Page last updated: 2024-09-04

h 256 and h 142

h 256 has been researched along with h 142 in 2 studies

Compound Research Comparison

Studies (h 256)	Trials (h 256)	Recent Studies (post-2010) (h 256)	Studies (h 142)	Trials (h 142)	Recent Studies (post-2010) (h 142)
5	0	1	20	2	0

Protein Interaction Comparison

Protein	Taxonomy	h 256 (IC50)	h 142 (IC50)
Renin	Homo sapiens (human)		0.001
Cathepsin D	Bos taurus (cattle)		0.007

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	1 (50.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Ishchenko, AV; Shakhnovich, EI	1
Atrash, B; Blundell, TL; Cooper, JB; Foundling, SI; Hallett, A; Hemmings, A; Jones, DM; Sibanda, BL; Szelke, M; Watson, FE	1

Other Studies

2 other study(ies) available for h 256 and h 142

Article	Year
SMall Molecule Growth 2001 (SMoG2001): an improved knowledge-based scoring function for protein-ligand interactions. Journal of medicinal chemistry, 2002, Jun-20, Volume: 45, Issue:13 Topics: Carbonic Anhydrases; Computing Methodologies; Databases, Factual; Ligands; Metalloendopeptidases; Metals; Molecular Conformation; Protein Binding; Proteins; Quantitative Structure-Activity Relationship; Statistics as Topic; Thermodynamics	2002
Inhibitors of aspartic proteinases and their relevance to the design of antihypertensive agents. Biochemical Society transactions, 1987, Volume: 15, Issue:4 Topics: Angiotensinogen; Antihypertensive Agents; Aspartic Acid Endopeptidases; Binding Sites; Endopeptidases; Humans; In Vitro Techniques; Models, Molecular; Molecular Conformation; Oligopeptides; Pepsin A; Protease Inhibitors; Renin	1987

Article

Year

SMall Molecule Growth 2001 (SMoG2001): an improved knowledge-based scoring function for protein-ligand interactions.

Journal of medicinal chemistry, 2002, Jun-20, Volume: 45, Issue:13

Topics: Carbonic Anhydrases; Computing Methodologies; Databases, Factual; Ligands; Metalloendopeptidases; Metals; Molecular Conformation; Protein Binding; Proteins; Quantitative Structure-Activity Relationship; Statistics as Topic; Thermodynamics

2002

Inhibitors of aspartic proteinases and their relevance to the design of antihypertensive agents.

Biochemical Society transactions, 1987, Volume: 15, Issue:4

Topics: Angiotensinogen; Antihypertensive Agents; Aspartic Acid Endopeptidases; Binding Sites; Endopeptidases; Humans; In Vitro Techniques; Models, Molecular; Molecular Conformation; Oligopeptides; Pepsin A; Protease Inhibitors; Renin

1987