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Volumn 47, Issue 6, 2017, Pages 932-945

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

Author keywords

Cellular activation; Homeostasis; Inhibitory receptors; Protein protein interactions; Signal transduction

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATASE; PHOSPHOINOSITIDE PHOSPHATASE; PHOSPHOINOSITIDE PHOSPHATASE SHIP1; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG; INPP5D PROTEIN, HUMAN; INPP5D PROTEIN, MOUSE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 5 PHOSPHATASE; PROTEIN;

EID: 85019964470     PISSN: 00142980     EISSN: 15214141     Source Type: Journal    
DOI: 10.1002/eji.201646795     Document Type: Review
Times cited : (90)

References (134)
  • 1
    • 0028263656 scopus 로고
    • B cell antigen receptor cross-linking induces phosphorylation of the p21ras 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. and Gold, M. R., B cell antigen receptor cross-linking induces phosphorylation of the p21ras oncoprotein activators SHC and mSOS1 as well as assembly of complexes containing SHC, GRB-2, mSOS1, and a 145-kDa tyrosine-phosphorylated protein. J. Immunol. 1994. 153: 623–636.
    • (1994) J. Immunol. , vol.153 , pp. 623-636
    • Saxton, T.M.1    van Oostveen, I.2    Bowtell, D.3    Aebersold, R.4    Gold, M.R.5
  • 2
    • 0028147237 scopus 로고
    • B cell antigen receptor stimulation induces formation of a Shc-Grb2 complex containing multiple tyrosine-phosphorylated proteins
    • Smit, L., de Vries-Smits, A. M., Bos, J. L. and Borst, J., B cell antigen receptor stimulation induces formation of a Shc-Grb2 complex containing multiple tyrosine-phosphorylated proteins. J. Biol. Chem. 1994. 269: 20209–20212.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20209-20212
    • Smit, L.1    de Vries-Smits, A.M.2    Bos, J.L.3    Borst, J.4
  • 3
    • 0030587116 scopus 로고    scopus 로고
    • 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. and Coggeshall, K. M., Negative signaling in B lymphocytes induces tyrosine phosphorylation of the 145-kDa inositol polyphosphate 5-phosphatase, SHIP. J. Immunol. 1996. 157: 2234–2238.
    • (1996) J. Immunol. , vol.157 , pp. 2234-2238
    • Chacko, G.W.1    Tridandapani, S.2    Damen, J.E.3    Liu, L.4    Krystal, G.5    Coggeshall, K.M.6
  • 4
    • 0029978202 scopus 로고    scopus 로고
    • 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. and Krystal, G., The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase. Proc. Natl. Acad. Sci. USA 1996. 93: 1689–1693.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1689-1693
    • Damen, J.E.1    Liu, L.2    Rosten, P.3    Humphries, R.K.4    Jefferson, A.B.5    Majerus, P.W.6    Krystal, G.7
  • 5
    • 0029859565 scopus 로고    scopus 로고
    • Cloning and characterization of human SHIP, the 145-kD inositol 5-phosphatase that associates with SHC after cytokine stimulation
    • Ware, M. D., Rosten, P., Damen, J. E., Liu, L., Humphries, R. K. and Krystal, G., Cloning and characterization of human SHIP, the 145-kD inositol 5-phosphatase that associates with SHC after cytokine stimulation. Blood 1996. 88: 2833–2840.
    • (1996) Blood , vol.88 , pp. 2833-2840
    • Ware, M.D.1    Rosten, P.2    Damen, J.E.3    Liu, L.4    Humphries, R.K.5    Krystal, G.6
  • 7
    • 0030937114 scopus 로고    scopus 로고
    • 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., Trask, B. and Rohrschneider, L. R., The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood. Blood 1997. 89: 1876–1885.
    • (1997) Blood , vol.89 , pp. 1876-1885
    • Geier, S.J.1    Algate, P.A.2    Carlberg, K.3    Flowers, D.4    Friedman, C.5    Trask, B.6    Rohrschneider, L.R.7
  • 9
    • 0034194516 scopus 로고    scopus 로고
    • Differential regulation of B cell development, activation, and death by the src homology 2 domain-containing 5' inositol phosphatase (SHIP)
    • Brauweiler, A., Tamir, I., Dal Porto, J., Benschop, R. J., Helgason, C. D., Humphries, R. K., Freed, J. H. et al., Differential regulation of B cell development, activation, and death by the src homology 2 domain-containing 5' inositol phosphatase (SHIP). J. Exp. Med. 2000. 191: 1545–1554.
    • (2000) J. Exp. Med. , vol.191 , pp. 1545-1554
    • Brauweiler, A.1    Tamir, I.2    Dal Porto, J.3    Benschop, R.J.4    Helgason, C.D.5    Humphries, R.K.6    Freed, J.H.7
  • 10
    • 0036196812 scopus 로고    scopus 로고
    • Regulation of the immune response by SHIP
    • March, M. E. and Ravichandran, K., Regulation of the immune response by SHIP. Semin. Immunol. 2002. 14: 37–47.
    • (2002) Semin. Immunol. , vol.14 , pp. 37-47
    • March, M.E.1    Ravichandran, K.2
  • 11
    • 0035496903 scopus 로고    scopus 로고
    • 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. W., Lemos, M. P., Desponts, C., Ghansah, T. et al., Embryonic and hematopoietic stem cells express a novel SH2-containing inositol 5'-phosphatase isoform that partners with the Grb2 adapter protein. Blood 2001. 98: 2028–2038.
    • (2001) Blood , vol.98 , pp. 2028-2038
    • Tu, Z.1    Ninos, J.M.2    Ma, Z.3    Wang, J.W.4    Lemos, M.P.5    Desponts, C.6    Ghansah, T.7
  • 12
    • 0034094822 scopus 로고    scopus 로고
    • Essential role for the C-terminal noncatalytic region of SHIP in FcgammaRIIB1-mediated inhibitory signaling
    • Aman, M. J., Walk, S. F., March, M. E., Su, H. P., Carver, D. J. and Ravichandran, K. S., Essential role for the C-terminal noncatalytic region of SHIP in FcgammaRIIB1-mediated inhibitory signaling. Mol. Cell Biol. 2000. 20: 3576–3589.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 3576-3589
    • Aman, M.J.1    Walk, S.F.2    March, M.E.3    Su, H.P.4    Carver, D.J.5    Ravichandran, K.S.6
  • 13
    • 67749118318 scopus 로고    scopus 로고
    • Regulation of the Src homology 2 domain-containing inositol 5'-phosphatase (SHIP1) by the cyclic AMP-dependent protein kinase
    • Zhang, J., Walk, S. F., Ravichandran, K. S. and Garrison, J. C., Regulation of the Src homology 2 domain-containing inositol 5'-phosphatase (SHIP1) by the cyclic AMP-dependent protein kinase. J. Biol. Chem. 2009. 284: 20070–20078.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20070-20078
    • Zhang, J.1    Walk, S.F.2    Ravichandran, K.S.3    Garrison, J.C.4
  • 14
    • 78049370024 scopus 로고    scopus 로고
    • 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. and Garrison, J. C., 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). J. Biol. Chem. 2010. 285: 34839–34849.
    • (2010) J. Biol. Chem. , vol.285 , pp. 34839-34849
    • Zhang, J.1    Ravichandran, K.S.2    Garrison, J.C.3
  • 15
    • 34548330713 scopus 로고    scopus 로고
    • Small-molecule agonists of SHIP1 inhibit the phosphoinositide 3-kinase pathway in hematopoietic cells
    • Ong, C. J., Ming-Lum, A., Nodwell, M., Ghanipour, A., Yang, L., Williams, D. E., Kim, J. et al., Small-molecule agonists of SHIP1 inhibit the phosphoinositide 3-kinase pathway in hematopoietic cells. Blood 2007. 110: 1942–1949.
    • (2007) Blood , vol.110 , pp. 1942-1949
    • Ong, C.J.1    Ming-Lum, A.2    Nodwell, M.3    Ghanipour, A.4    Yang, L.5    Williams, D.E.6    Kim, J.7
  • 16
    • 84987749012 scopus 로고    scopus 로고
    • The Dok-3/Grb2 adaptor module promotes inducible association of the lipid phosphatase SHIP with the BCR in a coreceptor-independent manner
    • Manno, B., Oellerich, T., Schnyder, T., Corso, J., Losing, M., Neumann, K., Urlaub, H. et al., The Dok-3/Grb2 adaptor module promotes inducible association of the lipid phosphatase SHIP with the BCR in a coreceptor-independent manner. Eur. J. Immunol. 2016. 46: 2520–2530.
    • (2016) Eur. J. Immunol. , vol.46 , pp. 2520-2530
    • Manno, B.1    Oellerich, T.2    Schnyder, T.3    Corso, J.4    Losing, M.5    Neumann, K.6    Urlaub, H.7
  • 17
    • 0029810421 scopus 로고    scopus 로고
    • Distinct mechanisms mediate SHC association with the activated and resting B cell antigen receptor
    • D'Ambrosio, D., Hippen, K. L. and Cambier, J. C., Distinct mechanisms mediate SHC association with the activated and resting B cell antigen receptor. Eur. J. Immunol. 1996. 26: 1960–1965.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 1960-1965
    • D'Ambrosio, D.1    Hippen, K.L.2    Cambier, J.C.3
  • 18
    • 0034029126 scopus 로고    scopus 로고
    • Dok-3, a novel adapter molecule involved in the negative regulation of immunoreceptor signaling
    • Lemay, S., Davidson, D., Latour, S. and Veillette, A., Dok-3, a novel adapter molecule involved in the negative regulation of immunoreceptor signaling. Mol. Cell Biol. 2000. 20: 2743–2754.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 2743-2754
    • Lemay, S.1    Davidson, D.2    Latour, S.3    Veillette, A.4
  • 19
    • 84962393747 scopus 로고    scopus 로고
    • SH2 domains serve as lipid-binding modules for pTyr-signaling proteins
    • Park, M. J., Sheng, R., Silkov, A., Jung, D. J., Wang, Z. G., Xin, Y., Kim, H. et al., SH2 domains serve as lipid-binding modules for pTyr-signaling proteins. Mol. Cell 2016. 62: 7–20.
    • (2016) Mol. Cell , vol.62 , pp. 7-20
    • Park, M.J.1    Sheng, R.2    Silkov, A.3    Jung, D.J.4    Wang, Z.G.5    Xin, Y.6    Kim, H.7
  • 20
    • 84864767849 scopus 로고    scopus 로고
    • A pleckstrin homology-related domain in SHIP1 mediates membrane localization during Fcgamma receptor-induced phagocytosis
    • Ming-Lum, A., Shojania, S., So, E., McCarrell, E., Shaw, E., Vu, D., Wang, I. et al., A pleckstrin homology-related domain in SHIP1 mediates membrane localization during Fcgamma receptor-induced phagocytosis. FASEB J. 2012. 26: 3163–3177.
    • (2012) FASEB J. , vol.26 , pp. 3163-3177
    • Ming-Lum, A.1    Shojania, S.2    So, E.3    McCarrell, E.4    Shaw, E.5    Vu, D.6    Wang, I.7
  • 21
    • 0030610802 scopus 로고    scopus 로고
    • Shc interaction with Src homology 2 domain containing inositol phosphatase (SHIP) in vivo requires the Shc-phosphotyrosine binding domain and two specific phosphotyrosines on SHIP
    • Lamkin, T. D., Walk, S. F., Liu, L., Damen, J. E., Krystal, G. and Ravichandran, K. S., Shc interaction with Src homology 2 domain containing inositol phosphatase (SHIP) in vivo requires the Shc-phosphotyrosine binding domain and two specific phosphotyrosines on SHIP. J. Biol. Chem. 1997. 272: 10396–10401.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10396-10401
    • Lamkin, T.D.1    Walk, S.F.2    Liu, L.3    Damen, J.E.4    Krystal, G.5    Ravichandran, K.S.6
  • 22
    • 0033710778 scopus 로고    scopus 로고
    • The RasGAP-binding protein p62dok is a mediator of inhibitory FcgammaRIIB signals in B cells
    • Tamir, I., Stolpa, J. C., Helgason, C. D., Nakamura, K., Bruhns, P., Daeron, M. and Cambier, J. C., The RasGAP-binding protein p62dok is a mediator of inhibitory FcgammaRIIB signals in B cells. Immunity 2000. 12: 347–358.
    • (2000) Immunity , vol.12 , pp. 347-358
    • Tamir, I.1    Stolpa, J.C.2    Helgason, C.D.3    Nakamura, K.4    Bruhns, P.5    Daeron, M.6    Cambier, J.C.7
  • 23
    • 0034705530 scopus 로고    scopus 로고
    • Enzymatic activity of the Src homology 2 domain-containing inositol phosphatase is regulated by a plasma membrane location
    • Phee, H., Jacob, A. and Coggeshall, K. M., Enzymatic activity of the Src homology 2 domain-containing inositol phosphatase is regulated by a plasma membrane location. J. Biol. Chem. 2000. 275: 19090–19097.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19090-19097
    • Phee, H.1    Jacob, A.2    Coggeshall, K.M.3
  • 24
    • 38449110993 scopus 로고    scopus 로고
    • Quantitative time-resolved phosphoproteomic analysis of mast cell signaling
    • Cao, L., Yu, K., Banh, C., Nguyen, V., Ritz, A., Raphael, B. J., Kawakami, Y. et al., Quantitative time-resolved phosphoproteomic analysis of mast cell signaling. J. Immunol. 2007. 179: 5864–5876.
    • (2007) J. Immunol. , vol.179 , pp. 5864-5876
    • Cao, L.1    Yu, K.2    Banh, C.3    Nguyen, V.4    Ritz, A.5    Raphael, B.J.6    Kawakami, Y.7
  • 25
    • 0033597350 scopus 로고    scopus 로고
    • The src homology domain 2-containing inositol phosphatase SHIP forms a ternary complex with Shc and Grb2 in antigen receptor-stimulated B lymphocytes
    • Harmer, S. L. and DeFranco, A. L., The src homology domain 2-containing inositol phosphatase SHIP forms a ternary complex with Shc and Grb2 in antigen receptor-stimulated B lymphocytes. J. Biol. Chem. 1999. 274: 12183–12191.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12183-12191
    • Harmer, S.L.1    DeFranco, A.L.2
  • 26
    • 0029835940 scopus 로고    scopus 로고
    • Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor Fc(gamma)RIIB
    • Ono, M., Bolland, S., Tempst, P. and Ravetch, J. V., Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor Fc(gamma)RIIB. Nature 1996. 383: 263–266.
    • (1996) Nature , vol.383 , pp. 263-266
    • Ono, M.1    Bolland, S.2    Tempst, P.3    Ravetch, J.V.4
  • 27
    • 0343307005 scopus 로고    scopus 로고
    • Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling
    • Ono, M., Okada, H., Bolland, S., Yanagi, S., Kurosaki, T. and Ravetch, J. V., Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling. Cell 1997. 90: 293–301.
    • (1997) Cell , vol.90 , pp. 293-301
    • Ono, M.1    Okada, H.2    Bolland, S.3    Yanagi, S.4    Kurosaki, T.5    Ravetch, J.V.6
  • 28
    • 33644701667 scopus 로고    scopus 로고
    • The SH2 domain-containing inositol 5-phosphatase SHIP1 is recruited to the intracytoplasmic domain of human FcgammaRIIB and is mandatory for negative regulation of B cell activation
    • Isnardi, I., Bruhns, P., Bismuth, G., Fridman, W. H. and Daeron, M., The SH2 domain-containing inositol 5-phosphatase SHIP1 is recruited to the intracytoplasmic domain of human FcgammaRIIB and is mandatory for negative regulation of B cell activation. Immunol. Lett. 2006. 104: 156–165.
    • (2006) Immunol. Lett. , vol.104 , pp. 156-165
    • Isnardi, I.1    Bruhns, P.2    Bismuth, G.3    Fridman, W.H.4    Daeron, M.5
  • 29
    • 0031985157 scopus 로고    scopus 로고
    • Association of tyrosine phosphatases SHP-1 and SHP-2, inositol 5-phosphatase SHIP with gp49B1, and chromosomal assignment of the gene
    • Kuroiwa, A., Yamashita, Y., Inui, M., Yuasa, T., Ono, M., Nagabukuro, A., Matsuda, Y. et al., Association of tyrosine phosphatases SHP-1 and SHP-2, inositol 5-phosphatase SHIP with gp49B1, and chromosomal assignment of the gene. J. Biol. Chem. 1998. 273: 1070–1074.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1070-1074
    • Kuroiwa, A.1    Yamashita, Y.2    Inui, M.3    Yuasa, T.4    Ono, M.5    Nagabukuro, A.6    Matsuda, Y.7
  • 30
    • 0037086351 scopus 로고    scopus 로고
    • Influence of SHIP on the NK repertoire and allogeneic bone marrow transplantation
    • Wang, J. W., Howson, J. M., Ghansah, T., Desponts, C., Ninos, J. M., May, S. L., Nguyen, K. H. et al., Influence of SHIP on the NK repertoire and allogeneic bone marrow transplantation. Science 2002. 295: 2094–2097.
    • (2002) Science , vol.295 , pp. 2094-2097
    • Wang, J.W.1    Howson, J.M.2    Ghansah, T.3    Desponts, C.4    Ninos, J.M.5    May, S.L.6    Nguyen, K.H.7
  • 31
    • 20444389785 scopus 로고    scopus 로고
    • Molecular basis for positive and negative signaling by the natural killer cell receptor 2B4 (CD244)
    • Eissmann, P., Beauchamp, L., Wooters, J., Tilton, J. C., Long, E. O. and Watzl, C., Molecular basis for positive and negative signaling by the natural killer cell receptor 2B4 (CD244). Blood 2005. 105: 4722–4729.
    • (2005) Blood , vol.105 , pp. 4722-4729
    • Eissmann, P.1    Beauchamp, L.2    Wooters, J.3    Tilton, J.C.4    Long, E.O.5    Watzl, C.6
  • 32
    • 0033004665 scopus 로고    scopus 로고
    • Differential association of cytoplasmic signalling molecules SHP-1, SHP-2, SHIP and phospholipase C-gamma1 with PECAM-1/CD31
    • Pumphrey, N. J., Taylor, V., Freeman, S., Douglas, M. R., Bradfield, P. F., Young, S. P., Lord, J. M. et al., Differential association of cytoplasmic signalling molecules SHP-1, SHP-2, SHIP and phospholipase C-gamma1 with PECAM-1/CD31. FEBS Lett. 1999. 450: 77–83.
    • (1999) FEBS Lett. , vol.450 , pp. 77-83
    • Pumphrey, N.J.1    Taylor, V.2    Freeman, S.3    Douglas, M.R.4    Bradfield, P.F.5    Young, S.P.6    Lord, J.M.7
  • 33
    • 0034610982 scopus 로고    scopus 로고
    • A dual role for Src homology 2 domain-containing inositol-5-phosphatase (SHIP) in immunity: aberrant development and enhanced function of b lymphocytes in ship -/- mice
    • Helgason, C. D., Kalberer, C. P., Damen, J. E., Chappel, S. M., Pineault, N., Krystal, G. and Humphries, R. K., A dual role for Src homology 2 domain-containing inositol-5-phosphatase (SHIP) in immunity: aberrant development and enhanced function of b lymphocytes in ship -/- mice. J. Exp. Med. 2000. 191: 781–794.
    • (2000) J. Exp. Med. , vol.191 , pp. 781-794
    • Helgason, C.D.1    Kalberer, C.P.2    Damen, J.E.3    Chappel, S.M.4    Pineault, N.5    Krystal, G.6    Humphries, R.K.7
  • 34
    • 84983802954 scopus 로고    scopus 로고
    • FcgammaRIIB-independent mechanisms controlling membrane localization of the inhibitory phosphatase SHIP in human B cells
    • Pauls, S. D., Ray, A., Hou, S., Vaughan, A. T., Cragg, M. S. and Marshall, A. J., FcgammaRIIB-independent mechanisms controlling membrane localization of the inhibitory phosphatase SHIP in human B cells. J. Immunol. 2016. 197: 1587–1596.
    • (2016) J. Immunol. , vol.197 , pp. 1587-1596
    • Pauls, S.D.1    Ray, A.2    Hou, S.3    Vaughan, A.T.4    Cragg, M.S.5    Marshall, A.J.6
  • 36
    • 0029803010 scopus 로고    scopus 로고
    • 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. et al., The inositol 5'-phosphatase SHIP binds to immunoreceptor signaling motifs and responds to high affinity IgE receptor aggregation. J. Biol. Chem. 1996. 271: 29271–29278.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29271-29278
    • Osborne, M.A.1    Zenner, G.2    Lubinus, M.3    Zhang, X.4    Songyang, Z.5    Cantley, L.C.6    Majerus, P.7
  • 37
    • 0036838678 scopus 로고    scopus 로고
    • The Src homology 2 domain-containing inositol 5-phosphatase negatively regulates Fcgamma receptor-mediated phagocytosis through immunoreceptor tyrosine-based activation motif-bearing phagocytic receptors
    • Nakamura, K., Malykhin, A. and Coggeshall, K. M., The Src homology 2 domain-containing inositol 5-phosphatase negatively regulates Fcgamma receptor-mediated phagocytosis through immunoreceptor tyrosine-based activation motif-bearing phagocytic receptors. Blood 2002. 100: 3374–3382.
    • (2002) Blood , vol.100 , pp. 3374-3382
    • Nakamura, K.1    Malykhin, A.2    Coggeshall, K.M.3
  • 38
    • 84945156965 scopus 로고    scopus 로고
    • SHIP-1 couples to the dectin-1 hemITAM and selectively modulates reactive oxygen species production in dendritic cells in response to Candida albicans
    • Blanco-Menendez, N., del Fresno, C., Fernandes, S., Calvo, E., Conde-Garrosa, R., Kerr, W. G. and Sancho, D., SHIP-1 couples to the dectin-1 hemITAM and selectively modulates reactive oxygen species production in dendritic cells in response to Candida albicans. J. Immunol. 2015. 195: 4466–4478.
    • (2015) J. Immunol. , vol.195 , pp. 4466-4478
    • Blanco-Menendez, N.1    del Fresno, C.2    Fernandes, S.3    Calvo, E.4    Conde-Garrosa, R.5    Kerr, W.G.6    Sancho, D.7
  • 39
    • 0029665083 scopus 로고    scopus 로고
    • p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity
    • Lioubin, M. N., Algate, P. A., Tsai, S., Carlberg, K., Aebersold, A. and Rohrschneider, L. R., p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity. Genes Dev. 1996. 10: 1084–1095.
    • (1996) Genes Dev. , vol.10 , pp. 1084-1095
    • Lioubin, M.N.1    Algate, P.A.2    Tsai, S.3    Carlberg, K.4    Aebersold, A.5    Rohrschneider, L.R.6
  • 40
    • 0033119739 scopus 로고    scopus 로고
    • 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. and Penninger, J. M., SHIP is a negative regulator of growth factor receptor-mediated PKB/Akt activation and myeloid cell survival. Genes Dev. 1999. 13: 786–791.
    • (1999) Genes Dev. , vol.13 , pp. 786-791
    • Liu, Q.1    Sasaki, T.2    Kozieradzki, I.3    Wakeham, A.4    Itie, A.5    Dumont, D.J.6    Penninger, J.M.7
  • 41
    • 0036151027 scopus 로고    scopus 로고
    • ITAMs versus ITIMs: striking a balance during cell regulation
    • Billadeau, D. D. and Leibson, P. J., ITAMs versus ITIMs: striking a balance during cell regulation. J. Clin. Invest. 2002. 109: 161–168.
    • (2002) J. Clin. Invest. , vol.109 , pp. 161-168
    • Billadeau, D.D.1    Leibson, P.J.2
  • 42
    • 33746256913 scopus 로고    scopus 로고
    • You say ITAM and I say ITIM, let's call the whole thing off: the ambiguity of immunoreceptor signalling
    • Barrow, A. D. and Trowsdale, J., You say ITAM and I say ITIM, let's call the whole thing off: the ambiguity of immunoreceptor signalling. Eur. J. Immunol. 2006. 36: 1646–1653.
    • (2006) Eur. J. Immunol. , vol.36 , pp. 1646-1653
    • Barrow, A.D.1    Trowsdale, J.2
  • 43
    • 84945315708 scopus 로고    scopus 로고
    • Of ITIMs, ITAMs, and ITAMis: revisiting immunoglobulin Fc receptor signaling
    • Getahun, A. and Cambier, J. C., Of ITIMs, ITAMs, and ITAMis: revisiting immunoglobulin Fc receptor signaling. Immunol. Rev. 2015. 268: 66–73.
    • (2015) Immunol. Rev. , vol.268 , pp. 66-73
    • Getahun, A.1    Cambier, J.C.2
  • 44
    • 10644277800 scopus 로고    scopus 로고
    • Two distinct tyrosine-based motifs enable the inhibitory receptor FcgammaRIIB to cooperatively recruit the inositol phosphatases SHIP1/2 and the adapters Grb2/Grap
    • Isnardi, I., Lesourne, R., Bruhns, P., Fridman, W. H., Cambier, J. C. and Daeron, M., Two distinct tyrosine-based motifs enable the inhibitory receptor FcgammaRIIB to cooperatively recruit the inositol phosphatases SHIP1/2 and the adapters Grb2/Grap. J. Biol. Chem. 2004. 279: 51931–51938.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51931-51938
    • Isnardi, I.1    Lesourne, R.2    Bruhns, P.3    Fridman, W.H.4    Cambier, J.C.5    Daeron, M.6
  • 46
    • 84863295500 scopus 로고    scopus 로고
    • Once phosphorylated, tyrosines in carboxyl terminus of protein-tyrosine kinase Syk interact with signaling proteins, including TULA-2, a negative regulator of mast cell degranulation
    • de Castro, R. O., Zhang, J., Groves, J. R., Barbu, E. A. and Siraganian, R. P., Once phosphorylated, tyrosines in carboxyl terminus of protein-tyrosine kinase Syk interact with signaling proteins, including TULA-2, a negative regulator of mast cell degranulation. J. Biol. Chem. 2012. 287: 8194–8204.
    • (2012) J. Biol. Chem. , vol.287 , pp. 8194-8204
    • de Castro, R.O.1    Zhang, J.2    Groves, J.R.3    Barbu, E.A.4    Siraganian, R.P.5
  • 47
    • 0032545343 scopus 로고    scopus 로고
    • The inositol phosphatase SHIP inhibits Akt/PKB activation in B cells
    • Aman, M. J., Lamkin, T. D., Okada, H., Kurosaki, T. and Ravichandran, K. S., The inositol phosphatase SHIP inhibits Akt/PKB activation in B cells. J. Biol. Chem. 1998. 273: 33922–33928.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33922-33928
    • Aman, M.J.1    Lamkin, T.D.2    Okada, H.3    Kurosaki, T.4    Ravichandran, K.S.5
  • 48
    • 0030991386 scopus 로고    scopus 로고
    • 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., Andjelkovic, M., Ingley, E., Reddy, K. K., Falck, J. R. and Hemmings, B. A., High affinity binding of inositol phosphates and phosphoinositides to the pleckstrin homology domain of RAC/protein kinase B and their influence on kinase activity. J. Biol. Chem. 1997. 272: 8474–8481.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8474-8481
    • Frech, M.1    Andjelkovic, M.2    Ingley, E.3    Reddy, K.K.4    Falck, J.R.5    Hemmings, B.A.6
  • 49
    • 85011306591 scopus 로고    scopus 로고
    • PI(3,4,5)P3 engagement restricts Akt activity to cellular membranes
    • e416
    • Ebner, M., Lucic, I., Leonard, T. A. and Yudushkin, I., PI(3,4,5)P3 engagement restricts Akt activity to cellular membranes. Mol. Cell 2017. 65: 416–431, e416.
    • (2017) Mol. Cell , vol.65 , pp. 416-431
    • Ebner, M.1    Lucic, I.2    Leonard, T.A.3    Yudushkin, I.4
  • 50
    • 84867214110 scopus 로고    scopus 로고
    • Interaction of TAPP adapter proteins with phosphatidylinositol (3,4)-bisphosphate regulates B-cell activation and autoantibody production
    • Landego, I., Jayachandran, N., Wullschleger, S., Zhang, T. T., Gibson, I. W., Miller, A., Alessi, D. R. et al., Interaction of TAPP adapter proteins with phosphatidylinositol (3,4)-bisphosphate regulates B-cell activation and autoantibody production. Eur. J. Immunol. 2012. 42: 2760–2770.
    • (2012) Eur. J. Immunol. , vol.42 , pp. 2760-2770
    • Landego, I.1    Jayachandran, N.2    Wullschleger, S.3    Zhang, T.T.4    Gibson, I.W.5    Miller, A.6    Alessi, D.R.7
  • 51
    • 85012005045 scopus 로고    scopus 로고
    • B-cell-intrinsic function of TAPP adaptors in controlling germinal center responses and autoantibody production in mice
    • Jayachandran, N., Landego, I., Hou, S., Alessi, D. R. and Marshall, A. J., B-cell-intrinsic function of TAPP adaptors in controlling germinal center responses and autoantibody production in mice. Eur. J. Immunol. 2017. 47: 280–290.
    • (2017) Eur. J. Immunol. , vol.47 , pp. 280-290
    • Jayachandran, N.1    Landego, I.2    Hou, S.3    Alessi, D.R.4    Marshall, A.J.5
  • 52
    • 0032055485 scopus 로고    scopus 로고
    • SHIP modulates immune receptor responses by regulating membrane association of Btk
    • Bolland, S., Pearse, R. N., Kurosaki, T. and Ravetch, J. V., SHIP modulates immune receptor responses by regulating membrane association of Btk. Immunity 1998. 8: 509–516.
    • (1998) Immunity , vol.8 , pp. 509-516
    • Bolland, S.1    Pearse, R.N.2    Kurosaki, T.3    Ravetch, J.V.4
  • 53
    • 0347364691 scopus 로고    scopus 로고
    • Two distinct waves of membrane-proximal B cell antigen receptor signaling differentially regulated by Src homology 2-containing inositol polyphosphate 5-phosphatase
    • Krahn, A. K., Ma, K., Hou, S., Duronio, V. and Marshall, A. J., Two distinct waves of membrane-proximal B cell antigen receptor signaling differentially regulated by Src homology 2-containing inositol polyphosphate 5-phosphatase. J. Immunol. 2004. 172: 331–339.
    • (2004) J. Immunol. , vol.172 , pp. 331-339
    • Krahn, A.K.1    Ma, K.2    Hou, S.3    Duronio, V.4    Marshall, A.J.5
  • 54
    • 10544219605 scopus 로고    scopus 로고
    • 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. J., Gout, I., Scaife, R., Margolis, R. L. et al., Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase. EMBO J. 1996. 15: 6241–6250.
    • (1996) EMBO J. , vol.15 , pp. 6241-6250
    • Salim, K.1    Bottomley, M.J.2    Querfurth, E.3    Zvelebil, M.J.4    Gout, I.5    Scaife, R.6    Margolis, R.L.7
  • 55
    • 0032055484 scopus 로고    scopus 로고
    • 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. O., Li, Z., Lin, S., Gout, I. et al., Phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: a target for SHIP-mediated inhibitory signals. EMBO J. 1998. 17: 1961–1972.
    • (1998) EMBO J. , vol.17 , pp. 1961-1972
    • Scharenberg, A.M.1    El-Hillal, O.2    Fruman, D.A.3    Beitz, L.O.4    Li, Z.5    Lin, S.6    Gout, I.7
  • 56
    • 0032533825 scopus 로고    scopus 로고
    • Role of the inositol phosphatase SHIP in B cell receptor-induced Ca2+ oscillatory response
    • Okada, H., Bolland, S., Hashimoto, A., Kurosaki, M., Kabuyama, Y., Iino, M., Ravetch, J. V. et al., Role of the inositol phosphatase SHIP in B cell receptor-induced Ca2+ oscillatory response. J. Immunol. 1998. 161: 5129–5132.
    • (1998) J. Immunol. , vol.161 , pp. 5129-5132
    • Okada, H.1    Bolland, S.2    Hashimoto, A.3    Kurosaki, M.4    Kabuyama, Y.5    Iino, M.6    Ravetch, J.V.7
  • 57
    • 0030975468 scopus 로고    scopus 로고
    • 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., Babic, I., Jirik, F. R. and Krystal, G., 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. J. Biol. Chem. 1997. 272: 8983–8988.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8983-8988
    • Liu, L.1    Damen, J.E.2    Hughes, M.R.3    Babic, I.4    Jirik, F.R.5    Krystal, G.6
  • 58
    • 0030923454 scopus 로고    scopus 로고
    • Activation-induced bi-dentate interaction of SHIP and Shc in B lymphocytes
    • Pradhan, M. and Coggeshall, K. M., Activation-induced bi-dentate interaction of SHIP and Shc in B lymphocytes. J. Cell. Biochem. 1997. 67: 32–42.
    • (1997) J. Cell. Biochem. , vol.67 , pp. 32-42
    • Pradhan, M.1    Coggeshall, K.M.2
  • 59
    • 0031065146 scopus 로고    scopus 로고
    • Negative signaling in B cells causes reduced Ras activity by reducing Shc-Grb2 interactions
    • Tridandapani, S., Chacko, G. W., Van Brocklyn, J. R. and Coggeshall, K. M., Negative signaling in B cells causes reduced Ras activity by reducing Shc-Grb2 interactions. J. Immunol. 1997. 158: 1125–1132.
    • (1997) J. Immunol. , vol.158 , pp. 1125-1132
    • Tridandapani, S.1    Chacko, G.W.2    Van Brocklyn, J.R.3    Coggeshall, K.M.4
  • 61
    • 20444375502 scopus 로고    scopus 로고
    • Src homology 2 domain-containing inositol-5-phosphatase 1 (SHIP1) negatively regulates TLR4-mediated LPS response primarily through a phosphatase activity- and PI-3K-independent mechanism
    • An, H., Xu, H., Zhang, M., Zhou, J., Feng, T., Qian, C., Qi, R. et al., Src homology 2 domain-containing inositol-5-phosphatase 1 (SHIP1) negatively regulates TLR4-mediated LPS response primarily through a phosphatase activity- and PI-3K-independent mechanism. Blood 2005. 105: 4685–4692.
    • (2005) Blood , vol.105 , pp. 4685-4692
    • An, H.1    Xu, H.2    Zhang, M.3    Zhou, J.4    Feng, T.5    Qian, C.6    Qi, R.7
  • 62
    • 84863995539 scopus 로고    scopus 로고
    • The inositol phosphatase SHIP-1 inhibits NOD2-induced NF-kappaB activation by disturbing the interaction of XIAP with RIP2
    • Conde, C., Rambout, X., Lebrun, M., Lecat, A., Di Valentin, E., Dequiedt, F., Piette, J. et al., The inositol phosphatase SHIP-1 inhibits NOD2-induced NF-kappaB activation by disturbing the interaction of XIAP with RIP2. PLoS One 2012. 7: e41005.
    • (2012) PLoS One , vol.7
    • Conde, C.1    Rambout, X.2    Lebrun, M.3    Lecat, A.4    Di Valentin, E.5    Dequiedt, F.6    Piette, J.7
  • 63
    • 79960406249 scopus 로고    scopus 로고
    • A balance of Bruton's tyrosine kinase and SHIP activation regulates B cell receptor cluster formation by controlling actin remodeling
    • Liu, C., Miller, H., Hui, K. L., Grooman, B., Bolland, S., Upadhyaya, A. and Song, W., A balance of Bruton's tyrosine kinase and SHIP activation regulates B cell receptor cluster formation by controlling actin remodeling. J. Immunol. 2011. 187: 230–239.
    • (2011) J. Immunol. , vol.187 , pp. 230-239
    • Liu, C.1    Miller, H.2    Hui, K.L.3    Grooman, B.4    Bolland, S.5    Upadhyaya, A.6    Song, W.7
  • 65
    • 79955013111 scopus 로고    scopus 로고
    • Evidence that the lipid phosphatase SHIP-1 regulates T lymphocyte morphology and motility
    • Harris, S. J., Parry, R. V., Foster, J. G., Blunt, M. D., Wang, A., Marelli-Berg, F., Westwick, J. et al., Evidence that the lipid phosphatase SHIP-1 regulates T lymphocyte morphology and motility. J. Immunol. 2011. 186: 4936–4945.
    • (2011) J. Immunol. , vol.186 , pp. 4936-4945
    • Harris, S.J.1    Parry, R.V.2    Foster, J.G.3    Blunt, M.D.4    Wang, A.5    Marelli-Berg, F.6    Westwick, J.7
  • 66
    • 15144353776 scopus 로고    scopus 로고
    • Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav
    • Han, J., Luby-Phelps, K., Das, B., Shu, X., Xia, Y., Mosteller, R. D., Krishna, U. M. et al., Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav. Science 1998. 279: 558–560.
    • (1998) Science , vol.279 , pp. 558-560
    • Han, J.1    Luby-Phelps, K.2    Das, B.3    Shu, X.4    Xia, Y.5    Mosteller, R.D.6    Krishna, U.M.7
  • 67
    • 0035951860 scopus 로고    scopus 로고
    • SHIP1, an SH2 domain containing polyinositol-5-phosphatase, regulates migration through two critical tyrosine residues and forms a novel signaling complex with DOK1 and CRKL
    • Sattler, M., Verma, S., Pride, Y. B., Salgia, R., Rohrschneider, L. R. and Griffin, J. D., SHIP1, an SH2 domain containing polyinositol-5-phosphatase, regulates migration through two critical tyrosine residues and forms a novel signaling complex with DOK1 and CRKL. J. Biol. Chem. 2001. 276: 2451–2458.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2451-2458
    • Sattler, M.1    Verma, S.2    Pride, Y.B.3    Salgia, R.4    Rohrschneider, L.R.5    Griffin, J.D.6
  • 68
    • 0041845112 scopus 로고    scopus 로고
    • SLP-76 coordinates Nck-dependent Wiskott-Aldrich syndrome protein recruitment with Vav-1/Cdc42-dependent Wiskott-Aldrich syndrome protein activation at the T cell-APC contact site
    • Zeng, R., Cannon, J. L., Abraham, R. T., Way, M., Billadeau, D. D., Bubeck-Wardenberg, J. and Burkhardt, J. K., SLP-76 coordinates Nck-dependent Wiskott-Aldrich syndrome protein recruitment with Vav-1/Cdc42-dependent Wiskott-Aldrich syndrome protein activation at the T cell-APC contact site. J. Immunol. 2003. 171: 1360–1368.
    • (2003) J. Immunol. , vol.171 , pp. 1360-1368
    • Zeng, R.1    Cannon, J.L.2    Abraham, R.T.3    Way, M.4    Billadeau, D.D.5    Bubeck-Wardenberg, J.6    Burkhardt, J.K.7
  • 69
    • 0033563167 scopus 로고    scopus 로고
    • The SH2-containing inositol-5'-phosphatase enhances LFA-1-mediated cell adhesion and defines two signaling pathways for LFA-1 activation
    • Rey-Ladino, J. A., Huber, M., Liu, L., Damen, J. E., Krystal, G. and Takei, F., The SH2-containing inositol-5'-phosphatase enhances LFA-1-mediated cell adhesion and defines two signaling pathways for LFA-1 activation. J. Immunol. 1999. 162: 5792–5799.
    • (1999) J. Immunol. , vol.162 , pp. 5792-5799
    • Rey-Ladino, J.A.1    Huber, M.2    Liu, L.3    Damen, J.E.4    Krystal, G.5    Takei, F.6
  • 70
    • 84930947441 scopus 로고    scopus 로고
    • Phosphatidylinositol (3,4) bisphosphate-specific phosphatases and effector proteins: a distinct branch of PI3K signaling
    • Li, H. and Marshall, A. J., Phosphatidylinositol (3,4) bisphosphate-specific phosphatases and effector proteins: a distinct branch of PI3K signaling. Cell. Signal. 2015. 27: 1789–1798.
    • (2015) Cell. Signal. , vol.27 , pp. 1789-1798
    • Li, H.1    Marshall, A.J.2
  • 71
    • 70349331525 scopus 로고    scopus 로고
    • Src homology 2 domain-containing inositol-5-phosphatase and CCAAT enhancer-binding protein beta are targeted by miR-155 in B cells of Emicro-MiR-155 transgenic mice
    • Costinean, S., Sandhu, S. K., Pedersen, I. M., Tili, E., Trotta, R., Perrotti, D., Ciarlariello, D. et al., Src homology 2 domain-containing inositol-5-phosphatase and CCAAT enhancer-binding protein beta are targeted by miR-155 in B cells of Emicro-MiR-155 transgenic mice. Blood 2009. 114: 1374–1382.
    • (2009) Blood , vol.114 , pp. 1374-1382
    • Costinean, S.1    Sandhu, S.K.2    Pedersen, I.M.3    Tili, E.4    Trotta, R.5    Perrotti, D.6    Ciarlariello, D.7
  • 73
    • 84897491448 scopus 로고    scopus 로고
    • MicroRNA 155 regulates Japanese encephalitis virus-induced inflammatory response by targeting Src homology 2-containing inositol phosphatase 1
    • Thounaojam, M. C., Kundu, K., Kaushik, D. K., Swaroop, S., Mahadevan, A., Shankar, S. K. and Basu, A., MicroRNA 155 regulates Japanese encephalitis virus-induced inflammatory response by targeting Src homology 2-containing inositol phosphatase 1. J. Virol. 2014. 88: 4798–4810.
    • (2014) J. Virol. , vol.88 , pp. 4798-4810
    • Thounaojam, M.C.1    Kundu, K.2    Kaushik, D.K.3    Swaroop, S.4    Mahadevan, A.5    Shankar, S.K.6    Basu, A.7
  • 74
    • 84902274347 scopus 로고    scopus 로고
    • MicroRNA-155 induction by Mycobacterium bovis BCG enhances ROS production through targeting SHIP1
    • Wang, J., Wu, M., Wen, J., Yang, K., Li, M., Zhan, X., Feng, L. et al., MicroRNA-155 induction by Mycobacterium bovis BCG enhances ROS production through targeting SHIP1. Mol. Immunol. 2014. 62: 29–36.
    • (2014) Mol. Immunol. , vol.62 , pp. 29-36
    • Wang, J.1    Wu, M.2    Wen, J.3    Yang, K.4    Li, M.5    Zhan, X.6    Feng, L.7
  • 75
    • 84991451244 scopus 로고    scopus 로고
    • MiR-155-regulated molecular network orchestrates cell fate in the innate and adaptive immune response to Mycobacterium tuberculosis
    • Rothchild, A. C., Sissons, J. R., Shafiani, S., Plaisier, C., Min, D., Mai, D., Gilchrist, M. et al., MiR-155-regulated molecular network orchestrates cell fate in the innate and adaptive immune response to Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 2016. 113: E6172–E6181.
    • (2016) Proc. Natl. Acad. Sci. USA , vol.113 , pp. E6172-E6181
    • Rothchild, A.C.1    Sissons, J.R.2    Shafiani, S.3    Plaisier, C.4    Min, D.5    Mai, D.6    Gilchrist, M.7
  • 76
    • 84958590325 scopus 로고    scopus 로고
    • miR-155 upregulation in dendritic cells is sufficient to break tolerance in vivo by negatively regulating SHIP1
    • Lind, E. F., Millar, D. G., Dissanayake, D., Savage, J. C., Grimshaw, N. K., Kerr, W. G. and Ohashi, P. S., miR-155 upregulation in dendritic cells is sufficient to break tolerance in vivo by negatively regulating SHIP1. J. Immunol. 2015. 195: 4632–4640.
    • (2015) J. Immunol. , vol.195 , pp. 4632-4640
    • Lind, E.F.1    Millar, D.G.2    Dissanayake, D.3    Savage, J.C.4    Grimshaw, N.K.5    Kerr, W.G.6    Ohashi, P.S.7
  • 77
    • 85013662743 scopus 로고    scopus 로고
    • MicroRNA-155 promotes G-CSF-induced mobilization of murine hematopoietic stem and progenitor cells via propagation of CXCL12 signaling
    • Itkin, T., Kumari, A., Schneider, E., Gur-Cohen, S., Ludwig, C., Brooks, R., Kollet, O. et al., MicroRNA-155 promotes G-CSF-induced mobilization of murine hematopoietic stem and progenitor cells via propagation of CXCL12 signaling. Leukemia 2017. 31: 1247–1250.
    • (2017) Leukemia , vol.31 , pp. 1247-1250
    • Itkin, T.1    Kumari, A.2    Schneider, E.3    Gur-Cohen, S.4    Ludwig, C.5    Brooks, R.6    Kollet, O.7
  • 78
    • 77951454047 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of SHIP promotes its proteasomal degradation
    • 402 e391
    • Ruschmann, J., Ho, V., Antignano, F., Kuroda, E., Lam, V., Ibaraki, M., Snyder, K. et al., Tyrosine phosphorylation of SHIP promotes its proteasomal degradation. Exp. Hematol. 2010. 38: 392–402, 402 e391.
    • (2010) Exp. Hematol. , vol.38 , pp. 392-402
    • Ruschmann, J.1    Ho, V.2    Antignano, F.3    Kuroda, E.4    Lam, V.5    Ibaraki, M.6    Snyder, K.7
  • 79
    • 84857013000 scopus 로고    scopus 로고
    • 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. et al., Therapeutic potential of SH2 domain-containing inositol-5'-phosphatase 1 (SHIP1) and SHIP2 inhibition in cancer. Mol. Med. 2012. 18: 65–75.
    • (2012) Mol. Med. , vol.18 , pp. 65-75
    • Fuhler, G.M.1    Brooks, R.2    Toms, B.3    Iyer, S.4    Gengo, E.A.5    Park, M.Y.6    Gumbleton, M.7
  • 80
    • 2642684541 scopus 로고    scopus 로고
    • 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. et al., Targeted disruption of SHIP leads to hemopoietic perturbations, lung pathology, and a shortened life span. Genes Dev. 1998. 12: 1610–1620.
    • (1998) Genes Dev. , vol.12 , pp. 1610-1620
    • Helgason, C.D.1    Damen, J.E.2    Rosten, P.3    Grewal, R.4    Sorensen, P.5    Chappel, S.M.6    Borowski, A.7
  • 81
    • 78651103582 scopus 로고    scopus 로고
    • SHIP deficiency causes Crohn's disease-like ileitis
    • Kerr, W. G., Park, M. Y., Maubert, M. and Engelman, R. W., SHIP deficiency causes Crohn's disease-like ileitis. Gut 2011. 60: 177–188.
    • (2011) Gut , vol.60 , pp. 177-188
    • Kerr, W.G.1    Park, M.Y.2    Maubert, M.3    Engelman, R.W.4
  • 82
    • 79959560604 scopus 로고    scopus 로고
    • Genetic segregation of inflammatory lung disease and autoimmune disease severity in SHIP-1-/- mice
    • Maxwell, M. J., Duan, M., Armes, J. E., Anderson, G. P., Tarlinton, D. M. and Hibbs, M. L., Genetic segregation of inflammatory lung disease and autoimmune disease severity in SHIP-1-/- mice. J. Immunol. 2011. 186: 7164–7175.
    • (2011) J. Immunol. , vol.186 , pp. 7164-7175
    • Maxwell, M.J.1    Duan, M.2    Armes, J.E.3    Anderson, G.P.4    Tarlinton, D.M.5    Hibbs, M.L.6
  • 83
    • 84941175989 scopus 로고    scopus 로고
    • Lineage-specific regulation of allergic airway inflammation by the lipid phosphatase Src homology 2 domain-containing inositol 5-phosphatase (SHIP-1)
    • e722
    • Gold, M. J., Hughes, M. R., Antignano, F., Hirota, J. A., Zaph, C. and McNagny, K. M., Lineage-specific regulation of allergic airway inflammation by the lipid phosphatase Src homology 2 domain-containing inositol 5-phosphatase (SHIP-1). J. Allergy. Clin. Immunol. 2015. 136: 725–736, e722.
    • (2015) J. Allergy. Clin. Immunol. , vol.136 , pp. 725-736
    • Gold, M.J.1    Hughes, M.R.2    Antignano, F.3    Hirota, J.A.4    Zaph, C.5    McNagny, K.M.6
  • 85
    • 79956349515 scopus 로고    scopus 로고
    • An ENU-induced mouse mutant of SHIP1 reveals a critical role of the stem cell isoform for suppression of macrophage activation
    • Nguyen, N. Y., Maxwell, M. J., Ooms, L. M., Davies, E. M., Hilton, A. A., Collinge, J. E., Hilton, D. J. et al., An ENU-induced mouse mutant of SHIP1 reveals a critical role of the stem cell isoform for suppression of macrophage activation. Blood 2011. 117: 5362–5371.
    • (2011) Blood , vol.117 , pp. 5362-5371
    • Nguyen, N.Y.1    Maxwell, M.J.2    Ooms, L.M.3    Davies, E.M.4    Hilton, A.A.5    Collinge, J.E.6    Hilton, D.J.7
  • 86
    • 33845932895 scopus 로고    scopus 로고
    • Src homology 2 domain-containing inositol 5-phosphatase 1 deficiency leads to a spontaneous allergic inflammation in the murine lung
    • Oh, S. Y., Zheng, T., Bailey, M. L., Barber, D. L., Schroeder, J. T., Kim, Y. K. and Zhu, Z., Src homology 2 domain-containing inositol 5-phosphatase 1 deficiency leads to a spontaneous allergic inflammation in the murine lung. J. Allergy. Clin. Immunol. 2007. 119: 123–131.
    • (2007) J. Allergy. Clin. Immunol. , vol.119 , pp. 123-131
    • Oh, S.Y.1    Zheng, T.2    Bailey, M.L.3    Barber, D.L.4    Schroeder, J.T.5    Kim, Y.K.6    Zhu, Z.7
  • 87
    • 68949112048 scopus 로고    scopus 로고
    • SHIP1 is a repressor of mast cell hyperplasia, cytokine production, and allergic inflammation in vivo
    • Haddon, D. J., Antignano, F., Hughes, M. R., Blanchet, M. R., Zbytnuik, L., Krystal, G. and McNagny, K. M., SHIP1 is a repressor of mast cell hyperplasia, cytokine production, and allergic inflammation in vivo. J. Immunol. 2009. 183: 228–236.
    • (2009) J. Immunol. , vol.183 , pp. 228-236
    • Haddon, D.J.1    Antignano, F.2    Hughes, M.R.3    Blanchet, M.R.4    Zbytnuik, L.5    Krystal, G.6    McNagny, K.M.7
  • 88
    • 33847281336 scopus 로고    scopus 로고
    • Relationship between spleen tyrosine kinase and phosphatidylinositol 5' phosphatase expression and secretion from human basophils in the general population
    • MacGlashan, D. W., Jr., Relationship between spleen tyrosine kinase and phosphatidylinositol 5' phosphatase expression and secretion from human basophils in the general population. J. Allergy. Clin. Immunol. 2007. 119: 626–633.
    • (2007) J. Allergy. Clin. Immunol. , vol.119 , pp. 626-633
    • MacGlashan, D.W.1
  • 89
    • 81955161811 scopus 로고    scopus 로고
    • Monophosphorylation of CD79a and CD79b ITAM motifs initiates a SHIP-1 phosphatase-mediated inhibitory signaling cascade required for B cell anergy
    • O'Neill, S. K., Getahun, A., Gauld, S. B., Merrell, K. T., Tamir, I., Smith, M. J., Dal Porto, J. M. et al., Monophosphorylation of CD79a and CD79b ITAM motifs initiates a SHIP-1 phosphatase-mediated inhibitory signaling cascade required for B cell anergy. Immunity 2011. 35: 746–756.
    • (2011) Immunity , vol.35 , pp. 746-756
    • O'Neill, S.K.1    Getahun, A.2    Gauld, S.B.3    Merrell, K.T.4    Tamir, I.5    Smith, M.J.6    Dal Porto, J.M.7
  • 90
    • 84939575389 scopus 로고    scopus 로고
    • B cell expression of the SH2-containing inositol 5-phosphatase (SHIP-1) is required to establish anergy to high affinity, proteinacious autoantigens
    • Akerlund, J., Getahun, A. and Cambier, J. C., B cell expression of the SH2-containing inositol 5-phosphatase (SHIP-1) is required to establish anergy to high affinity, proteinacious autoantigens. J. Autoimmun. 2015. 62: 45–54.
    • (2015) J. Autoimmun. , vol.62 , pp. 45-54
    • Akerlund, J.1    Getahun, A.2    Cambier, J.C.3
  • 91
    • 0033695963 scopus 로고    scopus 로고
    • Spontaneous autoimmune disease in Fc(gamma)RIIB-deficient mice results from strain-specific epistasis
    • Bolland, S. and Ravetch, J. V., Spontaneous autoimmune disease in Fc(gamma)RIIB-deficient mice results from strain-specific epistasis. Immunity 2000. 13: 277–285.
    • (2000) Immunity , vol.13 , pp. 277-285
    • Bolland, S.1    Ravetch, J.V.2
  • 92
    • 12844251399 scopus 로고    scopus 로고
    • Restoration of tolerance in lupus by targeted inhibitory receptor expression
    • McGaha, T. L., Sorrentino, B. and Ravetch, J. V., Restoration of tolerance in lupus by targeted inhibitory receptor expression. Science 2005. 307: 590–593.
    • (2005) Science , vol.307 , pp. 590-593
    • McGaha, T.L.1    Sorrentino, B.2    Ravetch, J.V.3
  • 93
    • 2442710233 scopus 로고    scopus 로고
    • A promoter haplotype of the immunoreceptor tyrosine-based inhibitory motif-bearing FcgammaRIIb alters receptor expression and associates with autoimmunity. I. Regulatory FCGR2B polymorphisms and their association with systemic lupus erythematosus
    • Su, K., Wu, J., Edberg, J. C., Li, X., Ferguson, P., Cooper, G. S., Langefeld, C. D. et al., A promoter haplotype of the immunoreceptor tyrosine-based inhibitory motif-bearing FcgammaRIIb alters receptor expression and associates with autoimmunity. I. Regulatory FCGR2B polymorphisms and their association with systemic lupus erythematosus. J. Immunol. 2004. 172: 7186–7191.
    • (2004) J. Immunol. , vol.172 , pp. 7186-7191
    • Su, K.1    Wu, J.2    Edberg, J.C.3    Li, X.4    Ferguson, P.5    Cooper, G.S.6    Langefeld, C.D.7
  • 94
    • 26444593959 scopus 로고    scopus 로고
    • FcgammaRIIB Ile232Thr transmembrane polymorphism associated with human systemic lupus erythematosus decreases affinity to lipid rafts and attenuates inhibitory effects on B cell receptor signaling
    • Kono, H., Kyogoku, C., Suzuki, T., Tsuchiya, N., Honda, H., Yamamoto, K., Tokunaga, K. et al., FcgammaRIIB Ile232Thr transmembrane polymorphism associated with human systemic lupus erythematosus decreases affinity to lipid rafts and attenuates inhibitory effects on B cell receptor signaling. Hum. Mol. Genet. 2005. 14: 2881–2892.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2881-2892
    • Kono, H.1    Kyogoku, C.2    Suzuki, T.3    Tsuchiya, N.4    Honda, H.5    Yamamoto, K.6    Tokunaga, K.7
  • 95
    • 77955373398 scopus 로고    scopus 로고
    • Protein phosphorylation and kinome profiling reveal altered regulation of multiple signaling pathways in B lymphocytes from patients with systemic lupus erythematosus
    • Taher, T. E., Parikh, K., Flores-Borja, F., Mletzko, S., Isenberg, D. A., Peppelenbosch, M. P. and Mageed, R. A., Protein phosphorylation and kinome profiling reveal altered regulation of multiple signaling pathways in B lymphocytes from patients with systemic lupus erythematosus. Arthritis Rheum. 2010. 62: 2412–2423.
    • (2010) Arthritis Rheum. , vol.62 , pp. 2412-2423
    • Taher, T.E.1    Parikh, K.2    Flores-Borja, F.3    Mletzko, S.4    Isenberg, D.A.5    Peppelenbosch, M.P.6    Mageed, R.A.7
  • 96
    • 84874196138 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase signaling pathway in normal and malignant B cells: activation mechanisms, regulation and impact on cellular functions
    • Pauls, S. D., Lafarge, S. T., Landego, I., Zhang, T. and Marshall, A. J., The phosphoinositide 3-kinase signaling pathway in normal and malignant B cells: activation mechanisms, regulation and impact on cellular functions. Front Immunol. 2012. 3: 224.
    • (2012) Front Immunol. , vol.3 , pp. 224
    • Pauls, S.D.1    Lafarge, S.T.2    Landego, I.3    Zhang, T.4    Marshall, A.J.5
  • 97
    • 79251553448 scopus 로고    scopus 로고
    • Inhibitor and activator: dual functions for SHIP in immunity and cancer
    • Kerr, W. G., Inhibitor and activator: dual functions for SHIP in immunity and cancer. Ann. NY Acad. Sci. 2011. 1217: 1–17.
    • (2011) Ann. NY Acad. Sci. , vol.1217 , pp. 1-17
    • Kerr, W.G.1
  • 100
    • 68649105674 scopus 로고    scopus 로고
    • Inactivation of SHIP1 in T-cell acute lymphoblastic leukemia due to mutation and extensive alternative splicing
    • Lo, T. C., Barnhill, L. M., Kim, Y., Nakae, E. A., Yu, A. L. and Diccianni, M. B., Inactivation of SHIP1 in T-cell acute lymphoblastic leukemia due to mutation and extensive alternative splicing. Leuk. Res. 2009. 33: 1562–1566.
    • (2009) Leuk. Res. , vol.33 , pp. 1562-1566
    • Lo, T.C.1    Barnhill, L.M.2    Kim, Y.3    Nakae, E.A.4    Yu, A.L.5    Diccianni, M.B.6
  • 101
    • 84865323036 scopus 로고    scopus 로고
    • Leukemia-associated mutations in SHIP1 inhibit its enzymatic activity, interaction with the GM-CSF receptor and Grb2, and its ability to inactivate PI3K/AKT signaling
    • Brauer, H., Strauss, J., Wegner, W., Muller-Tidow, C., Horstmann, M. and Jucker, M., Leukemia-associated mutations in SHIP1 inhibit its enzymatic activity, interaction with the GM-CSF receptor and Grb2, and its ability to inactivate PI3K/AKT signaling. Cell. Signal. 2012. 24: 2095–2101.
    • (2012) Cell. Signal. , vol.24 , pp. 2095-2101
    • Brauer, H.1    Strauss, J.2    Wegner, W.3    Muller-Tidow, C.4    Horstmann, M.5    Jucker, M.6
  • 103
    • 84929635151 scopus 로고    scopus 로고
    • Signalling thresholds and negative B-cell selection in acute lymphoblastic leukaemia
    • Chen, Z., Shojaee, S., Buchner, M., Geng, H., Lee, J. W., Klemm, L., Titz, B. et al., Signalling thresholds and negative B-cell selection in acute lymphoblastic leukaemia. Nature 2015. 521: 357–361.
    • (2015) Nature , vol.521 , pp. 357-361
    • Chen, Z.1    Shojaee, S.2    Buchner, M.3    Geng, H.4    Lee, J.W.5    Klemm, L.6    Titz, B.7
  • 104
    • 0033812025 scopus 로고    scopus 로고
    • Bilevel control of B-cell activation by the inositol 5-phosphatase SHIP
    • Brauweiler, A. M., Tamir, I. and Cambier, J. C., Bilevel control of B-cell activation by the inositol 5-phosphatase SHIP. Immunol. Rev. 2000. 176: 69–74.
    • (2000) Immunol. Rev. , vol.176 , pp. 69-74
    • Brauweiler, A.M.1    Tamir, I.2    Cambier, J.C.3
  • 105
    • 0036033109 scopus 로고    scopus 로고
    • SHIP represses mast cell activation and reveals that IgE alone triggers signaling pathways which enhance normal mast cell survival
    • Kalesnikoff, J., Lam, V. and Krystal, G., SHIP represses mast cell activation and reveals that IgE alone triggers signaling pathways which enhance normal mast cell survival. Mol. Immunol. 2002. 38: 1201–1206.
    • (2002) Mol. Immunol. , vol.38 , pp. 1201-1206
    • Kalesnikoff, J.1    Lam, V.2    Krystal, G.3
  • 106
    • 34547402441 scopus 로고    scopus 로고
    • 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. and Bolland, S., T cell-specific deletion of the inositol phosphatase SHIP reveals its role in regulating Th1/Th2 and cytotoxic responses. Proc. Natl. Acad. Sci. USA 2007. 104: 11382–11387.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 11382-11387
    • Tarasenko, T.1    Kole, H.K.2    Chi, A.W.3    Mentink-Kane, M.M.4    Wynn, T.A.5    Bolland, S.6
  • 107
    • 84863995822 scopus 로고    scopus 로고
    • Lineage extrinsic and intrinsic control of immunoregulatory cell numbers by SHIP
    • Collazo, M. M., Paraiso, K. H., Park, M. Y., Hazen, A. L. and Kerr, W. G., Lineage extrinsic and intrinsic control of immunoregulatory cell numbers by SHIP. Eur. J. Immunol. 2012. 42: 1785–1795.
    • (2012) Eur. J. Immunol. , vol.42 , pp. 1785-1795
    • Collazo, M.M.1    Paraiso, K.H.2    Park, M.Y.3    Hazen, A.L.4    Kerr, W.G.5
  • 110
  • 111
    • 33750530393 scopus 로고    scopus 로고
    • T cell receptor for antigen induces linker for activation of T cell-dependent activation of a negative signaling complex involving Dok-2, SHIP-1, and Grb-2
    • Dong, S., Corre, B., Foulon, E., Dufour, E., Veillette, A., Acuto, O. and Michel, F., T cell receptor for antigen induces linker for activation of T cell-dependent activation of a negative signaling complex involving Dok-2, SHIP-1, and Grb-2. J. Exp. Med. 2006. 203: 2509–2518.
    • (2006) J. Exp. Med. , vol.203 , pp. 2509-2518
    • Dong, S.1    Corre, B.2    Foulon, E.3    Dufour, E.4    Veillette, A.5    Acuto, O.6    Michel, F.7
  • 112
    • 77950937721 scopus 로고    scopus 로고
    • SHIP-1 inhibits CD95/APO-1/Fas-induced apoptosis in primary T lymphocytes and T leukemic cells by promoting CD95 glycosylation independently of its phosphatase activity
    • Charlier, E., Conde, C., Zhang, J., Deneubourg, L., Di Valentin, E., Rahmouni, S., Chariot, A. et al., SHIP-1 inhibits CD95/APO-1/Fas-induced apoptosis in primary T lymphocytes and T leukemic cells by promoting CD95 glycosylation independently of its phosphatase activity. Leukemia 2010. 24: 821–832.
    • (2010) Leukemia , vol.24 , pp. 821-832
    • Charlier, E.1    Conde, C.2    Zhang, J.3    Deneubourg, L.4    Di Valentin, E.5    Rahmouni, S.6    Chariot, A.7
  • 113
    • 84924533900 scopus 로고    scopus 로고
    • SHIP1 intrinsically regulates NK cell signaling and education, resulting in tolerance of an MHC class I-mismatched bone marrow graft in mice
    • Gumbleton, M., Vivier, E. and Kerr, W. G., SHIP1 intrinsically regulates NK cell signaling and education, resulting in tolerance of an MHC class I-mismatched bone marrow graft in mice. J. Immunol. 2015. 194: 2847–2854.
    • (2015) J. Immunol. , vol.194 , pp. 2847-2854
    • Gumbleton, M.1    Vivier, E.2    Kerr, W.G.3
  • 115
    • 84873726325 scopus 로고    scopus 로고
    • Recruitment of Grb2 and SHIP1 by the ITT-like motif of TIGIT suppresses granule polarization and cytotoxicity of NK cells
    • Liu, S., Zhang, H., Li, M., Hu, D., Li, C., Ge, B., Jin, B. et al., Recruitment of Grb2 and SHIP1 by the ITT-like motif of TIGIT suppresses granule polarization and cytotoxicity of NK cells. Cell. Death. Differ. 2013. 20: 456–464.
    • (2013) Cell. Death. Differ. , vol.20 , pp. 456-464
    • Liu, S.1    Zhang, H.2    Li, M.3    Hu, D.4    Li, C.5    Ge, B.6    Jin, B.7
  • 116
  • 117
    • 40049084080 scopus 로고    scopus 로고
    • Inappropriate recruitment and activity by the Src homology region 2 domain-containing phosphatase 1 (SHP1) is responsible for receptor dominance in the SHIP-deficient NK cell
    • Wahle, J. A., Paraiso, K. H., Kendig, R. D., Lawrence, H. R., Chen, L., Wu, J. and Kerr, W. G., Inappropriate recruitment and activity by the Src homology region 2 domain-containing phosphatase 1 (SHP1) is responsible for receptor dominance in the SHIP-deficient NK cell. J. Immunol. 2007. 179: 8009–8015.
    • (2007) J. Immunol. , vol.179 , pp. 8009-8015
    • Wahle, J.A.1    Paraiso, K.H.2    Kendig, R.D.3    Lawrence, H.R.4    Chen, L.5    Wu, J.6    Kerr, W.G.7
  • 119
    • 84865363457 scopus 로고    scopus 로고
    • Myeloid cell-specific expression of Ship1 regulates IL-12 production and immunity to helminth infection
    • Hadidi, S., Antignano, F., Hughes, M. R., Wang, S. K., Snyder, K., Sammis, G. M., Kerr, W. G. et al., Myeloid cell-specific expression of Ship1 regulates IL-12 production and immunity to helminth infection. Mucosal Immunol. 2012. 5: 535–543.
    • (2012) Mucosal Immunol. , vol.5 , pp. 535-543
    • Hadidi, S.1    Antignano, F.2    Hughes, M.R.3    Wang, S.K.4    Snyder, K.5    Sammis, G.M.6    Kerr, W.G.7
  • 120
    • 84953839980 scopus 로고    scopus 로고
    • Dendritic-cell expression of Ship1 regulates Th2 immunity to helminth infection in mice
    • Gold, M. J., Antignano, F., Hughes, M. R., Zaph, C. and McNagny, K. M., Dendritic-cell expression of Ship1 regulates Th2 immunity to helminth infection in mice. Eur. J. Immunol. 2016. 46: 122–130.
    • (2016) Eur. J. Immunol. , vol.46 , pp. 122-130
    • Gold, M.J.1    Antignano, F.2    Hughes, M.R.3    Zaph, C.4    McNagny, K.M.5
  • 121
    • 84945895385 scopus 로고    scopus 로고
    • Synthesis and initial evaluation of quinoline-based inhibitors of the SH2-containing inositol 5'-phosphatase (SHIP)
    • Russo, C. M., Adhikari, A. A., Wallach, D. R., Fernandes, S., Balch, A. N., Kerr, W. G. and Chisholm, J. D., Synthesis and initial evaluation of quinoline-based inhibitors of the SH2-containing inositol 5'-phosphatase (SHIP). Bioorg. Med. Chem. Lett. 2015. 25: 5344–5348.
    • (2015) Bioorg. Med. Chem. Lett. , vol.25 , pp. 5344-5348
    • Russo, C.M.1    Adhikari, A.A.2    Wallach, D.R.3    Fernandes, S.4    Balch, A.N.5    Kerr, W.G.6    Chisholm, J.D.7
  • 122
    • 84901846034 scopus 로고    scopus 로고
    • Discovery and development of small molecule SHIP phosphatase modulators
    • Viernes, D. R., Choi, L. B., Kerr, W. G. and Chisholm, J. D., Discovery and development of small molecule SHIP phosphatase modulators. Med. Res. Rev. 2014. 34: 795–824.
    • (2014) Med. Res. Rev. , vol.34 , pp. 795-824
    • Viernes, D.R.1    Choi, L.B.2    Kerr, W.G.3    Chisholm, J.D.4
  • 123
    • 84874408370 scopus 로고    scopus 로고
    • Characterization of AQX-1125, a small-molecule SHIP1 activator: part 1. Effects on inflammatory cell activation and chemotaxis in vitro and pharmacokinetic characterization in vivo
    • Stenton, G. R., Mackenzie, L. F., Tam, P., Cross, J. L., Harwig, C., Raymond, J., Toews, J. et al., Characterization of AQX-1125, a small-molecule SHIP1 activator: part 1. Effects on inflammatory cell activation and chemotaxis in vitro and pharmacokinetic characterization in vivo. Br. J. Pharmacol. 2013. 168: 1506–1518.
    • (2013) Br. J. Pharmacol. , vol.168 , pp. 1506-1518
    • Stenton, G.R.1    Mackenzie, L.F.2    Tam, P.3    Cross, J.L.4    Harwig, C.5    Raymond, J.6    Toews, J.7
  • 124
    • 84874449540 scopus 로고    scopus 로고
    • Characterization of AQX-1125, a small-molecule SHIP1 activator: part 2. Efficacy studies in allergic and pulmonary inflammation models in vivo
    • Stenton, G. R., Mackenzie, L. F., Tam, P., Cross, J. L., Harwig, C., Raymond, J., Toews, J. et al., Characterization of AQX-1125, a small-molecule SHIP1 activator: part 2. Efficacy studies in allergic and pulmonary inflammation models in vivo. Br. J. Pharmacol. 2013. 168: 1519–1529.
    • (2013) Br. J. Pharmacol. , vol.168 , pp. 1519-1529
    • Stenton, G.R.1    Mackenzie, L.F.2    Tam, P.3    Cross, J.L.4    Harwig, C.5    Raymond, J.6    Toews, J.7
  • 125
    • 84906237265 scopus 로고    scopus 로고
    • The effects of the novel SHIP1 activator AQX-1125 on allergen-induced responses in mild-to-moderate asthma
    • Leaker, B. R., Barnes, P. J., O'Connor, B. J., Ali, F. Y., Tam, P., Neville, J., Mackenzie, L. F. et al., The effects of the novel SHIP1 activator AQX-1125 on allergen-induced responses in mild-to-moderate asthma. Clin. Exp. Allergy 2014. 44: 1146–1153.
    • (2014) Clin. Exp. Allergy , vol.44 , pp. 1146-1153
    • Leaker, B.R.1    Barnes, P.J.2    O'Connor, B.J.3    Ali, F.Y.4    Tam, P.5    Neville, J.6    Mackenzie, L.F.7
  • 126
    • 84992389998 scopus 로고    scopus 로고
    • A phase II study of the efficacy and safety of the novel oral SHIP1 activator AQX-1125 in subjects with moderate to severe interstitial cystitis/bladder pain syndrome
    • Nickel, J. C., Egerdie, B., Davis, E., Evans, R., Mackenzie, L. and Shrewsbury, S. B., A phase II study of the efficacy and safety of the novel oral SHIP1 activator AQX-1125 in subjects with moderate to severe interstitial cystitis/bladder pain syndrome. J. Urol. 2016. 196: 747–754.
    • (2016) J. Urol. , vol.196 , pp. 747-754
    • Nickel, J.C.1    Egerdie, B.2    Davis, E.3    Evans, R.4    Mackenzie, L.5    Shrewsbury, S.B.6
  • 128
    • 77951624382 scopus 로고    scopus 로고
    • SHIP1 inhibition increases immunoregulatory capacity and triggers apoptosis of hematopoietic cancer cells
    • Brooks, R., Fuhler, G. M., Iyer, S., Smith, M. J., Park, M. Y., Paraiso, K. H., Engelman, R. W. et al., SHIP1 inhibition increases immunoregulatory capacity and triggers apoptosis of hematopoietic cancer cells. J. Immunol. 2010. 184: 3582–3589.
    • (2010) J. Immunol. , vol.184 , pp. 3582-3589
    • Brooks, R.1    Fuhler, G.M.2    Iyer, S.3    Smith, M.J.4    Park, M.Y.5    Paraiso, K.H.6    Engelman, R.W.7
  • 130
    • 85020158211 scopus 로고    scopus 로고
    • A small-molecule inhibitor of SHIP1 reverses age- and diet-associated obesity and metabolic syndrome
    • Srivastava, N., Iyer, S., Sudan, R., Youngs, C., Engelman, R. W., Howard, K. T., Russo, C. M. et al., A small-molecule inhibitor of SHIP1 reverses age- and diet-associated obesity and metabolic syndrome. JCI Insight 2016. 1: e88544.
    • (2016) JCI Insight , vol.1
    • Srivastava, N.1    Iyer, S.2    Sudan, R.3    Youngs, C.4    Engelman, R.W.5    Howard, K.T.6    Russo, C.M.7
  • 132
    • 39149097499 scopus 로고    scopus 로고
    • PI(3,4,5)P3 and PI(3,4)P2 levels correlate with PKB/akt phosphorylation at Thr308 and Ser473, respectively; PI(3,4)P2 levels determine PKB activity
    • Ma, K., Cheung, S. M., Marshall, A. J. and Duronio, V., PI(3,4,5)P3 and PI(3,4)P2 levels correlate with PKB/akt phosphorylation at Thr308 and Ser473, respectively; PI(3,4)P2 levels determine PKB activity. Cell. Signal. 2008. 20: 684–694.
    • (2008) Cell. Signal. , vol.20 , pp. 684-694
    • Ma, K.1    Cheung, S.M.2    Marshall, A.J.3    Duronio, V.4
  • 133
    • 0036310638 scopus 로고    scopus 로고
    • TAPP1 and TAPP2 are targets of phosphatidylinositol 3-kinase signaling in B cells: sustained plasma membrane recruitment triggered by the B-cell antigen receptor
    • Marshall, A. J., Krahn, A. K., Ma, K., Duronio, V. and Hou, S., TAPP1 and TAPP2 are targets of phosphatidylinositol 3-kinase signaling in B cells: sustained plasma membrane recruitment triggered by the B-cell antigen receptor. Mol. Cell Biol. 2002. 22: 5479–5491.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 5479-5491
    • Marshall, A.J.1    Krahn, A.K.2    Ma, K.3    Duronio, V.4    Hou, S.5
  • 134
    • 0035282732 scopus 로고    scopus 로고
    • SHIP's C-terminus is essential for its hydrolysis of PIP3 and inhibition of mast cell degranulation
    • Damen, J. E., Ware, M. D., Kalesnikoff, J., Hughes, M. R. and Krystal, G., SHIP's C-terminus is essential for its hydrolysis of PIP3 and inhibition of mast cell degranulation. Blood 2001. 97: 1343–1351.
    • (2001) Blood , vol.97 , pp. 1343-1351
    • Damen, J.E.1    Ware, M.D.2    Kalesnikoff, J.3    Hughes, M.R.4    Krystal, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.