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Volumn 6, Issue 5, 1999, Pages

The PIK-related kinases intercept conventional signaling pathways

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE; PHOSPHOTRANSFERASE; SIGNAL TRANSDUCTION;

EID: 0033133990     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(99)80070-2     Document Type: Article
Times cited : (61)

References (70)
  • 1
    • 0001490037 scopus 로고
    • Contribution à l'indépedance de l'athétose double idiopathique et congénitale
    • 1. Syllaba, L. & Henner, K. (1926). Contribution à l'indépedance de l'athétose double idiopathique et congénitale [Contributions to the independence of idiopathic and congenital double athetosis]. Rev. Neurol. 1, 541-562.
    • (1926) Rev. Neurol. , vol.1 , pp. 541-562
    • Syllaba, L.1    Henner, K.2
  • 2
    • 0002590341 scopus 로고
    • Ataxia-telangiectasia. A familial syndrome of progressive cerebellar ataxia, oculocutaneous telangiectasia and frequent pulmonary infection
    • 2. Boder, E. & Sedgwick, R.P. (1957). Ataxia-telangiectasia. A familial syndrome of progressive cerebellar ataxia, oculocutaneous telangiectasia and frequent pulmonary infection. USC Med. Bull. 9, 15-28.
    • (1957) USC Med. Bull. , vol.9 , pp. 15-28
    • Boder, E.1    Sedgwick, R.P.2
  • 3
    • 0016713286 scopus 로고
    • Rapamycin (AY-22,989), a new antifungal antibiotic. II. Fermentation, isolation and characterization
    • 3. Sehgal, S.N., Baker, H. & Vezina, C. (1975). Rapamycin (AY-22,989), a new antifungal antibiotic. II. Fermentation, isolation and characterization. J. Antibiot (Tokyo) 28, 727-732.
    • (1975) J. Antibiot (Tokyo) , vol.28 , pp. 727-732
    • Sehgal, S.N.1    Baker, H.2    Vezina, C.3
  • 4
    • 0016724057 scopus 로고
    • Rapamycin (AY-22,989), a new antifungal antibiotic. I. Taxonomy of the producing streptomycete and isolation of the active principle
    • 4. Vezina, C., Kudelski, A. & Sehgal, S.N. (1975). Rapamycin (AY-22,989), a new antifungal antibiotic. I. Taxonomy of the producing streptomycete and isolation of the active principle. J. Antibiot. (Tokyo) 28, 721-726.
    • (1975) J. Antibiot. (Tokyo) , vol.28 , pp. 721-726
    • Vezina, C.1    Kudelski, A.2    Sehgal, S.N.3
  • 5
    • 0026030568 scopus 로고
    • Chemistry and biology of the immunophilins and their immunosuppressive ligands
    • 5. Schreiber, S.L. (1991). Chemistry and biology of the immunophilins and their immunosuppressive ligands. Science 251, 283-287.
    • (1991) Science , vol.251 , pp. 283-287
    • Schreiber, S.L.1
  • 6
    • 0027382875 scopus 로고
    • Dominant missense mutations in a novel yeast protein related to mammalian phosphatidylinositol 3-kinase and VPS34 abrogate rapamycin cytotoxicity
    • 6. Cafferkey, R., et al., & Livi, G.P. (1993). Dominant missense mutations in a novel yeast protein related to mammalian phosphatidylinositol 3-kinase and VPS34 abrogate rapamycin cytotoxicity. Mol. Cell. Biol. 13, 6012-6023.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6012-6023
    • Cafferkey, R.1    Livi, G.P.2
  • 7
    • 0027311858 scopus 로고
    • Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression
    • 7. Kunz, J., Henriquez, R., Schneider, U., Deuter-Reinhard, M., Movva, N.R. & Hall, M.N. (1993). Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression. Cell 73, 585-596.
    • (1993) Cell , vol.73 , pp. 585-596
    • Kunz, J.1    Henriquez, R.2    Schneider, U.3    Deuter-Reinhard, M.4    Movva, N.R.5    Hall, M.N.6
  • 8
    • 0028360374 scopus 로고
    • A mammalian protein targeted by G1-arresting rapamycin-receptor complex
    • 8. Brown, E.J., et al., & Schreiber S.L. (1994). A mammalian protein targeted by G1-arresting rapamycin-receptor complex. Nature 369, 756-758.
    • (1994) Nature , vol.369 , pp. 756-758
    • Brown, E.J.1    Schreiber, S.L.2
  • 9
    • 0028239893 scopus 로고
    • RAFT1: A mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs
    • 9. Sabatini, D.M., Erdjument-Bromage, H., Lui, M., Tempst, P. & Snyder, S.H. (1994). RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs. Cell 78, 35-43.
    • (1994) Cell , vol.78 , pp. 35-43
    • Sabatini, D.M.1    Erdjument-Bromage, H.2    Lui, M.3    Tempst, P.4    Snyder, S.H.5
  • 10
    • 0029057336 scopus 로고
    • A single ataxia telangiectasia gene with a product similar to PI-3 kinase
    • 10. Savitsky, K., et al., & Shiloh Y. (1995). A single ataxia telangiectasia gene with a product similar to Pl-3 kinase. Science 268, 1749-1753.
    • (1995) Science , vol.268 , pp. 1749-1753
    • Savitsky, K.1    Shiloh, Y.2
  • 11
    • 0028137771 scopus 로고
    • TOR1 and TOR2 are structurally and functionally similar but not identical phosphatidylinositol kinase homologues in yeast
    • 11. Helliwell, S.B., Wagner, P., Kunz, J., Deuter-Reinhard, M., Henriquez, R. & Hall, M.N. (1994). TOR1 and TOR2 are structurally and functionally similar but not identical phosphatidylinositol kinase homologues in yeast. Mol. Biol. Cell. 5, 105-118.
    • (1994) Mol. Biol. Cell. , vol.5 , pp. 105-118
    • Helliwell, S.B.1    Wagner, P.2    Kunz, J.3    Deuter-Reinhard, M.4    Henriquez, R.5    Hall, M.N.6
  • 12
    • 0028800996 scopus 로고
    • PIK-related kinases: DNA repair, recombination, and cell cycle checkpoints
    • 12. Keith, C.T. & Schreiber, S.L. (1995). PIK-related kinases: DNA repair, recombination, and cell cycle checkpoints. Science 270, 50-51.
    • (1995) Science , vol.270 , pp. 50-51
    • Keith, C.T.1    Schreiber, S.L.2
  • 13
    • 0029156599 scopus 로고
    • DNA-dependent protein kinase catalytic subunit: A relative of phosphatidylinositol 3-kinase and the ataxia telangiectasia gene product
    • 13. Hartley, K.O., et al., & Jackson S.P. (1995). DNA-dependent protein kinase catalytic subunit: a relative of phosphatidylinositol 3-kinase and the ataxia telangiectasia gene product. Cell 82, 849-856.
    • (1995) Cell , vol.82 , pp. 849-856
    • Hartley, K.O.1    Jackson, S.P.2
  • 14
    • 0029089618 scopus 로고
    • The mei-41 gene of D. melanogaster is a structural and functional homolog of the human ataxia telangiectasia gene
    • 14. Hari, K.L., Santerre, A., Sekelsky, J.J., McKim, K.S., Boyd, J.B. & Hawley, R.S. (1995). The mei-41 gene of D. melanogaster is a structural and functional homolog of the human ataxia telangiectasia gene. Cell 82, 815-821.
    • (1995) Cell , vol.82 , pp. 815-821
    • Hari, K.L.1    Santerre, A.2    Sekelsky, J.J.3    McKim, K.S.4    Boyd, J.B.5    Hawley, R.S.6
  • 15
    • 0029827367 scopus 로고    scopus 로고
    • The Schizosaccharomyces pombe rad3 checkpoint gene
    • 15. Bentley, N.J., et al., & Carr A.M. (1996). The Schizosaccharomyces pombe rad3 checkpoint gene. EMBO J 15, 6641-6651.
    • (1996) EMBO J , vol.15 , pp. 6641-6651
    • Bentley, N.J.1    Carr, A.M.2
  • 16
    • 0028353634 scopus 로고
    • Mitotic checkpoint genes in budding yeast and the dependence of mitosis on DNA replication and repair
    • 16. Weinert, T.A., Kiser, G.L. & Hartwell, L.H. (1994). Mitotic checkpoint genes in budding yeast and the dependence of mitosis on DNA replication and repair. Genes Dev. 8, 652-665.
    • (1994) Genes Dev. , vol.8 , pp. 652-665
    • Weinert, T.A.1    Kiser, G.L.2    Hartwell, L.H.3
  • 17
    • 0027971222 scopus 로고
    • An essential gene, ESR1, is required for mitotic cell growth, DNA repair and meiotic recombination in Saccharomyces cerevisiae
    • 17. Kato, R. & Ogawa, H. (1994). An essential gene, ESR1, is required for mitotic cell growth, DNA repair and meiotic recombination in Saccharomyces cerevisiae. Nucleic Acids Res. 22, 3104-3112.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3104-3112
    • Kato, R.1    Ogawa, H.2
  • 18
    • 0029088371 scopus 로고
    • TEL1, a gene involved in controlling telomere length in S. cerevisiae, is homologous to the human ataxia telangiectasia gene
    • 18. Greenwell, P.W., Kronmal, S.L., Porter, S.E., Gassenhuber, J., Obermaier, B. & Petes, T.D. (1995). TEL1, a gene involved in controlling telomere length in S. cerevisiae, is homologous to the human ataxia telangiectasia gene. Cell 82, 823-829.
    • (1995) Cell , vol.82 , pp. 823-829
    • Greenwell, P.W.1    Kronmal, S.L.2    Porter, S.E.3    Gassenhuber, J.4    Obermaier, B.5    Petes, T.D.6
  • 19
    • 0029150855 scopus 로고
    • TEL1, an S. cerevisiae homolog of the human gene mutated in ataxia telangiectasia, is functionally related to the yeast checkpoint gene MEC1
    • 19. Morrow, D.M., Tagle, D.A., Shiloh, Y., Collins, F.S. & Mieter, P. (1995). TEL1, an S. cerevisiae homolog of the human gene mutated in ataxia telangiectasia, is functionally related to the yeast checkpoint gene MEC1. Cell 82, 831-840.
    • (1995) Cell , vol.82 , pp. 831-840
    • Morrow, D.M.1    Tagle, D.A.2    Shiloh, Y.3    Collins, F.S.4    Hieter, P.5
  • 20
    • 9244229490 scopus 로고    scopus 로고
    • CDNA cloning and gene mapping of a candidate human cell-cycle checkpoint protein
    • 20. Cimprich, K.A., Shin, T.B., Keith, C.T. & Schreiber, S.L. (1996). cDNA cloning and gene mapping of a candidate human cell-cycle checkpoint protein. Proc. Natl Acad. Sci. USA 93, 2850-2855.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2850-2855
    • Cimprich, K.A.1    Shin, T.B.2    Keith, C.T.3    Schreiber, S.L.4
  • 21
    • 0032493894 scopus 로고    scopus 로고
    • The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins
    • 21. McMahon, S.B., Van Buskirk, H.A., Dugan, K.A., Copeland, T.D. & Cole, M.D. (1998). The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins. Cell 94, 363-374.
    • (1998) Cell , vol.94 , pp. 363-374
    • McMahon, S.B.1    Van Buskirk, H.A.2    Dugan, K.A.3    Copeland, T.D.4    Cole, M.D.5
  • 22
    • 0032238342 scopus 로고    scopus 로고
    • The 400 kDa subunit of the PCAF histone acetylase complex belongs to the ATM superfamily
    • 22. Vassilev, A., et al., & Nakatani Y. (1998). The 400 kDa subunit of the PCAF histone acetylase complex belongs to the ATM superfamily. Mol. Cell 2, 869-875.
    • (1998) Mol. Cell , vol.2 , pp. 869-875
    • Vassilev, A.1    Nakatani, Y.2
  • 23
    • 0032254147 scopus 로고    scopus 로고
    • The ATM-related cofactor Tra1 is a component of the purified SAGA complex
    • 23. Grant, P.A., Schieltz, D., Pray-Grant, M.G., Yates, J.R. III & Workman, J.L. (1998). The ATM-related cofactor Tra1 is a component of the purified SAGA complex. Mol. Cell 2, 863-867.
    • (1998) Mol. Cell , vol.2 , pp. 863-867
    • Grant, P.A.1    Schieltz, D.2    Pray-Grant, M.G.3    Yates J.R. III4    Workman, J.L.5
  • 24
    • 0032500640 scopus 로고    scopus 로고
    • Tra1p is a component of the yeast Ada.Spt transcriptional regulatory complexes
    • 24. Saleh, A., et al., & Brandl C.J. (1998). Tra1p is a component of the yeast Ada. Spt transcriptional regulatory complexes. J. Biol. Chem. 273, 26559-26565.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26559-26565
    • Saleh, A.1    Brandl, C.J.2
  • 26
    • 0028939115 scopus 로고
    • Multiple independent inputs are required for activation of the p70 S6 kinase
    • 26. Weng, Q.P., Andrabi, K., Kozlowski, M.T., Grove, J.R. & Avruch, J. (1995). Multiple independent inputs are required for activation of the p70 S6 kinase. Mol. Cell. Biol. 15, 2333-2340.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2333-2340
    • Weng, Q.P.1    Andrabi, K.2    Kozlowski, M.T.3    Grove, J.R.4    Avruch, J.5
  • 27
    • 0033534615 scopus 로고    scopus 로고
    • Identification of kinase-phosphatase signaling modules composed of p70 S6 kinase-protein phosphatase 2A (PP2A) and p21-activated kinase-PP2A
    • 27. Westphal, R.S., Coffee, R.L. Jr., Marotta, A., Pelech, S.L. & Wadzinski, B.E. (1999). Identification of kinase-phosphatase signaling modules composed of p70 S6 kinase-protein phosphatase 2A (PP2A) and p21-activated kinase-PP2A. J. Biol. Chem. 274, 687-692.
    • (1999) J. Biol. Chem. , vol.274 , pp. 687-692
    • Westphal, R.S.1    Coffee R.L., Jr.2    Marotta, A.3    Pelech, S.L.4    Wadzinski, B.E.5
  • 28
    • 0029808294 scopus 로고    scopus 로고
    • Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases
    • 28. Di Como, C.J. & Arndt, K.T. (1996). Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases. Genes Dev. 10, 1904-1916.
    • (1996) Genes Dev. , vol.10 , pp. 1904-1916
    • Di Como, C.J.1    Arndt, K.T.2
  • 30
    • 0030984108 scopus 로고    scopus 로고
    • B cell receptor-associated protein alpha4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A
    • 30. Murata, K., Wu, J. & Brautigan, D.L. (1997). B cell receptor-associated protein alpha4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A. Proc. Natl Acad. Sci. USA 94, 10624-10629.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10624-10629
    • Murata, K.1    Wu, J.2    Brautigan, D.L.3
  • 31
    • 0032528434 scopus 로고    scopus 로고
    • Ig receptor binding protein 1 (alpha4) is associated with a rapamycin-sensitive signal transduction in lymphocytes through direct binding to the catalytic subunit of protein phosphatase 2A
    • 31. Inui, S., Sanjo, H., Maeda, K., Yamamoto, H., Miyamoto, E. & Sakaguchi, N. (1998). Ig receptor binding protein 1 (alpha4) is associated with a rapamycin-sensitive signal transduction in lymphocytes through direct binding to the catalytic subunit of protein phosphatase 2A. Blood 92, 539-546.
    • (1998) Blood , vol.92 , pp. 539-546
    • Inui, S.1    Sanjo, H.2    Maeda, K.3    Yamamoto, H.4    Miyamoto, E.5    Sakaguchi, N.6
  • 32
    • 0033551234 scopus 로고    scopus 로고
    • Protein phosphatase 2A interacts with the 70-kDa S6 kinase and is activated by inhibition of FKBP12-rapamycin associated protein
    • 32. Peterson, R.T., Desai, B.N., Hardwick, J.S. & Schreiber, S.L. (1999). Protein phosphatase 2A interacts with the 70-kDa S6 kinase and is activated by inhibition of FKBP12-rapamycin associated protein. Proc. Natl Acad. Sci. USA 96, 4438-4442.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 4438-4442
    • Peterson, R.T.1    Desai, B.N.2    Hardwick, J.S.3    Schreiber, S.L.4
  • 33
    • 0030066934 scopus 로고    scopus 로고
    • Rapamycin blocks the phosphorylation of 4E-BP1 and inhibits cap-dependent initiation of translation
    • 33. Beretta, L., Gingras, A.C., Svitkin, Y.V., Hall, M.N. & Sonenberg, N. (1996). Rapamycin blocks the phosphorylation of 4E-BP1 and inhibits cap-dependent initiation of translation. EMBO J. 15, 658-664.
    • (1996) EMBO J. , vol.15 , pp. 658-664
    • Beretta, L.1    Gingras, A.C.2    Svitkin, Y.V.3    Hall, M.N.4    Sonenberg, N.5
  • 34
    • 0032403058 scopus 로고    scopus 로고
    • The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits turnover of the tryptophan permease
    • 34. Schmidt, A., Beck, T., Koller, A., Kunz, J. & Hall, M.N. (1998). The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits turnover of the tryptophan permease. EMBO J. 17, 6924-6931.
    • (1998) EMBO J. , vol.17 , pp. 6924-6931
    • Schmidt, A.1    Beck, T.2    Koller, A.3    Kunz, J.4    Hall, M.N.5
  • 35
    • 0028172867 scopus 로고
    • Interleukin-2-mediated elimination of the p27Kip1 cyclin-dependent kinase inhibitor prevented by rapamycin
    • 35. Nourse, J., et al., & Roberts J.M. (1994). Interleukin-2-mediated elimination of the p27Kip1 cyclin-dependent kinase inhibitor prevented by rapamycin. Nature 372, 570-573.
    • (1994) Nature , vol.372 , pp. 570-573
    • Nourse, J.1    Roberts, J.M.2
  • 37
    • 0032516080 scopus 로고    scopus 로고
    • The TOR (target of rapamycin) signal transduction pathway regulates the stability of translation initiation factor elF4G in the yeast Saccharomyces cerevisiae
    • 37. Berset, C., Trachsel, H. & Altmann, M. (1998). The TOR (target of rapamycin) signal transduction pathway regulates the stability of translation initiation factor elF4G in the yeast Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 95, 4264-4269.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 4264-4269
    • Berset, C.1    Trachsel, H.2    Altmann, M.3
  • 39
    • 0031596416 scopus 로고    scopus 로고
    • Rapamycin induces the GO program of transcriptional repression in yeast by interfering with the TOR signaling pathway
    • 39. Zaragoza, D., Ghavidel, A., Heitman, J. & Schultz, M.C. (1998). Rapamycin induces the GO program of transcriptional repression in yeast by interfering with the TOR signaling pathway. Mol. Cell. Biol. 18, 4463-4470.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4463-4470
    • Zaragoza, D.1    Ghavidel, A.2    Heitman, J.3    Schultz, M.C.4
  • 40
    • 0026659046 scopus 로고
    • Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases
    • 40. Chung, J., Kuo, C.J., Crabtree, G.R. & Blenis, J. (1992). Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases. Cell 69, 1227-1236.
    • (1992) Cell , vol.69 , pp. 1227-1236
    • Chung, J.1    Kuo, C.J.2    Crabtree, G.R.3    Blenis, J.4
  • 41
    • 0032508504 scopus 로고    scopus 로고
    • Enhanced phosphorylation of p53 by ATM in response to DNA damage
    • 41. Banin, S., et al., & Ziv Y. (1998). Enhanced phosphorylation of p53 by ATM in response to DNA damage. Science 281, 1674-1677.
    • (1998) Science , vol.281 , pp. 1674-1677
    • Banin, S.1    Ziv, Y.2
  • 42
    • 0032508608 scopus 로고    scopus 로고
    • Activation of the ATM kinase by ionizing radiation and phosphorylation of p53
    • 42. Canman, C.E., et al., & Siliciano J.D. (1998). Activation of the ATM kinase by ionizing radiation and phosphorylation of p53. Science 281, 1677-1679.
    • (1998) Science , vol.281 , pp. 1677-1679
    • Canman, C.E.1    Siliciano, J.D.2
  • 43
    • 0030941458 scopus 로고    scopus 로고
    • P53, the cellular gatekeeper for growth and division
    • 43. Levine, A.J. (1997). p53, the cellular gatekeeper for growth and division. Cell 88, 323-331.
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 44
    • 0033555260 scopus 로고    scopus 로고
    • A role for ATR in the DNA damage-induced phosphorylation of p53
    • 44. Tibbetts, R.S., et al., & Abraham R.T. (1999). A role for ATR in the DNA damage-induced phosphorylation of p53. Genes Dev. 13, 152-157.
    • (1999) Genes Dev. , vol.13 , pp. 152-157
    • Tibbetts, R.S.1    Abraham, R.T.2
  • 45
    • 0032514485 scopus 로고    scopus 로고
    • DNA-dependent protein kinase acts upstream of p53 in response to DNA damage
    • 45. Woo, R.A., McLure, K.G., Lees-Miller, S.P., Rancourt, D.E. & Lee, P.W. (1998). DNA-dependent protein kinase acts upstream of p53 in response to DNA damage. Nature 394, 700-704.
    • (1998) Nature , vol.394 , pp. 700-704
    • Woo, R.A.1    McLure, K.G.2    Lees-Miller, S.P.3    Rancourt, D.E.4    Lee, P.W.5
  • 46
    • 0030924912 scopus 로고    scopus 로고
    • DNA repair. A sense-abl response?
    • 46. Brown, L & McCarthy, N. (1997). DNA repair. A sense-abl response? Nature 387, 450-451.
    • (1997) Nature , vol.387 , pp. 450-451
    • Brown, L.1    McCarthy, N.2
  • 47
    • 0029924347 scopus 로고    scopus 로고
    • Nuclear tyrosine kinases: From Abl to WEE1
    • 47. Pendergast, A.M. (1996). Nuclear tyrosine kinases: from Abl to WEE1. Curr. Opin. Cell Biol. 8, 174-181.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 174-181
    • Pendergast, A.M.1
  • 48
    • 0029664616 scopus 로고    scopus 로고
    • Rad-dependent response of the chk1-encoded protein kinase at the DNA damage checkpoint
    • 48. Walworth, N.C. & Bernards, R. (1996). rad-dependent response of the chk1-encoded protein kinase at the DNA damage checkpoint. Science 271, 353-356.
    • (1996) Science , vol.271 , pp. 353-356
    • Walworth, N.C.1    Bernards, R.2
  • 49
    • 0030768948 scopus 로고    scopus 로고
    • Cdc25 mitotic inducer targeted by chk1 DNA damage checkpoint kinase
    • 49. Furnari, B., Rhind, N. & Russell, P. (1997). Cdc25 mitotic inducer targeted by chk1 DNA damage checkpoint kinase. Science 277, 1495-1497.
    • (1997) Science , vol.277 , pp. 1495-1497
    • Furnari, B.1    Rhind, N.2    Russell, P.3
  • 50
    • 0031840253 scopus 로고    scopus 로고
    • ATM-dependent activation of p53 involves dephosphorylation and association with 14-3-3 proteins
    • 50. Waterman, M.J., Stavridi, E.S., Waterman, J.L. & Halazonetis, T.D. (1998). ATM-dependent activation of p53 involves dephosphorylation and association with 14-3-3 proteins. Nat. Genet. 19, 175-178.
    • (1998) Nat. Genet. , vol.19 , pp. 175-178
    • Waterman, M.J.1    Stavridi, E.S.2    Waterman, J.L.3    Halazonetis, T.D.4
  • 51
    • 0032548058 scopus 로고    scopus 로고
    • The 14-3-3 proteins positively regulate rapamycin-sensitive signaling
    • 51. Bertram, P.G., Zeng, C., Thorson, J., Shaw, A.S. & Zheng, X.F. (1998). The 14-3-3 proteins positively regulate rapamycin-sensitive signaling. Curr. Biol. 8, 1259-1267.
    • (1998) Curr. Biol. , vol.8 , pp. 1259-1267
    • Bertram, P.G.1    Zeng, C.2    Thorson, J.3    Shaw, A.S.4    Zheng, X.F.5
  • 52
    • 0029392854 scopus 로고
    • HEAT repeats in the Huntington's disease protein
    • 52. Andrade, M.A. & Bork, P. (1995). HEAT repeats in the Huntington's disease protein [letter]. Nat. Genet. 11, 115-116.
    • (1995) Nat. Genet. , vol.11 , pp. 115-116
    • Andrade, M.A.1    Bork, P.2
  • 53
    • 0033534405 scopus 로고    scopus 로고
    • The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs
    • 53. Groves, M.R., Hanlon, N., Turowski, P., Hemmings, B.A. & Barford, D. (1999). The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs. Cell 96, 99-110.
    • (1999) Cell , vol.96 , pp. 99-110
    • Groves, M.R.1    Hanlon, N.2    Turowski, P.3    Hemmings, B.A.4    Barford, D.5
  • 54
    • 0031887111 scopus 로고    scopus 로고
    • Amino acids stimulate phosphorylation of p70S6k and organization of rat adipocytes into multicelluiar clusters
    • 54. Fox, H.L., Kimball, S.R., Jefferson, L.S. & Lynch, C.J. (1998). Amino acids stimulate phosphorylation of p70S6k and organization of rat adipocytes into multicelluiar clusters. Am. J. Physiol. 274, C206-213.
    • (1998) Am. J. Physiol. , vol.274
    • Fox, H.L.1    Kimball, S.R.2    Jefferson, L.S.3    Lynch, C.J.4
  • 55
    • 0032486268 scopus 로고    scopus 로고
    • Amino acid sufficiency and mTOR regulate p70 S6 kinase and elF-4E BP1 through a common effector mechanism
    • 55. Hara, K., Yonezawa, K., Weng, Q.P., Kozlowski, M.T., Belham, C. & Avruch, J. (1998). Amino acid sufficiency and mTOR regulate p70 S6 kinase and elF-4E BP1 through a common effector mechanism. J. Biol. Chem. 273, 14484-14494.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14484-14494
    • Hara, K.1    Yonezawa, K.2    Weng, Q.P.3    Kozlowski, M.T.4    Belham, C.5    Avruch, J.6
  • 56
    • 0032512636 scopus 로고    scopus 로고
    • Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast
    • 56. Noda, T. & Ohsumi, Y. (1998). Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast. J. Biol. Chem. 273, 3963-3966.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3963-3966
    • Noda, T.1    Ohsumi, Y.2
  • 57
    • 0033534686 scopus 로고    scopus 로고
    • Amino acid-dependent control of p70(s6k). Involvement of tRNA aminoacylation in the regulation
    • 57. liboshi, Y., et al., & Terada N. (1999). Amino acid-dependent control of p70(s6k). Involvement of tRNA aminoacylation in the regulation. J. Biol. Chem. 274, 1092-1099.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1092-1099
    • Liboshi, Y.1    Terada, N.2
  • 58
    • 0029844048 scopus 로고    scopus 로고
    • Targeted disruption of ATM leads to growth retardation, chromosomal fragmentation during meiosis, immune defects, and thymic lymphoma
    • 58. Xu, Y., Ashley, T., Brainerd, E.E., Bronson, R.T., Meyn, M.S. & Baltimore, D. (1996). Targeted disruption of ATM leads to growth retardation, chromosomal fragmentation during meiosis, immune defects, and thymic lymphoma. Genes Dev. 10, 2411-2422.
    • (1996) Genes Dev. , vol.10 , pp. 2411-2422
    • Xu, Y.1    Ashley, T.2    Brainerd, E.E.3    Bronson, R.T.4    Meyn, M.S.5    Baltimore, D.6
  • 59
    • 15844426692 scopus 로고    scopus 로고
    • Atm-deficient mice: A paradigm of ataxia telangiectasia
    • 59. Barlow, C., et al., & Wynshaw-Boris A. (1996). Atm-deficient mice: a paradigm of ataxia telangiectasia. Cell 86, 159-171.
    • (1996) Cell , vol.86 , pp. 159-171
    • Barlow, C.1    Wynshaw-Boris, A.2
  • 60
    • 0032472330 scopus 로고    scopus 로고
    • Overexpression of a kinase-inactive ATR protein causes sensitivity to DNA-damaging agents and defects in cell cycle checkpoints
    • 60. Cliby, W.A., et al., & Friend S.H. (1998). Overexpression of a kinase-inactive ATR protein causes sensitivity to DNA-damaging agents and defects in cell cycle checkpoints. EMBO J. 17, 159-169.
    • (1998) EMBO J. , vol.17 , pp. 159-169
    • Cliby, W.A.1    Friend, S.H.2
  • 61
    • 10244227923 scopus 로고    scopus 로고
    • The Atr and Atm protein kinases associate with different sites along meiotically pairing chromosomes
    • 61. Keegan, K.S., et al., & Hoekstra M.F. (1996). The Atr and Atm protein kinases associate with different sites along meiotically pairing chromosomes. Genes Dev. 10, 2423-2437.
    • (1996) Genes Dev. , vol.10 , pp. 2423-2437
    • Keegan, K.S.1    Hoekstra, M.F.2
  • 62
    • 0028953951 scopus 로고
    • DNA-dependent kinase (p350) as a candidate gene for the murine SCID defect
    • 62. Kirchgessner, C.U., et al., & Brown J.M. (1995). DNA-dependent kinase (p350) as a candidate gene for the murine SCID defect. Science 267, 1178-1183.
    • (1995) Science , vol.267 , pp. 1178-1183
    • Kirchgessner, C.U.1    Brown, J.M.2
  • 63
    • 0028960511 scopus 로고
    • Defective DNA-dependent protein kinase activity is linked to V(D)J recombination and DNA repair defects associated with the murine scid mutation
    • 63. Blunt, T., et al., & Jeggo, P.A. (1995). Defective DNA-dependent protein kinase activity is linked to V(D)J recombination and DNA repair defects associated with the murine scid mutation. Cell 80, 813-823.
    • (1995) Cell , vol.80 , pp. 813-823
    • Blunt, T.1    Jeggo, P.A.2
  • 64
    • 0033104498 scopus 로고    scopus 로고
    • Structure of DNA-dependent protein kinase: Implications for its regulation by DNA
    • 64. Leuther, K.K., Hammarsten, O., Kornberg, R.D. & Chu, G. (1999). Structure of DNA-dependent protein kinase: implications for its regulation by DNA. EMBO J. 18, 1114-1123.
    • (1999) EMBO J. , vol.18 , pp. 1114-1123
    • Leuther, K.K.1    Hammarsten, O.2    Kornberg, R.D.3    Chu, G.4
  • 65
    • 0027397867 scopus 로고
    • The DNA-dependent protein kinase: Requirement for DNA ends and association with Ku antigen
    • 65. Gottlieb, T.M. & Jackson, S.P. (1993). The DNA-dependent protein kinase: requirement for DNA ends and association with Ku antigen. Cell 72, 131-142.
    • (1993) Cell , vol.72 , pp. 131-142
    • Gottlieb, T.M.1    Jackson, S.P.2
  • 66
    • 0030479340 scopus 로고    scopus 로고
    • TOR2 is required for organization of the actin cytoskeleton in yeast
    • 66. Schmidt, A., Kunz, J. & Hall, M.N. (1996). TOR2 is required for organization of the actin cytoskeleton in yeast. Proc. Natl Acad. Sci. USA 93, 13780-13785.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13780-13785
    • Schmidt, A.1    Kunz, J.2    Hall, M.N.3
  • 67
    • 0029071264 scopus 로고
    • TOR kinase domains are required for two distinct functions, only one of which is inhibited by rapamycin
    • 67. Zheng, X.F., Florentino, D., Chen, J., Crabtree, G.R. & Schreiber, S.L. (1995). TOR kinase domains are required for two distinct functions, only one of which is inhibited by rapamycin. Cell 82, 121-130.
    • (1995) Cell , vol.82 , pp. 121-130
    • Zheng, X.F.1    Florentino, D.2    Chen, J.3    Crabtree, G.R.4    Schreiber, S.L.5
  • 68
    • 0029821651 scopus 로고    scopus 로고
    • Dual roles of ATM in the cellular response to radiation and in cell growth control
    • 68. Xu, Y. & Baltimore, D. (1996). Dual roles of ATM in the cellular response to radiation and in cell growth control. Genes Dev. 10, 2401-2410.
    • (1996) Genes Dev. , vol.10 , pp. 2401-2410
    • Xu, Y.1    Baltimore, D.2
  • 69
    • 0032161269 scopus 로고    scopus 로고
    • A suppressor of two essential checkpoint genes identifies a novel protein that negatively affects dNTP pools
    • 69. Zhao, X., Muller, E.G. & Rothstein, R. (1998). A suppressor of two essential checkpoint genes identifies a novel protein that negatively affects dNTP pools. Mol. Cell 2, 329-340.
    • (1998) Mol. Cell , vol.2 , pp. 329-340
    • Zhao, X.1    Muller, E.G.2    Rothstein, R.3
  • 70
    • 0029842109 scopus 로고    scopus 로고
    • Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP
    • 70. Choi, J., Chen, J., Schreiber, S.L. & Clardy, J. (1996). Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP. Science 273, 239-242.
    • (1996) Science , vol.273 , pp. 239-242
    • Choi, J.1    Chen, J.2    Schreiber, S.L.3    Clardy, J.4


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