메뉴 건너뛰기




Volumn 179, Issue 8, 2007, Pages 5281-5290

Protein kinase C regulates expression and function of inhibitory killer cell Ig-like receptors in NK cells

Author keywords

[No Author keywords available]

Indexed keywords

CASEIN KINASE; KILLER CELL IMMUNOGLOBULIN LIKE RECEPTOR; KILLER CELL IMMUNOGLOBULIN LIKE RECEPTOR 3DL1; PHOSPHOTRANSFERASE; PROTEIN KINASE C; RECEPTOR; SERINE; THREONINE; CASEIN KINASE II; GLUTAMIC ACID; UNCLASSIFIED DRUG;

EID: 38449117450     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.179.8.5281     Document Type: Article
Times cited : (19)

References (56)
  • 1
    • 0027231011 scopus 로고
    • MHC class I expression on tumor targets inhibits natural killer cell-mediated cytotoxicity without interfering with target recognition
    • Kaufman, D. S., R. A. Schoon, and P. J. Leibson. 1993. MHC class I expression on tumor targets inhibits natural killer cell-mediated cytotoxicity without interfering with target recognition. J. Immunol. 150: 1429-1436.
    • (1993) J. Immunol , vol.150 , pp. 1429-1436
    • Kaufman, D.S.1    Schoon, R.A.2    Leibson, P.J.3
  • 3
    • 0031010992 scopus 로고    scopus 로고
    • Natural killer cell regulation during viral infection
    • Biron, C. A. 1997. Natural killer cell regulation during viral infection. Biochem. Soc. Trans. 25: 687-690.
    • (1997) Biochem. Soc. Trans , vol.25 , pp. 687-690
    • Biron, C.A.1
  • 4
    • 0032503029 scopus 로고    scopus 로고
    • Viral strategies of immune evasion
    • Ploegh, H. L. 1998. Viral strategies of immune evasion. Science 280: 248-253.
    • (1998) Science , vol.280 , pp. 248-253
    • Ploegh, H.L.1
  • 5
    • 0023129169 scopus 로고
    • NK susceptibility varies inversely with target cell class I HLA antigen expression
    • Storkus, W. J., D. N. Howell, R. D. Salter, J. R. Dawson, and P. Cresswell. 1987. NK susceptibility varies inversely with target cell class I HLA antigen expression. J. Immunol. 138: 1657-1659.
    • (1987) J. Immunol , vol.138 , pp. 1657-1659
    • Storkus, W.J.1    Howell, D.N.2    Salter, R.D.3    Dawson, J.R.4    Cresswell, P.5
  • 6
    • 0024822575 scopus 로고
    • Signal transduction mechanisms in human natural killer cells mediating antitumor immunity
    • Leibson, P. J., K. P. Windebank, T. J. Barna, and R. T. Abraham. 1989. Signal transduction mechanisms in human natural killer cells mediating antitumor immunity. Haematol. Blood Transfus. 32: 281-283.
    • (1989) Haematol. Blood Transfus , vol.32 , pp. 281-283
    • Leibson, P.J.1    Windebank, K.P.2    Barna, T.J.3    Abraham, R.T.4
  • 7
    • 0031860633 scopus 로고    scopus 로고
    • Natural killer cell receptors
    • Yokoyama, W. M. 1998. Natural killer cell receptors. Curr. Opin. Immunol. 10: 298-305.
    • (1998) Curr. Opin. Immunol , vol.10 , pp. 298-305
    • Yokoyama, W.M.1
  • 8
    • 0028332836 scopus 로고
    • NKB1: A natural killer cell receptor involved in the recognition of polymorphic HLA-B molecules
    • Litwin, V., J. Gumperz, P. Parham, J. H. Phillips, and L. L. Lanier. 1994. NKB1: a natural killer cell receptor involved in the recognition of polymorphic HLA-B molecules. J. Exp. Med. 180: 537-543.
    • (1994) J. Exp. Med , vol.180 , pp. 537-543
    • Litwin, V.1    Gumperz, J.2    Parham, P.3    Phillips, J.H.4    Lanier, L.L.5
  • 11
    • 0033559899 scopus 로고    scopus 로고
    • Differential roles of N- and C-terminal immunoreceptor tyrosine-based inhibition motifs during inhibition of cell activation by killer cell inhibitory receptors
    • Bruhns, P., P. Marchetti, W. H. Fridman, E. Vivier, and M. Daeron. 1999. Differential roles of N- and C-terminal immunoreceptor tyrosine-based inhibition motifs during inhibition of cell activation by killer cell inhibitory receptors. J. Immunol. 162: 3168-3175.
    • (1999) J. Immunol , vol.162 , pp. 3168-3175
    • Bruhns, P.1    Marchetti, P.2    Fridman, W.H.3    Vivier, E.4    Daeron, M.5
  • 12
    • 0037408363 scopus 로고    scopus 로고
    • Src homology region 2-containing protein tyrosine phosphatase-2 (SHP-2) can play a direct role in the inhibitory function of killer cell Ig-like receptors in human NK cells
    • Yusa, S., and K. S. Campbell. 2003. Src homology region 2-containing protein tyrosine phosphatase-2 (SHP-2) can play a direct role in the inhibitory function of killer cell Ig-like receptors in human NK cells. J. Immunol. 170: 4539-4547.
    • (2003) J. Immunol , vol.170 , pp. 4539-4547
    • Yusa, S.1    Campbell, K.S.2
  • 13
    • 2942530671 scopus 로고    scopus 로고
    • KIR2DL5 can inhibit human NK cell activation via recruitment of Src homology region 2-containing protein tyrosine phosphatase-2 (SHP-2)
    • Yusa, S., T. L. Catina, and K. S. Campbell. 2004. KIR2DL5 can inhibit human NK cell activation via recruitment of Src homology region 2-containing protein tyrosine phosphatase-2 (SHP-2). J. Immunol. 172: 7385-7392.
    • (2004) J. Immunol , vol.172 , pp. 7385-7392
    • Yusa, S.1    Catina, T.L.2    Campbell, K.S.3
  • 15
    • 0041534399 scopus 로고    scopus 로고
    • Vav1 dephosphorylation by the tyrosine phosphatase SHP-1 as a mechanism for inhibition of cellular cytotoxicity
    • Stebbins, C. C., C. Watzl, D. D. Billadeau, P. J. Leibson, D. N. Burshtyn, and E. O. Long. 2003. Vav1 dephosphorylation by the tyrosine phosphatase SHP-1 as a mechanism for inhibition of cellular cytotoxicity. Mol. Cell Biol. 23: 6291-6299.
    • (2003) Mol. Cell Biol , vol.23 , pp. 6291-6299
    • Stebbins, C.C.1    Watzl, C.2    Billadeau, D.D.3    Leibson, P.J.4    Burshtyn, D.N.5    Long, E.O.6
  • 16
    • 0030457304 scopus 로고    scopus 로고
    • Killer cell inhibitory receptor recognition of human leukocyte antigen (HLA) class I blocks formation of a pp36/PLC-γ signaling complex in human natural killer (NK) cells
    • Valiante, N. M., J. H. Phillips, L. L. Lanier, and P. Parham. 1996. Killer cell inhibitory receptor recognition of human leukocyte antigen (HLA) class I blocks formation of a pp36/PLC-γ signaling complex in human natural killer (NK) cells. J. Exp. Med. 184: 2243-2250.
    • (1996) J. Exp. Med , vol.184 , pp. 2243-2250
    • Valiante, N.M.1    Phillips, J.H.2    Lanier, L.L.3    Parham, P.4
  • 17
    • 0036784655 scopus 로고    scopus 로고
    • Molecular mechanism of the activation-induced cell death inhibition mediated by a p70 inhibitory killer cell Ig-like receptor in Jurkat T cells
    • Chwae, Y. J., M. J. Chang, S. M. Park, H. Yoon, H. J. Park, S. J. Kim, and J. Kim. 2002. Molecular mechanism of the activation-induced cell death inhibition mediated by a p70 inhibitory killer cell Ig-like receptor in Jurkat T cells. J. Immunol. 169: 3726-3735.
    • (2002) J. Immunol , vol.169 , pp. 3726-3735
    • Chwae, Y.J.1    Chang, M.J.2    Park, S.M.3    Yoon, H.4    Park, H.J.5    Kim, S.J.6    Kim, J.7
  • 18
    • 0033597937 scopus 로고    scopus 로고
    • Serine phosphorylation of the ligand-activated β-platelet-derived growth factor receptor by casein kinase I-γ2 inhibits the receptor's autophosphorylating activity
    • Bioukar, E. B., N. C. Marricco, D. Zuo, and L. Larose. 1999. Serine phosphorylation of the ligand-activated β-platelet-derived growth factor receptor by casein kinase I-γ2 inhibits the receptor's autophosphorylating activity. J. Biol. Chem. 274: 21457-21463.
    • (1999) J. Biol. Chem , vol.274 , pp. 21457-21463
    • Bioukar, E.B.1    Marricco, N.C.2    Zuo, D.3    Larose, L.4
  • 19
    • 0035054435 scopus 로고    scopus 로고
    • Interaction of CD163 with the regulatory subunit of casein kinase II (CKII) and dependence of CD163 signaling on CKII and protein kinase C
    • Ritter, M., C. Buechler, M. Kapinsky, and G. Schmitz. 2001. Interaction of CD163 with the regulatory subunit of casein kinase II (CKII) and dependence of CD163 signaling on CKII and protein kinase C. Eur. J. Immunol. 31: 999-1009.
    • (2001) Eur. J. Immunol , vol.31 , pp. 999-1009
    • Ritter, M.1    Buechler, C.2    Kapinsky, M.3    Schmitz, G.4
  • 20
    • 0034038868 scopus 로고    scopus 로고
    • Ser/Thr phosphorylation of hematopoietic specific protein 1 (HS1): Implication of protein kinase CK2
    • Ruzzene, M., A. M. Brunati, S. Sarno, O. Marin, A. Donella-Deana, and L. A. Pinna. 2000. Ser/Thr phosphorylation of hematopoietic specific protein 1 (HS1): implication of protein kinase CK2. Eur. J. Biochem. 267: 3065-3072.
    • (2000) Eur. J. Biochem , vol.267 , pp. 3065-3072
    • Ruzzene, M.1    Brunati, A.M.2    Sarno, S.3    Marin, O.4    Donella-Deana, A.5    Pinna, L.A.6
  • 21
    • 0034682546 scopus 로고    scopus 로고
    • The serine and threonine residues in the Ig-α cytoplasmic tail negatively regulate immunoreceptor tyrosine-based activation motif-mediated signal transduction
    • Muller, R., J. Wienands, and M. Reth. 2000. The serine and threonine residues in the Ig-α cytoplasmic tail negatively regulate immunoreceptor tyrosine-based activation motif-mediated signal transduction. Proc. Natl. Acad. Sci. USA 97: 8451-8454.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8451-8454
    • Muller, R.1    Wienands, J.2    Reth, M.3
  • 24
    • 0023945674 scopus 로고
    • Identification of the phosphorylation sites of clathrin light chain LCβ
    • Hill, B. L., K. Drickamer, F. M. Brodsky, and P. Parham. 1988. Identification of the phosphorylation sites of clathrin light chain LCβ. J. Biol. Chem. 263: 5499-5501.
    • (1988) J. Biol. Chem , vol.263 , pp. 5499-5501
    • Hill, B.L.1    Drickamer, K.2    Brodsky, F.M.3    Parham, P.4
  • 26
    • 0032400963 scopus 로고    scopus 로고
    • Differential CD5-dependent regulation of CD5-associated CK2 activity in mature and immature T cells: Implication on TCR/CD3-mediated activation
    • Raman, C., and R. P. Kimberly. 1998. Differential CD5-dependent regulation of CD5-associated CK2 activity in mature and immature T cells: implication on TCR/CD3-mediated activation. J. Immunol. 161: 5817-5820.
    • (1998) J. Immunol , vol.161 , pp. 5817-5820
    • Raman, C.1    Kimberly, R.P.2
  • 28
    • 0036473397 scopus 로고    scopus 로고
    • The role of β-arrestins in the termination and transduction of G-protein-coupled receptor signals
    • Luttrell, L. M., and R. J. Lefkowitz. 2002. The role of β-arrestins in the termination and transduction of G-protein-coupled receptor signals. J. Cell Sci. 115: 455-465.
    • (2002) J. Cell Sci , vol.115 , pp. 455-465
    • Luttrell, L.M.1    Lefkowitz, R.J.2
  • 29
    • 0037053280 scopus 로고    scopus 로고
    • Regulation of arrestin-3 phosphorylation by casein kinase II
    • Kim, Y. M., L. S. Barak, M. G. Caron, and J. L. Benovic. 2002. Regulation of arrestin-3 phosphorylation by casein kinase II. J. Biol. Chem. 277: 16837-16846.
    • (2002) J. Biol. Chem , vol.277 , pp. 16837-16846
    • Kim, Y.M.1    Barak, L.S.2    Caron, M.G.3    Benovic, J.L.4
  • 30
    • 0037094006 scopus 로고    scopus 로고
    • SHP-1- and phosphotyrosine-independent inhibitory signaling by a killer cell Ig-like receptor cytoplasmic domain in human NK cells
    • Yusa, S., T. L. Catina, and K. S. Campbell. 2002. SHP-1- and phosphotyrosine-independent inhibitory signaling by a killer cell Ig-like receptor cytoplasmic domain in human NK cells. J. Immunol. 168: 5047-5057.
    • (2002) J. Immunol , vol.168 , pp. 5047-5057
    • Yusa, S.1    Catina, T.L.2    Campbell, K.S.3
  • 32
    • 12444268260 scopus 로고    scopus 로고
    • Parallel purification of three catalytic subunits of the protein serine/threonine phosphatase 2A family (PP2A(C), PP4(C), and PP6(C)) and analysis of the interaction of PP2A(C) with alpha4 protein
    • Kloeker, S., R. Reed, J. L. McConnell, D. Chang, K. Tran, R. S. Westphal, B. K. Law, R. J. Colbran, M. Kamoun, K. S. Campbell, and B. E. Wadzinski. 2003. Parallel purification of three catalytic subunits of the protein serine/threonine phosphatase 2A family (PP2A(C), PP4(C), and PP6(C)) and analysis of the interaction of PP2A(C) with alpha4 protein. Protein Expr. Purif. 31: 19-33.
    • (2003) Protein Expr. Purif , vol.31 , pp. 19-33
    • Kloeker, S.1    Reed, R.2    McConnell, J.L.3    Chang, D.4    Tran, K.5    Westphal, R.S.6    Law, B.K.7    Colbran, R.J.8    Kamoun, M.9    Campbell, K.S.10    Wadzinski, B.E.11
  • 33
    • 0020983488 scopus 로고
    • Detection and quantification of phosphotyrosine in proteins
    • Cooper, J. A., B. M. Sefton, and T. Hunter. 1983. Detection and quantification of phosphotyrosine in proteins. Methods Enzymol. 99: 387-402.
    • (1983) Methods Enzymol , vol.99 , pp. 387-402
    • Cooper, J.A.1    Sefton, B.M.2    Hunter, T.3
  • 34
    • 0024558784 scopus 로고
    • Acid and base hydrolysis of phosphoproteins bound to immobilon facilitates analysis of phosphoamino acids in gelfractionated proteins
    • Kamps, M. P., and B. M. Sefton. 1989. Acid and base hydrolysis of phosphoproteins bound to immobilon facilitates analysis of phosphoamino acids in gelfractionated proteins. Anal. Biochem. 176: 22-27.
    • (1989) Anal. Biochem , vol.176 , pp. 22-27
    • Kamps, M.P.1    Sefton, B.M.2
  • 37
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs
    • Obenauer, J. C., L. C. Cantley, and M. B. Yaffe. 2003. Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Res. 31: 3635-3641.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3635-3641
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3
  • 39
    • 3342904976 scopus 로고    scopus 로고
    • Selective inhibition of the citrate-to-isocitrate reaction of cytosolic aconitase by phosphomimetic mutation of serine-711
    • Pitula, J. S., K. M. Deck, S. L. Clarke, S. A. Anderson, A. Vasanthakumar, and R. S. Eisenstein. 2004. Selective inhibition of the citrate-to-isocitrate reaction of cytosolic aconitase by phosphomimetic mutation of serine-711. Proc. Natl. Acad. Sci. USA 101: 10907-10912.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10907-10912
    • Pitula, J.S.1    Deck, K.M.2    Clarke, S.L.3    Anderson, S.A.4    Vasanthakumar, A.5    Eisenstein, R.S.6
  • 40
    • 0035413601 scopus 로고    scopus 로고
    • Protein kinase C: Structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions
    • Newton, A. C. 2001. Protein kinase C: structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions. Chem. Rev. 101: 2353-2364.
    • (2001) Chem. Rev , vol.101 , pp. 2353-2364
    • Newton, A.C.1
  • 41
    • 1242276189 scopus 로고    scopus 로고
    • D4476, a cell-permeant inhibitor of CK1, suppresses the site-specific phosphorylation and nuclear exclusion of FOXO1a
    • 5: 60-65
    • Rena, G., J. Bain, M. Elliott, and P. Cohen. 2004. D4476, a cell-permeant inhibitor of CK1, suppresses the site-specific phosphorylation and nuclear exclusion of FOXO1a. EMBO Rep. 5: 60-65.
    • (2004) EMBO Rep
    • Rena, G.1    Bain, J.2    Elliott, M.3    Cohen, P.4
  • 42
    • 0038127022 scopus 로고    scopus 로고
    • Protein kinase C is involved in 2B4 (CD244)-mediated cytotoxicity and AP-1 activation in natural killer cells
    • Chuang, S. S., J. K. Lee, and P. A. Mathew. 2003. Protein kinase C is involved in 2B4 (CD244)-mediated cytotoxicity and AP-1 activation in natural killer cells. Immunology 109: 432-439.
    • (2003) Immunology , vol.109 , pp. 432-439
    • Chuang, S.S.1    Lee, J.K.2    Mathew, P.A.3
  • 43
    • 0025935678 scopus 로고
    • Inhibition of the calpain-mediated proteolysis of protein kinase C enhances lytic activity in human NK cells
    • Shenoy, A. M., and Z. Brahmi. 1991. Inhibition of the calpain-mediated proteolysis of protein kinase C enhances lytic activity in human NK cells. Cell Immunol. 138: 24-34.
    • (1991) Cell Immunol , vol.138 , pp. 24-34
    • Shenoy, A.M.1    Brahmi, Z.2
  • 44
    • 0029932857 scopus 로고    scopus 로고
    • CD28-mediated cytotoxicity by the human leukemic NK cell line YT involves tyrosine phosphorylation, activation of phosphatidylinositol 3-kinase, and protein kinase C
    • Teng, J. M., X. R. Liu, G. B. Mills, and B. Dupont. 1996. CD28-mediated cytotoxicity by the human leukemic NK cell line YT involves tyrosine phosphorylation, activation of phosphatidylinositol 3-kinase, and protein kinase C. J. Immunol. 156: 3222-3232.
    • (1996) J. Immunol , vol.156 , pp. 3222-3232
    • Teng, J.M.1    Liu, X.R.2    Mills, G.B.3    Dupont, B.4
  • 46
    • 0034688172 scopus 로고    scopus 로고
    • + T cells is controlled by T-cell receptor engagement
    • + T cells is controlled by T-cell receptor engagement. Nature 403: 325-328.
    • (2000) Nature , vol.403 , pp. 325-328
    • Huard, B.1    Karlsson, L.2
  • 47
    • 0033527663 scopus 로고    scopus 로고
    • Association of β-arrestin with G protein-coupled receptors during clathrin-mediated endocytosis dictates the profile of receptor resensitization
    • Oakley, R. H., S. A. Laporte, J. A. Holt, L. S. Barak, and M. G. Caron. 1999. Association of β-arrestin with G protein-coupled receptors during clathrin-mediated endocytosis dictates the profile of receptor resensitization. J. Biol. Chem. 274: 32248-32257.
    • (1999) J. Biol. Chem , vol.274 , pp. 32248-32257
    • Oakley, R.H.1    Laporte, S.A.2    Holt, J.A.3    Barak, L.S.4    Caron, M.G.5
  • 48
    • 0030766471 scopus 로고    scopus 로고
    • 2-adrenergic receptor resensitization: Differential regulation of receptor resensitization in two distinct cell types
    • 2-adrenergic receptor resensitization: differential regulation of receptor resensitization in two distinct cell types. J. Biol. Chem. 272: 27005-27014.
    • (1997) J. Biol. Chem , vol.272 , pp. 27005-27014
    • Zhang, J.1    Barak, L.S.2    Winkler, K.E.3    Caron, M.G.4    Ferguson, S.S.5
  • 49
    • 4644314870 scopus 로고    scopus 로고
    • Regulation of SHP-1 tyrosine phosphatase in human platelets by serine phosphorylation at its C terminus
    • Jones, M. L., J. D. Craik, J. M. Gibbins, and A. W. Poole. 2004. Regulation of SHP-1 tyrosine phosphatase in human platelets by serine phosphorylation at its C terminus. J. Biol. Chem. 279: 40475-40483.
    • (2004) J. Biol. Chem , vol.279 , pp. 40475-40483
    • Jones, M.L.1    Craik, J.D.2    Gibbins, J.M.3    Poole, A.W.4
  • 50
    • 0035216604 scopus 로고    scopus 로고
    • Negative regulation of the SHPTP1 protein tyrosine phosphatase by protein kinase Cδ in response to DNA damage
    • Yoshida, K., and D. Kufe. 2001. Negative regulation of the SHPTP1 protein tyrosine phosphatase by protein kinase Cδ in response to DNA damage. Mol. Pharmacol. 60: 1431-1438.
    • (2001) Mol. Pharmacol , vol.60 , pp. 1431-1438
    • Yoshida, K.1    Kufe, D.2
  • 51
    • 13844294211 scopus 로고    scopus 로고
    • The casein kinase 1 family: Participation in multiple cellular processes in eukaryotes
    • Knippschild, U., A. Gocht, S. Wolff, N. Huber, J. Lohler, and M. Stoter. 2005. The casein kinase 1 family: participation in multiple cellular processes in eukaryotes. Cell Signal 17: 675-689.
    • (2005) Cell Signal , vol.17 , pp. 675-689
    • Knippschild, U.1    Gocht, A.2    Wolff, S.3    Huber, N.4    Lohler, J.5    Stoter, M.6
  • 52
    • 0343177223 scopus 로고    scopus 로고
    • A structural basis for substrate specificities of protein Ser/Thr kinases: Primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1
    • Songyang, Z., K. P. Lu, Y. T. Kwon, L. H. Tsai, O. Filhol, C. Cochet, D. A. Brickey, T. R. Soderling, C. Bartleson, D. J. Graves, et al. 1996. A structural basis for substrate specificities of protein Ser/Thr kinases: primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1. Mol. Cell Biol. 16: 6486-6493.
    • (1996) Mol. Cell Biol , vol.16 , pp. 6486-6493
    • Songyang, Z.1    Lu, K.P.2    Kwon, Y.T.3    Tsai, L.H.4    Filhol, O.5    Cochet, C.6    Brickey, D.A.7    Soderling, T.R.8    Bartleson, C.9    Graves, D.J.10
  • 53
    • 0035877111 scopus 로고    scopus 로고
    • CD45 function is regulated by an acidic 19-amino acid insert in domain II that serves as a binding and phosphoacceptor site for casein kinase 2
    • Greer, S. F., Y. Wang, C. Raman, and L. B. Justement. 2001. CD45 function is regulated by an acidic 19-amino acid insert in domain II that serves as a binding and phosphoacceptor site for casein kinase 2. J. Immunol. 166: 7208-7218.
    • (2001) J. Immunol , vol.166 , pp. 7208-7218
    • Greer, S.F.1    Wang, Y.2    Raman, C.3    Justement, L.B.4
  • 55
    • 0037031658 scopus 로고    scopus 로고
    • Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network
    • Doray, B., P. Ghosh, J. Griffith, H. J. Geuze, and S. Kornfeld. 2002. Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network. Science 297: 1700-1703.
    • (2002) Science , vol.297 , pp. 1700-1703
    • Doray, B.1    Ghosh, P.2    Griffith, J.3    Geuze, H.J.4    Kornfeld, S.5
  • 56
    • 0035242503 scopus 로고    scopus 로고
    • Catalytic activity of protein kinase CK1δ (casein kinase 1δ) is essential for its normal subcellular localization
    • Milne, D. M., P. Looby, and D. W. Meek. 2001. Catalytic activity of protein kinase CK1δ (casein kinase 1δ) is essential for its normal subcellular localization. Exp. Cell Res. 263: 43-54
    • (2001) Exp. Cell Res , vol.263 , pp. 43-54
    • Milne, D.M.1    Looby, P.2    Meek, D.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.