Page last updated: 2024-09-05

sb 203580 and skepinone-l

sb 203580 has been researched along with skepinone-l in 2 studies

Compound Research Comparison

Studies (sb 203580)	Trials (sb 203580)	Recent Studies (post-2010) (sb 203580)	Studies (skepinone-l)	Trials (skepinone-l)	Recent Studies (post-2010) (skepinone-l)
3,489	4	1,137	17	0	16

Protein Interaction Comparison

Protein	Taxonomy	skepinone-l (IC50)
Heat shock protein beta-1	Homo sapiens (human)	0.025
Cholesteryl ester transfer protein	Homo sapiens (human)	0.005
Mitogen-activated protein kinase 11	Homo sapiens (human)	0.0351
Mitogen-activated protein kinase 14	Homo sapiens (human)	0.0091

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	2 (100.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Fischer, S; Grütter, C; Koeberle, SC; Laufer, SA; Rauh, D; Schattel, V; Schollmeyer, D	1
Bauer, SM; Boeckler, FM; Fischer, S; Grütter, C; Koeberle, SC; Laufer, SA; Mayer-Wrangowski, SC; Niess, R; Rauh, D; Storch, K; Wentsch, HK; Zimmermann, M	1

Other Studies

2 other study(ies) available for sb 203580 and skepinone-l

Article	Year
Design, synthesis, and biological evaluation of novel disubstituted dibenzosuberones as highly potent and selective inhibitors of p38 mitogen activated protein kinase. Journal of medicinal chemistry, 2012, Jun-28, Volume: 55, Issue:12 Topics: Chemistry Techniques, Synthetic; Dibenzocycloheptenes; Drug Design; Humans; Hydrophobic and Hydrophilic Interactions; Inhibitory Concentration 50; Kinetics; Models, Molecular; p38 Mitogen-Activated Protein Kinases; Protein Conformation; Protein Kinase Inhibitors; Structure-Activity Relationship; Substrate Specificity	2012
Dibenzosuberones as p38 mitogen-activated protein kinase inhibitors with low ATP competitiveness and outstanding whole blood activity. Journal of medicinal chemistry, 2013, Jan-10, Volume: 56, Issue:1 Topics: Adenosine Triphosphate; Animals; Anti-Inflammatory Agents, Non-Steroidal; Binding Sites; Dibenzocycloheptenes; Hydrophobic and Hydrophilic Interactions; Lipopolysaccharides; Models, Molecular; p38 Mitogen-Activated Protein Kinases; Protein Binding; Solubility; Structure-Activity Relationship; Tumor Necrosis Factor-alpha	2013

Article

Year

Design, synthesis, and biological evaluation of novel disubstituted dibenzosuberones as highly potent and selective inhibitors of p38 mitogen activated protein kinase.

Journal of medicinal chemistry, 2012, Jun-28, Volume: 55, Issue:12

Topics: Chemistry Techniques, Synthetic; Dibenzocycloheptenes; Drug Design; Humans; Hydrophobic and Hydrophilic Interactions; Inhibitory Concentration 50; Kinetics; Models, Molecular; p38 Mitogen-Activated Protein Kinases; Protein Conformation; Protein Kinase Inhibitors; Structure-Activity Relationship; Substrate Specificity

2012

Dibenzosuberones as p38 mitogen-activated protein kinase inhibitors with low ATP competitiveness and outstanding whole blood activity.

Journal of medicinal chemistry, 2013, Jan-10, Volume: 56, Issue:1

Topics: Adenosine Triphosphate; Animals; Anti-Inflammatory Agents, Non-Steroidal; Binding Sites; Dibenzocycloheptenes; Hydrophobic and Hydrophilic Interactions; Lipopolysaccharides; Models, Molecular; p38 Mitogen-Activated Protein Kinases; Protein Binding; Solubility; Structure-Activity Relationship; Tumor Necrosis Factor-alpha

2013