메뉴 건너뛰기




Volumn 4, Issue 5, 2000, Pages 581-608

Serine/threonine-specific protein phosphatases and cancer

Author keywords

apoptosis; cancer; Cdk; cell cycle; cell survival; checkpoint control; cyclin; drug target; oncogene; protein kinase; protein phosphatase; protein phosphorylation; tumour suppressor

Indexed keywords


EID: 0000983084     PISSN: 14728222     EISSN: 17447631     Source Type: Journal    
DOI: 10.1517/14728222.4.5.581     Document Type: Review
Times cited : (3)

References (221)
  • 1
    • 0032960739 scopus 로고    scopus 로고
    • Defects in cell cycle control and cancer
    • BARTEK J, LUKAS J, BARTKOVA J: Defects in cell cycle control and cancer. J. Pathol. (1999) 187:95-99.
    • (1999) J. Pathol. , vol.187 , pp. 95-99
    • Bartek, J.1    Lukas, J.2    Bartkova, J.3
  • 3
    • 0033036758 scopus 로고    scopus 로고
    • Properties and potential applications of chemical inhibitors of cyclin-dependentkinases
    • MEIJER L, LECLERC S, LEOST M: Properties and potential applications of chemical inhibitors of cyclin-dependentkinases.Pharmacol. Ther. (1999) 82:279-284.
    • (1999) Pharmacol. Ther. , vol.82 , pp. 279-284
    • Meijer, L.1    Leclerc, S.2    Leost, M.3
  • 4
    • 0033063777 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: Initial approaches to exploit a novel therapeutic target
    • SAUSVILLE EA, ZAHAREVITZ D, GUSSIO R et al.: Cyclin-dependent kinases: initial approaches to exploit a novel therapeutic target. Pharmacol. Ther. (1999) 82:285-292.
    • (1999) Pharmacol. Ther. , vol.82 , pp. 285-292
    • Sausville, E.A.1    Zaharevitz, D.2    Gussio, R.3
  • 5
    • 0033399453 scopus 로고    scopus 로고
    • Anticancer drug targets: Cell cycle and checkpoint control
    • SHAPIRO GI, HARPER JW: Anticancer drug targets: cell cycle and checkpoint control. J. Clin. Invest. (1999) 104:1645-1653.
    • (1999) J. Clin. Invest. , vol.104 , pp. 1645-1653
    • Shapiro, G.I.1    Harper, J.W.2
  • 6
    • 0033400809 scopus 로고    scopus 로고
    • Apoptosis and cancer drug targeting
    • SELLERS WR, FISHER DE: Apoptosis and cancer drug targeting. J. Clin. Invest. (1999) 104:1655-1661.
    • (1999) J. Clin. Invest. , vol.104 , pp. 1655-1661
    • Sellers, W.R.1    Fisher, D.E.2
  • 7
    • 0031558235 scopus 로고    scopus 로고
    • Delivery of tumor suppressor genestoreverse the malignant phenotype
    • GIBSON NW, KENNEDY SP: Delivery of tumor suppressor genestoreverse the malignant phenotype. Adv. Drug Deliv. Rev. (1997) 26:119-133.
    • (1997) Adv. Drug Deliv. Rev. , vol.26 , pp. 119-133
    • Gibson, N.W.1    Kennedy, S.P.2
  • 8
    • 0032482939 scopus 로고    scopus 로고
    • Antiangiogenic gene therapy
    • FOLKMAN J: Antiangiogenic gene therapy. Proc. Natl. Acad. Sci. USA (1998) 95:9064-9066.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9064-9066
    • Folkman, J.1
  • 9
    • 49749165001 scopus 로고
    • The phosphorylase b to a converting enzyme of rabbit skeletal muscle
    • KREBS EG, FISCHER EH: The phosphorylase b to a converting enzyme of rabbit skeletal muscle. Biochim. Biophys. Acta (1956) 20:150-157.
    • (1956) Biochim. Biophys. Acta , vol.20 , pp. 150-157
    • Krebs, E.G.1    Fischer, E.H.2
  • 11
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The Yin and Yang of protein phosphorylation and signaling
    • HUNTER T: Protein kinases and phosphatases: the Yin and Yang of protein phosphorylation and signaling. Cell (1995) 80:225-236.
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 12
    • 0344306539 scopus 로고
    • Phosphotyrosine-a new protein modification
    • HUNTER T: Phosphotyrosine-a new protein modification. TrendsBiochem. Sci. (1982) 7:246-249.
    • (1982) TrendsBiochem. Sci. , vol.7 , pp. 246-249
    • Hunter, T.1
  • 13
    • 0033551070 scopus 로고    scopus 로고
    • New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway
    • CANTLEY LC, NEEL BG: New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway. Proc. Natl. Acad. Sci. USA (1999) 96:4240-4245.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4240-4245
    • Cantley, L.C.1    Neel, B.G.2
  • 14
    • 0034194403 scopus 로고    scopus 로고
    • Cell cycle arrest by the PTEN tumor suppressor is target cell specific and may require protein phosphatase activity
    • HLOBILKOVA A, GULDBERG P, THULLBERG M, ZEUTHEN J, LUKAS J, BARTEK J: Cell cycle arrest by the PTEN tumor suppressor is target cell specific and may require protein phosphatase activity. Exp. Cell Res. (2000) 256:571-577.
    • (2000) Exp. Cell Res. , vol.256 , pp. 571-577
    • Hlobilkova, A.1    Guldberg, P.2    Thullberg, M.3    Zeuthen, J.4    Lukas, J.5    Bartek, J.6
  • 16
    • 0032563947 scopus 로고    scopus 로고
    • Size control: Cell proliferation does not equal growth
    • O'FARRELL PH, SU TT: Size control: cell proliferation does not equal growth. Curr. Biol. (1998) 8:R687-R689.
    • (1998) Curr. Biol. , vol.8
    • O'Farrell, P.H.1    Tt, S.U.2
  • 17
    • 0033593316 scopus 로고    scopus 로고
    • Size control in animal development
    • CONLON I, RAFF MC: Size control in animal development. Cell (1999) 96:235-244.
    • (1999) Cell , vol.96 , pp. 235-244
    • Conlon, I.1    Raff, M.C.2
  • 18
    • 0033593572 scopus 로고    scopus 로고
    • Cell death in development
    • VAUX DL, KORSMEYER SJ: Cell death in development. Cell (1999) 96:245-254.
    • (1999) Cell , vol.96 , pp. 245-254
    • Vaux, D.L.1    Korsmeyer, S.J.2
  • 19
    • 0033866302 scopus 로고    scopus 로고
    • Measuring dimensions: The regulation of size and shape
    • DAY SJ, LAWRENCE PA: Measuring dimensions: the regulation of size and shape. Development (2000) 127:2977-2987.
    • (2000) Development , vol.127 , pp. 2977-2987
    • Day, S.J.1    Lawrence, P.A.2
  • 20
    • 0024473604 scopus 로고
    • G1 events and regulation of cell proliferation
    • PARDEE AB: G1 events and regulation of cell proliferation. Science (1989) 246:603-608.
    • (1989) Science , vol.246 , pp. 603-608
    • Pardee, A.B.1
  • 22
    • 0030657690 scopus 로고    scopus 로고
    • The restriction point and control of cell proliferation
    • PLANAS-SILVA MD, WEINBERG RA: The restriction point and control of cell proliferation. Curr. Opin. Cell Biol. (1997) 9:768-772.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 768-772
    • Planas-Silva, M.D.1    Weinberg, R.A.2
  • 23
    • 0028568315 scopus 로고
    • Cell cycle control and cancer
    • HARTWELL LH, KASTAN MB: Cell cycle control and cancer. Science (1994) 266:1821-1828.
    • (1994) Science , vol.266 , pp. 1821-1828
    • Hartwell, L.H.1    Kastan, M.B.2
  • 24
    • 0028051411 scopus 로고
    • Growth dysregulation in cancer cells
    • PARDEE AB: Growth dysregulation in cancer cells. Adv. Cancer Res. (1994) 65:213-228.
    • (1994) Adv. Cancer Res. , vol.65 , pp. 213-228
    • Pardee, A.B.1
  • 25
    • 0029849620 scopus 로고    scopus 로고
    • Cancer cell cycles
    • SHERR CJ: Cancer cell cycles. Science (1996) 274:1672-1677.
    • (1996) Science , vol.274 , pp. 1672-1677
    • Sherr, C.J.1
  • 28
    • 0031797414 scopus 로고    scopus 로고
    • Negative control elements of the cell cycle in human tumors
    • ADAMS PD, KAELIN JR. WG: Negative control elements of the cell cycle in human tumors. Curr. Opin. Cell Biol. (1998) 10:791-797.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 791-797
    • Adams, P.D.1    Kaelin Jr., W.G.2
  • 29
    • 0029317904 scopus 로고
    • Cyclin-dependent protein kinases: Key regulators of the eukaryotic cell cycle
    • NIGG EA: Cyclin-dependent protein kinases: key regulators of the eukaryotic cell cycle. BioEssays (1995) 17:471-480.
    • (1995) BioEssays , vol.17 , pp. 471-480
    • Nigg, E.A.1
  • 30
    • 0031466305 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: Engines, clocks and microprocessors
    • MORGAN DO: Cyclin-dependent kinases: engines, clocks and microprocessors. Ann. Rev. Cell Dev. Biol. (1997) 13:261-291.
    • (1997) Ann. Rev. Cell Dev. Biol. , vol.13 , pp. 261-291
    • Morgan, D.O.1
  • 31
    • 0031710479 scopus 로고    scopus 로고
    • The INK4a/ARF tumor suppressor: One gene-two products-two pathways
    • CHIN L, POMERANTZ J, DEPINHO RA: The INK4a/ARF tumor suppressor: one gene-two products-two pathways. TrendsBiochem. Sci. (1998) 23:291-296.
    • (1998) TrendsBiochem. Sci. , vol.23 , pp. 291-296
    • Chin, L.1    Pomerantz, J.2    Depinho, R.A.3
  • 32
    • 0031454404 scopus 로고    scopus 로고
    • Inhibitors of the Cip/Kip family
    • Vogt PK, Reed SI (Eds.), Springer Verlag, Berlin, Germany
    • HENGST L, REED SI: Inhibitors of the Cip/Kip family. In: Cyclin Dependent Kinase (CDK) Inhibitors (Vol 227). Vogt PK, Reed SI (Eds.), Springer Verlag, Berlin, Germany (1998):25-41.
    • (1998) Cyclin Dependent Kinase (CDK) Inhibitors , vol.227 , pp. 25-41
    • Hengst, L.1    Reed, S.I.2
  • 33
    • 0029051233 scopus 로고
    • Cyclin ubiquitination: The destructive end of mitosis
    • MURRAY AW: Cyclin ubiquitination: the destructive end of mitosis. Cell (1995) 81:149-152.
    • (1995) Cell , vol.81 , pp. 149-152
    • Murray, A.W.1
  • 34
    • 0030662522 scopus 로고    scopus 로고
    • Eliminating all obstacles: Regulated proteolysis in the eukaryotic cell cycle
    • HOYT MA: Eliminating all obstacles: regulated proteolysis in the eukaryotic cell cycle. Cell (1997) 91:149-151.
    • (1997) Cell , vol.91 , pp. 149-151
    • Hoyt, M.A.1
  • 35
    • 1342272916 scopus 로고    scopus 로고
    • How the cyclin became a cyclin: Regulated proteolysis in the cell cycle
    • KOEPP DM, HARPER JW, ELLEDGE SJ: How the cyclin became a cyclin: regulated proteolysis in the cell cycle. Cell (1999) 97:431-434.
    • (1999) Cell , vol.97 , pp. 431-434
    • Koepp, D.M.1    Harper, J.W.2    Elledge, S.J.3
  • 36
    • 0030309532 scopus 로고    scopus 로고
    • G1/S regulatory mechanisms from yeast to man
    • Meijer L, Guidet S, Vogel L (Eds.), Plenum Press, New York, NY, USA
    • REED SI: G1/S regulatory mechanisms from yeast to man. In: Progress in Cell Cycle Research (Vol 2). Meijer L, Guidet S, Vogel L (Eds.), Plenum Press, New York, NY, USA (1996):15-27.
    • (1996) Progress in Cell Cycle Research , vol.2 , pp. 15-27
    • Reed, S.I.1
  • 37
    • 0031309361 scopus 로고    scopus 로고
    • Aberrations of the G1-and G1/S-regulating genes in human cancer
    • Meijer L, Guidet S, Philippe M (Eds.), Plenum Press, New York, NY, USA
    • BARTKOVA J, LUKAS J, BARTEK J: Aberrations of the G1-and G1/S-regulating genes in human cancer. In: Progress in Cell Cycle Research (Vol 3). Meijer L, Guidet S, Philippe M (Eds.), Plenum Press, New York, NY, USA (1997):211-220.
    • (1997) Progress in Cell Cycle Research , vol.3 , pp. 211-220
    • Bartkova, J.1    Lukas, J.2    Bartek, J.3
  • 38
    • 0026716167 scopus 로고
    • The retinoblastoma gene and gene product
    • WEINBERG RA: The retinoblastoma gene and gene product. Cancer Surveys (1992) 12:43-57.
    • (1992) Cancer Surveys , vol.12 , pp. 43-57
    • Weinberg, R.A.1
  • 39
    • 0028170806 scopus 로고
    • The retinoblastoma protein: More than a tumor suppressor
    • RILEY DJ, LEE EYHP, LEE W-H: The retinoblastoma protein: more than a tumor suppressor. Ann. Rev. Cell Biol. (1994) 10:1-29.
    • (1994) Ann. Rev. Cell Biol. , vol.10 , pp. 1-29
    • Riley, D.J.1    Lee, E.Y.H.P.2    Lee, W.-H.3
  • 40
    • 0030561571 scopus 로고    scopus 로고
    • The retinoblastoma protein pathway and the restriction point
    • BARTEK J, BARTKOVA J, LUKAS J: The retinoblastoma protein pathway and the restriction point. Curr. Opin. Cell Biol. (1996) 8:805-814.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 805-814
    • Bartek, J.1    Bartkova, J.2    Lukas, J.3
  • 41
    • 0031016121 scopus 로고    scopus 로고
    • RB kinases and RB-binding proteins: New points of view
    • TAYA Y: RB kinases and RB-binding proteins: new points of view. Trends Biochem. Sci. (1997) 22:14-17.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 14-17
    • Taya, Y.1
  • 42
    • 0031935648 scopus 로고    scopus 로고
    • Control of pRB phosphorylation
    • MITTNACHT S: Control of pRB phosphorylation. Curr. Opin. Genet. Dev. (1998) 8:21-27.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 21-27
    • Mittnacht, S.1
  • 43
    • 0344671608 scopus 로고    scopus 로고
    • Functions of the retinoblastoma protein
    • KAELIN JR. WG: Functions of the retinoblastoma protein. BioEssays (1999) 21:950-958.
    • (1999) BioEssays , vol.21 , pp. 950-958
    • Kaelin Jr., W.G.1
  • 44
    • 0026058874 scopus 로고
    • The retinoblastoma gene product regulates progression through the G1 phase of the cell cycle
    • GOODRICH DW, PING WANG N, QIAN Y-W, LEE EYHP, LEE W-H: The retinoblastoma gene product regulates progression through the G1 phase of the cell cycle. Cell (1991) 67:293-302.
    • (1991) Cell , vol.67 , pp. 293-302
    • Goodrich, D.W.1    Ping Wang, N.2    Qian, Y.-W.3    Eyhp, L.4    Lee, W.-H.5
  • 45
    • 0028228907 scopus 로고
    • Absence of cyclin D/cdk complexes in cells lacking functional retinoblastoma protein
    • BATES S, PARRY D, BONETTA L, VOUSDEN KH, DICKSON C, PETERS G: Absence of cyclin D/cdk complexes in cells lacking functional retinoblastoma protein. Oncogene (1994) 9:1633-1640.
    • (1994) Oncogene , vol.9 , pp. 1633-1640
    • Bates, S.1    Parry, D.2    Bonetta, L.3    Vousden, K.H.4    Dickson, C.5    Peters, G.6
  • 46
    • 0028925360 scopus 로고
    • Cyclin D1 is dispensable for G1 control in retinoblastoma gene-deficient cells independently of cdk4 activity
    • LUKAS J, BARTKOVA J, ROHDE M, STRAUSS M, BARTEK J: Cyclin D1 is dispensable for G1 control in retinoblastoma gene-deficient cells independently of cdk4 activity. Mol. Cell. Biol. (1995) 15:2600-2611.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2600-2611
    • Lukas, J.1    Bartkova, J.2    Rohde, M.3    Strauss, M.4    Bartek, J.5
  • 48
    • 0029986337 scopus 로고    scopus 로고
    • Regulation of cyclin e transcription by E2Fs and retinoblastoma protein
    • GENG Y, EATON EN, PICÓN M etal: Regulation of cyclin E transcription by E2Fs and retinoblastoma protein. Oncogene (1996) 12:1173-1180.
    • (1996) Oncogene , vol.12 , pp. 1173-1180
    • Geng, Y.1    Eaton, E.N.2    Picón, M.3
  • 49
    • 0030783627 scopus 로고    scopus 로고
    • Phosphory-lated retinoblastoma protein stimulates DNA polymerase a
    • TAKEMURA M, KITAGAWA T, IZUTA S etal: Phosphory-lated retinoblastoma protein stimulates DNA polymerase a. Oncogene (1997) 15:2483-2492.
    • (1997) Oncogene , vol.15 , pp. 2483-2492
    • Takemura, M.1    Kitagawa, T.2    Izuta, S.3
  • 50
    • 0031454405 scopus 로고    scopus 로고
    • Cyclin-dependent kinase inhibitors and human cancer
    • Vogt PK, Reed SI (Eds.), Springer Verlag, Berlin, Germany
    • KAMB A: Cyclin-dependent kinase inhibitors and human cancer. In: Cyclin Dependent Kinase (CDK) Inhibitors (Vol 227). Vogt PK, Reed SI (Eds.), Springer Verlag, Berlin, Germany (1998):139-148.
    • (1998) Cyclin Dependent Kinase (CDK) Inhibitors , vol.227 , pp. 139-148
    • Kamb, A.1
  • 51
    • 0031451323 scopus 로고    scopus 로고
    • Roles of cyclin-dependent kinase inhibitors: Lessons from knockout mice
    • Vogt PK, Reed SI (Eds.), Springer Verlag, Berlin, Germany
    • KIYOKAWA H, KOFF A: Roles of cyclin-dependent kinase inhibitors: lessons from knockout mice. In: Cyclin Dependent Kinase (CDK) Inhibitors (Vol 227). Vogt PK, Reed SI (Eds.), Springer Verlag, Berlin, Germany (1998):105-120.
    • (1998) Cyclin Dependent Kinase (CDK) Inhibitors , vol.227 , pp. 105-120
    • Kiyokawa, H.1    Koff, A.2
  • 52
    • 0029054399 scopus 로고
    • Retinoblastoma-protein-dependent cell-cycle inhibition by the tumour suppressor p16
    • LUKAS J, PARRY D, AAGAARD L et al: Retinoblastoma-protein-dependent cell-cycle inhibition by the tumour suppressor p16. Nature (1995) 375:503-506.
    • (1995) Nature , vol.375 , pp. 503-506
    • Lukas, J.1    Parry, D.2    Aagaard, L.3
  • 54
    • 0029416998 scopus 로고
    • waf1/cip 1 arrests the growth of chicken embryo fibroblasts transformed by individual oncogenes
    • GIVOL I, GIVOL D, RULONG S, RESAU J, TSARFATY I, HUGHES SH: Overexpression of human p21waf1/cip1 arrests the growth of chicken embryo fibroblasts transformed by individual oncogenes. Oncogene (1995) 11:2609-2618.
    • (1995) Oncogene , vol.11 , pp. 2609-2618
    • Givol, I.1    Givol, D.2    Rulong, S.3    Resau, J.4    Tsarfaty, I.5    Hughes, S.H.6
  • 55
    • 0032129273 scopus 로고    scopus 로고
    • Overex pression of p27Kip1 inhibits the growth of both normal and transformed human mammary epithelial cells
    • SGAMBATO A, ZHANG Y-J, CIAPARRONE M etal: Overex pression of p27Kip1 inhibits the growth of both normal and transformed human mammary epithelial cells. Cancer Res. (1998) 58:3448-3454.
    • (1998) Cancer Res. , vol.58 , pp. 3448-3454
    • Sgambato, A.1    Zhang, Y.-J.2    Ciaparrone, M.3
  • 56
    • 0028973212 scopus 로고
    • CIP1 induces growth arrest, giant cell formation and apoptosis in human breast carcinoma cell lines
    • SHEIKH MS, ROCHEFORT H, GARCIA M: Overexpression of p21WAF1/CIP1 induces growth arrest, giant cell formation and apoptosis in human breast carcinoma cell lines. Oncogene (1995) 11:1899-1905.
    • (1995) Oncogene , vol.11 , pp. 1899-1905
    • Sheikh, M.S.1    Rochefort, H.2    Garcia, M.3
  • 57
    • 0031283291 scopus 로고    scopus 로고
    • Kip1 overexpression causes apoptotic death of mammalian cells
    • WANG X, GOROSPE M, HUANG Y, HOLBROOK NJ: p27Kip1 overexpression causes apoptotic death of mammalian cells. Oncogene (1997) 15:2991-2997.
    • (1997) Oncogene , vol.15 , pp. 2991-2997
    • Wang, X.1    Gorospe, M.2    Huang, Y.3    Holbrook, N.J.4
  • 58
    • 0032543305 scopus 로고    scopus 로고
    • Re-expression of p16INK4a in mesothelioma cells results in cell cycle arrest, cell death, tumor suppression and tumor regression
    • FRIZELLE SP, GRIM J, ZHOU J et al.: Re-expression of p16INK4a in mesothelioma cells results in cell cycle arrest, cell death, tumor suppression and tumor regression. Oncogene (1998) 16:3087-3095.
    • (1998) Oncogene , vol.16 , pp. 3087-3095
    • Frizelle, S.P.1    Grim, J.2    Zhou, J.3
  • 59
    • 0027970713 scopus 로고
    • DNA damage triggers a prolonged p53-dependent G1 arrest and long-term induction of Cip1 in normal human fibroblasts
    • DI LEONARDO A, LINKE SP, CLARKIN K, WAHL GM: DNA damage triggers a prolonged p53-dependent G1 arrest and long-term induction of Cip1 in normal human fibroblasts. GenesDev. (1994) 8:2540-2551.
    • (1994) GenesDev. , vol.8 , pp. 2540-2551
    • Leonardo A, D.I.1    Linke, S.P.2    Clarkin, K.3    Wahl, G.M.4
  • 60
    • 0028168242 scopus 로고
    • INK4Bis a potential effector of TGF-|5-induced cell cycle arrest
    • HANNON GJ, BEACH D: p15INK4Bis a potential effector of TGF-|5-induced cell cycle arrest. Nature (1994) 371:257-261.
    • (1994) Nature , vol.371 , pp. 257-261
    • Hannon, G.J.1    Beach, D.2
  • 61
    • 0029073142 scopus 로고
    • Transforming growth factor P induces the cyclin-dependent kinase inhibitor p21 through a p53-independent mechanism
    • DATTO MB, LI Y, PANUS JF, HOWE DJ, XIONG Y, WANG X-F: Transforming growth factor P induces the cyclin-dependent kinase inhibitor p21 through a p53-independent mechanism. Proc. Natl. Acad. Sci. USA (1995) 92:5545-5549.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5545-5549
    • Datto, M.B.1    Y, L.I.2    Panus, J.F.3    Howe, D.J.4    Xiong, Y.5    Wang, X.-F.6
  • 62
    • 0031975911 scopus 로고    scopus 로고
    • TGF-P1 induces the cyclin-dependent kinase inhibitor p27Kip1 mRNA and protein in murine B cells
    • KAMESAKI H, NISHIZAWA K, MICHAUD GY, COSSMAN J, KIYONO T: TGF-P1 induces the cyclin-dependent kinase inhibitor p27Kip1 mRNA and protein in murine B cells. J. Immunol. (1998) 160:770-777.
    • (1998) J. Immunol. , vol.160 , pp. 770-777
    • Kamesaki, H.1    Nishizawa, K.2    Michaud, G.Y.3    Cossman, J.4    Kiyono, T.5
  • 63
    • 0033575255 scopus 로고    scopus 로고
    • Suicidal tendencies: Apoptotic cell death by caspase family proteinases
    • WOLF BB, GREEN DR: Suicidal tendencies: apoptotic cell death by caspase family proteinases. J. Biol. Chem. (1999) 274:20049-20052.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20049-20052
    • Wolf, B.B.1    Green, D.R.2
  • 64
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates and functions during apoptosis
    • EARNSHAW WC, MARTINS LM, KAUFMANN SH: Mammalian caspases: structure, activation, substrates and functions during apoptosis. Ann. Rev. Biochem. (1999) 68: 383-424.
    • (1999) Ann. Rev. Biochem. , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 65
    • 0031945458 scopus 로고    scopus 로고
    • Cell cycle regulation and apoptosis
    • KING KL, CIDLOWSKI JA: Cell cycle regulation and apoptosis. Ann. Rev. Physiol. (1998) 60:601-617.
    • (1998) Ann. Rev. Physiol. , vol.60 , pp. 601-617
    • King, K.L.1    Cidlowski, J.A.2
  • 66
    • 0032575705 scopus 로고    scopus 로고
    • A matter of life and cell death
    • EVAN GI, LITTLEWOOD T: A matter of life and cell death. Science (1998) 281:1317-1322.
    • (1998) Science , vol.281 , pp. 1317-1322
    • Evan, G.I.1    Littlewood, T.2
  • 67
    • 0033377979 scopus 로고    scopus 로고
    • Control of the cell cycle and apoptosis
    • LUNDBERG AS, WEINBERG RA: Control of the cell cycle and apoptosis. Eur. J. Cancer (1999) 35:531-539.
    • (1999) Eur. J. Cancer , vol.35 , pp. 531-539
    • Lundberg, A.S.1    Weinberg, R.A.2
  • 70
    • 0030847760 scopus 로고    scopus 로고
    • Phosphorylation-dependent degradation of the cyclin-dependent kinase inhibitor p27Kip1
    • VLACH J, HENNECKE S, AMATI B: Phosphorylation-dependent degradation of the cyclin-dependent kinase inhibitor p27Kip1. EMBOJ. (1997) 16:5334-5344.
    • (1997) EMBOJ. , vol.16 , pp. 5334-5344
    • Vlach, J.1    Hennecke, S.2    Amati, B.3
  • 71
    • 0032511893 scopus 로고    scopus 로고
    • Interaction with cyclin-dependent kinases and PCNA modulates proteasome-dependent degradation of p21
    • CAYROL C, DUCOMMUN B: Interaction with cyclin-dependent kinases and PCNA modulates proteasome-dependent degradation of p21. Oncogene (1998) 17:2437-2444.
    • (1998) Oncogene , vol.17 , pp. 2437-2444
    • Cayrol, C.1    Ducommun, B.2
  • 72
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-XL
    • ZHA J, HARADA H, YANG E, JOCKEL J, KORSMEYER SJ: Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-XL. Cell (1996) 87:619-628.
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 73
    • 0032543578 scopus 로고    scopus 로고
    • 136
    • BLUME-JENSEN P, JANKNECHT R, HUNTER T: The Kit receptor promotes cell survival via activation of PI3-kinase and subsequent Akt-mediated phosphorylation of Bad on Ser136. Curr Biol. (1998) 8:779-782.
    • (1998) Curr Biol. , vol.8 , pp. 779-782
    • Blume-Jensen, P.1    Janknecht, R.2    Hunter, T.3
  • 74
    • 0032515027 scopus 로고    scopus 로고
    • Regulation of cell death protease caspase-9 by phosphorylation
    • CARDONE MH, ROY N, STENNICKE HR etal: Regulation of cell death protease caspase-9 by phosphorylation. Science (1998) 282:1318-1321.
    • (1998) Science , vol.282 , pp. 1318-1321
    • Cardone, M.H.1    Roy, N.2    Stennicke, H.R.3
  • 75
    • 0001109314 scopus 로고    scopus 로고
    • AN B: RB and apoptotic cell death
    • DOU QP, AN B: RB and apoptotic cell death. Front Biosci. (1998) 3:d419-430.
    • (1998) Front Biosci. , vol.3
    • Dou, Q.P.1
  • 76
    • 0032031417 scopus 로고    scopus 로고
    • The caspase-RB connection in cell death
    • TAN X, WANG JYJ: The caspase-RB connection in cell death. Trends Cell Biol. (1998) 8:116-120.
    • (1998) Trends Cell Biol. , vol.8 , pp. 116-120
    • Tan, X.1    Wang, J.Y.J.2
  • 77
    • 0033786378 scopus 로고    scopus 로고
    • Rb function in cell-cycle regulation and apoptosis
    • HARBOUR JW, DEAN DC: Rb function in cell-cycle regulation and apoptosis. Nature Cell Biol. (2000) 2:E65-E67.
    • (2000) Nature Cell Biol. , vol.2
    • Harbour, J.W.1    Dean, D.C.2
  • 78
    • 0033564697 scopus 로고    scopus 로고
    • CDK inhibitors: Positive and negative regulators of G1-phase progression
    • SHERR CJ, ROBERTS JM: CDK inhibitors: positive and negative regulators of G1-phase progression. Genes Dev (1999) 13:1501-1512.
    • (1999) Genes Dev , vol.13 , pp. 1501-1512
    • Sherr, C.J.1    Roberts, J.M.2
  • 79
    • 0029977751 scopus 로고    scopus 로고
    • E2F and cell proliferation: A world turned upside down
    • WEINBERG RA: E2F and cell proliferation: a world turned upside down. Cell (1996) 85:457-459.
    • (1996) Cell , vol.85 , pp. 457-459
    • Weinberg, R.A.1
  • 80
    • 0034069354 scopus 로고    scopus 로고
    • The paradox of E2F1: Oncogene and tumor suppressor gene
    • JOHNSON DG: The paradox of E2F1: oncogene and tumor suppressor gene. Mol. Carcinog. (2000) 27:151-157.
    • (2000) Mol. Carcinog. , vol.27 , pp. 151-157
    • Johnson, D.G.1
  • 83
    • 0030941458 scopus 로고    scopus 로고
    • P53, the cellular gatekeeper for growth and division
    • LEVINE AJ: p53, the cellular gatekeeper for growth and division. Cell (1997) 88:323-331.
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 84
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • HANAHAN D, WEINBERG RA: The hallmarks of cancer. Cell (2000) 100:57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 85
    • 0030790128 scopus 로고    scopus 로고
    • Novel protein serine/threonine phosphatases: Variety is the spice of life
    • COHEN PTW: Novel protein serine/threonine phosphatases: variety is the spice of life. Trends Biochem. Sci. (1997) 22:245-251.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 245-251
    • Cohen, P.T.W.1
  • 87
    • 0031860103 scopus 로고    scopus 로고
    • The structure and mechanism of protein phosphatases: Insights into catalysis and regulation
    • BARFORD D, DAS AK, EGLOFF MP: The structure and mechanism of protein phosphatases: insights into catalysis and regulation. Ann. Rev. Biophys. Biomol. Struct. (1998) 27:133-164.
    • (1998) Ann. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 133-164
    • Barford, D.1    Das, A.K.2    Egloff, M.P.3
  • 88
    • 0029094754 scopus 로고
    • Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
    • GOLDBERG J, HUANG H-B, KWON Y-G, GREENGARD P, NAIRN AC, KURIYAN J: Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature (1995) 376:745-753.
    • (1995) Nature , vol.376 , pp. 745-753
    • Goldberg, J.1    Huang, H.-B.2    Kwon, Y.-G.3    Greengard, P.4    Nairn, A.C.5    Kuriyan, J.6
  • 89
    • 0029583122 scopus 로고
    • Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate
    • EGLOFF M-P, COHEN PTW, REINEMER P, BARFORD D: Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate. J. Mol. Biol. (1995) 254:942-959.
    • (1995) J. Mol. Biol. , vol.254 , pp. 942-959
    • Egloff, M.-P.1    Ptw, C.2    Reinemer, P.3    Barford, D.4
  • 90
    • 0029133116 scopus 로고
    • X-ray structure of calcineurin inhibited by the immunophilin- immunosuppressant FKBP12-FK506 complex
    • GRIFFITH JP, KIM JL, KIM EE et al.: X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex. Cell (1995) 82:507-522.
    • (1995) Cell , vol.82 , pp. 507-522
    • Griffith, J.P.1    Kim, J.L.2    Kim, E.E.3
  • 91
    • 0032473425 scopus 로고    scopus 로고
    • The structure of the tetratricopeptide repeats of protein phosphatase 5: Implications for TPR-mediated protein-protein interactions
    • DAS AK, COHEN PTW, BARFORD D: The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBOJ. (1998) 17:1192-1199.
    • (1998) EMBOJ. , vol.17 , pp. 1192-1199
    • Das, A.K.1    Cohen, P.T.W.2    Barford, D.3
  • 92
    • 0028180517 scopus 로고
    • PP172, a testis-specific protein serine/threonine-phosphatase Type 1 catalytic subunit, is associated with a protein having high sequence homology with the 78-kDa glucose-regulated protein, a member of the 70-kDa heat shock protein family
    • CHUN Y-S, SHIMA H, NAGASAKI K, SUGIMURA T, NAGAO M: PP172, a testis-specific protein serine/threonine-phosphatase Type 1 catalytic subunit, is associated with a protein having high sequence homology with the 78-kDa glucose-regulated protein, a member of the 70-kDa heat shock protein family. Proc. Natl. Acad. Sci. USA (1994) 91:3319-3323.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3319-3323
    • Chun, Y.-S.1    Shima, H.2    Nagasaki, K.3    Sugimura, T.4    Nagao, M.5
  • 93
    • 0032159462 scopus 로고    scopus 로고
    • Physiologic importance of protein phosphatase inhibitors
    • OLIVIER CJ, SHENOLIKAR S: Physiologic importance of protein phosphatase inhibitors. Front. Biosci. (1998) 3:d961-972.
    • (1998) Front. Biosci. , vol.3
    • Olivier, C.J.1    Shenolikar, S.2
  • 94
    • 0033558440 scopus 로고    scopus 로고
    • Phosphorylase phosphatase: New horizons for an old enzyme
    • LEE EYC, ZHANG L, ZHAO S et al.: Phosphorylase phosphatase: new horizons for an old enzyme. Front Biosci. (1999) 4:d270-285.
    • (1999) Front Biosci. , vol.4
    • Eyc, L.1    Zhang, L.2    Zhao, S.3
  • 95
    • 0032535169 scopus 로고    scopus 로고
    • Role of PP2A in intracellular signal transduction pathways
    • SCHÖNTHAL AH: Role of PP2A in intracellular signal transduction pathways. Front. Biosci. (1998) 3:d1262-1273.
    • (1998) Front. Biosci. , vol.3
    • Schönthal, A.H.1
  • 96
    • 0034009389 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A panoply of enzymes
    • VIRSHUP DM: Protein phosphatase 2A: a panoply of enzymes. Curr. Opin. Cell Biol. (2000) 12:180-185.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 180-185
    • Virshup, D.M.1
  • 97
    • 80052081582 scopus 로고
    • Carboxyl methylation-a new regulatory mechanism for an old enzyme, protein phosphatase 2A
    • ZOLNIEROWICZ S, FAVRE B, HEMMINGS BA: Carboxyl methylation-a new regulatory mechanism for an old enzyme, protein phosphatase 2A. Adv. Prot. Phosphatases (1994) 8:355-369.
    • (1994) Adv. Prot. Phosphatases , vol.8 , pp. 355-369
    • Zolnierowicz, S.1    Favre, B.2    Hemmings, B.A.3
  • 98
    • 0002193472 scopus 로고    scopus 로고
    • Protein dephosphorylation and the intracellular control of the cell number
    • BERNDT N: Protein dephosphorylation and the intracellular control of the cell number. Front. Biosci. (1999) 4:d22-42.
    • (1999) Front. Biosci. , vol.4
    • Berndt, N.1
  • 99
    • 0031962883 scopus 로고    scopus 로고
    • G1 cyclin-dependent kinases are sufficient to initiate DNA synthesis in quiescent human fibroblasts
    • CONNELL-CROWLEY L, ELLEDGE SJ, HARPER JW: G1 cyclin-dependent kinases are sufficient to initiate DNA synthesis in quiescent human fibroblasts. Curr. Biol. (1998) 8:65-68.
    • (1998) Curr. Biol. , vol.8 , pp. 65-68
    • Connell-Crowley, L.1    Elledge, S.J.2    Harper, J.W.3
  • 100
    • 0001658828 scopus 로고
    • The enzymatic conversion of phosphorylase a to b
    • CORI GT, CORI CF: The enzymatic conversion of phosphorylase a to b. J. Biol. Chem. (1945) 158:321-332.
    • (1945) J. Biol. Chem. , vol.158 , pp. 321-332
    • Cori, G.T.1    Cori, C.F.2
  • 101
    • 0022542584 scopus 로고
    • Protein phosphorylation and oocyte maturation. II. Inhibition of starfish oocyte maturation by intracellular microinjection of protein phosphatases 1 and 2A and alkaline phosphatase
    • MEIJER L, PONDAVEN P, TUNG HYL, COHEN P, WALLACE RW: Protein phosphorylation and oocyte maturation. II. Inhibition of starfish oocyte maturation by intracellular microinjection of protein phosphatases 1 and 2A and alkaline phosphatase. Exp. Cell Res. (1986) 163:489-499.
    • (1986) Exp. Cell Res. , vol.163 , pp. 489-499
    • Meijer, L.1    Pondaven, P.2    Hyl, T.3    Cohen, P.4    Wallace, R.W.5
  • 102
    • 0024394856 scopus 로고
    • The bimGgene of Aspergillus nidulans, required for completion of anaphase, encodes a homolog of mammalian phosphoprotein phosphatase 1
    • DOONAN JH, MORRIS NR: The bimGgene of Aspergillus nidulans, required for completion of anaphase, encodes a homolog of mammalian phosphoprotein phosphatase 1. Cell (1989) 57:987-996.
    • (1989) Cell , vol.57 , pp. 987-996
    • Doonan, J.H.1    Morris, N.R.2
  • 103
    • 0024410089 scopus 로고
    • 2+ gene required for chromosome disjoining encodes one of two putative Type 1 protein phosphatases
    • OHKURA H, KINOSHITA N, MIYATANI S, TODA T, YANAGIDA M: The fission yeast dis2+gene required for chromosome disjoining encodes one of two putative Type 1 protein phosphatases. Cell (1989) 57:997-1007.
    • (1989) Cell , vol.57 , pp. 997-1007
    • Ohkura, H.1    Kinoshita, N.2    Ss, M.3    Toda, T.4    Yanagida, M.5
  • 104
    • 0024361523 scopus 로고
    • 1+ in fission yeast mitotic control
    • BOOHER RN, BEACH D: Involvement of a Type 1 protein phosphatase encoded by bws1+ in fission yeast mitotic control. Cell (1989) 57:1009-1016.
    • (1989) Cell , vol.57 , pp. 1009-1016
    • Booher, R.N.1    Beach, D.2
  • 105
    • 0025011050 scopus 로고
    • One of the protein phosphatase 1 isoenzymes in Drosophila is essential for mitosis
    • AXTON JM, DÓMBRADI V, COHEN PTW, GLOVER DM: One of the protein phosphatase 1 isoenzymes in Drosophila is essential for mitosis. Cell(1990) 63:33-46.
    • (1990) Cell , vol.63 , pp. 33-46
    • Axton, J.M.1    Dómbradi, V.2    Ptw, C.3    Glover, D.M.4
  • 106
    • 0026561879 scopus 로고
    • Protein phosphatase Type 1 in mammalian cell mitosis: Chromosomal localization and involvement in mitotic exit
    • FERNANDEZ A, BRAUTIGAN DL, LAMB NJC: Protein phosphatase Type 1 in mammalian cell mitosis: chromosomal localization and involvement in mitotic exit.J. Cell Biol. (1992) 116:1421-1430.
    • (1992) J. Cell Biol. , vol.116 , pp. 1421-1430
    • Fernandez, A.1    Brautigan, D.L.2    Lamb, N.J.C.3
  • 107
    • 0023648079 scopus 로고
    • Smooth muscle myosin phosphatase inhibition and force enhancement by black sponge toxin
    • TAKAI A, BIALOJAN C, TROSCHKA M, RUEGG JC: Smooth muscle myosin phosphatase inhibition and force enhancement by black sponge toxin. FEBS Lett. (1987) 217:81-84.
    • (1987) FEBS Lett. , vol.217 , pp. 81-84
    • Takai, A.1    Bialojan, C.2    Troschka, M.3    Ruegg, J.C.4
  • 108
    • 0024121562 scopus 로고
    • Okadaic acid: An additional non-phorbol-12-tetradecanoate-13-acetate-type tumor promoter
    • SUGANUMA M, FUJIKI H, SUGURI H et al.: Okadaic acid: an additional non-phorbol-12-tetradecanoate-13-acetate-type tumor promoter. Proc. Natl. Acad. Sci. USA (1988) 85:1768-1771.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1768-1771
    • Suganuma, M.1    Fujiki, H.2    Suguri, H.3
  • 109
    • 0024792262 scopus 로고
    • Protein phosphatases come of age
    • COHEN P, COHEN PTW: Protein phosphatases come of age. J. Biol. Chem. (1989) 264:21435-21438.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21435-21438
    • Cohen, P.1    Cohen, P.T.W.2
  • 110
    • 0025844920 scopus 로고
    • Growth arrest induced by transforming growth factor (51 is accompanied by protein phosphatase activation in human keratinocytes
    • GRUPPUSO PA, MIKUMO R, BRAUTIGAN DL, BRAUN L: Growth arrest induced by transforming growth factor (51 is accompanied by protein phosphatase activation in human keratinocytes. J. Biol. Chem. (1991) 266:3444-3448.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3444-3448
    • Gruppuso, P.A.1    Mikumo, R.2    Brautigan, D.L.3    Braun, L.4
  • 112
    • 0027458292 scopus 로고
    • Regulation of cell cycle progression and nuclear affinity of the retinoblastoma protein by protein phosphatases
    • ALBERTS AS, THORBURN AM, SHENOLIKAR S, MUMBY MC, FERAMISCOJ R: Regulation of cell cycle progression and nuclear affinity of the retinoblastoma protein by protein phosphatases. Proc. Natl. Acad. Sci. USA (1993) 90:388-392.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 388-392
    • Alberts, A.S.1    Thorburn, A.M.2    Shenolikar, S.3    Mumby, M.C.4    Feramiscoj, R.5
  • 113
    • 0027251721 scopus 로고
    • The retinoblas toma protein associates with the protein phosphatase Type 1 catalytic subunit
    • DURFEE T, BECHERER K, CHEN P-L etal: The retinoblas toma protein associates with the protein phosphatase Type 1 catalytic subunit. GenesDev. (1993) 7:555-569.
    • (1993) GenesDev. , vol.7 , pp. 555-569
    • Durfee, T.1    Becherer, K.2    Chen, P.-L.3
  • 114
    • 0003141398 scopus 로고
    • Phosphorylation of protein phosphatase 1 by cyclin-dependent kinases: A novel mechanism for cell cycle control?
    • BERNDT N: Phosphorylation of protein phosphatase 1 by cyclin-dependent kinases: a novel mechanism for cell cycle control? Adv. Prot. Phosphatases (1995) 9:63-86.
    • (1995) Adv. Prot. Phosphatases , vol.9 , pp. 63-86
    • Berndt, N.1
  • 115
    • 0028214026 scopus 로고
    • Phosphorylation and inactivation of protein phosphatase 1 by cyclin-dependent kinases
    • DOHADWALA M, DA CRUZ E SILVA EF, HALL FL et al: Phosphorylation and inactivation of protein phosphatase 1 by cyclin-dependent kinases. Proc. Natl. Acad. Sci. USA (1994) 91:6408-6412.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6408-6412
    • Dohadwala, M.1    Cruz E, D.A.2    Silva, E.F.3    Hall, F.L.4
  • 116
    • 0031172801 scopus 로고    scopus 로고
    • Constitutively active protein phosphatase 1a causes Rb-dependent G1 arrest in human cancer cells
    • BERNDT N, DOHADWALA M, LIU CWY: Constitutively active protein phosphatase 1a causes Rb-dependent G1 arrest in human cancer cells. Curr. Biol. (1997) 7:375-386.
    • (1997) Curr. Biol. , vol.7 , pp. 375-386
    • Berndt, N.1    Dohadwala, M.2    Cwy, L.3
  • 118
    • 0033515543 scopus 로고    scopus 로고
    • Discovery of a regulatory motif which controls the exposure of specific upstream CDK sites that determine both conformation and growth suppressing activity of pRb
    • DRISCOLL B, T'ANG A, HU Y-H et al.: Discovery of a regulatory motif which controls the exposure of specific upstream CDK sites that determine both conformation and growth suppressing activity of pRb. J. Biol. Chem. (1999) 274:9463-9471.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9463-9471
    • Driscoll, B.1    T'Ang, A.2    Hu, Y.-H.3
  • 119
    • 0032487925 scopus 로고    scopus 로고
    • Hypoxia-induced pRB hypo-phosphorylation results from downregulation of CDK and upregulation of PP1 activities
    • KRTOLICA A, KRUCHER NA, LUDLOW JW: Hypoxia-induced pRB hypo-phosphorylation results from downregulation of CDK and upregulation of PP1 activities. Oncogene (1998) 17:2295-2304.
    • (1998) Oncogene , vol.17 , pp. 2295-2304
    • Krtolica, A.1    Krucher, N.A.2    Ludlow, J.W.3
  • 120
    • 0025098525 scopus 로고
    • Cell cycle oscillation of phosphatase inhibitor-2 in rat fibroblasts coincident with p34cdc2 restriction
    • BRAUTIGAN DL, SUNWOO J, LABBÉ J-C, FERNANDEZ A, LAMB NJC: Cell cycle oscillation of phosphatase inhibitor-2 in rat fibroblasts coincident with p34cdc2 restriction. Nature (1990) 344:74-78.
    • (1990) Nature , vol.344 , pp. 74-78
    • Brautigan, D.L.1    Sunwoo, J.2    Labbé, J.-C.3    Fernandez, A.4    Lamb, N.J.C.5
  • 121
    • 0031434815 scopus 로고    scopus 로고
    • Multisite phosphorylation and the nuclear localization of phosphatase inhibitor 2-green fluorescent protein fusion protein during S phase of the cell growth cycle
    • KAKINOKI Y, SOMERS J, BRAUTIGAN DL: Multisite phosphorylation and the nuclear localization of phosphatase inhibitor 2-green fluorescent protein fusion protein during S phase of the cell growth cycle. J. Biol. Chem. (1997) 272:32308-32314.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32308-32314
    • Kakinoki, Y.1    Somers, J.2    Brautigan, D.L.3
  • 122
    • 0028003818 scopus 로고
    • Phosphorylation of dis2 protein phosphatase at the C-terminal cdc2 consensus and its potential role in cell cycle regula tion
    • YAMANO H, ISHII K, YANAGIDA M: Phosphorylation of dis2 protein phosphatase at the C-terminal cdc2 consensus and its potential role in cell cycle regula tion. EMBOJ. (1994) 13:5310-5318.
    • (1994) EMBOJ. , vol.13 , pp. 5310-5318
    • Yamano, H.1    Ishii, K.2    Yanagida, M.3
  • 123
    • 0031693120 scopus 로고    scopus 로고
    • Growth arrest of Schizosaccharomyces pombe following overexpression of mouse Type 1 protein phosphatases
    • SANGRADOR A, ANDRES I, EGUIRAUN A, LORENZO ML, ORTIZ JM: Growth arrest of Schizosaccharomyces pombe following overexpression of mouse Type 1 protein phosphatases. Mol. Gen. Genet. (1998) 259:449-456.
    • (1998) Mol. Gen. Genet. , vol.259 , pp. 449-456
    • Sangrador, A.1    Andres, I.2    Eguiraun, A.3    Lorenzo, M.L.4    Ortiz, J.M.5
  • 124
    • 12644291188 scopus 로고    scopus 로고
    • Cell cycle-dependent phosphorylation of mammalian protein phosphatase 1 by cdc2 kinase
    • KWON Y-G, LEE S-Y, CHOI Y, GREENGARD P, NAIRN AC: Cell cycle-dependent phosphorylation of mammalian protein phosphatase 1 by cdc2 kinase. Proc. Natl. Acad. Sci. USA (1997) 94:2168-2173.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2168-2173
    • Kwon, Y.-G.1    Lee, S.-Y.2    Choi, Y.3    Greengard, P.4    Nairn, A.C.5
  • 125
    • 0031569818 scopus 로고    scopus 로고
    • Protein phosphatase-1a, y1 and 8: Changes in phosphorylation and activity in mitotic HeLa cells and in cells released from the mitotic block
    • PUNTONI F, VILLA-MORUZZI E: Protein phosphatase-1a, y1 and 8: changes in phosphorylation and activity in mitotic HeLa cells and in cells released from the mitotic block. Arch. Biochem. Biophys. (1997) 340:177-184.
    • (1997) Arch. Biochem. Biophys. , vol.340 , pp. 177-184
    • Puntoni, F.1    Villa-Moruzzi, E.2
  • 126
    • 0034695599 scopus 로고    scopus 로고
    • Serine/threonine protein phosphatase Type 1y1 is required for the completion of cytokinesis in human A549 lung carcinoma cells
    • CHENG AY, DEAN NM, HONKANEN RE: Serine/threonine protein phosphatase Type 1y1 is required for the completion of cytokinesis in human A549 lung carcinoma cells. J. Biol. Chem. (2000) 275:1846-1854.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1846-1854
    • Cheng, A.Y.1    Dean, N.M.2    Honkanen, R.E.3
  • 127
    • 0026019658 scopus 로고
    • 22+ essential for a midmitotic transition encodes a leucine-rich repeat protein that positively modulates protein phosphatase-1
    • OHKURA H, YANAGIDA M: S. pombe gene sds22+ essential for a midmitotic transition encodes a leucine-rich repeat protein that positively modulates protein phosphatase-1. Cell(1991) 64:149-157.
    • (1991) Cell , vol.64 , pp. 149-157
    • Ohkura, H.1    Yanagida, M.2
  • 128
    • 0031055455 scopus 로고    scopus 로고
    • Identification of sds22 as an inhibitory subunit of protein phosphatase-1 in rat liver nuclei
    • DINISCHIOTU A, BEULLENS M, STALMANS W, BOLLEN M: Identification of sds22 as an inhibitory subunit of protein phosphatase-1 in rat liver nuclei. FEBS Lett. (1997) 402:141-144.
    • (1997) FEBS Lett. , vol.402 , pp. 141-144
    • Dinischiotu, A.1    Beullens, M.2    Stalmans, W.3    Bollen, M.4
  • 129
    • 0031058041 scopus 로고    scopus 로고
    • High molecular weight protein phosphatase Type 1 dephos-phorylates the retinoblastoma protein
    • NELSON DA, KRUCHER NA, LUDLOW JW: High molecular weight protein phosphatase Type 1 dephos-phorylates the retinoblastoma protein. J. Biol. Chem. (1997) 272:4528-4535.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4528-4535
    • Nelson, D.A.1    Krucher, N.A.2    Ludlow, J.W.3
  • 130
    • 0031587943 scopus 로고    scopus 로고
    • Association of protein phosphatase-18 with the retinoblastoma protein and reversible phosphatase activation in mitotic HeLa cells and in cells released from mitosis
    • PUNTONI F, VILLA-MORUZZI E: Association of protein phosphatase-18 with the retinoblastoma protein and reversible phosphatase activation in mitotic HeLa cells and in cells released from mitosis. Biochem. Biophys. Res. Commun. (1997) 235:704-708.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 704-708
    • Puntoni, F.1    Villa-Moruzzi, E.2
  • 131
    • 0026762801 scopus 로고
    • Dephosphorylation of cdc2 on threonine 161 is required for cdc2 kinase inactivation and normal anaphase
    • LORCA T, LABBÉ J-C, DEVAULT A etal: Dephosphorylation of cdc2 on threonine 161 is required for cdc2 kinase inactivation and normal anaphase. EMBO J. (1992) 11:2381-2390.
    • (1992) EMBO J. , vol.11 , pp. 2381-2390
    • Lorca, T.1    Labbé, J.-C.2    Devault, A.3
  • 132
    • 0029953320 scopus 로고    scopus 로고
    • Evidence that the endogenous histone H1 phosphatase in HeLa mitotic chromosomes is protein phosphatase 1, not protein phosphatase 2A.J
    • PAULSON JR, PATZLAFF JS, VALLIS AJ: Evidence that the endogenous histone H1 phosphatase in HeLa mitotic chromosomes is protein phosphatase 1, not protein phosphatase 2A.J. Cell Sci. (1996) 109:1437-1447.
    • (1996) Cell Sci. , vol.109 , pp. 1437-1447
    • Paulson, J.R.1    Patzlaff, J.S.2    Vallis, A.J.3
  • 133
    • 0030669555 scopus 로고    scopus 로고
    • Identification of protein phosphatase 1 as a mitoticlamin phosphatase
    • THOMPSON LJ, BOLLEN M, FIELDS AP: Identification of protein phosphatase 1 as a mitoticlamin phosphatase. J. Biol. Chem. (1997) 272:29693-29697.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29693-29697
    • Thompson, L.J.1    Bollen, M.2    Fields, A.P.3
  • 134
    • 0029826437 scopus 로고    scopus 로고
    • Requirement for PP1 phosphatase and 20S cyclosome/APC for the onset of anaphase is lessened by the dosage increase of a novel gene sds23+
    • ISHII K, KUMADA K, TODA T, YANAGIDA M: Requirement for PP1 phosphatase and 20S cyclosome/APC for the onset of anaphase is lessened by the dosage increase of a novel gene sds23+. EMBO J. (1996) 15:6629-6640.
    • (1996) EMBO J. , vol.15 , pp. 6629-6640
    • Ishii, K.1    Kumada, K.2    Toda, T.3    Yanagida, M.4
  • 135
    • 0025058599 scopus 로고
    • Cdc2 H1 kinase is negatively regulated by a Type 2A phosphatase in the Xenopus early embryonic cell cycle: Evidence from the effects of okadaic acid
    • FÉLIX M-A, COHEN P, KARSENTI E: Cdc2 H1 kinase is negatively regulated by a Type 2A phosphatase in the Xenopus early embryonic cell cycle: evidence from the effects of okadaic acid. EMBOJ. (1990) 9:675-683.
    • (1990) EMBOJ. , vol.9 , pp. 675-683
    • Félix, M.-A.1    Cohen, P.2    Karsenti, E.3
  • 136
    • 0027538301 scopus 로고
    • Dephosphorylation of cdc25-C by a Type 2A protein phosphatase: Specific regulation during the cell cycle in Xenopuseggextracts
    • CLARKE PR, HOFFMANN I, DRAETTA G, KARSENTI E: Dephosphorylation of cdc25-C by a Type 2A protein phosphatase: specific regulation during the cell cycle in Xenopuseggextracts. Mol.Biol. Cell(1993) 4:397-411.
    • (1993) Mol.Biol. Cell , vol.4 , pp. 397-411
    • Clarke, P.R.1    Hoffmann, I.2    Draetta, G.3    Karsenti, E.4
  • 137
  • 138
    • 0024996931 scopus 로고
    • Distinct, essential roles of Type 1 and 2Aprotein phosphatases in the control of the fission yeast cell division cycle
    • KINOSHITA N, OHKURA H, YANAGIDA M: Distinct, essential roles of Type 1 and 2Aprotein phosphatases in the control of the fission yeast cell division cycle. Cell (1990) 63:405-415.
    • (1990) Cell , vol.63 , pp. 405-415
    • Kinoshita, N.1    Ohkura, H.2    Yanagida, M.3
  • 139
    • 0031031397 scopus 로고    scopus 로고
    • HOX11 interacts with protein phosphatases PP2Aand PP1 and disrupts a G2/M cell-cycle checkpoint
    • KAWABE T, MUSLIN AJ, KORSMEYER SJ: HOX11 interacts with protein phosphatases PP2Aand PP1 and disrupts a G2/M cell-cycle checkpoint. Nature (1997) 385:454-458.
    • (1997) Nature , vol.385 , pp. 454-458
    • Kawabe, T.1    Muslin, A.J.2    Korsmeyer, S.J.3
  • 141
    • 0030755955 scopus 로고    scopus 로고
    • Protein phosphatase 2Ainhibits nuclear telomerase activity in human breast cancer cells
    • LI H, ZHAO L-L, FUNDER JW, LIU J-P: Protein phosphatase 2Ainhibits nuclear telomerase activity in human breast cancer cells. J. Biol. Chem. (1997) 272:16729-16732.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16729-16732
    • H, L.I.1    Zhao, L.-L.2    Funder, J.W.3    Liu, J.-P.4
  • 142
    • 0031939872 scopus 로고    scopus 로고
    • Telomerase activity, cell proliferation and cancer
    • GREIDER CW: Telomerase activity, cell proliferation and cancer. Proc. Natl. Acad. Sci. USA (1998) 95:90-92.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 90-92
    • Greider, C.W.1
  • 143
    • 0033527642 scopus 로고    scopus 로고
    • Distinct roles for PP1 and PP2Ain phosphorylation of the retinoblastoma protein.J
    • YAN Y, MUMBY MC: Distinct roles for PP1 and PP2Ain phosphorylation of the retinoblastoma protein.J. Biol Chem. (1999) 274:31917-31924.
    • (1999) Biol Chem. , vol.274 , pp. 31917-31924
    • Yan, Y.1    Mumby, M.C.2
  • 144
    • 0029976228 scopus 로고    scopus 로고
    • Positive regulation of cdc2 gene activity by protein phosphatase Type 2A
    • JARAMILLO-BABB VL, SUGARMAN JL, SCAVETTA R et al: Positive regulation of cdc2 gene activity by protein phosphatase Type 2A. J. Biol. Chem. (1996) 271:5988-5992.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5988-5992
    • Jaramillo-Babb, V.L.1    Sugarman, J.L.2    Scavetta, R.3
  • 146
    • 0025103372 scopus 로고
    • Polyoma small and middle Tantigens and SV40 small Tantigen form stable complexes with protein phosphatase 2A
    • PALLAS DC, SHAHRIK LK, MARTIN BL et al: Polyoma small and middle Tantigens and SV40 small Tantigen form stable complexes with protein phosphatase 2A. Cell (1990) 60:167-176.
    • (1990) Cell , vol.60 , pp. 167-176
    • Pallas, D.C.1    Shahrik, L.K.2    Martin, B.L.3
  • 147
    • 0025366151 scopus 로고
    • Association of protein phosphatase 2Awith polyoma virus medium tumor antigen
    • WALTER G, RUEDIGER R, SLAUGHTER C, MUMBY MC: Association of protein phosphatase 2Awith polyoma virus medium tumor antigen. Proc. Natl. Acad. Sci. USA (1990) 87:2521-2525.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2521-2525
    • Walter, G.1    Ruediger, R.2    Slaughter, C.3    Mumby, M.C.4
  • 149
    • 0027772552 scopus 로고
    • The interaction of SV40 small tumor antigen with protein phosphatase 2Astimulates the Map kinase pathway and induces cell proliferation
    • SONTAG E, FEDOROV S, KAMABAYASHI C, ROBBINS D, COBB MH, MUMBY MC: The interaction of SV40 small tumor antigen with protein phosphatase 2Astimulates the Map kinase pathway and induces cell proliferation. Cell (1993) 75:887-897.
    • (1993) Cell , vol.75 , pp. 887-897
    • Sontag, E.1    Fedorov, S.2    Kamabayashi, C.3    Robbins, D.4    Cobb, M.H.5    Mumby, M.C.6
  • 150
    • 0026786471 scopus 로고
    • Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation
    • CHEN J, MARTIN BL, BRAUTIGAN DL: Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation. Science (1992) 257:1261-1264.
    • (1992) Science , vol.257 , pp. 1261-1264
    • Chen, J.1    Martin, B.L.2    Brautigan, D.L.3
  • 151
    • 0028237871 scopus 로고
    • Tyrosine phospho rylation of protein phosphatase 2A in response to growth stimulation and v-src transformation of fibroblasts
    • CHEN J, PARSONS S, BRAUTIGAN DL: Tyrosine phospho rylation of protein phosphatase 2A in response to growth stimulation and v-src transformation of fibroblasts. J. Biol. Chem. (1994) 269:7957-7962.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7957-7962
    • Chen, J.1    Parsons, S.2    Brautigan, D.L.3
  • 152
    • 0029889342 scopus 로고    scopus 로고
    • The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A
    • LI M, MAKKINJE A, DAMUNI Z: The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A. J. Biol. Chem. (1996) 271:11059-11062.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11059-11062
    • M, L.I.1    Makkinje, A.2    Damuni, Z.3
  • 153
    • 0033565895 scopus 로고    scopus 로고
    • Expression of I2PP2A, inhibitor of protein phosphatase 2A, induces c-Jun and AP-1 activity
    • AL-MURRANI SWK, WOODGETT JR, DAMUNI Z: Expression of I2PP2A, inhibitor of protein phosphatase 2A, induces c-Jun and AP-1 activity. Biochem. J. (1999) 341:293-298.
    • (1999) Biochem. J. , vol.341 , pp. 293-298
    • Al-Murrani, S.W.K.1    Woodgett, J.R.2    Damuni, Z.3
  • 154
    • 0345517990 scopus 로고    scopus 로고
    • Reduction of Ha-ras-induced cellular transformation by elevated expression of protein phosphatase 2A
    • BAHARIANS Z, SCHÖNTHAL AH: Reduction of Ha-ras-induced cellular transformation by elevated expression of protein phosphatase 2A. Mol. Carcinog. (1999) 24:246-254.
    • (1999) Mol. Carcinog. , vol.24 , pp. 246-254
    • Baharians, Z.1    Schönthal, A.H.2
  • 155
    • 0028200722 scopus 로고
    • + in fission yeast: Mutant defects in cytokinesis, cell polarity, mating and spindle pole body positioning.J
    • YOSHIDA T, TODA T, YANAGIDA M: A calcineurin-like gene ppb1 + in fission yeast: Mutant defects in cytokinesis, cell polarity, mating and spindle pole body positioning.J. Cell Sci. (1994) 107:1725-1735.
    • (1994) Cell Sci. , vol.107 , pp. 1725-1735
    • Yoshida, T.1    Toda, T.2    Yanagida, M.3
  • 156
    • 0034214054 scopus 로고    scopus 로고
    • Calcineurin regulation of the mammalian G0/G1 checkpoint element, cyclin dependent kinase 4
    • BAKSH S, DECAPRIO JA, BURAKOFF SJ: Calcineurin regulation of the mammalian G0/G1 checkpoint element, cyclin dependent kinase 4. Oncogene (2000) 19:2820-2827.
    • (2000) Oncogene , vol.19 , pp. 2820-2827
    • Baksh, S.1    Decaprio, J.A.2    Burakoff, S.J.3
  • 157
    • 0030925222 scopus 로고    scopus 로고
    • Wip1, a novel human protein phosphatase that is induced in response to ionizing radiation in a p53-dependent manner
    • FISCELLA M, ZHANG HL, FAN SJ et al.: Wip1, a novel human protein phosphatase that is induced in response to ionizing radiation in a p53-dependent manner. Proc. Natl. Acad. Sci. USA (1997) 94:6048-6053.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6048-6053
    • Fiscella, M.1    Zhang, H.L.2    Fan, S.J.3
  • 158
    • 0030750557 scopus 로고    scopus 로고
    • FIN13, a novel growth factor-inducible serine-threonine phosphatase which can inhibit cell cycle progression
    • GUTHRIDGE MA, BELLOSTA P, TAVOLONIN, BASILICO C: FIN13, a novel growth factor-inducible serine-threonine phosphatase which can inhibit cell cycle progression. Mol. Cell. Biol. (1997) 17:5485-5498.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5485-5498
    • Guthridge, M.A.1    Bellosta, P.2    Tavolonin Basilico, C.3
  • 159
    • 0032524677 scopus 로고    scopus 로고
    • Serine/threonine protein phosphatase Type 5 acts upstream of p53 to regulate the induction of p21WAF1/Cip1 and mediate growth arrest
    • ZUO Z, DEAN NM, HONKANEN RE: Serine/threonine protein phosphatase Type 5 acts upstream of p53 to regulate the induction of p21WAF1/Cip1 and mediate growth arrest. J. Biol. Chem. (1998) 273:12250-12258.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12250-12258
    • Zuo, Z.1    Dean, N.M.2    Honkanen, R.E.3
  • 160
    • 0040370216 scopus 로고    scopus 로고
    • Ser/Thr protein phosphatase Type 5 (PP5) is a negative regulator of glucocorticoid receptor-mediated growth arrest
    • ZUO Z, URBAN G, SCAMMELL JG et al.: Ser/Thr protein phosphatase Type 5 (PP5) is a negative regulator of glucocorticoid receptor-mediated growth arrest. Biochemistry (1999) 38:8849-8857.
    • (1999) Biochemistry , vol.38 , pp. 8849-8857
    • Zuo, Z.1    Urban, G.2    Scammell, J.G.3
  • 161
    • 0030475875 scopus 로고    scopus 로고
    • The novel human protein serine/threonine phosphatase 6 is a functional homologue of budding yeast Sit4p and fission yeast ppe1, which are involved in cell cycle regulation
    • BASTIANS H, PONSTINGL H: The novel human protein serine/threonine phosphatase 6 is a functional homologue of budding yeast Sit4p and fission yeast ppe1, which are involved in cell cycle regulation.J. Cell Sci. (1996) 109:2865-2874.
    • (1996) J. Cell Sci. , vol.109 , pp. 2865-2874
    • Bastians, H.1    Ponstingl, H.2
  • 162
    • 0029125701 scopus 로고
    • Protease activation during apoptosis: Death by a thousand cuts?
    • MARTIN SJ, GREEN DR: Protease activation during apoptosis: death by a thousand cuts? Cell (1995) 82:349-352.
    • (1995) Cell , vol.82 , pp. 349-352
    • Martin, S.J.1    Green, D.R.2
  • 163
    • 0032055256 scopus 로고    scopus 로고
    • Different moieties of tautomycin involved in protein phosphatase inhibition and induction of apoptosis
    • KAWAMURA T, MATSUZAWA S, MIZUNO Y et al.: Different moieties of tautomycin involved in protein phosphatase inhibition and induction of apoptosis. Biochem. Pharmacol. (1998) 55:995-1003.
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 995-1003
    • Kawamura, T.1    Matsuzawa, S.2    Mizuno, Y.3
  • 164
    • 0026534111 scopus 로고
    • Specific protein dephosphory-lation in apoptosis induced by ionizing radiation and heat shock in human tumor lines
    • BAXTER GD, LAVIN MF: Specific protein dephosphory-lation in apoptosis induced by ionizing radiation and heat shock in human tumor lines. J. Immunol. (1992) 148:1949-1954.
    • (1992) J. Immunol. , vol.148 , pp. 1949-1954
    • Baxter, G.D.1    Lavin, M.F.2
  • 165
    • 0028986269 scopus 로고
    • Serine/threonine protein phosphatase is required for tobacco mosaic virus-mediated programmed cell death
    • DUNIGAN DD, MADLENER JC: Serine/threonine protein phosphatase is required for tobacco mosaic virus-mediated programmed cell death. Virology (1995) 207:460-466.
    • (1995) Virology , vol.207 , pp. 460-466
    • Dunigan, D.D.1    Madlener, J.C.2
  • 166
    • 0030462563 scopus 로고    scopus 로고
    • Specific cleavage of the retinoblastoma protein by an ICE-like protease in apoptosis
    • JÄNICKE RU, WALKER PA, LIN XY, PORTER AG: Specific cleavage of the retinoblastoma protein by an ICE-like protease in apoptosis. EMBO J. (1996) 15:6969-6978.
    • (1996) EMBO J. , vol.15 , pp. 6969-6978
    • Jänicke, R.U.1    Walker, P.A.2    Lin, X.Y.3    Porter, A.G.4
  • 167
    • 0030999788 scopus 로고    scopus 로고
    • Apoptosis is associated with cleavage of a 5 kDa fragment from RB which mimics dephosphorylation and modulates E2F binding
    • CHEN W, OTTERSON GA, LIPKOWITZ S, KHLEIF SN, COXON AB, KAYE FJ: Apoptosis is associated with cleavage of a 5 kDa fragment from RB which mimics dephosphorylation and modulates E2F binding. Oncogene (1997) 14:1243-1248.
    • (1997) Oncogene , vol.14 , pp. 1243-1248
    • Chen, W.1    Otterson, G.A.2    Lipkowitz, S.3    Khleif, S.N.4    Coxon, A.B.5    Kaye, F.J.6
  • 168
    • 0030899360 scopus 로고    scopus 로고
    • Degradation of retinoblastoma protein in tumor necrosis factor-and CD95-induced cell death
    • TAN X, MARTIN SJ, GREEN DR, WANG JYJ: Degradation of retinoblastoma protein in tumor necrosis factor-and CD95-induced cell death. J. Biol. Chem. (1997) 272:9613-9616.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9613-9616
    • Tan, X.1    Martin, S.J.2    Green, D.R.3    Wang, J.Y.J.4
  • 169
    • 0034720190 scopus 로고    scopus 로고
    • Caspase-dependent cleavage of the retinoblastoma protein is an early step in neuronal apoptosis
    • BOUTILLIER A-L, TRINH E, LOEFFLER J-P: Caspase-dependent cleavage of the retinoblastoma protein is an early step in neuronal apoptosis. Oncogene (2000) 19:2171-2178.
    • (2000) Oncogene , vol.19 , pp. 2171-2178
    • Boutillier, A.-L.1    Trinh, E.2    Loeffler, J.-P.3
  • 170
    • 0029052647 scopus 로고
    • Induction of a retinoblastoma phosphatase activity by anticancer drugs accompa nies p53-independent G1 arrest and apoptosis
    • DOU QP, AN B, WILL PL: Induction of a retinoblastoma phosphatase activity by anticancer drugs accompa nies p53-independent G1 arrest and apoptosis. Proc. Natl. Acad. Sci. USA (1995) 92:9019-9023.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9019-9023
    • Dou, Q.P.1    B, A.N.2    Will, P.L.3
  • 171
    • 0029897419 scopus 로고    scopus 로고
    • The involvement of protein phosphatases in the activation of ICE/CED-3 protease, intracellular acidification, DNA digestion and apoptosis
    • MORANA SJ, WOLF CM, LI J, REYNOLDS JE, BROWN MK, EASTMAN A: The involvement of protein phosphatases in the activation of ICE/CED-3 protease, intracellular acidification, DNA digestion and apoptosis. J. Biol. Chem. (1996) 271:18263-18271.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18263-18271
    • Morana, S.J.1    Wolf, C.M.2    J, L.I.3    Reynolds, J.E.4    Brown, M.K.5    Eastman, A.6
  • 172
    • 0033575960 scopus 로고    scopus 로고
    • The retinoblastoma tumor suppressor inhibits cellular proliferation through two distinct mechanisms: Inhibition of cell cycle progression and induction of cell death
    • KNUDSEN KE, WEBER E, ARDEN KC, CAVENEE WK, FERAMISCO JR, KNUDSEN ES: The retinoblastoma tumor suppressor inhibits cellular proliferation through two distinct mechanisms: inhibition of cell cycle progression and induction of cell death. Oncogene (1999) 18:5239-5245.
    • (1999) Oncogene , vol.18 , pp. 5239-5245
    • Knudsen, K.E.1    Weber, E.2    Arden, K.C.3    Cavenee, W.K.4    Feramisco, J.R.5    Knudsen, E.S.6
  • 173
    • 0033539931 scopus 로고    scopus 로고
    • Protein phosphatase-1 activation and association with the retinoblastoma protein in colcemid-induced apoptosis
    • PUNTONI F, VILLA-MORUZZI E: Protein phosphatase-1 activation and association with the retinoblastoma protein in colcemid-induced apoptosis. Biochem. Biophys. Res. Commun. (1999) 266:279-283.
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 279-283
    • Puntoni, F.1    Villa-Moruzzi, E.2
  • 174
    • 0342657806 scopus 로고    scopus 로고
    • Protein phosphatase 1a is a ras-activated Bad phosphatase that regulates interleukin-2 deprivation-induced apoptosis
    • AYLLÓN V, MARTÍNEZ AC, GARCÍA A, CAYLA X, REBOLLO A: Protein phosphatase 1a is a ras-activated Bad phosphatase that regulates interleukin-2 deprivation-induced apoptosis. EMBO J. (2000) 19:2237-2246.
    • (2000) EMBO J. , vol.19 , pp. 2237-2246
    • Ayllón, V.1    Martínez, A.C.2    García, A.3    Cayla, X.4    Rebollo, A.5
  • 175
    • 0031913730 scopus 로고    scopus 로고
    • Activation of a PP2A-like phosphatase and dephosphorylation of tau protein characterize onset of the execution phase of apoptosis
    • MILLS JC, LEE VMY, PITTMAN RN: Activation of a PP2A-like phosphatase and dephosphorylation of tau protein characterize onset of the execution phase of apoptosis.J. Cell Sci. (1998) 111:625-636.
    • (1998) J. Cell Sci. , vol.111 , pp. 625-636
    • Mills, J.C.1    Lee, V.M.Y.2    Pittman, R.N.3
  • 177
    • 0027994349 scopus 로고
    • The sphingomeylin cycle and the second messenger function of ceramide
    • HANNUN YA: The sphingomeylin cycle and the second messenger function of ceramide. J. Biol. Chem. (1994) 269:3125-3128.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3125-3128
    • Hannun, Y.A.1
  • 178
    • 0030959304 scopus 로고    scopus 로고
    • Bcl-2 phosphorylation required for anti-apoptosis function
    • ITO T, DENG X, CARR B, MAY WS: Bcl-2 phosphorylation required for anti-apoptosis function. J. Biol. Chem. (1997) 272:11671-11673.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11671-11673
    • Ito, T.1    Deng, X.2    Carr, B.3    May, W.S.4
  • 179
    • 0032566717 scopus 로고    scopus 로고
    • Afunctional role for mitochondrial protein kinase C(X in Bcl2 phosphorylation and suppression of apoptosis
    • RUVOLO PP, DENG X, CARR BK, MAY WS: Afunctional role for mitochondrial protein kinase C(X in Bcl2 phosphorylation and suppression of apoptosis. J. Biol. Chem. (1998) 273:25436-25442.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25436-25442
    • Ruvolo, P.P.1    Deng, X.2    Carr, B.K.3    May, W.S.4
  • 180
    • 0343457526 scopus 로고    scopus 로고
    • Reversible phosphorylation of Bcl2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A
    • DENG XM, ITO T, CARR B, MUMBY MC, MAY WS: Reversible phosphorylation of Bcl2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A. J. Biol. Chem. (1998) 273:34157-34163.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34157-34163
    • Deng, X.M.1    Ito, T.2    Carr, B.3    Mumby, M.C.4    May, W.S.5
  • 181
    • 0033575320 scopus 로고    scopus 로고
    • Ceramide induces bcl2 dephosphorylation via a mechanism involving mitochondrial PP2A
    • RUVOLO PP, DENGX, ITO T, CARB K, MAY WS: Ceramide induces bcl2 dephosphorylation via a mechanism involving mitochondrial PP2A. J. Biol. Chem. (1999) 274:20292-20300.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20292-20300
    • Ruvolo, P.P.1    Dengx Ito, T.2    Carb, K.3    May, W.S.4
  • 182
    • 14444273908 scopus 로고    scopus 로고
    • Regulation of protein phosphatase 2A activity by caspase-3 during apoptosis
    • SANTORO MF, ANNAND RR, ROBERTSON MM et al.: Regulation of protein phosphatase 2A activity by caspase-3 during apoptosis. J. Biol. Chem. (1998) 273:13119-13128.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13119-13128
    • Santoro, M.F.1    Annand, R.R.2    Robertson, M.M.3
  • 183
    • 0028971035 scopus 로고
    • 2+-activated cell death in mammalian cells
    • SHIBASAKI F, MCKEON F: Calcineurin functions in Ca2+-activated cell death in mammalian cells. J. Cell Biol. (1995) 131:735-743.
    • (1995) J. Cell Biol. , vol.131 , pp. 735-743
    • Shibasaki, F.1    McKeon, F.2
  • 184
    • 0033537768 scopus 로고    scopus 로고
    • 2+-induced apoptosis through calcineurin dephosphorylation of BAD
    • WANG HG, PATHAN N, ETHELL IM et al.: Ca2+-induced apoptosis through calcineurin dephosphorylation of BAD. Science (1999) 284:339-343.
    • (1999) Science , vol.284 , pp. 339-343
    • Wang, H.G.1    Pathan, N.2    Ethell, I.M.3
  • 185
    • 0033607543 scopus 로고    scopus 로고
    • High level calcineurin activity predisposes neuronal cells to apoptosis
    • ASAI A, QIU JH, NARITA Y et al.: High level calcineurin activity predisposes neuronal cells to apoptosis. J. Biol Chem. (1999) 274:34450-34458.
    • (1999) J. Biol Chem. , vol.274 , pp. 34450-34458
    • Asai, A.1    Qiu, J.H.2    Narita, Y.3
  • 186
    • 0030391148 scopus 로고    scopus 로고
    • Protein phosphatases-1 and-2A regulate tumor cell migration, invasion and cytoskeletal organization
    • YOUNG MRI: Protein phosphatases-1 and-2A regulate tumor cell migration, invasion and cytoskeletal organization. Adv. Exp. Med. Biol. (1996) 407:311-318.
    • (1996) Adv. Exp. Med. Biol. , vol.407 , pp. 311-318
    • Young, M.R.I.1
  • 187
    • 0345267245 scopus 로고    scopus 로고
    • Protein phosphatase-2A associates with the cytoskeleton to maintain cell spreading and reduced motility of nonmetastatic Lewis lung carcinoma cells: The loss of this regulatory control in metastatic cells
    • JACKSON J, MEISINGER J, PATEL S et al.: Protein phosphatase-2A associates with the cytoskeleton to maintain cell spreading and reduced motility of nonmetastatic Lewis lung carcinoma cells: the loss of this regulatory control in metastatic cells. Invasion Metastasis (1998) 17:199-209.
    • (1998) Invasion Metastasis , vol.17 , pp. 199-209
    • Jackson, J.1    Meisinger, J.2    Patel, S.3
  • 188
    • 0345267246 scopus 로고    scopus 로고
    • Endothelial cell response to human head and neck squamous cell carcinomas involves downregula-tion of protein phosphatases-1/2A, cytoskeletal depolymerization and increased motility
    • BENEFIELD J, MEISINGER J, PETRUZZELLI GJ, YOUNG MRI: Endothelial cell response to human head and neck squamous cell carcinomas involves downregula-tion of protein phosphatases-1/2A, cytoskeletal depolymerization and increased motility. Invasion Metastasis (1998) 17:210-220.
    • (1998) Invasion Metastasis , vol.17 , pp. 210-220
    • Benefield, J.1    Meisinger, J.2    Petruzzelli, G.J.3    Young, M.R.I.4
  • 189
    • 0034651747 scopus 로고    scopus 로고
    • A truncated isoform of the PP2A B56 subunit promotes cell motility through paxillin phosphorylation
    • ITO A, KATAOKA TR, WATANABE M et al: A truncated isoform of the PP2A B56 subunit promotes cell motility through paxillin phosphorylation. EMBO J. (2000) 19:562-571.
    • (2000) EMBO J. , vol.19 , pp. 562-571
    • Ito, A.1    Kataoka, T.R.2    Watanabe, M.3
  • 190
    • 0030807904 scopus 로고    scopus 로고
    • Cell cycle progression, growth and patterning in imaginal discs despite inhibition of cell division after inactivation of Drosophila Cdc2 kinase
    • WEIGMANN K, COHEN SM, LEHNER CF: Cell cycle progression, growth and patterning in imaginal discs despite inhibition of cell division after inactivation of Drosophila Cdc2 kinase. Development (1997) 124:3555-3563.
    • (1997) Development , vol.124 , pp. 3555-3563
    • Weigmann, K.1    Cohen, S.M.2    Lehner, C.F.3
  • 191
    • 0032568795 scopus 로고    scopus 로고
    • Coordination of growth and cell division in the Drosophilawing
    • NEUFELD TP, FLOR DE LA CRUZ A, JOHNSTON LA, EDGAR BA: Coordination of growth and cell division in the Drosophilawing. Cell (1998) 93:1183-1193.
    • (1998) Cell , vol.93 , pp. 1183-1193
    • Neufeld, T.P.1    Flor De La Cruz, A.2    Johnston, L.A.3    Edgar, B.A.4
  • 192
    • 0033258521 scopus 로고    scopus 로고
    • Cell-autonomous regulation of cell and organ growth in Drosophila by Akt/PKB
    • VERDU J, BURATOVICH MA, WILDER EL, BIRNBAUM MJ: Cell-autonomous regulation of cell and organ growth in Drosophila by Akt/PKB. Nature Cell Biol. (1999) 1:500-506.
    • (1999) Nature Cell Biol. , vol.1 , pp. 500-506
    • Verdu, J.1    Buratovich, M.A.2    Wilder, E.L.3    Birnbaum, M.J.4
  • 193
    • 0033572644 scopus 로고    scopus 로고
    • Drosophila tumor suppressor PTEN controls cell size and number by antagonizing the Chico/PI3-kinase signaling pathway
    • GOBERDHAN DCI, PARICIO N, GOODMAN EC, MLODZIK M, WILSON C: Drosophila tumor suppressor PTEN controls cell size and number by antagonizing the Chico/PI3-kinase signaling pathway. Genes Dev. (1999) 13:3244-3258.
    • (1999) Genes Dev. , vol.13 , pp. 3244-3258
    • Goberdhan, D.C.I.1    Paricio, N.2    Goodman, E.C.3    Mlodzik, M.4    Wilson, C.5
  • 194
    • 0033257556 scopus 로고    scopus 로고
    • From small flies come big discoveries about size control
    • EDGAR BA: From small flies come big discoveries about size control. Nature Cell Biol. (1999) 1:E191-E193.
    • (1999) Nature Cell Biol. , vol.1
    • Edgar, B.A.1
  • 195
    • 0026509456 scopus 로고
    • Is the inhibition of protein phosphatase 1 and 2A activities a general mechanism of tumor promotion in human cancer development?
    • FUJIKI H: Is the inhibition of protein phosphatase 1 and 2A activities a general mechanism of tumor promotion in human cancer development? Mol. Carcinog. (1992) 5:91-94.
    • (1992) Mol. Carcinog. , vol.5 , pp. 91-94
    • Fujiki, H.1
  • 196
    • 0032500792 scopus 로고    scopus 로고
    • Alterations of the PPP2R1B gene in human lung and colon cancer
    • WANG SS, ESPLIN ED, LI JL et al.: Alterations of the PPP2R1B gene in human lung and colon cancer. Science (1998) 282:284-287.
    • (1998) Science , vol.282 , pp. 284-287
    • Wang, S.S.1    Esplin, E.D.2    Jl, L.I.3
  • 197
    • 0034708257 scopus 로고    scopus 로고
    • Low frequency of alterations of the a (PPP2R1A) and P (PPP2R1B) isoforms of the subunit A of the serine-threonine phosphatase 2Ain human neoplasms
    • CALIN GA, DIIASIO MG, CAPRINI E et al: Low frequency of alterations of the a (PPP2R1A) and P (PPP2R1B) isoforms of the subunit A of the serine-threonine phosphatase 2Ain human neoplasms. Oncogene (2000) 19:1191-1195.
    • (2000) Oncogene , vol.19 , pp. 1191-1195
    • Calin, G.A.1    Diiasio, M.G.2    Caprini, E.3
  • 198
    • 0034628568 scopus 로고    scopus 로고
    • Somatic mutations and genetic polymorphisms of the PPP1R3 gene in patients with several types of cancers
    • TAKAKURA S, KOHNO T, SHIMIZU K, OHWADA S, OKAMOTO A, YOKOTA J: Somatic mutations and genetic polymorphisms of the PPP1R3 gene in patients with several types of cancers. Oncogene (2000) 19:836-840.
    • (2000) Oncogene , vol.19 , pp. 836-840
    • Takakura, S.1    Kohno, T.2    Shimizu, K.3    Ohwada, S.4    Okamoto, A.5    Yokota, J.6
  • 199
    • 0032514680 scopus 로고    scopus 로고
    • Delayed embryonic lethality in mice lacking protein phosphatase 2A catalytic subunit C(X
    • GOTZ J, PROBST A, EHLER E, HEMMINGS BA, KUES W: Delayed embryonic lethality in mice lacking protein phosphatase 2A catalytic subunit C(X. Proc. Natl. Acad. Sci. USA (1998) 95:12370-12375.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12370-12375
    • Gotz, J.1    Probst, A.2    Ehler, E.3    Hemmings, B.A.4    Kues, W.5
  • 200
    • 0028043251 scopus 로고
    • Enhanced expression of catalytic subunits of protein phosphatase Type 1 and high S-phase fraction in liposarcoma
    • SOGAWA K, YAMADA T, MASAKI T et al.: Enhanced expression of catalytic subunits of protein phosphatase Type 1 and high S-phase fraction in liposarcoma. Res. Commun. Mol. Pathol. Pharmacol. (1994) 85:359-362.
    • (1994) Res. Commun. Mol. Pathol. Pharmacol. , vol.85 , pp. 359-362
    • Sogawa, K.1    Yamada, T.2    Masaki, T.3
  • 201
    • 0028171242 scopus 로고
    • Enhanced expression of catalytic subunit isoform PP1γ1 of protein phosphatase Type 1 in malignant fibrous histiocytoma
    • YAMADA T, SOGAWA K, MASAKI T et al.: Enhanced expression of catalytic subunit isoform PP1γ1 of protein phosphatase Type 1 in malignant fibrous histiocytoma. Res. Commun. Mol. Pathol. Pharmacol. (1994) 86:125-128.
    • (1994) Res. Commun. Mol. Pathol. Pharmacol. , vol.86 , pp. 125-128
    • Yamada, T.1    Sogawa, K.2    Masaki, T.3
  • 202
    • 0028670098 scopus 로고
    • Selective increase in expression of isoform PP1γ1 of type-1 protein phosphatase in chondrosarcoma cells
    • SOGAWA K, YAMADA T, FUNAMOTO Y et al.: Selective increase in expression of isoform PP1γ1 of type-1 protein phosphatase in chondrosarcoma cells. Res. Commun. Mol. Pathol. Pharmacol. (1994) 86:375-378.
    • (1994) Res. Commun. Mol. Pathol. Pharmacol. , vol.86 , pp. 375-378
    • Sogawa, K.1    Yamada, T.2    Funamoto, Y.3
  • 203
    • 0028966023 scopus 로고
    • Enhanced expression of catalytic subunit isoform PP1γ1 of protein phosphatase Type 1 associated with malignancy of osteogenic tumor
    • SOGAWA K, YAMADA T, OKA S et al.: Enhanced expression of catalytic subunit isoform PP1γ1 of protein phosphatase Type 1 associated with malignancy of osteogenic tumor. Cancer Lett. (1995) 89:1-6.
    • (1995) Cancer Lett. , vol.89 , pp. 1-6
    • Sogawa, K.1    Yamada, T.2    Oka, S.3
  • 204
    • 0031590974 scopus 로고    scopus 로고
    • Enhanced expression of PP1γ1, a catalytic subunit isoform of protein phosphatase Type 1, in invasive ductal carcinomaofthebreast
    • SOGAWA K, MASAKI T, MIYAUCHI A et al.: Enhanced expression of PP1γ1, a catalytic subunit isoform of protein phosphatase Type 1, in invasive ductal carcinomaofthebreast. Cancer Lett. (1997) 112:263-268.
    • (1997) Cancer Lett. , vol.112 , pp. 263-268
    • Sogawa, K.1    Masaki, T.2    Miyauchi, A.3
  • 205
    • 0030941460 scopus 로고    scopus 로고
    • Ras signalling linked to the cell-cycle machinery by the retinoblas-toma protein
    • PEEPER DS, UPTON TM, LADHA MH et al.: Ras signalling linked to the cell-cycle machinery by the retinoblas-toma protein. Nature (1997) 386:177-180.
    • (1997) Nature , vol.386 , pp. 177-180
    • Peeper, D.S.1    Upton, T.M.2    Ladha, M.H.3
  • 206
    • 0031105404 scopus 로고    scopus 로고
    • Ras signalling is required for inactivation of the tumor suppressor pRb cell-cycle control protein
    • MITTNACHT S, PATERSON H, OLSON MF, MARSHALL CJ: Ras signalling is required for inactivation of the tumor suppressor pRb cell-cycle control protein. Curr. Biol. (1997) 7:219-221.
    • (1997) Curr. Biol. , vol.7 , pp. 219-221
    • Mittnacht, S.1    Paterson, H.2    Olson, M.F.3    Marshall, C.J.4
  • 207
    • 0028859923 scopus 로고
    • Cell cycle-dependent phosphorylation and dephosphorylation of the yeast DNA polymerase α-primaseBsubunit
    • FOIANI M, LIBERI G, LUCCHINI G, PLEVANI P: Cell cycle-dependent phosphorylation and dephosphorylation of the yeast DNA polymerase α-primaseBsubunit.Mol. Cell. Biol. (1995) 15:883-891.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 883-891
    • Foiani, M.1    Liberi, G.2    Lucchini, G.3    Plevani, P.4
  • 208
    • 0028784314 scopus 로고
    • Cell cycle phase-specific phosphorylation of human topoisomerase IIα
    • WELLS NJ, FRY AM, GUANO F, NORBURY C, HICKSON ID: Cell cycle phase-specific phosphorylation of human topoisomerase IIα. J. Biol. Chem. (1995) 270:28357-28363.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28357-28363
    • Wells, N.J.1    Fry, A.M.2    Guano, F.3    Norbury, C.4    Hickson, I.D.5
  • 209
    • 0026653422 scopus 로고
    • Transcrip-tional attenuation following cAMP induction requires PP-1-mediated dephosphorylation of CREB
    • HAGIWARA M, ALBERTS AS, BRINDLE P et al.: Transcrip-tional attenuation following cAMP induction requires PP-1-mediated dephosphorylation of CREB. Cell (1992) 70:105-113.
    • (1992) Cell , vol.70 , pp. 105-113
    • Hagiwara, M.1    Alberts, A.S.2    Brindle, P.3
  • 210
  • 211
    • 0030868950 scopus 로고    scopus 로고
    • cdc2
    • TRZEPACZ C, LOWY AM, KORDICH JJ, GRODEN J: Phosphorylation of the tumor suppressor adenoma-tous polyposis coli (APC) by the cyclin-dependent kinase p34cdc2. J. Biol. Chem. (1997) 272:21681-21684.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21681-21684
    • Trzepacz, C.1    Lowy, A.M.2    Kordich, J.J.3    Groden, J.4
  • 214
    • 0028881866 scopus 로고
    • The Rb2/p130 gene product is a nuclear protein whose phosphoryla-tion is cell cycle regulated
    • BALDI A, DELUCA A, CLAUDIO PP et al.: The Rb2/p130 gene product is a nuclear protein whose phosphoryla-tion is cell cycle regulated. J. Cell. Biochem. (1995) 59:402-408.
    • (1995) J. Cell. Biochem. , vol.59 , pp. 402-408
    • Baldi, A.1    Deluca, A.2    Claudio, P.P.3
  • 215
    • 0029987651 scopus 로고    scopus 로고
    • BRCA1 is a 220-kDa nuclear phosphoprotein that is expressed and phosphorylated in a cell cycle-dependent manner
    • CHEN Y, FARMER AA, CHEN C-F, JONES DC, CHEN P-L, LEE W-H: BRCA1 is a 220-kDa nuclear phosphoprotein that is expressed and phosphorylated in a cell cycle-dependent manner. Cancer Res. (1996) 56:3168-3172.
    • (1996) Cancer Res. , vol.56 , pp. 3168-3172
    • Chen, Y.1    Farmer, A.A.2    Chen, C.-F.3    Jones, D.C.4    Chen, P.-L.5    Lee, W.-H.6
  • 216
    • 0032101295 scopus 로고    scopus 로고
    • Differential subcellular localization of protein phosphatase-1 a, y1 and 8 isoforms during both interphase and mitosis in mammalian cells.J
    • ANDREASSEN PR, LACROIX FB, VILLA-MORUZZI E, MARGOLIS RL: Differential subcellular localization of protein phosphatase-1 a, y1 and 8 isoforms during both interphase and mitosis in mammalian cells.J. Cell Biol. (1998) 141:1207-1215.
    • (1998) Cell Biol. , vol.141 , pp. 1207-1215
    • Andreassen, P.R.1    Lacroix, F.B.2    Villa-Moruzzi, E.3    Margolis, R.L.4
  • 217
    • 0032573068 scopus 로고    scopus 로고
    • BRCA1 is associated with the centrosome during mitosis
    • HSU L-C, WHITE RL: BRCA1 is associated with the centrosome during mitosis. Proc. Natl. Acad. Sci. USA (1998) 95:12983-12988.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12983-12988
    • Hsu, L.-C.1    White, R.L.2
  • 219
    • 0032528624 scopus 로고    scopus 로고
    • Fostriecin-mediated G2-M-phase growth arrest correlates with abnormal centrosome replication, the formation of aberrant mitotic spindles and the inhibition of serine/threonine protein phosphatase activity
    • CHENG AY, BALCZON R, ZUO Z, KOONS JS, WALSH AH, HONKANEN RE: Fostriecin-mediated G2-M-phase growth arrest correlates with abnormal centrosome replication, the formation of aberrant mitotic spindles and the inhibition of serine/threonine protein phosphatase activity. Cancer Res. (1998) 58:3611-3619.
    • (1998) Cancer Res. , vol.58 , pp. 3611-3619
    • Cheng, A.Y.1    Balczon, R.2    Zuo, Z.3    Koons, J.S.4    Walsh, A.H.5    Honkanen, R.E.6
  • 220
    • 0030949419 scopus 로고    scopus 로고
    • Antisense to cyclin D1 inhibits the growth and tumorigenicity of human colon cancer cells
    • ARBER N, DOKI Y, HAN EKH et al.: Antisense to cyclin D1 inhibits the growth and tumorigenicity of human colon cancer cells. Cancer Res. (1997) 57:1569-1574.
    • (1997) Cancer Res. , vol.57 , pp. 1569-1574
    • Arber, N.1    Doki, Y.2    Ekh, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.