n-(n-(3-carboxyoxirane-2-carbonyl)leucyl)isoamylamine and n-(3-ethoxycarbonyloxirane-2-carbonyl)-isoleucyl-proline

n-(n-(3-carboxyoxirane-2-carbonyl)leucyl)isoamylamine has been researched along with n-(3-ethoxycarbonyloxirane-2-carbonyl)-isoleucyl-proline in 1 studies

Compound Research Comparison

Studies (n-(n-(3-carboxyoxirane-2-carbonyl)leucyl)isoamylamine)	Trials (n-(n-(3-carboxyoxirane-2-carbonyl)leucyl)isoamylamine)	Recent Studies (post-2010) (n-(n-(3-carboxyoxirane-2-carbonyl)leucyl)isoamylamine)	Studies (n-(3-ethoxycarbonyloxirane-2-carbonyl)-isoleucyl-proline)	Trials (n-(3-ethoxycarbonyloxirane-2-carbonyl)-isoleucyl-proline)	Recent Studies (post-2010) (n-(3-ethoxycarbonyloxirane-2-carbonyl)-isoleucyl-proline)
79	1	16	14	0	3

Protein Interaction Comparison

Protein	Taxonomy	n-(n-(3-carboxyoxirane-2-carbonyl)leucyl)isoamylamine (IC50)	n-(3-ethoxycarbonyloxirane-2-carbonyl)-isoleucyl-proline (IC50)
Cathepsin B	Bos taurus (cattle)		0.12
Cathepsin B	Homo sapiens (human)		0.0023

Research

Studies (1)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Ishida, T; Kitamura, K; Matsumoto, K; Murata, M; Tomoo, K; Watanabe, D; Yamamoto, A	1

Other Studies

1 other study(ies) available for n-(n-(3-carboxyoxirane-2-carbonyl)leucyl)isoamylamine and n-(3-ethoxycarbonyloxirane-2-carbonyl)-isoleucyl-proline

Article	Year
Quantitative evaluation of each catalytic subsite of cathepsin B for inhibitory activity based on inhibitory activity-binding mode relationship of epoxysuccinyl inhibitors by X-ray crystal structure analyses of complexes. Journal of molecular biology, 2006, Oct-06, Volume: 362, Issue:5 Topics: Animals; Binding Sites; Cathepsin B; Cattle; Crystallography, X-Ray; Cysteine Proteinase Inhibitors; Drug Design; Epoxy Compounds; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Inhibitory Concentration 50; Models, Molecular; Molecular Structure; Protein Conformation; Protein Structure, Secondary; Static Electricity; Structure-Activity Relationship; Substrate Specificity; Succinic Acid	2006

Article

Year

Quantitative evaluation of each catalytic subsite of cathepsin B for inhibitory activity based on inhibitory activity-binding mode relationship of epoxysuccinyl inhibitors by X-ray crystal structure analyses of complexes.

Journal of molecular biology, 2006, Oct-06, Volume: 362, Issue:5

Topics: Animals; Binding Sites; Cathepsin B; Cattle; Crystallography, X-Ray; Cysteine Proteinase Inhibitors; Drug Design; Epoxy Compounds; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Inhibitory Concentration 50; Models, Molecular; Molecular Structure; Protein Conformation; Protein Structure, Secondary; Static Electricity; Structure-Activity Relationship; Substrate Specificity; Succinic Acid

2006