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Volumn 295, Issue 1, 2003, Pages 71-82

Effects of Prenyl Pyrophosphates on the Binding of PKCγ with RACK1

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; DIPHOSPHATES; DNA, COMPLEMENTARY; EYE; MOLECULAR SEQUENCE DATA; PACLITAXEL; PENAEIDAE; PHOSPHORYLATION; POLYISOPRENYL PHOSPHATES; PROTEIN BINDING; PROTEIN KINASE C; RECEPTORS, CELL SURFACE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; TUBULIN;

EID: 0347781683     PISSN: 0022104X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (9)

References (61)
  • 1
    • 0027787664 scopus 로고
    • PKCγ mutant mice exhibit mild deficits in spatial and contextual learning
    • Abeliovich A, Paylor R, Chen C, Kim JJ, Wehner JM, Tonegawa S. 1993. PKCγ mutant mice exhibit mild deficits in spatial and contextual learning. Cell 75:1263-1271.
    • (1993) Cell , vol.75 , pp. 1263-1271
    • Abeliovich, A.1    Paylor, R.2    Chen, C.3    Kim, J.J.4    Wehner, J.M.5    Tonegawa, S.6
  • 2
    • 0029347192 scopus 로고
    • How does taxol stabilize microtubules?
    • Arnal I, Wade RH. 1995. How does taxol stabilize microtubules? Curr Biol 5:900-908.
    • (1995) Curr Biol , vol.5 , pp. 900-908
    • Arnal, I.1    Wade, R.H.2
  • 3
    • 0027369005 scopus 로고
    • Effects of insulin and phorbol esters on MARCKS (myristoylated alanine-rich C-kinase substrate) phosphorylation (and other parameters of protein kinase C activation) in rat adipocytes, rat soleus muscle and BC3H-1 myocytes
    • Arnold TP, Standaert ML, Hernandez H, Watson J, Mischak H, Kazanietz MG, Zhao L, Cooper DR, Farese RV. 1993. Effects of insulin and phorbol esters on MARCKS (myristoylated alanine-rich C-kinase substrate) phosphorylation (and other parameters of protein kinase C activation) in rat adipocytes, rat soleus muscle and BC3H-1 myocytes. Biochem J 295:155-164.
    • (1993) Biochem J , vol.295 , pp. 155-164
    • Arnold, T.P.1    Standaert, M.L.2    Hernandez, H.3    Watson, J.4    Mischak, H.5    Kazanietz, M.G.6    Zhao, L.7    Cooper, D.R.8    Farese, R.V.9
  • 4
    • 0032865258 scopus 로고    scopus 로고
    • Protein kinase C anchoring deficit in postmortem brains of Alzheimer's disease patients
    • Battaini F, Pascale A, Lucchi L, Pasinetti GM, Govoni S. 1999. Protein kinase C anchoring deficit in postmortem brains of Alzheimer's disease patients. Exp Neurol 159:559-564.
    • (1999) Exp Neurol , vol.159 , pp. 559-564
    • Battaini, F.1    Pascale, A.2    Lucchi, L.3    Pasinetti, G.M.4    Govoni, S.5
  • 5
    • 0033944650 scopus 로고    scopus 로고
    • The PKC targeting protein RACK1 interacts with the Epstein-Barr virus activator protein BZLF1
    • Baumann M, Gires O, Kolch W, Mischak H, Zeidler R, Pich D, Hammerschmidt. 2000. The PKC targeting protein RACK1 interacts with the Epstein-Barr virus activator protein BZLF1. Eur J Biochem 267:3891-3901.
    • (2000) Eur J Biochem , vol.267 , pp. 3891-3901
    • Baumann, M.1    Gires, O.2    Kolch, W.3    Mischak, H.4    Zeidler, R.5    Pich, D.6    Hammerschmidt7
  • 6
    • 0027392102 scopus 로고
    • The MARCKS family of cellular protein kinase C substrates
    • Blackshear PJ. 1993. The MARCKS family of cellular protein kinase C substrates. J Biol Chem 268:1501-1504.
    • (1993) J Biol Chem , vol.268 , pp. 1501-1504
    • Blackshear, P.J.1
  • 7
    • 0342998893 scopus 로고
    • Enzymatic modification of proteins with a geranylgeranyl isoprenoid
    • Casey PJ, Thissen JA, Moomaw JF. 1991. Enzymatic modification of proteins with a geranylgeranyl isoprenoid. Proc Natl Acad Sci U S A 89:8313-8316.
    • (1991) Proc Natl Acad Sci U S A , vol.89 , pp. 8313-8316
    • Casey, P.J.1    Thissen, J.A.2    Moomaw, J.F.3
  • 8
    • 0025863885 scopus 로고
    • The direct measurement of protein kinase C (PKC) activity in isolated membranes using a selective peptide substrate
    • Chakravarthy BR, Bussey A, Whitfield JF, Sidorska M, Williams RE, Durkin JP. 1991. The direct measurement of protein kinase C (PKC) activity in isolated membranes using a selective peptide substrate. Anal Biochem 196:144-150.
    • (1991) Anal Biochem , vol.196 , pp. 144-150
    • Chakravarthy, B.R.1    Bussey, A.2    Whitfield, J.F.3    Sidorska, M.4    Williams, R.E.5    Durkin, J.P.6
  • 9
    • 0029620817 scopus 로고
    • Impaired motor coordination correlates with persistent multiple climbing fiber innervation in PKCγ mutant mice
    • Chen C, Kano M, Abeliovich A, Chen L, Bao S, Kim JJ, Hashimoto K, Thompson RF, Tonegawa S. 1995. Impaired motor coordination correlates with persistent multiple climbing fiber innervation in PKCγ mutant mice. Cell 83:1233-1242.
    • (1995) Cell , vol.83 , pp. 1233-1242
    • Chen, C.1    Kano, M.2    Abeliovich, A.3    Chen, L.4    Bao, S.5    Kim, J.J.6    Hashimoto, K.7    Thompson, R.F.8    Tonegawa, S.9
  • 10
    • 0036850218 scopus 로고    scopus 로고
    • Effects of prenyl pyrophosphates on the binding of S-Ras with KSR
    • Chen C-H, Fan J-H, Chuang N-N. 2002. Effects of prenyl pyrophosphates on the binding of S-Ras with KSR. J Exp Zool 293:551-560.
    • (2002) J Exp Zool , vol.293 , pp. 551-560
    • Chen, C.-H.1    Fan, J.-H.2    Chuang, N.-N.3
  • 11
    • 0036508344 scopus 로고    scopus 로고
    • taxol, a synthetic peptide encoding the taxol binding region
    • taxol, a synthetic peptide encoding the taxol binding region. J Exp Zool 292:376-383.
    • (2002) J Exp Zool , vol.292 , pp. 376-383
    • Chen, W.-Y.1    Yang, Y.-M.2    Chuang, N.-N.3
  • 12
    • 0025026515 scopus 로고
    • Purification and some properties of alkaline phosphatase from the hepatopancreas of the shrimp Penaeus japonicus (Crustacea: Decapoda)
    • Chuang NN, Shih SL. 1990. Purification and some properties of alkaline phosphatase from the hepatopancreas of the shrimp Penaeus japonicus (Crustacea: Decapoda). J Exp Zool 256:1-7.
    • (1990) J Exp Zool , vol.256 , pp. 1-7
    • Chuang, N.N.1    Shih, S.L.2
  • 13
    • 0037083524 scopus 로고    scopus 로고
    • In vivo dehydroepiandrosterone restores age-associated defects in the protein kinase C signal transduction pathway and related functional responses
    • Corsini E, Lucchi L, Meroni M, Racchi M, Solerte B, Fioravanti M, Viviani B, Marinovich M, Govoni S, Galli CL. 2002. In vivo dehydroepiandrosterone restores age-associated defects in the protein kinase C signal transduction pathway and related functional responses. J Immunol 168:1753-1758.
    • (2002) J Immunol , vol.168 , pp. 1753-1758
    • Corsini, E.1    Lucchi, L.2    Meroni, M.3    Racchi, M.4    Solerte, B.5    Fioravanti, M.6    Viviani, B.7    Marinovich, M.8    Govoni, S.9    Galli, C.L.10
  • 14
    • 0034326627 scopus 로고    scopus 로고
    • Receptor for activated C-kinase (RACK1), a WD motif-containing protein, specifically associates with human type I IFN receptor
    • Croze E, Usacheva A, Asarnow D, Minshall RD, Perez HD, Colamonici O. 2000. Receptor for activated C-kinase (RACK1), a WD motif-containing protein, specifically associates with human type I IFN receptor. J Immunol 165:5127-5132.
    • (2000) J Immunol , vol.165 , pp. 5127-5132
    • Croze, E.1    Usacheva, A.2    Asarnow, D.3    Minshall, R.D.4    Perez, H.D.5    Colamonici, O.6
  • 15
    • 0030670399 scopus 로고    scopus 로고
    • The coatomer protein b′-COP, a selective binding protein (RACK) for protein kinase Cε
    • Csukai M, Chen C-H, De Matteis MA, Mochly-Rosen D. 1997. The coatomer protein b′-COP, a selective binding protein (RACK) for protein kinase Cε. J Biol Chem 272:29200-29206.
    • (1997) J Biol Chem , vol.272 , pp. 29200-29206
    • Csukai, M.1    Chen, C.-H.2    De Matteis, M.A.3    Mochly-Rosen, D.4
  • 16
    • 0028082161 scopus 로고
    • Protein kinase C - A question of specificity
    • Dekker LV, Parker PJ. 1994. Protein kinase C - a question of specificity. TIBS 19:73-77.
    • (1994) TIBS , vol.19 , pp. 73-77
    • Dekker, L.V.1    Parker, P.J.2
  • 17
    • 0025940718 scopus 로고
    • Isoprenoid modification and plasma membrane association: Critical factors for ras oncogenicity
    • Der CJ, Cox AD. 1991. Isoprenoid modification and plasma membrane association: critical factors for ras oncogenicity. Cancer Cells 3:331-340.
    • (1991) Cancer Cells , vol.3 , pp. 331-340
    • Der, C.J.1    Cox, A.D.2
  • 19
    • 0347885274 scopus 로고
    • Regulation of M-phase progression in Chaetopterus oocytes by protein kinase C subspecies in maturation of Xenopus laevis oocytes
    • Eckberg WR, Palazzo RE. 1992. Regulation of M-phase progression in Chaetopterus oocytes by protein kinase C subspecies in maturation of Xenopus laevis oocytes. Mol Cell Biol 12:3776-3783.
    • (1992) Mol Cell Biol , vol.12 , pp. 3776-3783
    • Eckberg, W.R.1    Palazzo, R.E.2
  • 20
    • 0026496318 scopus 로고
    • Effects of insulin and phorbol esters on subcellular distribution of protein kinase C isoforms in rat adipocytes
    • Farese RV, Standaert ML, Francois AJ, Ways K, Arnold TP, Hernanadez H, Cooper DR. 1992. Effects of insulin and phorbol esters on subcellular distribution of protein kinase C isoforms in rat adipocytes. Biochem J 288:319-323.
    • (1992) Biochem J , vol.288 , pp. 319-323
    • Farese, R.V.1    Standaert, M.L.2    Francois, A.J.3    Ways, K.4    Arnold, T.P.5    Hernanadez, H.6    Cooper, D.R.7
  • 22
    • 0026352185 scopus 로고
    • Protein kinase C substrate and inhibitor characteristics of peptides derived from the myristolylated alanine-rich C kinase substrate (MARCKS) protein phosphorylation site domain
    • Graff JM, Rajan RR, Randall RR, Nairn AC, Blackshear PJ. 1991. Protein kinase C substrate and inhibitor characteristics of peptides derived from the myristolylated alanine-rich C kinase substrate (MARCKS) protein phosphorylation site domain. J Biol Chem 266:14390-14398.
    • (1991) J Biol Chem , vol.266 , pp. 14390-14398
    • Graff, J.M.1    Rajan, R.R.2    Randall, R.R.3    Nairn, A.C.4    Blackshear, P.J.5
  • 23
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • Hancock JF, Magee AI, Childs JE, Marshall CJ. 1989. All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 57:1167-1177.
    • (1989) Cell , vol.57 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 25
    • 0029328339 scopus 로고
    • Purification of the δ isoenzyme of protein kinase C from the hepatopancreas of the shrimp Penaeus monodon with phosphorylation on tyrosine residues
    • Huang C-F, Chuang NN. 1995. Purification of the δ isoenzyme of protein kinase C from the hepatopancreas of the shrimp Penaeus monodon with phosphorylation on tyrosine residues. J Exp Zool 272:258-265.
    • (1995) J Exp Zool , vol.272 , pp. 258-265
    • Huang, C.-F.1    Chuang, N.N.2
  • 26
    • 0033135767 scopus 로고    scopus 로고
    • Facilitated geranylgeranylation of shrimp ras-encoded p25 fusion protein by the binding with guanosine diphosphate
    • Huang C-F, Chuang NN. 1999. Facilitated geranylgeranylation of shrimp ras-encoded p25 fusion protein by the binding with guanosine diphosphate. J Exp Zool 283:510-521.
    • (1999) J Exp Zool , vol.283 , pp. 510-521
    • Huang, C.-F.1    Chuang, N.N.2
  • 27
    • 0019805521 scopus 로고
    • Taxol-induced polymerization of purified tubulin. Mechanism of action
    • Kumar N. 1981. Taxol-induced polymerization of purified tubulin. Mechanism of action. J Biol Chem 256:10435-10441.
    • (1981) J Biol Chem , vol.256 , pp. 10435-10441
    • Kumar, N.1
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0018180634 scopus 로고
    • A simple method for stabilizing protein-sulfhydryl groups during SDS-gel electrophoresis
    • Lane LC. 1978. A simple method for stabilizing protein-sulfhydryl groups during SDS-gel electrophoresis. Anal Biochem 86:655-664.
    • (1978) Anal Biochem , vol.86 , pp. 655-664
    • Lane, L.C.1
  • 30
    • 0032031246 scopus 로고    scopus 로고
    • Characterization of an intracellular receptor for activated protein kinase C (RACK) from the mollusk Biomphalaria glabrata, the intermediate host for Schistosoma mansoni
    • Lardans V, Serra E, Capron A, Dissous C. 1998. Characterization of an intracellular receptor for activated protein kinase C (RACK) from the mollusk Biomphalaria glabrata, the intermediate host for Schistosoma mansoni. Exp Parasitol 88:194-199.
    • (1998) Exp Parasitol , vol.88 , pp. 194-199
    • Lardans, V.1    Serra, E.2    Capron, A.3    Dissous, C.4
  • 31
    • 0032529733 scopus 로고    scopus 로고
    • Carboxyl-terminal CFFL-sequence-specific monomeric protein geranylgeranyl transferase I from the eyes of the shrimp Penaeus japonicus
    • Lin R-S, Chuang NN. 1998. Carboxyl-terminal CFFL-sequence-specific monomeric protein geranylgeranyl transferase I from the eyes of the shrimp Penaeus japonicus. J Exp Zool 281:565-573.
    • (1998) J Exp Zool , vol.281 , pp. 565-573
    • Lin, R.-S.1    Chuang, N.N.2
  • 32
    • 0032528863 scopus 로고    scopus 로고
    • Phosducin induces a structural change in transducin βγ
    • Loew A, Ho YK, Blundell T, Bax B. 1998. Phosducin induces a structural change in transducin βγ. Structure 6:1007-1019.
    • (1998) Structure , vol.6 , pp. 1007-1019
    • Loew, A.1    Ho, Y.K.2    Blundell, T.3    Bax, B.4
  • 34
    • 0032493314 scopus 로고    scopus 로고
    • Specific isoprenyl group linked to transducin γ-subunit is a determinant of its unique signaling properties among G-proteins
    • Matsuda T, Hashimoto Y, Ueda H, Asano T, Matsuura Y, Doi T, Takao T, Shimonishi Y, Fukada Y. 1998. Specific isoprenyl group linked to transducin γ-subunit is a determinant of its unique signaling properties among G-proteins. Biochemistry 37:9843-9850.
    • (1998) Biochemistry , vol.37 , pp. 9843-9850
    • Matsuda, T.1    Hashimoto, Y.2    Ueda, H.3    Asano, T.4    Matsuura, Y.5    Doi, T.6    Takao, T.7    Shimonishi, Y.8    Fukada, Y.9
  • 35
    • 0022699646 scopus 로고
    • Solid-phase synthesis
    • Merrifield RB. 1986. Solid-phase synthesis. Science 232: 341-347.
    • (1986) Science , vol.232 , pp. 341-347
    • Merrifield, R.B.1
  • 36
    • 0019492995 scopus 로고
    • Ultrasensitive stain for proteins in polyacrylamide gel shows regional variation in cerebrospinal fluid proteins
    • Merril CR, Goldman D, Sedman SA, Ebert MH. 1981. Ultrasensitive stain for proteins in polyacrylamide gel shows regional variation in cerebrospinal fluid proteins. Science 211:1437-1438.
    • (1981) Science , vol.211 , pp. 1437-1438
    • Merril, C.R.1    Goldman, D.2    Sedman, S.A.3    Ebert, M.H.4
  • 37
    • 0031964645 scopus 로고    scopus 로고
    • Anchoring proteins for protein kinase C: A means for isozyme selectivity
    • Mochly-Rosen D, Gordon AS. 1998. Anchoring proteins for protein kinase C: a means for isozyme selectivity. FASEB J 12:35-42.
    • (1998) FASEB J , vol.12 , pp. 35-42
    • Mochly-Rosen, D.1    Gordon, A.S.2
  • 38
    • 0025908315 scopus 로고
    • Identification of intracellular receptor proteins for activated protein kinase C
    • Mochly-Rosen D, Khaner H, Lopez J. 1991. Identification of intracellular receptor proteins for activated protein kinase C. Proc Natl Acad Sci U S A 88:3997-4000.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 3997-4000
    • Mochly-Rosen, D.1    Khaner, H.2    Lopez, J.3
  • 40
    • 0034254946 scopus 로고    scopus 로고
    • Role of C-terminal domains of the G protein β subunit in the activation of effectors
    • Myung C-S, Garrison JC. 2000. Role of C-terminal domains of the G protein β subunit in the activation of effectors. Proc Natl Acad Sci U S A 97:9311-9316.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 9311-9316
    • Myung, C.-S.1    Garrison, J.C.2
  • 41
    • 0023764824 scopus 로고
    • The molecular heterogeneity of protein kinase C and its implications for cellular regulation
    • Nishizuka Y. 1988. The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature 334:661-665.
    • (1988) Nature , vol.334 , pp. 661-665
    • Nishizuka, Y.1
  • 43
    • 0030461567 scopus 로고    scopus 로고
    • Developmental differences in place-learning performance between C57BL/6 and DBA/2 mice parallel the ontogeny of hippocampal protein kinase C
    • Paylor R, Baskall-Baldini L, Yuva L, Wehner JM. 1996. Developmental differences in place-learning performance between C57BL/6 and DBA/2 mice parallel the ontogeny of hippocampal protein kinase C. Behav Neurosci 110: 1415-1425.
    • (1996) Behav Neurosci , vol.110 , pp. 1415-1425
    • Paylor, R.1    Baskall-Baldini, L.2    Yuva, L.3    Wehner, J.M.4
  • 44
    • 0035667276 scopus 로고    scopus 로고
    • Dehydroepiandrosterone and the relationship with aging and memory: A possible link with protein kinase C functional machinery
    • Racchi M, Govoni S, Solerte SB, Galli CL, Corsini E. 2001. Dehydroepiandrosterone and the relationship with aging and memory: a possible link with protein kinase C functional machinery. Brain Res Rev 37:287-293.
    • (2001) Brain Res Rev , vol.37 , pp. 287-293
    • Racchi, M.1    Govoni, S.2    Solerte, S.B.3    Galli, C.L.4    Corsini, E.5
  • 45
    • 0034702018 scopus 로고    scopus 로고
    • The influenza A virus M1 protein interacts with the cellular receptor of activated C kinase (RACK) 1 and can be phosphorylated by protein kinase C
    • Reinhardt J, Wolff T. 2000. The influenza A virus M1 protein interacts with the cellular receptor of activated C kinase (RACK) 1 and can be phosphorylated by protein kinase C. Vet Microbiol 74:87-100.
    • (2000) Vet Microbiol , vol.74 , pp. 87-100
    • Reinhardt, J.1    Wolff, T.2
  • 46
    • 0026061739 scopus 로고
    • Sequence requirement for peptide recognition by rat brain p21ras protein farnesyl transferase
    • Reiss Y, Staradley SJ, Gierasch LM, Brown MS. 1991. Sequence requirement for peptide recognition by rat brain p21ras protein farnesyl transferase. Proc Natl Acad Sci USA 88:732-736.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 732-736
    • Reiss, Y.1    Staradley, S.J.2    Gierasch, L.M.3    Brown, M.S.4
  • 47
    • 0028036338 scopus 로고
    • Cloning of an intracellular receptor for protein kinase C: A homologue of the β subunit of G proteins
    • Ron D, Chen C-H, Caldwell J, Jamieson L, Orr E, Mochly-Rosen D. 1994. Cloning of an intracellular receptor for protein kinase C: a homologue of the β subunit of G proteins. Proc Natl Acad Sci U S A 91:839-843.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 839-843
    • Ron, D.1    Chen, C.-H.2    Caldwell, J.3    Jamieson, L.4    Orr, E.5    Mochly-Rosen, D.6
  • 49
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Schagger H, von Jagow G. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Anal Biochem 166:368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 50
    • 0035474310 scopus 로고    scopus 로고
    • Adaptor proteins in protein kinase C-mediated signal transduction
    • Schechtman D, Mochly-Rosen D. 2001. Adaptor proteins in protein kinase C-mediated signal transduction. Oncogene 20:6339-6347.
    • (2001) Oncogene , vol.20 , pp. 6339-6347
    • Schechtman, D.1    Mochly-Rosen, D.2
  • 51
    • 0035354341 scopus 로고    scopus 로고
    • γ-like (GGL) domains; new frontiers in G-protein signaling and β-propeller scaffolding
    • γ-like (GGL) domains; new frontiers in G-protein signaling and β-propeller scaffolding. Biochem Pharmacol 61:1329-1337.
    • (2001) Biochem Pharmacol , vol.61 , pp. 1329-1337
    • Sondek, J.1    Siderovski, D.P.2
  • 52
    • 0033036638 scopus 로고    scopus 로고
    • Cloning, molecular analysis and differential cell localization of the p36 RACK analogue antigen from the parasite protozoon Crithidia fasciculate
    • Taladriz S, Gonzalez-Aseguinolaza G, Marquet A, Larraga V. 1999. Cloning, molecular analysis and differential cell localization of the p36 RACK analogue antigen from the parasite protozoon Crithidia fasciculate. FEBS Lett 443:375-380.
    • (1999) FEBS Lett , vol.443 , pp. 375-380
    • Taladriz, S.1    Gonzalez-Aseguinolaza, G.2    Marquet, A.3    Larraga, V.4
  • 54
    • 0028217907 scopus 로고
    • The binding of corticosterone to the class-θ glutathione S-transferase from the eyes of the shrimp Penaeus japonicus (Crustacea: Decapoda)
    • Tseng S-F, Chuang NN. 1994. The binding of corticosterone to the class-θ glutathione S-transferase from the eyes of the shrimp Penaeus japonicus (Crustacea: Decapoda). Comp Biochem Physiol 108B:215-219.
    • (1994) Comp Biochem Physiol , vol.108 B , pp. 215-219
    • Tseng, S.-F.1    Chuang, N.N.2
  • 55
    • 0028819741 scopus 로고
    • Alterations in the immunoreactivity for muscarinic acetylcholine receptors and colocalized PKCγ in mouse hippocampus induced by spatial discrimination learning
    • Van der Zee EA, Compaan JC, Bohus B, Luiten PGM. 1995. Alterations in the immunoreactivity for muscarinic acetylcholine receptors and colocalized PKCγ in mouse hippocampus induced by spatial discrimination learning. Hippocampus 5:349-362.
    • (1995) Hippocampus , vol.5 , pp. 349-362
    • Van Der Zee, E.A.1    Compaan, J.C.2    Bohus, B.3    Luiten, P.G.M.4
  • 56
    • 0026459312 scopus 로고
    • Changes in PKCγ immunoreactivity in mouse hippocampus induced by spatial discrimination learning
    • Van der Zee EA, Compaan JC, de Boer M, Luiten PGM. 1992. Changes in PKCγ immunoreactivity in mouse hippocampus induced by spatial discrimination learning. J Neurosci 12:4808-4818.
    • (1992) J Neurosci , vol.12 , pp. 4808-4818
    • Van Der Zee, E.A.1    Compaan, J.C.2    De Boer, M.3    Luiten, P.G.M.4
  • 57
    • 0027480946 scopus 로고
    • Colocalization of muscarinic acetylcholine receptors and protein kinase C gamma in rat parietal cortex
    • Van der Zee EA, Strosberg AD, Bohus B, Luiten PG. 1993. Colocalization of muscarinic acetylcholine receptors and protein kinase C gamma in rat parietal cortex. Brain Res Mol Brain Res 18:152-162.
    • (1993) Brain Res Mol Brain Res , vol.18 , pp. 152-162
    • Van Der Zee, E.A.1    Strosberg, A.D.2    Bohus, B.3    Luiten, P.G.4
  • 58
    • 0020009818 scopus 로고
    • Preparation of tubulin from brain
    • Williams RC, Lee JC. 1982. Preparation of tubulin from brain. Methods Enzymol 85:376-385.
    • (1982) Methods Enzymol , vol.85 , pp. 376-385
    • Williams, R.C.1    Lee, J.C.2
  • 59
    • 0026001936 scopus 로고
    • A protein geranylgeranyl transferase from bovine brain: Implications for protein prenylation specificity
    • Yokoyama K, Goodwin GW, Ghomashchi F, Glomset JA, Gelb MH. 1991. A protein geranylgeranyl transferase from bovine brain: implications for protein prenylation specificity. Proc Natl Acad Sci U S A 88:5320-5326.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 5320-5326
    • Yokoyama, K.1    Goodwin, G.W.2    Ghomashchi, F.3    Glomset, J.A.4    Gelb, M.H.5
  • 60
    • 0023785047 scopus 로고
    • Tissue distribution and developmental expression of protein kinase C isozymes
    • Yoshida Y, Huang FL, Nkabayashi H, Huang KP. 1988. Tissue distribution and developmental expression of protein kinase C isozymes. J Biol Chem 263:9868-9873.
    • (1988) J Biol Chem , vol.263 , pp. 9868-9873
    • Yoshida, Y.1    Huang, F.L.2    Nkabayashi, H.3    Huang, K.P.4
  • 61
    • 0030943198 scopus 로고    scopus 로고
    • Characterization of Ha-Ras, Ki-Ras4A, and Ki-Ras4B as in vitro substrates for farnesyl protein transferase and geranylgeranyl protein transferase type I
    • Zhang FL, Kirschmeier P, Carr D, James L, Bond RW, Wang L, Patton R, Windsor WT, Syto R, Zhang R, Bishop WR. 1997. Characterization of Ha-Ras, Ki-Ras4A, and Ki-Ras4B as in vitro substrates for farnesyl protein transferase and geranylgeranyl protein transferase type I. J Biol Chem 272:10232-10239.
    • (1997) J Biol Chem , vol.272 , pp. 10232-10239
    • Zhang, F.L.1    Kirschmeier, P.2    Carr, D.3    James, L.4    Bond, R.W.5    Wang, L.6    Patton, R.7    Windsor, W.T.8    Syto, R.9    Zhang, R.10    Bishop, W.R.11


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