메뉴 건너뛰기




Volumn 96, Issue 1, 1999, Pages 99-110

The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOPROTEIN PHOSPHATASE;

EID: 0033534405     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80963-0     Document Type: Article
Times cited : (371)

References (63)
  • 1
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F-1 ATPase
    • Abrahams, J.P., and Leslie, A.G.W. (1996). Methods used in the structure determination of bovine mitochondrial F-1 ATPase. Acta Crystallogr. D52, 30-42.
    • (1996) Acta Crystallogr. , vol.D52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 2
    • 0029392854 scopus 로고
    • HEAT repeats in the Huntington's disease protein
    • Andrade, M.A., and Bork, P. (1995). HEAT repeats in the Huntington's disease protein. Nature Genet. 11, 115-116.
    • (1995) Nature Genet. , vol.11 , pp. 115-116
    • Andrade, M.A.1    Bork, P.2
  • 3
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G.J. (1993). ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 6
    • 0024557105 scopus 로고
    • Isolation and partial characterization of an Mr 60,000 subunit of a type 2A phosphatase from rabbit reticulocytes
    • Chen, S.-C., Kramer, G., and Hardesty, B. (1989). Isolation and partial characterization of an Mr 60,000 subunit of a type 2A phosphatase from rabbit reticulocytes. J. Biol. Chem. 264, 7267-7275.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7267-7275
    • Chen, S.-C.1    Kramer, G.2    Hardesty, B.3
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 8
    • 0032563246 scopus 로고    scopus 로고
    • Crystallographic analysis of the recognition of a nuclear localisation signal by the nuclear import factor karypherin α
    • Conti, E., Uy, M., Leighton, L., Blobel, G., and Kuriyan, J. (1998). Crystallographic analysis of the recognition of a nuclear localisation signal by the nuclear import factor karypherin α. Cell 94, 193-204.
    • (1998) Cell , vol.94 , pp. 193-204
    • Conti, E.1    Uy, M.2    Leighton, L.3    Blobel, G.4    Kuriyan, J.5
  • 9
    • 0030047451 scopus 로고    scopus 로고
    • High complexity in the expression of the B′ subunit of protein phosphatase 2Ao
    • Csortos, C., Zolnierowicz, S., Bako, E., Durbin, S.D., and DePaoli-Roach, A.A. (1996). High complexity in the expression of the B′ subunit of protein phosphatase 2Ao. J. Biol. Chem. 271, 2578-2588.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2578-2588
    • Csortos, C.1    Zolnierowicz, S.2    Bako, E.3    Durbin, S.D.4    DePaoli-Roach, A.A.5
  • 10
    • 0032473425 scopus 로고    scopus 로고
    • The structure of the tetratricopeptide repeats of protein phosphatase 5: Implications for TPR-mediated protein-protein interactions
    • Das, A.K., Cohen, P.W., and Barford, D. (1998). The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J. 17, 1192-1199.
    • (1998) EMBO J. , vol.17 , pp. 1192-1199
    • Das, A.K.1    Cohen, P.W.2    Barford, D.3
  • 11
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for the multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de la Fortelle, E., and Bricogne, G. (1997). Maximum-likelihood heavy-atom parameter refinement for the multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 13
    • 0029825829 scopus 로고    scopus 로고
    • Expression in yeast of binding regions of karyopherins alpha and beta inhibits nuclear import and cell growth
    • Enenkel, C., Schulke, N., and Blobel, G. (1996). Expression in yeast of binding regions of karyopherins alpha and beta inhibits nuclear import and cell growth. Proc. Natl. Acad. Sci. USA 93, 12986-12991.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12986-12991
    • Enenkel, C.1    Schulke, N.2    Blobel, G.3
  • 14
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MOLSCRIPT that includes greatly enhanced colouring capbilities
    • Esnouf, R.M. (1997). An extensively modified version of MOLSCRIPT that includes greatly enhanced colouring capbilities. J. Mol. Graph. 15, 132-134.
    • (1997) J. Mol. Graph. , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 15
    • 0000746745 scopus 로고    scopus 로고
    • Multivariate characterisation of molecules for QSAR
    • Goodford, P. (1996). Multivariate characterisation of molecules for QSAR. J. Chemometrics 10, 107-117.
    • (1996) J. Chemometrics , vol.10 , pp. 107-117
    • Goodford, P.1
  • 16
    • 0032103078 scopus 로고    scopus 로고
    • Huntingtin: A single bait hooks many species
    • Gusella, J.F., and MacDonald, M.E. (1998). Huntingtin: a single bait hooks many species. Curr. Opin. Neurobiol. 8, 425-430.
    • (1998) Curr. Opin. Neurobiol. , vol.8 , pp. 425-430
    • Gusella, J.F.1    MacDonald, M.E.2
  • 17
    • 0026091769 scopus 로고
    • CDC55, a S. cerevisiae gene involved in cellular morphogenesis: Identification, characterisation, and homology to the B subunit of mammalian type 2A protein phosphatase
    • Healy, A.M., Zolnierowicz, S., Stapleton, A.E., Goebl, M., DePaoli-Roach, A.A., and Pringle, J.R. (1991). CDC55, a S. cerevisiae gene involved in cellular morphogenesis: identification, characterisation, and homology to the B subunit of mammalian type 2A protein phosphatase. Mol. Cell Biol. 11, 5767-5780.
    • (1991) Mol. Cell Biol. , vol.11 , pp. 5767-5780
    • Healy, A.M.1    Zolnierowicz, S.2    Stapleton, A.E.3    Goebl, M.4    DePaoli-Roach, A.A.5    Pringle, J.R.6
  • 18
    • 0025275038 scopus 로고
    • Alphaforms and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure
    • Hemmings, B.A., Adams-Pearson, C., Maurer, F., Mueller, P., Goris, J., Merlevede, W., Hofsteenge, J., and Stone, S.R. (1990). Alphaforms and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure. Biochemistry 29, 3166-3173.
    • (1990) Biochemistry , vol.29 , pp. 3166-3173
    • Hemmings, B.A.1    Adams-Pearson, C.2    Maurer, F.3    Mueller, P.4    Goris, J.5    Merlevede, W.6    Hofsteenge, J.7    Stone, S.R.8
  • 20
    • 0027277098 scopus 로고
    • On target with a new mechanism for the regulation of protein phosphorylation
    • Hubbard, M.J., and Cohen, P. (1993). On target with a new mechanism for the regulation of protein phosphorylation. Trends Biochem. Sei. 18, 172-177.
    • (1993) Trends Biochem. Sei. , vol.18 , pp. 172-177
    • Hubbard, M.J.1    Cohen, P.2
  • 21
    • 0030800831 scopus 로고    scopus 로고
    • Three-dimensional structure of the armadillo repeat region of beta-catenin
    • Huber, A.H., Nelson, W.J., and Weis, W.I. (1997). Three-dimensional structure of the armadillo repeat region of beta-catenin. Cell 90, 871-882.
    • (1997) Cell , vol.90 , pp. 871-882
    • Huber, A.H.1    Nelson, W.J.2    Weis, W.I.3
  • 22
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and dephosphorylation
    • Hunter, T. (1995). Protein kinases and phosphatases: the yin and yang of protein phosphorylation and dephosphorylation. Cell 80, 225-236.
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 23
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjeldgaard, M. (1991). Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 24
    • 0025036315 scopus 로고
    • Association of simian virus 40 small-t antigen with the 61-Kd component of a cellular protein complex
    • Joshi, B., and Rundell, K. (1990). Association of simian virus 40 small-t antigen with the 61-Kd component of a cellular protein complex. J. Virol. 64, 5649-5651.
    • (1990) J. Virol. , vol.64 , pp. 5649-5651
    • Joshi, B.1    Rundell, K.2
  • 25
    • 0028021165 scopus 로고
    • Comparison of heterotrmeric protein phosphatase 2A containing different B subunits
    • Kamibayashi, C., Estes, R., Lickteig, R.L., Yang, S.-I., Craft, C., and Mumby, M. (1994). Comparison of heterotrmeric protein phosphatase 2A containing different B subunits. J. Biol. Chem. 269, 20139-20148.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20139-20148
    • Kamibayashi, C.1    Estes, R.2    Lickteig, R.L.3    Yang, S.-I.4    Craft, C.5    Mumby, M.6
  • 26
    • 0024996931 scopus 로고
    • Distinct, essential roles of type 1 and type 2A protein phosphatases in the control of the fission yeast cell division cycle
    • Kinoshita, N., Ohkura, H., and Yanagida, M. (1990). Distinct, essential roles of type 1 and type 2A protein phosphatases in the control of the fission yeast cell division cycle. Cell 63, 405-415.
    • (1990) Cell , vol.63 , pp. 405-415
    • Kinoshita, N.1    Ohkura, H.2    Yanagida, M.3
  • 28
    • 0028911034 scopus 로고
    • A structural basis of the interactions between leucine-rice repeats and protein ligands
    • Kobe, B., and Deisenhofer, J. (1995). A structural basis of the interactions between leucine-rice repeats and protein ligands. Nature 374, 183-186.
    • (1995) Nature , vol.374 , pp. 183-186
    • Kobe, B.1    Deisenhofer, J.2
  • 29
    • 0029889342 scopus 로고    scopus 로고
    • The myeloid leukemiaassociated protein SET is a potent inhibitor of protein phosphatase 2A
    • Li, M., Makkinje, A., and Damuni, Z. (1996). The myeloid leukemiaassociated protein SET is a potent inhibitor of protein phosphatase 2A. J. Biol. Chem. 271, 11059-11062.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11059-11062
    • Li, M.1    Makkinje, A.2    Damuni, Z.3
  • 30
    • 0031470630 scopus 로고    scopus 로고
    • Evolutionary specialization of the nuclear targeting apparatus
    • Malik, H.S., Eickbush, T.H., and Goldfarb, D.S. (1997). Evolutionary specialization of the nuclear targeting apparatus. Proc. Natl. Acad. Sci. USA 94, 13738-13742.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13738-13742
    • Malik, H.S.1    Eickbush, T.H.2    Goldfarb, D.S.3
  • 32
    • 0028832251 scopus 로고
    • Identification of a new family of protein phosphatase 2A regulatory subunits
    • McCright, B., and Virshup, D.M. (1995). Identification of a new family of protein phosphatase 2A regulatory subunits. J. Biol. Chem. 270, 26123-26128.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26123-26128
    • McCright, B.1    Virshup, D.M.2
  • 33
    • 0029834655 scopus 로고    scopus 로고
    • The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm
    • McCright, B., Rivers, A.M., Audliln, S., and Virshup, D.M. (1996). The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm. J. Biol. Chem. 271, 22081-22089.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22081-22089
    • McCright, B.1    Rivers, A.M.2    Audliln, S.3    Virshup, D.M.4
  • 34
    • 0028057108 scopus 로고
    • Raster3D Version 2.0: A program for photorealistic molecular graphics
    • Merit, E.A., and Murphy, M.E.P. (1994). Raster3D Version 2.0: a program for photorealistic molecular graphics. Acta Crystallogr. D50, 869-873.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 869-873
    • Merit, E.A.1    Murphy, M.E.P.2
  • 36
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K., and Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 37
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data in oscillation mode
    • Otwinoski, A., and Minor, W. (1997). Processing of X-ray diffraction data in oscillation mode. Methods Enzymol. 276, 307-325.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-325
    • Otwinoski, A.1    Minor, W.2
  • 38
    • 0025103372 scopus 로고
    • Polyoma small and middle T antigens and SV40 small t antigen form stable complexes with protein phosphatase 2A
    • Pallas, D.C., Shahrik, L.K., Martin, B.L., Jaspers, S., Miller, T.B., Brautigan, D.L, and Roberts, T.M. (1990). Polyoma small and middle T antigens and SV40 small t antigen form stable complexes with protein phosphatase 2A. Cell 60, 167-176.
    • (1990) Cell , vol.60 , pp. 167-176
    • Pallas, D.C.1    Shahrik, L.K.2    Martin, B.L.3    Jaspers, S.4    Miller, T.B.5    Brautigan, D.L.6    Roberts, T.M.7
  • 39
    • 0030909826 scopus 로고    scopus 로고
    • Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution
    • published erratum appears in Science (1997), 276, 21.
    • Park, H.W., Boduluri, S.R., Moomaw, J.F., Casey, P.J., and Beese, L.S. (1997). Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution [published erratum appears in Science (1997), 276, 21]. Science 275, 1800-1804.
    • (1997) Science , vol.275 , pp. 1800-1804
    • Park, H.W.1    Boduluri, S.R.2    Moomaw, J.F.3    Casey, P.J.4    Beese, L.S.5
  • 40
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson, T., and Scott, J.D. (1997). Signaling through scaffold, anchoring, and adaptor proteins. Science 278, 2075-2080.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 41
    • 0024278397 scopus 로고
    • Structure of the lamprey yolk lipid-protein complex lipovitellin-phosvitin at 2.8 ANG resolution
    • Raag, R., Appelt, K., Xuong, N.H., and Banaszak, L. (1988). Structure of the lamprey yolk lipid-protein complex lipovitellin-phosvitin at 2.8 ANG resolution. J. Mol. Biol. 200, 553-570.
    • (1988) J. Mol. Biol. , vol.200 , pp. 553-570
    • Raag, R.1    Appelt, K.2    Xuong, N.H.3    Banaszak, L.4
  • 42
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A42, 140-149.
    • (1986) Acta Crystallogr. , vol.A42 , pp. 140-149
    • Read, R.J.1
  • 43
    • 0026661827 scopus 로고
    • Identification of binding sites on the regulatory A subunit of protein phosphatase 2A for the catalytic C subunit and for tumor antigens of Simian virus 40 and polyomavirus
    • Ruediger, R., Roeckel, D., Fait, J., Bergqvist, A., Magnusson, G., and Walter, G. (1992). Identification of binding sites on the regulatory A subunit of protein phosphatase 2A for the catalytic C subunit and for tumor antigens of Simian virus 40 and polyomavirus. Mol. Cell. Biol. 12, 4872-4882.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4872-4882
    • Ruediger, R.1    Roeckel, D.2    Fait, J.3    Bergqvist, A.4    Magnusson, G.5    Walter, G.6
  • 44
    • 0028082299 scopus 로고
    • Molecular model of the A subunit of protein phosphatase 2A: Interactions with other subunits and tumor antigens
    • Ruediger, R., Hentz, Fait, J., Mumby, M., and Gernot, W. (1994). Molecular model of the A subunit of protein phosphatase 2A: interactions with other subunits and tumor antigens. J. Virol. 68, 123-129.
    • (1994) J. Virol. , vol.68 , pp. 123-129
    • Ruediger, R.1    Hentz, A.2    Fait, J.3    Mumby, M.4    Gernot, W.5
  • 45
    • 0032541623 scopus 로고    scopus 로고
    • Structural basis for inhibition of the cyclin dependent kinase cdk6 by the tumour supporessor p16INK4a
    • Russo, A.A., Tong, L, Lee, J.-O., Jeffrey, P.D., and Pavletich, N.P. (1998). Structural basis for inhibition of the cyclin dependent kinase cdk6 by the tumour supporessor p16INK4a. Nature 395, 237-243.
    • (1998) Nature , vol.395 , pp. 237-243
    • Russo, A.A.1    Tong, L.2    Lee, J.-O.3    Jeffrey, P.D.4    Pavletich, N.P.5
  • 46
    • 0029018031 scopus 로고
    • Neurofilament-associated protein phosphatase 2A: Its possible role in preserving neurofilaments in filamentous states
    • Saito, T., Shima, H., Osawa, Y., Nagao, M., Hemmings, B.A., Kishimoto, T., and Hisanaga, S. (1995). Neurofilament-associated protein phosphatase 2A: its possible role in preserving neurofilaments in filamentous states. Biochemistry 34, 7376-7384.
    • (1995) Biochemistry , vol.34 , pp. 7376-7384
    • Saito, T.1    Shima, H.2    Osawa, Y.3    Nagao, M.4    Hemmings, B.A.5    Kishimoto, T.6    Hisanaga, S.7
  • 47
    • 0030446290 scopus 로고    scopus 로고
    • Deficiency of protein phosphatase 2A uncouples the nuclear and centrosome cycles and prevents attachment of microtubules to the kinetochore in Drosophila microtubule star (mts) embryos
    • Snaith, H.A., Armstrong, C.G., Quo, Y., Kaiser, K., and Cohen, P.T.W. (1996). Deficiency of protein phosphatase 2A uncouples the nuclear and centrosome cycles and prevents attachment of microtubules to the kinetochore in Drosophila microtubule star (mts) embryos. J. Cell Sci. 109, 3001-3012.
    • (1996) J. Cell Sci. , vol.109 , pp. 3001-3012
    • Snaith, H.A.1    Armstrong, C.G.2    Quo, Y.3    Kaiser, K.4    Cohen, P.T.W.5
  • 48
    • 0025647113 scopus 로고
    • Saccharomyces cerevisiae protein phosphatase 2A performs an essential cellular function and is encoded by two genes
    • Sneddon, A.A., Cohen, P.T.W., and Stark, M.J.R. (1990). Saccharomyces cerevisiae protein phosphatase 2A performs an essential cellular function and is encoded by two genes. EMBO J. 9, 4339-4346.
    • (1990) EMBO J. , vol.9 , pp. 4339-4346
    • Sneddon, A.A.1    Cohen, P.T.W.2    Stark, M.J.R.3
  • 49
    • 0027772552 scopus 로고
    • The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the map kinase pathway and induces cell proliferation
    • Sontag, E., Fedorov, S., Kamibayashi, C., Robbins, D., Cobb, M., and Mumby, M. (1993). The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the map kinase pathway and induces cell proliferation. Cell 75, 887-897.
    • (1993) Cell , vol.75 , pp. 887-897
    • Sontag, E.1    Fedorov, S.2    Kamibayashi, C.3    Robbins, D.4    Cobb, M.5    Mumby, M.6
  • 50
    • 0028924295 scopus 로고
    • A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle
    • Sontag, E., Nunbhakdi-Craig, V., Bloom, G.S., and Mumby, M.C. (1995). A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle. J. Cell Biol. 128, 1131-1144.
    • (1995) J. Cell Biol. , vol.128 , pp. 1131-1144
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Bloom, G.S.3    Mumby, M.C.4
  • 51
    • 0030769625 scopus 로고    scopus 로고
    • Protein phosphatase 2A is a critical regulator of protein kinase C zeta signaling targeted by SV40 small t to promote cell growth and NFκB activation
    • Sontag, E., Sontag, J.M., and Garcia, A. (1997). Protein phosphatase 2A is a critical regulator of protein kinase C zeta signaling targeted by SV40 small t to promote cell growth and NFκB activation. EMBO J. 16, 5662-5671.
    • (1997) EMBO J. , vol.16 , pp. 5662-5671
    • Sontag, E.1    Sontag, J.M.2    Garcia, A.3
  • 54
    • 0030874269 scopus 로고    scopus 로고
    • Modulation of the enzymatic properties of protein phosphatase 2A catalytic subunit by the recombinant 65-kDa regulatory subunit PR65-alpha
    • Turowski, P., Favre, B., Campbell, K.S., Lamb, N.J.C., and Hemmings, B.A. (1997). Modulation of the enzymatic properties of protein phosphatase 2A catalytic subunit by the recombinant 65-kDa regulatory subunit PR65-alpha. Eur. J. Biochem. 248, 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
  • 55
    • 0027244764 scopus 로고
    • Protein serine/threonine phosphatases and cell transformation
    • Walter, G., and Mumby, M. (1993). Protein serine/threonine phosphatases and cell transformation. Biochem. Biophys. Acta. 1155, 207-226
    • (1993) Biochem. Biophys. Acta. , vol.1155 , pp. 207-226
    • Walter, G.1    Mumby, M.2
  • 56
    • 0024351652 scopus 로고
    • Molecular cloning and sequence of cDNA encoding polyoma medium tumor antigen-associated 61-kDa protein
    • Walter, G., Ferre, F., Espiritu, O., and Carbone-Wiley, A. (1989) Molecular cloning and sequence of cDNA encoding polyoma medium tumor antigen-associated 61-kDa protein. Proc. Natl. Acad. Sci. USA 86, 8669-8672.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8669-8672
    • Walter, G.1    Ferre, F.2    Espiritu, O.3    Carbone-Wiley, A.4
  • 58
    • 0032523934 scopus 로고    scopus 로고
    • Phosphorylation of spliceosomal protein SAP 155 coupled with splicing catalysis
    • Wang, C., Chua, K., Seghezzi, W., Lees, E., Gozani, and Reed, R. (1998b). Phosphorylation of spliceosomal protein SAP 155 coupled with splicing catalysis. Genes Dev. 12, 1409-1414.
    • (1998) Genes Dev. , vol.12 , pp. 1409-1414
    • Wang, C.1    Chua, K.2    Seghezzi, W.3    Lees, E.4    Gozani5    Reed, R.6
  • 59
    • 0029129557 scopus 로고
    • Serine/threonine protein phosphatases
    • Wera, S., and Hemmings, B.A. (1995). Serine/threonine protein phosphatases. Biochem. J. 311, 17-29.
    • (1995) Biochem. J. , vol.311 , pp. 17-29
    • Wera, S.1    Hemmings, B.A.2
  • 60
    • 0029153084 scopus 로고
    • Deregulation of translational control of the 65-kDa regulatory subunit (PR65α) of protein phosphatase 2A leads to multinucleated cells
    • Wera, S., Fernandez, A., Lamb, N.J.C., Turowski, P., Hemmings-Mieszczak, M., Mayer-Jaeckel, R.E., and Hemmings, B.A. (1995). Deregulation of translational control of the 65-kDa regulatory subunit (PR65α) of protein phosphatase 2A leads to multinucleated cells. J. Biol. Chem. 270, 21374-21381.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21374-21381
    • Wera, S.1    Fernandez, A.2    Lamb, N.J.C.3    Turowski, P.4    Hemmings-Mieszczak, M.5    Mayer-Jaeckel, R.E.6    Hemmings, B.A.7
  • 61
    • 0032508714 scopus 로고    scopus 로고
    • A mammalian scaffold complex that selectively mediates MAP kinase activation
    • Whitmarsh, A.J., Cavangh, J., Tiurnier, C., Yasuda, J., and Davis, R. J. (1998). A mammalian scaffold complex that selectively mediates MAP kinase activation. Science 281, 1671-1674.
    • (1998) Science , vol.281 , pp. 1671-1674
    • Whitmarsh, A.J.1    Cavangh, J.2    Tiurnier, C.3    Yasuda, J.4    Davis, R.J.5
  • 62
    • 0030991668 scopus 로고    scopus 로고
    • Saccharomyces cerevisae homologs of mammalian B and B′ subunits of protein phosphatase 2A direct the enzyme to distinct cellular functions
    • Zhao, Y., Boguslawski, G., Zitomer, R.S., and DePaoli-Roach, A.A. (1997). Saccharomyces cerevisae homologs of mammalian B and B′ subunits of protein phosphatase 2A direct the enzyme to distinct cellular functions. J. Biol. Chem. 272, 8256-8262.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8256-8262
    • Zhao, Y.1    Boguslawski, G.2    Zitomer, R.S.3    DePaoli-Roach, A.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.