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1
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85031643208
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Special kinase projects on World Wide Web URL A web site maintained by the biopharmaceutical company Sugen that contains useful tables of kinases, phosphatases and signaling molecules from a variety of organisms
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Special kinase projects on World Wide Web URL: http://www.kinase.com A web site maintained by the biopharmaceutical company Sugen that contains useful tables of kinases, phosphatases and signaling molecules from a variety of organisms.
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2
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0025895590
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Constant expression and activity of protein phosphatase 2A in synchronized cells
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Ruediger R., van wart Hood J.E., Mumby M., Walter G. Constant expression and activity of protein phosphatase 2A in synchronized cells. Mol Cell Biol. 11:1991;4282-4285.
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(1991)
Mol Cell Biol
, vol.11
, pp. 4282-4285
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Ruediger, R.1
Van Wart Hood, J.E.2
Mumby, M.3
Walter, G.4
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3
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0032411638
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Protein phosphatase 2A is required for the initiation of chromosomal DNA replication
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Immunodeletion of PP2A heterotrimers from Xenopus egg extracts blocks initiation of chromosomal DNA replication, providing strong biochemical evidence for a critical function of PP2A.
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Lin X.H., Walter J., Scheidtmann K., Ohst K., Newport J., Walter G. Protein phosphatase 2A is required for the initiation of chromosomal DNA replication. Proc Natl Acad Sci USA. 95:1998;14693-14698. Immunodeletion of PP2A heterotrimers from Xenopus egg extracts blocks initiation of chromosomal DNA replication, providing strong biochemical evidence for a critical function of PP2A.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 14693-14698
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Lin, X.H.1
Walter, J.2
Scheidtmann, K.3
Ohst, K.4
Newport, J.5
Walter, G.6
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5
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0032946279
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Protein phosphatase 2A: Who shall regulate the regulator?
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Goldberg Y. Protein phosphatase 2A: who shall regulate the regulator? Biochem Pharmacol. 57:1999;321-328.
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(1999)
Biochem Pharmacol
, vol.57
, pp. 321-328
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Goldberg, Y.1
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6
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0033553570
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A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A
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Ogris E., Du X., Nelson K.C., Mak E.K., Yu X.X., Lane W.S., Pallas D.L. A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A. J Biol Chem. 274:1999;14382-14391.
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(1999)
J Biol Chem
, vol.274
, pp. 14382-14391
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Ogris, E.1
Du, X.2
Nelson, K.C.3
Mak, E.K.4
Yu, X.X.5
Lane, W.S.6
Pallas, D.L.7
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7
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0033560729
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Methylated C-terminal leucine residue of PP2A catalytic subunit is important for binding of regulatory Bα subunit
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Bryant J.C., Westphal R.S., Wadzinski B.E. Methylated C-terminal leucine residue of PP2A catalytic subunit is important for binding of regulatory Bα subunit. Biochem J. 339:1999;241-246.
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(1999)
Biochem J
, vol.339
, pp. 241-246
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Bryant, J.C.1
Westphal, R.S.2
Wadzinski, B.E.3
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8
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0033615004
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Association between src-kinases and the polyoma virus oncogene middle T-antigen requires PP2A and a specific sequence motif
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Glover H.R., Brewster C.E., Dilworth S.M. Association between src-kinases and the polyoma virus oncogene middle T-antigen requires PP2A and a specific sequence motif. Oncogene. 18:1999;4364-4370.
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(1999)
Oncogene
, vol.18
, pp. 4364-4370
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Glover, H.R.1
Brewster, C.E.2
Dilworth, S.M.3
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9
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0032865617
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Catalytically inactive protein phosphatase 2A can bind to polyomavirus middle tumor antigen and support complex formation with pp60(c-src)
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Ogris E., Mudrak I., Mak E., Gibson D., Pallas D.C. Catalytically inactive protein phosphatase 2A can bind to polyomavirus middle tumor antigen and support complex formation with pp60(c-src). J Virol. 73:1999;7390-7398.
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(1999)
J Virol
, vol.73
, pp. 7390-7398
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Ogris, E.1
Mudrak, I.2
Mak, E.3
Gibson, D.4
Pallas, D.C.5
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10
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0032567536
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Identification of structural elements involved in the interaction of simian virus 40 small tumor antigen with protein phosphatase 2A
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Mateer S.C., Fedorov S.A., Mumby M.C. Identification of structural elements involved in the interaction of simian virus 40 small tumor antigen with protein phosphatase 2A. J Biol Chem. 273:1998;35339-35346.
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(1998)
J Biol Chem
, vol.273
, pp. 35339-35346
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Mateer, S.C.1
Fedorov, S.A.2
Mumby, M.C.3
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11
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0031784937
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Signaling from polyomavirus middle T and small T defines different roles for protein phosphatase 2A
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Mullane K.P., Ratnofsky M., Cullere X., Schaffhausen B. Signaling from polyomavirus middle T and small T defines different roles for protein phosphatase 2A. Mol Cell Biol. 18:1998;7556-7564.
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(1998)
Mol Cell Biol
, vol.18
, pp. 7556-7564
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Mullane, K.P.1
Ratnofsky, M.2
Cullere, X.3
Schaffhausen, B.4
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12
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0033531933
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Regulation of protein phosphatase 2A activity by heat shock transcription factor 2
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This paper presents the unexpected finding that a transcription factor can bind to the subunit A of PP2A subunit in place of the C subunit. Does cellular stress regulate PP2A composition and activity?
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Hong Y., Sarge K.D. Regulation of protein phosphatase 2A activity by heat shock transcription factor 2. J Biol Chem. 274:1999;12967-12970. This paper presents the unexpected finding that a transcription factor can bind to the subunit A of PP2A subunit in place of the C subunit. Does cellular stress regulate PP2A composition and activity?
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(1999)
J Biol Chem
, vol.274
, pp. 12967-12970
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Hong, Y.1
Sarge, K.D.2
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13
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0032978487
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Vimentin dephosphorylation by protein phosphatase 2A is modulated by the targeting subunit B55
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A fraction of regulatory subunit B55 associates with vimentin and targets PP2A heterotrimers to the cytoskeleton; these data indicate that dynamic dephosphorylation of vimentin by PP2A maintains intermediate filament integrity.
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Turowski P., Myles T., Hemmings B.A., Fernandez A., Lamb N.J. Vimentin dephosphorylation by protein phosphatase 2A is modulated by the targeting subunit B55. Mol Biol Cell. 10:1999;1997-2015. A fraction of regulatory subunit B55 associates with vimentin and targets PP2A heterotrimers to the cytoskeleton; these data indicate that dynamic dephosphorylation of vimentin by PP2A maintains intermediate filament integrity.
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(1999)
Mol Biol Cell
, vol.10
, pp. 1997-2015
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Turowski, P.1
Myles, T.2
Hemmings, B.A.3
Fernandez, A.4
Lamb, N.J.5
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14
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0026661827
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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
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Ruediger R., Roeckel D., Fait J., Bergqvist A., Magnusson G., Walter G. 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. 12:1992;4872-4882.
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(1992)
Mol Cell Biol
, vol.12
, pp. 4872-4882
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Ruediger, R.1
Roeckel, D.2
Fait, J.3
Bergqvist, A.4
Magnusson, G.5
Walter, G.6
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15
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0028082299
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Molecular model of the A subunit of protein phosphatase 2A: Interaction with other subunits and tumor antigens
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Ruediger R., Hentz M., Fait J., Mumby M., Walter G. Molecular model of the A subunit of protein phosphatase 2A: interaction with other subunits and tumor antigens. J Virol. 68:1994;123-129.
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(1994)
J Virol
, vol.68
, pp. 123-129
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Ruediger, R.1
Hentz, M.2
Fait, J.3
Mumby, M.4
Walter, G.5
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16
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0032889238
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Binding specificity of protein phosphatase 2A core enzyme for regulatory B subunits and T antigens
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Ruediger R., Fields K., Walter G. Binding specificity of protein phosphatase 2A core enzyme for regulatory B subunits and T antigens. J Virol. 73:1999;839-842.
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(1999)
J Virol
, vol.73
, pp. 839-842
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Ruediger, R.1
Fields, K.2
Walter, G.3
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17
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0033534405
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The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs
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The crystal structure of the PP2A A subunit is presented; it forms a hook with a conserved inner face that probably brings the B and C subunits close together.
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Groves M.R., Hanlon N., Turowski P., Hemmings B.A., Barford D. The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs. Cell. 96:1999;99-110. The crystal structure of the PP2A A subunit is presented; it forms a hook with a conserved inner face that probably brings the B and C subunits close together.
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(1999)
Cell
, vol.96
, pp. 99-110
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Groves, M.R.1
Hanlon, N.2
Turowski, P.3
Hemmings, B.A.4
Barford, D.5
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18
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0028276611
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Different oligomeric forms of protein phosphatase 2A activate and inhibit simian virus 40 DNA replication
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Cegielska A., Shaffer S., Derua R., Goris J., Virshup D.M. Different oligomeric forms of protein phosphatase 2A activate and inhibit simian virus 40 DNA replication. Mol Cell Biol. 14:1994;4616-4623.
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(1994)
Mol Cell Biol
, vol.14
, pp. 4616-4623
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Cegielska, A.1
Shaffer, S.2
Derua, R.3
Goris, J.4
Virshup, D.M.5
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19
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0030874269
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Modulation of the enzymatic properties of protein phosphatase 2A catalytic subunit by the recombinant 65-kDa regulatory subunit PR65α
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Turowski P., Favre B., Campbell K.S., Lamb N.J., 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.
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(1997)
Eur J Biochem
, vol.248
, pp. 200-208
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Turowski, P.1
Favre, B.2
Campbell, K.S.3
Lamb, N.J.4
Hemmings, B.A.5
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20
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0032500792
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Alterations of the PPP2R1B gene in human lung and colon cancer
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The β isoform of the A subunit gene is altered in a fraction of human tumors; however, more work needs to be done to prove it is truly a tumor suppressor.
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Wang S.S., Esplin E.D., Li J.L., Huang L., Gazdar A., Minna J., Evans G.A. Alterations of the PPP2R1B gene in human lung and colon cancer. Science. 282:1998;284-287. The β isoform of the A subunit gene is altered in a fraction of human tumors; however, more work needs to be done to prove it is truly a tumor suppressor.
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(1998)
Science
, vol.282
, pp. 284-287
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Wang, S.S.1
Esplin, E.D.2
Li, J.L.3
Huang, L.4
Gazdar, A.5
Minna, J.6
Evans, G.A.7
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21
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0025103372
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Polyoma small and middle T antigens and SV40 small E antigens form stable complexes with protein phosphatase 2A
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Polkis D.C., Shahrik L.K., Martin E.L., Jaspers S., Miller T.E., Brautigan D.L., Roberts T.M. Polyoma small and middle T antigens and SV40 small E antigens form stable complexes with protein phosphatase 2A. Cell. 60:1990;167-176.
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(1990)
Cell
, vol.60
, pp. 167-176
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Polkis, D.C.1
Shahrik, L.K.2
Martin, E.L.3
Jaspers, S.4
Miller, T.E.5
Brautigan, D.L.6
Roberts, T.M.7
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22
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0025366151
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Association of protein phosphatase 2A with polyomer virus medium tumor antigen
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Walter G., Ruediger R., Slaughter C., Mumby M. Association of protein phosphatase 2A with polyomer virus medium tumor antigen. Proc Natl Acad Sci USA. 87:1990;2521-2525.
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(1990)
Proc Natl Acad Sci USA
, vol.87
, pp. 2521-2525
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Walter, G.1
Ruediger, R.2
Slaughter, C.3
Mumby, M.4
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23
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0031031397
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HOX11 interacts with protein phosphatases PP2A and PP1 and disrupts a G2/M cell-cycle checkpoint
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Kawabe T., Muslin A.J., Korsmeyer S.J. HOX11 interacts with protein phosphatases PP2A and PP1 and disrupts a G2/M cell-cycle checkpoint. Nature. 385:1997;454-458.
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(1997)
Nature
, vol.385
, pp. 454-458
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Kawabe, T.1
Muslin, A.J.2
Korsmeyer, S.J.3
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24
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0029889342
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The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A
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Li M., Makkinje A., Damuni Z. The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A. J Biol Chem. 271:1996;11059-11062.
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(1996)
J Biol Chem
, vol.271
, pp. 11059-11062
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Li, M.1
Makkinje, A.2
Damuni, Z.3
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25
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0033565895
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Expression of I2PP2A, an inhibitor of protein phosphatase 2A, induces c-Jun and AP-1 activity
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Al-Murrani S.W., Woodgett J.R., Damuni Z. Expression of I2PP2A, an inhibitor of protein phosphatase 2A, induces c-Jun and AP-1 activity. Biochem J. 341:1999;293-298.
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(1999)
Biochem J
, vol.341
, pp. 293-298
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Al-Murrani, S.W.1
Woodgett, J.R.2
Damuni, Z.3
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26
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0345517990
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Reduction of Ha-ras-induced cellular transformation by elevated expression of protein phosphatase type 2A
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Baharians Z., Schonthal A.H. Reduction of Ha-ras-induced cellular transformation by elevated expression of protein phosphatase type 2A. Mol Carcinog. 24:1999;246-254.
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(1999)
Mol Carcinog
, vol.24
, pp. 246-254
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Baharians, Z.1
Schonthal, A.H.2
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27
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0028931302
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Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney
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Li M., Guo H., Damuni Z. Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney. Biochemistry. 34:1995;1988-1996.
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(1995)
Biochemistry
, vol.34
, pp. 1988-1996
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Li, M.1
Guo, H.2
Damuni, Z.3
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28
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0033054167
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Modulation of oncogenic potential by alternative gene use in human prostate cancer
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1PP2A) are expressed in normal and cancerous prostate tissue, suggesting alterations in PP2A regulation during malignant transformation.
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1PP2A) are expressed in normal and cancerous prostate tissue, suggesting alterations in PP2A regulation during malignant transformation.
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(1999)
Nat Med
, vol.5
, pp. 275-279
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Kadkol, S.S.1
Brody, J.R.2
Pevsner, J.3
Bai, J.4
Pasternack, G.R.5
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29
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0032054828
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Wnt signaling: Why is everything so negative?
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Brown J.D., Moon R.T. Wnt signaling: why is everything so negative? Curr Opin Cell Biol. 10:1998;182-187.
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(1998)
Curr Opin Cell Biol
, vol.10
, pp. 182-187
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Brown, J.D.1
Moon, R.T.2
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30
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0033605639
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Regulation of beta-catenin signaling by the B56 subunit of protein phosphatase 2A
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Body axis formation and epithelial proliferation can be regulated by targeting PP2A to the adenomatous polyposis coli protein and its associated signaling molecules.
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Seeling J.M., Miller J.R., Gil R., Moon R.T., White R., Virshup D.M. Regulation of beta-catenin signaling by the B56 subunit of protein phosphatase 2A. Science. 283:1999;2089-2091. Body axis formation and epithelial proliferation can be regulated by targeting PP2A to the adenomatous polyposis coli protein and its associated signaling molecules.
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(1999)
Science
, vol.283
, pp. 2089-2091
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Seeling, J.M.1
Miller, J.R.2
Gil, R.3
Moon, R.T.4
White, R.5
Virshup, D.M.6
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31
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0033524929
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Identification of a domain of axin that binds to the serine/threonine Protein Phosphatase 2A and a self-binding domain
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This paper identifies the PP2A catalytic subunit as an axin-interacting protein, supporting other studies that put PP2A in the WNT signaling pathway.
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Hsu W., Zeng L., Costantini F. Identification of a domain of axin that binds to the serine/threonine Protein Phosphatase 2A and a self-binding domain. J Biol Chem. 274:1999;3439-3445. This paper identifies the PP2A catalytic subunit as an axin-interacting protein, supporting other studies that put PP2A in the WNT signaling pathway.
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(1999)
J Biol Chem
, vol.274
, pp. 3439-3445
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Hsu, W.1
Zeng, L.2
Costantini, F.3
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32
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0033577808
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Domains of axin involved in protein-protein interactions, Wnt pathway inhibition, and intracellular localization
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Structure/function analysis of axin shows that domains that interact with β-catenin and PP2Ac are not always essential for the down-regulation of signaling.
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Fagotto F., Jho E., Zeng L., Kurth T., Joos T., Kaufmann C., Costantini F. Domains of axin involved in protein-protein interactions, Wnt pathway inhibition, and intracellular localization. J Cell Biol. 145:1999;741-756. Structure/function analysis of axin shows that domains that interact with β-catenin and PP2Ac are not always essential for the down-regulation of signaling.
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(1999)
J Cell Biol
, vol.145
, pp. 741-756
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Fagotto, F.1
Jho, E.2
Zeng, L.3
Kurth, T.4
Joos, T.5
Kaufmann, C.6
Costantini, F.7
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33
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0033565533
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Wnt-induced dephosphorylation of axin releases beta-catenin from the axin complex
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Willert K., Shibamoto S., Nusse R. Wnt-induced dephosphorylation of axin releases beta-catenin from the axin complex. Genes Dev. 13:1999;1768-1773.
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(1999)
Genes Dev
, vol.13
, pp. 1768-1773
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Willert, K.1
Shibamoto, S.2
Nusse, R.3
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34
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0005125709
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Purification of replication protein C, a cellular protein involved in the initial stages of SV40 DNA replication in vitro
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Virshup D.M., Kelly T.J. Purification of replication protein C, a cellular protein involved in the initial stages of SV40 DNA replication in vitro. Proc Natl Acad Sci USA. 86:1989;3584-3588.
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(1989)
Proc Natl Acad Sci USA
, vol.86
, pp. 3584-3588
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Virshup, D.M.1
Kelly, T.J.2
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35
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0024833601
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Activation of SV40 DNA replication in vitro by cellular protein phosphatase 2A
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Virshup D.M., Kauffman M.G., Kelly T.J. Activation of SV40 DNA replication in vitro by cellular protein phosphatase 2A. EMBO J. 8:1989;3891-3898.
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(1989)
EMBO J
, vol.8
, pp. 3891-3898
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Virshup, D.M.1
Kauffman, M.G.2
Kelly, T.J.3
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36
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0033972224
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PR48, a novel regulatory subunit of PP2A, interacts with Cdc6 and modulates DNA replication in human cells
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in press
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Yan Z., Fedorov S.A., Mumby M.C., Williams R.S. PR48, a novel regulatory subunit of PP2A, interacts with Cdc6 and modulates DNA replication in human cells. Mol Cell Biol. 2000;. in press.
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(2000)
Mol Cell Biol
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Yan, Z.1
Fedorov, S.A.2
Mumby, M.C.3
Williams, R.S.4
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37
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0033552957
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Functional interaction between a novel protein phosphatase 2A regulatory subunit, PR59, and the retinoblastoma-related p107 protein
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The authors identify a novel PR72-related B subunit PR59 in a two-hybrid screen using the retinoblastoma related p107 protein as a bait. PR59 may recruit PP2A to dephosphorylate p107 and contribute to cell-cycle arrest.
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Voorhoeve P.M., Hijmans E.M., Bernards R. Functional interaction between a novel protein phosphatase 2A regulatory subunit, PR59, and the retinoblastoma-related p107 protein. Oncogene. 18:1999;515-524. The authors identify a novel PR72-related B subunit PR59 in a two-hybrid screen using the retinoblastoma related p107 protein as a bait. PR59 may recruit PP2A to dephosphorylate p107 and contribute to cell-cycle arrest.
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(1999)
Oncogene
, vol.18
, pp. 515-524
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Voorhoeve, P.M.1
Hijmans, E.M.2
Bernards, R.3
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38
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0033590629
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Rapid dephosphorylation of p107 following UV irradiation
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Voorhoeve P.M., Watson R.J., Farlie P.G., Bernards R., Lam E.W. Rapid dephosphorylation of p107 following UV irradiation. Oncogene. 18:1999;679-688.
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(1999)
Oncogene
, vol.18
, pp. 679-688
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Voorhoeve, P.M.1
Watson, R.J.2
Farlie, P.G.3
Bernards, R.4
Lam, E.W.5
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39
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0033153166
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Regulation of 4E-BP1 phosphorylation: A novel two-step mechanism
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Gingras A.C., Gygi S.P., Raught B., Polakiewicz R.D., Abraham R.T., Hoekstra M.F., Aebersold R., Sonenberg N. Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism. Genes Dev. 13:1999;1422-1437.
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(1999)
Genes Dev
, vol.13
, pp. 1422-1437
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Gingras, A.C.1
Gygi, S.P.2
Raught, B.3
Polakiewicz, R.D.4
Abraham, R.T.5
Hoekstra, M.F.6
Aebersold, R.7
Sonenberg, N.8
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40
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0029808294
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Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases
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Di Como C.J., Arndt K.T. Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases. Genes Dev. 10:1996;1904-1916.
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(1996)
Genes Dev
, vol.10
, pp. 1904-1916
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Di Como, C.J.1
Arndt, K.T.2
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41
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0033577745
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Tor proteins and protein phosphatase 2A reciprocally regulate Tap42 in controlling cell growth in yeast
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c; dephosphorylation of Tap42 by the CDC55-containing PP2A heterotrimer leads to dissociation of the complex.
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c; dephosphorylation of Tap42 by the CDC55-containing PP2A heterotrimer leads to dissociation of the complex.
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(1999)
EMBO J
, vol.18
, pp. 2782-2792
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Jiang, Y.1
Broach, J.R.2
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42
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0030984108
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B cell receptor-associated protein α4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A
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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.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 10624-10629
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Murata, K.1
Wu, J.2
Brautigan, D.L.3
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43
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0032577919
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Alpha 4 associates with protein phosphatases 2A, 4, and 6
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Chen J., Peterson R.T., Schreiber S.L. Alpha 4 associates with protein phosphatases 2A, 4, and 6. Biochem Biophys Res Commun. 247:1998;827-832.
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(1998)
Biochem Biophys Res Commun
, vol.247
, pp. 827-832
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Chen, J.1
Peterson, R.T.2
Schreiber, S.L.3
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44
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0032528434
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Ig receptor binding protein 1 (α4) is associated with a rapamycin-sensitive signal transduction in lymphocytes through direct binding to the catalytic subunit of protein phosphatase 2A
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Inui S., Sanjo H., Maeda K., Yamamoto H., Miyamoto E., Sakaguchi N. Ig receptor binding protein 1 (α4) is associated with a rapamycin-sensitive signal transduction in lymphocytes through direct binding to the catalytic subunit of protein phosphatase 2A. Blood. 92:1998;539-546.
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(1998)
Blood
, vol.92
, pp. 539-546
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Inui, S.1
Sanjo, H.2
Maeda, K.3
Yamamoto, H.4
Miyamoto, E.5
Sakaguchi, N.6
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45
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0031457622
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Signaling through scaffold, anchoring, and adaptor proteins
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Pawson T., Scott J.D. Signaling through scaffold, anchoring, and adaptor proteins. Science. 278:1997;2075-2080.
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Science
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Pawson, T.1
Scott, J.D.2
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46
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0032557245
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2+-calmodulin-dependent protein kinase IV and protein phosphatase 2A
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The authors show that PP2A binds to CamKIV, dephosphorylating and inactivating. Mechanisms that decrease phosphatase activity increase sensitivity to calcium signaling. This is an important example of PP2A in a signaling complex.
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2+-calmodulin-dependent protein kinase IV and protein phosphatase 2A. Science. 280:1998;1258-1261. The authors show that PP2A binds to CamKIV, dephosphorylating and inactivating. Mechanisms that decrease phosphatase activity increase sensitivity to calcium signaling. This is an important example of PP2A in a signaling complex.
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(1998)
Science
, vol.280
, pp. 1258-1261
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Westphal, R.S.1
Anderson, K.A.2
Means, A.R.3
Wadzinski, B.E.4
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47
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0033534615
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Identification of kinase-phosphatase signaling modules composed of p70 S6 kinase-protein phosphatase 2A (PP2A) and p21-activated kinase-PP2A
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PP2A is found in high-molecular complexes that contain both phosphatase and kinase activity. These complexes probably represent signaling structures with both on and off switches.
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Westphal R.S., Coffee R.L. Jr., Marotta A., Pelech S.L., Wadzinski B.E. Identification of kinase-phosphatase signaling modules composed of p70 S6 kinase-protein phosphatase 2A (PP2A) and p21-activated kinase-PP2A. J Biol Chem. 274:1999;687-692. PP2A is found in high-molecular complexes that contain both phosphatase and kinase activity. These complexes probably represent signaling structures with both on and off switches.
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(1999)
J Biol Chem
, vol.274
, pp. 687-692
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Westphal, R.S.1
Coffee R.L., Jr.2
Marotta, A.3
Pelech, S.L.4
Wadzinski, B.E.5
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48
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0030979386
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Regulation of protein phosphatase 2A by direct interaction with casein kinase 2alpha
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Heriche J.K., Lebrin F., Rabilloud T., Leroy D., Chambaz E.M., Goldberg Y. Regulation of protein phosphatase 2A by direct interaction with casein kinase 2alpha. Science. 276:1997;952-955.
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Science
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Heriche, J.K.1
Lebrin, F.2
Rabilloud, T.3
Leroy, D.4
Chambaz, E.M.5
Goldberg, Y.6
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49
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0027360098
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Adenovirus E4orf4 protein binds to protein phosphatase 2A and the complex down regulates E1A-enhanced junB transcription
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Kleinberger T., Shenk T. Adenovirus E4orf4 protein binds to protein phosphatase 2A and the complex down regulates E1A-enhanced junB transcription. J Virol. 67:1994;7556-7560.
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(1994)
J Virol
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Kleinberger, T.1
Shenk, T.2
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50
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0033621057
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Induction of apoptosis by adenovirus E4orf4 protein is specific to transformed cells and requires an interaction with protein phosphatase 2A
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Shtrichman R., Sharf R., Barr H., Dobner T., Kleinberger T. Induction of apoptosis by adenovirus E4orf4 protein is specific to transformed cells and requires an interaction with protein phosphatase 2A. Proc Natl Acad Sci USA. 96:1999;10080-10085.
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(1999)
Proc Natl Acad Sci USA
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Shtrichman, R.1
Sharf, R.2
Barr, H.3
Dobner, T.4
Kleinberger, T.5
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51
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0343457526
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Reversible phosphorylation of Bcl2, following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A
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Deng X., Ito T., Carr B., Mumby M., May W.S. Jr. Reversible phosphorylation of Bcl2, following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A. J Biol Chem. 273:1998;34157-34163.
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J Biol Chem
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Deng, X.1
Ito, T.2
Carr, B.3
Mumby, M.4
May W.S., Jr.5
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52
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0033575320
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Ceramide induces Bcl2 dephosphorylation via a mechanism involving mitochondrial PP2A
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Ruvolo P.P., Deng X., Ito T., Carr B.K., May W.S. Ceramide induces Bcl2 dephosphorylation via a mechanism involving mitochondrial PP2A. J Biol Chem. 274:1999;20296-20300.
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(1999)
J Biol Chem
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Ruvolo, P.P.1
Deng, X.2
Ito, T.3
Carr, B.K.4
May, W.S.5
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53
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0033523983
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Absence of PPP2R1B gene alterations in primary ovarian cancers
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Although loss of heterozygosity at the PP2A Aβ gene locus was common, one common polymorphism and no inactivating mutations were detected in 76 ovarian tumors. The authors caution that PPP2R1B may not be a tumor suppressor gene.
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Campbell I.G., Manolitsas T. Absence of PPP2R1B gene alterations in primary ovarian cancers. Oncogene. 18:1999;6367-6369. Although loss of heterozygosity at the PP2A Aβ gene locus was common, one common polymorphism and no inactivating mutations were detected in 76 ovarian tumors. The authors caution that PPP2R1B may not be a tumor suppressor gene.
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(1999)
Oncogene
, vol.18
, pp. 6367-6369
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Campbell, I.G.1
Manolitsas, T.2
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