203 related articles for article (PubMed ID: 37443832)
1. SHIP1 Is Present but Strongly Downregulated in T-ALL, and after Restoration Suppresses Leukemia Growth in a T-ALL Xenotransplantation Mouse Model.
Ehm P; Rietow R; Wegner W; Bußmann L; Kriegs M; Dierck K; Horn S; Streichert T; Horstmann M; Jücker M
Cells; 2023 Jul; 12(13):. PubMed ID: 37443832
[TBL] [Abstract][Full Text] [Related]
2. SHIP1, but not an AML-derived SHIP1 mutant, suppresses myeloid leukemia growth in a xenotransplantation mouse model.
Täger M; Horn S; Latuske E; Ehm P; Schaks M; Nalaskowski M; Fehse B; Fiedler W; Stocking C; Wellbrock J; Jücker M
Gene Ther; 2017 Nov; 24(11):749-753. PubMed ID: 29143813
[TBL] [Abstract][Full Text] [Related]
3. Leukemia-associated mutations in SHIP1 inhibit its enzymatic activity, interaction with the GM-CSF receptor and Grb2, and its ability to inactivate PI3K/AKT signaling.
Brauer H; Strauss J; Wegner W; Müller-Tidow C; Horstmann M; Jücker M
Cell Signal; 2012 Nov; 24(11):2095-101. PubMed ID: 22820502
[TBL] [Abstract][Full Text] [Related]
4. Reduced expression and activity of patient-derived SHIP1 phosphatase domain mutants.
Ehm P; Nelson N; Giehler S; Schaks M; Bettin B; Kirchmair J; Jücker M
Cell Signal; 2023 Jan; 101():110485. PubMed ID: 36208705
[TBL] [Abstract][Full Text] [Related]
5. Investigation of the function of the PI3-Kinase / AKT signaling pathway for leukemogenesis and therapy of acute childhood lymphoblastic leukemia (ALL).
Ehm P; Grottke A; Bettin B; Jücker M
Cell Signal; 2022 May; 93():110301. PubMed ID: 35259456
[TBL] [Abstract][Full Text] [Related]
6. JAK2-V617F is a negative regulation factor of SHIP1 protein and thus influences the AKT signaling pathway in patients with Myeloproliferative neoplasm (MPN).
Glück M; Dally L; Jücker M; Ehm P
Int J Biochem Cell Biol; 2022 Aug; 149():106229. PubMed ID: 35609769
[TBL] [Abstract][Full Text] [Related]
7. Nuclear accumulation of SHIP1 mutants derived from AML patients leads to increased proliferation of leukemic cells.
Nalaskowski MM; Ehm P; Rehbach C; Nelson N; Täger M; Modest K; Jücker M
Cell Signal; 2018 Sep; 49():87-94. PubMed ID: 29852247
[TBL] [Abstract][Full Text] [Related]
8. The depletion of Circ-PRKDC enhances autophagy and apoptosis in T-cell acute lymphoblastic leukemia via microRNA-653-5p/Reelin mediation of the PI3K/AKT/mTOR signaling pathway.
Ling Z; Fang ZG; Wu JY; Liu JJ
Kaohsiung J Med Sci; 2021 May; 37(5):392-401. PubMed ID: 33615686
[TBL] [Abstract][Full Text] [Related]
9. Activated Src kinases downstream of BCR-ABL and Flt3 induces proteasomal degradation of SHIP1 by phosphorylation of tyrosine 1021.
Ehm P; Bettin B; Jücker M
Biochim Biophys Acta Mol Cell Res; 2023 Jun; 1870(5):119467. PubMed ID: 36958526
[TBL] [Abstract][Full Text] [Related]
10. Dual inhibition of class IA phosphatidylinositol 3-kinase and mammalian target of rapamycin as a new therapeutic option for T-cell acute lymphoblastic leukemia.
Chiarini F; Falà F; Tazzari PL; Ricci F; Astolfi A; Pession A; Pagliaro P; McCubrey JA; Martelli AM
Cancer Res; 2009 Apr; 69(8):3520-8. PubMed ID: 19351820
[TBL] [Abstract][Full Text] [Related]
11. Targeted hyperactivation of AKT through inhibition of ectopic expressed SHIP1 induces cell death in colon carcinoma cells and derived metastases.
Ehm PAH; Linnebacher M; Block A; Rehbach C; Jücker M
Cell Signal; 2023 Aug; 108():110720. PubMed ID: 37207939
[TBL] [Abstract][Full Text] [Related]
12. Human Cytomegalovirus Glycoprotein-Initiated Signaling Mediates the Aberrant Activation of Akt.
Mahmud J; Miller MJ; Altman AM; Chan GC
J Virol; 2020 Jul; 94(16):. PubMed ID: 32493823
[TBL] [Abstract][Full Text] [Related]
13. Harnessing the PI3K/Akt/mTOR pathway in T-cell acute lymphoblastic leukemia: eliminating activity by targeting at different levels.
Bressanin D; Evangelisti C; Ricci F; Tabellini G; Chiarini F; Tazzari PL; Melchionda F; Buontempo F; Pagliaro P; Pession A; McCubrey JA; Martelli AM
Oncotarget; 2012 Aug; 3(8):811-23. PubMed ID: 22885370
[TBL] [Abstract][Full Text] [Related]
14. Tetrandrine and cepharanthine induce apoptosis through caspase cascade regulation, cell cycle arrest, MAPK activation and PI3K/Akt/mTOR signal modification in glucocorticoid resistant human leukemia Jurkat T cells.
Xu W; Wang X; Tu Y; Masaki H; Tanaka S; Onda K; Sugiyama K; Yamada H; Hirano T
Chem Biol Interact; 2019 Sep; 310():108726. PubMed ID: 31255635
[TBL] [Abstract][Full Text] [Related]
15. The SH2 inositol 5-phosphatase Ship1 is recruited in an SH2-dependent manner to the erythropoietin receptor.
Mason JM; Beattie BK; Liu Q; Dumont DJ; Barber DL
J Biol Chem; 2000 Feb; 275(6):4398-406. PubMed ID: 10660611
[TBL] [Abstract][Full Text] [Related]
16. Analysis of the FLVR motif of SHIP1 and its importance for the protein stability of SH2 containing signaling proteins.
Ehm PAH; Lange F; Hentschel C; Jepsen A; Glück M; Nelson N; Bettin B; de Bruyn Kops C; Kirchmair J; Nalaskowski M; Jücker M
Cell Signal; 2019 Nov; 63():109380. PubMed ID: 31377397
[TBL] [Abstract][Full Text] [Related]
17. The role of SHIP1 in T-lymphocyte life and death.
Gloire G; Erneux C; Piette J
Biochem Soc Trans; 2007 Apr; 35(Pt 2):277-80. PubMed ID: 17371259
[TBL] [Abstract][Full Text] [Related]
18. SHIP1 inhibits cell growth, migration, and invasion in non‑small cell lung cancer through the PI3K/AKT pathway.
Fu Q; Huang Y; Ge C; Li Z; Tian H; Li Q; Li H; Li R; Tao X; Xue Y; Wang Y; Yang G; Fang W; Song X
Oncol Rep; 2019 Apr; 41(4):2337-2350. PubMed ID: 30720128
[TBL] [Abstract][Full Text] [Related]
19. SHIP1, an SH2 domain containing polyinositol-5-phosphatase, regulates migration through two critical tyrosine residues and forms a novel signaling complex with DOK1 and CRKL.
Sattler M; Verma S; Pride YB; Salgia R; Rohrschneider LR; Griffin JD
J Biol Chem; 2001 Jan; 276(4):2451-8. PubMed ID: 11031258
[TBL] [Abstract][Full Text] [Related]
20. LINC00665 promotes the viability, migration and invasion of T cell acute lymphoblastic leukemia cells by targeting miR-101 via modulating PI3K/Akt pathway.
Abuduer M; A EZG
Tissue Cell; 2021 Aug; 71():101579. PubMed ID: 34171521
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
