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Journal Articles

Point mutations in the juxtamembrane domain of FLT3 define a new class of activating mutations in AML

Carola Reindl, Ksenia Bagrintseva, Sridhar Vempati, Susanne Schnittger, Joachim W. Ellwart, Katja Wenig, Karl-Peter Hopfner, Wolfgang Hiddemann, Karsten Spiekermann

Blood (2006) 107 (9): 3700–3707.

https://doi.org/10.1182/blood-2005-06-2596

Published: 2006

Journal Articles

Point Mutations Found in the Juxtamembrane Domain of FLT3 Define a New Class of Activating Mutations in AML.

Carola Reindl, Ksenia Bagrintseva, Susanne Schnittger, Joachim W. Ellwart, Katja Wenig, Karl-Peter Hopfner, Wolfgang Hiddemann, Karsten Spiekermann

Blood (2005) 106 (11): 4388.

https://doi.org/10.1182/blood.V106.11.4388.4388

Published: 2005

Journal Articles

FLT3-ITD-TKD dual mutants associated with AML confer resistance to FLT3 PTK inhibitors and cytotoxic agents by overexpression of Bcl-x(L)

Ksenia Bagrintseva, Stefanie Geisenhof, Ruth Kern, Sabine Eichenlaub, Carola Reindl, Joachim W. Ellwart, Wolfgang Hiddemann, Karsten Spiekermann

Blood (2005) 105 (9): 3679–3685.

https://doi.org/10.1182/blood-2004-06-2459

Published: 2005

Journal Articles

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

Ksenia Bagrintseva, Ruth Schwab, Tobias M. Kohl, Susanne Schnittger, Sabine Eichenlaub, Joachim W. Ellwart, Wolfgang Hiddemann, Karsten Spiekermann

Blood (2004) 103 (6): 2266–2275.

https://doi.org/10.1182/blood-2003-05-1653

Published: 2004

Journal Articles

The protein tyrosine kinase inhibitor SU5614 inhibits FLT3 and induces growth arrest and apoptosis in AML-derived cell lines expressing a constitutively activated FLT3

Karsten Spiekermann, Ralf J. Dirschinger, Ruth Schwab, Ksenia Bagrintseva, Florian Faber, Christian Buske, Susanne Schnittger, Louise M. Kelly, D. Gary Gilliland, Wolfgang Hiddemann

Blood (2003) 101 (4): 1494–1504.

https://doi.org/10.1182/blood-2002-04-1045

Published: 2003

Journal Articles

A new and recurrent activating length mutation in exon 20 of the FLT3 gene in acute myeloid leukemia

Karsten Spiekermann, Ksenia Bagrintseva, Claudia Schoch, Torsten Haferlach, Wolfgang Hiddemann, Susanne Schnittger

Blood (2002) 100 (9): 3423–3425.

https://doi.org/10.1182/blood-2002-03-0953

Published: 2002

NARROW

Point mutations in the juxtamembrane domain of FLT3 define a new class of activating mutations in AML

Point Mutations Found in the Juxtamembrane Domain of FLT3 Define a New Class of Activating Mutations in AML.

FLT3-ITD-TKD dual mutants associated with AML confer resistance to FLT3 PTK inhibitors and cytotoxic agents by overexpression of Bcl-x(L)

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

The protein tyrosine kinase inhibitor SU5614 inhibits FLT3 and induces growth arrest and apoptosis in AML-derived cell lines expressing a constitutively activated FLT3

A new and recurrent activating length mutation in exon 20 of the FLT3 gene in acute myeloid leukemia

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ASH Publications

American Society of Hematology

Point mutations in the juxtamembrane domain of FLT3 define a new class of activating mutations in AML

Point Mutations Found in the Juxtamembrane Domain of FLT3 Define a New Class of Activating Mutations in AML.

FLT3-ITD-TKD dual mutants associated with AML confer resistance to FLT3 PTK inhibitors and cytotoxic agents by overexpression of Bcl-x(L)

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

The protein tyrosine kinase inhibitor SU5614 inhibits FLT3 and induces growth arrest and apoptosis in AML-derived cell lines expressing a constitutively activated FLT3

A new and recurrent activating length mutation in exon 20 of the FLT3 gene in acute myeloid leukemia

Email alerts

ASH Publications

American Society of Hematology

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