메뉴 건너뛰기




Volumn 105, Issue 5, 2008, Pages 2029-2038

Activation of brain protein phosphatase-1I following cardiac arrest and resuscitation involving an interaction with 14-3-3γ

Author keywords

Apoptosis; Inhibitor 2; Protein phosphorylation

Indexed keywords

PHOSPHOPROTEIN PHOSPHATASE 1; TRANSFORMING GROWTH FACTOR BETA ACTIVATED KINASE 1;

EID: 43549119524     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2008.05300.x     Document Type: Article
Times cited : (6)

References (64)
  • 1
    • 0035968240 scopus 로고    scopus 로고
    • Neuronal Cdc-2-like protein kinase (Cdk5/p25) is associated with protein phosphatase-1 and phosphorylates inhibitor-2
    • Agarwal-Mawal A. Paudel H. K. (2001) Neuronal Cdc-2-like protein kinase (Cdk5/p25) is associated with protein phosphatase-1 and phosphorylates inhibitor-2. J. Biol. Chem. 276, 23712 23718.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23712-23718
    • Agarwal-Mawal, A.1    Paudel, H.K.2
  • 2
    • 0026668149 scopus 로고
    • 2+/calmodulin-dependent protein kinase II: Potential role in neuronal damage
    • 2+/calmodulin-dependent protein kinase II: potential role in neuronal damage. J. Neurochem. 58, 1743 1753.
    • (1992) J. Neurochem. , vol.58 , pp. 1743-1753
    • Aronowski, J.1    Grotto, J.C.2    Waxhan, M.N.3
  • 5
    • 0030697998 scopus 로고    scopus 로고
    • Interaction of phosphorylated tryptophan hydroxylase with 14-3-3 proteins
    • Banik U., Wang G.-A., Wagner P. D. Kaufman S. (1997) Interaction of phosphorylated tryptophan hydroxylase with 14-3-3 proteins. J. Biol. Chem. 272, 26219 26225.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26219-26225
    • Banik, U.1    Wang, G.-A.2    Wagner, P.D.3    Kaufman, S.4
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford A. A. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 76, 248 254.
    • (1976) Anal. Biochem. , vol.76 , pp. 248-254
    • Bradford, A.A.1
  • 10
    • 0019551730 scopus 로고
    • "western blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified cellulose and radiographic detection with antibody and radioiodinated protein a
    • Burnette W. N. (1981) "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified cellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112, 195 203.
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 11
    • 0023887866 scopus 로고
    • Oxygen free radical involvement in ischemia and reperfusion injury to brain
    • Cao W., Carney J. M., Duchon A., Floyd R. A. Chevion M. (1988) Oxygen free radical involvement in ischemia and reperfusion injury to brain. Neurosci. Lett. 88, 233 238.
    • (1988) Neurosci. Lett. , vol.88 , pp. 233-238
    • Cao, W.1    Carney, J.M.2    Duchon, A.3    Floyd, R.A.4    Chevion, M.5
  • 12
    • 0035149749 scopus 로고    scopus 로고
    • Reactive oxygen radicals in signaling and damage in the ischemic brain
    • Chan P. H. (2001) Reactive oxygen radicals in signaling and damage in the ischemic brain. J. Cereb. Blood Flow Metab. 21, 2 14.
    • (2001) J. Cereb. Blood Flow Metab. , vol.21 , pp. 2-14
    • Chan, P.H.1
  • 13
    • 4644317330 scopus 로고    scopus 로고
    • Inhibitors of protein phosphatase 1 and 2A differentially prevent intrinsic and extrinsic apoptosis pathways
    • Chatfield K. Eastman A. (2004) Inhibitors of protein phosphatase 1 and 2A differentially prevent intrinsic and extrinsic apoptosis pathways. Biochem. Biophys. Res. Commun. 323, 1313 1320.
    • (2004) Biochem. Biophys. Res. Commun. , vol.323 , pp. 1313-1320
    • Chatfield, K.1    Eastman, A.2
  • 14
    • 0028241170 scopus 로고
    • 14-3-3 proteins bind histone and affect both histone phosphorylation and dephosphorylation
    • Chen F. Wagner P. D. (1994) 14-3-3 proteins bind histone and affect both histone phosphorylation and dephosphorylation. FEBS Lett. 347, 128 132.
    • (1994) FEBS Lett. , vol.347 , pp. 128-132
    • Chen, F.1    Wagner, P.D.2
  • 15
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen P. (1989) The structure and regulation of protein phosphatases. Annu. Rev. Biochem. 58, 453 508.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 453-508
    • Cohen, P.1
  • 17
    • 0038060334 scopus 로고    scopus 로고
    • Ischemic tolerance and endogenous neuroprotection
    • Dirnagl U., Simon R. P. Hallenbeck J. M. (2003) Ischemic tolerance and endogenous neuroprotection. Trends Neurosci. 26, 248 254.
    • (2003) Trends Neurosci. , vol.26 , pp. 248-254
    • Dirnagl, U.1    Simon, R.P.2    Hallenbeck, J.M.3
  • 18
    • 0037287068 scopus 로고    scopus 로고
    • CaM kinase IIδ phosphorylation of 14-3-3b in vascular smooth muscle cells: Activation of class II HDAC repression
    • Ellis J. J., Valencia T. G., Zeng H., Roberts L. D., Deaton R. A. Grant S. R. (2003) CaM kinase IIδ phosphorylation of 14-3-3b in vascular smooth muscle cells: activation of class II HDAC repression. Mol. Cell. Biochem. 242, 153 161.
    • (2003) Mol. Cell. Biochem. , vol.242 , pp. 153-161
    • Ellis, J.J.1    Valencia, T.G.2    Zeng, H.3    Roberts, L.D.4    Deaton, R.A.5    Grant, S.R.6
  • 20
    • 0035798093 scopus 로고    scopus 로고
    • The neurobiology of slow synaptic transmission
    • Greengard P. (2001) The neurobiology of slow synaptic transmission. Science 294, 1024 1038.
    • (2001) Science , vol.294 , pp. 1024-1038
    • Greengard, P.1
  • 21
    • 0029040992 scopus 로고
    • A specific inhibitor of calcium/calmodulin-dependent protein kinase-II provides neuroprotection against NMDA- and hypoxia/hypoglycemia-induced cell death
    • Hajimohammaddreza L., Probert A. W., Coughenour L. L., Borosky S. A., Marcoux F. W., Boxer P. A. Wang K. K. W. (1995) A specific inhibitor of calcium/calmodulin-dependent protein kinase-II provides neuroprotection against NMDA- and hypoxia/hypoglycemia-induced cell death. J. Neurosci. 15, 4093 4101.
    • (1995) J. Neurosci. , vol.15 , pp. 4093-4101
    • Hajimohammaddreza, L.1    Probert, A.W.2    Coughenour, L.L.3    Borosky, S.A.4    Marcoux, F.W.5    Boxer, P.A.6    Wang, K.K.W.7
  • 22
    • 16744365194 scopus 로고    scopus 로고
    • Sphingosine-dependent protein kinase-1, directed to 14-3-3, is identified as the kinase domain of protein kinase Cδ
    • Hamaguchi A., Suzuki E., Murayama K. et al. (2003) Sphingosine-dependent protein kinase-1, directed to 14-3-3, is identified as the kinase domain of protein kinase Cδ. J. Biol. Chem. 278, 41557 41565.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41557-41565
    • Hamaguchi, A.1    Suzuki, E.2    Murayama, K.3
  • 23
    • 0020492531 scopus 로고
    • Reconstitution of Mg-ATP dependent protein phosphatase
    • Hemmings B. A., Resink T. J. Cohen P. (1982) Reconstitution of Mg-ATP dependent protein phosphatase. FEBS Lett. 150, 319 326.
    • (1982) FEBS Lett. , vol.150 , pp. 319-326
    • Hemmings, B.A.1    Resink, T.J.2    Cohen, P.3
  • 24
    • 0021162349 scopus 로고
    • DARPP-32, a dopamine-regulated neuronal phosphoprotein, is a potent inhibitor of protein phosphatase-1
    • Hemmings H. C. Jr., Greengard P., Tung H. Y. L. Cohen P. (1984a) DARPP-32, a dopamine-regulated neuronal phosphoprotein, is a potent inhibitor of protein phosphatase-1. Nature 310, 503 505.
    • (1984) Nature , vol.310 , pp. 503-505
    • Hemmings Jr., H.C.1    Greengard, P.2    Tung, H.Y.L.3    Cohen, P.4
  • 25
    • 0021702461 scopus 로고
    • DARPP-32, a dopamine- and adenosine 3′,5′-monophosphate- regulated neuronal phosphoprotein. I. Amino acid sequence around the phosphorylated threonine
    • Hemmings H. C. Jr., Williams K. R., Konigsberg W. H. Greengard P. (1984b) DARPP-32, a dopamine- and adenosine 3′,5′-monophosphate-regulated neuronal phosphoprotein. I. Amino acid sequence around the phosphorylated threonine. J. Biol. Chem. 259, 14486 14490.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14486-14490
    • Hemmings Jr., H.C.1    Williams, K.R.2    Konigsberg, W.H.3    Greengard, P.4
  • 26
    • 0027198862 scopus 로고
    • Identifying proteins from two-dimensional gel by molecular mass searching of peptide fragments in protein sequence databases
    • Henzel W. J., Billeci T. M., Stults J. T., Wong S. C., Grimley C. Watanabe C. (1993) Identifying proteins from two-dimensional gel by molecular mass searching of peptide fragments in protein sequence databases. Proc. Natl Acad. Sci. 90, 5011 5015.
    • (1993) Proc. Natl Acad. Sci. , vol.90 , pp. 5011-5015
    • Henzel, W.J.1    Billeci, T.M.2    Stults, J.T.3    Wong, S.C.4    Grimley, C.5    Watanabe, C.6
  • 27
    • 0023646584 scopus 로고
    • Analysis of the in vivo phosphorylation state of protein phosphatase inhibitor-2 from rabbit skeletal muscle by fast-atom bombardment mass spectrometry
    • Holmes C. F. B., Tonks N. K., Major H. Cohen P. (1987) Analysis of the in vivo phosphorylation state of protein phosphatase inhibitor-2 from rabbit skeletal muscle by fast-atom bombardment mass spectrometry. Biochim. Biophys. Acta 929, 208 219.
    • (1987) Biochim. Biophys. Acta , vol.929 , pp. 208-219
    • Holmes, C.F.B.1    Tonks, N.K.2    Major, H.3    Cohen, P.4
  • 28
    • 0036445163 scopus 로고    scopus 로고
    • Molecular mechanisms of cerebral ischemia-induced neuronal death
    • Hou S. I. MacManus J. P. (2002) Molecular mechanisms of cerebral ischemia-induced neuronal death. Int. Rev. Cytol. 221, 93 148.
    • (2002) Int. Rev. Cytol. , vol.221 , pp. 93-148
    • Hou, S.I.1    MacManus, J.P.2
  • 29
    • 0028981221 scopus 로고
    • 2+/calmodulin dependent protein kinase II to synaptic junctions in the vulnerable hippocampal CA1 region following transient ischemia
    • 2+/calmodulin dependent protein kinase II to synaptic junctions in the vulnerable hippocampal CA1 region following transient ischemia. J. Neurochem. 64, 277 284.
    • (1995) J. Neurochem. , vol.64 , pp. 277-284
    • Hu, B.-R.1    Wieloch, T.2
  • 30
    • 3142752692 scopus 로고    scopus 로고
    • Protein 14-3-3ζ binds to protein phosphatase PP1γ2 in bovine epididymal spermatozoa
    • Huang Z., Kimberley M., Khatra B. Vijayaraghavan S. (2004) Protein 14-3-3ζ binds to protein phosphatase PP1γ2 in bovine epididymal spermatozoa. Biol. Reprod. 71, 177 184.
    • (2004) Biol. Reprod. , vol.71 , pp. 177-184
    • Huang, Z.1    Kimberley, M.2    Khatra, B.3    Vijayaraghavan, S.4
  • 31
    • 0020540151 scopus 로고
    • The protein phosphatases involved in cellular regulation. 1. Classification and substrate specificities
    • Ingebritsen T. S. Cohen P. (1983) The protein phosphatases involved in cellular regulation. 1. Classification and substrate specificities. Eur. J. Biochem. 132, 255 261.
    • (1983) Eur. J. Biochem. , vol.132 , pp. 255-261
    • Ingebritsen, T.S.1    Cohen, P.2
  • 32
    • 0036667397 scopus 로고    scopus 로고
    • Serine/threonine protein phosphatases in apoptosis
    • Klumpp S. Krieglstein J. (2002) Serine/threonine protein phosphatases in apoptosis. Curr. Opin. Pharmacol. 2, 458 462.
    • (2002) Curr. Opin. Pharmacol. , vol.2 , pp. 458-462
    • Klumpp, S.1    Krieglstein, J.2
  • 33
    • 0022133358 scopus 로고
    • Oxygen radicals in cerebral vascular injury
    • Kontos H. A. (1985) Oxygen radicals in cerebral vascular injury. Circ. Res. 57, 508 516.
    • (1985) Circ. Res. , vol.57 , pp. 508-516
    • Kontos, H.A.1
  • 34
    • 0031953601 scopus 로고    scopus 로고
    • Calcium in ischemic cell death
    • Kristian T. Siesjo B. K. (1998) Calcium in ischemic cell death. Stroke 29, 705 718.
    • (1998) Stroke , vol.29 , pp. 705-718
    • Kristian, T.1    Siesjo, B.K.2
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680 685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0038168237 scopus 로고    scopus 로고
    • Phosphorylation of phosphatase inhibitor-2 at centrosomes during mitosis
    • Leach C., Shenolikar S. Brautigan D. L. (2003) Phosphorylation of phosphatase inhibitor-2 at centrosomes during mitosis. J. Biol. Chem. 278, 26015 26020.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26015-26020
    • Leach, C.1    Shenolikar, S.2    Brautigan, D.L.3
  • 37
    • 0032845121 scopus 로고    scopus 로고
    • Ischemic cell death in brain neurons
    • Lipton P. (1999) Ischemic cell death in brain neurons. Physiol. Rev. 79, 1431 1568.
    • (1999) Physiol. Rev. , vol.79 , pp. 1431-1568
    • Lipton, P.1
  • 38
    • 0036099593 scopus 로고    scopus 로고
    • Neurological outcome after experimental cardiopulmonary resuscitation: A result of delayed and potentially treatable neuronal injury
    • Liu X., Nozari A., Basu S., Ronquist G., Rubertsson S. Wiklund L. (2002) Neurological outcome after experimental cardiopulmonary resuscitation: a result of delayed and potentially treatable neuronal injury. Acta Anaesthesiol. Scand. 46, 537 546.
    • (2002) Acta Anaesthesiol. Scand. , vol.46 , pp. 537-546
    • Liu, X.1    Nozari, A.2    Basu, S.3    Ronquist, G.4    Rubertsson, S.5    Wiklund, L.6
  • 39
    • 0034661857 scopus 로고    scopus 로고
    • Regulation of BAD by cAMP dependent protein kinase is mediated via phosphorylation of a novel site, ser 155
    • Lizcano J. M., Morrice N. Cohen P. (2000) Regulation of BAD by cAMP dependent protein kinase is mediated via phosphorylation of a novel site, ser 155. Biochem. J. 349, 547 557.
    • (2000) Biochem. J. , vol.349 , pp. 547-557
    • Lizcano, J.M.1    Morrice, N.2    Cohen, P.3
  • 40
    • 0242389822 scopus 로고    scopus 로고
    • PP1 control of M phase entry exerted through 14-3-3-regulated Cdc25 dephosphorylation
    • Margolis S. S., Walsh S., Welser D. C., Yoshida M., Shenolikar S. Kornbluth S. (2003) PP1 control of M phase entry exerted through 14-3-3-regulated Cdc25 dephosphorylation. EMBO J. 22, 5734 5745.
    • (2003) EMBO J. , vol.22 , pp. 5734-5745
    • Margolis, S.S.1    Walsh, S.2    Welser, D.C.3    Yoshida, M.4    Shenolikar, S.5    Kornbluth, S.6
  • 41
    • 0035901755 scopus 로고    scopus 로고
    • Ischemia-induced inhibition of the initiation factor 2α phosphatase activity in the rat brain
    • Martin de la Vega C., Burda J. Salinas M. (2001) Ischemia-induced inhibition of the initiation factor 2α phosphatase activity in the rat brain. Neuroreport 12, 1021 1025.
    • (2001) Neuroreport , vol.12 , pp. 1021-1025
    • Martin De La Vega, C.1    Burda, J.2    Salinas, M.3
  • 42
    • 0037103005 scopus 로고    scopus 로고
    • Cerebral postischemic reperfusion-induced demethylation of the protein phosphatase-2A catalytic subunit
    • Martin de la Vega C., Burda J., Lobo M. V. T. Salinas M. (2002) Cerebral postischemic reperfusion-induced demethylation of the protein phosphatase-2A catalytic subunit. J. Neurosci. Res. 69, 540 549.
    • (2002) J. Neurosci. Res. , vol.69 , pp. 540-549
    • Martin De La Vega, C.1    Burda, J.2    Lobo, M.V.T.3    Salinas, M.4
  • 43
    • 0032125488 scopus 로고    scopus 로고
    • Neurodegeneration in excitotoxicity, global cerebral ischemia, and target deprivation: A perspective on contributions of apoptosis and necrosis
    • Martin L. J., Al-Abdulla N. A., Brambrink A. M., Kirsch J. R., Sieber F. E. Portera-Cailliau C. (1998) Neurodegeneration in excitotoxicity, global cerebral ischemia, and target deprivation: a perspective on contributions of apoptosis and necrosis. Brain Res. Bull. 46, 281 309.
    • (1998) Brain Res. Bull. , vol.46 , pp. 281-309
    • Martin, L.J.1    Al-Abdulla, N.A.2    Brambrink, A.M.3    Kirsch, J.R.4    Sieber, F.E.5    Portera-Cailliau, C.6
  • 44
    • 0029897419 scopus 로고    scopus 로고
    • The involvement of protein phosphatase in the activation of ICE/CED-3 protease, intracellular acidification, DNA digestion, and apoptosis
    • Morana S. J., Wolf C. M., Li J., Reynolds J. E., Brown M. K. Eastman A. (1996) The involvement of protein phosphatase in the activation of ICE/CED-3 protease, intracellular acidification, DNA digestion, and apoptosis. J. Biol. Chem. 271, 18263 18271.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18263-18271
    • Morana, S.J.1    Wolf, C.M.2    Li, J.3    Reynolds, J.E.4    Brown, M.K.5    Eastman, A.6
  • 45
    • 0033769047 scopus 로고    scopus 로고
    • Ischemia-induced phosphorylation of initiation factor 2 in differentiated PC12 cells: Role for initiation factor 2 phosphatase
    • Munoz F., Martin M. E., Manso-Tomico J., Berlanga J., Salinas M. Fando J. L. (2000) Ischemia-induced phosphorylation of initiation factor 2 in differentiated PC12 cells: role for initiation factor 2 phosphatase. J. Neurochem. 75, 2335 2345.
    • (2000) J. Neurochem. , vol.75 , pp. 2335-2345
    • Munoz, F.1    Martin, M.E.2    Manso-Tomico, J.3    Berlanga, J.4    Salinas, M.5    Fando, J.L.6
  • 46
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin A., Tanner J. W., Allen P. M. Shaw A. S. (1996) Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 84, 889 897.
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 47
    • 0033400237 scopus 로고    scopus 로고
    • Fas-mediated apoptosis in T cells involves the dephosphorylation of the retinoblastoma protein by type 1 protein phosphatase
    • N'cho M. Brahmi Z. (1999) Fas-mediated apoptosis in T cells involves the dephosphorylation of the retinoblastoma protein by type 1 protein phosphatase. Hum. Immunol. 60, 1183 1194.
    • (1999) Hum. Immunol. , vol.60 , pp. 1183-1194
    • N'Cho, M.1    Brahmi, Z.2
  • 48
    • 0025309904 scopus 로고
    • Oxidative damage to brain proteins, loss of glutamine synthetase activity, and production of free radicals during ischemia/reperfusion-induced injury to gerbil brain
    • Oliver C. N., Starke-Reed P. E., Stadtman E. R., Liu G. J., Carney J. M. Floyd R. A. (1990) Oxidative damage to brain proteins, loss of glutamine synthetase activity, and production of free radicals during ischemia/ reperfusion-induced injury to gerbil brain. Proc. Natl Acad. Sci. 87, 5144 5147.
    • (1990) Proc. Natl Acad. Sci. , vol.87 , pp. 5144-5147
    • Oliver, C.N.1    Starke-Reed, P.E.2    Stadtman, E.R.3    Liu, G.J.4    Carney, J.M.5    Floyd, R.A.6
  • 49
    • 2342651419 scopus 로고    scopus 로고
    • 14-3-3-Affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking
    • Pozuelo Rubio M., Geraghty K. M., Wong B. H. C., Wood N. T., Campbell D. G., Morrice N. Mackintosh C. (2004) 14-3-3-Affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking. Biochem. J. 379, 395 408.
    • (2004) Biochem. J. , vol.379 , pp. 395-408
    • Pozuelo Rubio, M.1    Geraghty, K.M.2    Wong, B.H.C.3    Wood, N.T.4    Campbell, D.G.5    Morrice, N.6    MacKintosh, C.7
  • 51
    • 0023774654 scopus 로고
    • Mechanisms of ischemic brain damage
    • Siesjo B. K. (1988) Mechanisms of ischemic brain damage. Crit. Care Med. 16, 954 963.
    • (1988) Crit. Care Med. , vol.16 , pp. 954-963
    • Siesjo, B.K.1
  • 55
    • 0021741403 scopus 로고
    • The protein phosphatases involved in cellular regulation: Comparison of native and reconstituted Mg-ATP dependent protein phosphatase
    • Tung H. Y. L. Cohen P. (1984) The protein phosphatases involved in cellular regulation: comparison of native and reconstituted Mg-ATP dependent protein phosphatase. Eur. J. Biochem. 145, 57 64.
    • (1984) Eur. J. Biochem. , vol.145 , pp. 57-64
    • Tung, H.Y.L.1    Cohen, P.2
  • 56
    • 0024577111 scopus 로고
    • Purification and characterization of protein phosphatase-1I activating kinase from bovine brain cytosolic and particulate fractions
    • Tung H. Y. L. Reed L. J. (1989) Purification and characterization of protein phosphatase-1I activating kinase from bovine brain cytosolic and particulate fractions. J. Biol. Chem. 264, 2985 2990.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2985-2990
    • Tung, H.Y.L.1    Reed, L.J.2
  • 58
    • 0038702246 scopus 로고    scopus 로고
    • Phosphatases in apoptosis: To be or not to be, PP2A is in the heart of the question
    • Van Hoof C. Goris J. (2003) Phosphatases in apoptosis: to be or not to be, PP2A is in the heart of the question. Biochim. Biophys. Acta 1640, 97 104.
    • (2003) Biochim. Biophys. Acta , vol.1640 , pp. 97-104
    • Van Hoof, C.1    Goris, J.2
  • 59
    • 0029120347 scopus 로고
    • Phosphorylation and activation of the ATP-Mg-dependent protein phosphatase by the mitogen-activated protein kinase
    • Wang Q. M., Guan K.-L., Roach P. J. DePaoli-Roach A. A. (1995) Phosphorylation and activation of the ATP-Mg-dependent protein phosphatase by the mitogen-activated protein kinase. J. Biol. Chem. 270, 18352 18358.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18352-18358
    • Wang, Q.M.1    Guan, K.-L.2    Roach, P.J.3    Depaoli-Roach, A.A.4
  • 60
    • 0035959632 scopus 로고    scopus 로고
    • Protein phosphatase-1α-mediated stimulation of apoptosis is associated with dephosphorylation of the retinoblastoma protein
    • Wang R.-H., Liu C. W. Y., Avramis V. I. Berndt N. (2001) Protein phosphatase-1α-mediated stimulation of apoptosis is associated with dephosphorylation of the retinoblastoma protein. Oncogene 20, 6111 6122.
    • (2001) Oncogene , vol.20 , pp. 6111-6122
    • Wang, R.-H.1    Liu, C.W.Y.2    Avramis, V.I.3    Berndt, N.4
  • 63
    • 0022345279 scopus 로고
    • Identification and characterization of an ATP Mg-dependent protein phosphatase from pig brain
    • Yang S. D. Fung Y.-L. (1985) Identification and characterization of an ATP Mg-dependent protein phosphatase from pig brain. J. Biol. Chem. 260, 13464 13470.
    • (1985) J. Biol. Chem. , vol.260 , pp. 13464-13470
    • Yang, S.D.1    Fung, Y.-L.2
  • 64
    • 0042433119 scopus 로고    scopus 로고
    • Erasure of kinase phosphorylation in astrocytes during oxygen-glucose deprivation is controlled by ATP levels and activation of protein phosphatases
    • Yung H. W. Tolkovsky A. M. (2003) Erasure of kinase phosphorylation in astrocytes during oxygen-glucose deprivation is controlled by ATP levels and activation of protein phosphatases. J. Neurochem. 86, 1281 1288.
    • (2003) J. Neurochem. , vol.86 , pp. 1281-1288
    • Yung, H.W.1    Tolkovsky, A.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.