SHIP is a negative regulator of growth factor receptor-mediated PKB/Akt activation and myeloid cell survival

The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate

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Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα

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Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN

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PI3K: Downstream AKTion Blocks Apoptosis

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Mechanisms and consequences of activation of protein kinase B/Akt

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The lipid phosphatase activity of PTEN is critical for its tumor supressor function

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Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase

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Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases

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Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor FeγRIIB

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Cell suicide for beginners

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Regulating GLUT4 vesicle dynamics by phosphoinositide kinases and phosphoinositide phosphatases

Shisheva, A. (2003) · Frontiers in bioscience · doi:10.2741/1101 · Cited by 27

Akt and SHP-1 are DC-intrinsic checkpoints for tumor immunity

Carmi, Y., Prestwood, T. R., Spitzer, M. H., Linde, I. L., Chabon, J. R., Reticker-Flynn, N. E., Bhattacharya, N., Zhang, H., Zhang, X., Basto, P. A., et al. (2016) · JCI Insight · doi:10.1172/jci.insight.89020 · Cited by 27

SHIP2, a factor associated with diet-induced obesity and insulin sensitivity, attenuates FGF signaling in vivo

Jurynec, M. J., & Grunwald, D. J. (2010) · Disease Models & Mechanisms · doi:10.1242/dmm.000703 · Cited by 26

Loss of the Nf1 Tumor Suppressor Gene Decreases Fas Antigen Expression in Myeloid Cells

Hiatt, K. K., Ingram, D. A., Huddleston, H. M., Spandau, D. F., Kapur, R., & Clapp, D. W. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63233-6 · Cited by 26

Stoichiometric Quantification of Akt Phosphorylation Using LC-MS/MS

Atrih, A., Turnock, D., Sellar, G. C., Thompson, A., Feuerstein, G., Ferguson, M. A. J., & Huang, J. T.-J. (2009) · Journal of Proteome Research · doi:10.1021/pr900572h · Cited by 25

A Key Role for the Phosphorylation of Ser440 by the Cyclic AMP-dependent Protein Kinase in Regulating the Activity of the Src Homology 2 Domain-containing Inositol 5′-Phosphatase (SHIP1)

Zhang, J., Ravichandran, K. S., & Garrison, J. C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.128827 · Cited by 25

Regulation of Hematopoietic Cell Development and Function Through Phosphoinositides

Elich, M., & Sauer, K. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00931 · Cited by 24

The inositol 5-phosphatase SHIP is expressed as 145 and 135 kDa proteins in blood and bone marrow cells in vivo, whereas carboxyl-truncated forms of SHIP are generated by proteolytic cleavage in vitro

Horn, S., Meyer, J., Heukeshoven, J., Fehse, B., Schulze, C., Li, S., Frey, J., Poll, S. N., Stocking, C., & Jücker, M. (2001) · Leukemia · doi:10.1038/sj.leu.2401990 · Cited by 24

Therapeutic potential of targeting mTOR in T-cell acute lymphoblastic leukemia (Review)

Evangelisti, C., Evangelisti, C., Chiarini, F., Lonetti, A., Buontempo, F., Bressanin, D., Cappellini, A., Orsini, E., McCubrey, J. A., & Martelli, A. M. (2014) · International Journal of Oncology · doi:10.3892/ijo.2014.2525 · Cited by 26

Combination of ginsenoside Rb1 and Rd protects the retina against bright light-induced degeneration

Bian, M., Du, X., Wang, P., Cui, J., Xu, J., Gu, J., Zhang, T., & Chen, Y. (2017) · Scientific Reports · doi:10.1038/s41598-017-06471-x · Cited by 23

PTEN and SHIP: Impact on lymphatic metastasis in breast cancer

Li, X., Li, K., Li, G., & Sun, L. (2018) · Journal of Cancer Research and Therapeutics · doi:10.4103/0973-1482.193894 · Cited by 23

The Shc-binding site of the βc subunit of the GM-CSF/IL-3/IL-5 receptors is a negative regulator of hematopoiesis

Ramshaw, H. S., Guthridge, M. A., Stomski, F. C., Barry, E. F., Ooms, L. M., Mitchell, C. A., Begley, C. G., & Lopez, A. F. (2007) · Blood · doi:10.1182/blood-2007-01-070391 · Cited by 23

The SH2 Domains of Inositol Polyphosphate 5-Phosphatases SHIP1 and SHIP2 Have Similar Ligand Specificity but Different Binding Kinetics

Zhang, Y., Wavreille, A., Kunys, A. R., & Pei, D. (2009) · Biochemistry · doi:10.1021/bi9012462 · Cited by 23

SHIP-1 deficiency in the myeloid compartment is insufficient to induce myeloid expansion or chronic inflammation

Maxwell, M. J., Srivastava, N., Park, M. Y., Tsantikos, E., Engelman, R. W., Kerr, W. G., & Hibbs, M. L. (2014) · Genes and Immunity · doi:10.1038/gene.2014.9 · Cited by 22

SHIP2 controls PtdIns(3,4,5)P3 levels and PKB activity in response to oxidative stress

Zhang, J., Liu, Z., Rasschaert, J., Bléro, D., Deneubourg, L., Schurmans, S., Erneux, C., & Pesesse, X. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.06.022 · Cited by 22

Effects of overexpression of the SH2-containing inositol phosphatase SHIP on proliferation and apoptosis of erythroid AS-E2 cells

Boer, A. J. M. D. J.-D., Drayer, A. L., & Vellenga, E. (2001) · Leukemia · doi:10.1038/sj.leu.2402261 · Cited by 22

Integrin-αIIbβ3-mediated outside-in signalling activates a negative feedback pathway to suppress platelet activation

Dai, B., Wu, P., Xue, F., Yang, R., Yu, Z., Dai, K., Ruan, C., Liu, G., Newman, P. J., & Gao, C. (2016) · Thrombosis and Haemostasis · doi:10.1160/th16-02-0096 · Cited by 21

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. A. H., Schaks, M., Nalaskowski, M. M., Fehse, B., Fiedler, W., Stocking, C., Wellbrock, J., et al. (2017) · Gene Therapy · doi:10.1038/gt.2017.88 · Cited by 21

Multiorgan failure with abnormal receptor metabolism in mice mimicking Samd9/9L syndromes

Nagamachi, A., Kanai, A., Nakamura, M., Okuda, H., Yokoyama, A., Shinriki, S., Matsui, H., & Inaba, T. (2020) · Journal of Clinical Investigation · doi:10.1172/jci140147 · Cited by 21

In situ detection of phospholipid and phosphoinositide metabolism

Prestwich, G. D., Chen, R., Feng, L., Ozaki, S., Ferguson, C. G., Drees, B. E., Neklason, D. A., Mostert, M. J., Porter-Gill, P. A., Kang, V. H., et al. (2002) · Advances in Enzyme Regulation · doi:10.1016/s0065-2571(01)00039-5 · Cited by 21

Immunosuppressive Signaling Pathways as Targeted Cancer Therapies

Damane, B. P., Hull, R., Bida, M., Durandt, C., Mulaudzi, T. V., Chatziioannou, A. A., & Dlamini, Z. (2022) · Biomedicines · doi:10.3390/biomedicines10030682 · Cited by 20

Computational Modeling of the Main Signaling Pathways Involved in Mast Cell Activation

Niarakis, A., Bounab, Y., Grieco, L., Roncagalli, R., Hesse, A.-M., Garin, J., MALISSEN, B., Daëron, M., & Thieffry, D. (2014) · Current topics in microbiology and immunology · doi:10.1007/978-3-319-07911-0_4 · Cited by 20

The inositol 5-phosphatase SHIP1 is a nucleo-cytoplasmic shuttling protein and enzymatically active in cell nuclei

Nalaskowski, M. M., Metzner, A., Brehm, M. A., Labiadh, S., Brauer, H., Grabinski, N., Mayr, G. W., & Jücker, M. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.07.012 · Cited by 20

The SH2 domain-containing 5-phosphatase SHIP2 is expressed in the germinal layers of embryo and adult mouse brain: increased expression in N-CAM-deficient mice

Muraille, É., Dassesse, D., Vanderwinden, J., Cremer, H., Rogister, B., Erneux, C., & Schiffmann, S. N. (2001) · Neuroscience · doi:10.1016/s0306-4522(01)00240-8 · Cited by 20

Mechanisms controlling membrane recruitment and activation of the autoinhibited SHIP1 inositol 5-phosphatase

Waddell, G. L., Drew, E. E., Rupp, H. P., & Hansen, S. D. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105022 · Cited by 19

Pharmacological Targeting of Phosphoinositide Lipid Kinases and Phosphatases in the Immune System: Success, Disappointment, and New Opportunities

Blunt, M. D., & Ward, S. G. (2012) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00226 · Cited by 20

SHIP negatively regulates type II immune responses in mast cells and macrophages

Dobranowski, P., & Sly, L. M. (2018) · Journal of Leukocyte Biology · doi:10.1002/jlb.3mir0817-340r · Cited by 19

Regulation of hematopoietic cell signaling by SHIP-1 inositol phosphatase: growth factors and beyond

Hibbs, M. L., Raftery, A. L., & Tsantikos, E. (2018) · Growth Factors · doi:10.1080/08977194.2019.1569649 · Cited by 19

Regulation of Signal Transduction by the Fcγ Receptor Family Members and Their Involvement in Autoimmunity

Coggeshall, K. M. (2001) · KARGER eBooks · doi:10.1159/000060554 · Cited by 19

PTEN--Coupling Tumor Suppression to Stem Cells?

Penninger, J. M., & Woodgett, J. R. (2001) · Science · doi:10.1126/science.1067931 · Cited by 19

An ENU-induced mouse mutant of SHIP1 reveals a critical role of the stem cell isoform for suppression of macrophage activation

Nguyen, N.-Y. N., Maxwell, M. J., Ooms, L. M., Davies, E. M., Hilton, A. A., Collinge, J. E., Hilton, D. J., Kile, B. T., Mitchell, C. A., Hibbs, M. L., et al. (2011) · Blood · doi:10.1182/blood-2011-01-331041 · Cited by 18

Balanced Interactions between Lyn, the p85α Regulatory Subunit of Class IA Phosphatidylinositol-3-Kinase, and SHIP Are Essential for Mast Cell Growth and Maturation

Ma, P., Vemula, S., Munugalavadla, V., Chen, J., Sims, E. K., Borneo, J., Kondo, T., Ramdas, B., Mali, R. S., Li, S., et al. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05750-11 · Cited by 18

SHIP-deficient mice provide insights into the regulation of dendritic cell development and function

Neill, L., Tien, A. H., Rey-Ladino, J., & Helgason, C. D. (2007) · Experimental Hematology · doi:10.1016/j.exphem.2007.01.048 · Cited by 18

Targeting phosphatidylinositol 3-kinase signaling in acute myelogenous leukemia

Evangelisti, C., Evangelisti, C., Bressanin, D., Buontempo, F., Chiarini, F., Lonetti, A., Soncin, M., Spartà, A., McCubrey, J. A., & Martelli, A. M. (2013) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2013.808333 · Cited by 18

The role of SHIP1 in T-lymphocyte life and death

Gloire, G., Erneux, C., & Piette, J. G. (2007) · Biochemical Society Transactions · doi:10.1042/bst0350277 · Cited by 19

Monocytic suppressor cells derived from human peripheral blood suppress xenogenic immune reactions

Maeda, A., Kawamura, T., Ueno, T., Usui, N., & Miyagawa, S. (2013) · Xenotransplantation · doi:10.1111/xen.12067 · Cited by 17

Regulation of hematopoietic cell function by inhibitory immunoglobulin G receptors and their inositol lipid phosphatase effectors

Cady, C. T., Rice, J. S., Ott, V. L., & Cambier, J. C. (2008) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00663.x · Cited by 17

Targeting Interactions Between Siglec-10 and α3β1 Integrin Enhances Macrophage-Mediated Phagocytosis of Pancreatic Cancer

Saini, P., Mirji, G., Islam, S. M. S., Simons, L. M., Bhat, S. A., Bonfanti, A. P., Muthumani, K., Agrawal, P., Cassel, J. A., Tang, H., et al. (2025) · Cancer Research · doi:10.1158/0008-5472.can-25-0977 · Cited by 16

SH2-Inositol Phosphatase 1 Negatively Influences Early Megakaryocyte Progenitors

Perez, L. E., Desponts, C., Parquet, N., & Kerr, W. G. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003565 · Cited by 16

Multiple signaling pathways are involved in the regulation of IGF-I receptor inhibition of PTEN-enhanced apoptosis

Wu, Y., Karas, M., Dupont, J., Zhao, H., Toyoshima, Y., & Roith, D. L. (2003) · Growth Hormone & IGF Research · doi:10.1016/j.ghir.2003.08.003 · Cited by 16

Role of SHIP-1 in the Adaptive Immune Responses to Aeroallergen in the Airway

Roongapinun, S., Oh, S.-Y., Wu, F., Panthong, A., Zheng, T., & Zhu, Z. (2010) · PLoS ONE · doi:10.1371/journal.pone.0014174 · Cited by 15

SHIP negatively regulates Flt3L-derived dendritic cell generation and positively regulates MyD88-independent TLR-induced maturation

Antignano, F., Ibaraki, M., Rüschmann, J., Jagdeo, J. M., & Krystal, G. (2010) · Journal of Leukocyte Biology · doi:10.1189/jlb.1209825 · Cited by 15

A critical role for FcgammaRIIB in up-regulation of Fas ligand induced by a microbial polysaccharide

Piccioni, M., Monari, C., Bevilacqua, S., Perito, S., Bistoni, F., Kozel, T. R., & Vecchiarelli, A. (2011) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2011.04415.x · Cited by 15

SHIP1/2 interaction with tyrosine phosphorylated peptides mimicking an immunoreceptor signalling motif

Pesesse, X., Backers, K., Moreau, C., Zhang, J., Bléro, D., Paternotte, N., & Erneux, C. (2006) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2006.01.013 · Cited by 15

Inpp5d haplodeficiency alleviates tau pathology in the PS19 mouse model of Tauopathy

Soni, D. M., Lin, P. B., Lee‐Gosselin, A., Lloyd, C. D., Mason, E., Ingraham, C. M., Perkins, A., Moutinho, M., Lamb, B. T., Chu, S., et al. (2024) · Alzheimer's & Dementia · doi:10.1002/alz.14078 · Cited by 14

SHIP, a novel factor to ameliorate extracellular matrix accumulation via suppressing PI3K/Akt/CTGF signaling in diabetic kidney disease

Li, F., Li, L., Cheng, M., Wang, X., Hao, J., Liu, S., & Duan, H. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.12.060 · Cited by 14

Gene transfer of SHIP-1 inhibits proliferation of juvenile myelomonocytic leukemia cells carrying KRAS2 or PTPN11 mutations

Metzner, A., Horstmann, M. A., Fehse, B., Ortmeyer, G., Niemeyer, C. M., Stocking, C., Mayr, G. W., & Jücker, M. (2007) · Gene Therapy · doi:10.1038/sj.gt.3302912 · Cited by 14

Regulation of the Src Homology 2-containing Inositol 5-Phosphatase SHIP1 in HIP1/PDGFβR-transformed Cells

Saint‐Dic, D., Chang, S. C., Taylor, G. S., Provot, M. M., & Ross, T. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008336200 · Cited by 14

Functional involvement of Akt signaling downstream of Jak1 in v-Abl–induced activation of hematopoietic cells

Oki, S., Limnander, A., Danial, N. N., & Rothman, P. B. (2002) · Blood · doi:10.1182/blood.v100.3.966 · Cited by 14

p66Shc Is a Negative Regulator of FcεRI-Dependent Signaling in Mast Cells

Ulivieri, C., Fanigliulo, D., Masi, G., Savino, M. T., Gamberucci, A., Pelicci, P. G., & Baldari, C. T. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1001391 · Cited by 12

The 5-Phosphatase SHIP2 Promotes Neutrophil Chemotaxis and Recruitment

Michael, M., McCormick, B., Anderson, K. E., Karmakar, U., Vermeren, M., Schurmans, S., Amour, A., & Vermeren, S. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.671756 · Cited by 11

Compound heterozygosity for Pten and SHIP augments T‐dependent humoral immune responses and cytokine production by CD4+ T cells

Moody, J. L., & Jirik, F. R. (2004) · Immunology · doi:10.1111/j.1365-2567.2004.01901.x · Cited by 11

Loss of Inpp5d has disease‐relevant and sex‐specific effects on glial transcriptomes

Dabin, L. C., Kersey, H., Kim, B., Acri, D. J., Sharify, D., Lee‐Gosselin, A., Lasagna‐Reeves, C. A., Oblak, A. L., Lamb, B. T., & Kim, J. (2024) · Alzheimer's & Dementia · doi:10.1002/alz.13901 · Cited by 10

Deficiency of Lipid Phosphatase SHIP Enables Long-Term Reconstitution of Hematopoietic Inductive Bone Marrow Microenvironment

Liang, O. D., Lu, J., Nombela‐Arrieta, C., Jia, Z., Zhao, L., Pivarnik, G., Mondal, S., Chai, L., Silberstein, L. E., & Luo, H. R. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.04.016 · Cited by 10

Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatase 1: A Meaningful and Independent Marker to Predict Stroke in the Chinese Population

Tu, W., Liu, X., Dong, H., Yan, Y. R., Wang, Y., & Chen, H. (2013) · Journal of Molecular Neuroscience · doi:10.1007/s12031-013-0206-2 · Cited by 10

Regulation of SHIP2 function through plasma membrane interaction

Deneubourg, L., Vanderwinden, J., & Erneux, C. (2009) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2009.10.009 · Cited by 10

Loss of lipid phosphatase SHIP1 promotes macrophage differentiation through suppression of dendritic cell differentiation

So, E. Y., Sun, C., Reginato, A. M., Dubielecka, P. M., Ouchi, T., & Liang, O. D. (2019) · Cancer Biology & Therapy · doi:10.1080/15384047.2018.1523846 · Cited by 10

miR-23b-3p regulates differentiation of osteoclasts by targeting PTEN via the PI3k/AKT pathway

Chai, J., Xu, L., & Liu, N. (2019) · Archives of Medical Science · doi:10.5114/aoms.2019.87520 · Cited by 9

Activated eosinophils in early life impair lung development and promote long-term lung damage

Raftery, A. L., O’Brien, C. A., Shad, A., L’Estrange-Stranieri, E., Hsu, A. T., Jacobsen, E. A., Harris, N. L., Tsantikos, E., & Hibbs, M. L. (2024) · Mucosal Immunology · doi:10.1016/j.mucimm.2024.06.003 · Cited by 9

Tumor suppressor p53 stole the AKT in hypoxia

Yun, Z., & Glazer, P. M. (2015) · Journal of Clinical Investigation · doi:10.1172/jci82058 · Cited by 9

Regulation of Microglial Signaling by Lyn and SHIP-1 in the Steady-State Adult Mouse Brain

Chu, E., Mychasiuk, R., Tsantikos, E., Raftery, A. L., L’Estrange-Stranieri, E., Dill, L. K., Semple, B. D., & Hibbs, M. L. (2023) · Cells · doi:10.3390/cells12192378 · Cited by 8

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. A. H. (2022) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2022.106229 · Cited by 8

Src kinases as targets for Bcell acute lymphoblastic leukaemia therapy

Li, S. (2005) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.9.2.329 · Cited by 8

Hallmark of Systemic Lupus Erythematosus: Role of B Cell Hyperactivity

Vincent, F. B., Figgett, W. A., & Hibbs, M. L. (2021) · Springer eBooks · doi:10.1007/978-3-030-85161-3_2 · Cited by 7

Proteomic Analysis of Protective Effects of Dl-3-n-Butylphthalide against mpp + -Induced Toxicity via downregulating P53 pathway in N2A Cells

Zhao, Y., Zhang, J., Zhang, Y., Li, S., Gao, Y., Cui, C., Liu, X., Xu, L., & Yang, G. (2023) · Proteome Science · doi:10.1186/s12953-022-00199-x · Cited by 7

Non-invasive visualization of the lipid product of class I PI3K in transgenic mouse models.

Sasaki, T., Sasaki, J., Watanabe, K., & Suzuki, A. (2007) · Biochemical Society Transactions · doi:10.1042/bst0350215 · Cited by 8

Parkinson’s Disease rs117896735 Variant Regulates INPP5F Expression in Brain Tissues and Increases Risk of Alzheimer’s Disease

Xue, F., Gao, L., Chen, T., Chen, H., Zhang, H., Wang, T., Han, Z., Gao, S., Wang, L., Hu, Y., et al. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220086 · Cited by 6

SHIP1 Is Present but Strongly Downregulated in T-ALL, and after Restoration Suppresses Leukemia Growth in a T-ALL Xenotransplantation Mouse Model

Ehm, P. A. H., Rietow, R., Wegner, W., Bußmann, L., Kriegs, M., Dierck, K., Horn, S., Streichert, T., Horstmann, M. A., & Jücker, M. (2023) · Cells · doi:10.3390/cells12131798 · Cited by 6

Phospholipid signalling: mediators in need of interdisciplinary techniques

Woscholski, R. (2006) · Signal Transduction · doi:10.1002/sita.200690018 · Cited by 6

hSHIP induces S-phase arrest and growth inhibition in cervical cancer HeLa cells

He, K., He, J., Wang, S., & Yan, J. (2010) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/s1673-8527(09)60043-6 · Cited by 6

p135 Src Homology 2 Domain-containing Inositol 5′-Phosphatase (SHIPβ) Isoform Can Substitute for p145 SHIP in FcγRIIB1-mediated Inhibitory Signaling in B Cells

March, M., Lucas, D. M., Aman, M. J., & Ravichandran, K. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003714200 · Cited by 6

Genome-wide studies define new genetic mechanisms of IgA vasculitisPreprint

Liu, L., Zhu, L., Monteiro-Martins, S., Griffin, A. T., Vlahos, L. J., Fujita, M., Berrouet, C. C., Zanoni, F., Marasà, M., Zhang, J. Y., et al. (2024) · medRxiv · doi:10.1101/2024.10.10.24315041 · Cited by 6

Selective deletion of SHIP-1 in hematopoietic cells in mice leads to severe lung inflammation involving ILC2 cells

Ye, X., Zhang, F., Li, Z., Wei, Y., Zhang, L., Wang, L., Tang, H., Chen, Z., Kerr, W. G., Zheng, T., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-88677-8 · Cited by 5

SHIP1 Controls Internal Platelet Contraction and αIIbβ3 Integrin Dynamics in Early Platelet Activation

Séverin, S., Consonni, A., Chicanne, G., Allart, S., Payrastre, B., & Gratacap, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24020958 · Cited by 5

Regulation of microglial responses after pediatric traumatic brain injury: exploring the role of SHIP-1

Chu, E., Mychasiuk, R., Green, T. R. F., Zamani, A., Dill, L. K., Sharma, R., Raftery, A. L., Tsantikos, E., Hibbs, M. L., & Semple, B. D. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1276495 · Cited by 4

Fc Receptors

Ravetch, J. V., & Bournazos, S. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95895-0.00005-2 · Cited by 4

Monocytic Suppressor Cells Derived From Peripheral Blood Suppress Xenogenic Natural Killer Cell Lysis

Maeda, A., Kawamura, T., Nakahata, K., Ueno, T., Usui, N., Eguchi, H., & Miyagawa, S. (2014) · Transplantation Proceedings · doi:10.1016/j.transproceed.2013.11.025 · Cited by 4

Regulation of Mast Cell Degranulation by SHIP

Huber, M., Damen, J. E., Ware, M. D., Hughes, M. R., Helgason, C. D., Humphries, R. K., & Gerald, K. (2000) · Elsevier eBooks · doi:10.1016/b978-012473335-0/50013-1 · Cited by 4

Environmental and inflammatory factors influencing concurrent gut and lung inflammation

Raftery, A. L., Pattaroni, C., Harris, N. L., Tsantikos, E., & Hibbs, M. L. (2024) · Inflammation Research · doi:10.1007/s00011-024-01953-x · Cited by 4

Amelioration of premature aging in Werner syndrome stem cells by targeting SHIP/AKT pathway

Tam, H.-Y., Liu, J., Yiu, T.-C., Leung, A. O.-W., Li, C., Gu, S., Rennert, O. M., Huang, B., & Cheung, H. (2025) · Cell & Bioscience · doi:10.1186/s13578-025-01355-4 · Cited by 3

Scaffold Proteins in Autoimmune Disorders

Joseph, J., Mathew, J., & Alexander, J. J. (2023) · Current Rheumatology Reviews · doi:10.2174/1573397119666230904151024 · Cited by 3

SHIP1 deficiency causes inflammation-dependent retardation in skeletal growth

Safari, F., Yeoh, W. J., Perret-Gentil, S., Klenke, F. M., Dolder, S., Hofstetter, W., & Krebs, P. (2024) · Life Science Alliance · doi:10.26508/lsa.202302297 · Cited by 3

Molecular and Cellular Basis of Chemoresistance in Ovarian Cancer

Asare-Werehene, M., Shieh, D., Song, Y. S., & Tsang, B. K. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813209-8.00035-2 · Cited by 4

Characterization of the substrate specificity of the inositol 5-phosphatase SHIP1

Nelson, N., Wundenberg, T., Lin, H., Rehbach, C., Horn, S., Windhorst, S., & Jücker, M. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.01.012 · Cited by 3

Mutation analysis of hematopoietic cell phosphatase gene in acute leukemia.

Luo, J., Liu, Z., Hao, H.-L., Wang, F., Dong, Z.-R., & Ryuzo, O. (2004) · PubMed · Cited by 2

Phosphatidylinositol 3-kinase, Phosphoinositides and Apoptosis

Sármay, G. (2006) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-47931-1_16 · Cited by 2

Regulation of Neutrophil Apoptosis

Mayadas, T. N. (2003) · Springer eBooks · doi:10.1007/978-2-8178-0761-4_13 · Cited by 2

Study of SHIP‐binding cell surface proteins suggests c‐kit as a SHIP‐interacting receptor in mast cells

Ott, V. L., Moffitt, L. A., & Cambier, J. C. (2005) · Signal Transduction · doi:10.1002/sita.200400029 · Cited by 2

The power of five – inositol polyphosphate 5‐phosphatase gene mutations at the intersection of development and disease

McGrath, M. J., Davies, E. M., Ooms, L. M., Nanayakkara, R., Gurung, R., Jones, E. I., & Mitchell, C. A. (2025) · FEBS Letters · doi:10.1002/1873-3468.70247 · Cited by 1

SH2-Containing Inositol 5′-Phosphatase Inhibits Transformation of Abelson Murine Leukemia Virus

Fessler, S. P., Rosenberg, N. E., & Baughn, L. B. (2011) · Journal of Virology · doi:10.1128/jvi.05115-11 · Cited by 1

Fc and Complement Receptors

Ravetch, J. V., & Carroll, M. C. (2004) · Elsevier eBooks · doi:10.1016/b978-012053641-2/50019-8 · Cited by 1

The Role of X-Linked Inhibitor of Apoptosis Protein in Chemoresistant Ovarian Cancer

Fraser, M. E., & Tsang, B. K. (2004) · Elsevier eBooks · doi:10.1016/b978-012444562-8/50038-0 · Cited by 1

The role of SHIP1 in modulating disease severity in the K/BxN serum transfer model of rheumatoid arthritis

Hirukawa, A. (2011) · cIRcle (University of British Columbia) · doi:10.14288/1.0072036 · Cited by 1

SHIP Inositol Phosphate Phosphatases

Rohrschneider, L. R. (2003) · Elsevier eBooks · doi:10.1016/b978-012124546-7/50509-x · Cited by 1

Myeloid Specific Ablation of SHIP1 Boosts ex vivo Expansion and Regulatory Function of Myeloid-Derived Suppressor Cells in Inflammatory ArthritisPreprint

So, E. Y., Choi, M. J., Lee, Y. E., Akosman, B., Jeong, E.-M., Reginato, A. M., & Liang, O. D. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.30.679529 · Cited by 1

Regulation of the p53 Response by Cellular Growth and Survival Factors

Brown, L. M., & Benchimol, S. (2005) · Springer eBooks · doi:10.1007/978-1-4020-2922-6_5 · Cited by 1

Inhibitory Receptors and Autoimmunity in the Mouse

Clatworthy, M. R., & SMITH, K. (2007) · Elsevier eBooks · doi:10.1016/b978-012369454-6/50090-x

Bayesian microarray one-way anova and grouping cell lines by equal expression levels

Lönnstedt, I. M., & Rimini, R. (2004)

Untersuchungen zur Funktion des PI3K/Akt-Signalweges für das Wachstum von disseminierten Tumorzelllinien von Patienten mit Malignomen

Grupp, K. (2013)

Studies into the function and regulation of SHIP

Rüschmann, J. (2009) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-7073

The role of SHIP in growth factor induced signalling

Huber, M., Helgason, C. D., Damen, J. E., Scheid, M. P., Duronio, V., Liu, L., Ware, M. D., Humphries, R. K., & Krystal, G. (1999) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(98)00049-2 · Cited by 63

Phosphatidylinositol (3,4,5)P₃ Is Essential but Not Sufficient for Protein Kinase B (PKB) Activation; Phosphatidylinositol (3,4)P₂ Is Required for PKB Phosphorylation at Ser-473 - Studies Using Cells From SH2-Containing Inositol-5-Phosphatase Knockout Mice

Scheid, M., Huber, M., Damen, J., Hughes, M., Kang, V., Neilsen, P., Prestwich, G., Krystal, G., & Duronio, V. (2002) · Max Planck Digital Library

(Experimental Medicine)

Antignano, F. L., & Antignano, F. L. (2009)

Phosphatidylinositol (3,4,5)P3 Is Essential but Not Sufficient for Protein Kinase B (PKB) Activation; Phosphatidylinositol (3,4)P2 Is Required for PKB Phosphorylation at Ser-473

Scheid, M. P., Huber, M., Damen, J. E., Hughes, M. R., Kang, V. H., Neilsen, P. O., Prestwich, G. D., Krystal, G., & Duronio, V. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106755200 · Cited by 166

Effects of SHIP Over Expression On the Invasion and Migration of K562 Cells and Its Mechanism.

Yang, L., Luo, J., Liu, X., & Wen, S.-P. (2009) · Blood · doi:10.1182/blood.v114.22.5051.5051