메뉴 건너뛰기




Volumn 81, Issue 4, 2005, Pages 975-983

The contribution of calpains in the down-regulation of Mdm2 and p53 proteolysis in reconstructed human epidermis in response to solar irradiation

Author keywords

[No Author keywords available]

Indexed keywords

MURINAE;

EID: 24644457026     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/2004-08-05-RA-262R.1     Document Type: Article
Times cited : (10)

References (65)
  • 1
    • 0027756186 scopus 로고
    • p53: At the crossroad of molecular carcinogenesis and risk assessment
    • Harris, C. C. (1993) p53: at the crossroad of molecular carcinogenesis and risk assessment. Science 262, 1980-1981.
    • (1993) Science , vol.262 , pp. 1980-1981
    • Harris, C.C.1
  • 3
    • 0025876591 scopus 로고    scopus 로고
    • The p53 tumor suppressor gene
    • Levine, A. J. (1997) The p53 tumor suppressor gene. Nature 351, 453-456.
    • (1997) Nature , vol.351 , pp. 453-456
    • Levine, A.J.1
  • 4
    • 0030941458 scopus 로고    scopus 로고
    • p53, the cellular gatekeeper for growth and division
    • Levine, A. J. (1997) p53, the cellular gatekeeper for growth and division. Cell 88, 323-331.
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 5
    • 0021616838 scopus 로고
    • UV irradiation stimulates levels of p53 cellular tumor antigen in transformed mouse cells
    • Maltzam, W. and L. Czyzyk (1984) UV irradiation stimulates levels of p53 cellular tumor antigen in transformed mouse cells. Mol. Cell. Biol. 4, 1689-1694.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 1689-1694
    • Maltzam, W.1    Czyzyk, L.2
  • 6
    • 0034610751 scopus 로고    scopus 로고
    • A unique, short sequence determines p53 gene basal and UV-inducible expression in normal human cells
    • Noda, A., Y. Toma-Aiba and Y. Fujiwara (2000) A unique, short sequence determines p53 gene basal and UV-inducible expression in normal human cells. Oncogene 19, 21-31.
    • (2000) Oncogene , vol.19 , pp. 21-31
    • Noda, A.1    Toma-Aiba, Y.2    Fujiwara, Y.3
  • 9
    • 0034028892 scopus 로고    scopus 로고
    • Role and regulation of p53 during an ultraviolet radiation-induced G1 cell cycle arrest
    • Geyer, R. K., H. Nagasawa, J. B. Little and C. G. Maki (2000) Role and regulation of p53 during an ultraviolet radiation-induced G1 cell cycle arrest. Cell Growth Differ. 11, 149-156.
    • (2000) Cell Growth Differ. , vol.11 , pp. 149-156
    • Geyer, R.K.1    Nagasawa, H.2    Little, J.B.3    Maki, C.G.4
  • 10
    • 0000516293 scopus 로고    scopus 로고
    • Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is involved in global genomic repair
    • Hwang, B. J., J. M. Ford, P. C. Hanawalt and G. Chu (1999) Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is involved in global genomic repair. Proc. Natl. Acad. Sci. USA 96, 424-428.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 424-428
    • Hwang, B.J.1    Ford, J.M.2    Hanawalt, P.C.3    Chu, G.4
  • 11
    • 0021616838 scopus 로고
    • UV irradiation stimulates levels of p53 cellular tumor antigen in nontransformed mouse cells
    • Maltzman, W. and L. Czyzyk (1984) UV irradiation stimulates levels of p53 cellular tumor antigen in nontransformed mouse cells. Mol. Cell. Biol. 4, 1689-1694.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 1689-1694
    • Maltzman, W.1    Czyzyk, L.2
  • 13
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat, M. H., S. N. Jones and K. H. Vousden (1997) Regulation of p53 stability by Mdm2. Nature 387, 299-303.
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 14
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt, Y., R. Maya, A. Kazaz and M. Oren (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
  • 15
    • 0032192140 scopus 로고    scopus 로고
    • The complexity of p53 modulation emerging patterns from divergent signals
    • Giaccia, A. J. and M. B. Kastan (1998) The complexity of p53 modulation emerging patterns from divergent signals. Genes Dev. 12, 2973-2983.
    • (1998) Genes Dev. , vol.12 , pp. 2973-2983
    • Giaccia, A.J.1    Kastan, M.B.2
  • 16
    • 0032475878 scopus 로고    scopus 로고
    • How loops, β sheets and α helices help us to understand p53
    • Prives, C. (1998) How loops, β sheets and α helices help us to understand p53. Cell 95, 5-8.
    • (1998) Cell , vol.95 , pp. 5-8
    • Prives, C.1
  • 17
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh, S. Y., M. Ikeda, Y. Taya and C. Prives (1997) DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell 91, 325-334.
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 18
    • 0029036680 scopus 로고
    • p53 in complex with DNA is resistant to ubiquitin dependent proteolysis in the presence of HPV-16 E6
    • Molinari, M. and J. Milner (1995) p53 in complex with DNA is resistant to ubiquitin dependent proteolysis in the presence of HPV-16 E6. Oncogene 10, 1849-1854.
    • (1995) Oncogene , vol.10 , pp. 1849-1854
    • Molinari, M.1    Milner, J.2
  • 19
    • 0034967925 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and proteasome inhibitors
    • Myung, J., K. B. Kim and C. M. Crews (2001) The ubiquitin-proteasome pathway and proteasome inhibitors. Med. Res. Rev. 21, 245-73.
    • (2001) Med. Res. Rev. , vol.21 , pp. 245-273
    • Myung, J.1    Kim, K.B.2    Crews, C.M.3
  • 20
    • 0031021991 scopus 로고    scopus 로고
    • The ubiquitin-mediated proteolytic pathway as a therapeutic area
    • Rolfe, M., M. I. Chiu and M. Pagano (1997) The ubiquitin-mediated proteolytic pathway as a therapeutic area. J. Mol. Med. 75, 5-17.
    • (1997) J. Mol. Med. , vol.75 , pp. 5-17
    • Rolfe, M.1    Chiu, M.I.2    Pagano, M.3
  • 21
    • 0030997067 scopus 로고    scopus 로고
    • Regulating protein degradation by ubiquitination
    • Weissman, A.M. (1997) Regulating protein degradation by ubiquitination. Immunol. Today 18, 189-198.
    • (1997) Immunol. Today , vol.18 , pp. 189-198
    • Weissman, A.M.1
  • 22
    • 0032192140 scopus 로고    scopus 로고
    • The complexity of p53 modulation: Emerging patterns from divergent signals
    • Giaccia, A. J. and M. B. Kastan (1998) The complexity of p53 modulation: emerging patterns from divergent signals. Genes Dev. 12, 2973-2983.
    • (1998) Genes Dev. , vol.12 , pp. 2973-2983
    • Giaccia, A.J.1    Kastan, M.B.2
  • 23
    • 0034705319 scopus 로고    scopus 로고
    • SUMO-1 modification of Mdm2 prevents its self ubiquitination and increases Mdm2 ability to ubiquitinate p53
    • Buschmann, T., S. Y. Fuchs, C. G. Lee, Z. Q. Pan and Z. Ronai (2000) SUMO-1 modification of Mdm2 prevents its self ubiquitination and increases Mdm2 ability to ubiquitinate p53. Cell 101, 753-762.
    • (2000) Cell , vol.101 , pp. 753-762
    • Buschmann, T.1    Fuchs, S.Y.2    Lee, C.G.3    Pan, Z.Q.4    Ronai, Z.5
  • 24
    • 0031014946 scopus 로고    scopus 로고
    • Proteolytic cleavage of human p53 by calpain: A potential regulator of protein stability
    • Kubbutat, M. H. and K. H. Vousden (1997) Proteolytic cleavage of human p53 by calpain: a potential regulator of protein stability. Mol. Cell Biol. 17, 460-468.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 460-468
    • Kubbutat, M.H.1    Vousden, K.H.2
  • 25
    • 0028088153 scopus 로고
    • Calpain: New perspectives in molecular diversity and physiological pathological involvement
    • Saido, T. C., H. Sorimachi and K. Suzuki (1994) Calpain: new perspectives in molecular diversity and physiological pathological involvement. FASEB J. 8, 814-822.
    • (1994) FASEB J. , vol.8 , pp. 814-822
    • Saido, T.C.1    Sorimachi, H.2    Suzuki, K.3
  • 26
    • 0025831476 scopus 로고
    • Calcium-activated neutral protease (calpain) system: Structure, function, and regulation
    • Croall, D. E. and G. N. Demartino (1991) Calcium-activated neutral protease (calpain) system: structure, function, and regulation. Physiol. Rev. 71, 813-847.
    • (1991) Physiol. Rev. , vol.71 , pp. 813-847
    • Croall, D.E.1    Demartino, G.N.2
  • 27
    • 0030992491 scopus 로고    scopus 로고
    • On the involvement of calpains in the degradation of the tumor suppressor protein p53
    • Gonen, H., D. Shkedy, S. Barnoy, N. S. Kosower and A. Ciechanover (1997) On the involvement of calpains in the degradation of the tumor suppressor protein p53. FEBS Lett. 406, 17-22.
    • (1997) FEBS Lett. , vol.406 , pp. 17-22
    • Gonen, H.1    Shkedy, D.2    Barnoy, S.3    Kosower, N.S.4    Ciechanover, A.5
  • 28
    • 0002938556 scopus 로고    scopus 로고
    • Calpain in signal transduction
    • (Edited by K. K. W. Wang and P. W. Yen), Taylor and Francis, Philadelphia
    • Fox, J. E. B. and T. C. Saido (1999) Calpain in signal transduction. In Calpain: Pharmacology and Toxicology of Calcium-Dependent Protease (Edited by K. K. W. Wang and P. W. Yen), pp. 103-126. Taylor and Francis, Philadelphia.
    • (1999) Calpain: Pharmacology and Toxicology of Calcium-Dependent Protease , pp. 103-126
    • Fox, J.E.B.1    Saido, T.C.2
  • 29
    • 0032860769 scopus 로고    scopus 로고
    • Calpain cleavage of integrin β cytoplasmic domains
    • Pfaff, M., X. Du and M. H. Ginsberg (1999) Calpain cleavage of integrin β cytoplasmic domains. FEBS Lett. 460, 17-22.
    • (1999) FEBS Lett. , vol.460 , pp. 17-22
    • Pfaff, M.1    Du, X.2    Ginsberg, M.H.3
  • 30
    • 0031028205 scopus 로고    scopus 로고
    • Calpain cleavage of focal adhesion proteins regulates the cytoskeletal attachment of integrin αIIbβ3 (platelet glycoprotein IIb/IIIa) and the cellular retraction of fibrin clots
    • Schoenwaelder S. M., Y. Yuan, P. Cooray, H. H. Salem and S. P. Jackson (1997) Calpain cleavage of focal adhesion proteins regulates the cytoskeletal attachment of integrin αIIbβ3 (platelet glycoprotein IIb/IIIa) and the cellular retraction of fibrin clots. J. Biol. Chem. 272, 1694-1702.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1694-1702
    • Schoenwaelder, S.M.1    Yuan, Y.2    Cooray, P.3    Salem, H.H.4    Jackson, S.P.5
  • 31
    • 0032697768 scopus 로고    scopus 로고
    • On the role of calpain and Rho protein in regulating integrin-induced signalling
    • Fox, J. E. (1999) On the role of calpain and Rho protein in regulating integrin-induced signalling. Thromb. Haemost. 82, 385-391.
    • (1999) Thromb. Haemost. , vol.82 , pp. 385-391
    • Fox, J.E.1
  • 32
    • 0034723310 scopus 로고    scopus 로고
    • Epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signalling pathway
    • Glading, A., P. Chang, D. A. Lauffenburger and A. Wells (2000) Epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signalling pathway. J. Biol. Chem. 275, 2390-2398.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2390-2398
    • Glading, A.1    Chang, P.2    Lauffenburger, D.A.3    Wells, A.4
  • 33
    • 0035968342 scopus 로고    scopus 로고
    • Membrane proximal ERK signalling is required for m-calpain activation downstream of epidermal growth factor receptor signalling
    • Glading, A., F. Überall, S. M. Keyse, D. A. Lauffenburger and A. Wells (2001) Membrane proximal ERK signalling is required for m-calpain activation downstream of epidermal growth factor receptor signalling. J. Biol. Chem. 276, 23341-23348.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23341-23348
    • Glading, A.1    Überall, F.2    Keyse, S.M.3    Lauffenburger, D.A.4    Wells, A.5
  • 35
    • 0027494395 scopus 로고
    • Calpain-catalyzed cleavage and subcellular relocation of protein phosphotyrosine phosphatase 1B (PTP-1B) in human platelets
    • Frangioni, J. V., A. Oda, M. Smith, E. W. Salzman and B. G. Neel (1993) Calpain-catalyzed cleavage and subcellular relocation of protein phosphotyrosine phosphatase 1B (PTP-1B) in human platelets. EMBO J. 12, 4843-4856.
    • (1993) EMBO J. , vol.12 , pp. 4843-4856
    • Frangioni, J.V.1    Oda, A.2    Smith, M.3    Salzman, E.W.4    Neel, B.G.5
  • 36
    • 0028964404 scopus 로고
    • Endogenous cleavage of phospholipase C-beta 3 by agonist-induced activation of calpain in human platelets
    • Banno Y., S. Nakashima, T. Hachiya and Y. Nozawa (1995) Endogenous cleavage of phospholipase C-beta 3 by agonist-induced activation of calpain in human platelets. J. Biol. Chem. 270, 4318-4324.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4318-4324
    • Banno, Y.1    Nakashima, S.2    Hachiya, T.3    Nozawa, Y.4
  • 39
    • 0026454458 scopus 로고
    • Positive regulation of mu-calpain action by polyphosphoinositides
    • Saido, T. C., M. Shibata, T. Takenawa, H. Murofushi and S. Suzuki (1992) Positive regulation of mu-calpain action by polyphosphoinositides. J. Biol. Chem. 267, 24585-24590.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24585-24590
    • Saido, T.C.1    Shibata, M.2    Takenawa, T.3    Murofushi, H.4    Suzuki, S.5
  • 40
    • 0033644826 scopus 로고    scopus 로고
    • Proteolysis of p53 protein by ubiquitous calpains
    • Piechaczyk, M. (2000) Proteolysis of p53 protein by ubiquitous calpains. Methods Mol. Biol. 144, 297-307.
    • (2000) Methods Mol. Biol. , vol.144 , pp. 297-307
    • Piechaczyk, M.1
  • 41
    • 0034086332 scopus 로고    scopus 로고
    • Calpain inhibitor 1 activates p53-dependent apoptosis in tumor cell lines
    • Atencio, I. A., M. Ramachandra, P. Shabram and G. W. Demers (2000) Calpain inhibitor 1 activates p53-dependent apoptosis in tumor cell lines. Cell Growth Diff. 11, 247-253.
    • (2000) Cell Growth Diff. , vol.11 , pp. 247-253
    • Atencio, I.A.1    Ramachandra, M.2    Shabram, P.3    Demers, G.W.4
  • 42
    • 0036484884 scopus 로고    scopus 로고
    • Comparison of gene expression profiles in human keratinocytes mono-layer cultures, reconstructed epidermis and normal human skin; transcriptional effects of retinoid treatments in reconstructed human epidermis
    • Bernard, F. X., N. Pedretti, M. Rosdy and A. Deguercy (2002) Comparison of gene expression profiles in human keratinocytes mono-layer cultures, reconstructed epidermis and normal human skin; transcriptional effects of retinoid treatments in reconstructed human epidermis. Exp. Dermatol. 11, 59-74.
    • (2002) Exp. Dermatol. , vol.11 , pp. 59-74
    • Bernard, F.X.1    Pedretti, N.2    Rosdy, M.3    Deguercy, A.4
  • 43
    • 0346993777 scopus 로고    scopus 로고
    • Transcriptional profiling of epidermal keratinocytes: Comparison of genes expressed in skin, cultured keratinocytes, and reconstructed human epidermis, using large DNA microarrays
    • Gazel, A., P. Ramphal, M. Rosdy, B. De Wever, C. Tornier, N. Hosein, B. Lee, M. Tomic-Canic and M. Blumenberg (2003) Transcriptional profiling of epidermal keratinocytes: comparison of genes expressed in skin, cultured keratinocytes, and reconstructed human epidermis, using large DNA microarrays. J. Invest. Dermatol. 121, 1459-1468.
    • (2003) J. Invest. Dermatol. , vol.121 , pp. 1459-1468
    • Gazel, A.1    Ramphal, P.2    Rosdy, M.3    De Wever, B.4    Tornier, C.5    Hosein, N.6    Lee, B.7    Tomic-Canic, M.8    Blumenberg, M.9
  • 44
    • 0034481392 scopus 로고    scopus 로고
    • Development of a highly sensitive in vitro phototoxicity assay using the SkinEthic reconstructed human epidermis
    • Bernard, F. X., C. Barrault, A. Deguercy, B. De Wever and M. Rosdy (2000) Development of a highly sensitive in vitro phototoxicity assay using the SkinEthic reconstructed human epidermis. Cell Biol. Toxicol. 16, 391-400.
    • (2000) Cell Biol. Toxicol. , vol.16 , pp. 391-400
    • Bernard, F.X.1    Barrault, C.2    Deguercy, A.3    De Wever, B.4    Rosdy, M.5
  • 45
    • 0025129824 scopus 로고
    • Terminal epidermal differentiation of human keratinocytes grown in chemically defined medium on inert filter substrates at the air-liquid interface
    • Rosdy, M. and L. C. Clauss (1990) Terminal epidermal differentiation of human keratinocytes grown in chemically defined medium on inert filter substrates at the air-liquid interface. J. Invest. Dermatol. 95, 409-414.
    • (1990) J. Invest. Dermatol. , vol.95 , pp. 409-414
    • Rosdy, M.1    Clauss, L.C.2
  • 46
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann, T. (1983) Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 65: 55-63.
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 48
    • 0027964904 scopus 로고
    • Immunochemical analysis of the interaction of p53 with MDM2 - Fine mapping of the MDM2 binding site on p53 using synthetic peptides
    • Picksley, S. M., B. Vojtesek, A. Spark and D. P. Lane (1994) Immunochemical analysis of the interaction of p53 with MDM2 - fine mapping of the MDM2 binding site on p53 using synthetic peptides. Oncogenes 9, 2523-2529.
    • (1994) Oncogenes , vol.9 , pp. 2523-2529
    • Picksley, S.M.1    Vojtesek, B.2    Spark, A.3    Lane, D.P.4
  • 49
    • 0033552613 scopus 로고    scopus 로고
    • Regulation of p53 stability
    • Ashcroft, M. and K. H. Vousden (1999) Regulation of p53 stability. Oncogene 18, 7637-7643.
    • (1999) Oncogene , vol.18 , pp. 7637-7643
    • Ashcroft, M.1    Vousden, K.H.2
  • 50
    • 0029852593 scopus 로고    scopus 로고
    • Sunscreens: Progress and perspectives on photoprotection of human skin against UVB and UVA radiation
    • Pathak, M. A. (1996) Sunscreens: progress and perspectives on photoprotection of human skin against UVB and UVA radiation. Dermatology 23, 783-800.
    • (1996) Dermatology , vol.23 , pp. 783-800
    • Pathak, M.A.1
  • 51
    • 0025396221 scopus 로고
    • The protective potential of the new superpotent sunscreen
    • Kaidbey, K. H. (1990) The protective potential of the new superpotent sunscreen. J. Am. Acad. Dermatol. 22, 449-452.
    • (1990) J. Am. Acad. Dermatol. , vol.22 , pp. 449-452
    • Kaidbey, K.H.1
  • 52
    • 0028233868 scopus 로고
    • Increase in p53 protein half-life in mouse keratinocytes following UV-B irradiation
    • Liu, M., K. Dhanwada, D. Birt, S. Hecht and J. Pelling (1994) Increase in p53 protein half-life in mouse keratinocytes following UV-B irradiation. Carcinogenesis 15, 1089-1092.
    • (1994) Carcinogenesis , vol.15 , pp. 1089-1092
    • Liu, M.1    Dhanwada, K.2    Birt, D.3    Hecht, S.4    Pelling, J.5
  • 53
    • 0031586030 scopus 로고    scopus 로고
    • Early ultraviolet B-induced G1 arrest and suppression of the malignant phenotype by wild-type p53 in human squamous cell carcinoma cells
    • Courtois S., C. Woodworth, H. Degreef and M. Garmyn (1997) Early ultraviolet B-induced G1 arrest and suppression of the malignant phenotype by wild-type p53 in human squamous cell carcinoma cells. Exp. Cell Res. 233, 135-144.
    • (1997) Exp. Cell Res. , vol.233 , pp. 135-144
    • Courtois, S.1    Woodworth, C.2    Degreef, H.3    Garmyn, M.4
  • 54
    • 0027528673 scopus 로고
    • High levels of p53 protein in UV-irradiated normal human skin
    • Hall, P. A., P. H. McKee, H. Menage, R. Dover and D. P. Lane (1993) High levels of p53 protein in UV-irradiated normal human skin. Oncogene 8, 203-207.
    • (1993) Oncogene , vol.8 , pp. 203-207
    • Hall, P.A.1    McKee, P.H.2    Menage, H.3    Dover, R.4    Lane, D.P.5
  • 58
    • 0033592868 scopus 로고    scopus 로고
    • Phosphorylation of Ser-20 mediates stabilization of human p53 in response to DNA damage
    • Chehab, N. H., A. Malikray, E. S. Stavridi, and T. D. Halaronetis (1999) Phosphorylation of Ser-20 mediates stabilization of human p53 in response to DNA damage. Proc. Natl. Acad. Sci. USA 96, 14973-14977.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14973-14977
    • Chehab, N.H.1    Malikray, A.2    Stavridi, E.S.3    Halaronetis, T.D.4
  • 59
    • 0031015044 scopus 로고    scopus 로고
    • Ubiquitination of p53 and p21 is differentially affected by ionizing and UV radiation
    • Maki, G. C. and P. M. Howley (1997) Ubiquitination of p53 and p21 is differentially affected by ionizing and UV radiation. Mol. Cell. Biol. 17, 355-363.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 355-363
    • Maki, G.C.1    Howley, P.M.2
  • 60
    • 0033523015 scopus 로고    scopus 로고
    • Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2
    • Maki, G. C. (1999) Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2. J. Biol. Chem. 274, 16531-16535.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16531-16535
    • Maki, G.C.1
  • 61
    • 0035895606 scopus 로고    scopus 로고
    • Downregulation of MDM2 stabilizes p53 by inhibiting p53 ubiquitination in response to specific alkylating agents
    • Inoue, T., R. K. Geyer, Z. K. Yu and C. G. Maki (2001) Downregulation of MDM2 stabilizes p53 by inhibiting p53 ubiquitination in response to specific alkylating agents. FEBS Lett. 490, 196-201.
    • (2001) FEBS Lett. , vol.490 , pp. 196-201
    • Inoue, T.1    Geyer, R.K.2    Yu, Z.K.3    Maki, C.G.4
  • 63
    • 0030025099 scopus 로고    scopus 로고
    • Inhibiting calpain, rescuing cells
    • Robinson, A. (1996) Inhibiting calpain, rescuing cells. C.M.A.J. 154, 193-195.
    • (1996) C.M.A.J. , vol.154 , pp. 193-195
    • Robinson, A.1
  • 64
    • 0027988820 scopus 로고
    • Calpain inhibition: An overview of its therapeutic potential
    • Wang, K. K. and P. W. Yuen (1994) Calpain inhibition: an overview of its therapeutic potential. Trends Pharmacol. Sci. 15, 412-419.
    • (1994) Trends Pharmacol. Sci. , vol.15 , pp. 412-419
    • Wang, K.K.1    Yuen, P.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.