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Volumn 1480, Issue 1-2, 2000, Pages 65-76

Characterisation of two protein phosphatase 2A holoenzymes from maize seedlings

Author keywords

Modulation of activity; Plant protein phosphatase 2A holoenzyme; Subunit composition

Indexed keywords

AMMONIUM SULFATE; HISTONE H1; HOLOENZYME; OKADAIC ACID; PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 2A; POLYLYSINE; PROTAMINE;

EID: 0034647853     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(00)00097-2     Document Type: Article
Times cited : (12)

References (56)
  • 1
    • 0030296869 scopus 로고    scopus 로고
    • Molecular mechanisms of the protein serine/threonine phosphatases
    • Barford D. Molecular mechanisms of the protein serine/threonine phosphatases. Trends Biochem. Sci. 21:1996;407-412.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 407-412
    • Barford, D.1
  • 4
    • 0033972224 scopus 로고    scopus 로고
    • PR48, a novel regulatory subunit of protein phosphatase 2A, interacts with cdc6 and modulates DNA replication in human cells
    • Yan Z., Fedorov S.A., Mumby M.C., Williams R.S. PR48, a novel regulatory subunit of protein phosphatase 2A, interacts with cdc6 and modulates DNA replication in human cells. Mol. Cell. Biol. 20:2000;1021-1029.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1021-1029
    • Yan, Z.1    Fedorov, S.A.2    Mumby, M.C.3    Williams, R.S.4
  • 5
    • 0000722806 scopus 로고
    • Control of protein phosphatase 2A by multiple families of regulatory subunits
    • Kamibayashi C., Mumby M.C. Control of protein phosphatase 2A by multiple families of regulatory subunits. Adv. Prot. Phosphatases. 9:1995;195-210.
    • (1995) Adv. Prot. Phosphatases , vol.9 , pp. 195-210
    • Kamibayashi, C.1    Mumby, M.C.2
  • 6
    • 0029827632 scopus 로고    scopus 로고
    • P53-Dependent association between cyclin G and the B′ subunit of protein phosphatase 2A
    • Okamoto K., Kamibayashi C., Serrano M., Prives C., Mumby M.C., Beach D. p53-Dependent association between cyclin G and the B′ subunit of protein phosphatase 2A. Mol. Cell. Biol. 16:1996;6593-6602.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6593-6602
    • Okamoto, K.1    Kamibayashi, C.2    Serrano, M.3    Prives, C.4    Mumby, M.C.5    Beach, D.6
  • 7
    • 0030466725 scopus 로고    scopus 로고
    • The catalytic subunit of protein phosphatase 2A associates with the translation termination factor eRF1
    • Andjelković N., Zolnierowicz S., Van Hoof C., Goris J., Hemmings B.A. The catalytic subunit of protein phosphatase 2A associates with the translation termination factor eRF1. EMBO J. 15:1996;7156-7167.
    • (1996) EMBO J. , vol.15 , pp. 7156-7167
    • Andjelković, N.1    Zolnierowicz, S.2    Van Hoof, C.3    Goris, J.4    Hemmings, B.A.5
  • 8
    • 0031031397 scopus 로고    scopus 로고
    • HOX1 interacts with protein phosphatases PP2A and PP1 and disrupts a G2/M cell-cycle checkpoint
    • Kawabe T., Muslin A.J., Korsmeyer S.J. HOX1 interacts with protein phosphatases PP2A and PP1 and disrupts a G2/M cell-cycle checkpoint. Nature. 385:1997;454-458.
    • (1997) Nature , vol.385 , pp. 454-458
    • Kawabe, T.1    Muslin, A.J.2    Korsmeyer, S.J.3
  • 9
    • 0033531933 scopus 로고    scopus 로고
    • Regulation of protein phosphatase 2A activity by heat shock transcription factor
    • Y. Hong, K.D., Sarge, Regulation of protein phosphatase 2A activity by heat shock transcription factor 2, J. Biol. Chem. (1999) 12967-12970.
    • (1999) J. Biol. Chem. , vol.2 , pp. 12967-12970
    • Y. Hong, K.D.1    Sarge2
  • 11
    • 0030984108 scopus 로고    scopus 로고
    • B-cell receptor associated protein α4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A
    • Murata K., Wu J., Brautigan D.L. B-cell receptor associated protein α4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A. Proc. Natl. Acad. Sci. USA. 94:1997;10624-10629.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10624-10629
    • Murata, K.1    Wu, J.2    Brautigan, D.L.3
  • 15
    • 0024991575 scopus 로고
    • Sucrose-phosphate synthase is dephosphorylated by protein phosphatase 2A in spinach leaves: Evidence from the effects of okadaic acid and microcystin
    • Siegl G., MacKintosh C., Stitt M. Sucrose-phosphate synthase is dephosphorylated by protein phosphatase 2A in spinach leaves: evidence from the effects of okadaic acid and microcystin. FEBS Lett. 270:1990;198-202.
    • (1990) FEBS Lett. , vol.270 , pp. 198-202
    • Siegl, G.1    MacKintosh, C.2    Stitt, M.3
  • 16
    • 0027372939 scopus 로고
    • Sucrose-phosphate synthase phosphatase, a type 2A protein phosphatase, changes its sensitivity towards inhibition by inorganic phosphate in spinach leaves
    • Weiner H., Weiner H., Stitt M. Sucrose-phosphate synthase phosphatase, a type 2A protein phosphatase, changes its sensitivity towards inhibition by inorganic phosphate in spinach leaves. FEBS Lett. 333:1993;159-164.
    • (1993) FEBS Lett. , vol.333 , pp. 159-164
    • Weiner, H.1    Weiner, H.2    Stitt, M.3
  • 17
    • 0026059954 scopus 로고
    • Plant protein phosphatases. Subcellular distribution, detection of protein phosphatase 2C and identification of protein phosphatase 2A as the major quinate dehydrogenase phosphatase
    • MacKintosh C., Coggins J., Cohen P. Plant protein phosphatases. Subcellular distribution, detection of protein phosphatase 2C and identification of protein phosphatase 2A as the major quinate dehydrogenase phosphatase. Biochem. J. 273:1991;733-738.
    • (1991) Biochem. J. , vol.273 , pp. 733-738
    • MacKintosh, C.1    Coggins, J.2    Cohen, P.3
  • 18
    • 0025276303 scopus 로고
    • Bryophyllum fedtschenkoi protein phosphatase 2A can dephosphorylate phosphoenolpyruvate carboxylase
    • Carter P.J., Nimmo H.G., Fewson C.A., Wilkins M.B. Bryophyllum fedtschenkoi protein phosphatase 2A can dephosphorylate phosphoenolpyruvate carboxylase. FEBS Lett. 263:1990;233-236.
    • (1990) FEBS Lett. , vol.263 , pp. 233-236
    • Carter, P.J.1    Nimmo, H.G.2    Fewson, C.A.3    Wilkins, M.B.4
  • 19
    • 0026768507 scopus 로고
    • Regulation of spinach-leaf nitrate reductase by reversible phosphorylation
    • MacKintosh C. Regulation of spinach-leaf nitrate reductase by reversible phosphorylation. Biochim. Biophys. Acta. 1137:1992;121-126.
    • (1992) Biochim. Biophys. Acta , vol.1137 , pp. 121-126
    • MacKintosh, C.1
  • 20
    • 0000798386 scopus 로고
    • Ethylene signal is transduced via protein phosphorylation events in plants
    • Raz V., Fluhr R. Ethylene signal is transduced via protein phosphorylation events in plants. Plant Cell. 5:1993;523-530.
    • (1993) Plant Cell , vol.5 , pp. 523-530
    • Raz, V.1    Fluhr, R.2
  • 21
    • 0028065895 scopus 로고
    • Protein phosphatase inhibitors activate anti-fungal defence response of soybean cotyledons and cell cultures
    • MacKintosh C., Lyon G.D., MacKintosh R.W. Protein phosphatase inhibitors activate anti-fungal defence response of soybean cotyledons and cell cultures. Plant J. 5:1994;137-147.
    • (1994) Plant J. , vol.5 , pp. 137-147
    • MacKintosh, C.1    Lyon, G.D.2    MacKintosh, R.W.3
  • 22
    • 0000182279 scopus 로고
    • Ablation of papillar cell function in Brassica flowers results in the loss of stigma receptivity to pollination
    • Kandasamy M.K., Thorsness M.K., Rundle S.J., Goldberg M.L., Nasrallah J.B., Nasrallah M.E. Ablation of papillar cell function in Brassica flowers results in the loss of stigma receptivity to pollination. Plant Cell. 5:1993;263-275.
    • (1993) Plant Cell , vol.5 , pp. 263-275
    • Kandasamy, M.K.1    Thorsness, M.K.2    Rundle, S.J.3    Goldberg, M.L.4    Nasrallah, J.B.5    Nasrallah, M.E.6
  • 23
    • 0027143049 scopus 로고
    • Effect of inhibitors of protein serine/threonine phosphatases on pollination in Brassica
    • Rundle S.J., Nasrallah M.E., Nasrallah J.B. Effect of inhibitors of protein serine/threonine phosphatases on pollination in Brassica. Plant Physiol. 103:1993;1165-1171.
    • (1993) Plant Physiol. , vol.103 , pp. 1165-1171
    • Rundle, S.J.1    Nasrallah, M.E.2    Nasrallah, J.B.3
  • 24
    • 0033021266 scopus 로고    scopus 로고
    • Molecular characterisation of catalytic-subunit cDNA sequences encoding protein phosphatases 1 and 2A and study of their roles in the gibberellin-dependent Osamy-c expression in rice
    • Chang M., Wang B., Chen X., Wu R. Molecular characterisation of catalytic-subunit cDNA sequences encoding protein phosphatases 1 and 2A and study of their roles in the gibberellin-dependent Osamy-c expression in rice. Plant Mol. Biol. 39:1999;105-115.
    • (1999) Plant Mol. Biol. , vol.39 , pp. 105-115
    • Chang, M.1    Wang, B.2    Chen, X.3    Wu, R.4
  • 26
    • 0029940505 scopus 로고    scopus 로고
    • A mutation in protein phosphatase 2A regulatory subunit A affects auxin transport in Arabidopsis
    • Garbers C., DeLong A., Deruére J., Bernasconi P., Söll D. A mutation in protein phosphatase 2A regulatory subunit A affects auxin transport in Arabidopsis. EMBO J. 15:1996;2115-2124.
    • (1996) EMBO J. , vol.15 , pp. 2115-2124
    • Garbers, C.1    DeLong, A.2    Deruére, J.3    Bernasconi, P.4    Söll, D.5
  • 27
    • 0027323054 scopus 로고
    • Protein phosphatase activity is required for light inducible gene expression in maize
    • Sheen J. Protein phosphatase activity is required for light inducible gene expression in maize. EMBO J. 12:1993;3497-3505.
    • (1993) EMBO J. , vol.12 , pp. 3497-3505
    • Sheen, J.1
  • 28
    • 0039613876 scopus 로고    scopus 로고
    • The RCN1-encoded A subunit of protein phosphatase activity in vivo
    • Druère J., Jackson K., Garbers C., Söll D., DeLong A. The RCN1-encoded A subunit of protein phosphatase activity in vivo. Plant J. 20:1999;389-399.
    • (1999) Plant J. , vol.20 , pp. 389-399
    • Druère, J.1    Jackson, K.2    Garbers, C.3    Söll, D.4    DeLong, A.5
  • 29
    • 0028047087 scopus 로고
    • Inhibitors of protein phosphatases 1 and 2A block the sugar-inducible gene expression in plants
    • Takeda S., Mano S., Ohto M., Nakamura K. Inhibitors of protein phosphatases 1 and 2A block the sugar-inducible gene expression in plants. Plant Physiol. 106:1994;567-574.
    • (1994) Plant Physiol. , vol.106 , pp. 567-574
    • Takeda, S.1    Mano, S.2    Ohto, M.3    Nakamura, K.4
  • 30
    • 0030934317 scopus 로고    scopus 로고
    • Differential expression of three Arabidopsis genes encoding the B′ regulatory subunit of protein phosphatase 2A
    • Latorre K.A., Harris D.M., Rundle S.J. Differential expression of three Arabidopsis genes encoding the B′ regulatory subunit of protein phosphatase 2A. Eur. J. Biochem. 245:1997;156-163.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 156-163
    • Latorre, K.A.1    Harris, D.M.2    Rundle, S.J.3
  • 31
    • 0027547244 scopus 로고
    • Protein phosphatases in higher plants: Multiplicity of type 2A phosphatases in Arabidopsis thaliana
    • Ariño J., Pérez-Callejón E., Cunillera N., Camps M., Posas F., Ferrer A. Protein phosphatases in higher plants: multiplicity of type 2A phosphatases in Arabidopsis thaliana. Plant Mol. Biol. 21:1993;475-485.
    • (1993) Plant Mol. Biol. , vol.21 , pp. 475-485
    • Ariño, J.1    Pérez-Callejón, E.2    Cunillera, N.3    Camps, M.4    Posas, F.5    Ferrer, A.6
  • 32
    • 0028519016 scopus 로고
    • Molecular characterisation of a fourth isoform of the catalytic subunit of protein phosphatase 2A from in Arabidopsis thaliana
    • Casamayor A., Pérez-Callejón E., Pujol G., Ariño J., Ferrer A. Molecular characterisation of a fourth isoform of the catalytic subunit of protein phosphatase 2A from in Arabidopsis thaliana. Plant Mol. Biol. 26:1994;523-528.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 523-528
    • Casamayor, A.1    Pérez-Callejón, E.2    Pujol, G.3    Ariño, J.4    Ferrer, A.5
  • 33
    • 0027248126 scopus 로고
    • Isolation and characterisation of a phosphoprotein phosphatase type 2A gene from alfalfa
    • Pirck M., Páy A., Heberle-Bors E., Hirt H. Isolation and characterisation of a phosphoprotein phosphatase type 2A gene from alfalfa. Mol. Gen. Genet. 240:1993;126-131.
    • (1993) Mol. Gen. Genet. , vol.240 , pp. 126-131
    • Pirck, M.1    Páy, A.2    Heberle-Bors, E.3    Hirt, H.4
  • 34
    • 0025605012 scopus 로고
    • Identification by molecular cloning of two cDNA sequences from the plant Brassica napus which are very similar to mammalian protein phosphatases-1 and -2A
    • MacKintosh R.W., Haycox G., Hardie D.G., Cohen P.T.W. Identification by molecular cloning of two cDNA sequences from the plant Brassica napus which are very similar to mammalian protein phosphatases-1 and -2A. FEBS Lett. 276:1990;156-160.
    • (1990) FEBS Lett. , vol.276 , pp. 156-160
    • MacKintosh, R.W.1    Haycox, G.2    Hardie, D.G.3    Cohen, P.T.W.4
  • 35
    • 0344832570 scopus 로고    scopus 로고
    • Multiple genes encoding serine/threonine protein phosphatases and their differential expression in Nicotiana tabacum
    • Suh M.C., Cho H.S., Kim Y.S., Liu J.R., Lee H-S. Multiple genes encoding serine/threonine protein phosphatases and their differential expression in Nicotiana tabacum. Plant Mol. Biol. 36:1998;315-322.
    • (1998) Plant Mol. Biol. , vol.36 , pp. 315-322
    • Suh, M.C.1    Cho, H.S.2    Kim, Y.S.3    Liu, J.R.4    Lee, H.-S.5
  • 36
    • 0344301980 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of two phosphatase 2A catalytic subunit genes from Arabidopsis thaliana
    • Pérez-Callejón E., Casamayor A., Pujol G., Camps M., Ferrer A., Ariño J. Molecular cloning and characterisation of two phosphatase 2A catalytic subunit genes from Arabidopsis thaliana. Gene. 209:1998;105-112.
    • (1998) Gene , vol.209 , pp. 105-112
    • Pérez-Callejón, E.1    Casamayor, A.2    Pujol, G.3    Camps, M.4    Ferrer, A.5    Ariño, J.6
  • 37
    • 0028535043 scopus 로고
    • Characterisation of cDNA and genomic clones encoding homologues of the 65 kDa regulatory subunit of protein phosphatase 2A in Arabidopsis thaliana
    • Slabas A.R., Fordham-Skelton A.P., Fletcher D., Martinez-Rivas J.M., Swinhoe R., Croy R.R.D., Evans L.M. Characterisation of cDNA and genomic clones encoding homologues of the 65 kDa regulatory subunit of protein phosphatase 2A in Arabidopsis thaliana. Plant Mol. Biol. 26:1994;1125-1138.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 1125-1138
    • Slabas, A.R.1    Fordham-Skelton, A.P.2    Fletcher, D.3    Martinez-Rivas, J.M.4    Swinhoe, R.5    Croy, R.R.D.6    Evans, L.M.7
  • 38
    • 0030152650 scopus 로고    scopus 로고
    • Characterisation of DNA sequences encoding a novel isoform of the 55 kDa B regulatory subunit of the type 2A protein serine/threonine phosphatase of Arabidopsis thaliana
    • Corum J.W. III, Hartung A.J., Stamey R.T., Rundle S.J. Characterisation of DNA sequences encoding a novel isoform of the 55 kDa B regulatory subunit of the type 2A protein serine/threonine phosphatase of Arabidopsis thaliana. Plant Mol. Biol. 31:1996;419-427.
    • (1996) Plant Mol. Biol. , vol.31 , pp. 419-427
    • Corum J.W. III1    Hartung, A.J.2    Stamey, R.T.3    Rundle, S.J.4
  • 39
    • 0029294103 scopus 로고
    • Characterisation of a cDNA encoding the 55 kDa B regulatory subunit of Arabidopsis protein phosphatase 2A
    • Rundle S.J., Hartung A.W., Corum J.W. III, O'Neill M. Characterisation of a cDNA encoding the 55 kDa B regulatory subunit of Arabidopsis protein phosphatase 2A. Plant Mol. Biol. 28:1995;257-266.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 257-266
    • Rundle, S.J.1    Hartung, A.W.2    Corum J.W. III3    O'Neill, M.4
  • 40
    • 0033558124 scopus 로고    scopus 로고
    • Molecular characterisation of the B′ regulatory subunit gene family of Arabidopsis protein phosphatase 2A
    • Haynes J.G., Hartung A.J., Hendershot J.D. III, Passingham R.S., Rundle S.J. Molecular characterisation of the B′ regulatory subunit gene family of Arabidopsis protein phosphatase 2A. Eur. J. Biochem. 260:1999;127-136.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 127-136
    • Haynes, J.G.1    Hartung, A.J.2    Hendershot J.D. III3    Passingham, R.S.4    Rundle, S.J.5
  • 42
    • 49749165001 scopus 로고
    • The phosphorylase b to a converting enzyme of rabbit skeletal muscle
    • Krebs E.G., Fischer E.H. The phosphorylase b to a converting enzyme of rabbit skeletal muscle. Biochim. Biophys. Acta. 20:1956;302-309.
    • (1956) Biochim. Biophys. Acta , vol.20 , pp. 302-309
    • Krebs, E.G.1    Fischer, E.H.2
  • 43
    • 0015912123 scopus 로고
    • The subunit structure of rabbit-skeletal-muscle phosphorylase kinase, and the molecular basis of its activation reactions
    • Cohen P. The subunit structure of rabbit-skeletal-muscle phosphorylase kinase, and the molecular basis of its activation reactions. Eur. J. Biochem. 34:1973;1-14.
    • (1973) Eur. J. Biochem. , vol.34 , pp. 1-14
    • Cohen, P.1
  • 44
    • 0028099583 scopus 로고
    • Diversity in the regulatory B-subunit of protein phosphatase 2A Identification of a novel isoform highly expressed in brain
    • Zolnierowicz S., Csortos C., Bondor J., Verin A., Mumby M.C., DePaoli-Roach A.A. Diversity in the regulatory B-subunit of protein phosphatase 2A Identification of a novel isoform highly expressed in brain. Biochemistry. 33:1994;11858-11867.
    • (1994) Biochemistry , vol.33 , pp. 11858-11867
    • Zolnierowicz, S.1    Csortos, C.2    Bondor, J.3    Verin, A.4    Mumby, M.C.5    DePaoli-Roach, A.A.6
  • 45
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 46
    • 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
  • 48
    • 0025877838 scopus 로고
    • Inhibitory effect of okadaic acid on the p-nitrophenyl phosphate phosphatase activity of protein phosphatases
    • Takai A., Mieskes G. Inhibitory effect of okadaic acid on the p-nitrophenyl phosphate phosphatase activity of protein phosphatases. Biochem. J. 275:1991;233-239.
    • (1991) Biochem. J. , vol.275 , pp. 233-239
    • Takai, A.1    Mieskes, G.2
  • 49
    • 0025961719 scopus 로고
    • Improved detection of human pancreatic proteins separated by two-dimensional isoelectric focusing/sodium dodecyl sulfate gel electrophoresis using a combined staining procedure
    • Hansler M., Appelt G., Rogos R. Improved detection of human pancreatic proteins separated by two-dimensional isoelectric focusing/sodium dodecyl sulfate gel electrophoresis using a combined staining procedure. J. Chromatogr. 563:1991;63-71.
    • (1991) J. Chromatogr. , vol.563 , pp. 63-71
    • Hansler, M.1    Appelt, G.2    Rogos, R.3
  • 52
    • 0033213260 scopus 로고    scopus 로고
    • The Arabidopsis homolog of yeast TAP42 and Mammalian α4 binds to the catalytic subunit of protein phosphatase 2A and is induced by chilling
    • Harris D.M., Myrick T.L., Rundle S.J. The Arabidopsis homolog of yeast TAP42 and Mammalian α4 binds to the catalytic subunit of protein phosphatase 2A and is induced by chilling. Plant Physiol. 121:1999;609-617.
    • (1999) Plant Physiol. , vol.121 , pp. 609-617
    • Harris, D.M.1    Myrick, T.L.2    Rundle, S.J.3
  • 53
    • 0023154421 scopus 로고
    • Purification and properties of polycation-stimulated phosphorylase phosphatases from rabbit skeletal muscle
    • Waelkens E., Goris J., Merlevede W. Purification and properties of polycation-stimulated phosphorylase phosphatases from rabbit skeletal muscle. J. Biol. Chem. 262:1987;1049-1056.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1049-1056
    • Waelkens, E.1    Goris, J.2    Merlevede, W.3
  • 54
    • 0027980812 scopus 로고
    • The phospho-opsin phosphatase from bovine rod outer segments. An insight into the mechanism of stimulation of type-2A protein phosphatase activity by protamine
    • King A.J., Andjelković N., Hemmings B.A., Akhtar M. The phospho-opsin phosphatase from bovine rod outer segments. An insight into the mechanism of stimulation of type-2A protein phosphatase activity by protamine. Eur. J. Biochem. 225:1994;383-394.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 383-394
    • King, A.J.1    Andjelković, N.2    Hemmings, B.A.3    Akhtar, M.4
  • 55
    • 0030874269 scopus 로고    scopus 로고
    • Modulation of the enzymatic properties of protein phosphatase 2A catalytic subunit by the recombinant 65-kDa regulatory subunit PR65α
    • Turowski P., Favre B., Campbell K.S., Lamb N.J.C., Hemmings B.A. Modulation of the enzymatic properties of protein phosphatase 2A catalytic subunit by the recombinant 65-kDa regulatory subunit PR65α Eur. J. Biochem. 248:1997;200-208.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 200-208
    • Turowski, P.1    Favre, B.2    Campbell, K.S.3    Lamb, N.J.C.4    Hemmings, B.A.5
  • 56
    • 0024970336 scopus 로고
    • Identification of the ATP+Mg-dependent and polycation-stimulated protein phosphatases in the germinal vesicle of the Xenopus oocyte
    • Jessus C., Goris J., Staquet S., Cayla X., Ozon R., Merlevede W. Identification of the ATP+Mg-dependent and polycation-stimulated protein phosphatases in the germinal vesicle of the Xenopus oocyte. Biochem. J. 260:1989;45-51.
    • (1989) Biochem. J. , vol.260 , pp. 45-51
    • Jessus, C.1    Goris, J.2    Staquet, S.3    Cayla, X.4    Ozon, R.5    Merlevede, W.6


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