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International Journal of Molecular Sciences|July 29, 2025
The Inositol-5-Phosphatase SHIP1: Expression, Regulation and Role in Acute Lymphoblastic LeukemiaPatrick Ehm, Manfred Jücker
Biochimica Et Biophysica Acta. Molecular Cell Research|March 23, 2023
Activated Src kinases downstream of BCR-ABL and Flt3 induces proteasomal degradation of SHIP1 by phosphorylation of tyrosine 1021Patrick Ehm, Bettina Bettin, Manfred Jücker
The International Journal of Biochemistry & Cell Biology|May 24, 2022
JAK2-V617F is a negative regulation factor of SHIP1 protein and thus influences the AKT signaling pathway in patients with Myeloproliferative neoplasm (MPN)Madeleine Glück, Lina Dally, Manfred Jücker, et al.
Nucleus (Austin, Tex.)|February 28, 2015
The tumor suppressor SHIP1 colocalizes in nucleolar cavities with p53 and components of PML nuclear bodiesPatrick Ehm, Marcus M Nalaskowski, Torsten Wundenberg, et al.
Analytical Biochemistry|June 16, 2012
A toolkit for graded expression of green fluorescent protein fusion proteins in mammalian cellsMarcus M Nalaskowski, Patrick Ehm, Susanne Giehler, et al.
Biochimie|March 18, 2014
Efficacious inhibition of Importin α/β-mediated nuclear import of human inositol phosphate multikinaseInga Kublun, Patrick Ehm, Maria A Brehm, et al.
Cellular Signalling|October 8, 2022
Reduced expression and activity of patient-derived SHIP1 phosphatase domain mutantsPatrick Ehm, Nina Nelson, Susanne Giehler, et al.
Cellular Signalling|June 1, 2018
Nuclear accumulation of SHIP1 mutants derived from AML patients leads to increased proliferation of leukemic cellsMarcus M Nalaskowski, Patrick Ehm, Christoph Rehbach, et al.
Biological Chemistry|June 22, 2012
Nucleocytoplasmic shuttling of human inositol phosphate multikinase is influenced by CK2 phosphorylationRüdiger Meyer, Marcus M Nalaskowski, Patrick Ehm, et al.
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