SHIP2 and its involvement in various diseases

Gene Dose of Apolipoprotein E Type 4 Allele and the Risk of Alzheimer's Disease in Late Onset Families

Corder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429 · see citing works

Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex

Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216 · see citing works

AKT/PKB signaling: navigating downstream

Manning, B. D., & Cantley, L. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.009 · Cited by 6,115 · see citing works

Insulin signalling and the regulation of glucose and lipid metabolism

Saltiel, A. R., & Kahn, C. R. (2001) · Nature · doi:10.1038/414799a · Cited by 5,326 · see citing works

Phosphoinositides in cell regulation and membrane dynamics

Di Paolo, G., & De Camilli, P. (2006) · Nature · doi:10.1038/nature05185 · Cited by 2,790 · see citing works

Insulin Resistance and a Diabetes Mellitus-Like Syndrome in Mice Lacking the Protein Kinase Akt2 (PKBβ)

Cho, H., Mu, J., Kim, J. K., Thorvaldsen, J. L., Chu, Q., Crenshaw, E. B., Kaestner, K. H., Bartolomei, M. S., Shulman, G. I., & Birnbaum, M. J. (2001) · Science · doi:10.1126/science.292.5522.1728 · Cited by 1,837 · see citing works

The role of apolipoprotein E in Alzheimer's disease

Kim, J., Basak, J. M., & Holtzman, D. M. (2009) · Neuron · doi:10.1016/j.neuron.2009.06.026 · Cited by 1,661 · see citing works

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 · see citing works

MicroRNA Signatures in Human Ovarian Cancer

Iorio, M. V., Visone, R., Leva, G. D., Donati, V. L., Petrocca, F., Casalini, P., Taccioli, C., Volinia, S., Liu, C.-G., Alder, H., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1936 · Cited by 1,396 · see citing works

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

Myers, M. P., Pass, I., Batty, I. H., KAAY, J. V. D., Stolarov, J. P., Hemmings, B. A., Wigler, M. H., Downes, C. P., & Tonks, N. K. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13513 · Cited by 1,161 · see citing works

Akt1/PKBα Is Required for Normal Growth but Dispensable for Maintenance of Glucose Homeostasis in Mice

Cho, H., Thorvaldsen, J. L., Chu, Q., Feng, F., & Birnbaum, M. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100462200 · Cited by 959 · see citing works

Survival signalling by Akt and eIF4E in oncogenesis and cancer therapy

Wendel, H., de Stanchina, E., Fridman, J. S., Malina, A., Ray, S., Kogan, S. C., Cordon‐Cardo, C., Pelletier, J., & Lowe, S. W. (2004) · Nature · doi:10.1038/nature02369 · Cited by 956 · see citing works

IRS proteins and the common path to diabetes

White, M. F. (2002) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00514.2001 · Cited by 925 · see citing works

Stability and Instability: Two Faces of Coronary Atherosclerosis

Davies, M. J. (1996) · Circulation · doi:10.1161/01.cir.94.8.2013 · Cited by 913 · see citing works

GSK-3β Regulates Phosphorylation of CRMP-2 and Neuronal Polarity

Yoshimura, T., Kawano, Y., Arimura, N., Kawabata, S., Kikuchi, A., & Kaibuchi, K. (2005) · Cell · doi:10.1016/j.cell.2004.11.012 · Cited by 877 · see citing works

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 719 · see citing works

The role of insulin receptor signaling in the brain

Plum, L., Schubert, M., & Brüning, J. C. (2005) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2005.01.008 · Cited by 604 · see citing works

Micro-RNA profiling in kidney and bladder cancers

Gottardo, F., Liu, C. G., Ferracin, M., Calin, G. A., Fassan, M., Bassi, P., Sevignani, C., Byrne, D., Negrini, M., Pagano, F. C., et al. (2007) · Urologic Oncology Seminars and Original Investigations · doi:10.1016/j.urolonc.2007.01.019 · Cited by 601 · see citing works

Morphogenesis in skin is governed by discrete sets of differentially expressed microRNAs

Yi, R., O'Carroll, D., Pasolli, H. A., Zhang, Z., Dietrich, F. S., Tarakhovsky, A., & Fuchs, E. (2006) · Nature Genetics · doi:10.1038/ng1744 · Cited by 555 · see citing works

Role for Akt3/Protein Kinase Bγ in Attainment of Normal Brain Size

Easton, R., Cho, H., Roovers, K., Shineman, D. W., Mizrahi, M., Forman, M. S., Lee, V. M. ‐., Szabolcs, M. J., de Jong, R., Oltersdorf, T., et al. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.5.1869-1878.2005 · Cited by 551 · see citing works

NGF-Induced Axon Growth Is Mediated by Localized Inactivation of GSK-3β and Functions of the Microtubule Plus End Binding Protein APC

Zhou, F., Zhou, J., Dedhar, S., Wu, Y.-H., & Snider, W. D. (2004) · Neuron · doi:10.1016/j.neuron.2004.05.011 · Cited by 528 · see citing works

Both the Establishment and the Maintenance of Neuronal Polarity Require Active Mechanisms

Jiang, H., Guo, W., Liang, X., & Rao, Y. (2005) · Cell · doi:10.1016/j.cell.2004.12.033 · Cited by 494 · see citing works

Insulin Receptor Substrate-2 Deficiency Impairs Brain Growth and Promotes Tau Phosphorylation

Schubert, M., Brazil, D. P., Burks, D. J., Kushner, J. A., Ye, J., Flint, C. L., Farhang-Fallah, J., Dikkes, P., Warot, X. M., Rio, C., et al. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-18-07084.2003 · Cited by 488 · see citing works

The Akt kinases: Isoform specificity in metabolism and cancer

Gonzalez, E., & McGraw, T. E. (2009) · Cell Cycle · doi:10.4161/cc.8.16.9335 · Cited by 478 · see citing works

Alzheimer's disease-like phosphorylation of the microtubule-associated protein tau by glycogen synthase kinase-3 in transfected mammalian cells

Lovestone, S., Reynolds, C. H., Latimer, D. A., Davis, D. R., Anderton, B. H., Gallo, J., Hanger, D. P., Mulot, S., Marquardt, B., Stabel, S., et al. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00246-3 · Cited by 470 · see citing works

High Affinity Binding of Inositol Phosphates and Phosphoinositides to the Pleckstrin Homology Domain of RAC/Protein Kinase B and Their Influence on Kinase Activity

Frech, M., Andjelković, M., Ingley, E., Reddy, K. K., Falck, J. R., & Hemmings, B. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.13.8474 · Cited by 446 · see citing works

Binding of the adenomatous polyposis coli protein to microtubules increases microtubule stability and is regulated by GSK3β phosphorylation

Zumbrunn, J., Kinoshita, K., Hyman, A. A., & Näthke, I. S. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00002-1 · Cited by 438 · see citing works

The Insulin-Like Growth Factor Axis

Bayés‐Genís, A., Conover, C. A., & Schwartz, R. S. (2000) · Circulation Research · doi:10.1161/01.res.86.2.125 · Cited by 418 · see citing works

The lipid phosphatase SHIP2 controls insulin sensitivity

Clément, S., Krause, U., Desmedt, F., Tanti, J., Behrends, J., Pesesse, X., Sasaki, T., Penninger, J. M., Doherty, M., Malaisse, W. J., et al. (2001) · Nature · doi:10.1038/35051094 · Cited by 377 · see citing works

miR-205 Exerts Tumor-Suppressive Functions in Human Prostate through Down-regulation of Protein Kinase Cε

Gandellini, P., Folini, M., Longoni, N., Pennati, M., Binda, M., Colecchia, M., Salvioni, R., Supino, R., Moretti, R. M., Limonta, P., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-2894 · Cited by 358 · see citing works

Suppression of Endothelial Cell Apoptosis by High Density Lipoproteins (HDL) and HDL-associated Lysosphingolipids

Nofer, J., Levkau, B., Wolinska, I., Junker, R., Fobker, M., von Eckardstein, A., Seedorf, U., & Assmann, G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103782200 · Cited by 358 · see citing works

Suppression of cell growth and invasion by miR-205 in breast cancer

Wu, H., Zhu, S., & Mo, Y. (2009) · Cell Research · doi:10.1038/cr.2009.18 · Cited by 354 · see citing works

Role for neuronal insulin resistance in neurodegenerative diseases

Schubert, M., Gautam, D., Surjo, D., Ueki, K., Baudler, S., Schubert, D., Kondo, T., Alber, J., Galldiks, N., Kustermann, E., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308724101 · Cited by 339 · see citing works

Spatial Sensing in Fibroblasts Mediated by 3′ Phosphoinositides

Haugh, J. M., Codazzi, F., Teruel, M. N., & Meyer, T. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.6.1269 · Cited by 304 · see citing works

Structure, function, and biology of SHIP proteins

Rohrschneider, L. R., Fuller, J. F., Wolf, I., Liu, Y., & Lucas, D. M. (2000) · Genes & Development · doi:10.1101/gad.14.5.505 · Cited by 294 · see citing works

MicroRNA-184 antagonizes microRNA-205 to maintain SHIP2 levels in epithelia

Yu, J., Ryan, D. G., Getsios, S., Oliveira-Fernandes, M., Fatima, A., & Lavker, R. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803992105 · Cited by 278 · see citing works

MicroRNA expression profiles in head and neck cancer cell lines

Tran, N., McLean, T., Zhang, X., Zhao, C. J., Thomson, J. M., O’Brien, C., & Rose, B. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.03.201 · Cited by 275 · see citing works

Absence of the lipid phosphatase SHIP2 confers resistance to dietary obesity

Sleeman, M. W., Wortley, K. E., Lai, K. V., Gowen, L. C., Kintner, J., Kline, W. O., García, K., Stitt, T. N., Yancopoulos, G. D., Wiegand, S. J., et al. (2005) · Nature Medicine · doi:10.1038/nm1178 · Cited by 255 · see citing works

Phox2 genes — from patterning to connectivity

Brunet, J., & Pattyn, A. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(02)00322-2 · Cited by 245 · see citing works

Identification of a Second SH2-Domain-Containing Protein Closely Related to the Phosphatidylinositol Polyphosphate 5-Phosphatase SHIP

Pesesse, X., Deleu, S., Smedt, F. D., Drayer, L., & Erneux, C. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7538 · Cited by 237 · see citing works

The role of the inositol polyphosphate 5-phosphatases in cellular function and human disease

Ooms, L. M., Horan, K., Rahman, P., Seaton, G., Gurung, R., Kethesparan, D. S., & Mitchell, C. A. (2009) · Biochemical Journal · doi:10.1042/bj20081673 · Cited by 224 · see citing works

Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells

Sperbera, B. R., Leight, S., Goedert, M., & Lee, V. M.-Y. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)11902-9 · Cited by 204 · see citing works

Inositol phosphates: proliferation, metabolism and function

Irvine, R. F., Moor, R. M., Pollock, W. K., Smith, P. M., & WREGGETT, K. A. (1988) · Philosophical transactions of the Royal Society of London. Series B, Biological sciences · doi:10.1098/rstb.1988.0077 · Cited by 190 · see citing works

5′ Phospholipid Phosphatase SHIP-2 Causes Protein Kinase B Inactivation and Cell Cycle Arrest in Glioblastoma Cells

Taylor, V., Wong, M. P., Brandts, C., Reilly, L., Dean, N. M., Cowsert, L. M., Moodie, S. A., & Stokoe, D. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.18.6860-6871.2000 · Cited by 182 · see citing works

Control of cell motility and tumour invasion by extracellular matrix interactions

Ruoslahti, E. I. (1992) · British Journal of Cancer · doi:10.1038/bjc.1992.250 · Cited by 179 · see citing works

EphA2 Receptor Tyrosine Kinase as a Promising Target for Cancer Therapeutics

Ireton, R. C., & Chen, J. (2005) · Current Cancer Drug Targets · doi:10.2174/1568009053765780 · Cited by 178 · see citing works

Overexpression of SH2-Containing Inositol Phosphatase 2 Results in Negative Regulation of Insulin-Induced Metabolic Actions in 3T3-L1 Adipocytes via Its 5′-Phosphatase Catalytic Activity

Wada, T., Sasaoka, T., Funaki, M., Hori, H., Murakami, S., Ishiki, M., Haruta, T., Asano, T., Ogawa, W., Ishihara, H., et al. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.5.1633-1646.2001 · Cited by 172 · see citing works

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 · see citing works

Cell biology of the movement of breast cancer cells: Intracellular signalling and the actin cytoskeleton

Jiang, P., Enomoto, A., & Takahashi, M. (2009) · Cancer Letters · doi:10.1016/j.canlet.2009.02.034 · Cited by 163 · see citing works

A Novel SH2-Containing Phosphatidylinositol 3,4,5-Trisphosphate 5-Phosphatase (SHIP2) Is Constitutively Tyrosine Phosphorylated and Associated With src Homologous and Collagen Gene (SHC) in Chronic Myelogenous Leukemia Progenitor Cells

Wisniewski, D., Strife, A., Swendeman, S., Erdjument-Bromage, H., Geromanos, S., Kavanaugh, W. M., Tempst, P., & Clarkson, B. (1999) · Blood · doi:10.1182/blood.v93.8.2707 · Cited by 162 · see citing works

The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin

Dyson, J. M., O’Malley, C. J., Becanovic, J., Munday, A. D., Berndt, M. C., Coghill, I. D., Nandurkar, H. H., Ooms, L. M., & Mitchell, C. A. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200104005 · Cited by 157 · see citing works

Akt as a therapeutic target in cancer

Steelman, L. S., Stadelman, K. M., Chappell, W. H., Horn, S., Bäsecke, J., Cervello, M., Nicoletti, F., Libra, M., Stivala, F., Martelli, A. M., et al. (2008) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.12.9.1139 · Cited by 141 · see citing works

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 · see citing works

Molecular Cloning of Rat SH2-Containing Inositol Phosphatase 2 (SHIP2) and Its Role in the Regulation of Insulin Signaling

Ishihara, H., Sasaoka, T., Hori, H., Wada, T., Hirai, H., Haruta, T., Langlois, W. J., & Kobayashi, M. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0888 · Cited by 132 · see citing works

Differential Regulation of EphA2 in Normal and Malignant Cells

Walker‐Daniels, J., Hess, A. R., Hendrix, M. J. C., & Kinch, M. S. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63899-0 · Cited by 130 · see citing works

The Gene INPPL1, Encoding the Lipid Phosphatase SHIP2, Is a Candidate for Type 2 Diabetes In Rat and Man

Marion, E., Kaisaki, P. J., Pouillon, V., Gueydan, C., Lévy, J., Bodson, A., Krzentowski, G., Daubresse, J., Mockel, J., Behrends, J., et al. (2002) · Diabetes · doi:10.2337/diabetes.51.7.2012 · Cited by 129 · see citing works

SH2-Containing Inositol 5′-Phosphatase SHIP2 Associates with the p130CasAdapter Protein and Regulates Cellular Adhesion and Spreading

Prasad, N. K., Topping, R. S., & Decker, S. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.4.1416-1428.2001 · Cited by 125 · see citing works

Role of protein kinase B in insulin-regulated glucose uptake

Welsh, G. I., Hers, I., Berwick, D. C., Dell, G., Wherlock, M., Birkin, R., Leney, S. E., & Tavaré, J. M. (2005) · Biochemical Society Transactions · doi:10.1042/bst0330346 · Cited by 120 · see citing works

Deletion of the PDGFR-β Gene Affects Key Fibroblast Functions Important for Wound Healing

Gao, Z., Sasaoka, T., Fujimori, T., Oya, T., Ishii, Y., Sabit, H., Kawaguchi, M., Kurotaki, Y., Naito, M., Wada, T., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m413081200 · Cited by 111 · see citing works

APOE-4 Genotype and Neurophysiological Vulnerability to Alzheimer's and Cognitive Aging

Bookheimer, S. Y., & Burggren, A. C. (2009) · Annual Review of Clinical Psychology · doi:10.1146/annurev.clinpsy.032408.153625 · Cited by 104 · see citing works

PTEN, but Not SHIP2, Suppresses Insulin Signaling through the Phosphatidylinositol 3-Kinase/Akt Pathway in 3T3-L1 Adipocytes

Tang, X., Powelka, A. M., Soriano, N. A., Czech, M., & Guilherme, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501949200 · Cited by 103 · see citing works

Role of Integrin-Linked Kinase in Nerve Growth Factor-Stimulated Neurite Outgrowth

Mills, J., Digicaylioglu, M. H., Legg, A. T., Young, C. E., Young, S. S., Barr, A. M., Fletcher, L., O’Connor, T. P., & Dedhar, S. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-05-01638.2003 · Cited by 102 · see citing works

SH2-containing 5′-Inositol Phosphatase, SHIP2, Regulates Cytoskeleton Organization and Ligand-dependent Down-regulation of the Epidermal Growth Factor Receptor

Prasad, K. N., & Decker, S. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m410289200 · Cited by 97 · see citing works

The SH2-Containing Inositol Polyphosphate 5-Phosphatase, Ship, Is Expressed During Hematopoiesis and Spermatogenesis

Liu, Q., Shalaby, F., Jones, J., Bouchard, D., & Dumont, D. J. (1998) · Blood · doi:10.1182/blood.v91.8.2753.2753_2753_2759 · Cited by 95 · see citing works

Association of SH2-Containing Inositol Phosphatase 2 With the Insulin Resistance of Diabetic db/db Mice

Hori, H., Sasaoka, T., Ishihara, H., Wada, T., Murakami, S., Ishiki, M., & Kobayashi, M. (2002) · Diabetes · doi:10.2337/diabetes.51.8.2387 · Cited by 88 · see citing works

Discovery and functional characterization of a novel small molecule inhibitor of the intracellular phosphatase, SHIP2

Suwa, A., Yamamoto, T. S., Sawada, A., Minoura, K., Hosogai, N., Tahara, A., Kurama, T., Shimokawa, T., & Aramori, I. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00358.x · Cited by 87 · see citing works

Polymorphisms in Type II SH2 Domain–Containing Inositol 5-Phosphatase (INPPL1, SHIP2) Are Associated With Physiological Abnormalities of the Metabolic Syndrome

Kaisaki, P. J., Délepine, M., Woon, P. Y., Sebag‐Montefiore, L., Wilder, S. P., Menzel, S., Vionnet, N., Marion, E., Riveline, J., Charpentier, G., et al. (2004) · Diabetes · doi:10.2337/diabetes.53.7.1900 · Cited by 86 · see citing works

A Positive Role of the PI3-K/Akt Signaling Pathway in PC12 Cell Differentiation

Kim, Y., Seger, R., V., S. B. C., Hwang, S., & Yoo, Y. S. (2004) · Molecules and Cells · doi:10.1016/s1016-8478(23)13124-4 · Cited by 85 · see citing works

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 · see citing works

SH2-containing inositol phosphatase 2 negatively regulates insulin-induced glycogen synthesis in L6 myotubes

Sasaoka, T., Hori, H., Wada, T., Ishiki, M., Haruta, T., Ishihara, H., & Kobayashi, M. (2001) · Diabetologia · doi:10.1007/s001250100645 · Cited by 85 · see citing works

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 · see citing works

Phosphoinositol phosphatase SHIP2 promotes cancer development and metastasis coupled with alterations in EGF receptor turnover

Prasad, N. K., Tandon, M., Badve, S., Snyder, P. W., & Nakshatri, H. (2007) · Carcinogenesis · doi:10.1093/carcin/bgm213 · Cited by 75 · see citing works

The SH2 Domain Containing Inositol 5-Phosphatase SHIP2 Controls Phosphatidylinositol 3,4,5-Trisphosphate Levels in CHO-IR Cells Stimulated by Insulin

Bléro, D., Smedt, F. D., Pesesse, X., Paternotte, N., Moreau, C., Payrastre, B., & Erneux, C. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4639 · Cited by 71 · see citing works

MicroRNA-205 inhibits tumor cell migration through down-regulating the expression of the LDL receptor-related protein 1

Song, H., & Bu, G. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.08.020 · Cited by 69 · see citing works

An essential role for the SHIP2-dependent negative feedback loop in neuritogenesis of nerve growth factor–stimulated PC12 cells

Aoki, K., Nakamura, T., Inoue, T., Meyer, T., & Matsuda, M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200609017 · Cited by 65 · see citing works

SHIP2 interaction with the cytoskeletal protein Vinexin

Paternotte, N., Zhang, J., Vandenbroere, I., Backers, K., Bléro, D., Kioka, N., Vanderwinden, J., Pirson, I., & Erneux, C. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04996.x · Cited by 64 · see citing works

Enteropathogenic Escherichia coli Recruits the Cellular Inositol Phosphatase SHIP2 to Regulate Actin-Pedestal Formation

Smith, K. A., Humphreys, D., Hume, P. J., & Koronakis, V. E. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2009.12.004 · Cited by 64 · see citing works

Smooth muscle cell phenotypes in atherosclerotic lesions

Shanahan, C. M., & Weissberg, P. L. (1999) · Current Opinion in Lipidology · doi:10.1097/00041433-199912000-00005 · Cited by 64 · see citing works

The SH2-domian-containing inositol 5-phosphatase (SHIP)-2 binds to c-Met directly via tyrosine residue 1356 and involves hepatocyte growth factor (HGF)-induced lamellipodium formation, cell scattering and cell spreading

Koch, A., Mancini, A., Bounkari, O. E., & Tamura, T. (2005) · Oncogene · doi:10.1038/sj.onc.1208558 · Cited by 63 · see citing works

Impact of Transgenic Overexpression of SH2-Containing Inositol 5′-Phosphatase 2 on Glucose Metabolism and Insulin Signaling in Mice

Kagawa, S., Soeda, Y., Ishihara, H., Oya, T., Sasahara, M., Yaguchi, S., Oshita, R., Wada, T., Tsuneki, H., & Sasaoka, T. (2007) · Endocrinology · doi:10.1210/en.2007-0820 · Cited by 63 · see citing works

NMR Studies of a Heterotypic Sam−Sam Domain Association: The Interaction between the Lipid Phosphatase Ship2 and the EphA2 Receptor,

Leone, M., Cellitti, J. F., & Pellecchia, M. (2008) · Biochemistry · doi:10.1021/bi801713f · Cited by 61 · see citing works

The PI3K effector Arap3 interacts with the PI(3,4,5)P3 phosphatase SHIP2 in a SAM domain-dependent manner

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Impact of the Liver-Specific Expression of SHIP2 (SH2-Containing Inositol 5′-Phosphatase 2) on Insulin Signaling and Glucose Metabolism in Mice

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The c-Cbl-associated protein and c-Cbl are two new partners of the SH2-containing inositol polyphosphate 5-phosphatase SHIP2

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SH2-containing Inositol Phosphatase 2 Predominantly Regulates Akt2, and Not Akt1, Phosphorylation at the Plasma Membrane in Response to Insulin in 3T3-L1 Adipocytes

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Impact of Src Homology 2-Containing Inositol 5′-Phosphatase 2 Gene Polymorphisms Detected in a Japanese Population on Insulin Signaling

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SHIP2 phosphoinositol phosphatase positively regulates EGFR-Akt pathway, CXCR4 expression, and cell migration in MDA-MB-231 breast cancer cells

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SHIP2 overexpression strongly reduces the proliferation rate of K562 erythroleukemia cell line

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PTEN and SHIP2 regulates PI3K/Akt pathway through focal adhesion kinase

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High Expression of Obesity-Linked Phosphatase SHIP2 in Invasive Breast Cancer Correlates with Reduced Disease-Free Survival

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The control of phosphatidylinositol 3,4-bisphosphate concentrations by activation of the Src homology 2 domain containing inositol polyphosphate 5-phosphatase 2, SHIP2

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Inhibitors of the Lipid Phosphatase SHIP2 Discovered by High Throughput Affinity Selection-Mass Spectrometry Screening of Combinatorial Libraries

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In vitro association of phosphatidylinositol 3-kinase activity with the activated insulin receptor tyrosine kinase.

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Evolution of cell interactions with extracellular matrix during carcinogenesis

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The Mouse SHIP2 (Inppl1) Gene: Complementary DNA, Genomic Structure, Promoter Analysis, and Gene Expression in the Embryo and Adult Mouse

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Normalization of Prandial Blood Glucose and Improvement of Glucose Tolerance by Liver-Specific Inhibition of SH2 Domain–Containing Inositol Phosphatase 2 (SHIP2) in Diabetic KKAy Mice

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Reversal of denervation-induced insulin resistance by SHIP2 protein synthesis blockade

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Regulating GLUT4 vesicle dynamics by phosphoinositide kinases and phosphoinositide phosphatases

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APOE4 -VLDL Inhibits the HDL-Activated Phosphatidylinositol 3-Kinase/Akt Pathway via the Phosphoinositol Phosphatase SHIP2

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Dual Role of Src Homology Domain 2-Containing Inositol Phosphatase 2 in the Regulation of Platelet-Derived Growth Factor and Insulin-Like Growth Factor I Signaling in Rat Vascular Smooth Muscle Cells

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The docking properties of SHIP2 influence both JIP1 tyrosine phosphorylation and JNK activity

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

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The association between the SH2‐containing inositol polyphosphate 5‐Phosphatase 2 (SHIP2) and the adaptor protein APS has an impact on biochemical properties of both partners

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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

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Specific Tyrosine Phosphorylations Mediate Signal-Dependent Stimulation of SHIP2 Inositol Phosphatase Activity, while the SH2 Domain Confers an Inhibitory Effect To Maintain the Basal Activity

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Antisense oligonucleotides against the lipid phosphatase SHIP2 improve muscle insulin sensitivity in a dietary rat model of the metabolic syndrome

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Vinexin β regulates the phosphorylation of epidermal growth factor receptor on the cell surface

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Association of SH-2 Containing Inositol 5′-Phosphatase 2 Gene Polymorphisms and Hyperglycemia

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Insulin Receptor Signaling in Normal and Insulin-Resistant StatesPreprint

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A molecular network of the aging human brain provides insights into the pathology and cognitive decline of Alzheimer’s disease

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Inositol 5-phosphatases: insights from the Lowe syndrome protein OCRL

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Lapatinib Resistance in Breast Cancer Cells Is Accompanied by Phosphorylation-Mediated Reprogramming of Glycolysis

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Shared pathways for neuroprogression and somatoprogression in neuropsychiatric disorders

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Phosphoinositides: Important lipids in the coordination of cell dynamics

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Phosphatidylinositol-3,4,5-Triphosphate and Cellular Signaling: Implications for Obesity and Diabetes

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Inositol lipid phosphatases in membrane trafficking and human disease

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Structural Basis for Phosphoinositide Substrate Recognition, Catalysis, and Membrane Interactions in Human Inositol Polyphosphate 5-Phosphatases

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PTEN and Other PtdIns(3,4,5)P3 Lipid Phosphatases in Breast Cancer

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SHIP2 multiple functions: A balance between a negative control of PtdIns(3,4,5)P 3 level, a positive control of PtdIns(3,4)P 2 production, and intrinsic docking properties

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SHIP2: Structure, Function and Inhibition

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MicroRNAs in the cornea: Role and implications for treatment of corneal neovascularization

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Discovery and Development of Small Molecule SHIP Phosphatase Modulators

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Liver and insulin resistance: New wine in old bottle!!!

Patel, B. M., & Goyal, R. K. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.172657 · Cited by 50 · see citing works

Suppression of SHIP2 contributes to tumorigenesis and proliferation of gastric cancer cells via activation of Akt

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Role of Phosphatidylinositol 3,4,5-Trisphosphate in Cell Signaling

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FcγRIIb-SHIP2 axis links Aβ to tau pathology by disrupting phosphoinositide metabolism in Alzheimer's disease model

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Evidence of SHIP2 Ser132 phosphorylation, its nuclear localization and stability

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A Synthetic Polyphosphoinositide Headgroup Surrogate in Complex with SHIP2 Provides a Rationale for Drug Discovery

Mills, S. J., Persson, C., Cozier, G. E., THOMAS, M. P., Tresaugues, L., Erneux, C., Riley, A. M., Nordlund, P., & Potter, B. V. L. (2012) · ACS Chemical Biology · doi:10.1021/cb200494d · Cited by 39 · see citing works

Targeting SHIP1 and SHIP2 in Cancer

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OxLDL-stimulated macrophage exosomes promote proatherogenic vascular smooth muscle cell viability and invasion via delivering miR-186–5p then inactivating SHIP2 mediated PI3K/AKT/mTOR pathway

Ren, L., Chen, S., Yao, D. S., & Yan, H. (2022) · Molecular Immunology · doi:10.1016/j.molimm.2022.02.018 · Cited by 36 · see citing works

Imatinib mesilate-induced phosphatidylinositol 3-kinase signalling and improved survival in insulin-producing cells: role of Src homology 2-containing inositol 5′-phosphatase interaction with c-Abl

Mokhtari, D., Al-Amin, R. A., Turpaev, K. T., Li, T., Idevall‐Hagren, O., Li, J., Wuttke, A., Fred, R. G., Ravassard, P., Scharfmann, R., et al. (2013) · Diabetologia · doi:10.1007/s00125-013-2868-2 · Cited by 35 · see citing works

INPPL1 gene mutations in opsismodysplasia

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How does SHIP 1/2 balance Ptd I ns(3,4) P 2 and does it signal independently of its phosphatase activity?

Xie, J., Erneux, C., & Pirson, I. (2013) · BioEssays · doi:10.1002/bies.201200168 · Cited by 31 · see citing works

SHIP2 signalling at the plasma membrane, in the nucleus and at focal contacts

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Helicobacter pylori CagA oncoprotein interacts with SHIP2 to increase its delivery into gastric epithelial cells

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High SHIP2 Expression Indicates Poor Survival in Colorectal Cancer

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MiRNAs as New Tools in Lesion Vitality Evaluation: A Systematic Review and Their Forensic Applications

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The Sam-Sam interaction between Ship2 and the EphA2 receptor: design and analysis of peptide inhibitors

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Identification of crizotinib derivatives as potent SHIP2 inhibitors for the treatment of Alzheimer's disease

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Exome sequencing identifies a novel INPPL1 mutation in opsismodysplasia

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The Functional Roles of the Src Homology 2 Domain-Containing Inositol 5-Phosphatases SHIP1 and SHIP2 in the Pathogenesis of Human Diseases

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

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Evidence for SH2 Domain-Containing 5′-Inositol Phosphatase-2 (SHIP2) Contributing to a Lymphatic Dysfunction

Agollah, G. D., Gonzalez‐Garay, M. L., Rasmussen, J. C., Tan, I., Aldrich, M. B., Darne, C. D., Fife, C. E., Guilliod, R., Maus, E. A., King, P. D., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0112548 · Cited by 19 · see citing works

Altered chondrocyte differentiation, matrix mineralization and MEK-Erk1/2 signaling in an INPPL1 catalytic knock-out mouse model of opsismodysplasia

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A new layer of phosphoinositide‐mediated allosteric regulation uncovered for SHIP2

Coq, J. L., Navajas, P. L., Martín, B. R., Alfonso, C., & Lietha, D. (2021) · The FASEB Journal · doi:10.1096/fj.202100561r · Cited by 17 · see citing works

Expansion and Functional Divergence of Inositol Polyphosphate 5-Phosphatases in Angiosperms

Zhang, Z., Li, Y., Luo, Z., Kong, S., Zhao, Y., Zhang, C., Zhang, W., Yuan, H., & Cheng, L. Z. (2019) · Genes · doi:10.3390/genes10050393 · Cited by 15 · see citing works

Induction of human chronic myeloid leukemia K562 cell apoptosis by virosecurinine and its molecular mechanism

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Transcriptomic identification of miR-205 target genes potentially involved in metastasis and survival of cutaneous malignant melanoma

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Metformin Effects on SHIP2, AMPKs and Gut Microbiota: Recent Updates on Pharmacology

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CD and NMR conformational studies of a peptide encompassing the Mid Loop interface of Ship2 – Sam

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Biochemistry and structure of phosphoinositide phosphatases

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New lipid interaction partners stimulate the inhibition of activated protein C by cell-penetrating protein C inhibitor

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Reception and intracellul ar mechanisms of insulin action (part 2)

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Expression, purification and characterization of the RhoA-binding domain of human SHIP2 in E.coli

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Phosphorylated SHIP2 on Y1135 localizes at focal adhesions and at the mitotic spindle in cancer cell lines

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AT1 receptor downregulation: A mechanism for improving glucose homeostasis

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Beyond PPARs and Metformin

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Underexpression of INPPL1 is associated with aggressive clinicopathologic characteristics in papillary thyroid carcinoma

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AS1949490, an inhibitor of 5′-lipid phosphatase SHIP2, promotes protein kinase C-dependent stabilization of brain-derived neurotrophic factor mRNA in cultured cortical neurons

Tsuneki, H., Yoshida, H., Okamoto, K., Yamaguchi, M., Endo, K., Nakano, A., Tsuda, M., Toyooka, N., Wada, T., & Sasaoka, T. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.02.003 · Cited by 6 · see citing works

Cellular Mechanisms of Insulin Action

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Abnormal elevated PTEN expression in the mouse antrum of a model of GIST KitK641E/K641E

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N1-Benzyl Tryptamine Pan-SHIP1/2 Inhibitors: Synthesis and Preliminary Biological Evaluation as Anti-Tumor Agents

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PIP3abundance overcomes PI3K signaling selectivity in invadopodia

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Structural Insights into the Binding Propensity of Human SHIP2 SH2 to Oncogenic CagA Isoforms from Helicobacter pylori

Wang, Z., Shan, Y., Wang, R., Zhou, H., Hu, R., Li, Y., Zhu, J., Yang, Y., & Liu, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911299 · Cited by 3 · see citing works

Expression, Purification, Crystallisation and X-ray Crystallographic Analysis of a Truncated Form of Human Src Homology 2 Containing Inositol 5-Phosphatase 2

Coq, J. L., Gallego, L. H., & Lietha, D. (2016) · The Protein Journal · doi:10.1007/s10930-016-9665-y · Cited by 3 · see citing works

Required hydrophobicity of fluorescent reporters for phosphatidylinositol family of lipid enzymes

Waybright, J. M., Huang, W., Proctor, A., Wang, X., Allbritton, N. L., & Zhang, Q. (2017) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-017-0633-y · Cited by 3 · see citing works

Discovery of aurones bearing two amine functionalities as SHIP2 inhibitors with insulin-sensitizing effect in rat myotubes

Lim, P. C., Yap, B. K., Tay, Y. J., Hanapi, N. A., Yusof, S. R., & Lee, C. Y. (2023) · RSC Medicinal Chemistry · doi:10.1039/d3md00360d · Cited by 2 · see citing works

Cellular Mechanisms of Insulin Action

Ciaraldi, T. P. (2017) · Springer eBooks · doi:10.1007/978-3-319-18741-9_5 · Cited by 2 · see citing works

Synthetic studies on the indane SHIP1 agonist AQX-1125

Dungan, O. M., Dormann, S., Fernandes, S., Duffy, B. C., Effiong, D., Kerr, W. G., & Chisholm, J. D. (2022) · Organic & Biomolecular Chemistry · doi:10.1039/d2ob00555g · Cited by 2 · see citing works

Screening for Kinase Inhibitors: From Biochemical to Cellular Assays

Eickhoff, J., & Choidas, A. (2011) · Methods and principles in medicinal chemistry · doi:10.1002/9783527633470.ch2 · Cited by 1 · see citing works

MicroRNA-205 Involvement in Cutaneous Melanoma

Rees, E. R. (2012) · QSpace (Queen's University Library) · Cited by 1 · see citing works

Mechanisms by which Imatinib (Gleevec) counteracts type 2 diabetes possible roles of phosphatidylinositol triphosphate phosphatases SHIP2 and PTEN

Li, T. (2011)

Novel inhibitors of lipid phosphatase SHIP2 and their effects on the phosphorylation of Akt kinase

Mehta, S. (2020) · Työväentutkimus Vuosikirja

Cellular Mechanisms of Insulin Action

Ciaraldi, T. P. (2015) · Springer eBooks · doi:10.1007/978-3-319-20797-1_5-1

Cross-talk between insulin and serotonin signaling in the brain : Involvement of the PI3K/Akt pathway and behavioral consequences in models of insulin resistance

Papazoglou, I. (2013) · HAL · doi:10.70675/06d278b5zf0a0z456dz9c4cz9dc680b45fd3

Etude de la polarité apico-basale dans les cellules épithéliales et son implication dans le cholangiocarcinome intrahépatique : contribution de l'inositol 5-phosphatase SHIP2

komaiha, O. H. (2017) · doi:10.70675/fee5c08fz47b2z48ffz91fbz259486ea6c20

Rôles de la PI3 kinase de classe II alpha et de la PI3K de classe III, vps34, dans la production et les fonctions plaquettaires

Valet, C. (2017) · theses.fr (ABES) · doi:10.70675/26457a9dz8bd0z483bz8f02zfd001dbcb339

Phosphoinositides in blood platelet : mapping of molecular species and evidence for a new localization and role of PI3P

Mujalli, A. (2018) · theses.fr (ABES) · doi:10.70675/b3647c54z4962z4d01za585zbff840437439

Small Molecule Insulin Sensitisers: New Leads and Targets for Next-Generation Insulin Sensitising Strategies

Lee, C. Y. (2026) · Medicinal Chemistry Research · doi:10.1007/s00044-026-03577-8

Decoding PIP signaling: structure and catalytic mechanisms of the human phosphoinositide 5-phosphatases

Martin, E., & Versées, W. (2026) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2026.2743893

BindingDB Entry 50021571: Discovery of aurones bearing two amine functionalities as SHIP2 inhibitors with insulin-sensitizing effect in rat myotubes.

BindingDB (2025) · UC San Diego · doi:10.7270/q2qf8zhz

BindingDB Entry 50003286: Identification of crizotinib derivatives as potent SHIP2 inhibitors for the treatment of Alzheimer's disease.

BindingDB (2020) · UC San Diego · doi:10.7270/q2sq9330

RESEARCH PAPER Discovery and functional characterization of a novel small molecule inhibitor of the intracellular phosphatase, SHIP2

Suwa, A., Yamamoto, T. S., Sawada, A., Minoura, K., Hosogai, N., Tahara, A., Kurama, T., Shimokawa, T., & Aramori, I. (2009)

SHIP2: An Emerging Target for the Treatment of Type 2 Diabetes Mellitus

Baumgartener, J. W. (2003) · Current Drug Targets - Immune Endocrine & Metabolic Disorders · doi:10.2174/1568008033340144 · Cited by 15 · see citing works

"SHIP2 et signalisation de l'insuline: quel rôle dans la pathogénèse et le traitement du diabète de type 2?"

Schurmans, S. (2003) · Dépôt institutionnel de l'Université libre de Bruxelles (Université Libre de Bruxelles)

["SHIP2 and insulin signaling: what is its role in the pathogenesis and treatment of type 2 diabetes?"].

Schurmans, S. (2003) · PubMed

The SH2 domain containing inositol polyphosphate 5-phosphatase-2: SHIP2

Dyson, J. M., Kong, A. M., Wiradjaja, F., Astle, M. V., Gurung, R., & Mitchell, C. A. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.05.003 · Cited by 56 · see citing works