type plasminogen activatorHomo sapiens (human)
tertiary granule membraneUrokinase-type plasminogen activatorHomo sapiens (human)
serine protease inhibitor complexUrokinase-type plasminogen activatorHomo sapiens (human)
protein complex involved in cell-matrix adhesionUrokinase-type plasminogen activatorHomo sapiens (human)
serine-type endopeptidase complexUrokinase-type plasminogen activatorHomo sapiens (human)
extracellular spaceUrokinase-type plasminogen activatorHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (12)

Assay IDTitleYearJournalArticle
AID459575Inhibition of human recombinant factor 9a by amidolytic assay2010Journal of medicinal chemistry, Feb-25, Volume: 53, Issue:4
Studies of benzothiophene template as potent factor IXa (FIXa) inhibitors in thrombosis.
AID459577Inhibition of uPA2010Journal of medicinal chemistry, Feb-25, Volume: 53, Issue:4
Studies of benzothiophene template as potent factor IXa (FIXa) inhibitors in thrombosis.
AID419413Inhibition of urokinase2009Journal of medicinal chemistry, May-28, Volume: 52, Issue:10
Large-scale application of high-throughput molecular mechanics with Poisson-Boltzmann surface area for routine physics-based scoring of protein-ligand complexes.
AID215662Inhibition of Human kidney cell urokinase2002Bioorganic & medicinal chemistry letters, Feb-11, Volume: 12, Issue:3
Design and synthesis of 4,5-disubstituted-thiophene-2-amidines as potent urokinase inhibitors.
AID215988Inhibition of urokinase-type plasminogen activator (microPa)2002Bioorganic & medicinal chemistry letters, Aug-05, Volume: 12, Issue:15
4-Aminoarylguanidine and 4-aminobenzamidine derivatives as potent and selective urokinase-type plasminogen activator inhibitors.
AID459576Inhibition of factor 10 by amidolytic assay2010Journal of medicinal chemistry, Feb-25, Volume: 53, Issue:4
Studies of benzothiophene template as potent factor IXa (FIXa) inhibitors in thrombosis.
AID215837In vitro inhibitory activity against Urokinase-type plasminogen activator (microPa)2001Bioorganic & medicinal chemistry letters, Apr-09, Volume: 11, Issue:7
Synthesis of thiophene-2-carboxamidines containing 2-aminothiazoles and their biological evaluation as urokinase inhibitors.
AID1811Experimentally measured binding affinity data derived from PDB2000Chemistry & biology, Apr, Volume: 7, Issue:4
Structural basis for selectivity of a small molecule, S1-binding, submicromolar inhibitor of urokinase-type plasminogen activator.
AID977610Experimentally measured binding affinity data (Ki) for protein-ligand complexes derived from PDB2000Chemistry & biology, Apr, Volume: 7, Issue:4
Structural basis for selectivity of a small molecule, S1-binding, submicromolar inhibitor of urokinase-type plasminogen activator.
AID977610Experimentally measured binding affinity data (Ki) for protein-ligand complexes derived from PDB2004Journal of molecular biology, Nov-19, Volume: 344, Issue:2
Dissecting and designing inhibitor selectivity determinants at the S1 site using an artificial Ala190 protease (Ala190 uPA).
AID1811Experimentally measured binding affinity data derived from PDB2004Journal of molecular biology, Nov-19, Volume: 344, Issue:2
Dissecting and designing inhibitor selectivity determinants at the S1 site using an artificial Ala190 protease (Ala190 uPA).
AID493017Wombat Data for BeliefDocking2002Bioorganic & medicinal chemistry letters, Feb-11, Volume: 12, Issue:3
Design and synthesis of 4,5-disubstituted-thiophene-2-amidines as potent urokinase 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's6 (85.71)29.6817
2010's1 (14.29)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: 12.96

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 Index12.96 (24.57)
Research Supply Index2.08 (2.92)
Research Growth Index5.04 (4.65)
Search Engine Demand Index0.00 (26.88)
Search Engine Supply Index0.00 (0.95)

This Compound (12.96)

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%
Other7 (100.00%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]
SubstanceRelationship StrengthStudiesTrialsClassesRoles
benzamidine
benzamidine: RN given refers to parent cpd. benzamidine : A carboxamidine that is benzene carrying an amidino group.		210benzenes;
carboxamidine		serine protease inhibitor
amiloride
Amiloride: A pyrazine compound inhibiting SODIUM reabsorption through SODIUM CHANNELS in renal EPITHELIAL CELLS. This inhibition creates a negative potential in the luminal membranes of principal cells, located in the distal convoluted tubule and collecting duct. Negative potential reduces secretion of potassium and hydrogen ions. Amiloride is used in conjunction with DIURETICS to spare POTASSIUM loss. (From Gilman et al., Goodman and Gilman's The Pharmacological Basis of Therapeutics, 9th ed, p705). amiloride : A member of the class of pyrazines resulting from the formal monoacylation of guanidine with the carboxy group of 3,5-diamino-6-chloropyrazine-2-carboxylic acid.		2.0510aromatic amine;
guanidines;
organochlorine compound;
pyrazines		diuretic;
sodium channel blocker
2-aminotetralin
2-aminotetralin: RN given refers to parent cpd without isomeric designation; structure		2.0510tetralins
3-carboxy-thioxanthone-10,10-dioxide
[no description available]		2.0510
doxantrazole
doxantrazole: structure		2.0510
1-aminoisoquinoline
[no description available]		2.0510
beta-naphthamidine
beta-naphthamidine: RN given refers to parent cpd		2.0510
benzamidine
[no description available]		2.4120carboxamidinium ion
a-317567
A-317567: acid sensing ion channel blocker; structure in first source		2.0510
ConditionIndicatedRelationship StrengthStudiesTrials