메뉴 건너뛰기




Volumn 220, Issue 1-2, 2004, Pages 1-7

Human follitropin receptor (FSHR) interacts with the adapter protein 14-3-3τ

Author keywords

14 3 3 Protein; Follitropin receptor (human); G protein coupled receptor; Signal transduction

Indexed keywords

CYCLIC AMP; CYTOPLASM PROTEIN; FOLLITROPIN RECEPTOR; G PROTEIN COUPLED RECEPTOR; PROTEIN 14 3 3; TAU PROTEIN;

EID: 2942605821     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2004.04.012     Document Type: Article
Times cited : (38)

References (47)
  • 1
    • 0031475025 scopus 로고    scopus 로고
    • Mutations of the conserved DRS motif in the second intracellular loop of the gonadotropin-releasing hormone receptor affect expression, activation, and internalization
    • Arora K.K., Cheng Z.Y., Catt K.J. Mutations of the conserved DRS motif in the second intracellular loop of the gonadotropin-releasing hormone receptor affect expression, activation, and internalization. Mol. Endocrinol. 11:1997;1203-1212
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1203-1212
    • Arora, K.K.1    Cheng, Z.Y.2    Catt, K.J.3
  • 2
    • 0032940072 scopus 로고    scopus 로고
    • Histone deacetylases: Transcriptional repression with SINers and NuRDs
    • Ayer D.E. Histone deacetylases: transcriptional repression with SINers and NuRDs. Trends Cell Biol. 9:1999;193-198
    • (1999) Trends Cell Biol. , vol.9 , pp. 193-198
    • Ayer, D.E.1
  • 3
    • 0029809348 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinases by gonadotropins and cyclic adenosine 5'-monophosphates in porcine granulosa cells
    • Cameron M.R., Foster J.S., Bukovsky A., Wimalasena J. Activation of mitogen-activated protein kinases by gonadotropins and cyclic adenosine 5'-monophosphates in porcine granulosa cells. Biol. Reprod. 55:1996;111-119
    • (1996) Biol. Reprod. , vol.55 , pp. 111-119
    • Cameron, M.R.1    Foster, J.S.2    Bukovsky, A.3    Wimalasena, J.4
  • 4
    • 0033812354 scopus 로고    scopus 로고
    • Characterization of a novel transcript of 14-3-3 theta in Sertoli cells
    • Chaudhary J., Skinner M.K. Characterization of a novel transcript of 14-3-3 theta in Sertoli cells. J. Androl. 21:2000;730-738
    • (2000) J. Androl. , vol.21 , pp. 730-738
    • Chaudhary, J.1    Skinner, M.K.2
  • 5
    • 0026599048 scopus 로고
    • One-step transformation of yeast in stationary phase
    • Chen D.C., Yang B.C., Kuo T.T. One-step transformation of yeast in stationary phase. Curr. Genet. 21:1992;83-84
    • (1992) Curr. Genet. , vol.21 , pp. 83-84
    • Chen, D.C.1    Yang, B.C.2    Kuo, T.T.3
  • 6
    • 0035253751 scopus 로고    scopus 로고
    • Induction and repression of DAN1 and the family of anaerobic mannoprotein genes in Saccharomyces cerevisiae occurs through a complex array of regulatory sites
    • Cohen B.D., Sertil O., Abramova N.E., Davies K.J., Lowry C.V. Induction and repression of DAN1 and the family of anaerobic mannoprotein genes in Saccharomyces cerevisiae occurs through a complex array of regulatory sites. Nucleic Acids Res. 29:2001;799-808
    • (2001) Nucleic Acids Res. , vol.29 , pp. 799-808
    • Cohen, B.D.1    Sertil, O.2    Abramova, N.E.3    Davies, K.J.4    Lowry, C.V.5
  • 8
    • 0344825788 scopus 로고    scopus 로고
    • Follicle-stimulating hormone promotes nuclear exclusion of the forkhead transcription factor FoxO1a via phosphatidylinositol 3-kinase in porcine granulosa cells
    • Cunningham M.A., Zhu Q., Unterman T.G., Hammond J.M. Follicle-stimulating hormone promotes nuclear exclusion of the forkhead transcription factor FoxO1a via phosphatidylinositol 3-kinase in porcine granulosa cells. Endocrinology. 144:2003;5585-5594
    • (2003) Endocrinology , vol.144 , pp. 5585-5594
    • Cunningham, M.A.1    Zhu, Q.2    Unterman, T.G.3    Hammond, J.M.4
  • 9
    • 0036370475 scopus 로고    scopus 로고
    • Molecular, structural, and cellular biology of follitropin and follitropin receptor
    • Litwack, G. (Ed.), Academic Press, New York
    • Dias, J.A., Cohen, B.D., Lindau-Shepard, B., Nechamen, C.A., Peterson, A.J., Schmidt, A., 2002. Molecular, structural, and cellular biology of follitropin and follitropin receptor. In: Litwack, G. (Ed.), Vitamins and Hormones, first ed. Academic Press, New York, pp. 249-322.
    • (2002) Vitamins and Hormones, First Ed. , pp. 249-322
    • Dias, J.A.1    Cohen, B.D.2    Lindau-Shepard, B.3    Nechamen, C.A.4    Peterson, A.J.5    Schmidt, A.6
  • 10
    • 0041529686 scopus 로고    scopus 로고
    • Protein kinase a blocks Raf-1 activity by stimulating 14-3-3 binding and blocking Raf-1 interaction with Ras
    • Dumaz N., Marais R. Protein kinase A blocks Raf-1 activity by stimulating 14-3-3 binding and blocking Raf-1 interaction with Ras. J. Biol. Chem. 278:2003;29819-29823
    • (2003) J. Biol. Chem. , vol.278 , pp. 29819-29823
    • Dumaz, N.1    Marais, R.2
  • 11
    • 0033033914 scopus 로고    scopus 로고
    • Activation mechanism of human oxytocin receptor: A combined study of experimental and computer-simulated mutagenesis
    • Fanelli F., Barbier P., Zanchetta D., De Benedetti P.G., Chini B. Activation mechanism of human oxytocin receptor: a combined study of experimental and computer-simulated mutagenesis. Mol. Pharmacol. 56:1999;214-225
    • (1999) Mol. Pharmacol. , vol.56 , pp. 214-225
    • Fanelli, F.1    Barbier, P.2    Zanchetta, D.3    De Benedetti, P.G.4    Chini, B.5
  • 12
    • 0033579441 scopus 로고    scopus 로고
    • Binding of 14-3-3 protein to the plasma membrane H+-ATPase AHA2 involves the three C-terminal residues Tyr946-Thr-Val and requires phosphorylation of Thr947
    • Fuglsang A.T., Visconti S., Drumm K., Jahn T., Stensballe A., Mattei B., Jensen O.N., Aducci P., Palmgren M.G. Binding of 14-3-3 protein to the plasma membrane H+-ATPase AHA2 involves the three C-terminal residues Tyr946-Thr-Val and requires phosphorylation of Thr947. J. Biol. Chem. 274:1999;36774-36780
    • (1999) J. Biol. Chem. , vol.274 , pp. 36774-36780
    • Fuglsang, A.T.1    Visconti, S.2    Drumm, K.3    Jahn, T.4    Stensballe, A.5    Mattei, B.6    Jensen, O.N.7    Aducci, P.8    Palmgren, M.G.9
  • 13
    • 0034463096 scopus 로고    scopus 로고
    • Follicle-stimulating hormone (FSH) stimulates phosphorylation and activation of protein kinase B (PKB/Akt) and serum and glucocorticoid-induced kinase (Sgk): Evidence for a kinase-independent signaling by FSH in granulosa cells
    • Gonzalez-Robayna I.J., Falender A.E., Ochsner S., Firestone G.L., Richards J.S. Follicle-stimulating hormone (FSH) stimulates phosphorylation and activation of protein kinase B (PKB/Akt) and serum and glucocorticoid-induced kinase (Sgk): evidence for A kinase-independent signaling by FSH in granulosa cells. Mol. Endocrinol. 14:2000;1283-1300
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1283-1300
    • Gonzalez-Robayna, I.J.1    Falender, A.E.2    Ochsner, S.3    Firestone, G.L.4    Richards, J.S.5
  • 14
    • 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., Schreiber S.L. Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization. Proc. Natl. Acad. Sci. U.S.A. 97:2000;7835-7840
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 7835-7840
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 15
    • 0028785484 scopus 로고
    • Truncation of the C-terminal tail of the follitropin receptor does not impair the agonist- or phorbol ester-induced receptor phosphorylation and uncoupling
    • Hipkin R.W., Liu X., Ascoli M. Truncation of the C-terminal tail of the follitropin receptor does not impair the agonist- or phorbol ester-induced receptor phosphorylation and uncoupling. J. Biol. Chem. 270:1995;26683-26689
    • (1995) J. Biol. Chem. , vol.270 , pp. 26683-26689
    • Hipkin, R.W.1    Liu, X.2    Ascoli, M.3
  • 16
    • 2142721829 scopus 로고    scopus 로고
    • Interference of BAD (Bcl-xL/Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11
    • Hsu S.Y., Kaipia A., Zhu L., Hsueh A.J. Interference of BAD (Bcl-xL/Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11. Mol. Endocrinol. 11:1997;1858-1867
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1858-1867
    • Hsu, S.Y.1    Kaipia, A.2    Zhu, L.3    Hsueh, A.J.4
  • 17
    • 0030934805 scopus 로고    scopus 로고
    • Regulation of ovarian follicle atresia
    • [Review] [89 refs.]
    • Kaipia A., Hsueh A.J. Regulation of ovarian follicle atresia. Ann. Rev. Physiol. 59:1997;349-363. [Review] [89 refs.]
    • (1997) Ann. Rev. Physiol. , vol.59 , pp. 349-363
    • Kaipia, A.1    Hsueh, A.J.2
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0033304637 scopus 로고    scopus 로고
    • Role of G protein-coupled receptor kinases on the agonist-induced phosphorylation and internalization of the follitropin receptor
    • Lazari M.F., Liu X., Nakamura K., Benovic J.L., Ascoli M. Role of G protein-coupled receptor kinases on the agonist-induced phosphorylation and internalization of the follitropin receptor. Mol. Endocrinol. 13:1999;866-878
    • (1999) Mol. Endocrinol. , vol.13 , pp. 866-878
    • Lazari, M.F.1    Liu, X.2    Nakamura, K.3    Benovic, J.L.4    Ascoli, M.5
  • 22
    • 0031786371 scopus 로고    scopus 로고
    • Follicle stimulating hormone (FSH) activates the p38 mitogen-activated protein kinase pathway, inducing small heat shock protein phosphorylation and cell rounding in immature rat ovarian granulosa cells
    • Maizels E.T., Cottom J., Jones J.C., Hunzicker-Dunn M. Follicle stimulating hormone (FSH) activates the p38 mitogen-activated protein kinase pathway, inducing small heat shock protein phosphorylation and cell rounding in immature rat ovarian granulosa cells. Endocrinology. 139:1998;3353-3356
    • (1998) Endocrinology , vol.139 , pp. 3353-3356
    • Maizels, E.T.1    Cottom, J.2    Jones, J.C.3    Hunzicker-Dunn, M.4
  • 24
    • 0032230332 scopus 로고    scopus 로고
    • The agonist-induced phosphorylation of the rat follitropin receptor maps to the first and third intracellular loops
    • Nakamura K., Hipkin R.W., Ascoli M. The agonist-induced phosphorylation of the rat follitropin receptor maps to the first and third intracellular loops. Mol. Endocrinol. 12:1998;580-591
    • (1998) Mol. Endocrinol. , vol.12 , pp. 580-591
    • Nakamura, K.1    Hipkin, R.W.2    Ascoli, M.3
  • 25
    • 0037471203 scopus 로고    scopus 로고
    • Point mutations in follitropin receptor result in ER retention
    • Nechamen C.A., Dias J.A. Point mutations in follitropin receptor result in ER retention. Mol. Cell. Endocrinol. 201:2003;123-131
    • (2003) Mol. Cell. Endocrinol. , vol.201 , pp. 123-131
    • Nechamen, C.A.1    Dias, J.A.2
  • 26
    • 2942601056 scopus 로고    scopus 로고
    • Human follicle stimulating hormone (FSH) receptor interacts with the adaptor protein APPL: Potential involvement of the PI3K pathway in FSH signaling
    • in press.
    • Nechamen, C.A., Thomas, R.M., Cohen, B.D., Acevedo, G., Poulikakos, P.I., Testa, J.R., Dias, J.A., 2004. Human follicle stimulating hormone (FSH) receptor interacts with the adaptor protein APPL: potential involvement of the PI3K pathway in FSH signaling. Biol. Reprod., in press.
    • (2004) Biol. Reprod.
    • Nechamen, C.A.1    Thomas, R.M.2    Cohen, B.D.3    Acevedo, G.4    Poulikakos, P.I.5    Testa, J.R.6    Dias, J.A.7
  • 27
    • 0025963513 scopus 로고
    • Primary structure of a human protein kinase regulator protein
    • Nielsen P.J. Primary structure of a human protein kinase regulator protein. Biochim. Biophys. Acta. 1088:1991;425-428
    • (1991) Biochim. Biophys. Acta , vol.1088 , pp. 425-428
    • Nielsen, P.J.1
  • 28
    • 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., Morrison D.K. Protein phosphatase 2A positively regulates ras signaling by dephosphorylating KSR1 and Raf-1 on critical 14-3-3 binding sites. Curr. Biol. 13:2003;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
  • 29
    • 0033531936 scopus 로고    scopus 로고
    • The zeta á isoform of 14-3-3á proteins interacts with the third intracellular loop of different alpha 2-adrenergic receptor subtypes
    • Prezeau L., Richman J.G., Edwards S.W., Limbird L.E. The zeta á isoform of 14-3-3á proteins interacts with the third intracellular loop of different alpha 2-adrenergic receptor subtypes. J. Biol. Chem. 274:1999;13462-13469
    • (1999) J. Biol. Chem. , vol.274 , pp. 13462-13469
    • Prezeau, L.1    Richman, J.G.2    Edwards, S.W.3    Limbird, L.E.4
  • 30
    • 0028245033 scopus 로고
    • Follitropin (FSH) and a phorbol ester stimulate the phosphorylation of the FSH receptor in intact cells
    • Quintana J., Hipkin R.W., Sanchez-Yague J., Ascoli M. Follitropin (FSH) and a phorbol ester stimulate the phosphorylation of the FSH receptor in intact cells. J. Biol. Chem. 269:1994;8772-8779
    • (1994) J. Biol. Chem. , vol.269 , pp. 8772-8779
    • Quintana, J.1    Hipkin, R.W.2    Sanchez-Yague, J.3    Ascoli, M.4
  • 31
    • 0035868368 scopus 로고    scopus 로고
    • Roles of the forkhead in rhabdomyosarcoma (FKHR) phosphorylation sites in regulating 14-3-3 binding, transactivation and nuclear targeting
    • Rena G., Prescott A.R., Guo S., Cohen P., Unterman T.G. Roles of the forkhead in rhabdomyosarcoma (FKHR) phosphorylation sites in regulating 14-3-3 binding, transactivation and nuclear targeting. Biochem. J. 354:2001;605-612
    • (2001) Biochem. J. , vol.354 , pp. 605-612
    • Rena, G.1    Prescott, A.R.2    Guo, S.3    Cohen, P.4    Unterman, T.G.5
  • 32
    • 0035154289 scopus 로고    scopus 로고
    • New signaling pathways for hormones and cyclic adenosine 3′,5′-monophosphate action in endocrine cells
    • [Review] [119 refs.]
    • Richards J.S. New signaling pathways for hormones and cyclic adenosine 3′, 5′-monophosphate action in endocrine cells. Mol. Endocrinol. 15:2001;209-218. [Review] [119 refs.]
    • (2001) Mol. Endocrinol. , vol.15 , pp. 209-218
    • Richards, J.S.1
  • 33
    • 0029977450 scopus 로고    scopus 로고
    • Follitropin conformational stability mediated by loop 2 beta effects follitropin-receptor interaction
    • Roth K.E., Dias J.A. Follitropin conformational stability mediated by loop 2 beta effects follitropin-receptor interaction. Biochemistry. 35:1996;7928-7935
    • (1996) Biochemistry , vol.35 , pp. 7928-7935
    • Roth, K.E.1    Dias, J.A.2
  • 34
    • 0037131334 scopus 로고    scopus 로고
    • Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3
    • Sato S., Fujita N., Tsuruo T. Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3. J. Biol. Chem. 277:2002;39360-39367
    • (2002) J. Biol. Chem. , vol.277 , pp. 39360-39367
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 35
    • 0033974265 scopus 로고    scopus 로고
    • Mutational analysis of the highly conserved arginine within the Glu/Asp-Arg-Tyr motif of the alpha(1b)-adrenergic receptor: Effects on receptor isomerization and activation
    • Scheer A., Costa T., Fanelli F., De Benedetti P.G., Mhaouty-Kodja S., Abuin L., Nenniger-Tosato M., Cotecchia S. Mutational analysis of the highly conserved arginine within the Glu/Asp-Arg-Tyr motif of the alpha(1b)-adrenergic receptor: effects on receptor isomerization and activation. Mol. Pharmacol. 57:2000;219-231
    • (2000) Mol. Pharmacol. , vol.57 , pp. 219-231
    • Scheer, A.1    Costa, T.2    Fanelli, F.3    De Benedetti, P.G.4    Mhaouty-Kodja, S.5    Abuin, L.6    Nenniger-Tosato, M.7    Cotecchia, S.8
  • 36
    • 0035968185 scopus 로고    scopus 로고
    • Hormone-induced conformational change of the purified soluble hormone binding domain of follitropin receptor complexed with single chain follitropin
    • Schmidt A., MacColl R., Lindau-Shepard B., Buckler D.R., Dias J.A. Hormone-induced conformational change of the purified soluble hormone binding domain of follitropin receptor complexed with single chain follitropin. J. Biol. Chem. 276:2001;23373-23381
    • (2001) J. Biol. Chem. , vol.276 , pp. 23373-23381
    • Schmidt, A.1    MacColl, R.2    Lindau-Shepard, B.3    Buckler, D.R.4    Dias, J.A.5
  • 37
    • 0034682812 scopus 로고    scopus 로고
    • BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival
    • Tan Y., Demeter M.R., Ruan H., Comb M.J. BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival. J. Biol. Chem. 275:2000;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
  • 38
    • 0037187331 scopus 로고    scopus 로고
    • Structural determinants in the second intracellular loop of the human follicle-stimulating hormone receptor are involved in G(s) protein activation
    • Timossi C., Maldonado D., Vizcaino A., Lindau-Shepard B., Conn P.M., Ulloa-Aguirre A. Structural determinants in the second intracellular loop of the human follicle-stimulating hormone receptor are involved in G(s) protein activation. Mol. Cell. Endocrinol. 189:2002;157-168
    • (2002) Mol. Cell. Endocrinol. , vol.189 , pp. 157-168
    • Timossi, C.1    Maldonado, D.2    Vizcaino, A.3    Lindau-Shepard, B.4    Conn, P.M.5    Ulloa-Aguirre, A.6
  • 39
    • 0034847625 scopus 로고    scopus 로고
    • Using the yeast interaction trap and other two-hybrid-based approaches to study protein-protein interactions
    • [Review] [28 refs.]
    • Toby G.G., Golemis E.A. Using the yeast interaction trap and other two-hybrid-based approaches to study protein-protein interactions. Methods (Duluth). 24:2001;201-217. [Review] [28 refs.]
    • (2001) Methods (Duluth) , vol.24 , pp. 201-217
    • Toby, G.G.1    Golemis, E.A.2
  • 40
    • 0036479325 scopus 로고    scopus 로고
    • 14-3-3 Proteins: Active cofactors in cellular regulation by serine/threonine phosphorylation
    • Tzivion G., Avruch J. 14-3-3 Proteins: active cofactors in cellular regulation by serine/threonine phosphorylation. J. Biol. Chem. 277:2002;3061-3064
    • (2002) J. Biol. Chem. , vol.277 , pp. 3061-3064
    • Tzivion, G.1    Avruch, J.2
  • 41
    • 0035473486 scopus 로고    scopus 로고
    • 14-3-3 Proteins; Bringing new definitions to scaffolding
    • Tzivion G., Shen Y.H., Zhu J. 14-3-3 Proteins; bringing new definitions to scaffolding. Oncogene. 20:2001;6331-6338
    • (2001) Oncogene , vol.20 , pp. 6331-6338
    • Tzivion, G.1    Shen, Y.H.2    Zhu, J.3
  • 42
    • 0031695446 scopus 로고    scopus 로고
    • Structure-function relationship of follicle-stimulating hormone and its receptor
    • Ulloa-Aguirre A., Timossi C. Structure-function relationship of follicle-stimulating hormone and its receptor. Hum. Reprod. Update. 4:1998;260-283
    • (1998) Hum. Reprod. Update , vol.4 , pp. 260-283
    • Ulloa-Aguirre, A.1    Timossi, C.2
  • 43
    • 0034650872 scopus 로고    scopus 로고
    • 14-3-3 Isotypes facilitate coupling of protein kinase C-zeta to Raf-1: Negative regulation by 14-3-3 phosphorylation
    • van der Hoeven P.C.J., van der Wal J.C.M., Ruurs P., Van Dijk M.C.M., van Blitterswijk W.J. 14-3-3 Isotypes facilitate coupling of protein kinase C-zeta to Raf-1: negative regulation by 14-3-3 phosphorylation. Biochem. J. 345:2000;297-306
    • (2000) Biochem. J. , vol.345 , pp. 297-306
    • Van Der Hoeven, P.C.J.1    Van Der Wal, J.C.M.2    Ruurs, P.3    Van Dijk, M.C.M.4    Van Blitterswijk, W.J.5
  • 44
    • 0034788964 scopus 로고    scopus 로고
    • 14-3-3 Proteins: Key regulators of cell division, signalling and apoptosis
    • van Hemert M.J., Steensma H.Y., van Heusden G.P. 14-3-3 Proteins: key regulators of cell division, signalling and apoptosis. Bioessays. 23:2001;936-946
    • (2001) Bioessays , vol.23 , pp. 936-946
    • Van Hemert, M.J.1    Steensma, H.Y.2    Van Heusden, G.P.3
  • 45
    • 0037184945 scopus 로고    scopus 로고
    • Regulated interactions of the alpha 2A adrenergic receptor with spinophilin, 14-3-3zeta, and arrestin 3
    • Wang Q., Limbird L.E. Regulated interactions of the alpha 2A adrenergic receptor with spinophilin, 14-3-3zeta, and arrestin 3. J. Biol. Chem. 277:2002;50589-50596
    • (2002) J. Biol. Chem. , vol.277 , pp. 50589-50596
    • Wang, Q.1    Limbird, L.E.2
  • 46
    • 0013887696 scopus 로고
    • Clonal analysis of differentiated function in animal cell culture. I. Possible correlated maintenance of differentiated function and the diploid karyotype
    • Yasumura Y., Buonassisi V., Sato G. Clonal analysis of differentiated function in animal cell culture. I. Possible correlated maintenance of differentiated function and the diploid karyotype. Cancer Res. 26:1966;529-535
    • (1966) Cancer Res. , vol.26 , pp. 529-535
    • Yasumura, Y.1    Buonassisi, V.2    Sato, G.3
  • 47
    • 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. 87:1996;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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.