ag-1296 and su 5614

ag-1296 has been researched along with su 5614 in 2 studies

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	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Duyster, J; Grundler, R; Miething, C; Peschel, C; Steudel, C; Thiede, C	1
Bagrintseva, K; Eichenlaub, S; Ellwart, JW; Hiddemann, W; Kohl, TM; Schnittger, S; Schwab, R; Spiekermann, K	1

Other Studies

2 other study(ies) available for ag-1296 and su 5614

Article	Year
Sensitivity toward tyrosine kinase inhibitors varies between different activating mutations of the FLT3 receptor. Blood, 2003, Jul-15, Volume: 102, Issue:2 Topics: Acute Disease; Amino Acid Substitution; Animals; Cell Division; Cell Line; Codon; DNA-Binding Proteins; Drug Resistance; Enzyme Activation; Enzyme Inhibitors; fms-Like Tyrosine Kinase 3; Hematopoietic Stem Cells; Humans; Indoles; Leukemia, Myeloid; Membrane Proteins; Mice; Milk Proteins; Mutagenesis, Insertional; Mutation, Missense; Neoplasm Proteins; Phosphorylation; Protein Processing, Post-Translational; Proto-Oncogene Proteins; Receptor Protein-Tyrosine Kinases; Recombinant Proteins; Sequence Deletion; STAT5 Transcription Factor; Staurosporine; Structure-Activity Relationship; Trans-Activators; Transfection; Tyrphostins	2003
Mutations in the tyrosine kinase domain of FLT3 define a new molecular mechanism of acquired drug resistance to PTK inhibitors in FLT3-ITD-transformed hematopoietic cells. Blood, 2004, Mar-15, Volume: 103, Issue:6 Topics: Acute Disease; Animals; Antimetabolites, Antineoplastic; Antineoplastic Agents; Apoptosis; Cell Division; Cell Line, Transformed; Cytarabine; DNA-Binding Proteins; Drug Resistance, Neoplasm; Enzyme Inhibitors; fms-Like Tyrosine Kinase 3; Genistein; Humans; Indoles; Leukemia, Myeloid; MAP Kinase Signaling System; Milk Proteins; Mutagenesis; Phenotype; Phosphorylation; Protein Structure, Tertiary; Proto-Oncogene Proteins; Receptor Protein-Tyrosine Kinases; STAT5 Transcription Factor; Staurosporine; Trans-Activators; Tyrphostins	2004

Article

Year

Sensitivity toward tyrosine kinase inhibitors varies between different activating mutations of the FLT3 receptor.

Blood, 2003, Jul-15, Volume: 102, Issue:2

Topics: Acute Disease; Amino Acid Substitution; Animals; Cell Division; Cell Line; Codon; DNA-Binding Proteins; Drug Resistance; Enzyme Activation; Enzyme Inhibitors; fms-Like Tyrosine Kinase 3; Hematopoietic Stem Cells; Humans; Indoles; Leukemia, Myeloid; Membrane Proteins; Mice; Milk Proteins; Mutagenesis, Insertional; Mutation, Missense; Neoplasm Proteins; Phosphorylation; Protein Processing, Post-Translational; Proto-Oncogene Proteins; Receptor Protein-Tyrosine Kinases; Recombinant Proteins; Sequence Deletion; STAT5 Transcription Factor; Staurosporine; Structure-Activity Relationship; Trans-Activators; Transfection; Tyrphostins

2003

Mutations in the tyrosine kinase domain of FLT3 define a new molecular mechanism of acquired drug resistance to PTK inhibitors in FLT3-ITD-transformed hematopoietic cells.

Blood, 2004, Mar-15, Volume: 103, Issue:6

Topics: Acute Disease; Animals; Antimetabolites, Antineoplastic; Antineoplastic Agents; Apoptosis; Cell Division; Cell Line, Transformed; Cytarabine; DNA-Binding Proteins; Drug Resistance, Neoplasm; Enzyme Inhibitors; fms-Like Tyrosine Kinase 3; Genistein; Humans; Indoles; Leukemia, Myeloid; MAP Kinase Signaling System; Milk Proteins; Mutagenesis; Phenotype; Phosphorylation; Protein Structure, Tertiary; Proto-Oncogene Proteins; Receptor Protein-Tyrosine Kinases; STAT5 Transcription Factor; Staurosporine; Trans-Activators; Tyrphostins

2004