메뉴 건너뛰기




Volumn 20, Issue 5, 2007, Pages 285-292

The 14-3-3ζ-GPIb-IX-V complex as an antiplatelet target

Author keywords

[No Author keywords available]

Indexed keywords

ANTITHROMBOCYTIC AGENT; CALMODULIN; FUSICOCCIN; GLYCOPROTEIN; GLYCOPROTEIN1B IX V; ISOPROTEIN; NEW DRUG; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEIN 14 3 3ZETA; UNCLASSIFIED DRUG; PROTEIN 14 3 3; THROMBIN RECEPTOR;

EID: 34548426190     PISSN: 02140934     EISSN: None     Source Type: Journal    
DOI: 10.1358/dnp.2007.20.5.1120215     Document Type: Review
Times cited : (24)

References (53)
  • 1
    • 33646926129 scopus 로고    scopus 로고
    • 14-3-3 proteins: A historic-overview
    • Aitken, A. 14-3-3 proteins: A historic-overview. Semin Cancer Biol 2006, 16: 162-72.
    • (2006) Semin Cancer Biol , vol.16 , pp. 162-172
    • Aitken, A.1
  • 4
    • 84884800657 scopus 로고    scopus 로고
    • The glycoprotein Ib-LX-V complex
    • 2nd edition, A. Michelson Ed, Academic Press: San Diego
    • Andrews, R.K., Berndt, M.C. and López, J.A. The glycoprotein Ib-LX-V complex. In: Platelets, 2nd edition, A. Michelson (Ed.), Academic Press: San Diego 2006, 145-63.
    • (2006) Platelets , pp. 145-163
    • Andrews, R.K.1    Berndt, M.C.2    López, J.A.3
  • 5
    • 33745103749 scopus 로고    scopus 로고
    • Does isoform diversity explain functional differences in the 14-3-3 protein family?
    • Kjarland, E., Keen, T.J. and Kleppe, R. Does isoform diversity explain functional differences in the 14-3-3 protein family? Curr Pharmaceut Biotech 2006, 7: 217-23.
    • (2006) Curr Pharmaceut Biotech , vol.7 , pp. 217-223
    • Kjarland, E.1    Keen, T.J.2    Kleppe, R.3
  • 6
    • 3242788127 scopus 로고    scopus 로고
    • Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
    • MacKintosh, C. Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes. Biochem J 2004, 381: 329-42.
    • (2004) Biochem J , vol.381 , pp. 329-342
    • MacKintosh, C.1
  • 7
    • 0345059753 scopus 로고    scopus 로고
    • The 14-3-3 cancer connection
    • Hermeking, H. The 14-3-3 cancer connection. Nat Reviews 2003, 3: 931-43.
    • (2003) Nat Reviews , vol.3 , pp. 931-943
    • Hermeking, H.1
  • 8
    • 0029922841 scopus 로고    scopus 로고
    • Identification of a binding sequence for the 14-3-3 protein within the cytoplasmic domain of the adhesion receptor, platelet glycoprotein Ibα
    • Du, X., Fox, J.E. and Pei, S. Identification of a binding sequence for the 14-3-3 protein within the cytoplasmic domain of the adhesion receptor, platelet glycoprotein Ibα. J Biol Chem 1996, 271: 7362-7.
    • (1996) J Biol Chem , vol.271 , pp. 7362-7367
    • Du, X.1    Fox, J.E.2    Pei, S.3
  • 9
    • 0032512413 scopus 로고    scopus 로고
    • Binding of purified 14-3-3ζ signaling protein to discrete amino acid sequences within the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex
    • Andrews, R.K., Harris, S.J., McNally, T. and Berndt, M.C. Binding of purified 14-3-3ζ signaling protein to discrete amino acid sequences within the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex. Biochemistry 1998, 37: 638-47.
    • (1998) Biochemistry , vol.37 , pp. 638-647
    • Andrews, R.K.1    Harris, S.J.2    McNally, T.3    Berndt, M.C.4
  • 10
    • 0032519507 scopus 로고    scopus 로고
    • Human signaling protein 14-3-3ζ interacts with platelet glycoprotein Ib subunits Ibα and Ibβ
    • Calverley, D.C., Kavanagh, T.J. and Roth, G.J. Human signaling protein 14-3-3ζ interacts with platelet glycoprotein Ib subunits Ibα and Ibβ. Blood 1998, 91: 1295-303.
    • (1998) Blood , vol.91 , pp. 1295-1303
    • Calverley, D.C.1    Kavanagh, T.J.2    Roth, G.J.3
  • 11
    • 0033584855 scopus 로고    scopus 로고
    • The cytoplasmic domain of the platelet glycoprotein Ibα is phosphorylated at serine 609
    • Bodnar, R.J., Gu, M., Li, Z., Englund, G.D. and Du, X. The cytoplasmic domain of the platelet glycoprotein Ibα is phosphorylated at serine 609. J Biol Chem 1999, 274: 33474-9.
    • (1999) J Biol Chem , vol.274 , pp. 33474-33479
    • Bodnar, R.J.1    Gu, M.2    Li, Z.3    Englund, G.D.4    Du, X.5
  • 13
    • 0034649783 scopus 로고    scopus 로고
    • Cytoplasmic domains of GPIbα and GPIbβ regulate 14-3-3ζ binding to GPIb/IX/V
    • Feng, S., Christodoulides, N., Resendiz, J.C., Berndt, M.C. and Kroll, M.H. Cytoplasmic domains of GPIbα and GPIbβ regulate 14-3-3ζ binding to GPIb/IX/V. Blood 2000, 95: 551-7.
    • (2000) Blood , vol.95 , pp. 551-557
    • Feng, S.1    Christodoulides, N.2    Resendiz, J.C.3    Berndt, M.C.4    Kroll, M.H.5
  • 14
    • 3142583189 scopus 로고    scopus 로고
    • Identification of a novel 14-3-3ζ binding site within the cytoplasmic tail of platelet glycoprotein Ibα
    • Mangin, P., David, T., Lavaud, V. et al. Identification of a novel 14-3-3ζ binding site within the cytoplasmic tail of platelet glycoprotein Ibα. Blood 2004, 104: 420-7.
    • (2004) Blood , vol.104 , pp. 420-427
    • Mangin, P.1    David, T.2    Lavaud, V.3
  • 15
    • 24744453957 scopus 로고    scopus 로고
    • A critical role for 14-3-3ζ protein in regulating the VWF binding function of platelet glycoprotein Ib-IX and its therapeutic implications
    • Dai, K., Bodnar, R., Berndt, M.C. and Du, X. A critical role for 14-3-3ζ protein in regulating the VWF binding function of platelet glycoprotein Ib-IX and its therapeutic implications. Blood 2005, 106: 1975-81.
    • (2005) Blood , vol.106 , pp. 1975-1981
    • Dai, K.1    Bodnar, R.2    Berndt, M.C.3    Du, X.4
  • 17
    • 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. et al. Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways. Nature 1995, 376: 188-91.
    • (1995) Nature , vol.376 , pp. 188-191
    • Xiao, B.1    Smerdon, S.J.2    Jones, D.H.3
  • 18
    • 0032568665 scopus 로고    scopus 로고
    • 14-3-3ζ binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove
    • Petosa, C., Masters, S.C., Bankston, L.A. et al. 14-3-3ζ binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove. J Biol Chem 1998, 273: 16305-10.
    • (1998) J Biol Chem , vol.273 , pp. 16305-16310
    • Petosa, C.1    Masters, S.C.2    Bankston, L.A.3
  • 19
    • 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. and 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. Sem Cancer Biol 2006, 16: 173-82.
    • (2006) Sem Cancer Biol , vol.16 , pp. 173-182
    • Gardino, A.K.1    Smerdon, S.J.2    Yaffe, M.B.3
  • 20
    • 0141815677 scopus 로고    scopus 로고
    • The dimeric versus monomeric status of 14-3-3ζ 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. The dimeric versus monomeric status of 14-3-3ζ is controlled by phosphorylation of Ser58 at the dimer interface. J Biol Chem 2003, 278: 36323-7.
    • (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
  • 21
    • 29344452931 scopus 로고    scopus 로고
    • Protein kinase A phosphorylates and regulates dimerization of 14-3-3ε
    • Gu, Y.M., Jin, Y.H., Choi, J.K., Baek, K.H., Yeo, C.Y. and Lee, K.Y. Protein kinase A phosphorylates and regulates dimerization of 14-3-3ε. FEBS Lett 2006, 580: 305-10.
    • (2006) FEBS Lett , vol.580 , pp. 305-310
    • Gu, Y.M.1    Jin, Y.H.2    Choi, J.K.3    Baek, K.H.4    Yeo, C.Y.5    Lee, K.Y.6
  • 22
    • 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. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 1996, 84: 889-97.
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 23
    • 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. et al. Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display. Biochemistry 1999, 38: 12499-504.
    • (1999) Biochemistry , vol.38 , pp. 12499-12504
    • Wang, B.1    Yang, H.2    Liu, Y.C.3
  • 24
    • 16844375641 scopus 로고    scopus 로고
    • Glycoprotein (GP)VI is associated with GPIb-IX-V on the membrane of resting and activated platelets
    • Arthur, J.F., Matzaris, M., Gardiner, E.E. et al. Glycoprotein (GP)VI is associated with GPIb-IX-V on the membrane of resting and activated platelets. Thromb Haemostas 2005, 93: 716-23.
    • (2005) Thromb Haemostas , vol.93 , pp. 716-723
    • Arthur, J.F.1    Matzaris, M.2    Gardiner, E.E.3
  • 25
    • 0024336047 scopus 로고
    • Cyclic AMP-dependent phosphorylation of glycoprotein Ib inhibits collagen-induced polymerization of actin in platelets
    • Fox, J.E.B. and Berndt, M.C. Cyclic AMP-dependent phosphorylation of glycoprotein Ib inhibits collagen-induced polymerization of actin in platelets. J Biol Chem 1989, 264: 9520-6.
    • (1989) J Biol Chem , vol.264 , pp. 9520-9526
    • Fox, J.E.B.1    Berndt, M.C.2
  • 26
    • 0037033024 scopus 로고    scopus 로고
    • Regulation of glycoprotein Ib-IX-von Willebrand factor interaction by cAMP-dependent protein kinase-mediated phosphorylation at Ser166 of glycoprotein Ibβ
    • Bodnar, R.J., Xi, X., Li, Z., Berndt, M.C. and Du, X. Regulation of glycoprotein Ib-IX-von Willebrand factor interaction by cAMP-dependent protein kinase-mediated phosphorylation at Ser166 of glycoprotein Ibβ. J Biol Chem 2002, 277: 47080-7.
    • (2002) J Biol Chem , vol.277 , pp. 47080-47087
    • Bodnar, R.J.1    Xi, X.2    Li, Z.3    Berndt, M.C.4    Du, X.5
  • 27
    • 33751002655 scopus 로고    scopus 로고
    • Inhibition of adhesive and signaling functions of the platelet GPIb-V-IX complex by a cell penetrating GPIbα peptide
    • David, T., Ohlmann, P., Eckly, A. et al. Inhibition of adhesive and signaling functions of the platelet GPIb-V-IX complex by a cell penetrating GPIbα peptide. J Thromb Haemost 2006, 4: 2645-55.
    • (2006) J Thromb Haemost , vol.4 , pp. 2645-2655
    • David, T.1    Ohlmann, P.2    Eckly, A.3
  • 28
    • 8644224220 scopus 로고    scopus 로고
    • Megakaryocyte proliferation and ploidy regulated by the cytoplasmic tail of glycoprotein Ibα
    • Kanaji, T., Russell, S., Cunningham, J., Izuhara, K., Fox, J.E. and Ware, J. Megakaryocyte proliferation and ploidy regulated by the cytoplasmic tail of glycoprotein Ibα. Blood 2004, 104: 3161-8.
    • (2004) Blood , vol.104 , pp. 3161-3168
    • Kanaji, T.1    Russell, S.2    Cunningham, J.3    Izuhara, K.4    Fox, J.E.5    Ware, J.6
  • 29
    • 0033564953 scopus 로고    scopus 로고
    • The glycoprotein Ib/IX complex regulates cell proliferation
    • Feng, S., Christodoulides, N. and Kroll, M.H. The glycoprotein Ib/IX complex regulates cell proliferation. Blood 1999, 93: 4256-63.
    • (1999) Blood , vol.93 , pp. 4256-4263
    • Feng, S.1    Christodoulides, N.2    Kroll, M.H.3
  • 30
    • 0030840587 scopus 로고    scopus 로고
    • The cytoplasmic domain of glycoprotein (GP)Ibα constrains the lateral diffusion of the GPIb-IX complex and modulates von Willebrand factor binding
    • Dong, J.-F., Li, C.O., Sae-Tung, G., Hyun, W., Afshar-Kharghan, V. and Lopez, J.A. The cytoplasmic domain of glycoprotein (GP)Ibα constrains the lateral diffusion of the GPIb-IX complex and modulates von Willebrand factor binding. Biochemistry 1997, 36: 12421-7.
    • (1997) Biochemistry , vol.36 , pp. 12421-12427
    • Dong, J.-F.1    Li, C.O.2    Sae-Tung, G.3    Hyun, W.4    Afshar-Kharghan, V.5    Lopez, J.A.6
  • 31
    • 0037528704 scopus 로고    scopus 로고
    • Role of the intracellular domains of GPIb in controlling the adhesive properties of the platelet GPIb/V/IX complex
    • Perrault, C., Mangin, P., Santer, M. et al. Role of the intracellular domains of GPIb in controlling the adhesive properties of the platelet GPIb/V/IX complex. Blood 2003, 101: 3477-84.
    • (2003) Blood , vol.101 , pp. 3477-3484
    • Perrault, C.1    Mangin, P.2    Santer, M.3
  • 32
    • 33749635803 scopus 로고    scopus 로고
    • A global proteomics approach identifies novel phosphorylated signaling proteins in GPVI-activated platelets: Involvement of G6f, a novel platelet Grb2-binding membrane adapter
    • Garcia, A., Senis, Y.A., Antrobus, R. et al. A global proteomics approach identifies novel phosphorylated signaling proteins in GPVI-activated platelets: Involvement of G6f, a novel platelet Grb2-binding membrane adapter. Proteomics 2006, 6: 5332-543.
    • (2006) Proteomics , vol.6 , pp. 5332-5543
    • Garcia, A.1    Senis, Y.A.2    Antrobus, R.3
  • 33
    • 0042357139 scopus 로고    scopus 로고
    • 14-3-3ζ mediates integrin-induced activation of Cdc42 and Rac. Platelet glycoprotein Ib-IX regulates integrin-induced signaling by sequestering 14-3-3ζ
    • Bialkowska, K., Zaffran, Y., Meyer, S.C. and Fox, J.E.B. 14-3-3ζ mediates integrin-induced activation of Cdc42 and Rac. Platelet glycoprotein Ib-IX regulates integrin-induced signaling by sequestering 14-3-3ζ. J Biol Chem 2003, 278: 33342-50.
    • (2003) J Biol Chem , vol.278 , pp. 33342-33350
    • Bialkowska, K.1    Zaffran, Y.2    Meyer, S.C.3    Fox, J.E.B.4
  • 34
    • 0029958763 scopus 로고    scopus 로고
    • Identification of 14-3-3 proteins in human platelets: Effects of synthetic peptides on protein kinase C activation
    • Wheeler-Jones, C.P., Learmonth, M.P., Martin, H. and Aitken, A. Identification of 14-3-3 proteins in human platelets: Effects of synthetic peptides on protein kinase C activation. Biochem J 1996, 315: 41-7.
    • (1996) Biochem J , vol.315 , pp. 41-47
    • Wheeler-Jones, C.P.1    Learmonth, M.P.2    Martin, H.3    Aitken, A.4
  • 35
    • 33645089713 scopus 로고    scopus 로고
    • Upregulated expression of 14-3-3 proteins in astrocytes from human cerebrovascular ischemic lesions
    • Kawamoto, Y., Akiguchi, I., Tomimoto, H., Shirakashi, Y., Honjo, Y. and Budka, H. Upregulated expression of 14-3-3 proteins in astrocytes from human cerebrovascular ischemic lesions. Stroke 2006, 37: 830-5.
    • (2006) Stroke , vol.37 , pp. 830-835
    • Kawamoto, Y.1    Akiguchi, I.2    Tomimoto, H.3    Shirakashi, Y.4    Honjo, Y.5    Budka, H.6
  • 37
    • 0033120915 scopus 로고    scopus 로고
    • In vivo and in vitro association of 14-3-3ε isoform with calmodulin: Implication for signal transduction and cell proliferation
    • Luk, S.C., Ngai, S.M., Tsui, S.K., Fung, K.P., Lee, C.Y. and Wave, M.M. In vivo and in vitro association of 14-3-3ε isoform with calmodulin: Implication for signal transduction and cell proliferation. J Cell Biochem 1999, 73: 31-5.
    • (1999) J Cell Biochem , vol.73 , pp. 31-35
    • Luk, S.C.1    Ngai, S.M.2    Tsui, S.K.3    Fung, K.P.4    Lee, C.Y.5    Wave, M.M.6
  • 38
    • 23944467523 scopus 로고    scopus 로고
    • Roles of 14-3-3 and calmodulin binding in subcellular localization and function of the small G-protein Rem2
    • Beguin, P., Mahalakshmi, R.N., Nagashima, K. et al. Roles of 14-3-3 and calmodulin binding in subcellular localization and function of the small G-protein Rem2. Biochem J 2005, 390: 67-75.
    • (2005) Biochem J , vol.390 , pp. 67-75
    • Beguin, P.1    Mahalakshmi, R.N.2    Nagashima, K.3
  • 39
    • 19444378365 scopus 로고    scopus 로고
    • 14-3-3 and calmodulin control subcellular distribution of Kir/Gem and its regulation of cell shape and calcium channel activity
    • Beguin, P., Mahalakshmi, R.N., Nagashima, K. et al. 14-3-3 and calmodulin control subcellular distribution of Kir/Gem and its regulation of cell shape and calcium channel activity. J Cell Sci 2005, 118: 1923-34.
    • (2005) J Cell Sci , vol.118 , pp. 1923-1934
    • Beguin, P.1    Mahalakshmi, R.N.2    Nagashima, K.3
  • 41
    • 0035437184 scopus 로고    scopus 로고
    • Interaction of calmodulin with the cytoplasmic domain of the platelet membrane GPIb-IX-V complex
    • Andrews, R.K., Munday, A.D., Mitchell, C.A. and Berndt, M.C. Interaction of calmodulin with the cytoplasmic domain of the platelet membrane GPIb-IX-V complex. Blood 2001, 98: 681-7.
    • (2001) Blood , vol.98 , pp. 681-687
    • Andrews, R.K.1    Munday, A.D.2    Mitchell, C.A.3    Berndt, M.C.4
  • 42
    • 7044232239 scopus 로고    scopus 로고
    • Regulation of platelet membrane levels of glycoprotein VI by a platelet-derived metalloproteinase
    • Gardiner, E.E., Arthur, J.F., Kahn, M.L., Berndt, M.C. and Andrews, R.K. Regulation of platelet membrane levels of glycoprotein VI by a platelet-derived metalloproteinase. Blood 2004, 104: 3611-7.
    • (2004) Blood , vol.104 , pp. 3611-3617
    • Gardiner, E.E.1    Arthur, J.F.2    Kahn, M.L.3    Berndt, M.C.4    Andrews, R.K.5
  • 43
    • 0037416221 scopus 로고    scopus 로고
    • Structural view of a fungal toxin acting on a 14-3-3 regulatory complex
    • Wurtele, M., Jelich-Ottmann, C., Wittinghofer, A. and Oecking, C. Structural view of a fungal toxin acting on a 14-3-3 regulatory complex. EMBO J 2003, 22: 987-94.
    • (2003) EMBO J , vol.22 , pp. 987-994
    • Wurtele, M.1    Jelich-Ottmann, C.2    Wittinghofer, A.3    Oecking, C.4
  • 44
    • 33644960040 scopus 로고    scopus 로고
    • Delineation of exoenzyme S residues that mediate the interaction 14-3-3 and its biological activity
    • Yasmin, L., Jansson, A.L., Panahandeh, T., Palmer, R.H., Francis, M.S. and Hallberg, B. Delineation of exoenzyme S residues that mediate the interaction 14-3-3 and its biological activity. FEBS J 2006, 273: 638-46.
    • (2006) FEBS J , vol.273 , pp. 638-646
    • Yasmin, L.1    Jansson, A.L.2    Panahandeh, T.3    Palmer, R.H.4    Francis, M.S.5    Hallberg, B.6
  • 45
    • 0032474838 scopus 로고    scopus 로고
    • A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity
    • Tzivion, G., Luo, Z. and Avruch, J. A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity. Nature 1998, 394: 88-92.
    • (1998) Nature , vol.394 , pp. 88-92
    • Tzivion, G.1    Luo, Z.2    Avruch, J.3
  • 46
    • 33750481912 scopus 로고    scopus 로고
    • Characterization of apoptosis induced by marine natural products in non small cell lung cancer A549 cells
    • Catassi, A., Cesario, A., Arzani, D. et al. Characterization of apoptosis induced by marine natural products in non small cell lung cancer A549 cells. Cell Mol Life Sci 2006, 63: 2377-86.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 2377-2386
    • Catassi, A.1    Cesario, A.2    Arzani, D.3
  • 47
    • 33645520585 scopus 로고    scopus 로고
    • Sensitizing hormone-refractory prostate cancer cells to drug treatment by targeting 14-3-3σ
    • Han, B., Xie, H., Chen, Q. and Zhang, J.-T. Sensitizing hormone-refractory prostate cancer cells to drug treatment by targeting 14-3-3σ. Mol Cancer Ther 2006, 5: 903-12.
    • (2006) Mol Cancer Ther , vol.5 , pp. 903-912
    • Han, B.1    Xie, H.2    Chen, Q.3    Zhang, J.-T.4
  • 48
    • 13444257670 scopus 로고    scopus 로고
    • Unchanged survival rates of 14-3-3γ knockout mice after inoculation with pathological prion protein
    • Steinacker, P., Schwarz, P., Reim, K. et al. Unchanged survival rates of 14-3-3γ knockout mice after inoculation with pathological prion protein. Mol Cell Biol 2005, 25: 1339-46.
    • (2005) Mol Cell Biol , vol.25 , pp. 1339-1346
    • Steinacker, P.1    Schwarz, P.2    Reim, K.3
  • 49
    • 33748325681 scopus 로고    scopus 로고
    • Identification of 14-3-3ε substrates from embryonic murine brain
    • Ballif, B.A., Cao, Z., Schwartz, D., Carraway, K.L. and Gygi, S.P. Identification of 14-3-3ε substrates from embryonic murine brain. J Proteome Res 2006, 5: 2372-9.
    • (2006) J Proteome Res , vol.5 , pp. 2372-2379
    • Ballif, B.A.1    Cao, Z.2    Schwartz, D.3    Carraway, K.L.4    Gygi, S.P.5
  • 50
    • 33845989449 scopus 로고    scopus 로고
    • Transgenic mouse proteomics identifies new 14-3-3 associated proteins involved in cytoskeletal rearrangements and cell signaling
    • Angrand, P.O., Segura, I., Volkel, P. et al. Transgenic mouse proteomics identifies new 14-3-3 associated proteins involved in cytoskeletal rearrangements and cell signaling. Mol Cell Proteomics 2006, 5: 2211-27.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 2211-2227
    • Angrand, P.O.1    Segura, I.2    Volkel, P.3
  • 51
    • 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. 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: 1436-50.
    • (2004) Curr Biol , vol.14 , pp. 1436-1450
    • Jin, J.1    Smith, F.D.2    Stark, C.3
  • 52
    • 3543035767 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins
    • Meek, S.E., Lane, W.S. and Piwnica-Worms, H. Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins. J Biol Chem 2004, 279: 32046-54.
    • (2004) J Biol Chem , vol.279 , pp. 32046-32054
    • Meek, S.E.1    Lane, W.S.2    Piwnica-Worms, H.3
  • 53
    • 33749492783 scopus 로고    scopus 로고
    • Phospho-specific recognition by 14-3-3 proteins and antibodies monitored by a high throughput label-free optical biosensor
    • Wu, M., Coblitz, B., Shikano, S. et al. Phospho-specific recognition by 14-3-3 proteins and antibodies monitored by a high throughput label-free optical biosensor. FEBS Lett 2006, 580: 5681-9.
    • (2006) FEBS Lett , vol.580 , pp. 5681-5689
    • Wu, M.1    Coblitz, B.2    Shikano, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.