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Volumn 14, Issue 4, 2000, Pages 594-601

The interaction between EEN and Abi-1, two MLL fusion partners, and synaptojanin and dynamin: Implications for leukaemogenesis

Author keywords

Abi 1; EEN family; MLL; SH3 domain; Synaptojanin

Indexed keywords

DYNAMIN; PHOSPHATASE; SYNAPTOJANIN; UNCLASSIFIED DRUG;

EID: 0034119048     PISSN: 08876924     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.leu.2401692     Document Type: Article
Times cited : (36)

References (72)
  • 2
    • 0026936328 scopus 로고
    • A trithorax-like gene is interrupted by chromosome 11q23 translocations in acute leukaemias
    • Djabali M, Selleri L, Parry P, Bower M, Young BD, Evans GA. A trithorax-like gene is interrupted by chromosome 11q23 translocations in acute leukaemias. Nat Genet 1992; 2: 113-118.
    • (1992) Nat Genet , vol.2 , pp. 113-118
    • Djabali, M.1    Selleri, L.2    Parry, P.3    Bower, M.4    Young, B.D.5    Evans, G.A.6
  • 3
    • 0026496887 scopus 로고
    • The t(4;11) chromosome translocation of human acute leukaemias fuses the ALL-1 gene, related to Drosophila trithorax, to the AF-4 gene
    • Gu Y, Nakamura T, Alder H, Prasad R, Canaani O, Cimino G, Croce CM, Canaani E. The t(4;11) chromosome translocation of human acute leukaemias fuses the ALL-1 gene, related to Drosophila trithorax, to the AF-4 gene. Cell 1992; 71: 701-708.
    • (1992) Cell , vol.71 , pp. 701-708
    • Gu, Y.1    Nakamura, T.2    Alder, H.3    Prasad, R.4    Canaani, O.5    Cimino, G.6    Croce, C.M.7    Canaani, E.8
  • 4
    • 0026454451 scopus 로고
    • Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukaemias
    • Tkachuk DC, Kohler S, Cleary ML. Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukaemias. Cell 1992; 71: 691-700.
    • (1992) Cell , vol.71 , pp. 691-700
    • Tkachuk, D.C.1    Kohler, S.2    Cleary, M.L.3
  • 5
    • 0029018546 scopus 로고
    • Molecular basis of 11q23 rearrangements in hematopoietic malignant proliferations
    • Bernard OA, Berger R. Molecular basis of 11q23 rearrangements in hematopoietic malignant proliferations. Genes Chromosom Cancer 1995; 13: 75-85.
    • (1995) Genes Chromosom Cancer , vol.13 , pp. 75-85
    • Bernard, O.A.1    Berger, R.2
  • 6
    • 0028857948 scopus 로고
    • The leukaemia-associated protein (LAP) domain, a cysteine-rich motif, is present in a wide range of proteins, including MLL, AF10, and MLLT6 proteins
    • Sana V, Chaplin T, Gregorini A, Ayton P, Young BD The leukaemia-associated protein (LAP) domain, a cysteine-rich motif, is present in a wide range of proteins, including MLL, AF10, and MLLT6 proteins. Proc Natl Acad Sci USA 1995; 92: 9737-9741.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9737-9741
    • Sana, V.1    Chaplin, T.2    Gregorini, A.3    Ayton, P.4    Young, B.D.5
  • 7
    • 0028861418 scopus 로고
    • The PHD finger: Implications for chromatin-mediated transcriptional regulation
    • Aasland R, Gibson TJ, Stewart AF. The PHD finger: implications for chromatin-mediated transcriptional regulation. Trends Biochem Sci 1995; 20: 56-59.
    • (1995) Trends Biochem Sci , vol.20 , pp. 56-59
    • Aasland, R.1    Gibson, T.J.2    Stewart, A.F.3
  • 8
    • 0032566001 scopus 로고    scopus 로고
    • Isolation and characterization of a pufferfish MLL (mixed lineage leukaemia)-like gene (fMLL) reveals evolutionary conservation in vertebrate genes related to Drosophila trithorax
    • Caldas C, Kim M-H, MacGregor A, Cain D, Aparicio S, Wiedemann LM. Isolation and characterization of a pufferfish MLL (mixed lineage leukaemia)-like gene (fMLL) reveals evolutionary conservation in vertebrate genes related to Drosophila trithorax. Oncogene 1998; 16: 3233-3241.
    • (1998) Oncogene , vol.16 , pp. 3233-3241
    • Caldas, C.1    Kim, M.-H.2    MacGregor, A.3    Cain, D.4    Aparicio, S.5    Wiedemann, L.M.6
  • 9
    • 0030954681 scopus 로고    scopus 로고
    • Defects in yolk sac hematopoiesis in MLL-null embryos
    • Hess JL, Yu BD, Li B, Hanson R, Korsmeyer SJ. Defects in yolk sac hematopoiesis in MLL-null embryos. Blood 1997; 90: 1799-1806.
    • (1997) Blood , vol.90 , pp. 1799-1806
    • Hess, J.L.1    Yu, B.D.2    Li, B.3    Hanson, R.4    Korsmeyer, S.J.5
  • 11
    • 0031457440 scopus 로고    scopus 로고
    • Fifty years of studies of the biology and therapy of childhood leukaemia
    • Kersey JH. Fifty years of studies of the biology and therapy of childhood leukaemia. Blood 1997; 90: 4243-4251.
    • (1997) Blood , vol.90 , pp. 4243-4251
    • Kersey, J.H.1
  • 12
    • 0030791974 scopus 로고    scopus 로고
    • Immortalization and leukemic transformation of a myelomonocytic precursor by retrovirally transduced HRX-ENL
    • Lavau C, Szilvassy SJ, Slany R, Cleary ML. Immortalization and leukemic transformation of a myelomonocytic precursor by retrovirally transduced HRX-ENL. EMBO J 1997; 16: 4226-4237.
    • (1997) EMBO J , vol.16 , pp. 4226-4237
    • Lavau, C.1    Szilvassy, S.J.2    Slany, R.3    Cleary, M.L.4
  • 13
    • 0031972784 scopus 로고    scopus 로고
    • The oncogenic capacity of HRX-ENL requires the transcriptional transactivation activity of ENL and the DNA binding motifs of HRX
    • Slany RK, Lavau C, Cleary ML The oncogenic capacity of HRX-ENL requires the transcriptional transactivation activity of ENL and the DNA binding motifs of HRX. Mol Cell Biol 1998; 18: 122-129.
    • (1998) Mol Cell Biol , vol.18 , pp. 122-129
    • Slany, R.K.1    Lavau, C.2    Cleary, M.L.3
  • 14
  • 15
    • 0028135353 scopus 로고
    • Cloning of ELL, a gene that fuses to MLL in a t(11;19)(q23;p13.1) in acute myeloid leukaemia
    • Thirman MJ, Levitan DA, Kobayashi H, Simon MC, Rowley JD. Cloning of ELL, a gene that fuses to MLL in a t(11;19)(q23;p13.1) in acute myeloid leukaemia. Proc Natl Acad Sci USA 1994; 91: 12110-12114.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12110-12114
    • Thirman, M.J.1    Levitan, D.A.2    Kobayashi, H.3    Simon, M.C.4    Rowley, J.D.5
  • 16
    • 0028939520 scopus 로고
    • Cloning of several species of MLL/MEN chimeric cDNAs in myeloid leukaemia with t(11;19)(q23;p13.1) translocation
    • Mitani K, Kanda Y, Ogawa S, Tanaka T, Inazawa J, Yazaki Y, Hirai H. Cloning of several species of MLL/MEN chimeric cDNAs in myeloid leukaemia with t(11;19)(q23;p13.1) translocation. Blood 1995; 85: 2017-2024.
    • (1995) Blood , vol.85 , pp. 2017-2024
    • Mitani, K.1    Kanda, Y.2    Ogawa, S.3    Tanaka, T.4    Inazawa, J.5    Yazaki, Y.6    Hirai, H.7
  • 19
    • 0031439397 scopus 로고    scopus 로고
    • Adenoviral E1A-associated protein p300 is involved in acute myeloid leukaemia with t(11;22)(q23;q13)
    • Ida K, Kitabayashi I, Taki T, Taniwaki M, Noro K, Yamamoto M, Ohki M, Hayashi Y. Adenoviral E1A-associated protein p300 is involved in acute myeloid leukaemia with t(11;22)(q23;q13). Blood 1997; 90: 4699-4704.
    • (1997) Blood , vol.90 , pp. 4699-4704
    • Ida, K.1    Kitabayashi, I.2    Taki, T.3    Taniwaki, M.4    Noro, K.5    Yamamoto, M.6    Ohki, M.7    Hayashi, Y.8
  • 21
    • 0031797572 scopus 로고    scopus 로고
    • A new case of translocation t(6;11)(q21;q23) in a therapy-related acute myeloid leukaemia resulting in an MLL-AF6q21 fusion
    • Bernard OA, Hillion J, LeConiat M, Berger R. A new case of translocation t(6;11)(q21;q23) in a therapy-related acute myeloid leukaemia resulting in an MLL-AF6q21 fusion. Genes Chromosom Cancer 1998; 22: 221-224.
    • (1998) Genes Chromosom Cancer , vol.22 , pp. 221-224
    • Bernard, O.A.1    Hillion, J.2    Leconiat, M.3    Berger, R.4
  • 25
    • 0028169259 scopus 로고
    • ENL, the gene fused with HRX in t(11;19) leukaemias, encodes a nuclear protein with transcriptional activation potential in lymphoid and myeloid cells
    • Rubnitz JE, Morrissey J, Savage PA, Cleary ML. ENL, the gene fused with HRX in t(11;19) leukaemias, encodes a nuclear protein with transcriptional activation potential in lymphoid and myeloid cells. Blood 1994; 84: 1747-1752.
    • (1994) Blood , vol.84 , pp. 1747-1752
    • Rubnitz, J.E.1    Morrissey, J.2    Savage, P.A.3    Cleary, M.L.4
  • 28
    • 0028215338 scopus 로고
    • A novel gene, AF-1p, fused to HRX in t(1;11)(p32;q23), is not related to AF-4, AF-9 nor ENL
    • Bernard OA, Mauchauffe M, Mecucci C, Van Den Berghe H, Berger R. A novel gene, AF-1p, fused to HRX in t(1;11)(p32;q23), is not related to AF-4, AF-9 nor ENL. Oncogcne 1994; 9: 1039-1045.
    • (1994) Oncogcne , vol.9 , pp. 1039-1045
    • Bernard, O.A.1    Mauchauffe, M.2    Mecucci, C.3    Van Den Berghe, H.4    Berger, R.5
  • 29
    • 0000778884 scopus 로고    scopus 로고
    • EEN encodes for a member of a new family of proteins containing an Src homology 3 domain and is the third gene located on chromosome 19p13 that fuses to MLL in human leukaemia
    • So CW, Caldas C, Liu M-M, Chen S-J, Huang Q-H, Gu L-J, Sham MH, Wiedemann LM, Chan LC. EEN encodes for a member of a new family of proteins containing an Src homology 3 domain and is the third gene located on chromosome 19p13 that fuses to MLL in human leukaemia. Proc Natl Acad Sci USA 1997; 94: 2563-2568.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2563-2568
    • So, C.W.1    Caldas, C.2    Liu, M.-M.3    Chen, S.-J.4    Huang, Q.-H.5    Gu, L.-J.6    Sham, M.H.7    Wiedemann, L.M.8    Chan, L.C.9
  • 30
    • 0032529489 scopus 로고    scopus 로고
    • ABI-1, a human homolog to mouse Ab1-interactor 1, fuses the MLL gene in acute myeloid leukaemia with t(10;11)(p11.2;q23)
    • Taki T, Shibuya N, Taniwaki M, Hanada R, Morishita K, Bessho F, Yanagisawa M, Hayashi Y. ABI-1, a human homolog to mouse Ab1-interactor 1, fuses the MLL gene in acute myeloid leukaemia with t(10;11)(p11.2;q23). Blood 1998; 92: 1125-1130.
    • (1998) Blood , vol.92 , pp. 1125-1130
    • Taki, T.1    Shibuya, N.2    Taniwaki, M.3    Hanada, R.4    Morishita, K.5    Bessho, F.6    Yanagisawa, M.7    Hayashi, Y.8
  • 31
    • 0031149052 scopus 로고    scopus 로고
    • A novel SH3-containing human gene family preferentially expressed in the central nervous system
    • Giachino C, Lantelme E, Lanzetti L, Saccone S, Bella-Valle G, Migone N. A novel SH3-containing human gene family preferentially expressed in the central nervous system. Genomics 1997; 41: 427-434.
    • (1997) Genomics , vol.41 , pp. 427-434
    • Giachino, C.1    Lantelme, E.2    Lanzetti, L.3    Saccone, S.4    Bella-Valle, G.5    Migone, N.6
  • 33
    • 0030739938 scopus 로고    scopus 로고
    • The SH3p4/SH3p8/SH3p13 protein family: Binding partners for synaptojanin and dynamin via a GrB2-like Src homology 3 domain
    • Ringstad N, Nemoto Y, De Camilli P. The SH3p4/SH3p8/SH3p13 protein family: binding partners for synaptojanin and dynamin via a GrB2-like Src homology 3 domain. Proc Natl Acad Sci USA 1997; 94: 8569-8574.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8569-8574
    • Ringstad, N.1    Nemoto, Y.2    De Camilli, P.3
  • 35
    • 0026608178 scopus 로고
    • C. Elegans cell-signalling gene sem-5 encodes a protein with SH2 and SH3 domains
    • Clark SG, Stern MJ, Horvitz HR. C. elegans cell-signalling gene sem-5 encodes a protein with SH2 and SH3 domains. Nature 1992; 356: 140-344.
    • (1992) Nature , vol.356 , pp. 140-344
    • Clark, S.G.1    Stern, M.J.2    Horvitz, H.R.3
  • 36
    • 0026630991 scopus 로고
    • Corkscrew encodes a putative protein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso
    • Perkins LA, Larsen I, Perrimon N. Corkscrew encodes a putative protein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso. Cell 1992; 70: 225-236.
    • (1992) Cell , vol.70 , pp. 225-236
    • Perkins, L.A.1    Larsen, I.2    Perrimon, N.3
  • 37
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson T. Protein modules and signalling networks. Nature 1995; 373: 573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 39
    • 0028073746 scopus 로고
    • p145, a major GrB2-binding protein in brain, is co-localized with dynamin in nerve terminals where it undergoes activity-dependent dephosphorylation
    • McPherson PS, Takei K, Schmid SL, De Camilli P. p145, a major GrB2-binding protein in brain, is co-localized with dynamin in nerve terminals where it undergoes activity-dependent dephosphorylation. J Biol Chem 1994; 269: 30132-30139.
    • (1994) J Biol Chem , vol.269 , pp. 30132-30139
    • McPherson, P.S.1    Takei, K.2    Schmid, S.L.3    De Camilli, P.4
  • 41
    • 0027133450 scopus 로고
    • Microtubules and Src homology 3 domains stimulate the dynamin GTPase via its C-terminal domain
    • Herskovits JS, Shpetner HS, Burgess CC, Vallee RB. Microtubules and Src homology 3 domains stimulate the dynamin GTPase via its C-terminal domain. Proc Natl Acad Sci USA 1993; 90: 11468-11472.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11468-11472
    • Herskovits, J.S.1    Shpetner, H.S.2    Burgess, C.C.3    Vallee, R.B.4
  • 42
    • 0031026631 scopus 로고    scopus 로고
    • The dynamins: Redundnat or distinct functions for an expanding family of related GTPases?
    • Urrutia R, Henley JR, Cook T, McNiven MA. The dynamins: redundnat or distinct functions for an expanding family of related GTPases? Proc Natl Acad Sci USA 1997; 94: 377-384.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 377-384
    • Urrutia, R.1    Henley, J.R.2    Cook, T.3    McNiven, M.A.4
  • 43
    • 0025006964 scopus 로고
    • Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins
    • Obar RA, Collins CA, Hammarback JA, Shpetner HS, Vallee RB. Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins. Nature 1990; 347: 256-261.
    • (1990) Nature , vol.347 , pp. 256-261
    • Obar, R.A.1    Collins, C.A.2    Hammarback, J.A.3    Shpetner, H.S.4    Vallee, R.B.5
  • 45
    • 0029773891 scopus 로고    scopus 로고
    • Tissue-specific alternative splicing generates two synaptojanin isoforms with differential membrane binding properties
    • Ramjaun AR, McPherson PS. Tissue-specific alternative splicing generates two synaptojanin isoforms with differential membrane binding properties. J Biol Chem 1996; 271: 24856-24861
    • (1996) J Biol Chem , vol.271 , pp. 24856-24861
    • Ramjaun, A.R.1    McPherson, P.S.2
  • 46
    • 0031434562 scopus 로고    scopus 로고
    • Synaptojanin 1: Localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15
    • Haffner C, Takei K, Chen H, Ringstad N, Hudson A, Butler MH, Salcini AE, Di Fiore PP, DeCamilli P. Synaptojanin 1: localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15. FEBS Lett 1997; 419: 175-180.
    • (1997) FEBS Lett , vol.419 , pp. 175-180
    • Haffner, C.1    Takei, K.2    Chen, H.3    Ringstad, N.4    Hudson, A.5    Butler, M.H.6    Salcini, A.E.7    Di Fiore, P.P.8    Decamilli, P.9
  • 48
    • 0029281993 scopus 로고
    • SH3 domains. Minding your p's and q's
    • Mayer BJ, Eck MJ. SH3 domains. Minding your p's and q's. Curr Biol 1995; 5: 364-367.
    • (1995) Curr Biol , vol.5 , pp. 364-367
    • Mayer, B.J.1    Eck, M.J.2
  • 49
    • 0027962645 scopus 로고
    • Two binding orientations for peptides to the Src SH3 domain: Development of a general model tor SH3-ligand interactions
    • Feng S, Chen JK, Yu H, Simon JA, Schreiber SL. Two binding orientations for peptides to the Src SH3 domain: development of a general model tor SH3-ligand interactions. Science 1994; 266: 1241-1247.
    • (1994) Science , vol.266 , pp. 1241-1247
    • Feng, S.1    Chen, J.K.2    Yu, H.3    Simon, J.A.4    Schreiber, S.L.5
  • 50
    • 0029789753 scopus 로고    scopus 로고
    • Exclusion of Int-6 from PML nuclear bodies by binding to the HTLV-I Tax oncoprotein
    • Desbois C, Rousset R, Bantignies F, Jalinot P. Exclusion of Int-6 from PML nuclear bodies by binding to the HTLV-I Tax oncoprotein. Science 1996; 273: 951-953.
    • (1996) Science , vol.273 , pp. 951-953
    • Desbois, C.1    Rousset, R.2    Bantignies, F.3    Jalinot, P.4
  • 51
    • 0030831166 scopus 로고    scopus 로고
    • HTLV-I Tax self-association in optimal transactivation function
    • Jin DY, Jeang KT. HTLV-I Tax self-association in optimal transactivation function. Nucleic Acids Res 1997; 25: 379-387.
    • (1997) Nucleic Acids Res , vol.25 , pp. 379-387
    • Jin, D.Y.1    Jeang, K.T.2
  • 53
    • 0032497845 scopus 로고    scopus 로고
    • The diversity and possible functions of the inositol polyphosphate 5-phosphatases
    • Erneux C, Govaerts C, Communi D, Pesesse X. The diversity and possible functions of the inositol polyphosphate 5-phosphatases. Biochim Biophys Acta 1998; 1436: 185-199.
    • (1998) Biochim Biophys Acta , vol.1436 , pp. 185-199
    • Erneux, C.1    Govaerts, C.2    Communi, D.3    Pesesse, X.4
  • 54
    • 0032147185 scopus 로고    scopus 로고
    • Endocytosis proteins and cancer: A potential link?
    • Floyd S, De Camilli P. Endocytosis proteins and cancer: a potential link? Trends Cell Biol 1998; 8: 299-101.
    • (1998) Trends Cell Biol , vol.8 , pp. 299-1101
    • Floyd, S.1    De Camilli, P.2
  • 55
    • 0032479156 scopus 로고    scopus 로고
    • High-affinity binding of epidermal growth factor (EGF) to EGF receptor is disrupted by overexpression of mutant dynamin (K44A)
    • Ringerike T, Stang E, Johannessen LE, Sandnes D, Levy FO, Madshus IH. High-affinity binding of epidermal growth factor (EGF) to EGF receptor is disrupted by overexpression of mutant dynamin (K44A). J Biol Chem 1998; 27: 16659-16642.
    • (1998) J Biol Chem , vol.27 , pp. 16659-116642
    • Ringerike, T.1    Stang, E.2    Johannessen, L.E.3    Sandnes, D.4    Levy, F.O.5    Madshus, I.H.6
  • 56
    • 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 JE, Liu L, Rosten P, Humphries RK, Jefferson AB, Majerus PW, 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
  • 57
  • 59
    • 0027366440 scopus 로고
    • Agonist-stimulated synthesis of phosphatidylinositol (3,4,5)-trisphosphate: A new intracellular signalling system?
    • Stephens LR, Jackson TR, Hawkins PT. Agonist-stimulated synthesis of phosphatidylinositol (3,4,5)-trisphosphate: a new intracellular signalling system? Biochim Biophys Acta 1993; 1179: 27-75.
    • (1993) Biochim Biophys Acta , vol.1179 , pp. 27-75
    • Stephens, L.R.1    Jackson, T.R.2    Hawkins, P.T.3
  • 60
    • 0032579532 scopus 로고    scopus 로고
    • Lipid-regulated kinases: Some common themes at last
    • Downward J. Lipid-regulated kinases: some common themes at last. Science 1998; 279: 673-674.
    • (1998) Science , vol.279 , pp. 673-674
    • Downward, J.1
  • 62
    • 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 JE, Hughes MR, Babic I, Jirik FR, 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
  • 63
    • 0028963084 scopus 로고
    • Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor
    • Yao R, Cooper GM. Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor. Science 1995; 267: 2003-2006.
    • (1995) Science , vol.267 , pp. 2003-2006
    • Yao, R.1    Cooper, G.M.2
  • 65
    • 3643119742 scopus 로고    scopus 로고
    • The phosphoinositol phosphatase activity of PTEN mediates a serum-sensitive G1 growth arrest in glioma cells
    • Furnari FB, Huang HJ, Cavenee WK. The phosphoinositol phosphatase activity of PTEN mediates a serum-sensitive G1 growth arrest in glioma cells. Cancer Res 1998; 58: 5002-5008.
    • (1998) Cancer Res , vol.58 , pp. 5002-5008
    • Furnari, F.B.1    Huang, H.J.2    Cavenee, W.K.3
  • 66
    • 0030728479 scopus 로고    scopus 로고
    • Growth suppression of glioma cells by PTEN requires a functional phosphatase catalytic domain
    • Furnari FB, Lin H, Huang HS, Cavenee WK. Growth suppression of glioma cells by PTEN requires a functional phosphatase catalytic domain. Proc Natl Acad Sci USA 1997; 94: 12479-12484.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12479-12484
    • Furnari, F.B.1    Lin, H.2    Huang, H.S.3    Cavenee, W.K.4
  • 67
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • Maehama T, Dixon JE. The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J Biol Chem 1998; 273: 13375-13378.
    • (1998) J Biol Chem , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 70
    • 0028844631 scopus 로고
    • Ab1-interactor-1, a novel SH3 protein binding to the carboxy-terminal portion of the Ab1 protein, suppresses v-abl transforming activity
    • Shi Y, Alin K, Goff SP. Ab1-interactor-1, a novel SH3 protein binding to the carboxy-terminal portion of the Ab1 protein, suppresses v-abl transforming activity. Genes Dev 1995; 9: 2583-2597.
    • (1995) Genes Dev , vol.9 , pp. 2583-2597
    • Shi, Y.1    Alin, K.2    Goff, S.P.3
  • 71
    • 0031032916 scopus 로고    scopus 로고
    • Isolation and characterization of e3B1, an eps8 binding protein that regulates cell growth
    • Biesova Z, Piccoli C, Wong WT. Isolation and characterization of e3B1, an eps8 binding protein that regulates cell growth. Oncogene 1997; 14: 233-241.
    • (1997) Oncogene , vol.14 , pp. 233-241
    • Biesova, Z.1    Piccoli, C.2    Wong, W.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.