메뉴 건너뛰기




Volumn 48, Issue 46, 2009, Pages 11075-11083

The SH2 domains of inositol polyphosphate 5-phosphatases SHIP1 and SHIP2 have similar ligand specificity but different binding kinetics

Author keywords

[No Author keywords available]

Indexed keywords

BINDING AFFINITIES; BINDING BEHAVIORS; BINDING KINETICS; CIS-TRANS ISOMERIZATION; CONFORMATIONAL ISOMERS; CONSENSUS SEQUENCE; DIPHOSPHATES; DISSOCIATION RATES; IN-VIVO; KINETIC STUDY; LIGAND SPECIFICITY; PEPTIDE LIBRARY; PHOSPHATIDYLINOSITOL; POLYPHOSPHATES; POTENTIAL MECHANISM; PROLINE RESIDUES; PROLYL BONDS; SEQUENCE IDENTITY; SEQUENCE SPECIFICITY; SH2 DOMAIN; SITE DIRECTED MUTAGENESIS; SPECIFICITY PROFILE; SURFACE PLASMONS; TISSUE DISTRIBUTIONS; TRANS CONFIGURATION; TRIPHOSPHATE; TWO DOMAINS;

EID: 72749093773     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9012462     Document Type: Article
Times cited : (21)

References (47)
  • 1
    • 0024453294 scopus 로고
    • Inositol phosphates and cell signaling
    • Berridge, M. J., and Irvine, R. F. (1989) Inositol phosphates and cell signaling. Nature 341, 197-205.
    • (1989) Nature , vol.341 , pp. 197-205
    • Berridge, M.J.1    Irvine, R.F.2
  • 2
    • 0029993517 scopus 로고    scopus 로고
    • Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation
    • James, S. R., Downes, C. P., Gigg, R., Grove, S. J., Holmes, A. B., and Alessi, D. R. (1996) Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation. Biochem. J. 315, 709-713.
    • (1996) Biochem. J. , vol.315 , pp. 709-713
    • James, S.R.1    Downes, C.P.2    Gigg, R.3    Grove, S.J.4    Holmes, A.B.5    Alessi, D.R.6
  • 4
  • 6
    • 0036033109 scopus 로고    scopus 로고
    • SHIP represses mast cell activation and reveals that IgE alone triggers signaling pathways which enhance normalmast cell survival
    • Kalesnikoff, J., Lam, V., and Krystal, G. (2002) SHIP represses mast cell activation and reveals that IgE alone triggers signaling pathways which enhance normalmast cell survival. Mol. Immunol. 38, 1201-1206.
    • (2002) Mol. Immunol. , vol.38 , pp. 1201-1206
    • Kalesnikoff, J.1    Lam, V.2    Krystal, G.3
  • 7
    • 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. (1999) SHIP is a negative regulator of growth factor receptor-mediated PKB/Akt activation and myeloid cell survival. Genes Dev. 13, 786-791. (Pubitemid 29169837)
    • (1999) Genes and Development , vol.13 , Issue.7 , 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
  • 10
    • 30444450889 scopus 로고    scopus 로고
    • The inositol phosphatase SHIP-2 down regulates FcγR-mediated phagocytosis in murine macrophages independently of SHIP-1
    • Ai, J., Maturu, A., Johnson, W., Wang, Y., Marsh, C. B., and Tridandapani, S. (2005) The inositol phosphatase SHIP-2 down regulates FcγR-mediated phagocytosis in murine macrophages independently of SHIP-1. Blood 107, 813-820.
    • (2005) Blood , vol.107 , pp. 813-820
    • Ai, J.1    Maturu, A.2    Johnson, W.3    Wang, Y.4    Marsh, C.B.5    Tridandapani, S.6
  • 11
    • 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. (1997) The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood. Blood 89, 1876-1885. (Pubitemid 27132101)
    • (1997) Blood , vol.89 , Issue.6 , 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
  • 12
    • 0032523199 scopus 로고    scopus 로고
    • The SH2-containing inositol polyphosphate 5-phosphatase, ship, is expressed during hematopoiesis and spermatogenesis
    • Liu, Q., Shalaby, F., Jones, J., Bouchard, D., and Dumont, D. J. (1998) The SH2-containing inositol polyphosphate 5-phosphatase, SHIP, is expressed during hematopoiesis and spermatogenesis. Blood 91, 2753-2759. (Pubitemid 28227525)
    • (1998) Blood , vol.91 , Issue.8 , pp. 2753-2759
    • Liu, Q.1    Shalaby, F.2    Jones, J.3    Bouchard, D.4    Dumont, D.J.5
  • 13
    • 0031590449 scopus 로고    scopus 로고
    • Identification of a second SH2-domain-conatining protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP
    • Pesesse, X., Deleu, S., De Smedt, F., Drayer, L., and Erneux, C. (1997) Identification of a second SH2-domain-conatining protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP. Biochem. Biophys. Res. Commun. 239, 697-700.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 697-700
    • Pesesse, X.1    Deleu, S.2    De Smedt, F.3    Drayer, L.4    Erneux, C.5
  • 14
    • 0033379824 scopus 로고    scopus 로고
    • The mouse SHIP2 (Inppl1) gene: Complementary DNA, genomic structure, promoter analysis, and gene expression in the embryo and adult mouse
    • DOI 10.1006/geno.1999.5995
    • Schurmans, S., Carrio, R., Behrends, J., Pouillon, V., Merino, J., and Clement, S. (1999) The mouse SHIP2 (Inppl1) gene: complementary DNA, genomic structure, promoter analysis, and gene expression in the embryo and adult mouse. Genomics 62, 260-271. (Pubitemid 30053942)
    • (1999) Genomics , vol.62 , Issue.2 , pp. 260-271
    • Schurmans, S.1    Carrio, R.2    Behrends, J.3    Pouillon, V.4    Merino, J.5    Clement, S.6
  • 15
    • 0042744852 scopus 로고    scopus 로고
    • SHIP-2 forms a tetrameric complex with filamin, actin, and GPIb-IX-V: Localization of SHIP-2 to the activated platelet actin cytoskeleton
    • DOI 10.1182/blood-2002-09-2897
    • Dyson, J. M., Munday, A. D., Kong, A. M., Huysmans, R. D., Matzaris, M., Layton, M. J., Nandurkar, H. H., Berndt, M. C., and Mitchell, C. A. (2003) SHIP-2 forms a tetrameric complex with filamin, actin, and GPIb-IX-V: localization of SHIP-2 to the activated platelet actin cytoskeleton. Blood 102, 940-948. (Pubitemid 36917787)
    • (2003) Blood , vol.102 , Issue.3 , pp. 940-948
    • Dyson, J.M.1    Munday, A.D.2    Kong, A.M.3    Huysmans, R.D.4    Matzaris, M.5    Layton, M.J.6    Nandurkar, H.H.7    Berndt, M.C.8    Mitchell, C.A.9
  • 16
    • 0345688084 scopus 로고    scopus 로고
    • SH2-containing inositol 5-phosphatases 1 and 2 in blood platelets: Their interactions and roles in the control of phosphatidylinositol 3,4,5-trisphosphate levels
    • Giuriato, S., Pesesse, X., Bodin, S., Sasaki, T., Viala, C., Marion, E., Penninger, J., Schurmans, S., Erneux, C., and Payrastre, B. (2003) SH2-containing inositol 5-phosphatases 1 and 2 in blood platelets: their interactions and roles in the control of phosphatidylinositol 3,4,5-trisphosphate levels. Biochem. J. 376, 199-207.
    • (2003) Biochem. J. , vol.376 , pp. 199-207
    • Giuriato, S.1    Pesesse, X.2    Bodin, S.3    Sasaki, T.4    Viala, C.5    Marion, E.6    Penninger, J.7    Schurmans, S.8    Erneux, C.9    Payrastre, B.10
  • 17
    • 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-trisphosphate 5-phosphatase
    • Damen, J. E., Liu, L., Rosten, P., Humphries, R. K., Jefferson, A. B., Majerus, P. W., and Krystal, G. (1996) The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase. Proc. Natl. Acad. Sci. U.S.A. 93, 1689-1693.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 18
    • 0034741604 scopus 로고    scopus 로고
    • Co-clustering of Fcγ and B cell receptors induces dephosphorylation of the Grb2-associated binder 1 docking protein
    • Koncz, G., Toth, G. K., Bokonyi, G., Keri, G., Pecht, I., Medgyesi, D., Gergely, J., and Sarmay, G. (2001) Co-clustering of Fcγ and B cell receptors induces dephosphorylation of the Grb2-associated binder 1 docking protein. Eur. J. Biochem. 268, 3898-3906.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3898-3906
    • Koncz, G.1    Toth, G.K.2    Bokonyi, G.3    Keri, G.4    Pecht, I.5    Medgyesi, D.6    Gergely, J.7    Sarmay, G.8
  • 19
    • 0035044042 scopus 로고    scopus 로고
    • Scaffolding protein Gab2 mediates differentiation signaling downstream of Fms receptor tyrosine kinase
    • Liu, Y., Jenkins, B., Shin, J. L., and Rohrschneider, L. R. (2001) Scaffolding protein Gab2 mediates differentiation signaling downstream of Fms receptor tyrosine kinase. Mol. Cell. Biol. 21, 3047-3056.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3047-3056
    • Liu, Y.1    Jenkins, B.2    Shin, J.L.3    Rohrschneider, L.R.4
  • 20
    • 0034669936 scopus 로고    scopus 로고
    • Stem cell factor induces phosphatidylinositol 3'-kinase-dependent Lyn/Tec/Dok-1 complex formation in hematopoietic cells
    • van Dijk, T. B., Akker, E., Amelsvoort, M. P., Mano, H., Lowenberg, B., and von Lindern, M. (2000) Stem cell factor induces phosphatidylinositol 3′-kinase-dependent Lyn/Tec/Dok-1 complex formation in hematopoietic cells. Blood 96, 3406-3413. (Pubitemid 30836319)
    • (2000) Blood , vol.96 , Issue.10 , pp. 3406-3413
    • Van Dijk, T.B.1    Van Den Akker, E.2    Parren-Van Amelsvoort, M.3    Mano, H.4    Lowenberg, B.5    Von Lindern, M.6
  • 21
    • 0034060769 scopus 로고    scopus 로고
    • The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the Dok1 phosphoprotein in Bcr-Abl transformed cells
    • DOI 10.1016/S0898-6568(00)00073-5, PII S0898656800000735
    • Dunant, N. M., Wisniewski, D., Strife, A., Clarkson, B., and Resh, M. D. (2000) The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the Dok1 phosphoprotein in Bcr-Abl transformed cells. Cell. Signalling 12, 317-326. (Pubitemid 30261547)
    • (2000) Cellular Signalling , vol.12 , Issue.5 , pp. 317-326
    • Dunant, N.M.1    Wisniewski, D.2    Strife, A.3    Clarkson, B.4    Resh, M.D.5
  • 22
    • 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. (2000) Dok-3, a novel adapter molecule involved in the negative regulation of immunoreceptor signaling. Mol. Cell. Biol. 20, 2743-2754.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2743-2754
    • Lemay, S.1    Davidson, D.2    Latour, S.3    Veillette, A.4
  • 23
    • 0030892128 scopus 로고    scopus 로고
    • Interleukin-3 induces the association of the inositol 5-phosphatase SHIP with SHP2
    • Liu, L., Damen, J. E., Ware, M. D., and Krystal, G. (1997) Interleukin-3 induces the association of the inositol 5-phosphatase SHIP with SHP2. J. Biol. Chem. 272, 10998-11001.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10998-11001
    • Liu, L.1    Damen, J.E.2    Ware, M.D.3    Krystal, G.4
  • 24
    • 0030663034 scopus 로고    scopus 로고
    • 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
    • Sattler, M., Salgia, R., Shrikhande, G., Verma, S., Choi, J. L., Rohrschneider, L. R., and Griffin, J. D. (1997) 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. Oncogene 15, 2379-2384. (Pubitemid 27496988)
    • (1997) Oncogene , vol.15 , Issue.19 , pp. 2379-2384
    • Sattler, M.1    Salgia, R.2    Shrikhande, G.3    Verma, S.4    Choi, J.-L.5    Rohrschneider, L.R.6    Griffin, J.D.7
  • 25
    • 33745132197 scopus 로고    scopus 로고
    • Src homology 2 (SH2)-containing 5′-inositol phosphatase localizes to podosomes, and the SH2 domain is implicated in the attenuation of bone resorption in osteoclasts
    • DOI 10.1210/en.2005-1309
    • Yogo, K., Mizutamari, M., Mishima, K., Takenouchi, H., Ishida-Kitagawa, N., Sasaki, T., and Takeya, T. (2006) Src homology 2 (SH2)-containing 5′-inositol phosphatase localizes to podosomes, and the SH2 domain is implicated in the attenuation of bone resorption in osteoclasts. Endocrinology 147, 3307-3317. (Pubitemid 43901121)
    • (2006) Endocrinology , vol.147 , Issue.7 , pp. 3307-3317
    • Yogo, K.1    Mizutamari, M.2    Mishima, K.3    Takenouchi, H.4    Ishida-Kitagawa, N.5    Sasaki, T.6    Takeya, T.7
  • 26
    • 44849107712 scopus 로고    scopus 로고
    • Non-T cell activation linker promotes mast cell survival by dampening the recruitment of SHIP1 by linker for activation of T cells
    • Roget, K., Malissen, M., Malbec, O., Malissen, B., and Daeron, M. (2008) Non-T cell activation linker promotes mast cell survival by dampening the recruitment of SHIP1 by linker for activation of T cells. J. Immunol. 180, 3689-3698.
    • (2008) J. Immunol. , vol.180 , pp. 3689-3698
    • Roget, K.1    Malissen, M.2    Malbec, O.3    Malissen, B.4    Daeron, M.5
  • 27
    • 0035146370 scopus 로고    scopus 로고
    • Cas adapter protein and regulates cellular adhesion and spreading
    • Cas adapter protein and regulates cellular adhesion and spreading. Mol. Cell. Biol. 21, 1416-1428.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1416-1428
    • Prasad, N.1    Topping, R.S.2    Decker, S.J.3
  • 28
    • 0029835940 scopus 로고    scopus 로고
    • Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor FcγRIIB
    • DOI 10.1038/383263a0
    • Ono, M., Bolland, S., Tempst, P., and Ravetch, J. V. (1996) Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor Fc(gamma)RIIB. Nature 383, 263-266. (Pubitemid 26317676)
    • (1996) Nature , vol.383 , Issue.6597 , pp. 263-266
    • Ono, M.1    Bolland, S.2    Tempst, P.3    Ravetch, J.V.4
  • 29
    • 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., Burn, P., and Kochan, J. P. (1996) The inositol 5′-phosphatase SHIP binds to immunoreceptor signaling motifs and responds to high affinity IgE receptor aggregation. J. Biol. Chem. 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    Burn, P.8    Kochan, J.P.9
  • 30
    • 0030946792 scopus 로고    scopus 로고
    • The negative signaling molecule SH2 domain-containing inositolpolyphosphate 5-phosphatase (SHIP) binds to the tyrosine-phosphorylated beta subunit of the high affinity IgE receptor
    • Kimura, T., Sakamoto, H., Appella, E., and Siraganian, R. P. (1997) The negative signaling molecule SH2 domain-containing inositolpolyphosphate 5-phosphatase (SHIP) binds to the tyrosine-phosphorylated beta subunit of the high affinity IgE receptor. J. Biol. Chem. 272, 13991-13996.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13991-13996
    • Kimura, T.1    Sakamoto, H.2    Appella, E.3    Siraganian, R.P.4
  • 31
    • 0034635485 scopus 로고    scopus 로고
    • The SH2 inositol 5-phosphatase Ship1 is recruited in an SH2-dependent manner to the erythropoietin receptor
    • Mason, J. M., Beattie, B. K., Liu, Q., Dumont, D. J., and Barber, D. L. (2000) The SH2 inositol 5-phosphatase Ship1 is recruited in an SH2-dependent manner to the erythropoietin receptor. J. Biol. Chem. 275, 4398-4406.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4398-4406
    • Mason, J.M.1    Beattie, B.K.2    Liu, Q.3    Dumont, D.J.4    Barber, D.L.5
  • 32
    • 0242632619 scopus 로고    scopus 로고
    • The SH2 domain containing inositol 5-phosphatase SHIP2 associates to the immunoreceptor tyrosine-based inhibition motif of FcγRIIB in B cells under negative signaling
    • Muraille, E., Bruhns, P., Pesesse, X., Daeron, M., and Erneux, C. (2000) The SH2 domain containing inositol 5-phosphatase SHIP2 associates to the immunoreceptor tyrosine-based inhibition motif of FcγRIIB in B cells under negative signaling. Immunol. Lett. 72, 7-15.
    • (2000) Immunol. Lett. , vol.72 , pp. 7-15
    • Muraille, E.1    Bruhns, P.2    Pesesse, X.3    Daeron, M.4    Erneux, C.5
  • 33
    • 9144266369 scopus 로고    scopus 로고
    • SHIP2 is recruited to the cell membrane upon macrophage colony-stimulating factor (M-CSF) stimulation and regulates M-CSF-induced signaling
    • Wang, Y. J., Keogh, R. J., Hunter, M. G., Mitchell, C. A., Frey, R. S., and Javaid, K.; et al. (2004) SHIP2 is recruited to the cell membrane upon macrophage colony-stimulating factor (M-CSF) stimulation and regulates M-CSF-induced signaling. J. Immunol. 173, 6820-6830.
    • (2004) J. Immunol. , vol.173 , pp. 6820-6830
    • Wang, Y.J.1    Keogh, R.J.2    Hunter, M.G.3    Mitchell, C.A.4    Frey, R.S.5    Javaid, K.6
  • 34
    • 24644500492 scopus 로고    scopus 로고
    • Decoding protein-protein interactions through combinatorial chemistry: Sequence specificity of SHP-1, SHP-2, and SHIP SH2 domains
    • Sweeney, M. C., Wavreille, A. S., Park, J., Butchar, J. P., Tridandapani, S., and Pei, D. (2005) Decoding protein-protein interactions through combinatorial chemistry: sequence specificity of SHP-1, SHP-2, and SHIP SH2 domains. Biochemistry 44, 14932-14947.
    • (2005) Biochemistry , vol.44 , pp. 14932-14947
    • Sweeney, M.C.1    Wavreille, A.S.2    Park, J.3    Butchar, J.P.4    Tridandapani, S.5    Pei, D.6
  • 35
    • 0141563651 scopus 로고    scopus 로고
    • An improved method for rapid sequencing of support-bound peptides by partial Edman degradation and mass spectrometry
    • Sweeney, M. C., and Pei, D. (2003) An improved method for rapid sequencing of support-bound peptides by partial Edman degradation and mass spectrometry. J. Comb. Chem. 5, 218-222.
    • (2003) J. Comb. Chem. , vol.5 , pp. 218-222
    • Sweeney, M.C.1    Pei, D.2
  • 36
    • 33747621649 scopus 로고    scopus 로고
    • Traceless capping agent for peptide sequencing by partial Edman degradation and mass spectrometry
    • Thakkar, A., Wavreille, A. S., and Pei, D. (2006) Traceless capping agent for peptide sequencing by partial Edman degradation and mass spectrometry. Anal. Chem. 78, 5935-5939.
    • (2006) Anal. Chem. , vol.78 , pp. 5935-5939
    • Thakkar, A.1    Wavreille, A.S.2    Pei, D.3
  • 37
    • 0029760874 scopus 로고    scopus 로고
    • In vivo and in vitro specificity of protein tyrosine kinases for immunoglobulin G receptor (FcγRII) phosphorylation
    • Bewarder, N., Weinrich, V., Budde, P., Hartmann, D., Flaswinkel, H., Reth, M., and Frey, J. R. (1996) In vivo and in vitro specificity of protein tyrosine kinases for immunoglobulin G receptor (FcγRII) phosphorylation. Mol. Cell. Biol. 16, 4735-4743.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4735-4743
    • Bewarder, N.1    Weinrich, V.2    Budde, P.3    Hartmann, D.4    Flaswinkel, H.5    Reth, M.6    Frey, J.R.7
  • 38
    • 33745988276 scopus 로고    scopus 로고
    • Sequence specificity of SHP-1 and SHP-2 Src homology 2 domains: Critical roles of residues beyond the pY+3 position
    • Imhof, D., Wavreille, A.-S., May, A., Zacharias, M., Tridandapani, S., and Pei, D. (2006) Sequence specificity of SHP-1 and SHP-2 Src homology 2 domains: critical roles of residues beyond the pY+3 position. J. Biol. Chem. 281, 20271-20282.
    • (2006) J. Biol. Chem. , vol.281 , pp. 20271-20282
    • Imhof, D.1    Wavreille, A.-S.2    May, A.3    Zacharias, M.4    Tridandapani, S.5    Pei, D.6
  • 39
    • 39049154319 scopus 로고    scopus 로고
    • Motif decomposition of the phosphotyrosine proteome reveals a new N-terminal binding motif for SHIP2
    • Miller, M. L., Hanke, S., Hinsby, A. M., Friis, C., Brunak, S., Mann, M., and Blom, N. (2008) Motif decomposition of the phosphotyrosine proteome reveals a new N-terminal binding motif for SHIP2. Mol. Cell. Proteomics 7, 181-192.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 181-192
    • Miller, M.L.1    Hanke, S.2    Hinsby, A.M.3    Friis, C.4    Brunak, S.5    Mann, M.6    Blom, N.7
  • 40
    • 2942733237 scopus 로고    scopus 로고
    • Changes in structural dynamics of the Grb2 adaptor protein upon binding of phosphotyrosine ligand to its SH2 domain
    • de Mol, N. J., Catalina, M. I., Fischer, M. J. E., Broutin, I., Maier, C. S., and Heck, A. J. R. (2004) Changes in structural dynamics of the Grb2 adaptor protein upon binding of phosphotyrosine ligand to its SH2 domain. Biochim. Biophys. Acta 1700, 53-64.
    • (2004) Biochim. Biophys. Acta , vol.1700 , pp. 53-64
    • De Mol, N.J.1    Catalina, M.I.2    Fischer, M.J.E.3    Broutin, I.4    Maier, C.S.5    Heck, A.J.R.6
  • 41
    • 0036895828 scopus 로고    scopus 로고
    • Structural characterization of a proline-driven conformational switch within the Itk SH2 domain
    • Mallis, R. J., Brazin, K. N., Fulton, D. B., and Andreotti, A. H. (2002) Structural characterization of a proline-driven conformational switch within the Itk SH2 domain. Nat. Struct. Biol. 9, 900-905.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 900-905
    • Mallis, R.J.1    Brazin, K.N.2    Fulton, D.B.3    Andreotti, A.H.4
  • 42
    • 0018143763 scopus 로고
    • Acid catalysis of the formation of the slow-folding species of Rnase A: Evidence that the reaction is proline isomerization
    • Schmid, F. X., and Baldwin, R. L. (1978) Acid catalysis of the formation of the slow-folding species of Rnase A: evidence that the reaction is proline isomerization. Proc. Natl. Acad. Sci. U.S.A. 75, 4764-4768.
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 4764-4768
    • Schmid, F.X.1    Baldwin, R.L.2
  • 43
    • 33748205100 scopus 로고    scopus 로고
    • SHIP1/2 interaction with tyrosine phosphorylated peptides mimicking an immunoreceptor signaling motif
    • Pesesse, X., Backers, K., Moreau, C., Zhang, J., Blero, D., Paternotte, N., and Erneux, C. (2006) SHIP1/2 interaction with tyrosine phosphorylated peptides mimicking an immunoreceptor signaling motif. Adv. Enzymol. Regul. 46, 142-153.
    • (2006) Adv. Enzymol. Regul. , vol.46 , pp. 142-153
    • Pesesse, X.1    Backers, K.2    Moreau, C.3    Zhang, J.4    Blero, D.5    Paternotte, N.6    Erneux, C.7
  • 44
    • 0027409064 scopus 로고
    • Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free forms
    • DOI 10.1016/0092-8674(93)90405-F
    • Waksman, G., Shoelson, S. E., Pant, N., Cowban, D., and Kuriyan, J. (1993) Binding of high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell 72, 779-790. (Pubitemid 23093885)
    • (1993) Cell , vol.72 , Issue.5 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3    Cowburn, D.4    Kuriyan, J.5
  • 46
    • 0344196904 scopus 로고    scopus 로고
    • SAM domains: Uniform structure, diversity of function
    • Kim, C. A., and Bowie, J. U. (2003) SAM domains: uniform structure, diversity of function. Trends Biochem. Sci. 28, 625-628.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 625-628
    • Kim, C.A.1    Bowie, J.U.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.