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Volumn 10, Issue 8, 1999, Pages 2703-2734

Molecular interaction map of the mammalian cell cycle control and DNA repair systems

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; CYCLIN D1; CYCLINE; PROTEIN; PROTEIN MDM2; PROTEIN P53; RNA; TRANSCRIPTION FACTOR E2F;

EID: 0032776303     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.10.8.2703     Document Type: Article
Times cited : (432)

References (263)
  • 1
    • 0030872645 scopus 로고    scopus 로고
    • Interaction between replication protein A and p53 is disrupted after UV damage in a DNA repair-dependent manner
    • Abramova, N.A., Russell, J., Botchan, M., and Li, R. (1997). Interaction between replication protein A and p53 is disrupted after UV damage in a DNA repair-dependent manner. Proc. Natl. Acad. Sci. USA 94, 7186-7191.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7186-7191
    • Abramova, N.A.1    Russell, J.2    Botchan, M.3    Li, R.4
  • 3
    • 0030602813 scopus 로고    scopus 로고
    • Skp1 connects cell cycle regulation to the ubiquitin proteolysis machinery through a novel motif, the F-box
    • Bai, C., Sen, P., Hofmann, K., Ma, L., Goebl, M., Harper, J.W., and Elledge, S.J. (1996). Skp1 connects cell cycle regulation to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell 86, 263-274.
    • (1996) Cell , vol.86 , pp. 263-274
    • Bai, C.1    Sen, P.2    Hofmann, K.3    Ma, L.4    Goebl, M.5    Harper, J.W.6    Elledge, S.J.7
  • 4
    • 0032508504 scopus 로고    scopus 로고
    • Enhanced phosphorylation of p53 by ATM in response to DNA damage
    • Banin, S., et al. (1998). Enhanced phosphorylation of p53 by ATM in response to DNA damage. Science 281, 1674-1677.
    • (1998) Science , vol.281 , pp. 1674-1677
    • Banin, S.1
  • 5
    • 0030795331 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of RNA polymerase II carboxyl-terminal domain by the Abl-related gene product
    • Baskaran, R., Chiang, G.G., Mysliwiec, T., Kruh, G.D., and Wang, J.Y.J. (1997a). Tyrosine phosphorylation of RNA polymerase II carboxyl-terminal domain by the Abl-related gene product. J. Biol. Chem. 272, 18905-18909.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18905-18909
    • Baskaran, R.1    Chiang, G.G.2    Mysliwiec, T.3    Kruh, G.D.4    Wang, J.Y.J.5
  • 6
    • 0027361837 scopus 로고
    • Tyrosine phosphorylation of mammalian RNA polymerase II carboxyterminal domain
    • Baskaran, R., Dahmus, M.E., and Wang, J.Y.J. (1993). Tyrosine phosphorylation of mammalian RNA polymerase II carboxyterminal domain. Proc. Natl. Acad. Sci. USA 90, 11167-11171.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11167-11171
    • Baskaran, R.1    Dahmus, M.E.2    Wang, J.Y.J.3
  • 7
    • 0030925565 scopus 로고    scopus 로고
    • Ataxia telangiectasia mutant protein activates c-Abl tyrosine kinase in response to ionizing radiation
    • Baskaran, R., et al. (1997b). Ataxia telangiectasia mutant protein activates c-Abl tyrosine kinase in response to ionizing radiation. Nature 387, 516-519.
    • (1997) Nature , vol.387 , pp. 516-519
    • Baskaran, R.1
  • 9
    • 0031835432 scopus 로고    scopus 로고
    • RB and c-Myc activate expression of the E-cadherin gene in epithelial cells through interaction with transcription factor AP2
    • Batsche, E., Muchardt, C., Behrens, J., Hurst, H.C., and Cremisi, C. (1998). RB and c-Myc activate expression of the E-cadherin gene in epithelial cells through interaction with transcription factor AP2. Mol. Cell. Biol. 18, 3647-3658.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3647-3658
    • Batsche, E.1    Muchardt, C.2    Behrens, J.3    Hurst, H.C.4    Cremisi, C.5
  • 10
    • 0026786124 scopus 로고
    • Inhibition of DNA binding by the phosphorylation of poly ADP-ribose polymerase protein catalyzed by protein kinase C
    • Bauer, P., Farkas, G., Buday, L., Mikala, G., Meszaros, G., Kun, E., and Farago, A. (1992). Inhibition of DNA binding by the phosphorylation of poly ADP-ribose polymerase protein catalyzed by protein kinase C. Biochem Biophys Res Commun 187, 730-736.
    • (1992) Biochem Biophys Res Commun , vol.187 , pp. 730-736
    • Bauer, P.1    Farkas, G.2    Buday, L.3    Mikala, G.4    Meszaros, G.5    Kun, E.6    Farago, A.7
  • 11
    • 0030766963 scopus 로고    scopus 로고
    • The human rad51 protein: Polarity of strand transfer and stimulation by hRPA
    • Bauman, P., and West, S.C. (1997). The human rad51 protein: polarity of strand transfer and stimulation by hRPA. EMBO J. 16, 5198-5206.
    • (1997) EMBO J. , vol.16 , pp. 5198-5206
    • Bauman, P.1    West, S.C.2
  • 12
    • 0033555521 scopus 로고    scopus 로고
    • Growth/cell cycle regulation of Sp1 phosphorylation
    • Black, A.R., Jensen, D., Lin, S.-Y., and Azizkhan, J.C. (1999). Growth/cell cycle regulation of Sp1 phosphorylation. J. Biol. Chem. 274, 1207-1215.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1207-1215
    • Black, A.R.1    Jensen, D.2    Lin, S.-Y.3    Azizkhan, J.C.4
  • 13
    • 0029759341 scopus 로고    scopus 로고
    • Single-stranded-DNA binding alters human replication protein A structure and facilitates interaction with DNA-dependent protein kinase
    • Blackwell, L.J., Borowiec, J.A., and Masrangelo, I.A. (1996). Single-stranded-DNA binding alters human replication protein A structure and facilitates interaction with DNA-dependent protein kinase. Mol. Cell. Biol. 16, 4798-4807.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4798-4807
    • Blackwell, L.J.1    Borowiec, J.A.2    Masrangelo, I.A.3
  • 14
    • 0027468265 scopus 로고
    • Binding of Ku protein to DNA. Measurement of affinity for ends and demonstration of binding to nicks
    • Blier, P., Griffith, A., Craft, J., and Hardin, J. (1993). Binding of Ku protein to DNA. Measurement of affinity for ends and demonstration of binding to nicks. J. Biol. Chem. 268, 7594-7610.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7594-7610
    • Blier, P.1    Griffith, A.2    Craft, J.3    Hardin, J.4
  • 15
    • 0031030449 scopus 로고    scopus 로고
    • Structure of the single-stranded-DNA-binding domain of replication protein a bound to DNA
    • Bochkarev, A., Pfuetzner, R.A., Edwards, A.M., and Frappier, L. (1997). Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. Nature 385, 176-181.
    • (1997) Nature , vol.385 , pp. 176-181
    • Bochkarev, A.1    Pfuetzner, R.A.2    Edwards, A.M.3    Frappier, L.4
  • 16
    • 0030803797 scopus 로고    scopus 로고
    • Human myt1 is a cell cycle-regulated kinase that inhibits cdc2 but not cdk2 activity
    • Booher, R.N., Holman, P.S., and Fattaey, A. (1997). Human myt1 is a cell cycle-regulated kinase that inhibits cdc2 but not cdk2 activity. J. Biol. Chem. 272, 22300-22306.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22300-22306
    • Booher, R.N.1    Holman, P.S.2    Fattaey, A.3
  • 17
    • 0031282325 scopus 로고    scopus 로고
    • Design of a synthetic Mdm2-binding mini-protein that activates the p53 response in vivo
    • Bottger, A., Bottger, V., Sparks, A., Liu, W.L., Howard, S.F., and Lane, D.P. (1997). Design of a synthetic Mdm2-binding mini-protein that activates the p53 response in vivo. Curr. Biol. 7, 860-869.
    • (1997) Curr. Biol. , vol.7 , pp. 860-869
    • Bottger, A.1    Bottger, V.2    Sparks, A.3    Liu, W.L.4    Howard, S.F.5    Lane, D.P.6
  • 18
    • 0030848209 scopus 로고    scopus 로고
    • Role of protein-protein interactions in the function of replication protein A (RPA): RPA modulates the activity of DNA polymerase alpha by multiple mechanisms
    • Braun, K.A., Lao, Y., He, Z., Ingles, C.J., and Wold, M.S. (1997). Role of protein-protein interactions in the function of replication protein A (RPA): RPA modulates the activity of DNA polymerase alpha by multiple mechanisms. Biochemistry 36, 8443-8454.
    • (1997) Biochemistry , vol.36 , pp. 8443-8454
    • Braun, K.A.1    Lao, Y.2    He, Z.3    Ingles, C.J.4    Wold, M.S.5
  • 19
    • 0032484989 scopus 로고    scopus 로고
    • Retinoblastoma protein recruits histone deacetylase to repress transcription
    • Brehm, A., Miska, E.A., McCance, D.J., Reid, J.L., Bannister, A.J., and Kouzarides, T. (1998). Retinoblastoma protein recruits histone deacetylase to repress transcription. Nature 391, 597-601.
    • (1998) Nature , vol.391 , pp. 597-601
    • Brehm, A.1    Miska, E.A.2    McCance, D.J.3    Reid, J.L.4    Bannister, A.J.5    Kouzarides, T.6
  • 21
  • 22
    • 0033023893 scopus 로고    scopus 로고
    • Gadd45, a p53-responsive stress protein, modifies DNA accessibility on damaged chromatin
    • Carrier, F., et al. (1999). Gadd45, a p53-responsive stress protein, modifies DNA accessibility on damaged chromatin. Mol. Cell. Biol. 19, 1673-1685.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1673-1685
    • Carrier, F.1
  • 23
    • 0032490832 scopus 로고    scopus 로고
    • E2F-6: A novel member of the E2F family is an inhibitor of E2F-dependent transcription
    • Cartwright, P., Muller, H., Wagener, C., Holm, K., and Helin, K. (1998). E2F-6: a novel member of the E2F family is an inhibitor of E2F-dependent transcription. Oncogene 17, 611-623.
    • (1998) Oncogene , vol.17 , pp. 611-623
    • Cartwright, P.1    Muller, H.2    Wagener, C.3    Holm, K.4    Helin, K.5
  • 24
    • 0030009738 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase is inactivated by autophosphorylation of the catalytic subunit
    • Chan, D.W., and Lees-Miller, S.P. (1996). The DNA-dependent protein kinase is inactivated by autophosphorylation of the catalytic subunit. J. Biol. Chem. 271, 8936-8941.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8936-8941
    • Chan, D.W.1    Lees-Miller, S.P.2
  • 26
    • 11944257840 scopus 로고
    • Direct interaction of Gadd45 with PCNA and evidence for competitive interaction of Gadd45 and p21Waf1/Cip1 with PCNA
    • Chen, I.T., Smith, M.L., O'Connor, P.M., and Fornace, A.J., Jr. (1995). Direct interaction of Gadd45 with PCNA and evidence for competitive interaction of Gadd45 and p21Waf1/Cip1 with PCNA. Oncogene 11, 1931-1937.
    • (1995) Oncogene , vol.11 , pp. 1931-1937
    • Chen, I.T.1    Smith, M.L.2    O'Connor, P.M.3    Fornace A.J., Jr.4
  • 27
    • 0032159062 scopus 로고    scopus 로고
    • Stable interaction between the products of the BRCA1 and BRCA2 tumor suppressor genes in mitotic and meiotic cells
    • Chen, J., et al. (1998). Stable interaction between the products of the BRCA1 and BRCA2 tumor suppressor genes in mitotic and meiotic cells. Mol. Cell 2, 317-328.
    • (1998) Mol. Cell , vol.2 , pp. 317-328
    • Chen, J.1
  • 28
    • 0030955170 scopus 로고    scopus 로고
    • Proteolytic cleavage of the mdm2 oncoprotein during apoptosis
    • Chen, L., Marechal, V., Moreau, J., Levine, A.J., and Chen, J. (1997). Proteolytic cleavage of the mdm2 oncoprotein during apoptosis. J. Biol. Chem. 272, 22966-22973.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22966-22973
    • Chen, L.1    Marechal, V.2    Moreau, J.3    Levine, A.J.4    Chen, J.5
  • 29
    • 0029830342 scopus 로고    scopus 로고
    • Retinoblastoma protein positively regulates terminal adipocyte differentiation through direct interaction with C/EBPs
    • Chen, P.L., Riley, D.J., Chen, Y., and Lee, W.-H. (1996a). Retinoblastoma protein positively regulates terminal adipocyte differentiation through direct interaction with C/EBPs. Genes & Dev. 10, 2794-2804.
    • (1996) Genes & Dev. , vol.10 , pp. 2794-2804
    • Chen, P.L.1    Riley, D.J.2    Chen, Y.3    Lee, W.-H.4
  • 30
    • 0030031409 scopus 로고    scopus 로고
    • Retinoblastoma protein directly interacts with and activates the transcription factor NF-IL6
    • Chen, P.L., Riley, D.J., Chen-Kiang, S., and Lee, W.H. (1996b). Retinoblastoma protein directly interacts with and activates the transcription factor NF-IL6. Proc. Natl. Acad. Sci. USA 93, 465-469.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 465-469
    • Chen, P.L.1    Riley, D.J.2    Chen-Kiang, S.3    Lee, W.H.4
  • 31
    • 0030794423 scopus 로고    scopus 로고
    • In vivo evidence for binding of p53 to consensus binding sites in the p21 and GADD45 genes in response to ionizing radiation
    • Chin, P.L., Momand, J., and Pfeifer, G.P. (1997). In vivo evidence for binding of p53 to consensus binding sites in the p21 and GADD45 genes in response to ionizing radiation. Oncogene 15, 87-99.
    • (1997) Oncogene , vol.15 , pp. 87-99
    • Chin, P.L.1    Momand, J.2    Pfeifer, G.P.3
  • 32
    • 0029957947 scopus 로고    scopus 로고
    • Turnover of cyclin E by the ubiquitin-proteasome pathway is regulated by CDK2 binding and cyclin phosphorylation
    • Clurman, B.E., Sheaff, R.J., Thress, K., Groudine, M., and Robers, J.M. (1996). Turnover of cyclin E by the ubiquitin-proteasome pathway is regulated by CDK2 binding and cyclin phosphorylation. Genes & Dev. 10, 1979-1990.
    • (1996) Genes & Dev. , vol.10 , pp. 1979-1990
    • Clurman, B.E.1    Sheaff, R.J.2    Thress, K.3    Groudine, M.4    Robers, J.M.5
  • 33
    • 0030602823 scopus 로고    scopus 로고
    • Budding yeast Skp1 encodes an evolutionarily conserved kinetochore protein required for cell cycle progression
    • Connelly, C., and Hieter, P. (1996). Budding yeast Skp1 encodes an evolutionarily conserved kinetochore protein required for cell cycle progression. Cell 86, 275-285.
    • (1996) Cell , vol.86 , pp. 275-285
    • Connelly, C.1    Hieter, P.2
  • 34
    • 0032522224 scopus 로고    scopus 로고
    • Functional association of poly(ADP-ribose) polymerase with DNA polymerase α-primase complex: A link between DNA strand break detection and DNA replication
    • Dantzer, F., Nasheuer, H.-P., Vonesch, J.-L., de Murcia, G., and Menissier-deMurcia, J. (1998). Functional association of poly(ADP-ribose) polymerase with DNA polymerase α-primase complex: a link between DNA strand break detection and DNA replication. Nucleic Acids Res. 26, 1891-1898.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1891-1898
    • Dantzer, F.1    Nasheuer, H.-P.2    Vonesch, J.-L.3    De Murcia, G.4    Menissier-Demurcia, J.5
  • 35
    • 0029086190 scopus 로고
    • Association of p107 with Sp1: Genetically separable regions of p107 are involved in regulation of E2F- and Sp1-dependent transcription
    • Datta, P.K., Raychaudhuri, P., and Bagchi, S. (1995). Association of p107 with Sp1: genetically separable regions of p107 are involved in regulation of E2F- and Sp1-dependent transcription. Mol. Cell. Biol. 15, 5444-5452.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5444-5452
    • Datta, P.K.1    Raychaudhuri, P.2    Bagchi, S.3
  • 36
    • 0029049577 scopus 로고
    • Cellular targets for activation by the E2F1 transcription factor include DNA synthesis and G1/S-regulatory genes
    • DeGregori, J., Kowalik, T., and Nevins, J.R. (1995). Cellular targets for activation by the E2F1 transcription factor include DNA synthesis and G1/S-regulatory genes. Mol. Cell. Biol. 15, 4215-4224.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4215-4224
    • DeGregori, J.1    Kowalik, T.2    Nevins, J.R.3
  • 37
  • 39
    • 0028950016 scopus 로고
    • Effects of phosphorylation by CAK on cyclin binding by cdc2 and cdk2
    • Desai, D., Wessling, H.C., Fisher, R.P., and Morgan, D.O. (1995). Effects of phosphorylation by CAK on cyclin binding by cdc2 and cdk2. Mol. Cell. Biol. 15, 345-350.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 345-350
    • Desai, D.1    Wessling, H.C.2    Fisher, R.P.3    Morgan, D.O.4
  • 40
    • 0024356877 scopus 로고
    • Hela nuclear protein recognizing DNA termini and translocating on DNA forming a regular DNA-multimeric protein complex
    • deVries, E., van Driel, W., Bergsma, W.G., Arnberg, A. C., and van den Vliet, P.C. (1989). HeLa nuclear protein recognizing DNA termini and translocating on DNA forming a regular DNA-multimeric protein complex. J. Mol. Biol. 208, 65-78.
    • (1989) J. Mol. Biol. , vol.208 , pp. 65-78
    • DeVries, E.1    Van Driel, W.2    Bergsma, W.G.3    Arnberg, A.C.4    Van Den Vliet, P.C.5
  • 41
    • 0030916209 scopus 로고    scopus 로고
    • Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway
    • Diehl, J.A., Zindy, F., and Sherr, C.J. (1997). Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway. Genes & Dev. 11, 957-972.
    • (1997) Genes & Dev. , vol.11 , pp. 957-972
    • Diehl, J.A.1    Zindy, F.2    Sherr, C.J.3
  • 43
    • 0027358857 scopus 로고
    • Inhibition of DNA replication factor RPA by p53
    • Dutta, A., Ruppert, J.M., Aster, J.C., and Winchester, E. (1993). Inhibition of DNA replication factor RPA by p53. Nature 365, 79-82.
    • (1993) Nature , vol.365 , pp. 79-82
    • Dutta, A.1    Ruppert, J.M.2    Aster, J.C.3    Winchester, E.4
  • 44
    • 0026539144 scopus 로고
    • cdc2 family kinases phosphorylate a human cell DNA replication factor, RPA, and activate DNA replication
    • Dutta, A., and Stillman, B. (1992). cdc2 family kinases phosphorylate a human cell DNA replication factor, RPA, and activate DNA replication. EMBO J. 11, 2189-2199.
    • (1992) EMBO J. , vol.11 , pp. 2189-2199
    • Dutta, A.1    Stillman, B.2
  • 45
    • 0028966940 scopus 로고
    • Src homology 2 domain as a specificity determinant in the c-Abl-mediated tyrosine phosphorylation of the RNA polymerase II carboxyl-terminal repeated domain
    • Duyster, J., Baskaran, R., and Wang, J.Y.J. (1995). Src homology 2 domain as a specificity determinant in the c-Abl-mediated tyrosine phosphorylation of the RNA polymerase II carboxyl-terminal repeated domain. Proc. Natl. Acad. Sci. USA 92, 1555-1559.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1555-1559
    • Duyster, J.1    Baskaran, R.2    Wang, J.Y.J.3
  • 46
    • 0030990095 scopus 로고    scopus 로고
    • Specific regulation of E2F family members by cyclin-dependent kinases
    • Dynlacht, B.D., Moberg, K., Lees, J.A., Harlow, E., and Zhu, L. (1997). Specific regulation of E2F family members by cyclin-dependent kinases. Mol. Cell. Biol. 17, 3867-3875.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3867-3875
    • Dynlacht, B.D.1    Moberg, K.2    Lees, J.A.3    Harlow, E.4    Zhu, L.5
  • 47
    • 0032146274 scopus 로고    scopus 로고
    • The regulation of E2F by pRB-family proteins
    • Dyson, N. (1998). The regulation of E2F by pRB-family proteins [Review]. Genes & Dev. 12, 2245-2262.
    • (1998) Genes & Dev. , vol.12 , pp. 2245-2262
    • Dyson, N.1
  • 48
    • 0031987277 scopus 로고    scopus 로고
    • Regulation of p53 downstream genes
    • el-Deiry, W.S. (1998). Regulation of p53 downstream genes. Semin. Cancer Biol. 8, 345-357.
    • (1998) Semin. Cancer Biol. , vol.8 , pp. 345-357
    • El-Deiry, W.S.1
  • 50
    • 0030957746 scopus 로고    scopus 로고
    • Identification of the MDM2 oncoprotein as a substrate for CPP32-like apoptotic proteases
    • Erhardt, P., Tomaselli, K.J., and Cooper, G.M. (1997). Identification of the MDM2 oncoprotein as a substrate for CPP32-like apoptotic proteases. J. Biol. Chem. 272, 15049-15052.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15049-15052
    • Erhardt, P.1    Tomaselli, K.J.2    Cooper, G.M.3
  • 51
    • 0031013308 scopus 로고    scopus 로고
    • Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein
    • Evans, E., Fellows, J., Coffer, A., and Wood, R.D. (1997a). Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein. EMBO J. 16, 625-638.
    • (1997) EMBO J. , vol.16 , pp. 625-638
    • Evans, E.1    Fellows, J.2    Coffer, A.3    Wood, R.D.4
  • 52
    • 0030732132 scopus 로고    scopus 로고
    • Mechanism of open complex and dual incision formation by human nucleotide excision repair factors
    • Evans, E., Moggs, J.G., Hwang, J., Egly, J., and Wood, R.D. (1997b). Mechanism of open complex and dual incision formation by human nucleotide excision repair factors. EMBO J. 16, 6559-6573.
    • (1997) EMBO J. , vol.16 , pp. 6559-6573
    • Evans, E.1    Moggs, J.G.2    Hwang, J.3    Egly, J.4    Wood, R.D.5
  • 53
    • 0032168984 scopus 로고    scopus 로고
    • The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase
    • Ferreira, R., Magnaghi-Jaulin, L., Robin, P., Harel-Bellan, A., and Trouche, D. (1998). The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase. Proc. Natl. Acad. Sci. USA 95, 10493-10498.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10493-10498
    • Ferreira, R.1    Magnaghi-Jaulin, L.2    Robin, P.3    Harel-Bellan, A.4    Trouche, D.5
  • 54
    • 0027994603 scopus 로고
    • A novel cyclin associates with MO15/cdk7 to form the cdk-activating kinase
    • Fisher, R.P., and Morgan, D.O. (1994). A novel cyclin associates with MO15/cdk7 to form the cdk-activating kinase. Cell 78, 713-724.
    • (1994) Cell , vol.78 , pp. 713-724
    • Fisher, R.P.1    Morgan, D.O.2
  • 55
    • 0031724593 scopus 로고    scopus 로고
    • Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6
    • Freedman, D.A., and Levine, A.J. (1998). Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6. Mol. Cell. Biol. 18, 7288-7293.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7288-7293
    • Freedman, D.A.1    Levine, A.J.2
  • 56
    • 0032893878 scopus 로고    scopus 로고
    • Regulation of the p53 protein by the MDM2 oncoprotein - 38th G.H.A. Clowes memorial award lecture
    • Freedman, D.A., and Levine, A.J. (1999). Regulation of the p53 protein by the MDM2 oncoprotein - 38th G.H.A. Clowes Memorial Award Lecture. Cancer Res. 59, 1-7.
    • (1999) Cancer Res. , vol.59 , pp. 1-7
    • Freedman, D.A.1    Levine, A.J.2
  • 57
    • 0032512057 scopus 로고    scopus 로고
    • Mdm2 association with p53 targets its ubiquitination
    • Fuchs, S.Y., Adler, V., Buschmann, T., Wu, X., and Ronai, Z. (1998). Mdm2 association with p53 targets its ubiquitination. Oncogene 17, 2543-2547.
    • (1998) Oncogene , vol.17 , pp. 2543-2547
    • Fuchs, S.Y.1    Adler, V.2    Buschmann, T.3    Wu, X.4    Ronai, Z.5
  • 58
    • 0030667428 scopus 로고    scopus 로고
    • Hyperphosphorylation of the N-terminal domain of Cdc25 regulates activity toward Cyclin B1/Cdc2 but not Cyclin A/Cdk2
    • Gabrielli, B.G., Clark, J.M., McCormack, A.K., and Ellem, K.A.O. (1997). Hyperphosphorylation of the N-terminal domain of Cdc25 regulates activity toward Cyclin B1/Cdc2 but not Cyclin A/Cdk2. J. Biol. Chem. 272, 28607-28614.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28607-28614
    • Gabrielli, B.G.1    Clark, J.M.2    McCormack, A.K.3    Ellem, K.A.O.4
  • 59
    • 0029779280 scopus 로고    scopus 로고
    • Cdc25 cell-cycle phosphatase as a target of c-myc
    • Galaktionov, K., Chen, X., and Beach, D. (1996). Cdc25 cell-cycle phosphatase as a target of c-myc. Nature 382, 511-517.
    • (1996) Nature , vol.382 , pp. 511-517
    • Galaktionov, K.1    Chen, X.2    Beach, D.3
  • 60
    • 0029042689 scopus 로고
    • Raf-1 interaction with Cdc25 phosphatase ties mitogenic signal transduction to cell cycle activation
    • Galaktionov, K., Jessus, C., and Beach, D. (1995). Raf-1 interaction with Cdc25 phosphatase ties mitogenic signal transduction to cell cycle activation. Genes & Dev. 9, 1046-1058.
    • (1995) Genes & Dev. , vol.9 , pp. 1046-1058
    • Galaktionov, K.1    Jessus, C.2    Beach, D.3
  • 61
    • 0030767281 scopus 로고    scopus 로고
    • The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21
    • Gary, R., Ludwig, D.L., Cornelius, H.L., MacInnes, M.A., and Park, M.S. (1997). The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21. J. Biol. Chem. 272, 24522-24529.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24522-24529
    • Gary, R.1    Ludwig, D.L.2    Cornelius, H.L.3    MacInnes, M.A.4    Park, M.S.5
  • 62
    • 0031697988 scopus 로고    scopus 로고
    • Characterization of ATM expression, localization, and associated DNA-dependent protein kinase activity
    • Gately, D.P., Hittle, J.C., Chan, C.K.T., and Yen, T.J. (1998). Characterization of ATM expression, localization, and associated DNA-dependent protein kinase activity. Mol. Biol. Cell 9, 2361-2374.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2361-2374
    • Gately, D.P.1    Hittle, J.C.2    Chan, C.K.T.3    Yen, T.J.4
  • 63
    • 0028949627 scopus 로고
    • Transcriptional activation by Myc is under negative control by the transcriptional factor AP-2
    • Gaubatz, S., Imhof, A., Dosch, R., Werner, O., Mitchell, P., Buettner, R., and Eilers, M. (1995). Transcriptional activation by Myc is under negative control by the transcriptional factor AP-2. EMBO J. 14, 1508-1519.
    • (1995) EMBO J. , vol.14 , pp. 1508-1519
    • Gaubatz, S.1    Imhof, A.2    Dosch, R.3    Werner, O.4    Mitchell, P.5    Buettner, R.6    Eilers, M.7
  • 64
    • 0032482981 scopus 로고    scopus 로고
    • Unusual proliferation arrest and transcriptional control properties of a newly discovered E2F family member, E2F-6
    • Gaubatz, S., Wood, J.G., and Livingston, D.M. (1998). Unusual proliferation arrest and transcriptional control properties of a newly discovered E2F family member, E2F-6. Proc. Natl. Acad. Sci. USA 95, 9190-9195.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9190-9195
    • Gaubatz, S.1    Wood, J.G.2    Livingston, D.M.3
  • 65
    • 0031018324 scopus 로고    scopus 로고
    • The influence of the proliferating cell nuclear antigen-interacting domain of p21(CIP1) on DNA synthesis catalyzed by the human and Saccharomyces cerevisiae polymerase delta holoenzymes
    • Gibbs, E., Kelman, Z., Gulbis, J.M., O'Donnell, M., Kuriyan, J., Burgers, P.M.J., and Hurwitz, J. (1997). The influence of the proliferating cell nuclear antigen-interacting domain of p21(CIP1) on DNA synthesis catalyzed by the human and Saccharomyces cerevisiae polymerase delta holoenzymes. J. Biol. Chem. 272, 2373-2381.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2373-2381
    • Gibbs, E.1    Kelman, Z.2    Gulbis, J.M.3    O'Donnell, M.4    Kuriyan, J.5    Burgers, P.M.J.6    Hurwitz, J.7
  • 66
    • 0029835157 scopus 로고    scopus 로고
    • Studies on the in vitro phosphorylation of HSSB-p34 and -p107 by cyclin-dependent kinases: Cyclin-substrate interactions dictate the efficiency of phosphorylation
    • Gibbs, E., Pan, Z.-Q., Niu, H., and Hurwitz, J. (1996). Studies on the in vitro phosphorylation of HSSB-p34 and -p107 by cyclin-dependent kinases: cyclin-substrate interactions dictate the efficiency of phosphorylation. J. Biol. Chem. 271, 22847-22854.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22847-22854
    • Gibbs, E.1    Pan, Z.-Q.2    Niu, H.3    Hurwitz, J.4
  • 67
    • 0032535244 scopus 로고    scopus 로고
    • Polo-like kinases: A team that plays throughout mitosis
    • Glover, D.M., Hagan, I.M., and Tavares, A.A.M. (1998). Polo-like kinases: a team that plays throughout mitosis. Genes & Dev. 12, 1377-3787.
    • (1998) Genes & Dev. , vol.12 , pp. 1377-3787
    • Glover, D.M.1    Hagan, I.M.2    Tavares, A.A.M.3
  • 68
    • 0032403121 scopus 로고    scopus 로고
    • Interaction of human Rad51 recombination protein with single-stranded DNA binding protein, RPA
    • Golub, E.I., Gupta, R., Haaf, T., Wold, M.S., and Radding, C.M. (1998). Interaction of human Rad51 recombination protein with single-stranded DNA binding protein, RPA. Nucleic Acids Res. 26, 5388-5393.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5388-5393
    • Golub, E.I.1    Gupta, R.2    Haaf, T.3    Wold, M.S.4    Radding, C.M.5
  • 69
    • 0029868656 scopus 로고    scopus 로고
    • Proteolytic mapping of human replication protein A: Evidence for multiple structural domains and a conformational change upon interaction with single-stranded DNA
    • Gomes, X.V., Henricksen, L.A., and Wold, M.S. (1996). Proteolytic mapping of human replication protein A: evidence for multiple structural domains and a conformational change upon interaction with single-stranded DNA. Biochemistry 35, 5586-5595.
    • (1996) Biochemistry , vol.35 , pp. 5586-5595
    • Gomes, X.V.1    Henricksen, L.A.2    Wold, M.S.3
  • 70
    • 0031038744 scopus 로고    scopus 로고
    • The function of BCR/ABL and related proto-oncogenes
    • Gotoh, A., and Broxmeyer, H.E. (1997). The function of BCR/ABL and related proto-oncogenes. Curr. Opin. Hematol. 4, 3-11.
    • (1997) Curr. Opin. Hematol. , vol.4 , pp. 3-11
    • Gotoh, A.1    Broxmeyer, H.E.2
  • 72
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu, W., and Roeder, R.G. (1997). Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90, 595-606.
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 73
    • 0027977923 scopus 로고
    • Cloning and characterization of human and murine homologues of the Drosophila polo serine-threonine kinase
    • Hamanaka, R., Maloid, S., Smith, M.R., O'Connell, C.D., Longo, D.L., and Ferris, D.K. (1994). Cloning and characterization of human and murine homologues of the Drosophila polo serine-threonine kinase. Cell Growth & Differ. 5, 249-257.
    • (1994) Cell Growth & Differ. , vol.5 , pp. 249-257
    • Hamanaka, R.1    Maloid, S.2    Smith, M.R.3    O'Connell, C.D.4    Longo, D.L.5    Ferris, D.K.6
  • 74
    • 0031842101 scopus 로고    scopus 로고
    • Requirement of cyclin E-cdk2 inhibition in p16ink4a-mediated growth suppression
    • Hang, H., Chou, H.S., and Zhu, L. (1998). Requirement of cyclin E-cdk2 inhibition in p16ink4a-mediated growth suppression. Mol. Cell. Biol. 18, 5284-5290.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5284-5290
    • Hang, H.1    Chou, H.S.2    Zhu, L.3
  • 75
    • 0029825798 scopus 로고    scopus 로고
    • Mutation of phosphoserine 389 affects p53 function in vivo
    • Hao, M., Lowy, A.M., Kapoor, M., Deffie, A., Liu, G., and Lozano, G. (1997). Mutation of phosphoserine 389 affects p53 function in vivo. J. Biol. Chem. 271, 29380-29385.
    • (1997) J. Biol. Chem. , vol.271 , pp. 29380-29385
    • Hao, M.1    Lowy, A.M.2    Kapoor, M.3    Deffie, A.4    Liu, G.5    Lozano, G.6
  • 76
    • 0029797841 scopus 로고    scopus 로고
    • Degradation of E2F by the ubiquitin-proteasome pathway: Regulation by retinoblastoma family proteins and adenovirus transforming proteins
    • Hateboer, G., Kerkhoven, R.M., Shvarts, A., Bernards, R., and Beijersbergen, R.L. (1996). Degradation of E2F by the ubiquitin-proteasome pathway: regulation by retinoblastoma family proteins and adenovirus transforming proteins. Genes & Dev. 10, 2960-2970.
    • (1996) Genes & Dev. , vol.10 , pp. 2960-2970
    • Hateboer, G.1    Kerkhoven, R.M.2    Shvarts, A.3    Bernards, R.4    Beijersbergen, R.L.5
  • 77
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt, Y., Maya, R., Kazaz, A., and Oren, M. (1997). Mdm2 promotes the rapid degradation of p53. Nature 387, 296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 78
    • 0028929611 scopus 로고
    • RPA involvement in the damage-recognition and incision steps of nucleotide excision repair
    • He, Z., Henricksen, L.A., Wold, M.S., and Ingles, C.J. (1995). RPA involvement in the damage-recognition and incision steps of nucleotide excision repair. Nature 374, 566-569.
    • (1995) Nature , vol.374 , pp. 566-569
    • He, Z.1    Henricksen, L.A.2    Wold, M.S.3    Ingles, C.J.4
  • 79
    • 0032535115 scopus 로고    scopus 로고
    • Mitotic silencing of human rRNA synthesis: Inactivation of the promoter selectivity factor SL1 by cdc2/cyclin B-mediated phosphorylation
    • Heix, J., Vente, A., Voit, R., Budde, A., Michaelidis, T.M., and Grummt, I. (1998). Mitotic silencing of human rRNA synthesis: inactivation of the promoter selectivity factor SL1 by cdc2/cyclin B-mediated phosphorylation. EMBO J. 17, 7373-7381.
    • (1998) EMBO J. , vol.17 , pp. 7373-7381
    • Heix, J.1    Vente, A.2    Voit, R.3    Budde, A.4    Michaelidis, T.M.5    Grummt, I.6
  • 80
    • 0031886093 scopus 로고    scopus 로고
    • Regulation of cell proliferation by the E2F transcription factors
    • Helin, K. (1998). Regulation of cell proliferation by the E2F transcription factors. Curr. Opin. Genet. Dev. 8, 28-35.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 28-35
    • Helin, K.1
  • 81
    • 0029083459 scopus 로고
    • Progression of carcinoma cells is associated with alterations in chromatin structure and factor binding at the E-cadherin promoter in vivo
    • Hennig, G., Behrens, J., Truss, M., Frisch, S., Reichmann, E., and Birchmeier, W. (1995). Progression of carcinoma cells is associated with alterations in chromatin structure and factor binding at the E-cadherin promoter in vivo. Oncogene 11, 475-484.
    • (1995) Oncogene , vol.11 , pp. 475-484
    • Hennig, G.1    Behrens, J.2    Truss, M.3    Frisch, S.4    Reichmann, E.5    Birchmeier, W.6
  • 82
    • 0030066481 scopus 로고    scopus 로고
    • Mechanisms identified in the transcriptional control of epithelial gene expression
    • Hennig, G., Lowrick, O., Birchmeier, W., and Behrens, J. (1996). Mechanisms identified in the transcriptional control of epithelial gene expression. J. Biol. Chem. 271, 595-602.
    • (1996) J. Biol. Chem. , vol.271 , pp. 595-602
    • Hennig, G.1    Lowrick, O.2    Birchmeier, W.3    Behrens, J.4
  • 83
    • 0029740726 scopus 로고    scopus 로고
    • Phosphorylation of human replication protein A by the DNA-dependent protein kinase in involved in the modulation of DNA replication
    • Henricksen, L.A., Carter, T., Dutta, A., and Wold, M.S. (1996). Phosphorylation of human replication protein A by the DNA-dependent protein kinase in involved in the modulation of DNA replication. Nucleic Acids Res. 24, 3107-3112.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3107-3112
    • Henricksen, L.A.1    Carter, T.2    Dutta, A.3    Wold, M.S.4
  • 84
    • 0028245269 scopus 로고
    • Recombinant replication protein A: Expression, complex formation, and functional characterization
    • Henricksen, L.A., Umbricht, C.B., and Wold, M.S. (1994). Recombinant replication protein A: expression, complex formation, and functional characterization. J. Biol. Chem. 269, 11121-11132.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11121-11132
    • Henricksen, L.A.1    Umbricht, C.B.2    Wold, M.S.3
  • 86
    • 0029851287 scopus 로고    scopus 로고
    • Interaction of D-type cyclins with a novel myb-like transcription factor, DMP1
    • Hirai, H., and Sherr, C.J. (1996). Interaction of D-type cyclins with a novel myb-like transcription factor, DMP1. Mol. Cell. Biol. 16, 6457-6467.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6457-6467
    • Hirai, H.1    Sherr, C.J.2
  • 87
    • 0027509501 scopus 로고
    • Phosphorylation and activation of human cdc25c by cdc2-cyclin B and its involvement in the self-amplification of MPF at mitosis
    • Hoffman, I., Clarke, P.R., Marcote, M.J., Karsenti, E., and Draetta, G. (1993). Phosphorylation and activation of human cdc25C by cdc2-cyclin B and its involvement in the self-amplification of MPF at mitosis. EMBO J. 12, 53-63.
    • (1993) EMBO J. , vol.12 , pp. 53-63
    • Hoffman, I.1    Clarke, P.R.2    Marcote, M.J.3    Karsenti, E.4    Draetta, G.5
  • 88
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda, R., Tanaka, H., and Yasuda, H. (1997). Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett. 420, 25-27.
    • (1997) FEBS Lett. , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 89
    • 0033521621 scopus 로고    scopus 로고
    • Association of p19ARF with mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
    • Honda, R., and Yasuda, H. (1999). Association of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53. EMBO J. 18, 22-27.
    • (1999) EMBO J. , vol.18 , pp. 22-27
    • Honda, R.1    Yasuda, H.2
  • 90
    • 0028673142 scopus 로고
    • Regulation of the cryptic sequence-specific DNA-binding function of p53 by protein kinases
    • Hupp, T.R., and Lane, D.P. (1994). Regulation of the cryptic sequence-specific DNA-binding function of p53 by protein kinases. Cold Spring Harbor Symp. Quant. Biol. 59, 195-206.
    • (1994) Cold Spring Harbor Symp. Quant. Biol. , vol.59 , pp. 195-206
    • Hupp, T.R.1    Lane, D.P.2
  • 91
    • 0033616608 scopus 로고    scopus 로고
    • Induction of ARF tumor suppressor gene expression and cell cycle arrest by transcription factor DMP1
    • Inoue, K., Roussel, M.F., and Sherr, C.J. (1999). Induction of ARF tumor suppressor gene expression and cell cycle arrest by transcription factor DMP1. Proc. Natl. Acad. Sci. USA 96, 3993-3998.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3993-3998
    • Inoue, K.1    Roussel, M.F.2    Sherr, C.J.3
  • 92
    • 0031937638 scopus 로고    scopus 로고
    • Gene expression and cell cycle arrest mediated by transcription factor DMP1 is antagonized by D-type cyclins through a cyclin-dependent-kinase-independent mechanism
    • Inoue, K., and Sherr, C.J. (1998). Gene expression and cell cycle arrest mediated by transcription factor DMP1 is antagonized by D-type cyclins through a cyclin-dependent-kinase-independent mechanism. Mol. Cell. Biol. 18, 1590-1600.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1590-1600
    • Inoue, K.1    Sherr, C.J.2
  • 93
    • 0029019737 scopus 로고
    • Human cyclins B1 and B2 are localized to strikingly different structures: B1 to microtubules, B2 primarily to the Golgi apparatus
    • Jackman, M., Firth, M., and Pines, J. (1995). Human cyclins B1 and B2 are localized to strikingly different structures: B1 to microtubules, B2 primarily to the Golgi apparatus. EMBO J. 14, 1646-1654.
    • (1995) EMBO J. , vol.14 , pp. 1646-1654
    • Jackman, M.1    Firth, M.2    Pines, J.3
  • 94
    • 0030612165 scopus 로고    scopus 로고
    • Cyclins and G2/M transition
    • Jackman, M.R., and Pines, J.N. (1997). Cyclins and G2/M transition. Cancer Surv. 29, 47-73.
    • (1997) Cancer Surv. , vol.29 , pp. 47-73
    • Jackman, M.R.1    Pines, J.N.2
  • 96
    • 0030771841 scopus 로고    scopus 로고
    • Binding of Ku and c-Abl at the kinase homology region of DNA-dependent protein kinase catalytic subunit
    • Jin, S., Kharbanda, S., Mayer, B., Kufe, D., and Weaver, D.T. (1997). Binding of Ku and c-Abl at the kinase homology region of DNA-dependent protein kinase catalytic subunit. J. Biol. Chem. 272, 24763-24766.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24763-24766
    • Jin, S.1    Kharbanda, S.2    Mayer, B.3    Kufe, D.4    Weaver, D.T.5
  • 97
    • 0027483739 scopus 로고
    • Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA
    • Jones, C.J., and Wood, R.D. (1993). Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA. Biochemistry 32, 12096-12104.
    • (1993) Biochemistry , vol.32 , pp. 12096-12104
    • Jones, C.J.1    Wood, R.D.2
  • 98
    • 0027501841 scopus 로고
    • Wild-type p53 can mediate sequence-specific transactivation of an internal promoter within the mdm2 gene
    • Juven, T., Barak, Y., Zauberman, A., George, D.L., and Oren, M. (1993). Wild-type p53 can mediate sequence-specific transactivation of an internal promoter within the mdm2 gene. Oncogene 8, 3411-3416.
    • (1993) Oncogene , vol.8 , pp. 3411-3416
    • Juven, T.1    Barak, Y.2    Zauberman, A.3    George, D.L.4    Oren, M.5
  • 100
    • 0032539816 scopus 로고    scopus 로고
    • Functional activation of p53 via phosphorylation following DNA damage by UV but not γ radiation
    • Kapoor, M., and Lozano, G. (1998). Functional activation of p53 via phosphorylation following DNA damage by UV but not γ radiation. Proc. Natl. Acad. Sci. USA 95, 2835-2837.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2835-2837
    • Kapoor, M.1    Lozano, G.2
  • 101
    • 0029926303 scopus 로고    scopus 로고
    • Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F
    • Karlseder, J., Rotheneder, H., and Wintersberger, E. (1996). Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F. Mol. Cell. Biol. 16, 1659-1667.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1659-1667
    • Karlseder, J.1    Rotheneder, H.2    Wintersberger, E.3
  • 103
    • 0028793807 scopus 로고
    • Gadd45 is a nuclear cell cycle regulated protein which interacts with p21cip1
    • Kearsey, J.M., Coates, P.J., Prescott, A.R., Warbrick, E., and Hall, P.A. (1995). Gadd45 is a nuclear cell cycle regulated protein which interacts with p21Cip1. Oncogene 11, 1675-1683.
    • (1995) Oncogene , vol.11 , pp. 1675-1683
    • Kearsey, J.M.1    Coates, P.J.2    Prescott, A.R.3    Warbrick, E.4    Hall, P.A.5
  • 104
    • 0031045565 scopus 로고    scopus 로고
    • PCNA: Structure, functions and interactions
    • Kelman, Z. (1997). PCNA: structure, functions and interactions [Review]. Oncogene 14, 629-640.
    • (1997) Oncogene , vol.14 , pp. 629-640
    • Kelman, Z.1
  • 106
    • 0029892484 scopus 로고    scopus 로고
    • Role of the 70-kDa subunit of human replication protein A (I). Single-stranded DNA binding activity, but not polymerase stimulatory activity, is required for DNA replication
    • Kim, D.K., Stigger, E., and Lee, S.-H. (1996). Role of the 70-kDa subunit of human replication protein A (I). Single-stranded DNA binding activity, but not polymerase stimulatory activity, is required for DNA replication. J. Biol. Chem. 271, 15124-15129.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15124-15129
    • Kim, D.K.1    Stigger, E.2    Lee, S.-H.3
  • 107
    • 0030670332 scopus 로고    scopus 로고
    • p53 is phosphorylated in vitro and in vivo by the delta and epsilon isoforms of casein kinase 1 and enhances the level of casein kinase 1 delta in response to topoisomerase-directed drugs
    • Knippschild, U., Milne, D.M., Campbell, L.E., DeMaggio, A.J., Christenson, E., Hoekstra, M., and Meek, D.W. (1997). p53 is phosphorylated in vitro and in vivo by the delta and epsilon isoforms of casein kinase 1 and enhances the level of casein kinase 1 delta in response to topoisomerase-directed drugs. Oncogene 15, 1727-1736.
    • (1997) Oncogene , vol.15 , pp. 1727-1736
    • Knippschild, U.1    Milne, D.M.2    Campbell, L.E.3    DeMaggio, A.J.4    Christenson, E.5    Hoekstra, M.6    Meek, D.W.7
  • 109
    • 0032568043 scopus 로고    scopus 로고
    • Functional capabilities of molecular network components controlling the mammalian G1/S cell cycle phase transition
    • Kohn, K.W. (1998). Functional capabilities of molecular network components controlling the mammalian G1/S cell cycle phase transition. Oncogene 16, 1065-1075.
    • (1998) Oncogene , vol.16 , pp. 1065-1075
    • Kohn, K.W.1
  • 110
    • 0029559027 scopus 로고
    • Cyclin A-kinase regulation of E2F-1 DNA binding function underlies suppression of an S phase checkpoint
    • Krek, W., Xu, G., and Livingston, D.M. (1995). Cyclin A-kinase regulation of E2F-1 DNA binding function underlies suppression of an S phase checkpoint. Cell 83, 1149-1158.
    • (1995) Cell , vol.83 , pp. 1149-1158
    • Krek, W.1    Xu, G.2    Livingston, D.M.3
  • 111
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbatat, M.H.G., Jones, S.N., and Vousden, K.H. (1997). Regulation of p53 stability by Mdm2. Nature 387, 299-303.
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbatat, M.H.G.1    Jones, S.N.2    Vousden, K.H.3
  • 112
    • 0030575937 scopus 로고    scopus 로고
    • Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain
    • Kussie, P.H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A.J., and Pavletich, N.P. (1996). Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science 274, 948-953.
    • (1996) Science , vol.274 , pp. 948-953
    • Kussie, P.H.1    Gorina, S.2    Marechal, V.3    Elenbaas, B.4    Moreau, J.5    Levine, A.J.6    Pavletich, N.P.7
  • 114
    • 0033118927 scopus 로고    scopus 로고
    • Timing of cyclin E gene expression depends on the regulated association of a bipartite repressor element with a novel E2F complex
    • Le Cam, L., Polanowska, J., Fabbrizio, E., Olivier, M., Philips, A., Eaton, E.N., Classon, M., Geng, Y., and Sardet, C. (1999). Timing of cyclin E gene expression depends on the regulated association of a bipartite repressor element with a novel E2F complex. EMBO J. 18, 1878-1890.
    • (1999) EMBO J. , vol.18 , pp. 1878-1890
    • Le Cam, L.1    Polanowska, J.2    Fabbrizio, E.3    Olivier, M.4    Philips, A.5    Eaton, E.N.6    Classon, M.7    Geng, Y.8    Sardet, C.9
  • 115
    • 0032575079 scopus 로고    scopus 로고
    • Functional interplay between p53 and E2F through coactivator p300
    • Lee, C.-W., Sorensen, T.S., Shikama, N., and La Thangue, N.B. (1998a). Functional interplay between p53 and E2F through coactivator p300. Oncogene 16, 2695-2710.
    • (1998) Oncogene , vol.16 , pp. 2695-2710
    • Lee, C.-W.1    Sorensen, T.S.2    Shikama, N.3    La Thangue, N.B.4
  • 116
    • 2642601106 scopus 로고    scopus 로고
    • Structure of the retinoblastoma tumor-suppressor pocket domain bound to a peptide from HPV E7
    • Lee, J.O., Russo, A.A., and Pavletich, N.P. (1998b). Structure of the retinoblastoma tumor-suppressor pocket domain bound to a peptide from HPV E7. Nature 391, 859-865.
    • (1998) Nature , vol.391 , pp. 859-865
    • Lee, J.O.1    Russo, A.A.2    Pavletich, N.P.3
  • 117
    • 0032482986 scopus 로고    scopus 로고
    • Mutation of the polo-box disrupts localization and mitotic functions of the mammalian polo kinase Plk
    • Lee, K.S., Grenfell, T.Z., Yarm, F.R., and Erickson, R.L. (1998c). Mutation of the polo-box disrupts localization and mitotic functions of the mammalian polo kinase Plk. Proc. Natl. Acad. Sci. USA 95, 9301-9306.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9301-9306
    • Lee, K.S.1    Grenfell, T.Z.2    Yarm, F.R.3    Erickson, R.L.4
  • 118
    • 1842378642 scopus 로고    scopus 로고
    • The MDM2 C-terminal region binds to TAFII250 and is required for MDM2 regulation of the cyclin A promoter
    • Leveillard, T., and Wasylyk, B. (1997). The MDM2 C-terminal region binds to TAFII250 and is required for MDM2 regulation of the cyclin A promoter. J. Biol. Chem. 272, 30651-30661.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30651-30661
    • Leveillard, T.1    Wasylyk, B.2
  • 119
    • 0030692134 scopus 로고    scopus 로고
    • An interaction between DNA ligase I and proliferating cell nuclear antigen: Implications for Okazaki fragment syntheses and joining
    • Levin, D.S., Bai, W., Yan, N., O'Donnell, M., and Tomkinson, A.E. (1997). An interaction between DNA ligase I and proliferating cell nuclear antigen: implications for Okazaki fragment syntheses and joining. Proc. Natl. Acad. Sci. USA 94, 12863-12868.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12863-12868
    • Levin, D.S.1    Bai, W.2    Yan, N.3    O'Donnell, M.4    Tomkinson, A.E.5
  • 120
    • 0032486386 scopus 로고    scopus 로고
    • Integrins regulate the association and phosphorylation of paxillin by c-Abl
    • Lewis, J.M., and Schwartz, M.A. (1998). Integrins regulate the association and phosphorylation of paxillin by c-Abl. J. Biol. Chem. 273, 14225-14230.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14225-14230
    • Lewis, J.M.1    Schwartz, M.A.2
  • 122
    • 0032516786 scopus 로고    scopus 로고
    • Interactions of the transcription/DNA repair factor TFIIH and XP repair proteins with DNA lesions in a cell-free repair assay
    • Li, R.-Y., Calsou, P., Jones, C.J., and Salles, B. (1998). Interactions of the transcription/DNA repair factor TFIIH and XP repair proteins with DNA lesions in a cell-free repair assay. J. Mol. Biol. 281, 211-218.
    • (1998) J. Mol. Biol. , vol.281 , pp. 211-218
    • Li, R.-Y.1    Calsou, P.2    Jones, C.J.3    Salles, B.4
  • 123
    • 0031059531 scopus 로고    scopus 로고
    • Tying loose ends: Roles of Ku and DNA-dependent protein kinase in the repair of double-strand breaks
    • Lieber, M.R., Grawunder, U., Wu, X., and Yaneva, M. (1997). Tying loose ends: roles of Ku and DNA-dependent protein kinase in the repair of double-strand breaks. Curr. Opin. Genet. Dev. 7, 99-104.
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 99-104
    • Lieber, M.R.1    Grawunder, U.2    Wu, X.3    Yaneva, M.4
  • 125
    • 0029981560 scopus 로고    scopus 로고
    • Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction
    • Lin, S.-Y., Black, A.R., Kostic, D., Pajovic, S., Hoover, C.N., and Azizkhan, J.C. (1996a). Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction. Mol. Cell. Biol. 16, 1668-1675.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1668-1675
    • Lin, S.-Y.1    Black, A.R.2    Kostic, D.3    Pajovic, S.4    Hoover, C.N.5    Azizkhan, J.C.6
  • 126
    • 0030054869 scopus 로고    scopus 로고
    • Dissection of functional domains of the human DNA replication protein complex replication protein A
    • Lin, Y.L., Chen, C., Keshav, K.F., Winchester, E., and Dutta, A. (1996b). Dissection of functional domains of the human DNA replication protein complex replication protein A. J. Biol. Chem. 271, 17190-17198.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17190-17198
    • Lin, Y.L.1    Chen, C.2    Keshav, K.F.3    Winchester, E.4    Dutta, A.5
  • 127
    • 0031053117 scopus 로고    scopus 로고
    • The human myt1 kinase preferentially phosphorylates cdc2 on threonine 14 and localizes to the endoplasmic reticulum and Golgi complex
    • Liu, F., Stanton, J.J., Wu, Z., and Piwnica-Worms, H. (1997). The human myt1 kinase preferentially phosphorylates cdc2 on threonine 14 and localizes to the endoplasmic reticulum and Golgi complex. Mol. Cell. Biol. 17, 571-583.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 571-583
    • Liu, F.1    Stanton, J.J.2    Wu, Z.3    Piwnica-Worms, H.4
  • 128
    • 0030610565 scopus 로고    scopus 로고
    • The CDK7-cycH-p36 complex of TFIIH phosphorylates p53, enhancing its sequence-specific DNA binding activity in vitro
    • Lu, H., Fisher, R., Bailey, P., and Levine, A. (1997). The CDK7-cycH-p36 complex of TFIIH phosphorylates p53, enhancing its sequence-specific DNA binding activity in vitro. Mol. Cell. Biol. 17, 5923-5934.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5923-5934
    • Lu, H.1    Fisher, R.2    Bailey, P.3    Levine, A.4
  • 129
    • 0032568633 scopus 로고    scopus 로고
    • UV radiation, but not y radiation or etoposide-induced DNA damage, results in the phosphorylation of the murine p53 protein at serine-389
    • Lu, H., Taya, Y., Ikeda, M., and Levine, A.J. (1998). UV radiation, but not y radiation or etoposide-induced DNA damage, results in the phosphorylation of the murine p53 protein at serine-389. Proc. Natl. Acad. Sci. USA 95, 6399-6402.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6399-6402
    • Lu, H.1    Taya, Y.2    Ikeda, M.3    Levine, A.J.4
  • 131
    • 0031951182 scopus 로고    scopus 로고
    • Functional inactivation of the retinoblastoma protein requires sequential modification by at least two distinct cyclin-cdk complexes
    • Lundberg, A.S., and Weinberg, R.A. (1998). Functional inactivation of the retinoblastoma protein requires sequential modification by at least two distinct cyclin-cdk complexes. Mol. Cell. Biol. 18, 753-761.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 753-761
    • Lundberg, A.S.1    Weinberg, R.A.2
  • 132
    • 0032549001 scopus 로고    scopus 로고
    • Rb interacts with histone deacetylase to repress transcription
    • Luo, R.X., Postigo, A.A., and Dean, D.C. (1998). Rb interacts with histone deacetylase to repress transcription. Cell 92, 463-473.
    • (1998) Cell , vol.92 , pp. 463-473
    • Luo, R.X.1    Postigo, A.A.2    Dean, D.C.3
  • 133
    • 0029952441 scopus 로고    scopus 로고
    • In vivo ubiquitination and proteasome-mediated degradation of p53
    • Maki, C.G., Huibregtse, J.M., and Howley, P.M. (1996). In vivo ubiquitination and proteasome-mediated degradation of p53. Cancer Res. 56, 2649-2654.
    • (1996) Cancer Res. , vol.56 , pp. 2649-2654
    • Maki, C.G.1    Huibregtse, J.M.2    Howley, P.M.3
  • 135
    • 0031844311 scopus 로고    scopus 로고
    • XRCC1 is specifically associate with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage
    • Masson, M., Niedergang, C., Schreiber, V., Muller, S., Menissier-de Murcia, J., and de Murcia, G. (1998). XRCC1 is specifically associate with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage. Mol. Cell. Biol. 18, 3563-3571.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3563-3571
    • Masson, M.1    Niedergang, C.2    Schreiber, V.3    Muller, S.4    Menissier-De Murcia, J.5    De Murcia, G.6
  • 136
    • 17544367892 scopus 로고    scopus 로고
    • Replication protein A confers structure-specific endonuclease activities to the XPF-ERCC1 and XPG subunits of human DNA repair excision nuclease
    • Matsunaga, T., Park, C.H., Bessho, R., Mu, D., and Sancar, A. (1996). Replication protein A confers structure-specific endonuclease activities to the XPF-ERCC1 and XPG subunits of human DNA repair excision nuclease. J. Biol. Chem. 271, 11047-11050.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11047-11050
    • Matsunaga, T.1    Park, C.H.2    Bessho, R.3    Mu, D.4    Sancar, A.5
  • 137
    • 0028366116 scopus 로고
    • D-type cyclin-binding regions of proliferating cell nuclear antigen
    • Matsuoka, S., Yamaguchi, M., and Matsukage, A. (1994). D-type cyclin-binding regions of proliferating cell nuclear antigen. J. Biol. Chem. 269, 11030-11036.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11030-11036
    • Matsuoka, S.1    Yamaguchi, M.2    Matsukage, A.3
  • 138
    • 0029880475 scopus 로고    scopus 로고
    • Demonstration of cyclin-dependent kinase inhibitory serine/threonine kinase in bovine thymus
    • Matsuura, I., and Wang, J.H. (1996). Demonstration of cyclin-dependent kinase inhibitory serine/threonine kinase in bovine thymus. J. Biol. Chem. 271, 5443-5450.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5443-5450
    • Matsuura, I.1    Wang, J.H.2
  • 139
    • 0030665146 scopus 로고    scopus 로고
    • Mdm2 phosphorylation by DNA-dependent protein kinase prevents interaction with p53
    • Mayo, L.D., Turchi, J.J., and Berberich, S.J. (1997). Mdm2 phosphorylation by DNA-dependent protein kinase prevents interaction with p53. Cancer Res. 57, 5013-5016.
    • (1997) Cancer Res. , vol.57 , pp. 5013-5016
    • Mayo, L.D.1    Turchi, J.J.2    Berberich, S.J.3
  • 140
    • 0002070843 scopus 로고    scopus 로고
    • The p130 pocket protein: Keeping order at cell cycle exit/re-entrance transitions
    • Mayol, X., and Grana, X. (1998). The p130 pocket protein: keeping order at cell cycle exit/re-entrance transitions. Front. Biosci. 3, d11-d24.
    • (1998) Front. Biosci. , vol.3
    • Mayol, X.1    Grana, X.2
  • 141
    • 0029028963 scopus 로고
    • Circuit simulation of genetic networks
    • McAdams, H.H., and Shapiro, L. (1995). Circuit simulation of genetic networks. Science 269, 650-656.
    • (1995) Science , vol.269 , pp. 650-656
    • McAdams, H.H.1    Shapiro, L.2
  • 142
    • 0031971228 scopus 로고    scopus 로고
    • Multisite phosphorylation and the integration of stress signals at p53
    • Meek, D.W. (1998). Multisite phosphorylation and the integration of stress signals at p53. Cell. Signal. 10, 159-166.
    • (1998) Cell. Signal. , vol.10 , pp. 159-166
    • Meek, D.W.1
  • 143
    • 0030825813 scopus 로고    scopus 로고
    • p53 protein stability in tumor cells is not determined by mutation but is dependent on Mdm2 binding
    • Midgley, C.A., and Lane, D.P. (1997). p53 protein stability in tumor cells is not determined by mutation but is dependent on Mdm2 binding. Oncogene 15, 1179-1189.
    • (1997) Oncogene , vol.15 , pp. 1179-1189
    • Midgley, C.A.1    Lane, D.P.2
  • 144
    • 0030899811 scopus 로고    scopus 로고
    • Complex formation between p53 and replication protein A inhibits the sequence-specific DNA binding of p53 and is regulated by single-stranded DNA
    • Miller, S.D., Moses, K., Jayaraman, L., and Prives, C. (1997). Complex formation between p53 and replication protein A inhibits the sequence-specific DNA binding of p53 and is regulated by single-stranded DNA. Mol. Cell. Biol. 17, 2194-2201.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2194-2201
    • Miller, S.D.1    Moses, K.2    Jayaraman, L.3    Prives, C.4
  • 145
    • 0028966941 scopus 로고
    • p53 is phosphorylated in vitro and in vivo by an UV radiation-induced protein kinase characteristic of the c-Jun kinase, JNK1
    • Milne, D., Campbell, L., Campbell, D., and Meek, D. (1995). p53 is phosphorylated in vitro and in vivo by an UV radiation-induced protein kinase characteristic of the c-Jun kinase, JNK1. J. Biol. Chem. 270, 5511-5518.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5511-5518
    • Milne, D.1    Campbell, L.2    Campbell, D.3    Meek, D.4
  • 146
    • 0028363749 scopus 로고
    • Phosphorylation of the tumor suppressor protein p53 by mitogen-activated protein kinases
    • Milne, D., Campbell, D., Caudwell, F., and Meek, D. (1994). Phosphorylation of the tumor suppressor protein p53 by mitogen-activated protein kinases. J. Biol. Chem. 269, 9253-9260.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9253-9260
    • Milne, D.1    Campbell, D.2    Caudwell, F.3    Meek, D.4
  • 147
    • 0027227980 scopus 로고
    • Dominant negative alleles of RAD52 reveal a DNA repair/recombination complex including Rad51 and Rad52
    • Milne, G.T., and Weaver, D.T. (1993). Dominant negative alleles of RAD52 reveal a DNA repair/recombination complex including Rad51 and Rad52. Genes & Dev. 7, 1755-1765.
    • (1993) Genes & Dev. , vol.7 , pp. 1755-1765
    • Milne, G.T.1    Weaver, D.T.2
  • 148
    • 0029911744 scopus 로고    scopus 로고
    • Analysis of incision sites produced by human cell extracts and purified proteins during nucleotide excision repair of a 1,3-intrastrand d(GpTpG)-cisplatin adduct
    • Moggs, J.G., Yarema, K.J., Essigmann, J.M., and Wood, R.D. (1996). Analysis of incision sites produced by human cell extracts and purified proteins during nucleotide excision repair of a 1,3-intrastrand d(GpTpG)-cisplatin adduct. J. Biol. Chem. 271, 7177-7186.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7177-7186
    • Moggs, J.G.1    Yarema, K.J.2    Essigmann, J.M.3    Wood, R.D.4
  • 149
    • 0026649648 scopus 로고
    • The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p5 -mediated transactivation
    • Momand, J., Zambetti, G.P., Olson, D.C., George, D., and Levine, A.J. (1992). The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p5 -mediated transactivation. Cell 69, 1237-1245.
    • (1992) Cell , vol.69 , pp. 1237-1245
    • Momand, J.1    Zambetti, G.P.2    Olson, D.C.3    George, D.4    Levine, A.J.5
  • 151
    • 0028931265 scopus 로고
    • Principles of CDK regulation
    • Morgan, D.O. (1995). Principles of CDK regulation. Nature 374, 131-134.
    • (1995) Nature , vol.374 , pp. 131-134
    • Morgan, D.O.1
  • 152
    • 0030034524 scopus 로고    scopus 로고
    • Transcriptional activation of the human proliferating cell nuclear antigen promoter by p53
    • Morris, G.F., Bischoff, J.R., and Mathews, M.B. (1996). Transcriptional activation of the human proliferating cell nuclear antigen promoter by p53. Proc. Natl. Acad. Sci. USA 93, 895-899.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 895-899
    • Morris, G.F.1    Bischoff, J.R.2    Mathews, M.B.3
  • 153
    • 0031038379 scopus 로고    scopus 로고
    • Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen
    • Mossi, R., Jonsson, Z.O., Allen, B.L., Hardin, S.H., and Hubacher, U. (1997). Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen. J. Biol. Chem. 272, 1769-1776.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1769-1776
    • Mossi, R.1    Jonsson, Z.O.2    Allen, B.L.3    Hardin, S.H.4    Hubacher, U.5
  • 154
    • 0029870677 scopus 로고    scopus 로고
    • Reaction-mechanism of human DNA-repair excision nuclease
    • Mu, D., Hsu, D.S., and Sancar, A. (1996). Reaction-mechanism of human DNA-repair excision nuclease. J. Biol. Chem. 271, 8285-8294.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8285-8294
    • Mu, D.1    Hsu, D.S.2    Sancar, A.3
  • 156
    • 0030944206 scopus 로고    scopus 로고
    • Model for XPC-independent transcription-coupled repair of pyrimidine dimers in humans
    • Mu, D., and Sancar, A. (1997). Model for XPC-independent transcription-coupled repair of pyrimidine dimers in humans. J. Biol. Chem. 272, 7570-7573.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7570-7573
    • Mu, D.1    Sancar, A.2
  • 157
    • 0030925492 scopus 로고    scopus 로고
    • KARP-1: A novel leucine zipper protein expressed from the Ku86 autoantigen locus is implicated in the control of DNA-dependent protein kinase activity
    • Myung, K., He, D.M., Lee, S.E., and Hendrickson, E.A. (1997). KARP-1: a novel leucine zipper protein expressed from the Ku86 autoantigen locus is implicated in the control of DNA-dependent protein kinase activity. EMBO J. 16, 3172-3184.
    • (1997) EMBO J. , vol.16 , pp. 3172-3184
    • Myung, K.1    He, D.M.2    Lee, S.E.3    Hendrickson, E.A.4
  • 158
    • 0032560473 scopus 로고    scopus 로고
    • KARP-1 is induced by DNA damage in a p53- and ataxia telangiectasia mutated-dependent manner
    • Myung, K., Braastad, C., He, D.M., and Hendrickson, E.A. (1998). KARP-1 is induced by DNA damage in a p53- and ataxia telangiectasia mutated-dependent manner. Proc. Natl. Acad. Sci. USA 95, 7664-7669.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7664-7669
    • Myung, K.1    Braastad, C.2    He, D.M.3    Hendrickson, E.A.4
  • 159
    • 0030996226 scopus 로고    scopus 로고
    • A sequence in the N-terminal region of human uracil-DNA glycosylase with homology to XPA interacts with the C-terminal part of the 34-kDa subunit of replication protein a
    • Nagelhus, T.A., et al. (1997). A sequence in the N-terminal region of human uracil-DNA glycosylase with homology to XPA interacts with the C-terminal part of the 34-kDa subunit of replication protein A. J. Biol. Chem. 272, 6561-6566.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6561-6566
    • Nagelhus, T.A.1
  • 160
    • 0032962641 scopus 로고    scopus 로고
    • Requirement of ATM in phosphorylation of the human p53 protein at serine 15 following DNA double-strand breaks
    • Nakagawa, K., Taya, Y., Tamai, K., and Yamaizumi, M. (1999). Requirement of ATM in phosphorylation of the human p53 protein at serine 15 following DNA double-strand breaks. Mol. Cell. Biol. 19, 2828-2834.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2828-2834
    • Nakagawa, K.1    Taya, Y.2    Tamai, K.3    Yamaizumi, M.4
  • 163
    • 0031815596 scopus 로고    scopus 로고
    • Toward an understanding of the functional complexity of the E2F and retinoblastoma families
    • Nevins, J.R. (1998). Toward an understanding of the functional complexity of the E2F and retinoblastoma families. Cell Growth Differ. 9, 585-593.
    • (1998) Cell Growth Differ. , vol.9 , pp. 585-593
    • Nevins, J.R.1
  • 164
    • 0032556870 scopus 로고    scopus 로고
    • Rad52 protein stimulates DNA strand exchange by Rad51 and replication
    • New, J., Sugiyama, T., Zaitseva, E., and Kowalczykowski, S. (1998). Rad52 protein stimulates DNA strand exchange by Rad51 and replication. Nature 391, 407-410.
    • (1998) Nature , vol.391 , pp. 407-410
    • New, J.1    Sugiyama, T.2    Zaitseva, E.3    Kowalczykowski, S.4
  • 165
    • 0030924695 scopus 로고    scopus 로고
    • Mapping of amino acid residues in the p34 subunit of human single-stranded DNA-binding protein phosphorylated by DNA-dependent protein kinase and cdc2 kinase in vitro
    • Niu, H., Erdjumeni-Bromage, H., Pan, Z.-Q., Lee, S.-H., Tempst, P., and Hurwitz, J. (1997). Mapping of amino acid residues in the p34 subunit of human single-stranded DNA-binding protein phosphorylated by DNA-dependent protein kinase and cdc2 kinase in vitro. J. Biol. Chem. 272, 12634-12641.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12634-12641
    • Niu, H.1    Erdjumeni-Bromage, H.2    Pan, Z.-Q.3    Lee, S.-H.4    Tempst, P.5    Hurwitz, J.6
  • 166
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko, V.V., Schiltz, R.L., Russanova, V., Howard, B.H., and Nakatani, Y. (1996). The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87, 953-959.
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 168
    • 0028129498 scopus 로고
    • Cyclin D1-mediated inhibition of repair and replicative DNA synthesis in human fibroblasts
    • Pagano, M., Theodoras, A.M., Tam, S.W., and Draetta, G.F. (1994). Cyclin D1-mediated inhibition of repair and replicative DNA synthesis in human fibroblasts. Genes & Dev. 8, 1627-1639.
    • (1994) Genes & Dev. , vol.8 , pp. 1627-1639
    • Pagano, M.1    Theodoras, A.M.2    Tam, S.W.3    Draetta, G.F.4
  • 169
    • 0027203552 scopus 로고
    • Reconstitution of cyclin-dependent cdc2 and cdk2 kinase activities in vitro
    • Pan, Z.-Q., and Hurwitz, J. (1993). Reconstitution of cyclin-dependent cdc2 and cdk2 kinase activities in vitro. J. Biol. Chem. 268, 20443-20451.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20443-20451
    • Pan, Z.-Q.1    Hurwitz, J.2
  • 170
    • 0029768921 scopus 로고    scopus 로고
    • Physical interaction between human RAD52 and RPA is required for homologous recombination in mammalian cells
    • Park, M.S., Ludwig, D.L., Stigger, E., and Lee, S.H. (1996). Physical interaction between human RAD52 and RPA is required for homologous recombination in mammalian cells. J. Biol. Chem. 271, 18996-19000.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18996-19000
    • Park, M.S.1    Ludwig, D.L.2    Stigger, E.3    Lee, S.H.4
  • 172
    • 0030611095 scopus 로고    scopus 로고
    • Mitotic and G2 checkpoint control: Regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216
    • Peng, C.-Y., Graves, P.R., Thoma, R.S., Wu, Z., Shaw, A.S., and Piwnica-Worms, H. (1997). Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216. Science 277, 1501-1505.
    • (1997) Science , vol.277 , pp. 1501-1505
    • Peng, C.-Y.1    Graves, P.R.2    Thoma, R.S.3    Wu, Z.4    Shaw, A.S.5    Piwnica-Worms, H.6
  • 173
    • 0030614504 scopus 로고    scopus 로고
    • Regulation of NF-κB by cyclin-dependent kinases associated with the p300 coactivator
    • Perkins, N.D., Felzien, L.K., Betts, J.C., Leung, K., Beach, D.H., and Nabel, G.J. (1997). Regulation of NF-κB by cyclin-dependent kinases associated with the p300 coactivator. Science 275, 523-527.
    • (1997) Science , vol.275 , pp. 523-527
    • Perkins, N.D.1    Felzien, L.K.2    Betts, J.C.3    Leung, K.4    Beach, D.H.5    Nabel, G.J.6
  • 174
    • 0027933911 scopus 로고
    • The differential localization of human cyclins A and B is due to a cytoplasmic retention signal in cyclin B
    • Pines, J., and Hunter, T. (1994). The differential localization of human cyclins A and B is due to a cytoplasmic retention signal in cyclin B. EMBO J. 13, 3772-3781.
    • (1994) EMBO J. , vol.13 , pp. 3772-3781
    • Pines, J.1    Hunter, T.2
  • 175
    • 0032549704 scopus 로고    scopus 로고
    • The ink4a tumor suppressor gene product, p19arf, interacts with MDM2 and neutralizes MDM2's inhibition of p53
    • Pomerantz, J., et al. (1998). The ink4a tumor suppressor gene product, p19arf, interacts with MDM2 and neutralizes MDM2's inhibition of p53. Cell 92, 713-723.
    • (1998) Cell , vol.92 , pp. 713-723
    • Pomerantz, J.1
  • 176
    • 0032475878 scopus 로고    scopus 로고
    • Signaling to p53:Breaking the MDM2-p53 circuit
    • Prives, C. (1998). Signaling to p53:breaking the MDM2-p53 circuit. Cell 95, 5-8.
    • (1998) Cell , vol.95 , pp. 5-8
    • Prives, C.1
  • 177
    • 11944262588 scopus 로고
    • Regulation of the level of the oncoprotein p53 in nontransformed and transformed cells
    • Reihsaus, E., Kohler, M., Kraiss, S., Oren, M., and Montenarh, M. (1990). Regulation of the level of the oncoprotein p53 in nontransformed and transformed
    • (1990) Oncogene , vol.5 , pp. 137-145
    • Reihsaus, E.1    Kohler, M.2    Kraiss, S.3    Oren, M.4    Montenarh, M.5
  • 178
    • 0032518917 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human HIV rev protein
    • Roth, J., Dobbelstein, M., Freedman, D., Shenk, T., and Levine, A.J. (1998). Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human HIV rev protein. EMBO J. 17, 554-564.
    • (1998) EMBO J. , vol.17 , pp. 554-564
    • Roth, J.1    Dobbelstein, M.2    Freedman, D.3    Shenk, T.4    Levine, A.J.5
  • 181
    • 0029828941 scopus 로고    scopus 로고
    • Sequential binding of DNA repair proteins RPA and ERCC1 to XPA in vitro
    • Saijo, M., Kuraoka, I., Masutani, C., Hanaoka, F., and Tanaka, K. (1996). Sequential binding of DNA repair proteins RPA and ERCC1 to XPA in vitro. Nucleic Acids Res. 24, 4719-4724.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4719-4724
    • Saijo, M.1    Kuraoka, I.2    Masutani, C.3    Hanaoka, F.4    Tanaka, K.5
  • 183
    • 0030790778 scopus 로고    scopus 로고
    • Phosphorylation of serine 392 stabilizes the tetramer formation of tumor suppressor protein p53
    • Sakaguchi, K., Sakamoto, H., Lewis, M.S., Anderson, C.W., Erickson, J.W., Appella, E., and Xie, D. (1997). Phosphorylation of serine 392 stabilizes the tetramer formation of tumor suppressor protein p53. Biochemistry 36, 10117-10124.
    • (1997) Biochemistry , vol.36 , pp. 10117-10124
    • Sakaguchi, K.1    Sakamoto, H.2    Lewis, M.S.3    Anderson, C.W.4    Erickson, J.W.5    Appella, E.6    Xie, D.7
  • 184
    • 0030867582 scopus 로고    scopus 로고
    • Conservation of the Chk1 checkpoint pathway in mammals: Linkage of DNA damage to Cdk regulation through Cdc25
    • Sanchez, Y., Wong, C., Thoma, R.S., Richman, R., Wu, Z., Piwnica-Worms, H., and Elledge, S.J. (1997). Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to Cdk regulation through Cdc25. Science 277, 1497-1501.
    • (1997) Science , vol.277 , pp. 1497-1501
    • Sanchez, Y.1    Wong, C.2    Thoma, R.S.3    Richman, R.4    Wu, Z.5    Piwnica-Worms, H.6    Elledge, S.J.7
  • 185
    • 0030850047 scopus 로고    scopus 로고
    • Dynamic changes of BRCA1 subnuclear location and phosphorylation state are initiated by DNA damage
    • Scully, R., Chen, J., Ochs, R.L., Keegan, K., Hoekstra, M., Feunteun, J., and Livingston, D.M. (1997a). Dynamic changes of BRCA1 subnuclear location and phosphorylation state are initiated by DNA damage. Cell 90, 425-435.
    • (1997) Cell , vol.90 , pp. 425-435
    • Scully, R.1    Chen, J.2    Ochs, R.L.3    Keegan, K.4    Hoekstra, M.5    Feunteun, J.6    Livingston, D.M.7
  • 187
    • 0028238213 scopus 로고
    • Immediate early up-regulation of bax expression by p53 but not TGFβ1: A paradigm for distinct apoptotic pathways
    • Selvakumaran, M., Lin, H.K., Miyatashita, T., Wang, H.G., Krajewski, S., Reed, J.C., Hoffman, B., and Liebermann, D. (1994a). Immediate early up-regulation of bax expression by p53 but not TGFβ1: a paradigm for distinct apoptotic pathways. Oncogene 9, 1791-8.
    • (1994) Oncogene , vol.9 , pp. 1791-1798
    • Selvakumaran, M.1    Lin, H.K.2    Miyatashita, T.3    Wang, H.G.4    Krajewski, S.5    Reed, J.C.6    Hoffman, B.7    Liebermann, D.8
  • 188
    • 0028331457 scopus 로고
    • The novel primary response gene MyD118 and the proto-oncogenes myb, myc, and bcl-2 modulate transforming growth factor beta 1-induced apoptosis of myeloid leukemia cells
    • Selvakumaran, M., Lin, H.K., Sjin, R.T.T., Reed, J.C., Liebermann, D., and Hoffman, B. (1994b). The novel primary response gene MyD118 and the proto-oncogenes myb, myc, and bcl-2 modulate transforming growth factor beta 1-induced apoptosis of myeloid leukemia cells. Mol. Cell. Biol. 14, 2352-2360.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2352-2360
    • Selvakumaran, M.1    Lin, H.K.2    Sjin, R.T.T.3    Reed, J.C.4    Liebermann, D.5    Hoffman, B.6
  • 189
    • 0032489377 scopus 로고    scopus 로고
    • Cyclin-dependent kinase inhibitor p16INK4A inhibits phosphorylation of RNA polymerase II by general transcription factor TFIIH
    • Serizawa, H. (1998). Cyclin-dependent kinase inhibitor p16INK4A inhibits phosphorylation of RNA polymerase II by general transcription factor TFIIH. J. Biol. Chem. 273, 5427-5430.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5427-5430
    • Serizawa, H.1
  • 190
    • 0029805888 scopus 로고    scopus 로고
    • The molecular basis of E2F-1/DP-1-induced S-phase entry and apoptosis
    • Shan, B., Farmer, A.A., and Lee, W.H. (1996). The molecular basis of E2F-1/DP-1-induced S-phase entry and apoptosis. Cell Growth & Differ. 7, 689-697.
    • (1996) Cell Growth & Differ. , vol.7 , pp. 689-697
    • Shan, B.1    Farmer, A.A.2    Lee, W.H.3
  • 191
    • 0033104517 scopus 로고    scopus 로고
    • Replication-mediated DNA damage by camptothecin induces phosphorylation of RPA by DNA-dependent protein kinase and dissociates DNA-PK/RPA complexes
    • Shao, R.-G., Cao, C.-X., Zhang, H., Kohn, K.W., Wold, M.S., and Pommier, Y. (1999). Replication-mediated DNA damage by camptothecin induces phosphorylation of RPA by DNA-dependent protein kinase and dissociates DNA-PK/RPA complexes. EMBO J. 18, 1397-1406.
    • (1999) EMBO J. , vol.18 , pp. 1397-1406
    • Shao, R.-G.1    Cao, C.-X.2    Zhang, H.3    Kohn, K.W.4    Wold, M.S.5    Pommier, Y.6
  • 193
    • 0032191393 scopus 로고    scopus 로고
    • Tumor surveillance via the ARF-p53 pathway
    • Sherr, C.J. (1998). Tumor surveillance via the ARF-p53 pathway. Genes & Dev. 12, 2984-2991.
    • (1998) Genes & Dev. , vol.12 , pp. 2984-2991
    • Sherr, C.J.1
  • 194
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh, S., Ikeda, M., Taya, Y., and Prives, C. (1997). DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell 91, 325-334.
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 195
    • 0033118933 scopus 로고    scopus 로고
    • DNA damage-inducible phosphorylation of p53 at N-terminal sites including a novel site, Ser20, requires tetramerization
    • Shieh, S.-Y., Taya, Y., and Prives, C. (1999). DNA damage-inducible phosphorylation of p53 at N-terminal sites including a novel site, Ser20, requires tetramerization. EMBO J. 18, 1815-1823.
    • (1999) EMBO J. , vol.18 , pp. 1815-1823
    • Shieh, S.-Y.1    Taya, Y.2    Prives, C.3
  • 196
    • 0028868432 scopus 로고
    • Wild-type human p53 transactivates the human proliferating cell nuclear antigen promoter
    • Shivakumar, C.V., Brown, D.R., Deb, S., and Deb, S.F. (1995). Wild-type human p53 transactivates the human proliferating cell nuclear antigen promoter. Mol. Cell. Biol. 15, 6785-6795.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6785-6795
    • Shivakumar, C.V.1    Brown, D.R.2    Deb, S.3    Deb, S.F.4
  • 201
    • 0031741234 scopus 로고    scopus 로고
    • Failure of hairpin-ended and nicked DNA to activate DNA-dependent protein kinase: Implications for V(D)J recombination
    • Smider, V., Rathmell, W.K., Brown, G., Lewis, S., and Chu, G. (1998). Failure of hairpin-ended and nicked DNA to activate DNA-dependent protein kinase: implications for V(D)J recombination. Mol. Cell. Biol. 18, 6853-6858.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6853-6858
    • Smider, V.1    Rathmell, W.K.2    Brown, G.3    Lewis, S.4    Chu, G.5
  • 204
    • 0032533860 scopus 로고    scopus 로고
    • The COOH-terminal region of pRb2/p130 binds to histone deacetylase 1 (HDAC1), enhancing transcriptional repression of the E2F-dependent cyclin A promoter
    • Stiegler, P., De Luca, A., Bagella, L., and Giordano, A. (1998). The COOH-terminal region of pRb2/p130 binds to histone deacetylase 1 (HDAC1), enhancing transcriptional repression of the E2F-dependent cyclin A promoter. Cancer Res. 58, 5049-5052.
    • (1998) Cancer Res. , vol.58 , pp. 5049-5052
    • Stiegler, P.1    De Luca, A.2    Bagella, L.3    Giordano, A.4
  • 205
    • 0028157927 scopus 로고
    • Reconstitution of functional human single-stranded DNA binding protein from individual subunits expressed by recombinant baculoviruses
    • Stigger, E., Dean, F.B., Hurwitz, J., and Lee, S.-H. (1994). Reconstitution of functional human single-stranded DNA binding protein from individual subunits expressed by recombinant baculoviruses. Proc. Natl. Acad. Sci. USA 91, 579-583.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 579-583
    • Stigger, E.1    Dean, F.B.2    Hurwitz, J.3    Lee, S.-H.4
  • 206
    • 0032502760 scopus 로고    scopus 로고
    • Functional analysis of human replication protein A in nucleotide excision repair
    • Stigger, E., Drissi, R., and Lee, S.-H. (1998). Functional analysis of human replication protein A in nucleotide excision repair. J. Biol. Chem. 273, 9337-9343.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9337-9343
    • Stigger, E.1    Drissi, R.2    Lee, S.-H.3
  • 207
    • 0032169516 scopus 로고    scopus 로고
    • The alternative product from the human CDKN2A locus, p14(ARF), participates in a regulatory feedback loop with p53 and MDM2
    • Stott, F.J., et al. (1998). The alternative product from the human CDKN2A locus, p14(ARF), participates in a regulatory feedback loop with p53 and MDM2. EMBO J. 17, 5001-5014.
    • (1998) EMBO J. , vol.17 , pp. 5001-5014
    • Stott, F.J.1
  • 209
    • 0030688064 scopus 로고    scopus 로고
    • Two human homologs of rad23 are functionally interchangeable in complex formation and stimulation of XPC repair activity
    • Sugasawa, K., et al. (1997). Two human homologs of Rad23 are functionally interchangeable in complex formation and stimulation of XPC repair activity. Mol. Cell. Biol. 17, 6924-6931.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6924-6931
    • Sugasawa, K.1
  • 210
    • 0028966935 scopus 로고
    • Regulation of the sequence-specific DNA binding function of p53 by protein kinase C and protein phosphatases
    • Takenaka, I., Morin, F., Seizinger, B., and Kley, N. (1995). Regulation of the sequence-specific DNA binding function of p53 by protein kinase C and protein phosphatases. J. Biol. Chem. 270, 5405-5411.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5405-5411
    • Takenaka, I.1    Morin, F.2    Seizinger, B.3    Kley, N.4
  • 211
    • 0032031417 scopus 로고    scopus 로고
    • The caspase-RB connection in cell death
    • Tan, X.Q., and Wang, J.Y.J. (1998). The caspase-RB connection in cell death. Trends Cell Biol. 8, 116-120.
    • (1998) Trends Cell Biol. , vol.8 , pp. 116-120
    • Tan, X.Q.1    Wang, J.Y.J.2
  • 212
    • 0032980646 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53
    • Tao, W., and Levine, A.J. (1999). Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53. Proc. Natl. Acad. Sci. USA 96, 3077-3080.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3077-3080
    • Tao, W.1    Levine, A.J.2
  • 213
    • 0028089946 scopus 로고
    • Cell cycle analysis of the activity, subcellular localization, and subunit composition of human CAK (CDK-activating kinase)
    • Tassan, J.P., Schultz, S.J., Bartek, J., and Nigg, E.A. (1994). Cell cycle analysis of the activity, subcellular localization, and subunit composition of human CAK (CDK-activating kinase). J. Cell Biol. 127, 467-478.
    • (1994) J. Cell Biol. , vol.127 , pp. 467-478
    • Tassan, J.P.1    Schultz, S.J.2    Bartek, J.3    Nigg, E.A.4
  • 214
    • 0029014496 scopus 로고
    • Requirement for tyrosine phosphorylation of cdk4 in G1 arrest induced by UV irradiation
    • Terada, Y., Tatsuka, M., Jinno, S., and Okayama, H. (1995). Requirement for tyrosine phosphorylation of cdk4 in G1 arrest induced by UV irradiation. Nature 376, 358-362.
    • (1995) Nature , vol.376 , pp. 358-362
    • Terada, Y.1    Tatsuka, M.2    Jinno, S.3    Okayama, H.4
  • 215
    • 0242464153 scopus 로고    scopus 로고
    • HBP1 - An HMG box transcriptional repressor that is targeted by the retinoblastoma family
    • Tevosian, S.G., Shih, H.H., Mendelson, K.G., Sheppard, K.A., Paulson, K.E., and Yee, A.S. (1997). HBP1 - an HMG box transcriptional repressor that is targeted by the retinoblastoma family. Genes & Dev. 11, 383-396.
    • (1997) Genes & Dev. , vol.11 , pp. 383-396
    • Tevosian, S.G.1    Shih, H.H.2    Mendelson, K.G.3    Sheppard, K.A.4    Paulson, K.E.5    Yee, A.S.6
  • 216
    • 0032127947 scopus 로고    scopus 로고
    • Suppression of the p300-dependent mdm2 negative-feedback loop induces the p53 apoptotic function
    • Thomas, A., and White, E. (1998). Suppression of the p300-dependent mdm2 negative-feedback loop induces the p53 apoptotic function. Genes & Dev. 12, 1975-1985.
    • (1998) Genes & Dev. , vol.12 , pp. 1975-1985
    • Thomas, A.1    White, E.2
  • 218
    • 0030860911 scopus 로고    scopus 로고
    • Repression of p53-mediated transcription by MDM2: A dual mechanism
    • Thut, C.J., Goodrich, J.A., and Tjian, R. (1997). Repression of p53-mediated transcription by MDM2: a dual mechanism. Genes & Dev. 11, 1974-86.
    • (1997) Genes & Dev. , vol.11 , pp. 1974-1986
    • Thut, C.J.1    Goodrich, J.A.2    Tjian, R.3
  • 220
    • 0027997561 scopus 로고
    • Detecting the ability of viral, bacterial and eukaryotic replication proteins to track along DNA
    • Tinker, R.L., Kassavetis, G.A., and Geiduschek, E.P. (1994). Detecting the ability of viral, bacterial and eukaryotic replication proteins to track along DNA. EMBO J. 13, 5330-5337.
    • (1994) EMBO J. , vol.13 , pp. 5330-5337
    • Tinker, R.L.1    Kassavetis, G.A.2    Geiduschek, E.P.3
  • 222
    • 0032474838 scopus 로고    scopus 로고
    • A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity
    • Tzivion, G., Luo, Z., and Avruch, J. (1998). A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity. Nature 394, 88-92.
    • (1998) Nature , vol.394 , pp. 88-92
    • Tzivion, G.1    Luo, Z.2    Avruch, J.3
  • 224
    • 0030761351 scopus 로고    scopus 로고
    • ATM-dependent telomere loss in aging human diploid fibroblasts and DNA damage lead to the posttranslational activation of p53 protein involving poly(ADP-ribose) polymerase
    • Vaziri, H., West, M.D., Allsopp, R.C., Davison, T.S., Wu, Y.-S., Arrowsmith, C.H., Poirier, G.G., and Benchimol, S. (1997). ATM-dependent telomere loss in aging human diploid fibroblasts and DNA damage lead to the posttranslational activation of p53 protein involving poly(ADP-ribose) polymerase. EMBO J. 19, 6018-6033.
    • (1997) EMBO J. , vol.19 , pp. 6018-6033
    • Vaziri, H.1    West, M.D.2    Allsopp, R.C.3    Davison, T.S.4    Wu, Y.-S.5    Arrowsmith, C.H.6    Poirier, G.G.7    Benchimol, S.8
  • 226
    • 0032499719 scopus 로고    scopus 로고
    • Assembly, subunit composition and footprint of human DNA repair excision nuclease
    • Wakasugi, M., and Sancar, A. (1998). Assembly, subunit composition and footprint of human DNA repair excision nuclease. Proc. Natl. Acad. Sci. USA 95, 6669-6674.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6669-6674
    • Wakasugi, M.1    Sancar, A.2
  • 227
    • 0031724929 scopus 로고    scopus 로고
    • Raf-1 physically interacts with rb and regulates its function: A link between mitogenic signaling and cell cycle regulation
    • Wang, S., Ghosh, R.N., and Chellappan, S.P. (1998). Raf-1 physically interacts with Rb and regulates its function: a link between mitogenic signaling and cell cycle regulation. Mol. Cell. Biol. 18, 7487-7498.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7487-7498
    • Wang, S.1    Ghosh, R.N.2    Chellappan, S.P.3
  • 228
    • 0028989236 scopus 로고
    • p53 modulation of TFIIH-associated nucleotide excision repair activity
    • Wang, X., et al. (1995). p53 modulation of TFIIH-associated nucleotide excision repair activity. Nat. Genet. 10, 188-195.
    • (1995) Nat. Genet. , vol.10 , pp. 188-195
    • Wang, X.1
  • 229
    • 0029003061 scopus 로고
    • Increased and altered DNA binding of human p53 by S and G2/M but not G1 cyclin-dependent kinases
    • Wang, Y., and Prives, C. (1995). Increased and altered DNA binding of human p53 by S and G2/M but not G1 cyclin-dependent kinases. Nature 376, 88-91.
    • (1995) Nature , vol.376 , pp. 88-91
    • Wang, Y.1    Prives, C.2
  • 230
    • 0031816342 scopus 로고    scopus 로고
    • Inhibition of cyclin D1 kinase activity is associated with E2F-mediated inhibition of cyclin D1 promoter activity through E2F and Sp1
    • Watanabe, G., Albanese, C., Lee, R.J., Reutens, A., Vairo, G., Henglein, B., and Pestell, R.G. (1998). Inhibition of cyclin D1 kinase activity is associated with E2F-mediated inhibition of cyclin D1 promoter activity through E2F and Sp1. Mol. Cell. Biol. 18, 3212-3222.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3212-3222
    • Watanabe, G.1    Albanese, C.2    Lee, R.J.3    Reutens, A.4    Vairo, G.5    Henglein, B.6    Pestell, R.G.7
  • 231
    • 0031840253 scopus 로고    scopus 로고
    • ATM-dependent activation of p53 involves dephosphorylation and association with 14-3-3
    • Waterman, M.J.F., Stavridi, E.S., Waterman, J.L.F., and Halazonetis, T.D. (1998). ATM-dependent activation of p53 involves dephosphorylation and association with 14-3-3. Nat. Genet. 19, 175-178.
    • (1998) Nat. Genet. , vol.19 , pp. 175-178
    • Waterman, M.J.F.1    Stavridi, E.S.2    Waterman, J.L.F.3    Halazonetis, T.D.4
  • 232
    • 0029033861 scopus 로고
    • The retinoblastoma protein and cell cycle control
    • Weinberg, R.A. (1995). The retinoblastoma protein and cell cycle control. Cell 81, 323-330.
    • (1995) Cell , vol.81 , pp. 323-330
    • Weinberg, R.A.1
  • 233
    • 0028802094 scopus 로고
    • Disruption of retinoblastoma protein function by coexpression of its C pocket fragment
    • Welch, P.J., and Wang, J.Y.J. (1995). Disruption of retinoblastoma protein function by coexpression of its C pocket fragment. Genes & Dev. 9, 31-46.
    • (1995) Genes & Dev. , vol.9 , pp. 31-46
    • Welch, P.J.1    Wang, J.Y.J.2
  • 234
    • 0030570439 scopus 로고    scopus 로고
    • ADP-ribosylation of wild-type p53 in vitro: Binding of p53 to specific p533 consensus sequence prevents its modification
    • Wesierska, J., Schmid, H., and Cerni, C. (1996). ADP-ribosylation of wild-type p53 in vitro: binding of p53 to specific p533 consensus sequence prevents its modification. Biochem. Biophys. Res. Commun. 224, 96-102.
    • (1996) Biochem. Biophys. Res. Commun. , vol.224 , pp. 96-102
    • Wesierska, J.1    Schmid, H.2    Cerni, C.3
  • 235
    • 0031708232 scopus 로고    scopus 로고
    • Productive and nonproductive complexes of Ku and DNA-dependent protein kinase at DNA termini
    • West, R.B., Yaneva, M., and Lieber, M.R. (1998). Productive and nonproductive complexes of Ku and DNA-dependent protein kinase at DNA termini. Mol. Cell. Biol. 18, 5908-5920.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5908-5920
    • West, R.B.1    Yaneva, M.2    Lieber, M.R.3
  • 236
    • 0031862730 scopus 로고    scopus 로고
    • Growth suppression by an E2F-binding-defective retinoblastoma protein (RB): Contribution from the RB C pocket
    • Whitaker, L.L., Su, H., Baskaran, R., Knudsen, E.S., and Wang, J.Y.J. (1998). Growth suppression by an E2F-binding-defective retinoblastoma protein (RB): contribution from the RB C pocket. Mol. Cell. Biol. 18, 4032-4042.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4032-4042
    • Whitaker, L.L.1    Su, H.2    Baskaran, R.3    Knudsen, E.S.4    Wang, J.Y.J.5
  • 237
    • 0030908093 scopus 로고    scopus 로고
    • Replication protein a: A heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism
    • Wold, M.S. (1997). Replication protein A: a heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism. Annu. Rev. Biochem. 66, 61-92.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 61-92
    • Wold, M.S.1
  • 238
    • 0029737650 scopus 로고    scopus 로고
    • Activation of cyclin E/cdk2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E
    • Won, K.A., and Reed, S.I. (1996). Activation of cyclin E/cdk2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E. EMBO J. 15, 4182-4193.
    • (1996) EMBO J. , vol.15 , pp. 4182-4193
    • Won, K.A.1    Reed, S.I.2
  • 239
    • 0027244853 scopus 로고
    • The p53-mdm2 autoregulatory feedback loop
    • Wu, X., Bayle, J.H., Olson, D., and Levine, A.J. (1993). The p53-mdm2 autoregulatory feedback loop. Genes & Dev. 7, 1126-1132.
    • (1993) Genes & Dev. , vol.7 , pp. 1126-1132
    • Wu, X.1    Bayle, J.H.2    Olson, D.3    Levine, A.J.4
  • 240
    • 0029885134 scopus 로고    scopus 로고
    • Processing of branched DNA intermediates by a complex of human FEN-1 and PCNA
    • Wu, X., Li, J., Li, X., Hsieh, C.L., Burgers, P.M., and Lieber, M.R. (1996). Processing of branched DNA intermediates by a complex of human FEN-1 and PCNA. Nucleic Acids Res. 24, 2036-2043.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2036-2043
    • Wu, X.1    Li, J.2    Li, X.3    Hsieh, C.L.4    Burgers, P.M.5    Lieber, M.R.6
  • 242
    • 0032947176 scopus 로고    scopus 로고
    • p53-mediated regulation of proliferating cell nuclear antigen expression in cells exposed to ionizing radiation
    • Xu, J., and Morris, G.F. (1999). p53-mediated regulation of proliferating cell nuclear antigen expression in cells exposed to ionizing radiation. Mol. Cell. Biol. 19, 12-20.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 12-20
    • Xu, J.1    Morris, G.F.2
  • 243
    • 0028019279 scopus 로고
    • Cyclin A/CDK2 binds directly to E2F1 and inhibits the DNA-binding activity of E2F1/DP1 by phosphorylation
    • Xu, M., Sheppard, K.A., Peng, C.Y., Yee, A.S., and Piwnica-Worms, H. (1994). Cyclin A/CDK2 binds directly to E2F1 and inhibits the DNA-binding activity of E2F1/DP1 by phosphorylation. Mol. Cell. Biol. 14, 8420-8431.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8420-8431
    • Xu, M.1    Sheppard, K.A.2    Peng, C.Y.3    Yee, A.S.4    Piwnica-Worms, H.5
  • 244
    • 0032954205 scopus 로고    scopus 로고
    • Regulation of cyclin A-Cdk2 by SCF component Skp1 and F-box protein Skp2
    • Yam, C.H., Ng, R.W.M., Siu, W.Y., Lau, A.W.S., and Poon, R.Y.C. (1999). Regulation of cyclin A-Cdk2 by SCF component Skp1 and F-box protein Skp2. Mol. Cell. Biol. 19, 635-645.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 635-645
    • Yam, C.H.1    Ng, R.W.M.2    Siu, W.Y.3    Lau, A.W.S.4    Poon, R.Y.C.5
  • 245
    • 0030746109 scopus 로고    scopus 로고
    • Interaction of DNA-dependent protein kinase with DNA and with Ku: Biochemical and atomic-force microscopy studies
    • Yaneva, M., Kowalewski, R., and Lieber, M.R. (1997). Interaction of DNA-dependent protein kinase with DNA and with Ku: biochemical and atomic-force microscopy studies. EMBO J. 16, 5098-5112.
    • (1997) EMBO J. , vol.16 , pp. 5098-5112
    • Yaneva, M.1    Kowalewski, R.2    Lieber, M.R.3
  • 246
    • 0032540088 scopus 로고    scopus 로고
    • Regulation of the p53 protein by protein kinase C alpha and protein kinase C zeta
    • Youmell, M., Park, S.J., Basu, S., and Price, B.D. (1998). Regulation of the p53 protein by protein kinase C alpha and protein kinase C zeta. Biochem. Biophys. Res. Commun. 245, 514-518.
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 514-518
    • Youmell, M.1    Park, S.J.2    Basu, S.3    Price, B.D.4
  • 247
    • 0029959878 scopus 로고    scopus 로고
    • Genotoxic drugs induce interaction of the c-Abl tyrosine kinase and tumor suppressor protein p53
    • Yuan, Z.-M., Huang, Y., Fan, M.-M., Sawyers, C., Kharbanda, S., and Kufe, D. (1996). Genotoxic drugs induce interaction of the c-Abl tyrosine kinase and tumor suppressor protein p53. J. Biol. Chem. 271, 26457-26460.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26457-26460
    • Yuan, Z.-M.1    Huang, Y.2    Fan, M.-M.3    Sawyers, C.4    Kharbanda, S.5    Kufe, D.6
  • 248
    • 0032512750 scopus 로고    scopus 로고
    • Regulation of Rad51 function by c-Abl in response to DNA damage
    • Yuan, Z.-M., et al. (1998). Regulation of Rad51 function by c-Abl in response to DNA damage. J. Biol. Chem. 273, 3799-3802.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3799-3802
    • Yuan, Z.-M.1
  • 249
    • 0033593199 scopus 로고    scopus 로고
    • Role for p300 in stabilization of p53 in the response to DNA damage
    • Yuan, Z.-M., et al. (1999). Role for p300 in stabilization of p53 in the response to DNA damage. J. Biol. Chem. 274, 1883-1886.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1883-1886
    • Yuan, Z.-M.1
  • 250
    • 0031696265 scopus 로고    scopus 로고
    • High mobility group proteins 1 and 2 can function as DNA-binding regulatory components for DNA-dependent protein kinase in vitro
    • Yumoto, Y., Shirakawa, H., Yoshida, M., Suwa, A., Watanabe, F., and Teraoka, H. (1998). High mobility group proteins 1 and 2 can function as DNA-binding regulatory components for DNA-dependent protein kinase in vitro. J. Biochem. 124, 519-527.
    • (1998) J. Biochem. , vol.124 , pp. 519-527
    • Yumoto, Y.1    Shirakawa, H.2    Yoshida, M.3    Suwa, A.4    Watanabe, F.5    Teraoka, H.6
  • 251
    • 0030918714 scopus 로고    scopus 로고
    • Differential phosphorylation of the retinoblastoma protein by G1/S cyclin-dependent kinases
    • Zarakowska, R., and Mittnacht, S. (1997). Differential phosphorylation of the retinoblastoma protein by G1/S cyclin-dependent kinases. J. Biol. Chem. 272, 12738-12746.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12738-12746
    • Zarakowska, R.1    Mittnacht, S.2
  • 252
    • 0029131447 scopus 로고
    • A functional p53-responsive intronic promoter is contained within the human mdm2 gene
    • Zauberman, A., Flusberg, D., Haupt, Y., Barak, Y., and Oren, M. (1995). A functional p53-responsive intronic promoter is contained within the human mdm2 gene. Nucleic Acids Res. 23, 2584-2592.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2584-2592
    • Zauberman, A.1    Flusberg, D.2    Haupt, Y.3    Barak, Y.4    Oren, M.5
  • 253
    • 0030810633 scopus 로고    scopus 로고
    • Sites of UV-induced phosphorylation of the p34 subunit of replication protein A from Hela cells
    • Zernik-Kobak, M., Vasunia, K., Connelly, M., Anderson, C.W., and Dixon, K. (1997). Sites of UV-induced phosphorylation of the p34 subunit of replication protein A from HeLa cells. J. Biol. Chem. 272, 23896-23904.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23896-23904
    • Zernik-Kobak, M.1    Vasunia, K.2    Connelly, M.3    Anderson, C.W.4    Dixon, K.5
  • 254
    • 0033529121 scopus 로고    scopus 로고
    • Association with Cdc2 and inhibition of Cdc2/Cyclin B1 kinase activity by the p53-regulated protein Gadd45
    • in press
    • Zhan, Q., Antinore, M.J., Wang, X.W., Carrier, F., Smith, M.L., Harris, C.C., and Fornace, A.J.J. (1999). Association with Cdc2 and inhibition of Cdc2/Cyclin B1 kinase activity by the p53-regulated protein Gadd45. Oncogene (in press).
    • (1999) Oncogene
    • Zhan, Q.1    Antinore, M.J.2    Wang, X.W.3    Carrier, F.4    Smith, M.L.5    Harris, C.C.6    Fornace, A.J.J.7
  • 255
    • 0031946364 scopus 로고    scopus 로고
    • Tumor suppressor p53 can participate in transcriptional induction of the GADD45 promoter in the absence of direct DNA binding
    • Zhan, Q., Chen, I.-T., Antinore, M.J., and Fornace, A.J.J. (1998). Tumor suppressor p53 can participate in transcriptional induction of the GADD45 promoter in the absence of direct DNA binding. Mol. Cell. Biol. 18, 2768-2778.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2768-2778
    • Zhan, Q.1    Chen, I.-T.2    Antinore, M.J.3    Fornace, A.J.J.4
  • 256
    • 0027944228 scopus 로고
    • Induction of bax by genotoxic stress in human cells correlates with normal status and apoptosis
    • erratum 10, 1259
    • Zhan, Q., Fan, S., Bae, I., Guillouf, C., Liebermann, D.A., O'Connor, P.M., and Fornace, A.J., Jr. (1994a). Induction of bax by genotoxic stress in human cells correlates with normal status and apoptosis. Oncogene 9, 3743-3751 (erratum 10, 1259).
    • (1994) Oncogene , vol.9 , pp. 3743-3751
    • Zhan, Q.1    Fan, S.2    Bae, I.3    Guillouf, C.4    Liebermann, D.A.5    O'Connor, P.M.6    Fornace A.J., Jr.7
  • 258
    • 0028169236 scopus 로고
    • p21-containing cyclin kinases exist in both active and inactive states
    • Zhang, H., Hannon, G.J., and Beach, D. (1994). p21-containing cyclin kinases exist in both active and inactive states. Genes & Dev. 8, 1750-1758.
    • (1994) Genes & Dev. , vol.8 , pp. 1750-1758
    • Zhang, H.1    Hannon, G.J.2    Beach, D.3
  • 259
    • 0028980273 scopus 로고
    • p19Skp1 and p45Skp2 are essential elements of the cyclin A/CDK2 S-phase kinase
    • Zhang, H., Kobayashi, R., Galaktionov, K., and Beach, D. (1995). p19Skp1 and p45Skp2 are essential elements of the cyclin A/CDK2 S-phase kinase. Cell 82, 915-925.
    • (1995) Cell , vol.82 , pp. 915-925
    • Zhang, H.1    Kobayashi, R.2    Galaktionov, K.3    Beach, D.4
  • 261
    • 0027440552 scopus 로고
    • Proliferating cell nuclear antigen and p21 are components of multiple cell cycle kinase complexes
    • Zhang, H., Xiong, Y., and Beach, D. (1993). Proliferating cell nuclear antigen and p21 are components of multiple cell cycle kinase complexes. Mol. Cell. Biol. 4, 897-906.
    • (1993) Mol. Cell. Biol. , vol.4 , pp. 897-906
    • Zhang, H.1    Xiong, Y.2    Beach, D.3
  • 262
    • 0032549711 scopus 로고    scopus 로고
    • ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways
    • Zhang, Y., Xiong, Y., and Yarbrough, W.G. (1998b). ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways. Cell 92, 725-734.
    • (1998) Cell , vol.92 , pp. 725-734
    • Zhang, Y.1    Xiong, Y.2    Yarbrough, W.G.3
  • 263
    • 0029054133 scopus 로고
    • Differential roles of two tandem E2F sites in repression of the human p107 promoter by retinoblastoma and p107 proteins
    • Zhu, L., Xie, E., and Chang, L.S. (1995). Differential roles of two tandem E2F sites in repression of the human p107 promoter by retinoblastoma and p107 proteins. Mol. Cell. Biol. 15, 3552-3562.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3552-3562
    • Zhu, L.1    Xie, E.2    Chang, L.S.3


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