메뉴 건너뛰기




Volumn 22, Issue 7, 2011, Pages 713-719

The 14-3-3 proteins in regulation of cellular metabolism

Author keywords

14 3 3 Proteins; Cell signaling; Membrane association; Metabolism; Tyrosine hydroxylase

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; INSULIN; MAMMALIAN TARGET OF RAPAMYCIN; PROTEIN 14 3 3;

EID: 80455164541     PISSN: 10849521     EISSN: 10963634     Source Type: Journal    
DOI: 10.1016/j.semcdb.2011.08.008     Document Type: Review
Times cited : (133)

References (93)
  • 1
    • 3543035767 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins
    • Meek S.E., Lane W.S., Piwnica-Worms H. Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins. J Biol Chem 2004, 279:32046-32054.
    • (2004) J Biol Chem , vol.279 , pp. 32046-32054
    • Meek, S.E.1    Lane, W.S.2    Piwnica-Worms, H.3
  • 2
    • 2342651419 scopus 로고    scopus 로고
    • 14-3-3-Affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking
    • Pozuelo Rubio M., Geraghty K.M., Wong B.H., Wood N.T., Campbell D.G., Morrice N., et al. 14-3-3-Affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking. Biochem J 2004, 379:395-408.
    • (2004) Biochem J , vol.379 , pp. 395-408
    • Pozuelo Rubio, M.1    Geraghty, K.M.2    Wong, B.H.3    Wood, N.T.4    Campbell, D.G.5    Morrice, N.6
  • 3
    • 4344598183 scopus 로고    scopus 로고
    • Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization
    • Jin J., Smith F.D., Stark C., Wells C.D., Fawcett J.P., Kulkarni S., et al. Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. Curr Biol 2004, 14:1436-1450.
    • (2004) Curr Biol , vol.14 , pp. 1436-1450
    • Jin, J.1    Smith, F.D.2    Stark, C.3    Wells, C.D.4    Fawcett, J.P.5    Kulkarni, S.6
  • 4
    • 33745103749 scopus 로고    scopus 로고
    • Does isoform diversity explain functional differences in the 14-3-3 protein family?
    • Kjarland E., Keen T.J., Kleppe R. Does isoform diversity explain functional differences in the 14-3-3 protein family?. Curr Pharm Biotechnol 2006, 7:217-223.
    • (2006) Curr Pharm Biotechnol , vol.7 , pp. 217-223
    • Kjarland, E.1    Keen, T.J.2    Kleppe, R.3
  • 5
    • 77955250361 scopus 로고    scopus 로고
    • Proteomic and biochemical analysis of 14-3-3-binding proteins during C2-ceramide-induced apoptosis
    • Pozuelo-Rubio M. Proteomic and biochemical analysis of 14-3-3-binding proteins during C2-ceramide-induced apoptosis. FEBS J 2010, 277:3321-3342.
    • (2010) FEBS J , vol.277 , pp. 3321-3342
    • Pozuelo-Rubio, M.1
  • 6
    • 67649235671 scopus 로고    scopus 로고
    • Proteomic profiling of tandem affinity purified 14-3-3 protein complexes in Arabidopsis thaliana
    • Chang I.F., Curran A., Woolsey R., Quilici D., Cushman J.C., Mittler R., et al. Proteomic profiling of tandem affinity purified 14-3-3 protein complexes in Arabidopsis thaliana. Proteomics 2009, 9:2967-2985.
    • (2009) Proteomics , vol.9 , pp. 2967-2985
    • Chang, I.F.1    Curran, A.2    Woolsey, R.3    Quilici, D.4    Cushman, J.C.5    Mittler, R.6
  • 7
    • 56749144036 scopus 로고    scopus 로고
    • Proteomic analysis of bovine sperm YWHA binding partners identify proteins involved in signaling and metabolism
    • Puri P., Myers K., Kline D., Vijayaraghavan S. Proteomic analysis of bovine sperm YWHA binding partners identify proteins involved in signaling and metabolism. Biol Reprod 2008, 79:1183-1191.
    • (2008) Biol Reprod , vol.79 , pp. 1183-1191
    • Puri, P.1    Myers, K.2    Kline, D.3    Vijayaraghavan, S.4
  • 8
    • 21044434194 scopus 로고    scopus 로고
    • Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer
    • Benzinger A., Muster N., Koch H.B., Yates J.R., Hermeking H. Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer. Mol Cell Proteomics 2005, 4:785-795.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 785-795
    • Benzinger, A.1    Muster, N.2    Koch, H.B.3    Yates, J.R.4    Hermeking, H.5
  • 9
    • 0031470652 scopus 로고    scopus 로고
    • The structural basis for 14-3-3:phosphopeptide binding specificity
    • Yaffe M.B., Rittinger K., Volinia S., Caron P.R., Aitken A., Leffers H., et al. The structural basis for 14-3-3:phosphopeptide binding specificity. Cell 1997, 91:961-971.
    • (1997) Cell , vol.91 , pp. 961-971
    • Yaffe, M.B.1    Rittinger, K.2    Volinia, S.3    Caron, P.R.4    Aitken, A.5    Leffers, H.6
  • 11
    • 79951673886 scopus 로고    scopus 로고
    • Structurally constrained residues outside the binding motif are essential in the interaction of 14-3-3 and phosphorylated partner
    • Uhart M., Iglesias A.A., Bustos D.M. Structurally constrained residues outside the binding motif are essential in the interaction of 14-3-3 and phosphorylated partner. J Mol Biol 2011, 406:552-557.
    • (2011) J Mol Biol , vol.406 , pp. 552-557
    • Uhart, M.1    Iglesias, A.A.2    Bustos, D.M.3
  • 13
    • 47849083299 scopus 로고    scopus 로고
    • A combined proteome and ultrastructural localization analysis of 14-3-3 proteins in transformed human amnion (AMA) cells: definition of a framework to study isoform-specific differences
    • Moreira J.M., Shen T., Ohlsson G., Gromov P., Gromova I., Celis J.E. A combined proteome and ultrastructural localization analysis of 14-3-3 proteins in transformed human amnion (AMA) cells: definition of a framework to study isoform-specific differences. Mol Cell Proteomics 2008, 7:1225-1240.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1225-1240
    • Moreira, J.M.1    Shen, T.2    Ohlsson, G.3    Gromov, P.4    Gromova, I.5    Celis, J.E.6
  • 14
    • 45449088882 scopus 로고    scopus 로고
    • Identification of different isoforms of 14-3-3 protein family in human dermal and epidermal layers
    • Kilani R.T., Medina A., Aitken A., Jalili R.B., Carr M., Ghahary A. Identification of different isoforms of 14-3-3 protein family in human dermal and epidermal layers. Mol Cell Biochem 2008, 314:161-169.
    • (2008) Mol Cell Biochem , vol.314 , pp. 161-169
    • Kilani, R.T.1    Medina, A.2    Aitken, A.3    Jalili, R.B.4    Carr, M.5    Ghahary, A.6
  • 15
    • 68849118196 scopus 로고    scopus 로고
    • 14-3-3sigma gene silencing during melanoma progression and its role in cell cycle control and cellular senescence
    • Schultz J., Ibrahim S.M., Vera J., Kunz M. 14-3-3sigma gene silencing during melanoma progression and its role in cell cycle control and cellular senescence. Mol Cancer 2009, 8:53.
    • (2009) Mol Cancer , vol.8 , pp. 53
    • Schultz, J.1    Ibrahim, S.M.2    Vera, J.3    Kunz, M.4
  • 16
    • 33645036070 scopus 로고    scopus 로고
    • Upregulation of 14-3-3 isoforms in acute rat myocardial injuries induced by burn and lipopolysaccharide
    • He M., Zhang J., Shao L., Huang Q., Chen J., Chen H., et al. Upregulation of 14-3-3 isoforms in acute rat myocardial injuries induced by burn and lipopolysaccharide. Clin Exp Pharmacol Physiol 2006, 33:374-380.
    • (2006) Clin Exp Pharmacol Physiol , vol.33 , pp. 374-380
    • He, M.1    Zhang, J.2    Shao, L.3    Huang, Q.4    Chen, J.5    Chen, H.6
  • 17
    • 27744441297 scopus 로고    scopus 로고
    • The 14-3-3 gene expression specificity in response to stress is promoter-dependent
    • Aksamit A., Korobczak A., Skala J., Lukaszewicz M., Szopa J. The 14-3-3 gene expression specificity in response to stress is promoter-dependent. Plant Cell Physiol 2005, 46:1635-1645.
    • (2005) Plant Cell Physiol , vol.46 , pp. 1635-1645
    • Aksamit, A.1    Korobczak, A.2    Skala, J.3    Lukaszewicz, M.4    Szopa, J.5
  • 18
    • 33947715721 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-delta upregulates 14-3-3 epsilon in human endothelial cells via CCAAT/enhancer binding protein-beta
    • Brunelli L., Cieslik K.A., Alcorn J.L., Vatta M., Baldini A. Peroxisome proliferator-activated receptor-delta upregulates 14-3-3 epsilon in human endothelial cells via CCAAT/enhancer binding protein-beta. Circ Res 2007, 100:e59-e71.
    • (2007) Circ Res , vol.100
    • Brunelli, L.1    Cieslik, K.A.2    Alcorn, J.L.3    Vatta, M.4    Baldini, A.5
  • 19
    • 77955890374 scopus 로고    scopus 로고
    • Defective erythroid differentiation in miR-451 mutant mice mediated by 14-3-3zeta
    • Patrick D.M., Zhang C.C., Tao Y., Yao H., Qi X., Schwartz R.J., et al. Defective erythroid differentiation in miR-451 mutant mice mediated by 14-3-3zeta. Genes Dev 2010, 24:1614-1619.
    • (2010) Genes Dev , vol.24 , pp. 1614-1619
    • Patrick, D.M.1    Zhang, C.C.2    Tao, Y.3    Yao, H.4    Qi, X.5    Schwartz, R.J.6
  • 20
    • 77950250954 scopus 로고    scopus 로고
    • MicroRNA-375 is downregulated in gastric carcinomas and regulates cell survival by targeting PDK1 and 14-3-3zeta
    • Tsukamoto Y., Nakada C., Noguchi T., Tanigawa M., Nguyen L.T., Uchida T., et al. MicroRNA-375 is downregulated in gastric carcinomas and regulates cell survival by targeting PDK1 and 14-3-3zeta. Cancer Res 2010, 70:2339-2349.
    • (2010) Cancer Res , vol.70 , pp. 2339-2349
    • Tsukamoto, Y.1    Nakada, C.2    Noguchi, T.3    Tanigawa, M.4    Nguyen, L.T.5    Uchida, T.6
  • 21
    • 0038757833 scopus 로고    scopus 로고
    • 14-3-3epsilon is important for neuronal migration by binding to NUDEL: a molecular explanation for Miller-Dieker syndrome
    • Toyo-oka K., Shionoya A., Gambello M.J., Cardoso C., Leventer R., Ward H.L., et al. 14-3-3epsilon is important for neuronal migration by binding to NUDEL: a molecular explanation for Miller-Dieker syndrome. Nat Genet 2003, 34:274-285.
    • (2003) Nat Genet , vol.34 , pp. 274-285
    • Toyo-oka, K.1    Shionoya, A.2    Gambello, M.J.3    Cardoso, C.4    Leventer, R.5    Ward, H.L.6
  • 22
    • 53349156385 scopus 로고    scopus 로고
    • Identification of YWHAE, a gene encoding 14-3-3epsilon, as a possible susceptibility gene for schizophrenia
    • Ikeda M., Hikita T., Taya S., Uraguchi-Asaki J., Toyo-oka K., Wynshaw-Boris A., et al. Identification of YWHAE, a gene encoding 14-3-3epsilon, as a possible susceptibility gene for schizophrenia. Hum Mol Genet 2008, 17:3212-3222.
    • (2008) Hum Mol Genet , vol.17 , pp. 3212-3222
    • Ikeda, M.1    Hikita, T.2    Taya, S.3    Uraguchi-Asaki, J.4    Toyo-oka, K.5    Wynshaw-Boris, A.6
  • 23
    • 79959766877 scopus 로고    scopus 로고
    • No association of the YWHAE gene with schizophrenia, major depressive disorder or bipolar disorder in the Han Chinese population
    • Liu J., Zhou G., Ji W., Li J., Li T., Wang T., et al. No association of the YWHAE gene with schizophrenia, major depressive disorder or bipolar disorder in the Han Chinese population. Behav Genet 2011, 41:557-564.
    • (2011) Behav Genet , vol.41 , pp. 557-564
    • Liu, J.1    Zhou, G.2    Ji, W.3    Li, J.4    Li, T.5    Wang, T.6
  • 24
    • 79958157611 scopus 로고    scopus 로고
    • Meta-analysis of heterogeneous data sources for genome-scale identification of risk genes in complex phenotypes
    • Pers T.H., Hansen N.T., Lage K., Koefoed P., Dworzynski P., Miller M.L., et al. Meta-analysis of heterogeneous data sources for genome-scale identification of risk genes in complex phenotypes. Genet Epidemiol 2011, 35:318-332.
    • (2011) Genet Epidemiol , vol.35 , pp. 318-332
    • Pers, T.H.1    Hansen, N.T.2    Lage, K.3    Koefoed, P.4    Dworzynski, P.5    Miller, M.L.6
  • 26
    • 13444257670 scopus 로고    scopus 로고
    • Unchanged survival rates of 14-3-3gamma knockout mice after inoculation with pathological prion protein
    • Steinacker P., Schwarz P., Reim K., Brechlin P., Jahn O., Kratzin H., et al. Unchanged survival rates of 14-3-3gamma knockout mice after inoculation with pathological prion protein. Mol Cell Biol 2005, 25:1339-1346.
    • (2005) Mol Cell Biol , vol.25 , pp. 1339-1346
    • Steinacker, P.1    Schwarz, P.2    Reim, K.3    Brechlin, P.4    Jahn, O.5    Kratzin, H.6
  • 27
    • 77950801121 scopus 로고    scopus 로고
    • Zebrafish gene knockdowns imply roles for human YWHAG in infantile spasms and cardiomegaly
    • Komoike Y., Fujii K., Nishimura A., Hiraki Y., Hayashidani M., Shimojima K., et al. Zebrafish gene knockdowns imply roles for human YWHAG in infantile spasms and cardiomegaly. Genesis 2010, 48:233-243.
    • (2010) Genesis , vol.48 , pp. 233-243
    • Komoike, Y.1    Fujii, K.2    Nishimura, A.3    Hiraki, Y.4    Hayashidani, M.5    Shimojima, K.6
  • 28
    • 55549087214 scopus 로고    scopus 로고
    • An obligatory heterodimer of 14-3-3beta and 14-3-3epsilon is required for aldosterone regulation of the epithelial sodium channel
    • Liang X., Butterworth M.B., Peters K.W., Walker W.H., Frizzell R.A. An obligatory heterodimer of 14-3-3beta and 14-3-3epsilon is required for aldosterone regulation of the epithelial sodium channel. J Biol Chem 2008, 283:27418-27425.
    • (2008) J Biol Chem , vol.283 , pp. 27418-27425
    • Liang, X.1    Butterworth, M.B.2    Peters, K.W.3    Walker, W.H.4    Frizzell, R.A.5
  • 29
    • 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., Aitken A. Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: implications for function as adapter proteins. FEBS Lett 1995, 368:55-58.
    • (1995) FEBS Lett , vol.368 , pp. 55-58
    • Jones, D.H.1    Ley, S.2    Aitken, A.3
  • 30
    • 0037449905 scopus 로고    scopus 로고
    • Mammalian and yeast 14-3-3 isoforms form distinct patterns of dimers in vivo
    • Chaudhri M., Scarabel M., Aitken A. Mammalian and yeast 14-3-3 isoforms form distinct patterns of dimers in vivo. Biochem Biophys Res Commun 2003, 300:679-685.
    • (2003) Biochem Biophys Res Commun , vol.300 , pp. 679-685
    • Chaudhri, M.1    Scarabel, M.2    Aitken, A.3
  • 31
    • 66349125931 scopus 로고    scopus 로고
    • 14-3-3zeta/tau heterodimers regulate Slingshot activity in migrating keratinocytes
    • Kligys K., Yao J., Yu D., Jones J.C. 14-3-3zeta/tau heterodimers regulate Slingshot activity in migrating keratinocytes. Biochem Biophys Res Commun 2009, 383:450-454.
    • (2009) Biochem Biophys Res Commun , vol.383 , pp. 450-454
    • Kligys, K.1    Yao, J.2    Yu, D.3    Jones, J.C.4
  • 32
    • 0019510125 scopus 로고
    • A new activator protein that activates tryptophan 5-monooxygenase and tyrosine 3-monooxygenase in the presence of Ca2+-, calmodulin-dependent protein kinase. Purification and characterization
    • Yamauchi T., Nakata H., Fujisawa H. A new activator protein that activates tryptophan 5-monooxygenase and tyrosine 3-monooxygenase in the presence of Ca2+-, calmodulin-dependent protein kinase. Purification and characterization. J Biol Chem 1981, 256:5404-5409.
    • (1981) J Biol Chem , vol.256 , pp. 5404-5409
    • Yamauchi, T.1    Nakata, H.2    Fujisawa, H.3
  • 33
    • 0036914587 scopus 로고    scopus 로고
    • Metabolic enzymes as targets for 14-3-3 proteins
    • Huber S.C., MacKintosh C., Kaiser W.M. Metabolic enzymes as targets for 14-3-3 proteins. Plant Mol Biol 2002, 50:1053-1063.
    • (2002) Plant Mol Biol , vol.50 , pp. 1053-1063
    • Huber, S.C.1    MacKintosh, C.2    Kaiser, W.M.3
  • 34
    • 29244476034 scopus 로고    scopus 로고
    • The regulatory phosphorylated serine in full-length nitrate redutase is necessary for optimal binding to a 14-3-3 protein
    • Provan F., Haavik J., Lillo C. The regulatory phosphorylated serine in full-length nitrate redutase is necessary for optimal binding to a 14-3-3 protein. Plant Sci 2006, 170:394-398.
    • (2006) Plant Sci , vol.170 , pp. 394-398
    • Provan, F.1    Haavik, J.2    Lillo, C.3
  • 35
    • 0037662761 scopus 로고    scopus 로고
    • 14-3-3 Proteins find new partners in plant cell signalling
    • Roberts M.R. 14-3-3 Proteins find new partners in plant cell signalling. Trends Plant Sci 2003, 8:218-223.
    • (2003) Trends Plant Sci , vol.8 , pp. 218-223
    • Roberts, M.R.1
  • 36
    • 70449285205 scopus 로고
    • Factors affecting the activity of muscle phosphorylase b kinase
    • Krebs E.G., Graves D.J., Fischer E.H. Factors affecting the activity of muscle phosphorylase b kinase. J Biol Chem 1959, 234:2867-2873.
    • (1959) J Biol Chem , vol.234 , pp. 2867-2873
    • Krebs, E.G.1    Graves, D.J.2    Fischer, E.H.3
  • 37
    • 60449087924 scopus 로고    scopus 로고
    • Analysis of the protein complex associated with 14-3-3 epsilon by a deuterated-leucine labeling quantitative proteomics strategy
    • Liang S., Yu Y., Yang P., Gu S., Xue Y., Chen X. Analysis of the protein complex associated with 14-3-3 epsilon by a deuterated-leucine labeling quantitative proteomics strategy. J Chromatogr B Analyt Technol Biomed Life Sci 2009, 877:627-634.
    • (2009) J Chromatogr B Analyt Technol Biomed Life Sci , vol.877 , pp. 627-634
    • Liang, S.1    Yu, Y.2    Yang, P.3    Gu, S.4    Xue, Y.5    Chen, X.6
  • 38
    • 0041312686 scopus 로고    scopus 로고
    • 14-3-3s Regulate fructose-2,6-bisphosphate levels by binding to PKB-phosphorylated cardiac fructose-2,6-bisphosphate kinase/phosphatase
    • Pozuelo Rubio M., Peggie M., Wong B.H., Morrice N., MacKintosh C. 14-3-3s Regulate fructose-2,6-bisphosphate levels by binding to PKB-phosphorylated cardiac fructose-2,6-bisphosphate kinase/phosphatase. EMBO J 2003, 22:3514-3523.
    • (2003) EMBO J , vol.22 , pp. 3514-3523
    • Pozuelo Rubio, M.1    Peggie, M.2    Wong, B.H.3    Morrice, N.4    MacKintosh, C.5
  • 39
    • 0023652643 scopus 로고
    • Brain 14-3-3 protein is an activator protein that activates tryptophan 5-monooxygenase and tyrosine 3-monooxygenase in the presence of Ca2+, calmodulin-dependent protein kinase II
    • Ichimura T., Isobe T., Okuyama T., Yamauchi T., Fujisawa H. Brain 14-3-3 protein is an activator protein that activates tryptophan 5-monooxygenase and tyrosine 3-monooxygenase in the presence of Ca2+, calmodulin-dependent protein kinase II. FEBS Lett 1987, 219:79-82.
    • (1987) FEBS Lett , vol.219 , pp. 79-82
    • Ichimura, T.1    Isobe, T.2    Okuyama, T.3    Yamauchi, T.4    Fujisawa, H.5
  • 40
    • 39749177631 scopus 로고    scopus 로고
    • Activation and stabilization of human tryptophan hydroxylase 2 by phosphorylation and 14-3-3 binding
    • Winge I., McKinney J.A., Ying M., D'Santos C.S., Kleppe R., Knappskog P.M., et al. Activation and stabilization of human tryptophan hydroxylase 2 by phosphorylation and 14-3-3 binding. Biochem J 2008, 410:195-204.
    • (2008) Biochem J , vol.410 , pp. 195-204
    • Winge, I.1    McKinney, J.A.2    Ying, M.3    D'Santos, C.S.4    Kleppe, R.5    Knappskog, P.M.6
  • 41
    • 0035019161 scopus 로고    scopus 로고
    • Interaction of phosphorylated tyrosine hydroxylase with 14-3-3 proteins: evidence for a phosphoserine 40-dependent association
    • Kleppe R., Toska K., Haavik J. Interaction of phosphorylated tyrosine hydroxylase with 14-3-3 proteins: evidence for a phosphoserine 40-dependent association. J Neurochem 2001, 77:1097-1107.
    • (2001) J Neurochem , vol.77 , pp. 1097-1107
    • Kleppe, R.1    Toska, K.2    Haavik, J.3
  • 42
    • 0033598762 scopus 로고    scopus 로고
    • Stimulus-coupled interaction of tyrosine hydroxylase with 14-3-3 proteins
    • Itagaki C., Isobe T., Taoka M., Natsume T., Nomura N., Horigome T., et al. Stimulus-coupled interaction of tyrosine hydroxylase with 14-3-3 proteins. Biochemistry 1999, 38:15673-15680.
    • (1999) Biochemistry , vol.38 , pp. 15673-15680
    • Itagaki, C.1    Isobe, T.2    Taoka, M.3    Natsume, T.4    Nomura, N.5    Horigome, T.6
  • 43
    • 0030697998 scopus 로고    scopus 로고
    • Interaction of phosphorylated tryptophan hydroxylase with 14-3-3 proteins
    • Banik U., Wang G.A., Wagner P.D., Kaufman S. Interaction of phosphorylated tryptophan hydroxylase with 14-3-3 proteins. J Biol Chem 1997, 272:26219-26225.
    • (1997) J Biol Chem , vol.272 , pp. 26219-26225
    • Banik, U.1    Wang, G.A.2    Wagner, P.D.3    Kaufman, S.4
  • 45
    • 0025212130 scopus 로고
    • PH-dependent release of catecholamines from tyrosine hydroxylase and the effect of phosphorylation of Ser-40
    • Haavik J., Martinez A., Flatmark T. pH-dependent release of catecholamines from tyrosine hydroxylase and the effect of phosphorylation of Ser-40. FEBS Lett 1990, 262:363-365.
    • (1990) FEBS Lett , vol.262 , pp. 363-365
    • Haavik, J.1    Martinez, A.2    Flatmark, T.3
  • 46
    • 4143079145 scopus 로고    scopus 로고
    • Phosphorylation of Ser19 increases both Ser40 phosphorylation and enzyme activity of tyrosine hydroxylase in intact cells
    • Bobrovskaya L., Dunkley P.R., Dickson P.W. Phosphorylation of Ser19 increases both Ser40 phosphorylation and enzyme activity of tyrosine hydroxylase in intact cells. J Neurochem 2004, 90:857-864.
    • (2004) J Neurochem , vol.90 , pp. 857-864
    • Bobrovskaya, L.1    Dunkley, P.R.2    Dickson, P.W.3
  • 47
    • 0035798644 scopus 로고    scopus 로고
    • Phosphorylation of Ser(19) alters the conformation of tyrosine hydroxylase to increase the rate of phosphorylation of Ser(40)
    • Bevilaqua L.R., Graham M.E., Dunkley P.R., von Nagy-Felsobuki E.I., Dickson P.W. Phosphorylation of Ser(19) alters the conformation of tyrosine hydroxylase to increase the rate of phosphorylation of Ser(40). J Biol Chem 2001, 276:40411-40416.
    • (2001) J Biol Chem , vol.276 , pp. 40411-40416
    • Bevilaqua, L.R.1    Graham, M.E.2    Dunkley, P.R.3    von Nagy-Felsobuki, E.I.4    Dickson, P.W.5
  • 48
    • 13244292476 scopus 로고    scopus 로고
    • Different properties of the central and peripheral forms of human tryptophan hydroxylase
    • McKinney J., Knappskog P.M., Haavik J. Different properties of the central and peripheral forms of human tryptophan hydroxylase. J Neurochem 2005, 92:311-320.
    • (2005) J Neurochem , vol.92 , pp. 311-320
    • McKinney, J.1    Knappskog, P.M.2    Haavik, J.3
  • 49
    • 12844265993 scopus 로고    scopus 로고
    • Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N-acetyltransferase mediated by phosphoserine-205
    • Ganguly S., Weller J.L., Ho A., Chemineau P., Malpaux B., Klein D.C. Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N-acetyltransferase mediated by phosphoserine-205. Proc Natl Acad Sci U S A 2005, 102:1222-1227.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 1222-1227
    • Ganguly, S.1    Weller, J.L.2    Ho, A.3    Chemineau, P.4    Malpaux, B.5    Klein, D.C.6
  • 50
    • 67650914230 scopus 로고    scopus 로고
    • AMPK in health and disease
    • Steinberg G.R., Kemp B.E. AMPK in health and disease. Physiol Rev 2009, 89:1025-1078.
    • (2009) Physiol Rev , vol.89 , pp. 1025-1078
    • Steinberg, G.R.1    Kemp, B.E.2
  • 51
    • 12144287284 scopus 로고    scopus 로고
    • LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1
    • Lizcano J.M., Goransson O., Toth R., Deak M., Morrice N.A., Boudeau J., et al. LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1. EMBO J 2004, 23:833-843.
    • (2004) EMBO J , vol.23 , pp. 833-843
    • Lizcano, J.M.1    Goransson, O.2    Toth, R.3    Deak, M.4    Morrice, N.A.5    Boudeau, J.6
  • 52
    • 0036847993 scopus 로고    scopus 로고
    • Drosophila 14-3-3/PAR-5 is an essential mediator of PAR-1 function in axis formation
    • Benton R., Palacios I.M., St Johnston D. Drosophila 14-3-3/PAR-5 is an essential mediator of PAR-1 function in axis formation. Dev Cell 2002, 3:659-671.
    • (2002) Dev Cell , vol.3 , pp. 659-671
    • Benton, R.1    Palacios, I.M.2    St Johnston, D.3
  • 53
    • 30544437191 scopus 로고    scopus 로고
    • 14-3-3 Cooperates with LKB1 to regulate the activity and localization of QSK and SIK
    • Al-Hakim A.K., Goransson O., Deak M., Toth R., Campbell D.G., Morrice N.A., et al. 14-3-3 Cooperates with LKB1 to regulate the activity and localization of QSK and SIK. J Cell Sci 2005, 118:5661-5673.
    • (2005) J Cell Sci , vol.118 , pp. 5661-5673
    • Al-Hakim, A.K.1    Goransson, O.2    Deak, M.3    Toth, R.4    Campbell, D.G.5    Morrice, N.A.6
  • 54
    • 27144506185 scopus 로고    scopus 로고
    • The CREB coactivator TORC2 is a key regulator of fasting glucose metabolism
    • Koo S.H., Flechner L., Qi L., Zhang X., Screaton R.A., Jeffries S., et al. The CREB coactivator TORC2 is a key regulator of fasting glucose metabolism. Nature 2005, 437:1109-1111.
    • (2005) Nature , vol.437 , pp. 1109-1111
    • Koo, S.H.1    Flechner, L.2    Qi, L.3    Zhang, X.4    Screaton, R.A.5    Jeffries, S.6
  • 55
    • 5344228270 scopus 로고    scopus 로고
    • The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector
    • Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G., Jeffries S., et al. The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector. Cell 2004, 119:61-74.
    • (2004) Cell , vol.119 , pp. 61-74
    • Screaton, R.A.1    Conkright, M.D.2    Katoh, Y.3    Best, J.L.4    Canettieri, G.5    Jeffries, S.6
  • 56
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • Wullschleger S., Loewith R., Hall M.N. TOR signaling in growth and metabolism. Cell 2006, 124:471-484.
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 57
    • 65249176304 scopus 로고    scopus 로고
    • ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery
    • Jung C.H., Jun C.B., Ro S.H., Kim Y.M., Otto N.M., Cao J., et al. ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery. Mol Biol Cell 2009, 20:1992-2003.
    • (2009) Mol Biol Cell , vol.20 , pp. 1992-2003
    • Jung, C.H.1    Jun, C.B.2    Ro, S.H.3    Kim, Y.M.4    Otto, N.M.5    Cao, J.6
  • 58
    • 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., Guan K.L. 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 2003, 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
  • 59
    • 0037160104 scopus 로고    scopus 로고
    • Regulation of TSC2 by 14-3-3 binding
    • Li Y., Inoki K., Yeung R., Guan K.L. Regulation of TSC2 by 14-3-3 binding. J Biol Chem 2002, 277:44593-44596.
    • (2002) J Biol Chem , vol.277 , pp. 44593-44596
    • Li, Y.1    Inoki, K.2    Yeung, R.3    Guan, K.L.4
  • 60
    • 38349056675 scopus 로고    scopus 로고
    • Hypoxia regulates TSC1/2-mTOR signaling and tumor suppression through REDD1-mediated 14-3-3 shuttling
    • DeYoung M.P., Horak P., Sofer A., Sgroi D., Ellisen L.W. Hypoxia regulates TSC1/2-mTOR signaling and tumor suppression through REDD1-mediated 14-3-3 shuttling. Genes Dev 2008, 22:239-251.
    • (2008) Genes Dev , vol.22 , pp. 239-251
    • DeYoung, M.P.1    Horak, P.2    Sofer, A.3    Sgroi, D.4    Ellisen, L.W.5
  • 62
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • Kim J., Kundu M., Viollet B., Guan K.L. AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat Cell Biol 2011, 13:132-141.
    • (2011) Nat Cell Biol , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 63
    • 78149476877 scopus 로고    scopus 로고
    • The association of AMPK with ULK1 regulates autophagy
    • Lee J.W., Park S., Takahashi Y., Wang H.G. The association of AMPK with ULK1 regulates autophagy. PLoS One 2010, 5:e15394.
    • (2010) PLoS One , vol.5
    • Lee, J.W.1    Park, S.2    Takahashi, Y.3    Wang, H.G.4
  • 64
    • 79951680318 scopus 로고    scopus 로고
    • Regulation of autophagic activity by 14-3-3zeta proteins associated with class III phosphatidylinositol-3-kinase
    • Pozuelo-Rubio M. Regulation of autophagic activity by 14-3-3zeta proteins associated with class III phosphatidylinositol-3-kinase. Cell Death Differ 2011, 18:479-492.
    • (2011) Cell Death Differ , vol.18 , pp. 479-492
    • Pozuelo-Rubio, M.1
  • 65
    • 33644865025 scopus 로고    scopus 로고
    • Evidence that Ser87 of BimEL is phosphorylated by Akt and regulates BimEL apoptotic function
    • Qi X.J., Wildey G.M., Howe P.H. Evidence that Ser87 of BimEL is phosphorylated by Akt and regulates BimEL apoptotic function. J Biol Chem 2006, 281:813-823.
    • (2006) J Biol Chem , vol.281 , pp. 813-823
    • Qi, X.J.1    Wildey, G.M.2    Howe, P.H.3
  • 66
    • 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., Korsmeyer S.J. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell 1996, 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
  • 67
    • 0037449733 scopus 로고    scopus 로고
    • 14-3-3 Interacts directly with and negatively regulates pro-apoptotic Bax
    • Nomura M., Shimizu S., Sugiyama T., Narita M., Ito T., Matsuda H., et al. 14-3-3 Interacts directly with and negatively regulates pro-apoptotic Bax. J Biol Chem 2003, 278:2058-2065.
    • (2003) J Biol Chem , vol.278 , pp. 2058-2065
    • Nomura, M.1    Shimizu, S.2    Sugiyama, T.3    Narita, M.4    Ito, T.5    Matsuda, H.6
  • 68
    • 34250894388 scopus 로고    scopus 로고
    • BH3-only proteins and BH3 mimetics induce autophagy by competitively disrupting the interaction between Beclin 1 and Bcl-2/Bcl-X(L)
    • Maiuri M.C., Criollo A., Tasdemir E., Vicencio J.M., Tajeddine N., Hickman J.A., et al. BH3-only proteins and BH3 mimetics induce autophagy by competitively disrupting the interaction between Beclin 1 and Bcl-2/Bcl-X(L). Autophagy 2007, 3:374-376.
    • (2007) Autophagy , vol.3 , pp. 374-376
    • Maiuri, M.C.1    Criollo, A.2    Tasdemir, E.3    Vicencio, J.M.4    Tajeddine, N.5    Hickman, J.A.6
  • 71
    • 34548359244 scopus 로고    scopus 로고
    • PRAS40 is a target for mammalian target of rapamycin complex 1 and is required for signaling downstream of this complex
    • Fonseca B.D., Smith E.M., Lee V.H., MacKintosh C., Proud C.G. PRAS40 is a target for mammalian target of rapamycin complex 1 and is required for signaling downstream of this complex. J Biol Chem 2007, 282:24514-24524.
    • (2007) J Biol Chem , vol.282 , pp. 24514-24524
    • Fonseca, B.D.1    Smith, E.M.2    Lee, V.H.3    MacKintosh, C.4    Proud, C.G.5
  • 72
    • 34247148430 scopus 로고    scopus 로고
    • Substrate specificity and effect on GLUT4 translocation of the Rab GTPase-activating protein Tbc1d1
    • Roach W.G., Chavez J.A., Miinea C.P., Lienhard G.E. Substrate specificity and effect on GLUT4 translocation of the Rab GTPase-activating protein Tbc1d1. Biochem J 2007, 403:353-358.
    • (2007) Biochem J , vol.403 , pp. 353-358
    • Roach, W.G.1    Chavez, J.A.2    Miinea, C.P.3    Lienhard, G.E.4
  • 73
    • 4644300287 scopus 로고    scopus 로고
    • Insulin stimulation of GLUT4 exocytosis, but not its inhibition of endocytosis, is dependent on RabGAP AS160
    • Zeigerer A., McBrayer M.K., McGraw T.E. Insulin stimulation of GLUT4 exocytosis, but not its inhibition of endocytosis, is dependent on RabGAP AS160. Mol Biol Cell 2004, 15:4406-4415.
    • (2004) Mol Biol Cell , vol.15 , pp. 4406-4415
    • Zeigerer, A.1    McBrayer, M.K.2    McGraw, T.E.3
  • 74
    • 38749110036 scopus 로고    scopus 로고
    • Complementary regulation of TBC1D1 and AS160 by growth factors, insulin and AMPK activators
    • Chen S., Murphy J., Toth R., Campbell D.G., Morrice N.A., Mackintosh C. Complementary regulation of TBC1D1 and AS160 by growth factors, insulin and AMPK activators. Biochem J 2008, 409:449-459.
    • (2008) Biochem J , vol.409 , pp. 449-459
    • Chen, S.1    Murphy, J.2    Toth, R.3    Campbell, D.G.4    Morrice, N.A.5    Mackintosh, C.6
  • 75
    • 78650897555 scopus 로고    scopus 로고
    • Mice with AS160/TBC1D4-Thr649Ala knockin mutation are glucose intolerant with reduced insulin sensitivity and altered GLUT4 trafficking
    • Chen S., Wasserman D.H., MacKintosh C., Sakamoto K. Mice with AS160/TBC1D4-Thr649Ala knockin mutation are glucose intolerant with reduced insulin sensitivity and altered GLUT4 trafficking. Cell Metab 2011, 13:68-79.
    • (2011) Cell Metab , vol.13 , pp. 68-79
    • Chen, S.1    Wasserman, D.H.2    MacKintosh, C.3    Sakamoto, K.4
  • 76
    • 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., et al. 14-3-3 Connects glycogen synthase kinase-3 beta to tau within a brain microtubule-associated tau phosphorylation complex. J Biol Chem 2003, 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
  • 77
    • 79952119614 scopus 로고    scopus 로고
    • ER stress inhibits mTORC2 and Akt signaling through GSK-3beta-mediated phosphorylation of rictor
    • Chen C.H., Shaikenov T., Peterson T.R., Aimbetov R., Bissenbaev A.K., Lee S.W., et al. ER stress inhibits mTORC2 and Akt signaling through GSK-3beta-mediated phosphorylation of rictor. Sci Signal 2011, 4:ra10.
    • (2011) Sci Signal , vol.4
    • Chen, C.H.1    Shaikenov, T.2    Peterson, T.R.3    Aimbetov, R.4    Bissenbaev, A.K.5    Lee, S.W.6
  • 78
    • 37549000623 scopus 로고    scopus 로고
    • Muscle-specific deletion of rictor impairs insulin-stimulated glucose transport and enhances Basal glycogen synthase activity
    • Kumar A., Harris T.E., Keller S.R., Choi K.M., Magnuson M.A., Lawrence J.C. Muscle-specific deletion of rictor impairs insulin-stimulated glucose transport and enhances Basal glycogen synthase activity. Mol Cell Biol 2008, 28:61-70.
    • (2008) Mol Cell Biol , vol.28 , pp. 61-70
    • Kumar, A.1    Harris, T.E.2    Keller, S.R.3    Choi, K.M.4    Magnuson, M.A.5    Lawrence, J.C.6
  • 79
    • 33646898172 scopus 로고    scopus 로고
    • Structural determinants of 14-3-3 binding specificities and regulation of subcellular localization of 14-3-3-ligand complexes: a comparison of the X-ray crystal structures of all human 14-3-3 isoforms
    • Gardino A.K., Smerdon S.J., Yaffe M.B. Structural determinants of 14-3-3 binding specificities and regulation of subcellular localization of 14-3-3-ligand complexes: a comparison of the X-ray crystal structures of all human 14-3-3 isoforms. Semin Cancer Biol 2006, 16:173-182.
    • (2006) Semin Cancer Biol , vol.16 , pp. 173-182
    • Gardino, A.K.1    Smerdon, S.J.2    Yaffe, M.B.3
  • 80
    • 33745196467 scopus 로고    scopus 로고
    • Reversible membrane interaction of BAD requires two C-terminal lipid binding domains in conjunction with 14-3-3 protein binding
    • Hekman M., Albert S., Galmiche A., Rennefahrt U.E., Fueller J., Fischer A., et al. Reversible membrane interaction of BAD requires two C-terminal lipid binding domains in conjunction with 14-3-3 protein binding. J Biol Chem 2006, 281:17321-17336.
    • (2006) J Biol Chem , vol.281 , pp. 17321-17336
    • Hekman, M.1    Albert, S.2    Galmiche, A.3    Rennefahrt, U.E.4    Fueller, J.5    Fischer, A.6
  • 81
    • 23944495537 scopus 로고    scopus 로고
    • 14-3-3 Protein interacts with nuclear localization sequence of forkhead transcription factor FoxO4
    • Obsilova V., Vecer J., Herman P., Pabianova A., Sulc M., Teisinger J., et al. 14-3-3 Protein interacts with nuclear localization sequence of forkhead transcription factor FoxO4. Biochemistry 2005, 44:11608-11617.
    • (2005) Biochemistry , vol.44 , pp. 11608-11617
    • Obsilova, V.1    Vecer, J.2    Herman, P.3    Pabianova, A.4    Sulc, M.5    Teisinger, J.6
  • 82
    • 33745949394 scopus 로고    scopus 로고
    • 14-3-3 Proteins: regulation of endoplasmic reticulum localization and surface expression of membrane proteins
    • Shikano S., Coblitz B., Wu M., Li M. 14-3-3 Proteins: regulation of endoplasmic reticulum localization and surface expression of membrane proteins. Trends Cell Biol 2006, 16:370-375.
    • (2006) Trends Cell Biol , vol.16 , pp. 370-375
    • Shikano, S.1    Coblitz, B.2    Wu, M.3    Li, M.4
  • 83
    • 80054034515 scopus 로고    scopus 로고
    • Membrane proteins as 14-3-3 clients in functional regulation and intracellular transport
    • Smith A.J., Daut J., Schwappach B. Membrane proteins as 14-3-3 clients in functional regulation and intracellular transport. Physiology (Bethesda) 2011, 26:181-191.
    • (2011) Physiology (Bethesda) , vol.26 , pp. 181-191
    • Smith, A.J.1    Daut, J.2    Schwappach, B.3
  • 84
    • 70349501375 scopus 로고    scopus 로고
    • Linking new paradigms in protein chemistry to reversible membrane-protein interactions
    • Halskau O., Muga A., Martinez A. Linking new paradigms in protein chemistry to reversible membrane-protein interactions. Curr Protein Pept Sci 2009, 10:339-359.
    • (2009) Curr Protein Pept Sci , vol.10 , pp. 339-359
    • Halskau, O.1    Muga, A.2    Martinez, A.3
  • 85
    • 79954448500 scopus 로고    scopus 로고
    • The binding of 14-3-3γ to membranes studied by intrinsic fluorescence spectroscopy
    • Bustad H.J., Underhaug J., Halskau O., Martinez A. The binding of 14-3-3γ to membranes studied by intrinsic fluorescence spectroscopy. FEBS Lett 2011, 585:1163-1168.
    • (2011) FEBS Lett , vol.585 , pp. 1163-1168
    • Bustad, H.J.1    Underhaug, J.2    Halskau, O.3    Martinez, A.4
  • 87
    • 76249088643 scopus 로고    scopus 로고
    • A biochemical and functional protein complex involving dopamine synthesis and transport into synaptic vesicles
    • Cartier E.A., Parra L.A., Baust T.B., Quiroz M., Salazar G., Faundez V., et al. A biochemical and functional protein complex involving dopamine synthesis and transport into synaptic vesicles. J Biol Chem 2010, 285:1957-1966.
    • (2010) J Biol Chem , vol.285 , pp. 1957-1966
    • Cartier, E.A.1    Parra, L.A.2    Baust, T.B.3    Quiroz, M.4    Salazar, G.5    Faundez, V.6
  • 88
    • 54049105746 scopus 로고    scopus 로고
    • Regulation of nuclear import/export of carbohydrate response element-binding protein (ChREBP): interaction of an alpha-helix of ChREBP with the 14-3-3 proteins and regulation by phosphorylation
    • Sakiyama H., Wynn R.M., Lee W.R., Fukasawa M., Mizuguchi H., Gardner K.H., et al. Regulation of nuclear import/export of carbohydrate response element-binding protein (ChREBP): interaction of an alpha-helix of ChREBP with the 14-3-3 proteins and regulation by phosphorylation. J Biol Chem 2008, 283:24899-24908.
    • (2008) J Biol Chem , vol.283 , pp. 24899-24908
    • Sakiyama, H.1    Wynn, R.M.2    Lee, W.R.3    Fukasawa, M.4    Mizuguchi, H.5    Gardner, K.H.6
  • 89
    • 0037138389 scopus 로고    scopus 로고
    • How do 14-3-3 proteins work? - Gatekeeper phosphorylation and the molecular anvil hypothesis
    • Yaffe M.B. How do 14-3-3 proteins work? - Gatekeeper phosphorylation and the molecular anvil hypothesis. FEBS Lett 2002, 513:53-57.
    • (2002) FEBS Lett , vol.513 , pp. 53-57
    • Yaffe, M.B.1
  • 91
    • 85029434436 scopus 로고    scopus 로고
    • Seminars in cell and developmental biology [this issue].
    • Fu H, et al. Seminars in cell and developmental biology 2011;22 [this issue].
    • (2011) , Issue.22
    • Fu H1
  • 92
    • 79956048261 scopus 로고    scopus 로고
    • The phytotoxin fusicoccin promotes platelet aggregation via 14-3-3-glycoprotein Ib-IX-V interaction
    • Camoni L., Di Lucente C., Visconti S., Aducci P. The phytotoxin fusicoccin promotes platelet aggregation via 14-3-3-glycoprotein Ib-IX-V interaction. Biochem J 2011, 436:429-436.
    • (2011) Biochem J , vol.436 , pp. 429-436
    • Camoni, L.1    Di Lucente, C.2    Visconti, S.3    Aducci, P.4
  • 93
    • 80455160346 scopus 로고    scopus 로고
    • 14-3-3 Proteins As Signaling Integration Points for Cell Cycle Control and Apoptosis. Sem Cell Dev Bio.(submitted).
    • Gardino A, Yaffe M. 14-3-3 Proteins As Signaling Integration Points for Cell Cycle Control and Apoptosis. Sem Cell Dev Bio 2011.(submitted).
    • (2011)
    • Gardino A1    Yaffe, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.