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Volumn 117, Issue 10, 2004, Pages 1875-1884

Unlocking the code of 14-3-3

Author keywords

14 3 3; Cancer; Neurodegenerative disorders; Phosphoserine; Signal transduction

Indexed keywords

APOPTOSIS INDUCING FACTOR; BINDING PROTEIN; BRAIN PROTEIN; CYTOSKELETON PROTEIN; ISOPROTEIN; ONCOPROTEIN; PHOSPHOPROTEIN PHOSPHATASE 1; PHOSPHOPROTEIN PHOSPHATASE 2A; PHOSPHOSERINE; PHOSPHOTHREONINE; PROTEIN 14 3 3; TRANSCRIPTION FACTOR; TUBERIN; TUMOR SUPPRESSOR PROTEIN;

EID: 2942552470     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.01171     Document Type: Article
Times cited : (414)

References (136)
  • 2
    • 0037631324 scopus 로고    scopus 로고
    • 14-3-3 connects glycogen synthase kinase-3 beta to tau within a brain microtubule-associated tau phosphorylation complex
    • Agarwal-Mawal, A., Qureshi, H. Y., Cafferty, P. W., Yuan, Z., Han, D., Lin, R. and Paudel, H. K. (2003). 14-3-3 connects glycogen synthase kinase-3 beta to tau within a brain microtubule-associated tau phosphorylation complex. J. Biol. Chem. 278, 12722-12728.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12722-12728
    • Agarwal-Mawal, A.1    Qureshi, H.Y.2    Cafferty, P.W.3    Yuan, Z.4    Han, D.5    Lin, R.6    Paudel, H.K.7
  • 3
    • 0036914288 scopus 로고    scopus 로고
    • Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants
    • Aitken, A. (2002). Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants. Plant Mol. Biol. 50, 993-1010.
    • (2002) Plant Mol. Biol. , vol.50 , pp. 993-1010
    • Aitken, A.1
  • 4
    • 0028970251 scopus 로고
    • 14-3-3 alpha and delta are the phosphorylated forms of raf-activating 14-3-3 beta and zeta. In vivo stoichiometric phosphorylation in brain at a Ser-Pro-Glu-Lys MOTIF
    • Aitken, A., Howell, S., Jones, D., Madrazo, J. and Patel, Y. (1995). 14-3-3 alpha and delta are the phosphorylated forms of raf-activating 14-3-3 beta and zeta. In vivo stoichiometric phosphorylation in brain at a Ser-Pro-Glu-Lys MOTIF. J. Biol. Chem. 270, 5706-5709.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5706-5709
    • Aitken, A.1    Howell, S.2    Jones, D.3    Madrazo, J.4    Patel, Y.5
  • 5
    • 0035854674 scopus 로고    scopus 로고
    • BRCA1 is a selective co-activator of 14-3-3 sigma gene transcription in mouse embryonic stem cells
    • Aprelikova, O., Pace, A. J., Fang, B., Koller, B. H. and Liu, E. T. (2001). BRCA1 is a selective co-activator of 14-3-3 sigma gene transcription in mouse embryonic stem cells. J. Biol. Chem. 276, 25647-25650.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25647-25650
    • Aprelikova, O.1    Pace, A.J.2    Fang, B.3    Koller, B.H.4    Liu, E.T.5
  • 7
    • 0037249343 scopus 로고    scopus 로고
    • Akt phosphorylates the Yes-associated protein, YAP, to induce interaction with 14-3-3 and attenuation of p73-mediated apoptosis
    • Basu, S., Totty, N. F., Irwin, M. S., Sudol, M. and Downward, J. (2003). Akt phosphorylates the Yes-associated protein, YAP, to induce interaction with 14-3-3 and attenuation of p73-mediated apoptosis. Mol. Cell 11, 11-23.
    • (2003) Mol. Cell , vol.11 , pp. 11-23
    • Basu, S.1    Totty, N.F.2    Irwin, M.S.3    Sudol, M.4    Downward, J.5
  • 10
    • 0141722623 scopus 로고    scopus 로고
    • 14-3-3 proteins in the nervous system
    • Berg, D., Holzmann, C. and Riess, O. (2003). 14-3-3 proteins in the nervous system. Nat. Rev. Neurosci. 4, 752-762.
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 752-762
    • Berg, D.1    Holzmann, C.2    Riess, O.3
  • 13
    • 0032959886 scopus 로고    scopus 로고
    • Identification of constitutive and ras-inducible phosphorylation sites of KSR: Implications for 14-3-3 binding, mitogen-activated protein kinase binding, and KSR overexpression
    • Cacace, A. M., Michaud, N. R., Therrien, M., Mathes, K., Copeland, T., Rubin, G. M. and Morrison, D. K. (1999). Identification of constitutive and ras-inducible phosphorylation sites of KSR: implications for 14-3-3 binding, mitogen-activated protein kinase binding, and KSR overexpression. Mol. Cell Biol. 19, 229-240.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 229-240
    • Cacace, A.M.1    Michaud, N.R.2    Therrien, M.3    Mathes, K.4    Copeland, T.5    Rubin, G.M.6    Morrison, D.K.7
  • 14
    • 0035918148 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase signaling inhibits DAF-16 DNA binding and function via 14-3-3-dependent and 14-3-3-independent pathways
    • Cahill, C. M., Tzivion, G., Nasrin, N., Ogg, S., Dore, J., Ruvkun, G. and Alexander-Bridges, M. (2001). Phosphatidylinositol 3-kinase signaling inhibits DAF-16 DNA binding and function via 14-3-3-dependent and 14-3-3-independent pathways. J. Biol. Chem. 276, 13402-13410.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13402-13410
    • Cahill, C.M.1    Tzivion, G.2    Nasrin, N.3    Ogg, S.4    Dore, J.5    Ruvkun, G.6    Alexander-Bridges, M.7
  • 15
    • 0037385481 scopus 로고    scopus 로고
    • Refinement of a 400-kb critical region allows genotypic differentiation between isolated lissencephaly, Miller-Dieker syndrome, and other phenotypes secondary to deletions of 17p13.3
    • Cardoso, C., Leventer, R. J., Ward, H. L., Toyo-Oka, K., Chung, J., Gross, A., Martin, C. L., Allanson, J., Pilz, D. T., Olney, A. H. et al. (2003). Refinement of a 400-kb critical region allows genotypic differentiation between isolated lissencephaly, Miller-Dieker syndrome, and other phenotypes secondary to deletions of 17p13.3. Am. J. Hum. Genet. 72, 918-930.
    • (2003) Am. J. Hum. Genet. , vol.72 , pp. 918-930
    • Cardoso, C.1    Leventer, R.J.2    Ward, H.L.3    Toyo-Oka, K.4    Chung, J.5    Gross, A.6    Martin, C.L.7    Allanson, J.8    Pilz, D.T.9    Olney, A.H.10
  • 16
    • 0041356888 scopus 로고    scopus 로고
    • Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner
    • Castro, A. F., Rebhun, J. F., Clark, G. J. and Quilliam, L. A. (2003). Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner. J. Biol. Chem. 278, 32493-32496.
    • (2003) J. Biol. Chem. , vol.278 , pp. 32493-32496
    • Castro, A.F.1    Rebhun, J.F.2    Clark, G.J.3    Quilliam, L.A.4
  • 17
    • 0037705415 scopus 로고    scopus 로고
    • 14-3-3beta is a p90 ribosomal S6 kinase (RSK) isoform 1-binding protein that negatively regulates RSK kinase activity
    • Cavet, M. E., Lehoux, S. and Berk, B. C. (2003). 14-3-3beta is a p90 ribosomal S6 kinase (RSK) isoform 1-binding protein that negatively regulates RSK kinase activity. J. Biol. Chem. 278, 18376-18383.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18376-18383
    • Cavet, M.E.1    Lehoux, S.2    Berk, B.C.3
  • 18
    • 0033533612 scopus 로고    scopus 로고
    • 14-3-3Sigma is required to prevent mitotic catastrophe after DNA damage
    • Chan, T. A., Hermeking, H., Lengauer, C., Kinzler, K. W. and Vogelstein, B. (1999). 14-3-3Sigma is required to prevent mitotic catastrophe after DNA damage. Nature 401, 616-620.
    • (1999) Nature , vol.401 , pp. 616-620
    • Chan, T.A.1    Hermeking, H.2    Lengauer, C.3    Kinzler, K.W.4    Vogelstein, B.5
  • 19
  • 20
    • 0037449905 scopus 로고    scopus 로고
    • Mammalian and yeast 14-3-3 isoforms form distinct patterns of dimers in vivo
    • Chaudhri, M., Scarabel, M. and Aitken, A. (2003). Mammalian and yeast 14-3-3 isoforms form distinct patterns of dimers in vivo. Biochem. Biophys. Res. Commun. 300, 679-685.
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 679-685
    • Chaudhri, M.1    Scarabel, M.2    Aitken, A.3
  • 22
    • 0142027900 scopus 로고    scopus 로고
    • Chk1 kinase negatively regulates mitotic function of Cdc25A phosphatase through 14-3-3 binding
    • Chen, M. S., Ryan, C. E. and Piwnica-Worms, H. (2003). Chk1 kinase negatively regulates mitotic function of Cdc25A phosphatase through 14-3-3 binding. Mol. Cell Biol. 23, 7488-7497.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 7488-7497
    • Chen, M.S.1    Ryan, C.E.2    Piwnica-Worms, H.3
  • 23
    • 0043193866 scopus 로고    scopus 로고
    • Protein phosphatase 2A dephosphorylation of phosphoserine 112 plays the gatekeeper role for BAD-mediated apoptosis
    • Chiang, C. W., Kanies, C., Kim, K. W., Fang, W. B., Parkhurst, C., Xie, M., Henry, T. and Yang, E. (2003). Protein phosphatase 2A dephosphorylation of phosphoserine 112 plays the gatekeeper role for BAD-mediated apoptosis. Mol. Cell Biol. 23, 6350-6362.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 6350-6362
    • Chiang, C.W.1    Kanies, C.2    Kim, K.W.3    Fang, W.B.4    Parkhurst, C.5    Xie, M.6    Henry, T.7    Yang, E.8
  • 25
    • 0037081563 scopus 로고    scopus 로고
    • Protein phosphatase 1-targeted in many directions
    • Cohen, P. T. (2002). Protein phosphatase 1-targeted in many directions. J. Cell Sci. 115, 241-256.
    • (2002) J. Cell Sci. , vol.115 , pp. 241-256
    • Cohen, P.T.1
  • 26
    • 0033635235 scopus 로고    scopus 로고
    • 14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation
    • Datta, S. R., Katsov, A., Hu, L., Petros, A., Fesik, S. W., Yaffe, M. B. and Greenberg, M. E. (2000). 14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation. Mol. Cell 6, 41-51.
    • (2000) Mol. Cell , vol.6 , pp. 41-51
    • Datta, S.R.1    Katsov, A.2    Hu, L.3    Petros, A.4    Fesik, S.W.5    Yaffe, M.B.6    Greenberg, M.E.7
  • 27
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt
    • del Peso, L., Gonzalez-Garcia, M., Page, C., Herrera, R. and Nunez, G. (1997). Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 278, 687-689.
    • (1997) Science , vol.278 , pp. 687-689
    • del Peso, L.1    Gonzalez-Garcia, M.2    Page, C.3    Herrera, R.4    Nunez, G.5
  • 28
    • 0034729189 scopus 로고    scopus 로고
    • Downregulation of 14-3-3sigma prevents clonal evolution and leads to immortalization of primary human keratinocytes
    • Dellambra, E., Golisano, O., Bondanza, S., Siviero, E., Lacal, P., Molinari, M., D'Atri, S. and de Luca, M. (2000). Downregulation of 14-3-3sigma prevents clonal evolution and leads to immortalization of primary human keratinocytes. J. Cell Biol. 149, 1117-1130.
    • (2000) J. Cell Biol. , vol.149 , pp. 1117-1130
    • Dellambra, E.1    Golisano, O.2    Bondanza, S.3    Siviero, E.4    Lacal, P.5    Molinari, M.6    D'Atri, S.7    de Luca, M.8
  • 29
    • 0037080956 scopus 로고    scopus 로고
    • Regulation of Raf-1 activation and signalling by dephosphorylation
    • Dhillon, A. S., Meikle, S., Yazici, Z., Eulitz, M. and Kolch, W. (2002). Regulation of Raf-1 activation and signalling by dephosphorylation. EMBO J. 21, 64-71.
    • (2002) EMBO J. , vol.21 , pp. 64-71
    • Dhillon, A.S.1    Meikle, S.2    Yazici, Z.3    Eulitz, M.4    Kolch, W.5
  • 31
    • 0027486966 scopus 로고
    • Lissencephaly. A human brain malformation associated with deletion of the LIS1 gene located at chromosome 17p13
    • Dobyns, W. B., Reiner, O., Carrozzo, R. and Ledbetter, D. H. (1993). Lissencephaly. A human brain malformation associated with deletion of the LIS1 gene located at chromosome 17p13. JAMA 270, 2838-2842.
    • (1993) JAMA , vol.270 , pp. 2838-2842
    • Dobyns, W.B.1    Reiner, O.2    Carrozzo, R.3    Ledbetter, D.H.4
  • 32
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard, L. and Helenius, A. (2003). Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell. Biol. 4, 181-191.
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 33
    • 0037846441 scopus 로고    scopus 로고
    • Serine 776 of ataxin-1 is critical for polyglutamine-induced disease in SCA1 transgenic mice
    • Emamian, E. S., Kaytor, M. D., Duvick, L. A., Zu, T., Tousey, S. K., Zoghbi, H. Y., Clark, H. B. and Orr, H. T. (2003). Serine 776 of ataxin-1 is critical for polyglutamine-induced disease in SCA1 transgenic mice. Neuron 38, 375-387.
    • (2003) Neuron. , vol.38 , pp. 375-387
    • Emamian, E.S.1    Kaytor, M.D.2    Duvick, L.A.3    Zu, T.4    Tousey, S.K.5    Zoghbi, H.Y.6    Clark, H.B.7    Orr, H.T.8
  • 37
    • 0041707637 scopus 로고    scopus 로고
    • 14-3-3 acts as an intramolecular bridge to regulate cdc25B localization and activity
    • Giles, N., Forrest, A. and Gabrielli, B. (2003). 14-3-3 acts as an intramolecular bridge to regulate cdc25B localization and activity. J. Biol. Chem. 278, 28580-28587.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28580-28587
    • Giles, N.1    Forrest, A.2    Gabrielli, B.3
  • 38
    • 0036794093 scopus 로고    scopus 로고
    • 14-3-3 regulates actin dynamics by stabilizing phosphorylated cofilin
    • Gohla, A. and Bokoch, G. M. (2002). 14-3-3 regulates actin dynamics by stabilizing phosphorylated cofilin. Curr. Biol. 12, 1704-1710.
    • (2002) Curr. Biol. , vol.12 , pp. 1704-1710
    • Gohla, A.1    Bokoch, G.M.2
  • 39
    • 0035810050 scopus 로고    scopus 로고
    • Localization of human Cdc25C is regulated both by nuclear export and 14-3-3 protein binding
    • Graves, P. R., Lovly, C. M., Uy, G. L. and Piwnica-Worms, H. (2001). Localization of human Cdc25C is regulated both by nuclear export and 14-3-3 protein binding. Oncogene 20, 1839-1851.
    • (2001) Oncogene , vol.20 , pp. 1839-1851
    • Graves, P.R.1    Lovly, C.M.2    Uy, G.L.3    Piwnica-Worms, H.4
  • 40
    • 0036671331 scopus 로고    scopus 로고
    • Use of 14-3-3 in the diagnosis of Creutzfeldt-Jakob disease
    • Green, A. J. (2002). Use of 14-3-3 in the diagnosis of Creutzfeldt-Jakob disease. Biochem. Soc. Trans. 30, 382-386.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 382-386
    • Green, A.J.1
  • 41
    • 0034608955 scopus 로고    scopus 로고
    • Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization
    • Grozinger, C. M. and Schreiber, S. L. (2000). Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization. Proc. Natl. Acad. Sci. USA 97, 7835-7840.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7835-7840
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 43
    • 0034682667 scopus 로고    scopus 로고
    • 14-3-3zeta is an effector of tau protein phosphorylation
    • Hashiguchi, M., Sobue, K. and Paudel, H. K. (2000). 14-3-3zeta is an effector of tau protein phosphorylation. J. Biol. Chem. 275, 25247-25254.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25247-25254
    • Hashiguchi, M.1    Sobue, K.2    Paudel, H.K.3
  • 46
    • 0029840653 scopus 로고    scopus 로고
    • The 14-3-3 brain protein in cerebrospinal fluid as a marker for transmissible spongiform encephalopathies
    • Hsich, G., Kenney, K., Gibbs, C. J., Lee, K. H. and Harrington, M. G. (1996). The 14-3-3 brain protein in cerebrospinal fluid as a marker for transmissible spongiform encephalopathies. N. Engl. J. Med. 335, 924-930.
    • (1996) N. Engl. J. Med. , vol.335 , pp. 924-930
    • Hsich, G.1    Kenney, K.2    Gibbs, C.J.3    Lee, K.H.4    Harrington, M.G.5
  • 47
    • 0043127125 scopus 로고    scopus 로고
    • Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
    • Inoki, K., Li, Y., Xu, T. and Guan, K. L. (2003). Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling. Genes Dev. 17, 1829-1834.
    • (2003) Genes Dev. , vol.17 , pp. 1829-1834
    • Inoki, K.1    Li, Y.2    Xu, T.3    Guan, K.L.4
  • 48
    • 0034597517 scopus 로고    scopus 로고
    • Frequent hypermethylation of CpG islands and loss of expression of the 14-3-3 sigma gene in human hepatocellular carcinoma
    • Iwata, N., Yamamoto, H., Sasaki, S., Itoh, F., Suzuki, H., Kikuchi, T., Kaneto, H., Iku, S., Ozeki, I., Karino, Y. et al. (2000). Frequent hypermethylation of CpG islands and loss of expression of the 14-3-3 sigma gene in human hepatocellular carcinoma. Oncogene 19, 5298-5302.
    • (2000) Oncogene , vol.19 , pp. 5298-5302
    • Iwata, N.1    Yamamoto, H.2    Sasaki, S.3    Itoh, F.4    Suzuki, H.5    Kikuchi, T.6    Kaneto, H.7    Iku, S.8    Ozeki, I.9    Karino, Y.10
  • 49
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • Janssens, V. and Goris, J. (2001). Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem. J. 353, 417-439.
    • (2001) Biochem. J. , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 50
    • 0035811597 scopus 로고    scopus 로고
    • Protein phosphatases 1 and 2A promote Raf-1 activation by regulating 14-3-3 interactions
    • Jaumot, M. and Hancock, J. F. (2001). Protein phosphatases 1 and 2A promote Raf-1 activation by regulating 14-3-3 interactions. Oncogene 20, 3949-3958.
    • (2001) Oncogene , vol.20 , pp. 3949-3958
    • Jaumot, M.1    Hancock, J.F.2
  • 51
    • 0042242580 scopus 로고    scopus 로고
    • Regulation of Chk1 includes chromatin association and 14-3-3 binding following phosphorylation on Ser-345
    • Jiang, K., Pereira, E., Maxfield, M., Russell, B., Goudelock, D. M. and Sanchez, Y. (2003). Regulation of Chk1 includes chromatin association and 14-3-3 binding following phosphorylation on Ser-345. J. Biol. Chem. 278, 25207-25217.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25207-25217
    • Jiang, K.1    Pereira, E.2    Maxfield, M.3    Russell, B.4    Goudelock, D.M.5    Sanchez, Y.6
  • 52
    • 0029067231 scopus 로고
    • Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: Implications for function as adapter proteins
    • Jones, D. H., Ley, S. and Aitken, A. (1995). Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: implications for function as adapter proteins. FEBS Lett. 368, 55-58.
    • (1995) FEBS Lett. , vol.368 , pp. 55-58
    • Jones, D.H.1    Ley, S.2    Aitken, A.3
  • 54
    • 0035902509 scopus 로고    scopus 로고
    • A germ-line Tsc1 mutation causes tumor development and embryonic lethality that are similar, but not identical to, those caused by Tsc2 mutation in mice
    • Kobayashi, T., Minowa, O., Sugitani, Y., Takai, S., Mitani, H., Kobayashi, E., Noda, T. and Hino, O. (2001). A germ-line Tsc1 mutation causes tumor development and embryonic lethality that are similar, but not identical to, those caused by Tsc2 mutation in mice. Proc. Natl. Acad. Sci. USA 98, 8762-8767.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8762-8767
    • Kobayashi, T.1    Minowa, O.2    Sugitani, Y.3    Takai, S.4    Mitani, H.5    Kobayashi, E.6    Noda, T.7    Hino, O.8
  • 56
    • 0033134794 scopus 로고    scopus 로고
    • Binding of 14-3-3 proteins and nuclear export control the intracellular localization of the mitotic inducer Cdc25
    • Kumagai, A. and Dunphy, W. G. (1999). Binding of 14-3-3 proteins and nuclear export control the intracellular localization of the mitotic inducer Cdc25. Gene Dev. 13, 1067-1072.
    • (1999) Gene Dev. , vol.13 , pp. 1067-1072
    • Kumagai, A.1    Dunphy, W.G.2
  • 57
    • 0034725698 scopus 로고    scopus 로고
    • Association of the cyclin-dependent kinases and 14-3-3 sigma negatively regulates cell cycle progression
    • Laronga, C., Yang, H. Y., Neal, C. and Lee, M. H. (2000). Association of the cyclin-dependent kinases and 14-3-3 sigma negatively regulates cell cycle progression. J. Biol. Chem. 275, 23106-23112.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23106-23112
    • Laronga, C.1    Yang, H.Y.2    Neal, C.3    Lee, M.H.4
  • 58
    • 0029970593 scopus 로고    scopus 로고
    • Neurofibrillary tangles of Alzheimer's disease brains contain 14-3-3 proteins
    • Layfield, R., Fergusson, J., Aitken, A., Lowe, J., Landon, M. and Mayer, R. J. (1996). Neurofibrillary tangles of Alzheimer's disease brains contain 14-3-3 proteins. Neurosci. Lett. 209, 57-60.
    • (1996) Neurosci. Lett. , vol.209 , pp. 57-60
    • Layfield, R.1    Fergusson, J.2    Aitken, A.3    Lowe, J.4    Landon, M.5    Mayer, R.J.6
  • 59
    • 0025904444 scopus 로고
    • A68: A major subunit of paired helical filaments and derivatized forms of normal Tau
    • Lee, V. M., Balin, B. J., Otvos, L., Jr and Trojanowski, J. Q. (1991). A68: a major subunit of paired helical filaments and derivatized forms of normal Tau. Science 251, 675-678.
    • (1991) Science , vol.251 , pp. 675-678
    • Lee, V.M.1    Balin, B.J.2    Otvos Jr., L.3    Trojanowski, J.Q.4
  • 61
    • 0027326971 scopus 로고
    • Molecular cloning and expression of the transformation sensitive epithelial marker stratifin. A member of a protein family that has been involved in the protein kinase C signalling pathway
    • Leffers, H., Madsen, P., Rasmussen, H. H., Honore, B., Andersen, A. H., Walbum, E., Vandekerckhove, J. and Celis, J. E. (1993). Molecular cloning and expression of the transformation sensitive epithelial marker stratifin. A member of a protein family that has been involved in the protein kinase C signalling pathway. J. Mol. Biol. 231, 982-998.
    • (1993) J. Mol. Biol. , vol.231 , pp. 982-998
    • Leffers, H.1    Madsen, P.2    Rasmussen, H.H.3    Honore, B.4    Andersen, A.H.5    Walbum, E.6    Vandekerckhove, J.7    Celis, J.E.8
  • 62
    • 0035451327 scopus 로고    scopus 로고
    • LIS1: From cortical malformation to essential protein of cellular dynamics
    • Leventer, R. J., Cardoso, C., Ledbetter, D. H. and Dobyns, W. B. (2001). LIS1: from cortical malformation to essential protein of cellular dynamics. Trends Neurosci. 24, 489-492.
    • (2001) Trends Neurosci. , vol.24 , pp. 489-492
    • Leventer, R.J.1    Cardoso, C.2    Ledbetter, D.H.3    Dobyns, W.B.4
  • 63
    • 0038190932 scopus 로고    scopus 로고
    • The p38 and MK2 kinase cascade phosphorylates tuberin, the tuberous sclerosis 2 gene product, and enhances its interaction with 14-3-3
    • Li, Y., Inoki, K., Vacratsis, P. and Guan, K. L. (2003). The p38 and MK2 kinase cascade phosphorylates tuberin, the tuberous sclerosis 2 gene product, and enhances its interaction with 14-3-3. J. Biol. Chem. 278, 13663-13671.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13663-13671
    • Li, Y.1    Inoki, K.2    Vacratsis, P.3    Guan, K.L.4
  • 64
    • 0036297889 scopus 로고    scopus 로고
    • 14-3-3 antagonizes Ras-mediated Raf-1 recruitment to the plasma membrane to maintain signaling fidelity
    • Light, Y., Paterson, H. and Marais, R. (2002). 14-3-3 antagonizes Ras-mediated Raf-1 recruitment to the plasma membrane to maintain signaling fidelity. Mol. Cell. Biol. 22, 4984-4996.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4984-4996
    • Light, Y.1    Paterson, H.2    Marais, R.3
  • 66
    • 0037112527 scopus 로고    scopus 로고
    • 14-3-3 interacts with the tumor suppressor tuberin at Akt phosphorylation site(s)
    • Liu, M. Y., Cai, S., Espejo, A., Bedford, M. T. and Walker, C. L. (2002). 14-3-3 interacts with the tumor suppressor tuberin at Akt phosphorylation site(s). Cancer Res. 62, 6475-6480.
    • (2002) Cancer Res. , vol.62 , pp. 6475-6480
    • Liu, M.Y.1    Cai, S.2    Espejo, A.3    Bedford, M.T.4    Walker, C.L.5
  • 67
    • 0034661857 scopus 로고    scopus 로고
    • Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155
    • Lizcano, J. M., Morrice, N. and Cohen, P. (2000). Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155. Biochem. J. 349, 547-557.
    • (2000) Biochem. J. , vol.349 , pp. 547-557
    • Lizcano, J.M.1    Morrice, N.2    Cohen, P.3
  • 68
    • 0036884733 scopus 로고    scopus 로고
    • Pathogenesis of Parkinson's disease: Dopamine, vesicles and alpha-synuclein
    • Lotharius, J. and Brundin, P. (2002). Pathogenesis of Parkinson's disease: dopamine, vesicles and alpha-synuclein. Nat. Rev. Neurosci. 3, 932-942.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 932-942
    • Lotharius, J.1    Brundin, P.2
  • 69
    • 0036606360 scopus 로고    scopus 로고
    • ER transport signals and trafficking of potassium channels and receptors
    • Ma, D. and Jan, L. Y. (2002). ER transport signals and trafficking of potassium channels and receptors. Curr. Opin. Neurobiol. 12, 287-292.
    • (2002) Curr. Opin. Neurobiol. , vol.12 , pp. 287-292
    • Ma, D.1    Jan, L.Y.2
  • 70
    • 0038540963 scopus 로고    scopus 로고
    • United at last: The tuberous sclerosis complex gene products connect the phosphomositide 3-kinase/Akt pathway to mammalian target of rapamycin (mTOR) signalling
    • Manning, B. D. and Cantley, L. C. (2003). United at last: the tuberous sclerosis complex gene products connect the phosphomositide 3-kinase/Akt pathway to mammalian target of rapamycin (mTOR) signalling. Biochem. Soc. Trans. 31, 573-578.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 573-578
    • Manning, B.D.1    Cantley, L.C.2
  • 71
    • 0242389822 scopus 로고    scopus 로고
    • PP1 control of M phase entry exerted through 14-3-3-regulated Cdc25 dephosphorylation
    • Margolis, S. S., Walsh, S., Weiser, D. C., Yoshida, M., Shenolikr, S. and Kornbluth, S. (2003). PP1 control of M phase entry exerted through 14-3-3-regulated Cdc25 dephosphorylation. EMBO J. 22, 5734-5745.
    • (2003) EMBO J. , vol.22 , pp. 5734-5745
    • Margolis, S.S.1    Walsh, S.2    Weiser, D.C.3    Yoshida, M.4    Shenolikr, S.5    Kornbluth, S.6
  • 72
    • 0033586783 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with a nonphosphorylated protein ligand, exoenzyme S of Pseudomonas aeruginosa
    • Masters, S. C., Pederson, K. J., Zhang, L., Barbieri, J. T. and Fu, H. (1999). Interaction of 14-3-3 with a nonphosphorylated protein ligand, exoenzyme S of Pseudomonas aeruginosa. Biochemistry 38, 5216-5221.
    • (1999) Biochemistry , vol.38 , pp. 5216-5221
    • Masters, S.C.1    Pederson, K.J.2    Zhang, L.3    Barbieri, J.T.4    Fu, H.5
  • 73
    • 0032924812 scopus 로고    scopus 로고
    • Characterization of colonic polyps by two-dimensional gel electrophoresis
    • Melis, R. and White, R. (1999). Characterization of colonic polyps by two-dimensional gel electrophoresis. Electrophoresis 20, 1055-1064.
    • (1999) Electrophoresis , vol.20 , pp. 1055-1064
    • Melis, R.1    White, R.2
  • 76
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin, A. J., Tanner, J. W., Allen, P. M. and Shaw, A. S. (1996). Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 84, 889-897.
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 77
    • 0034528346 scopus 로고    scopus 로고
    • 14-3-3 proteins: Regulation of subcellular localization by molecular interference
    • Muslin, A. J. and Xing, H. (2000). 14-3-3 proteins: regulation of subcellular localization by molecular interference. Cell Signal. 12, 703-709.
    • (2000) Cell Signal. , vol.12 , pp. 703-709
    • Muslin, A.J.1    Xing, H.2
  • 78
  • 82
    • 0037112329 scopus 로고    scopus 로고
    • Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals
    • O'Kelly, I., Butler, M. H., Zilberberg, N. and Goldstein, S. A. (2002). Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals. Cell 111, 577-588.
    • (2002) Cell , vol.111 , pp. 577-588
    • O'Kelly, I.1    Butler, M.H.2    Zilberberg, N.3    Goldstein, S.A.4
  • 83
    • 0035917466 scopus 로고    scopus 로고
    • Crystal structure of the 14-3-3zeta: Serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation
    • Obsil, T., Ghirlando, R., Klein, D. C., Ganguly, S. and Dyda, F. (2001). Crystal structure of the 14-3-3zeta: serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation. Cell 105, 257-267.
    • (2001) Cell , vol.105 , pp. 257-267
    • Obsil, T.1    Ghirlando, R.2    Klein, D.C.3    Ganguly, S.4    Dyda, F.5
  • 84
    • 0032741978 scopus 로고    scopus 로고
    • Tsc2(+/-) mice develop tumors in multiple sites that express gelsolin and are influenced by genetic background
    • Onda, H., Lueck, A., Marks, P. W., Warren, H. B. and Kwiatkowski, D. J. (1999). Tsc2(+/-) mice develop tumors in multiple sites that express gelsolin and are influenced by genetic background. J. Clin. Invest. 104, 687-695.
    • (1999) J. Clin. Invest. , vol.104 , pp. 687-695
    • Onda, H.1    Lueck, A.2    Marks, P.W.3    Warren, H.B.4    Kwiatkowski, D.J.5
  • 85
    • 0042178312 scopus 로고    scopus 로고
    • Protein phosphatase 2A positively regulates Ras signaling by dephosphorylating KSR1 and Raf-1 on critical 14-3-3 binding sites
    • Ory, S., Zhou, M., Conrads, T. P., Veenstra, T. D. and Morrison, D. K. (2003). Protein phosphatase 2A positively regulates Ras signaling by dephosphorylating KSR1 and Raf-1 on critical 14-3-3 binding sites. Curr. Biol. 13, 1356-1364.
    • (2003) Curr. Biol. , vol.13 , pp. 1356-1364
    • Ory, S.1    Zhou, M.2    Conrads, T.P.3    Veenstra, T.D.4    Morrison, D.K.5
  • 86
    • 0030832166 scopus 로고    scopus 로고
    • Proteome profiling of bladder squamous cell carcinomas: Identification of markers that define their degree of differentiation
    • Ostergaard, M., Rasmussen, H. H., Nielsen, H. V., Vorum, H., Orntoft, T. F., Wolf, H. and Celis, J. E. (1997). Proteome profiling of bladder squamous cell carcinomas: identification of markers that define their degree of differentiation. Cancer Res. 57, 4111-4117.
    • (1997) Cancer Res. , vol.57 , pp. 4111-4117
    • Ostergaard, M.1    Rasmussen, H.H.2    Nielsen, H.V.3    Vorum, H.4    Orntoft, T.F.5    Wolf, H.6    Celis, J.E.7
  • 88
    • 0036786954 scopus 로고    scopus 로고
    • The 14-3-3 proteins Rad24 and Rad25 negatively regulate Byr2 by affecting its localization in Schizosaccharomyces pombe
    • Ozoe, F., Kurokawa, R., Kobayashi, Y., Jeong, H. T., Tanaka, K., Sen, K., Nakagawa, T., Matsuda, H. and Kawamukai, M. (2002). The 14-3-3 proteins Rad24 and Rad25 negatively regulate Byr2 by affecting its localization in Schizosaccharomyces pombe. Mol. Cell. Biol. 22, 7105-7119.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7105-7119
    • Ozoe, F.1    Kurokawa, R.2    Kobayashi, Y.3    Jeong, H.T.4    Tanaka, K.5    Sen, K.6    Nakagawa, T.7    Matsuda, H.8    Kawamukai, M.9
  • 89
    • 0033516674 scopus 로고    scopus 로고
    • Tumor necrosis factor induces phosphorylation and translocation of BAD through a phosphatidylinositide-3-OH kinase-dependent pathway
    • Pastorino, J. G., Tafani, M. and Farber, J. L. (1999). Tumor necrosis factor induces phosphorylation and translocation of BAD through a phosphatidylinositide-3-OH kinase-dependent pathway. J. Biol. Chem. 274, 19411-19416.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19411-19416
    • Pastorino, J.G.1    Tafani, M.2    Farber, J.L.3
  • 90
    • 0026355413 scopus 로고
    • Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations
    • Pearson, R. B. and Kemp, B. E. (1991). Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations. Methods Enzymol. 200, 62-81.
    • (1991) Methods Enzymol. , vol.200 , pp. 62-81
    • Pearson, R.B.1    Kemp, B.E.2
  • 91
    • 0030611095 scopus 로고    scopus 로고
    • Miotic and G2 checkpoint control: Regulation of 14-3-3 protein binding by phosphorylation of Cdc25c on serine 216
    • Peng, C.-Y., Graves, P. R., Thomas, R. S., Wu, Z., Shaw, A. S. and Piwnica-Worms, H. (1997). Miotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25c on serine 216. Science 277, 1501-1505.
    • (1997) Science , vol.277 , pp. 1501-1505
    • Peng, C.-Y.1    Graves, P.R.2    Thomas, R.S.3    Wu, Z.4    Shaw, A.S.5    Piwnica-Worms, H.6
  • 93
    • 0037092442 scopus 로고    scopus 로고
    • A role for alpha-synuclein in the regulation of dopamine biosynthesis
    • Perez, R. G., Waymire, J. C., Lin, E., Liu, J. J., Guo, F. and Zigmond, M. J. (2002). A role for alpha-synuclein in the regulation of dopamine biosynthesis. J. Neurosci. 22, 3090-3099.
    • (2002) J. Neurosci. , vol.22 , pp. 3090-3099
    • Perez, R.G.1    Waymire, J.C.2    Lin, E.3    Liu, J.J.4    Guo, F.5    Zigmond, M.J.6
  • 94
    • 0032568665 scopus 로고    scopus 로고
    • 14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove
    • Petosa, C., Masters, S. C., Bankston, L. A., Pohl, J., Wang, B., Fu, H. and Liddington, R. C. (1998). 14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove. J. Biol. Chem. 273, 16305-16310.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16305-16310
    • Petosa, C.1    Masters, S.C.2    Bankston, L.A.3    Pohl, J.4    Wang, B.5    Fu, H.6    Liddington, R.C.7
  • 95
    • 0043092653 scopus 로고    scopus 로고
    • Proteomic identification of 14-3-3zeta as a mitogen-activated protein kinase-activated protein kinase 2 substrate: Role in dimer formation and ligand binding
    • Powell, D. W., Rane, M. J., Joughin, B. A., Kalmukova, R., Hong, J. H., Tidor, B., Dean, W. L., Pierce, W. M., Klein, J. B., Yaffe, M. B. et al. (2003). Proteomic identification of 14-3-3zeta as a mitogen-activated protein kinase-activated protein kinase 2 substrate: role in dimer formation and ligand binding. Mol. Cell. Biol. 23, 5376-5387.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5376-5387
    • Powell, D.W.1    Rane, M.J.2    Joughin, B.A.3    Kalmukova, R.4    Hong, J.H.5    Tidor, B.6    Dean, W.L.7    Pierce, W.M.8    Klein, J.B.9    Yaffe, M.B.10
  • 96
    • 0026901457 scopus 로고
    • Complementary DNA cloning of a novel epithelial cell marker protein, HME1, that may be down-regulated in neoplastic mammary cells
    • Prasad, G. L., Valverius, E. M., McDuffie, E. and Cooper, H. L. (1992). Complementary DNA cloning of a novel epithelial cell marker protein, HME1, that may be down-regulated in neoplastic mammary cells. Cell Growth Differ. 3, 507-513.
    • (1992) Cell Growth Differ. , vol.3 , pp. 507-513
    • Prasad, G.L.1    Valverius, E.M.2    McDuffie, E.3    Cooper, H.L.4
  • 98
    • 0034067992 scopus 로고    scopus 로고
    • Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: Differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase-3beta
    • Reynolds, C. H., Betts, J. C., Blackstock, W. P., Nebreda, A. R. and Anderton, B. H. (2000). Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase-3beta. J. Neurochem. 74, 1587-1595.
    • (2000) J. Neurochem. , vol.74 , pp. 1587-1595
    • Reynolds, C.H.1    Betts, J.C.2    Blackstock, W.P.3    Nebreda, A.R.4    Anderton, B.H.5
  • 99
    • 0033180582 scopus 로고    scopus 로고
    • Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding
    • Rittinger, K., Budman, J., Xu, J., Volinia, S., Cantley, L. C., Smerdon, S. J., Gamblin, S. J. and Yaffe, M. B. (1999). Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding. Mol. Cell 4, 153-166.
    • (1999) Mol. Cell , vol.4 , pp. 153-166
    • Rittinger, K.1    Budman, J.2    Xu, J.3    Volinia, S.4    Cantley, L.C.5    Smerdon, S.J.6    Gamblin, S.J.7    Yaffe, M.B.8
  • 100
    • 0034817007 scopus 로고    scopus 로고
    • Data mining the Arabidopsis genome reveals fifteen 14-3-3 genes. Expression is demonstrated for two out of five novel genes
    • Rosenquist, M., Alsterfjord, M., Larsson, C. and Sommarin, M. (2001). Data mining the Arabidopsis genome reveals fifteen 14-3-3 genes. Expression is demonstrated for two out of five novel genes. Plant Physiol. 127, 142-149.
    • (2001) Plant Physiol. , vol.127 , pp. 142-149
    • Rosenquist, M.1    Alsterfjord, M.2    Larsson, C.3    Sommarin, M.4
  • 101
    • 0030867582 scopus 로고    scopus 로고
    • Conservation of the Chk1 checkpoint pathway in mammals: Linkage of DNA damage to Cdk regultion through Cdc25
    • Sanchez, Y., Wong, C., Thoma, R., Richman, R., Wu, Z., Piwnica-Worms, H. and Elledge, S. (1997). Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to Cdk regultion through Cdc25. Science 277, 1497-1501.
    • (1997) Science , vol.277 , pp. 1497-1501
    • Sanchez, Y.1    Wong, C.2    Thoma, R.3    Richman, R.4    Wu, Z.5    Piwnica-Worms, H.6    Elledge, S.7
  • 102
    • 0042679580 scopus 로고    scopus 로고
    • The MSP receptor regulates alpha6beta4 and alpha3beta1 integrins via 14-3-3 proteins in keratinocyte migration
    • Santoro, M. M., Gaudino, G. and Marchisio, P. C. (2003a). The MSP receptor regulates alpha6beta4 and alpha3beta1 integrins via 14-3-3 proteins in keratinocyte migration. Dev. Cell 5, 257-271.
    • (2003) Dev. Cell , vol.5 , pp. 257-271
    • Santoro, M.M.1    Gaudino, G.2    Marchisio, P.C.3
  • 103
    • 0347986619 scopus 로고    scopus 로고
    • Protein phosphatase 1 binds to phospho-Ser-1394 of the macrophage-stimulating protein receptor
    • Santoro, M. M., Gaudino, G. and Villa-Moruzzi, E. (2003b). Protein phosphatase 1 binds to phospho-Ser-1394 of the macrophage-stimulating protein receptor. Biochem. J. 376, 587-594.
    • (2003) Biochem. J. , vol.376 , pp. 587-594
    • Santoro, M.M.1    Gaudino, G.2    Villa-Moruzzi, E.3
  • 106
    • 0037462662 scopus 로고    scopus 로고
    • 14-3-3beta binds to and negatively regulates the tuberous sclerosis complex 2 (TSC2) tumor suppressor gene product, tuberin
    • Shumway, S. D., Li, Y. and Xiong, Y. (2003). 14-3-3beta binds to and negatively regulates the tuberous sclerosis complex 2 (TSC2) tumor suppressor gene product, tuberin. J. Biol. Chem. 278, 2089-2092.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2089-2092
    • Shumway, S.D.1    Li, Y.2    Xiong, Y.3
  • 108
    • 0034662605 scopus 로고    scopus 로고
    • Inactivation of the 14-3-3 sigma gene is associated with 5′ CpG island hypermethylation in human cancers
    • Suzuki, H., Itoh, F., Toyota, M., Kikuchi, T., Kakiuchi, H. and Imai, K. (2000). Inactivation of the 14-3-3 sigma gene is associated with 5′ CpG island hypermethylation in human cancers. Cancer Res. 60, 4353-4357.
    • (2000) Cancer Res. , vol.60 , pp. 4353-4357
    • Suzuki, H.1    Itoh, F.2    Toyota, M.3    Kikuchi, T.4    Kakiuchi, H.5    Imai, K.6
  • 109
    • 0034682812 scopus 로고    scopus 로고
    • BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival
    • Tan, Y., Demeter, M. R., Ruan, H. and Comb, M. J. (2000). BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival. J. Biol. Chem. 275, 25865-25869.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25865-25869
    • Tan, Y.1    Demeter, M.R.2    Ruan, H.3    Comb, M.J.4
  • 110
    • 0000040623 scopus 로고    scopus 로고
    • Association of the TLX-2 homeodomain and 14-3-3eta signaling proteins
    • Tang, S. J., Suen, T. C., McInnes, R. R. and Buchwald, M. (1998). Association of the TLX-2 homeodomain and 14-3-3eta signaling proteins. J. Biol. Chem. 273, 25356-25363.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25356-25363
    • Tang, S.J.1    Suen, T.C.2    McInnes, R.R.3    Buchwald, M.4
  • 111
    • 0042701991 scopus 로고    scopus 로고
    • Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activatingg protein complex toward Rheb
    • Tee, A. R., Manning, B. D., Roux, P. P., Cantley, L. C. and Blenis, J. (2003). Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activatingg protein complex toward Rheb. Curr. Biol. 13, 1259-1268.
    • (2003) Curr. Biol. , vol.13 , pp. 1259-1268
    • Tee, A.R.1    Manning, B.D.2    Roux, P.P.3    Cantley, L.C.4    Blenis, J.5
  • 113
    • 0036479325 scopus 로고    scopus 로고
    • 14-3-3 proteins: Active cofactors in cellular regulation by serine/threonine phosphorylation
    • Tzivion, G. and Avruch, J. (2002). 14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation. J. Biol. Chem. 277, 3061-3064.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3061-3064
    • Tzivion, G.1    Avruch, J.2
  • 114
    • 1842832448 scopus 로고    scopus 로고
    • 14-3-3 protein is a component of Lewy bodies in Parkinson's disease - Mutation analysis and association studies of 14-3-3 eta
    • Ubl, A., Berg, D., Holzmann, C., Kruger, R., Berger, K., Arzberger, T., Bornemann, A. and Riess, O. (2002). 14-3-3 protein is a component of Lewy bodies in Parkinson's disease - mutation analysis and association studies of 14-3-3 eta. Brain Res. Mol. Brain Res. 108, 33-39.
    • (2002) Brain Res. Mol. Brain Res. , vol.108 , pp. 33-39
    • Ubl, A.1    Berg, D.2    Holzmann, C.3    Kruger, R.4    Berger, K.5    Arzberger, T.6    Bornemann, A.7    Riess, O.8
  • 115
    • 0035821727 scopus 로고    scopus 로고
    • Hypermethylation of 14-3-3 sigma (stratifin) is an early event in breast cancer
    • Umbricht, C. B., Evron, E., Gabrielson, E., Ferguson, A., Marks, J. and Sukumar, S. (2001). Hypermethylation of 14-3-3 sigma (stratifin) is an early event in breast cancer. Oncogene 20, 3348-3353.
    • (2001) Oncogene , vol.20 , pp. 3348-3353
    • Umbricht, C.B.1    Evron, E.2    Gabrielson, E.3    Ferguson, A.4    Marks, J.5    Sukumar, S.6
  • 116
    • 0034788964 scopus 로고    scopus 로고
    • 14-3-3 proteins: Key regulators of cell division, signalling and apoptosis
    • van Hemert, M. J., Steensma, H. Y. and van Heusden, G. P. (2001). 14-3-3 proteins: key regulators of cell division, signalling and apoptosis. Bioessays 23, 936-946.
    • (2001) Bioessays , vol.23 , pp. 936-946
    • van Hemert, M.J.1    Steensma, H.Y.2    van Heusden, G.P.3
  • 118
    • 0033592326 scopus 로고    scopus 로고
    • Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display
    • Wang, B., Yang, H., Liu, Y. C., Jelinek, T., Zhang, L., Ruoslahti, E. and Fu, H. (1999). Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display. Biochemistry 38, 12499-12504.
    • (1999) Biochemistry , vol.38 , pp. 12499-12504
    • Wang, B.1    Yang, H.2    Liu, Y.C.3    Jelinek, T.4    Zhang, L.5    Ruoslahti, E.6    Fu, H.7
  • 119
    • 0029815121 scopus 로고    scopus 로고
    • Molecular evolution of the 14-3-3 protein family
    • Wang, W. and Shakes, D. C. (1996). Molecular evolution of the 14-3-3 protein family. J. Mol. Evol. 43, 384-398.
    • (1996) J. Mol. Evol. , vol.43 , pp. 384-398
    • Wang, W.1    Shakes, D.C.2
  • 121
    • 0031840253 scopus 로고    scopus 로고
    • ATM-dependent activation of p53 involves dephosphorylation and association with 14-3-3 proteins
    • Waterman, M. J., Stavridi, E. S., Waterman, J. L. and 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
  • 123
    • 0141815677 scopus 로고    scopus 로고
    • The dimeric versus monomeric status of 14-3-3zeta is controlled by phosphorylation of Ser58 at the dimer interface
    • Woodcock, J. M., Murphy, J., Stomski, F. C., Berndt, M. C. and Lopez, A. F. (2003). The dimeric versus monomeric status of 14-3-3zeta is controlled by phosphorylation of Ser58 at the dimer interface. J. Biol. Chem. 278, 36323-36327.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36323-36327
    • Woodcock, J.M.1    Murphy, J.2    Stomski, F.C.3    Berndt, M.C.4    Lopez, A.F.5
  • 124
    • 0028979375 scopus 로고
    • Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways
    • Xiao, B., Smerdon, S. J., Jones, D. H., Dodson, G. G., Soneji, Y., Aitken, A. and Gamblin, S. J. (1995). Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways. Nature 376, 188-191.
    • (1995) Nature , vol.376 , pp. 188-191
    • Xiao, B.1    Smerdon, S.J.2    Jones, D.H.3    Dodson, G.G.4    Soneji, Y.5    Aitken, A.6    Gamblin, S.J.7
  • 125
    • 0036278335 scopus 로고    scopus 로고
    • Dopamine-dependent neurotoxicity of alpha-synuclein: A mechanism for selective neurodegeneration in Parkinson disease
    • Xu, J., Kao, S. Y., Lee, F. J., Song, W., Jin, L. W. and Yankner, B. A. (2002). Dopamine-dependent neurotoxicity of alpha-synuclein: a mechanism for selective neurodegeneration in Parkinson disease. Nat. Med. 8, 600-606.
    • (2002) Nat. Med. , vol.8 , pp. 600-606
    • Xu, J.1    Kao, S.Y.2    Lee, F.J.3    Song, W.4    Jin, L.W.5    Yankner, B.A.6
  • 126
    • 0037138389 scopus 로고    scopus 로고
    • How do 14-3-3 proteins work? Gatekeeper phosphorylation and the molecular anvil hypothesis
    • Yaffe, M. B. (2002). How do 14-3-3 proteins work? Gatekeeper phosphorylation and the molecular anvil hypothesis. FEBS Lett. 513, 53-57.
    • (2002) FEBS Lett. , vol.513 , pp. 53-57
    • Yaffe, M.B.1
  • 128
    • 0141529779 scopus 로고    scopus 로고
    • 14-3-3 sigma positively regulates p53 and suppresses tumor growth
    • Yang, H. Y., Wen, Y. Y., Chen, C. H., Lozano, G. and Lee, M. H. (2003). 14-3-3 sigma positively regulates p53 and suppresses tumor growth. Mol. Cell. Biol. 23, 7096-7107.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7096-7107
    • Yang, H.Y.1    Wen, Y.Y.2    Chen, C.H.3    Lozano, G.4    Lee, M.H.5
  • 129
    • 0033561439 scopus 로고    scopus 로고
    • Maintenance of G2 arrest in the Xenopus oocyte: A role for 14-3-3-mediated inhibition of Cdc25 nuclear import
    • Yang, J., Winkler, K., Yoshida, M. and Kornbluth, S. (1999). Maintenance of G2 arrest in the Xenopus oocyte: a role for 14-3-3-mediated inhibition of Cdc25 nuclear import. EMBO J. 18, 2174-2183.
    • (1999) EMBO J. , vol.18 , pp. 2174-2183
    • Yang, J.1    Winkler, K.2    Yoshida, M.3    Kornbluth, S.4
  • 130
    • 0031881032 scopus 로고    scopus 로고
    • The genetic basis of tuberous sclerosis
    • Young, J. and Povey, S. (1998). The genetic basis of tuberous sclerosis. Mol. Med. Today 4, 313-319.
    • (1998) Mol. Med. Today , vol.4 , pp. 313-319
    • Young, J.1    Povey, S.2
  • 131
    • 0037447231 scopus 로고    scopus 로고
    • 14-3-3 dimers probe the assembly status of multimeric membrane proteins
    • Yuan, H., Michelsen, K. and Schwappach, B. (2003). 14-3-3 dimers probe the assembly status of multimeric membrane proteins. Curr. Biol. 13, 638-646.
    • (2003) Curr. Biol. , vol.13 , pp. 638-646
    • Yuan, H.1    Michelsen, K.2    Schwappach, B.3
  • 132
    • 0035168621 scopus 로고    scopus 로고
    • The spinocerebellar ataxia type 1 protein, ataxin-1, has RNA-binding activity that is inversely affected by the length of its polyglutamine tract
    • Yue, S., Serra, H. G., Zoghbi, H. Y., Orr, H. T., Waymire, J. C., Lin, E., Liu, J. J., Guo, F. and Zigmond, M. J. (2001). The spinocerebellar ataxia type 1 protein, ataxin-1, has RNA-binding activity that is inversely affected by the length of its polyglutamine tract. Hum. Mol. Genet. 10, 25-30.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 25-30
    • Yue, S.1    Serra, H.G.2    Zoghbi, H.Y.3    Orr, H.T.4    Waymire, J.C.5    Lin, E.6    Liu, J.J.7    Guo, F.8    Zigmond, M.J.9
  • 133
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
    • Zha, J., Harada, H., Yang, E., Jockel, J. and Korsmeyer, S. J. (1996). Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell 87, 619-628.
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 134
    • 0035798551 scopus 로고    scopus 로고
    • Identification of a novel interaction of 14-3-3 with p190RhoGEF
    • Zhai, J., Lin, H., Shamim, M., Schlaepfer, W. W. and Canete-Soler, R. (2001). Identification of a novel interaction of 14-3-3 with p190RhoGEF. J. Biol. Chem. 276, 41318-41324.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41318-41324
    • Zhai, J.1    Lin, H.2    Shamim, M.3    Schlaepfer, W.W.4    Canete-Soler, R.5
  • 135
    • 0038141979 scopus 로고    scopus 로고
    • Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins
    • Zhang, Y., Gao, X., Saucedo, L. J., Ru, B., Edgar, B. A. and Pan, D. (2003). Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins. Nat. Cell Biol. 5, 578-581.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 578-581
    • Zhang, Y.1    Gao, X.2    Saucedo, L.J.3    Ru, B.4    Edgar, B.A.5    Pan, D.6
  • 136
    • 0036301210 scopus 로고    scopus 로고
    • Solution structure and functional analysis of the cysteine-rich C1 domain of kinase suppressor of Ras (KSR)
    • Zhou, M., Horita, D. A., Waugh, D. S., Byrd, R. A. and Morrison, D. K. (2002). Solution structure and functional analysis of the cysteine-rich C1 domain of kinase suppressor of Ras (KSR). J. Mol. Biol. 315, 435-446.
    • (2002) J. Mol. Biol. , vol.315 , pp. 435-446
    • Zhou, M.1    Horita, D.A.2    Waugh, D.S.3    Byrd, R.A.4    Morrison, D.K.5


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