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O-GlcNAcylation of STAT5 controls tyrosine phosphorylation and oncogenic transcription in STAT5-dependent malignancies

Leukemia, 2017-10, Vol.31 (10), p.2132-2142

2017

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c-Kit is required for growth and survival of the cells of origin of Brca1-mutation-associated breast cancer

Oncogene, 2012-02, Vol.31 (7), p.869-883

2012

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Tumor cell resistance against targeted therapeutics: the density of cultured glioma tumor cells enhances Stat3 activity and offers protection against the tyrosine kinase inhibitor canertinib

MedChemComm, 2017-01, Vol.8 (1), p.96-102

2017

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Mammary gland factor (MGF) is a novel member of the cytokine regulated transcription factor gene family and confers the prolactin response

The EMBO journal, 1994-05, Vol.13 (9), p.2182-2191

1994

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Functional interactions between Stat5 and the glucocorticoid receptor

Nature (London), 1996-10, Vol.383 (6602), p.726-728

1996

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Prolactin induces phosphorylation of Tyr694 of Stat5 (MGF), a prerequisite for DNA binding and induction of transcription

The EMBO journal, 1994-09, Vol.13 (18), p.4361-4369

1994

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Peptides As Drugs: Discovery and Development

Peptides as Drugs, 2009, p.1-8

Groner, Bernd

1, 2009

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Cloning and Expression of Stat5 and an Additional Homologue (Stat5b) Involved in Prolactin Signal Transduction in Mouse Mammary Tissue

Proceedings of the National Academy of Sciences - PNAS, 1995-09, Vol.92 (19), p.8831-8835

1995

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p300/CBP is required for transcriptional induction by interleukin-4 and interacts with Stat6

Nucleic acids research, 1999-07, Vol.27 (13), p.2722

1999

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Specific DNA binding of Stat5, but not of glucocorticoid receptor, is required for their functional cooperation in the regulation of gene transcription

Molecular and Cellular Biology, 1997-11, Vol.17 (11), p.6708-6716

1997

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Identification of tyrosine residues within the intracellular domain of the erythropoietin receptor crucial for STAT5 activation

The EMBO journal, 1996-05, Vol.15 (10), p.2434-2441

1996

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Deletion of the carboxyl-terminal transactivation domain of MGF-Stat5 results in sustained DNA binding and a dominant negative phenotype

Molecular and Cellular Biology, 1996-10, Vol.16 (10), p.5691-5700

1996

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Prolactin, growth hormone, erythropoietin and granulocyte‐macrophage colony stimulating factor induce MGF‐Stat5 DNA binding activity

The EMBO journal, 1995-05, Vol.14 (9), p.2005-2013

1995

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The function of Stat3 in tumor cells and their microenvironment

Seminars in cell & developmental biology, 2008-08, Vol.19 (4), p.341-350

2008

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Activation of Stat5 by Interleukin 2 Requires a Carboxyl-Terminal Region of the Interleukin 2 Receptor β Chain but is not Essential for the Proliferative Signal Transmission

Proceedings of the National Academy of Sciences - PNAS, 1995-06, Vol.92 (12), p.5482-5486

1995

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sparing procedure to clear the mouse mammary fat pad of epithelial components for transplantation analysis

Laboratory animals (London), 2008, Vol.42 (1), p.104-110

2008

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Comparative assessment of clinical rating scales in Wilson's disease

BMC neurology, 2017-07, Vol.17 (1), p.140-140, Article 140

2017

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Interactions in the transcriptional regulation exerted by Stat5 and by members of the steroid hormone receptor family

Journal of steroid biochemistry and molecular biology, 1999-04, Vol.69 (1), p.195-204

1999

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Cytotoxic T Lymphocytes with a Grafted Recognition Specificity for ERBB2- Expressing Tumor Cells

Proceedings of the National Academy of Sciences - PNAS, 1994-05, Vol.91 (10), p.4318-4322

1994

Volltextzugriff (PDF)

Tumor cell resistance against targeted therapeutics: the density of cultured glioma tumor cells enhances Stat3 activity and offers protection against the tyrosine kinase inhibitor canertinibThe authors declare no conflict of interest

2017-01

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Interleukin-3, Erythropoietin, and Prolactin Activate a STAT5-like Factor in Lymphoid Cells (∗)

The Journal of biological chemistry, 1995-07, Vol.270 (27), p.15942-15945

1995

Volltextzugriff (PDF)

Tumor cell resistance against targeted therapeutics: the density of cultured glioma tumor cells enhances Stat3 activity and offers protection against the tyrosine kinase inhibitor canertinib† †The authors declare no conflict of interest

MedChemComm, 2016-10, Vol.8 (1), p.96-102

2016

Volltextzugriff (PDF)

The nuclear factor YY1 participates in repression of the beta-casein gene promoter in mammary epithelial cells and is counteracted by mammary gland factor during lactogenic hormone induction

Molecular and Cellular Biology, 1994-01, Vol.14 (1), p.128-137

1994

Volltextzugriff (PDF)

Down-regulation and phosphorylation of glucocorticoid receptors in cultured cells. Investigations with a monospecific antiserum against a bacterially expressed receptor fragment

The Journal of biological chemistry, 1989-08, Vol.264 (24), p.14396-14402

1989

Volltextzugriff (PDF)

Thrombopoietin activates a STAT5‐like factor in hematopoietic cells

The EMBO journal, 1995-06, Vol.14 (12), p.2847-2856

1995

Volltextzugriff (PDF)

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O-GlcNAcylation of STAT5 controls tyrosine phosphorylation and oncogenic transcription in STAT5-dependent malignancies

c-Kit is required for growth and survival of the cells of origin of Brca1-mutation-associated breast cancer

Tumor cell resistance against targeted therapeutics: the density of cultured glioma tumor cells enhances Stat3 activity and offers protection against the tyrosine kinase inhibitor canertinib

Mammary gland factor (MGF) is a novel member of the cytokine regulated transcription factor gene family and confers the prolactin response

Functional interactions between Stat5 and the glucocorticoid receptor

Prolactin induces phosphorylation of Tyr694 of Stat5 (MGF), a prerequisite for DNA binding and induction of transcription

Peptides As Drugs: Discovery and Development

Cloning and Expression of Stat5 and an Additional Homologue (Stat5b) Involved in Prolactin Signal Transduction in Mouse Mammary Tissue

p300/CBP is required for transcriptional induction by interleukin-4 and interacts with Stat6

Specific DNA binding of Stat5, but not of glucocorticoid receptor, is required for their functional cooperation in the regulation of gene transcription

Identification of tyrosine residues within the intracellular domain of the erythropoietin receptor crucial for STAT5 activation

Deletion of the carboxyl-terminal transactivation domain of MGF-Stat5 results in sustained DNA binding and a dominant negative phenotype

Prolactin, growth hormone, erythropoietin and granulocyte‐macrophage colony stimulating factor induce MGF‐Stat5 DNA binding activity

The function of Stat3 in tumor cells and their microenvironment

Activation of Stat5 by Interleukin 2 Requires a Carboxyl-Terminal Region of the Interleukin 2 Receptor β Chain but is not Essential for the Proliferative Signal Transmission

sparing procedure to clear the mouse mammary fat pad of epithelial components for transplantation analysis

Comparative assessment of clinical rating scales in Wilson's disease

Interactions in the transcriptional regulation exerted by Stat5 and by members of the steroid hormone receptor family

Cytotoxic T Lymphocytes with a Grafted Recognition Specificity for ERBB2- Expressing Tumor Cells

Tumor cell resistance against targeted therapeutics: the density of cultured glioma tumor cells enhances Stat3 activity and offers protection against the tyrosine kinase inhibitor canertinibThe authors declare no conflict of interest

Interleukin-3, Erythropoietin, and Prolactin Activate a STAT5-like Factor in Lymphoid Cells (∗)

Tumor cell resistance against targeted therapeutics: the density of cultured glioma tumor cells enhances Stat3 activity and offers protection against the tyrosine kinase inhibitor canertinib† †The authors declare no conflict of interest

The nuclear factor YY1 participates in repression of the beta-casein gene promoter in mammary epithelial cells and is counteracted by mammary gland factor during lactogenic hormone induction

Down-regulation and phosphorylation of glucocorticoid receptors in cultured cells. Investigations with a monospecific antiserum against a bacterially expressed receptor fragment

Thrombopoietin activates a STAT5‐like factor in hematopoietic cells

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