Page last updated: 2024-09-05

sb 203580 and 5-iodotubercidin

sb 203580 has been researched along with 5-iodotubercidin in 2 studies

Compound Research Comparison

Studies (sb 203580)	Trials (sb 203580)	Recent Studies (post-2010) (sb 203580)	Studies (5-iodotubercidin)	Trials (5-iodotubercidin)	Recent Studies (post-2010) (5-iodotubercidin)
3,489	4	1,137	140	0	42

Protein Interaction Comparison

Protein	Taxonomy	5-iodotubercidin (IC50)
Chain A, Mitogen-activated protein kinase 3	Homo sapiens (human)	0.9
Mitogen-activated protein kinase 1	Homo sapiens (human)	1.2
Adenosine kinase	Homo sapiens (human)	0.1583
Adenosine kinase	Mycobacterium tuberculosis H37Rv	1.2
Dual specificity tyrosine-phosphorylation-regulated kinase 1A	Homo sapiens (human)	0.071
Histone-lysine N-methyltransferase, H3 lysine-79 specific	Homo sapiens (human)	7

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	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
Bullock, AN; Fedorov, O; Knapp, S; Marsden, B; Müller, S; Pogacic, V; Rellos, P; Schwaller, J; Sundström, M	1
Coll, JT; Fleming, MA; Ford, PJ; Fox, T; Galullo, V; Germann, UA; Pazhanisamy, S; Porter, MD; Su, MS; Wilson, KP; Xie, X	1

Other Studies

2 other study(ies) available for sb 203580 and 5-iodotubercidin

Article	Year
A systematic interaction map of validated kinase inhibitors with Ser/Thr kinases. Proceedings of the National Academy of Sciences of the United States of America, 2007, Dec-18, Volume: 104, Issue:51 Topics: Amino Acid Sequence; Binding Sites; Clinical Trials as Topic; Drug Evaluation, Preclinical; Enzyme Stability; Humans; Molecular Sequence Data; Phylogeny; Protein Array Analysis; Protein Conformation; Protein Kinase Inhibitors; Protein Serine-Threonine Kinases	2007
A single amino acid substitution makes ERK2 susceptible to pyridinyl imidazole inhibitors of p38 MAP kinase. Protein science : a publication of the Protein Society, 1998, Volume: 7, Issue:11 Topics: Adenosine Triphosphate; Amino Acid Substitution; Animals; Binding Sites; Calcium-Calmodulin-Dependent Protein Kinases; Crystallization; Crystallography, X-Ray; Enzyme Inhibitors; Humans; Hydrogen Bonding; Imidazoles; Mice; Mitogen-Activated Protein Kinase 1; Mitogen-Activated Protein Kinases; Models, Molecular; Mutagenesis; p38 Mitogen-Activated Protein Kinases; Phosphorylation; Pyridines; Structure-Activity Relationship; Tubercidin	1998

Article

Year

A systematic interaction map of validated kinase inhibitors with Ser/Thr kinases.

Proceedings of the National Academy of Sciences of the United States of America, 2007, Dec-18, Volume: 104, Issue:51

Topics: Amino Acid Sequence; Binding Sites; Clinical Trials as Topic; Drug Evaluation, Preclinical; Enzyme Stability; Humans; Molecular Sequence Data; Phylogeny; Protein Array Analysis; Protein Conformation; Protein Kinase Inhibitors; Protein Serine-Threonine Kinases

2007

A single amino acid substitution makes ERK2 susceptible to pyridinyl imidazole inhibitors of p38 MAP kinase.

Protein science : a publication of the Protein Society, 1998, Volume: 7, Issue:11

Topics: Adenosine Triphosphate; Amino Acid Substitution; Animals; Binding Sites; Calcium-Calmodulin-Dependent Protein Kinases; Crystallization; Crystallography, X-Ray; Enzyme Inhibitors; Humans; Hydrogen Bonding; Imidazoles; Mice; Mitogen-Activated Protein Kinase 1; Mitogen-Activated Protein Kinases; Models, Molecular; Mutagenesis; p38 Mitogen-Activated Protein Kinases; Phosphorylation; Pyridines; Structure-Activity Relationship; Tubercidin

1998