Structure, function, and biology of SHIP proteins

PTEN , a Putative Protein Tyrosine Phosphatase Gene Mutated in Human Brain, Breast, and Prostate Cancer

Li, J., Yen, C., Liaw, D., Podsypanina, K., Bose, S., Wang, S. I., Puc, J., Miliaresis, C., Rodgers, L., McCombie, R., et al. (1997) · Science · doi:10.1126/science.275.5308.1943 · Cited by 4,785

Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers

Steck, P. A., Pershouse, M. A., Jasser, S. A., Yung, W. K. A., Lin, H., Ligon, A. H., Langford, L. A., Baumgard, M. L., Hattier, T., Davis, T., et al. (1997) · Nature Genetics · doi:10.1038/ng0497-356 · Cited by 2,742

SH2 domains recognize specific phosphopeptide sequences

Songyang, Z. (1993) · Cell · doi:10.1016/0092-8674(93)90404-e · Cited by 2,620

Signal Transduction through MAP Kinase Cascades

Lewis, T. S., Shapiro, P. S., & Ahn, N. G. (1998) · Advances in cancer research · doi:10.1016/s0065-230x(08)60765-4 · Cited by 1,759

Targeted Disruption of the Mouse Stat1 Gene Results in Compromised Innate Immunity to Viral Disease

Durbin, J. E., Hackenmiller, R., Simon, M. C., & Levy, D. E. (1996) · Cell · doi:10.1016/s0092-8674(00)81289-1 · Cited by 1,539

Pten is essential for embryonic development and tumour suppression

Cristofano, A. D., Pesce, B., Cordon‐Cardo, C., & Pandolfi, P. P. (1998) · Nature Genetics · doi:10.1038/1235 · Cited by 1,518

Protein Kinase B Kinases That Mediate Phosphatidylinositol 3,4,5-Trisphosphate-Dependent Activation of Protein Kinase B

Stephens, L., Anderson, K. E., Stokoe, D., Erdjument‐Bromage, H., Painter, G. F., Holmes, A. B., Gaffney, P. R. J., Reese, C. B., McCormick, F. P., Tempst, P., et al. (1998) · Science · doi:10.1126/science.279.5351.710 · Cited by 1,061

Specific Inhibition of Stat3 Signal Transduction by PIAS3

Chung, C. D., Liao, J., Liu, B., Rao, X., Jay, P., Berta, P., & Shuai, K. (1997) · Science · doi:10.1126/science.278.5344.1803 · Cited by 980

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

Rozakis-Adcock, M., McGlade, J. C., Mbamalu, G., Pelicci, G., Daly, R. J., Li, W., Batzer, A., Thomas, S. Μ., Brugge, J. S., Pelicci, P. G., et al. (1992) · Nature · doi:10.1038/360689a0 · Cited by 973

Mutation of Pten/Mmac1 in mice causes neoplasia in multiple organ systems

Podsypanina, K., Ellenson, L. H., Nemes, A., Gu, J., Tamura, M., Yamada, K. M., Cordon‐Cardo, C., Cattoretti, G., Fisher, P. E., & Parsons, R. E. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.4.1563 · Cited by 947

Genetic regulation of osteoclast development and function

Teitelbaum, S. L., & Ross, F. P. (2003) · Nature Reviews Genetics · doi:10.1038/nrg1122 · Cited by 1,720

The protein kinase B/Akt signalling pathway in human malignancy

Nicholson, K. M., & Anderson, N. G. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(01)00271-6 · Cited by 1,665

Phosphoinositides: Tiny Lipids With Giant Impact on Cell Regulation

Balla, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00028.2012 · Cited by 1,638

Synthesis and Function of 3-Phosphorylated Inositol Lipids

Vanhaesebroeck, B., Leevers, S. J., Ahmadi, K., Timms, J., Katso, R., Driscoll, P. C., Woscholski, R., Parker, P. J., & Waterfield, M. D. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.535 · Cited by 1,535

Immune Inhibitory Receptors

Ravetch, J. V., & Lanier, L. L. (2000) · Science · doi:10.1126/science.290.5489.84 · Cited by 1,278

Structure, regulation and function of PKB/AKT—a major therapeutic target

Hanada, M., Feng, J., & Hemmings, B. A. (2003) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.11.009 · Cited by 739

JAK/STAT, Raf/MEK/ERK, PI3K/Akt and BCR-ABL in cell cycle progression and leukemogenesis

Steelman, L. S., Pohnert, S. C., Shelton, J. G., Franklin, R. A., Bertrand, F. E., & McCubrey, J. A. (2004) · Leukemia · doi:10.1038/sj.leu.2403241 · Cited by 705

Signaling Cross Talk between TGF-β/Smad and Other Signaling PathwaysPreprint

Luo, K. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022137 · Cited by 671

Targeting phosphoinositide 3-kinase—Moving towards therapy

Marone, R., Cmiljanović, V., Giese, B., & Wymann, M. P. (2007) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2007.10.003 · Cited by 560

Signalling through Class I PI3Ks in mammalian cells

Hawkins, P. T., Anderson, K. E., Davidson, K., & Stephens, L. R. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340647 · Cited by 540

Phosphoinositide 3-kinase signalling pathways

Cantrell, D. A. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.8.1439 · Cited by 539

Oncogenic PI3K and its role in cancer

Samuels, Y., & Ericson, K. (2005) · Current Opinion in Oncology · doi:10.1097/01.cco.0000198021.99347.b9 · Cited by 519

Crk family adaptors–signalling complex formation and biological roles

Feller, S. M. (2001) · Oncogene · doi:10.1038/sj.onc.1204779 · Cited by 468

Domains, Motifs, and Scaffolds: The Role of Modular Interactions in the Evolution and Wiring of Cell Signaling Circuits

Bhattacharyya, R. P., Reményi, A., Yeh, B. J., & Lim, W. A. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142710 · Cited by 458

PTEN function: how normal cells control it and tumour cells lose it

Leslie, N. R., & Downes, C. P. (2004) · Biochemical Journal · doi:10.1042/bj20040825 · Cited by 447

PTEN: The down side of PI 3-kinase signalling

Leslie, N. R., & Downes, C. P. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(01)00234-0 · Cited by 415

Regulation of myeloid development and function by colony stimulating factors

Barreda, D. R. (2003) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2003.09.010 · Cited by 416

Phosphoinositide signalling in cancer: beyond PI3K and PTEN

Bunney, T. D., & Katan, M. (2010) · Nature Reviews Cancer · doi:10.1038/nrc2842 · Cited by 400

P hosphoinositide 3-K inase : Diverse Roles in Immune Cell Activation

Deane, J. A., & Fruman, D. A. (2004) · Annual Review of Immunology · doi:10.1146/annurev.immunol.22.012703.104721 · Cited by 347

Molecular Balance between the Regulatory and Catalytic Subunits of Phosphoinositide 3-Kinase Regulates Cell Signaling and Survival

Ueki, K., Fruman, D. A., Brachmann, S. M., Tseng, Y., Cantley, L. C., & Kahn, C. R. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.3.965-977.2002 · Cited by 285

SHIP-deficient mice are severely osteoporotic due to increased numbers of hyper-resorptive osteoclasts

Takeshita, S., Namba, N., Zhao, J. J., Jiang, Y., Genant, H. K., Silva, M. J., Brodt, M. D., Helgason, C. D., Kalesnikoff, J., Rauh, M. J., et al. (2002) · Nature Medicine · doi:10.1038/nm752 · Cited by 250

Negative Regulation of Immunoreceptor Signaling

Veillette, A., Latour, S., & Davidson, D. (2002) · Annual Review of Immunology · doi:10.1146/annurev.immunol.20.081501.130710 · Cited by 242

Phosphoinositides : key players in cell signalling, in time and space

Payrastre, B., Missy, K., Giuriato, S., Bodin, S., Plantavid, M. M., & Gratacap, M. (2001) · Cellular Signalling · doi:10.1016/s0898-6568(01)00158-9 · Cited by 224

Understanding PTEN regulation: PIP2, polarity and protein stability

Leslie, N. R., Batty, I. H., Maccario, H., Davidson, L., & Downes, C. P. (2008) · Oncogene · doi:10.1038/onc.2008.243 · Cited by 221

miR-155 regulates IFN-γ production in natural killer cells

Trotta, R., Chen, L., Ciarlariello, D., Josyula, S., Mao, C., Costinean, S., Yu, L., Butchar, J. P., Tridandapani, S., Croce, C. M., et al. (2012) · Blood · doi:10.1182/blood-2011-12-398099 · Cited by 204

Molecular mechanisms of transformation by the BCR-ABL oncogene

Sattler, M., & Griffin, J. D. (2003) · Seminars in Hematology · doi:10.1053/shem.2003.50034 · Cited by 205

BMP4 and Madh5 regulate the erythroid response to acute anemia

Lenox, L. E., Perry, J. M., & Paulson, R. F. (2005) · Blood · doi:10.1182/blood-2004-02-0703 · Cited by 197

Phosphoinositide signaling disorders in human diseases

Pendaries, C., Tronchère, H., Plantavid, M. M., & Payrastre, B. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00437-x · Cited by 197

Regulation of integrin-mediated cellular responses through assembly of a CAS/Crk scaffold

Chodniewicz, D., & Klemke, R. L. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.03.006 · Cited by 201

Akt/PKB: one kinase, many modifications

Risso, G., Blaustein, M., Pozzi, B., Mammi, P., & Srebrow, A. (2015) · Biochemical Journal · doi:10.1042/bj20150041 · Cited by 191

The p85 regulatory subunit of phosphoinositide 3-kinase down-regulates IRS-1 signaling via the formation of a sequestration complex

Luo, J., Field, S. J., Lee, J. Y., Engelman, J. A., & Cantley, L. C. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200503088 · Cited by 174

Identification of Insulin Receptor Substrate 1 (IRS-1) and IRS-2 as Signaling Intermediates in the α6β4 Integrin-Dependent Activation of Phosphoinositide 3-OH Kinase and Promotion of Invasion

Shaw, L. M. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.15.5082-5093.2001 · Cited by 172

Activin/TGF-β induce apoptosis through Smad-dependent expression of the lipid phosphatase SHIP

Valderrama-Carvajal, H., Cocolakis, E., Lacerte, A., Lee, E., Krystal, G., Ali, S., & Lebrun, J. J. (2002) · Nature Cell Biology · doi:10.1038/ncb885 · Cited by 169

Inhibitory Receptors on Lymphocytes: Insights from Infections

Odorizzi, P. M., & Wherry, E. J. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1100038 · Cited by 175

A Regulatory Role for Src Homology 2 Domain–Containing Inositol 5′-Phosphatase (Ship) in Phagocytosis Mediated by Fcγ Receptors and Complement Receptor 3 (α M β 2; Cd11b/Cd18)

Cox, D., Dale, B. M., Kashiwada, M., Helgason, C. D., & Greenberg, S. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.193.1.61 · Cited by 158

Phosphatases in cell–matrix adhesion and migration

Larsen, M., Tremblay, M. L., & Yamada, K. M. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1199 · Cited by 143

Regulation of EphA2 Receptor Endocytosis by SHIP2 Lipid Phosphatase via Phosphatidylinositol 3-Kinase-dependent Rac1 Activation

Zhuang, G., Hunter, S., Hwang, Y., & Chen, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608509200 · Cited by 139

Isoform-specific phosphoinositide 3-kinase inhibitors as therapeutic agents

Ward, S. G. (2003) · Current Opinion in Pharmacology · doi:10.1016/s1471-4892(03)00078-x · Cited by 139

PI 3-K and T-cell activation: limitations of T-leukemic cell lines as signaling models

Astoul, E. (2001) · Trends in Immunology · doi:10.1016/s1471-4906(01)01973-1 · Cited by 133

SHIP Negatively Regulates IgE + Antigen-Induced IL-6 Production in Mast Cells by Inhibiting NF-κB Activity

Kalesnikoff, J., Baur, N., Leitges, M., Hughes, M. R., Damen, J. E., Huber, M., & Krystal, G. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.9.4737 · Cited by 130

In vivo analysis of 3-phosphoinositide dynamics during Dictyostelium phagocytosis and chemotaxis

Dormann, D., Weijer, G., DOWLER, S., & Weijer, C. J. (2004) · Journal of Cell Science · doi:10.1242/jcs.01579 · Cited by 131

The tumor suppressor activity of SOCS-1

Rottapel, R. K., Ilangumaran, S., Neale, C., Rose, J. L., Ho, J., Nguyen, M. H.-H., Barber, D. L., Dubreuil, P. C., & Sepulveda, P. D. (2002) · Oncogene · doi:10.1038/sj.onc.1205537 · Cited by 129

Possible dominant-negative mutation of the SHIP gene in acute myeloid leukemia

Luo, J.-M., Yoshida, H., Komura, S., Ohishi, N., Pan, L., Shigeno, K., Hanamura, I., Miura, K., Iida, S., Ueda, R., et al. (2003) · Leukemia · doi:10.1038/sj.leu.2402725 · Cited by 127

PI3K inhibition in inflammation: Toward tailored therapies for specific diseases

Ghigo, A., Damilano, F., Braccini, L., & Hirsch, E. (2010) · BioEssays · doi:10.1002/bies.200900150 · Cited by 126

PTEN in Neural Precursor Cells: Regulation of Migration, Apoptosis, and Proliferation

Li, L., Liu, F., Salmonsen, R. A., Turner, T. K., Litofsky, N. S., Cristofano, A. D., Pandolfi, P. P., Jones, S. N., Recht, L. D., & Ross, A. H. (2002) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2002.1115 · Cited by 125

Therapeutic Potential of Phosphoinositide 3-Kinase Inhibitors

Ward, S. G., Sotsios, Y., Dowden, J., Bruce, I., & Finan, P. M. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(03)00048-6 · Cited by 124

Phosphoinositide-Regulated Kinases and Phosphoinositide Phosphatases

Leslie, N. R., Biondi, R. M., & Alessi, D. R. (2001) · Chemical Reviews · doi:10.1021/cr000091i · Cited by 121

3'-phosphoinositide-dependent kinase-1 (PDK-1) in PI 3-kinase signaling

Störz, P. (2002) · Frontiers in bioscience · doi:10.2741/storz · Cited by 119

Evidence That SHIP-1 Contributes to Phosphatidylinositol 3,4,5-Trisphosphate Metabolism in T Lymphocytes and Can Regulate Novel Phosphoinositide 3-Kinase Effectors

Freeburn, R. W., Wright, K. L., Burgess, S., Astoul, E., Cantrell, D. A., & Ward, S. G. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.10.5441 · Cited by 121

IVIg-mediated amelioration of murine ITP via FcγRIIB is independent of SHIP1, SHP-1, and Btk activity

Crow, A. R., Song, S. M., Freedman, J. J., Helgason, C. D., Humphries, R. K., Siminovitch, K. A., & Lazarus, A. H. (2003) · Blood · doi:10.1182/blood-2003-01-0023 · Cited by 119

Regulation of immune cell signaling by SHIP1: A phosphatase, scaffold protein, and potential therapeutic target

Pauls, S. D., & Marshall, A. J. (2017) · European Journal of Immunology · doi:10.1002/eji.201646795 · Cited by 118

Lipid phosphatases as drug discovery targets for type 2 diabetes

Lazar, D. F., & Saltiel, A. R. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2007 · Cited by 114

Phosphoinositide phosphatases in cell biology and disease

Yang, L., & Bankaitis, V. A. (2010) · Progress in Lipid Research · doi:10.1016/j.plipres.2009.12.001 · Cited by 128

Basophil FcɛRI histamine release parallels expression of Src-homology 2–containing inositol phosphatases in chronic idiopathic urticaria

Vonakis, B. M., Vasagar, K., Gibbons, S. P., Gober, L. M., Sterba, P. M., Chang, H., & Saini, S. S. (2006) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2006.09.035 · Cited by 116

Inhibitor and activator: dual functions for SHIP in immunity and cancer

Kerr, W. G. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05869.x · Cited by 112

Therapeutic Potential of SH2 Domain-Containing Inositol-5′-Phosphatase 1 (SHIP1) and SHIP2 Inhibition in Cancer

Fuhler, G. M., Brooks, R., Toms, B., Iyer, S., Gengo, E. A., Park, M.-Y., Gumbleton, M., Viernes, D. R., Chisholm, J. D., & Kerr, W. G. (2012) · Molecular Medicine · doi:10.2119/molmed.2011.00178 · Cited by 109

Phosphoinositide 3-kinases in T lymphocyte activation

Ward, S. G., & Cantrell, D. A. (2001) · Current Opinion in Immunology · doi:10.1016/s0952-7915(00)00223-5 · Cited by 107

INPP5D expression is associated with risk for Alzheimer's disease and induced by plaque-associated microglia

Tsai, A. P., Lin, P. B.-C., Dong, C., Moutinho, M., Casali, B. T., Liu, Y., Lamb, B. T., Landreth, G. E., Oblak, A. L., & Nho, K. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105303 · Cited by 104

Immunoreceptors on neutrophils

van Rees, D. J., Szilagyi, K., Kuijpers, T. W., Matlung, H. L., & van den Berg, T. K. (2016) · Seminars in Immunology · doi:10.1016/j.smim.2016.02.004 · Cited by 100

T cell-specific deletion of the inositol phosphatase SHIP reveals its role in regulating Th1/Th2 and cytotoxic responses

Tarasenko, T., Kole, H. K., Chi, A. W., Mentink‐Kane, M. M., Wynn, T. A., & Bolland, S. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0704853104 · Cited by 97

Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease

Terzioglu, G., & Young-Pearse, T. L. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00674-9 · Cited by 91

PTEN, but not SHIP and SHIP2, suppresses the PI3K/Akt pathway and induces growth inhibition and apoptosis of myeloma cells

Choi, Y., Zhang, J., Murga, C., Yu, H., Koller, E., Monia, B. P., Gutkind, J. S., & Li, W. (2002) · Oncogene · doi:10.1038/sj.onc.1205650 · Cited by 93

Downstream of Kinase, p62 dok , Is a Mediator of FcγRIIB Inhibition of FcεRI Signaling

Ott, V. L., Tamir, I., Niki, M., Pandolfi, P. P., & Cambier, J. C. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.9.4430 · Cited by 92

Targeting c-Kit mutations: basic science to novel therapies

Sattler, M., & Salgia, R. (2003) · Leukemia Research · doi:10.1016/j.leukres.2003.10.004 · Cited by 92

Coordinate suppression of B cell lymphoma by PTEN and SHIP phosphatases

Miletic, A. V., Anzelon-Mills, A. N., Mills, D. M., Omori, S. A., Pedersen, I. M., Shin, D., Ravetch, J. V., Bolland, S. M., Morse, H. C., & Rickert, R. C. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem.20091962 · Cited by 87

Alteration of phosphatidylinositol 3-kinase cascade in the multilobulated nuclear formation of adult T cell leukemia/lymphoma (ATLL)

Fukuda, R.-I., Hayashi, A., Utsunomiya, A., Nukada, Y., Fukui, R., Itoh, K., Tezuka, K., Ohashi, K., Mizuno, K., Sakamoto, M., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507184102 · Cited by 87

The termination of PI3K signalling by SHIP1 and SHIP2 inositol 5-phosphatases

Backers, K., Bléro, D., Paternotte, N., Zhang, J., & Erneux, C. (2003) · Advances in Enzyme Regulation · doi:10.1016/s0065-2571(02)00043-2 · Cited by 85

The Src Homology 2 Domain Containing Inositol 5-Phosphatase SHIP2 Is Recruited to the Epidermal Growth Factor (EGF) Receptor and Dephosphorylates Phosphatidylinositol 3,4,5-Trisphosphate in EGF-stimulated COS-7 Cells

Pesesse, X., Dewaste, V., Smedt, F. D., Laffargue, M., Giuriato, S., Moreau, C., Payrastre, B., & Erneux, C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103537200 · Cited by 82

Fcγ Receptors on Mast Cells: Activatory and Inhibitory Regulation of Mediator Release

Tkaczyk, C., Okayama, Y., Metcalfe, D. D., & Gilfillan, A. M. (2004) · International Archives of Allergy and Immunology · doi:10.1159/000077213 · Cited by 84

Class I PI 3-kinases: Function and evolution

Kriplani, N., Hermida, M. A., Brown, E. R., & Leslie, N. R. (2015) · Advances in Biological Regulation · doi:10.1016/j.jbior.2015.05.002 · Cited by 83

The PI3' Kinase Pathway in Interferon Signaling

Kaur, S., Shahab Uddin, M. S., & Platanias, L. C. (2005) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2005.25.780 · Cited by 84

Identification of the human erythropoietin receptor region required for Stat1 and Stat3 activation

Kirito, K., Nakajima, K., Watanabe, T., Uchida, M., Tanaka, M., Ozawa, K., & Komatsu, N. (2002) · Blood · doi:10.1182/blood.v99.1.102 · Cited by 82

Phosphoinositide Lipid Phosphatases: Natural Regulators of Phosphoinositide 3-Kinase Signaling in T Lymphocytes

Harris, S. J., Parry, R. V., Westwick, J. K., & Ward, S. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.r700044200 · Cited by 81

Embryonic and hematopoietic stem cells express a novel SH2–containing inositol 5′-phosphatase isoform that partners with the Grb2 adapter protein

Tu, Z., Ninos, J. M., Ma, Z., Wang, J., Lemos, M. P., Desponts, C., Ghansah, T., Howson, J. M., & Kerr, W. G. (2001) · Blood · doi:10.1182/blood.v98.7.2028 · Cited by 82

Phosphoinositide phosphatases in a network of signalling reactions

Bléro, D., Payrastre, B., Schurmans, S., & Erneux, C. (2007) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-007-0304-5 · Cited by 82

PI(3,4)P2 Signaling in Cancer and Metabolism

Gozzelino, L., Santis, M. C. D., Gulluni, F., Hirsch, E., & Martini, M. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00360 · Cited by 79

Aging of the brain, neurotrophin signaling, and Alzheimer's disease: Is IGF1-R the common culprit?

Puglielli, L. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.01.010 · Cited by 61

Inositol Polyphosphate Phosphatases in Human Disease

Hakim, S., Bertucci, M. C., Conduit, S. E., Vuong, D. L., & Mitchell, C. A. (2012) · Current topics in microbiology and immunology · doi:10.1007/978-94-007-5025-8_12 · Cited by 77

INPP5D regulates inflammasome activation in human microglia

Chou, V., Pearse, R. V., Aylward, A. J., Ashour, N., Taga, M., Terzioglu, G., Fujita, M., Fancher, S. B., Sigalov, A., Benoit, C. R., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42819-w · Cited by 79

Differential expression of SHIP1 in CD56bright and CD56dim NK cells provides a molecular basis for distinct functional responses to monokine costimulation

Trotta, R. (2004) · Blood · doi:10.1182/blood-2004-10-4072 · Cited by 77

SH2-containing inositol 5-phosphatases 1 and 2 in blood platelets: their interactions and roles in the control of phosphatidylinositol 3,4,5-trisphosphate levels

Giuriato, S., Pesesse, X., Bodin, S., Sasaki, T., Viala, C., Marion, E., Penninger, J. M., Schurmans, S., Erneux, C., & Payrastre, B. (2003) · Biochemical Journal · doi:10.1042/bj20030581 · Cited by 78

SHIP2 and its involvement in various diseases

Suwa, A., Kurama, T., & Shimokawa, T. (2010) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2010.492780 · Cited by 74

Microglial INPP5D limits plaque formation and glial reactivity in the PSAPP mouse model of Alzheimer's disease

Castranio, E. L., Hasel, P., Haure‐Mirande, J., Ramirez Jimenez, A. V., Hamilton, B. W., Kim, R. D., Glabe, C. G., Wang, M., Zhang, B., Gandy, S., et al. (2023) · Alzheimer's & Dementia · doi:10.1002/alz.12821 · Cited by 74

Mechanisms of Transformation by the BCR/ABL Oncogene

Sattler, M., & Griffin, J. D. (2001) · International Journal of Hematology · doi:10.1007/bf02981952 · Cited by 74

Calcium signaling inhibits interleukin-12 production and activates CD83+ dendritic cells that induce Th2 cell development

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