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

Essential Role of Phosphoinositide Metabolism in Synaptic Vesicle Recycling

Cremona, O., Paolo, G. D., Wenk, M. R., Lüthi, A., Kim, W. T., Takei, K., DANIELL, L. W., Nemoto, Y., Shears, S. B., Flavell, R. A., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)81649-9 · Cited by 836

High cancer susceptibility and embryonic lethality associated with mutation of the PTEN tumor suppressor gene in mice

Suzuki, A., de la Pompa, J. L., Stambolic, V., Elia, A., Sasaki, T., Barrantes, I. D. B., Ho, A., Wakeham, A. C., ltie, A., Khoo, W., et al. (1998) · Current Biology · doi:10.1016/s0960-9822(07)00488-5 · Cited by 826

P-TEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphatase

Myers, M. P., Stolarov, J. P., Eng, C., Li, J., Wang, S. I., Wigler, M. H., Parsons, R. E., & Tonks, N. K. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.17.9052 · Cited by 775

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

Ono, M., Bolland, S. M., Tempst, P., & Ravetch, J. V. (1996) · Nature · doi:10.1038/383263a0 · Cited by 773

Inhibition of Stat1-mediated gene activation by PIAS1

Liu, B., Liao, J., Rao, X., Kushner, S. A., Chung, C. D., Chang, D. D., & Shuai, K. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10626 · Cited by 765

A Grb2-associated docking protein in EGF- and insulin-receptor signalling

Holgado-Madruga, M., Emlet, D. R., Moscatello, D. K., Godwin, A. K., & Wong, A. J. (1996) · Nature · doi:10.1038/379560a0 · Cited by 672

The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase.

Damen, J. E., Liu, L., Rosten, P., Humphries, R. K., Jefferson, A. B., Majerus, P. W., & Krystal, G. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.4.1689 · Cited by 633

PTEN: a tumour suppressor that functions as a phospholipid phosphatase

Maehama, T. (1999) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01519-6 · Cited by 599

A presynaptic inositol-5-phosphatase

McPherson, P. S., Garcia, E. P., Slepnev, V. I., David, C., Zhang, X., Grabs, D., Sossini, W. S., Bauerfeind, R., Nemoto, Y., & Camilli, P. V. D. (1996) · Nature · doi:10.1038/379353a0 · Cited by 585

Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase.

Salim, K., Bottomley, M. J., Querfurth, E., Zvelebil, M., Gout, I. T., Scaife, R. M., Margolis, R. L., Gigg, R., Smith, C. I., Driscoll, P. C., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01014.x · Cited by 562

Targeted disruption of SHIP leads to hemopoietic perturbations, lung pathology, and a shortened life span

Helgason, C. D., Damen, J. E., Rosten, P., Grewal, R., Sorensen, P., Chappel, S. M., Borowski, A., Jirik, F., Krystal, G., & Humphries, R. K. (1998) · Genes & Development · doi:10.1101/gad.12.11.1610 · Cited by 556

An Alternative to SH2 Domains for Binding Tyrosine-Phosphorylated Proteins

Kavanaugh, W. M., & Williams, L. T. (1994) · Science · doi:10.1126/science.7527937 · Cited by 499

Deletion of SHIP or SHP-1 Reveals Two Distinct Pathways for Inhibitory Signaling

Ono, M., Okada, H., Bolland, S. M., Yanagi, S., Kurosaki, T., & Ravetch, J. V. (1997) · Cell · doi:10.1016/s0092-8674(00)80337-2 · Cited by 490

The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase

Attree, O., Olivos-Glander, I. M., Okabe, I., Bailey, L. C., Nelson, D. L., Lewis, R. A., Mclnnes, R. R., & Nussbaum, R. L. (1992) · Nature · doi:10.1038/358239a0 · Cited by 482

A Comparative Analysis of the Phosphoinositide Binding Specificity of Pleckstrin Homology Domains

Rameh, L. E., Arvidsson, A., Carraway, K. L., Couvillon, A. D., Rathbun, G. A., Crompton, A. M., VanRenterghem, B., Czech, M., Ravichandran, K. S., Burakoff, S. J., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.22059 · Cited by 459

GENETIC ANALYSIS OF B CELL ANTIGEN RECEPTOR SIGNALING

Kurosaki, T. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.555 · Cited by 432

Phosphatidylinositol‐3,4,5‐trisphosphate (PtdIns‐3,4,5‐P3)/Tec kinase‐dependent calcium signaling pathway: a target for SHIP‐mediated inhibitory signals

Scharenberg, A. M., El-Hillal, O., Fruman, D. A., Beitz, L., Li, Z., Lin, S., Gout, I. T., Cantley, L. C., Rawlings, D. J., & Kinet, J.-P. (1998) · The EMBO Journal · doi:10.1093/emboj/17.7.1961 · Cited by 428

p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity.

Lioubin, M. N., Algate, P. A., Tsai, S., Carlberg, K., Aebersold, A., & Rohrschneider, L. R. (1996) · Genes & Development · doi:10.1101/gad.10.9.1084 · Cited by 418

Btk/Tec kinases regulate sustained increases in intracellular Ca2+ following B‐cell receptor activation

Fluckiger, A.-C., Li, Z., Kato, R. M., Wahl, M. I., Ochs, H. D., Longnecker, R., Kinet, J.-P., Witte, O. N., Scharenberg, A. M., & Rawlings, D. J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.7.1973 · Cited by 399

SHIP Modulates Immune Receptor Responses by Regulating Membrane Association of Btk

Bolland, S. M., Pearse, R. N., Kurosaki, T., & Ravetch, J. V. (1998) · Immunity · doi:10.1016/s1074-7613(00)80555-5 · Cited by 384

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

Liu, Q., Sasaki, T., Kozieradzki, I., Wakeham, A., Itie, A., Dumont, D. J., & Penninger, J. M. (1999) · Genes & Development · doi:10.1101/gad.13.7.786 · Cited by 341

Structure and function of theprotein tyrosine phosphatases

Fauman, E. B., & Saper, M. A. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10059-1 · Cited by 340

The Disabled 1 Phosphotyrosine-Binding Domain Binds to the Internalization Signals of Transmembrane Glycoproteins and to Phospholipids

Howell, B. W., Lanier, L. M., Frank, R., Gertler, F. B., & Cooper, J. A. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.7.5179 · Cited by 317

The src homology 2-containing inositol phosphatase (SHIP) is the gatekeeper of mast cell degranulation

Huber, M., Helgason, C. D., Damen, J. E., Liu, L., Humphries, R. K., & Krystal, G. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.19.11330 · Cited by 314

Cloning of p97/Gab2, the Major SHP2-Binding Protein in Hematopoietic Cells, Reveals a Novel Pathway for Cytokine-Induced Gene Activation

Gu, H., Pratt, J. C., Burakoff, S. J., & Neel, B. G. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80288-9 · Cited by 304

Suppression of extracellular signals and cell proliferation through EGF receptor binding by (−)-epigallocatechin gallate in human A431 epidermoid carcinoma cells

Liang, Y., Lin‐Shiau, S., Chen, C.-F., & Lin, J.-K. (1997) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(19971001)67:1 · Cited by 293

The PTB domain: a new protein module implicated in signal transduction

van der Geer, P., & Pawson, T. J. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)89043-x · Cited by 245

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 240

Gab-Family Adapter Proteins Act Downstream of Cytokine and Growth Factor Receptors and T- and B-Cell Antigen Receptors

Nishida, K., Yoshida, Y., Itoh, M., Fukada, T., Ohtani, T., Shirogane, T., Atsumi, T., Takahashi-Tezuka, M., Ishihara, K., Hibi, M., et al. (1999) · Blood · doi:10.1182/blood.v93.6.1809.406k35_1809_1816 · Cited by 239

The Role of Phosphatases in Inositol Signaling Reactions

Majerus, P. W., Kisseleva, M. V., & Norris, F. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.16.10669 · Cited by 224

The c-Mpl Ligand (Thrombopoietin) Stimulates Tyrosine Phosphorylation of Jak2, Shc, and c-Mpl

Drachman, J. G., Griffin, J. D., & Kaushansky, K. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.4979 · Cited by 223

Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2

Kavanaugh, W. M., Pot, D. A., Chin, S. M., Deuter-Reinhard, M., Jefferson, A. B., Norris, F. A., Masiarz, F. R., Cousens, L. S., Majerus, P. W., & Williams, L. T. (1996) · Current Biology · doi:10.1016/s0960-9822(02)00511-0 · Cited by 217

Mutation of the Pleckstrin Homology Domain of Bruton's Tyrosine Kinase in Immunodeficiency Impaired Inositol 1,3,4,5-Tetrakisphosphate Binding Capacity

Fukuda, M., Kojima, T., Kabayama, H., & Mikoshiba, K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.48.30303 · Cited by 201

Recruitment of an alternatively spliced form of synaptojanin 2 to mitochondria by the interaction with the PDZ domain of a mitochondrial outer membrane protein

Nemoto, Y., & Camilli, P. V. D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.11.2991 · Cited by 195

Erythropoietin stimulates the tyrosine phosphorylation of Shc and its association with Grb2 and a 145-Kd tyrosine phosphorylated protein

Damen, J., Liu, L., Cutler, R., & Krystal, G. (1993) · Blood · doi:10.1182/blood.v82.8.2296.2296 · Cited by 193

Multiple Cytokines Stimulate the Binding of a Common 145-Kilodalton Protein to Shc at the Grb2 Recognition Site of Shc

Liu, L., Damen, J. E., Cutler, R. L., & Krystal, G. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.10.6926 · Cited by 181

Role of the rasGAP-associated docking protein p62dokin negative regulation of B cell receptor-mediated signalingPreprint

Yamanashi, Y., Tamura, T., Kanamori, T., Yamane, H., Nariuchi, H., Yamamoto, T. S., & Baltimore, D. (2000) · Genes & Development · doi:10.1101/gad.14.1.11 · Cited by 181

SH2 Domains Exhibit High-Affinity Binding to Tyrosine-Phosphorylated Peptides Yet Also Exhibit Rapid Dissociation and Exchange

Felder, S., Zhou, M., Hu, P. J., Ureña, J. M., Ullrich, A., Chaudhuri, M. K., White, M. F., Shoelson, S. E., & Schlessinger, J. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.3.1449 · Cited by 177

The Inositol 5′-Phosphatase SHIP Binds to Immunoreceptor Signaling Motifs and Responds to High Affinity IgE Receptor Aggregation

Osborne, M. A., Zenner, G., Lubinus, M., Zhang, X., Songyang, Z., Cantley, L. C., Majerus, P. W., Burn, P., & Kochan, J. P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.46.29271 · Cited by 174

B cell antigen receptor cross-linking induces phosphorylation of the p21 ras oncoprotein activators SHC and mSOS1 as well as assembly of complexes containing SHC, GRB-2, mSOS1, and a 145-kDa tyrosine-phosphorylated protein.

Saxton, T. M., van Oostveen, I., Bowtell, D., Aebersold, R., & Gold, M. R. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.153.2.623 · Cited by 164

Negative signaling in B lymphocytes induces tyrosine phosphorylation of the 145-kDa inositol polyphosphate 5-phosphatase, SHIP

Chacko, G. W., Tridandapani, S., Damen, J. E., Liu, L., Krystal, G., & Coggeshall, K. M. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.157.6.2234 · Cited by 164

The Inositol Phosphatase SHIP Inhibits Akt/PKB Activation in B Cells

Aman, M. J., Lamkin, T. D., Okada, H., Kurosaki, T., & Ravichandran, K. S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.51.33922 · Cited by 162

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

The Cys(X)5Arg Catalytic Motif in Phosphoester Hydrolysis

Zhang, Z., Wang, Y., Wu, L., Fauman, E. B., Stuckey, J. A., Schubert, H., Saper, M. A., & Dixon, J. E. (1994) · Biochemistry · doi:10.1021/bi00255a007 · Cited by 158

Inhibitory receptors, ITIM sequences and phosphatases

Unkeless, J. C., & Jin, J. (1997) · Current Opinion in Immunology · doi:10.1016/s0952-7915(97)80079-9 · Cited by 154

Shc phosphorylation in myeloid cells is regulated by granulocyte macrophage colony-stimulating factor, interleukin-3, and steel factor and is constitutively increased by p210BCR/ABL.

Matsuguchi, T., Salgia, R., Hallek, M. J., Eder, M., Druker, B. J., Ernst, T. J., & Griffin, J. D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37647-0 · Cited by 149

Differential association of phosphatases with hematopoietic co‐receptors bearing immunoreceptor tyrosine‐based inhibition motifs

Vely, F., Olivero, S., Olcese, L., Moretta, A., Damen, J. E., Liu, L., Krystal, G., Cambier, J. C., Daëron, M., & Vivier, É. (1997) · European Journal of Immunology · doi:10.1002/eji.1830270825 · Cited by 143

The Negative Signaling Molecule SH2 Domain-containing Inositol-Polyphosphate 5-Phosphatase (SHIP) Binds to the Tyrosine-phosphorylated β Subunit of the High Affinity IgE Receptor

Kimura, T., Sakamoto, H., Appella, E., & Siraganian, R. P. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.21.13991 · Cited by 141

Inhibitory signaling by B cell FcγRIIb

Coggeshall, K. M. (1998) · Current Opinion in Immunology · doi:10.1016/s0952-7915(98)80169-6 · Cited by 134

The Btk subfamily of cytoplasmic tyrosine kinases: structure, regulation and function

Rawlings, D. J. (1995) · Seminars in Immunology · doi:10.1006/smim.1995.0028 · Cited by 127

FcγRIIB1 Inhibition of BCR-Mediated Phosphoinositide Hydrolysis and Ca2+ Mobilization Is Integrated by CD19 Dephosphorylation

Hippen, K. L., Buhl, A. M., D’Ambrosio, D., Nakamura, K., Persin, C., & Cambier, J. C. (1997) · Immunity · doi:10.1016/s1074-7613(00)80509-9 · Cited by 120

The Src Homology 2 (SH2) Domain of SH2-containing Inositol Phosphatase (SHIP) Is Essential for Tyrosine Phosphorylation of SHIP, Its Association with Shc, and Its Induction of Apoptosis

Liu, L., Damen, J. E., Hughes, M. R., Babić, I., Jirik, F. R., & Krystal, G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.14.8983 · Cited by 119

The catalytic role of Cys124 in the dual specificity phosphatase VHR.

Zhou, G. W., Denu, J. M., Wu, L. J., & Dixon, J. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)46898-6 · Cited by 119

Synaptojanin Inhibition of Phospholipase D Activity by Hydrolysis of Phosphatidylinositol 4,5-Bisphosphate

Chung, J.-K., Sekiya, F., Kang, H.-S., Lee, C., Han, J., Kim, S. R., Bae, Y. S., Morris, A. J., & Rhee, S. G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.25.15980 · Cited by 119

Shc Interaction with Src Homology 2 Domain Containing Inositol Phosphatase (SHIP) in VivoRequires the Shc-Phosphotyrosine Binding Domain and Two Specific Phosphotyrosines on SHIP

Lamkin, T. D., Walk, S. F., Liu, L., Damen, J. E., Krystal, G., & Ravichandran, K. S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.16.10396 · Cited by 118

Shc, Grb2, Sosl, and a 150-Kilodalton Tyrosine-Phosphorylated Protein Form Complexes with Fms in Hematopoietic Cells

Lioubin, M. N., Myles, G. M., Carlberg, K., Bowtell, D. D. L., & Rohrschneider, L. R. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.9.5682-5691.1994 · Cited by 117

BCR/ABL Directly Inhibits Expression of SHIP, an SH2-Containing Polyinositol-5-Phosphatase Involved in the Regulation of Hematopoiesis

Sattler, M., Verma, S., Byrne, C. H., Shrikhande, G., Winkler, T., Algate, P. A., Rohrschneider, L. R., & Griffin, J. D. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.11.7473 · Cited by 111

Erythropoietin Induces the Tyrosine Phosphorylation of GAB1 and Its Association With SHC, SHP2, SHIP, and Phosphatidylinositol 3-Kinase

Lecoq‐Lafon, C., Verdier, F., Fichelson, S., Chrétien, S., Gisselbrecht, S., Lacombe, C., & Mayeux, P. (1999) · Blood · doi:10.1182/blood.v93.8.2578 · Cited by 110

Bruton's Tyrosine Kinase is a Key Regulator in B‐Cell Development

Rawlings, D. J., & Witte, O. N. (1994) · Immunological Reviews · doi:10.1111/j.1600-065x.1994.tb00849.x · Cited by 107

Synaptojanin 2, a Novel Synaptojanin Isoform with a Distinct Targeting Domain and Expression Pattern

Nemoto, Y., Arribas, M., Haffner, C., & Camilli, P. V. D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.49.30817 · Cited by 103

Cloning and characterization of human SHIP, the 145-kD inositol 5- phosphatase that associates with SHC after cytokine stimulation

Ware, M., Rosten, P., Damen, J., Liu, L., Humphries, R., & Krystal, G. (1996) · Blood · doi:10.1182/blood.v88.8.2833.bloodjournal8882833 · Cited by 96

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

The Isolation and Characterization of cDNA Encoding Human and Rat Brain Inositol Polyphosphate 4-Phosphatase

Norris, F. A., Auethavekiat, V., & Majerus, P. W. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.27.16128 · Cited by 94

Tyrosine Phosphorylation and Relocation of SHIP Are Integrin-mediated in Thrombin-stimulated Human Blood Platelets

Giuriato, S., Payrastre, B., Drayer, A. L., Plantavid, M. M., Woscholski, R., Parker, P. J., Erneux, C., & Chap, H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.43.26857 · Cited by 93

Negative Signaling Pathways of the Killer Cell Inhibitory Receptor and FcγRIIb1 Require Distinct Phosphatases

Gupta, N., Scharenberg, A. M., Burshtyn, D. N., Wagtmann, N. R., Lioubin, M. N., Rohrschneider, L. R., Kinet, J.-P., & Long, E. O. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.3.473 · Cited by 90

Negative signaling in B cells causes reduced Ras activity by reducing Shc-Grb2 interactions

Tridandapani, S., Chacko, G. W., Brocklyn, J. R. V., & Coggeshall, K. M. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.158.3.1125 · Cited by 90

Induction of Macrophage Colony-Stimulating Factor-Dependent Growth and Differentiation after Introduction of the Murine c-fms Gene into FDC-P1 Cells

Rohrschneider, L. R., & Metcalf, D. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.11.5081 · Cited by 84

Co-ligation of the Antigen and Fc Receptors Gives Rise to the Selective Modulation of Intracellular Signaling in B Cells

Kiener, P. A., Lioubin, M. N., Rohrschneider, L. R., Ledbetter, J. A., Nadler, S. G., & Diegel, M. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.6.3838 · Cited by 83

The Human SHIP Gene Is Differentially Expressed in Cell Lineages of the Bone Marrow and Blood

Geier, S. J., Algate, P. A., Carlberg, K., Flowers, D., Friedman, C. L., Trask, B. J., & Rohrschneider, L. R. (1997) · Blood · doi:10.1182/blood.v89.6.1876 · Cited by 82

Activation-induced Association of a 145-kDa Tyrosine-phosphorylated Protein with Shc and Syk in B Lymphocytes and Macrophages

Crowley, M. T., Harmer, S. L., & DeFranco, A. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.2.1145 · Cited by 81

The phosphatidylinositol polyphosphate 5-phosphatase SHIP and the protein tyrosine phosphatase SHP-2 form a complex in hematopoietic cells which can be regulated by BCR/ABL and growth factors

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Association of Tyrosine Phosphatases SHP-1 and SHP-2, Inositol 5-Phosphatase SHIP with gp49B1, and Chromosomal Assignment of the Gene

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