메뉴 건너뛰기




Volumn 24, Issue 4, 2002, Pages 243-248

Role of the ubiquitin-proteasome protein degradation pathway in carcinogenesis, tumor progression and susceptibility to tumor treatment

Author keywords

Cancer; Proteasomes

Indexed keywords

CD23 ANTIGEN; HYPOXIA INDUCIBLE FACTOR 1ALPHA; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEASOME; PROTEASOME INHIBITOR; PROTEIN BCL 2; PROTEIN P21; UBIQUITIN;

EID: 0036971557     PISSN: 02043564     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (2)

References (70)
  • 1
    • 0036240701 scopus 로고    scopus 로고
    • The proteasome: A novel target for cancer chemotherapy
    • Almond JB, Cohen JM. The proteasome: a novel target for cancer chemotherapy. Leukemia 2002; 16: 433-41.
    • (2002) Leukemia , vol.16 , pp. 433-441
    • Almond, J.B.1    Cohen, J.M.2
  • 2
    • 0034653998 scopus 로고    scopus 로고
    • c-Myc hot spot mutations in lymphomas result in inefficient ubiquitination and decreased proteasome-mediated turnover
    • Bahram F, von der Lehr N, Cetinkaya C, Larsson LG. c-Myc hot spot mutations in lymphomas result in inefficient ubiquitination and decreased proteasome-mediated turnover. Blood 2000; 95: 2104-10.
    • (2000) Blood , vol.95 , pp. 2104-2110
    • Bahram, F.1    Von der Lehr, N.2    Cetinkaya, C.3    Larsson, L.G.4
  • 3
    • 17844369428 scopus 로고    scopus 로고
    • The tuberous sclerosis-1 (TSC1) gene product hamartin suppresses cell growth and augments the expression of the TSC2 product tuberin by inhibiting its ubiquitination
    • Benvenuto G, Li S, Brown SJ, Braverman R, Vass WC, Cheadle JP, Halley DJ, Sampson JR, Wieneeke R, DeClue JE. The tuberous sclerosis-1 (TSC1) gene product hamartin suppresses cell growth and augments the expression of the TSC2 product tuberin by inhibiting its ubiquitination. Oncogene 2000; 19: 6306-16.
    • (2000) Oncogene , vol.19 , pp. 6306-6316
    • Benvenuto, G.1    Li, S.2    Brown, S.J.3    Braverman, R.4    Vass, W.C.5    Cheadle, J.P.6    Halley, D.J.7    Sampson, J.R.8    Wieneeke, R.9    DeClue, J.E.10
  • 4
    • 0030728767 scopus 로고    scopus 로고
    • The human papillomavirus E7 oncoprotein functionally interacts with the S4 subunit of the 26 S proteasome
    • Berezutskaya E, Bagehi S. The human papillomavirus E7 oncoprotein functionally interacts with the S4 subunit of the 26 S proteasome. J Biol Chem 1997; 272: 30135-40.
    • (1997) J Biol Chem , vol.272 , pp. 30135-30140
    • Berezutskaya, E.1    Bagehi, S.2
  • 5
    • 0029844034 scopus 로고    scopus 로고
    • Novel cellular markers in breast cancer: Differential presence of p23K and p30.33K prosomal antigens in tumors of Parsi and non-Parsi women
    • Bhui AJ, Bureau JP, Abbas A, Mondal A, Scherrer K, Kurkure A, Therwath A. Novel cellular markers in breast cancer: differential presence of p23K and p30.33K prosomal antigens in tumors of Parsi and non-Parsi women. Int J Oncol 1996; 9: 669-77.
    • (1996) Int J Oncol , vol.9 , pp. 669-677
    • Bhui, A.J.1    Bureau, J.P.2    Abbas, A.3    Mondal, A.4    Scherrer, K.5    Kurkure, A.6    Therwath, A.7
  • 6
    • 0030871772 scopus 로고    scopus 로고
    • Proliferation markers and cell cycle associated expression of prosomes in breast cancers of Parsis and non-Parsis
    • Bhui AJ, Bureau JP, Parikh VA, Kukreti R, Scherrer K, Mondal A, Therwath A. Proliferation markers and cell cycle associated expression of prosomes in breast cancers of Parsis and non-Parsis. Int J Oncol 1997; 11: 297-304.
    • (1997) Int J Oncol , vol.11 , pp. 297-304
    • Bhui, A.J.1    Bureau, J.P.2    Parikh, V.A.3    Kukreti, R.4    Scherrer, K.5    Mondal, A.6    Therwath, A.7
  • 8
    • 0033023882 scopus 로고    scopus 로고
    • Identification of protein instability determinants in the carboxy-terminal region of c-Myb removed as a result of retroviral integration in murine monocytic leukemias
    • Bies J, Nazarov V, Wolff L. Identification of protein instability determinants in the carboxy-terminal region of c-Myb removed as a result of retroviral integration in murine monocytic leukemias. J Virol 1999; 73: 2038-44.
    • (1999) J Virol , vol.73 , pp. 2038-2044
    • Bies, J.1    Nazarov, V.2    Wolff, L.3
  • 9
    • 0031105196 scopus 로고    scopus 로고
    • Prosomes (proteasomes) changes during differentiation are related to the type of inducer
    • Bureau JP, Henry L, Baz A, Scherrer K, Chateau MT. Prosomes (proteasomes) changes during differentiation are related to the type of inducer. Mol Biol Rep 1997; 24: 57-62.
    • (1997) Mol Biol Rep , vol.24 , pp. 57-62
    • Bureau, J.P.1    Henry, L.2    Baz, A.3    Scherrer, K.4    Chateau, M.T.5
  • 12
    • 0034041823 scopus 로고    scopus 로고
    • Role of p53 in cell cycle regulation and apoptosis following exposure to proteasome inhibitors
    • Chen F, Chang D, Goh M, Klibanov SA, Ljungman M. Role of p53 in cell cycle regulation and apoptosis following exposure to proteasome inhibitors. Cell Growth Differ 2000; 11: 239-46.
    • (2000) Cell Growth Differ , vol.11 , pp. 239-246
    • Chen, F.1    Chang, D.2    Goh, M.3    Klibanov, S.A.4    Ljungman, M.5
  • 13
    • 0035491589 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of BRCA1 protein in MCF-7 human breast cancer cells
    • Choi YH. Proteasome-mediated degradation of BRCA1 protein in MCF-7 human breast cancer cells. Int J Oncol 2001; 19: 687-93.
    • (2001) Int J Oncol , vol.19 , pp. 687-693
    • Choi, Y.H.1
  • 14
    • 0035353155 scopus 로고    scopus 로고
    • Regulation of the nuclear proteasome activity in myelomonocytic human leukemia cells after adriamycin treatment
    • Ciftci O, Ullrich O, Schmidt CA, Diestel A, Hass R. Regulation of the nuclear proteasome activity in myelomonocytic human leukemia cells after adriamycin treatment. Blood 2001; 97: 2830-8.
    • (2001) Blood , vol.97 , pp. 2830-2838
    • Ciftci, O.1    Ullrich, O.2    Schmidt, C.A.3    Diestel, A.4    Hass, R.5
  • 15
    • 0029957947 scopus 로고    scopus 로고
    • Turnover of cyclin E by the ubiquitin-proteasome pathway is regulated by cdk2 binding and cyclin phosphorylation
    • Clurman BE, Sheaff RJ, Thress K, Groudine M, Roberts JM. Turnover of cyclin E by the ubiquitin-proteasome pathway is regulated by cdk2 binding and cyclin phosphorylation. Genes Dev 1996; 10: 1979-90.
    • (1996) Genes Dev , vol.10 , pp. 1979-1990
    • Clurman, B.E.1    Sheaff, R.J.2    Thress, K.3    Groudine, M.4    Roberts, J.M.5
  • 16
    • 0344915169 scopus 로고    scopus 로고
    • Manipulation of the ubiquitin-proteasome pathway in cachexia: Pentoxifylline suppresses the activation of 20S and 26S proteasomes in muscles from tumor-bearing rats
    • Combaret L, Ralliere C, Taillandier D, Tanaka K, Attaix D. Manipulation of the ubiquitin-proteasome pathway in cachexia: pentoxifylline suppresses the activation of 20S and 26S proteasomes in muscles from tumor-bearing rats. Mol Biol Rep 1999; 26: 95-100.
    • (1999) Mol Biol Rep , vol.26 , pp. 95-100
    • Combaret, L.1    Ralliere, C.2    Taillandier, D.3    Tanaka, K.4    Attaix, D.5
  • 17
    • 0032523919 scopus 로고    scopus 로고
    • Oncogenic Abl and Src tyrosine kinases elicit the ubiquitin-dependent degradation of target proteins through a Ras-independent pathway
    • Dai Z, Quackenbush RC, Courtney KD, Grove M, Cortez D, Reuther GW, Pendergast AM. Oncogenic Abl and Src tyrosine kinases elicit the ubiquitin-dependent degradation of target proteins through a Ras-independent pathway. Genes Dev 1998; 12: 1415-24.
    • (1998) Genes Dev , vol.12 , pp. 1415-1424
    • Dai, Z.1    Quackenbush, R.C.2    Courtney, K.D.3    Grove, M.4    Cortez, D.5    Reuther, G.W.6    Pendergast, A.M.7
  • 18
    • 0029784408 scopus 로고    scopus 로고
    • p53-dependent cell cycle arrest induced by N-acetyl-L-leucinyl-L-leucinyl-L-norleucinal in platelet-derived growth factor-stimulated human fibroblasts
    • Dietrich C, Bartsch T, Schanz F, Oesch F, Wieser RJ. p53-dependent cell cycle arrest induced by N-acetyl-L-leucinyl-L-leucinyl-L-norleucinal in platelet-derived growth factor-stimulated human fibroblasts. Proc Natl Acad Sci USA 1996; 93: 10815-9.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10815-10819
    • Dietrich, C.1    Bartsch, T.2    Schanz, F.3    Oesch, F.4    Wieser, R.J.5
  • 19
    • 0033104901 scopus 로고    scopus 로고
    • Constitutive degradation of PML/RARalpha through the proteasome pathway mediates retinoic acid resistance
    • Fanelli M, Minucci S, Gelmetti V, Nervi C, Gambacorti-Passerini C, Pelicci PG. Constitutive degradation of PML/RARalpha through the proteasome pathway mediates retinoic acid resistance. Blood 1999; 93: 1477-81.
    • (1999) Blood , vol.93 , pp. 1477-1481
    • Fanelli, M.1    Minucci, S.2    Gelmetti, V.3    Nervi, C.4    Gambacorti-Passerini, C.5    Pelicci, P.G.6
  • 21
    • 0034672376 scopus 로고    scopus 로고
    • Variations in proteasome subunit composition and enzymatic activity in B-lymphoma lines and normal B cells
    • Frisan T, Levitsky V, Masucci MG. Variations in proteasome subunit composition and enzymatic activity in B-lymphoma lines and normal B cells. Int J Cancer 2000; 88: 881-8.
    • (2000) Int J Cancer , vol.88 , pp. 881-888
    • Frisan, T.1    Levitsky, V.2    Masucci, M.G.3
  • 22
    • 0035097842 scopus 로고    scopus 로고
    • c-myc overexpression activates alternative pathways for intracellular proteolysis in lymphoma cells
    • Gavioli R, Frisan T, Vertuani S, Bornkamm GW, Masucci MG. c-myc overexpression activates alternative pathways for intracellular proteolysis in lymphoma cells. Nat Cell Biol 2001; 3: 283-8.
    • (2001) Nat Cell Biol , vol.3 , pp. 283-288
    • Gavioli, R.1    Frisan, T.2    Vertuani, S.3    Bornkamm, G.W.4    Masucci, M.G.5
  • 23
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 2002; 82: 373-428.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 25
    • 0036104603 scopus 로고    scopus 로고
    • Not just research tools - Proteasome inhibitors offer therapeutic promise
    • Goldberg AL, Rock K. Not just research tools - proteasome inhibitors offer therapeutic promise. Nature Med 2002; 8: 338-40.
    • (2002) Nature Med , vol.8 , pp. 338-340
    • Goldberg, A.L.1    Rock, K.2
  • 26
    • 0034059667 scopus 로고    scopus 로고
    • c-Myc proteolysis by the ubiquitin-proteasome pathway: Stabilization of c-Myc in Burkitt's lymphoma cells
    • Gregory MA, Hann SR. c-Myc proteolysis by the ubiquitin-proteasome pathway: stabilization of c-Myc in Burkitt's lymphoma cells. Mol Cell Biol 2000; 20: 2423-35.
    • (2000) Mol Cell Biol , vol.20 , pp. 2423-2435
    • Gregory, M.A.1    Hann, S.R.2
  • 27
    • 0029912242 scopus 로고    scopus 로고
    • Inhibitors of the proteasome pathway interfere with induction of nitric oxide synthase in macrophages by blocking activation of transcription factor NF-kappa B
    • Griscavage JM, Wilk S, Ignarro LJ. Inhibitors of the proteasome pathway interfere with induction of nitric oxide synthase in macrophages by blocking activation of transcription factor NF-kappa B. Proc Natl Acad Sci USA 1996; 93: 3308-12.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3308-3312
    • Griscavage, J.M.1    Wilk, S.2    Ignarro, L.J.3
  • 28
    • 0033598173 scopus 로고    scopus 로고
    • Ubiquitin-dependent degradation of active Src
    • Hakak Y, Martin GS. Ubiquitin-dependent degradation of active Src. Curr Biol 1999; 9: 1039-42.
    • (1999) Curr Biol , vol.9 , pp. 1039-1042
    • Hakak, Y.1    Martin, G.S.2
  • 30
    • 0033978257 scopus 로고    scopus 로고
    • Reduced stability of retinoblastoma protein by gankyrin, an oncogenic ankyrin-repeat protein overexpressed in hepatomas
    • Higashitsuji H, Itoh K, Nagao T, Dawson S, Nonoguchi K, Kido T, Mayer RJ, Arii S, Fujita J. Reduced stability of retinoblastoma protein by gankyrin, an oncogenic ankyrin-repeat protein overexpressed in hepatomas. Nat Med 2000; 6: 96-9.
    • (2000) Nat Med , vol.6 , pp. 96-99
    • Higashitsuji, H.1    Itoh, K.2    Nagao, T.3    Dawson, S.4    Nonoguchi, K.5    Kido, T.6    Mayer, R.J.7    Arii, S.8    Fujita, J.9
  • 31
    • 0029820095 scopus 로고    scopus 로고
    • The retinoblastoma gene product protects E2F-1 from degradation by the ubiquitin-proteasome pathway
    • Hofmann F, Martelli F, Livingston DM, Wang Z. The retinoblastoma gene product protects E2F-1 from degradation by the ubiquitin-proteasome pathway. Genes Dev 1996; 10: 2949-59.
    • (1996) Genes Dev , vol.10 , pp. 2949-2959
    • Hofmann, F.1    Martelli, F.2    Livingston, D.M.3    Wang, Z.4
  • 32
    • 0035947731 scopus 로고    scopus 로고
    • Requirement for HDM2 activity in the rapid degradation of p53 in neuroblastoma
    • Isaacs JS, Saito S, Neckers LM. Requirement for HDM2 activity in the rapid degradation of p53 in neuroblastoma. J Biol Chem 2001; 276: 18497-506.
    • (2001) J Biol Chem , vol.276 , pp. 18497-18506
    • Isaacs, J.S.1    Saito, S.2    Neckers, L.M.3
  • 34
    • 0033536637 scopus 로고    scopus 로고
    • The tyrosine-kinase negative regulator c-Cbl a RING type, E2-dependent ubiquitin protein ligase
    • Joazeiro CA, Wing SS, Huang H, Leverson JD, Hunter T, Liu YC. The tyrosine-kinase negative regulator c-Cbl a RING type, E2-dependent ubiquitin protein ligase. Science 1999; 286: 309-12.
    • (1999) Science , vol.286 , pp. 309-312
    • Joazeiro, C.A.1    Wing, S.S.2    Huang, H.3    Leverson, J.D.4    Hunter, T.5    Liu, Y.C.6
  • 35
    • 0035254934 scopus 로고    scopus 로고
    • Systemic deficits in transporter for antigen presentation (TAP)-1 or proteasome subunit LMP2 have little or no effect on tumor incidence
    • Johnsen AK, France J, Nagy N, Askew D, Abdul-Karim FW, Gerson SL, Sy M-S, Harding CV. Systemic deficits in transporter for antigen presentation (TAP)-1 or proteasome subunit LMP2 have little or no effect on tumor incidence. Int J Cancer 2001; 91: 366-72.
    • (2001) Int J Cancer , vol.91 , pp. 366-372
    • Johnsen, A.K.1    France, J.2    Nagy, N.3    Askew, D.4    Abdul-Karim, F.W.5    Gerson, S.L.6    Sy, M.-S.7    Harding, C.V.8
  • 36
    • 0034641615 scopus 로고    scopus 로고
    • Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex
    • Kamura T, Sato S, Iwai K, Czyzyk-Krzeska M, Conaway RC, Conaway JW. Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex. Proc Natl Acad Sci U S A 2000; 97: 10430-5.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10430-10435
    • Kamura, T.1    Sato, S.2    Iwai, K.3    Czyzyk-Krzeska, M.4    Conaway, R.C.5    Conaway, J.W.6
  • 37
    • 0035866817 scopus 로고    scopus 로고
    • Mechanism of specific nuclear transport of adriamycin: The mode of nuclear translocation of adriamycin-proteasome complex
    • Kiyomiya K, Matsuo S, Kurebe M. Mechanism of specific nuclear transport of adriamycin: the mode of nuclear translocation of adriamycin-proteasome complex. Cancer Res 2001; 61: 2467-71.
    • (2001) Cancer Res , vol.61 , pp. 2467-2471
    • Kiyomiya, K.1    Matsuo, S.2    Kurebe, M.3
  • 38
    • 0030775380 scopus 로고    scopus 로고
    • Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1
    • Levitskaya J, Sharipo A, Leonchiks A, Ciechanover A, Masucci MG. Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1. Proc Natl Acad Sci U S A 1997; 94: 12616-21.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 12616-12621
    • Levitskaya, J.1    Sharipo, A.2    Leonchiks, A.3    Ciechanover, A.4    Masucci, M.G.5
  • 39
    • 0033595124 scopus 로고    scopus 로고
    • Promoter specificity and stability control of the p53-related protein p73
    • Lee CW, La Thangue NB. Promoter specificity and stability control of the p53-related protein p73. Oncogene 1999; 18: 4171-81.
    • (1999) Oncogene , vol.18 , pp. 4171-4181
    • Lee, C.W.1    La Thangue, N.B.2
  • 41
    • 0034934948 scopus 로고    scopus 로고
    • Activation of ATP-ubiquitin-dependent proteolysis in skeletal muscle in vivo and murine myoblasts in vitro by a proteolysis-inducing factor (PIF)
    • Lorite MJ, Smith HJ, Arnold JA, Morris A, Thompson MG, Tisdale MJ. Activation of ATP-ubiquitin-dependent proteolysis in skeletal muscle in vivo and murine myoblasts in vitro by a proteolysis-inducing factor (PIF). Br J Cancer 2001; 85: 297-302.
    • (2001) Br J Cancer , vol.85 , pp. 297-302
    • Lorite, M.J.1    Smith, H.J.2    Arnold, J.A.3    Morris, A.4    Thompson, M.G.5    Tisdale, M.J.6
  • 42
    • 0035820074 scopus 로고    scopus 로고
    • UV light-induced degradation of RNA polymerase II is dependent on the Cockayne's syndrome A and B proteins but not p53 or MLH1
    • McKay BC, Chen F, Clarke ST, Wiggin HE, Harley LM, Ljungman M. UV light-induced degradation of RNA polymerase II is dependent on the Cockayne's syndrome A and B proteins but not p53 or MLH1. Murat Res 2001; 485: 93-105.
    • (2001) Murat Res , vol.485 , pp. 93-105
    • McKay, B.C.1    Chen, F.2    Clarke, S.T.3    Wiggin, H.E.4    Harley, L.M.5    Ljungman, M.6
  • 43
    • 0035798622 scopus 로고    scopus 로고
    • 26S proteasome-mediated degradation of topoisomerase II cleavable complexes
    • Mao Y, Desai SD, Ting CY, Hwang J, Liu LF. 26S proteasome-mediated degradation of topoisomerase II cleavable complexes. J Biol Chem 2001; 276: 40652-8.
    • (2001) J Biol Chem , vol.276 , pp. 40652-40658
    • Mao, Y.1    Desai, S.D.2    Ting, C.Y.3    Hwang, J.4    Liu, L.F.5
  • 44
    • 0035284812 scopus 로고    scopus 로고
    • Proteasomes modulate balance among proapoptotic and antiapoptotic Bcl-2 family members and compromise functioning of the electron transport chain in leukemic cells
    • Marshansky V, Wang X, Bertrand R, Luo H, Duguid W, Chinnadurai G, Kanaan N, Vu MD, Wu J. Proteasomes modulate balance among proapoptotic and antiapoptotic Bcl-2 family members and compromise functioning of the electron transport chain in leukemic cells. J Immunol 2001; 166: 3130-42.
    • (2001) J Immunol , vol.166 , pp. 3130-3142
    • Marshansky, V.1    Wang, X.2    Bertrand, R.3    Luo, H.4    Duguid, W.5    Chinnadurai, G.6    Kanaan, N.7    Vu, M.D.8    Wu, J.9
  • 45
    • 0035970007 scopus 로고    scopus 로고
    • Proteins associated with the promyelocytic leukemia gene product (PML)-containing nuclear body move to the nucleolus upon inhibition of proteasome-dependent protein degradation
    • Mattsson K, Pokrovskaja K, Kiss C, Klein G, Szekely L. Proteins associated with the promyelocytic leukemia gene product (PML)-containing nuclear body move to the nucleolus upon inhibition of proteasome-dependent protein degradation. Proc Natl Acad Sci U S A 2001; 98: 1012-7.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 1012-1017
    • Mattsson, K.1    Pokrovskaja, K.2    Kiss, C.3    Klein, G.4    Szekely, L.5
  • 46
    • 0029964851 scopus 로고    scopus 로고
    • Signal transduction through beta-catenin and specification of cell fate during embryogenesis
    • Miller JR, Moon RT. Signal transduction through beta-catenin and specification of cell fate during embryogenesis. Genes Dev 1996; 10: 2527-39.
    • (1996) Genes Dev , vol.10 , pp. 2527-2539
    • Miller, J.R.1    Moon, R.T.2
  • 47
    • 0034813575 scopus 로고    scopus 로고
    • The Xeroderma pigmentosum group E gene product ddb2 is a specific target of cullin 4a in mammalian cells
    • Nag A, Bondar T, Shiv S, Raychaudhuri P. The Xeroderma pigmentosum group E gene product ddb2 is a specific target of cullin 4a in mammalian cells. Mol Cell Biol 2001; 21: 6738-47.
    • (2001) Mol Cell Biol , vol.21 , pp. 6738-6747
    • Nag, A.1    Bondar, T.2    Shiv, S.3    Raychaudhuri, P.4
  • 49
    • 0036678959 scopus 로고    scopus 로고
    • Role and function of the 26S proteasome in proliferation and apoptosis
    • Naujokat C, Hoffman S. Role and function of the 26S proteasome in proliferation and apoptosis. Laboratory Investigation 2002; 82: 965-80.
    • (2002) Laboratory Investigation , vol.82 , pp. 965-980
    • Naujokat, C.1    Hoffman, S.2
  • 50
    • 0033542081 scopus 로고    scopus 로고
    • Glucose starvation and hypoxia induce nuclear accumulation of proteasome in cancer cells
    • Ogiso Y, Tomida A, Kim HD, Tsuruo T. Glucose starvation and hypoxia induce nuclear accumulation of proteasome in cancer cells. Biochem Biophys Res Commun 1999; 258: 448-52.
    • (1999) Biochem Biophys Res Commun , vol.258 , pp. 448-452
    • Ogiso, Y.1    Tomida, A.2    Kim, H.D.3    Tsuruo, T.4
  • 51
    • 0035337151 scopus 로고    scopus 로고
    • Ionizing radiation affects 26S proteasome function and associated molecular responses, even at low doses
    • Pajonk F, McBride WH. Ionizing radiation affects 26S proteasome function and associated molecular responses, even at low doses. Radiother Oncol 2001; 59: 203-12.
    • (2001) Radiother Oncol , vol.59 , pp. 203-212
    • Pajonk, F.1    McBride, W.H.2
  • 52
    • 0027427249 scopus 로고
    • The yeast DOA4 gene encodes a deubiquitination enzyme related to a product of the human tre-2 oncogene
    • Papa FR, Hochstrasser M. The yeast DOA4 gene encodes a deubiquitination enzyme related to a product of the human tre-2 oncogene. Nature 1993; 366: 313-9.
    • (1993) Nature , vol.366 , pp. 313-319
    • Papa, F.R.1    Hochstrasser, M.2
  • 54
    • 0035955745 scopus 로고    scopus 로고
    • The von Hippel-Lindau protein interacts with heteronuclear ribonucleoprotein a2 and regulates its expression
    • Pioli PA, Rigby WF. The von Hippel-Lindau protein interacts with heteronuclear ribonucleoprotein a2 and regulates its expression. J Biol Chem 2001; 276: 40346-52.
    • (2001) J Biol Chem , vol.276 , pp. 40346-40352
    • Pioli, P.A.1    Rigby, W.F.2
  • 55
    • 0033895709 scopus 로고    scopus 로고
    • Wnt signalling and cancer
    • Polakis P. Wnt signalling and cancer. Genes Dev; 2000; 14: 1837-51.
    • (2000) Genes Dev , vol.14 , pp. 1837-1851
    • Polakis, P.1
  • 56
    • 0034985241 scopus 로고    scopus 로고
    • Deoxycholic acid suppresses p53 by stimulating proteasome-mediated p53 protein degradation
    • Qiao D, Gaitonde SV, Qi W, Martinez JD. Deoxycholic acid suppresses p53 by stimulating proteasome-mediated p53 protein degradation. Carcinogenesis 2001; 22: 957-64.
    • (2001) Carcinogenesis , vol.22 , pp. 957-964
    • Qiao, D.1    Gaitonde, S.V.2    Qi, W.3    Martinez, J.D.4
  • 57
    • 0030871048 scopus 로고    scopus 로고
    • Loss of beta-catenin regulation by the APC tumor suppressor protein correlates with loss of structure due to common somatic mutations of the gene
    • Rubinfeld B, Albert I, Porfiri E, Mukemitsu S, Polakis P. Loss of beta-catenin regulation by the APC tumor suppressor protein correlates with loss of structure due to common somatic mutations of the gene. Cancer Research 1997; 57: 4624-30.
    • (1997) Cancer Research , vol.57 , pp. 4624-4630
    • Rubinfeld, B.1    Albert, I.2    Porfiri, E.3    Mukemitsu, S.4    Polakis, P.5
  • 59
    • 0035800838 scopus 로고    scopus 로고
    • Oncogenic ras represses transforming growth factor-beta /Smad signaling by degrading tumor suppressor Smad4
    • Saha D, Datta PK, Beauchamp RD. Oncogenic ras represses transforming growth factor-beta /Smad signaling by degrading tumor suppressor Smad4. J Biol Chem 2001; 276: 29531-7.
    • (2001) J Biol Chem , vol.276 , pp. 29531-29537
    • Saha, D.1    Datta, P.K.2    Beauchamp, R.D.3
  • 61
    • 0036484289 scopus 로고    scopus 로고
    • High frequency of a non-functional TAP1/LMP2 promoter polymorphism in human tumors
    • Seliger B, Boch M, Ritz V, Huber C. High frequency of a non-functional TAP1/LMP2 promoter polymorphism in human tumors. Int J Oncol 2002; 20: 349-59.
    • (2002) Int J Oncol , vol.20 , pp. 349-359
    • Seliger, B.1    Boch, M.2    Ritz, V.3    Huber, C.4
  • 62
    • 0035875767 scopus 로고    scopus 로고
    • cis-Inhibition of proteasomal degradation by viral repeats: Impact of length and amino acid composition
    • Sharipo A, Imreh M, Leonchiks A, Branden C, Masucci MG. cis-Inhibition of proteasomal degradation by viral repeats: impact of length and amino acid composition. FEBS Lett 2001; 499: 137-42.
    • (2001) FEBS Lett , vol.499 , pp. 137-142
    • Sharipo, A.1    Imreh, M.2    Leonchiks, A.3    Branden, C.4    Masucci, M.G.5
  • 63
    • 0036616727 scopus 로고    scopus 로고
    • Identification of an intronic TG repeat polymorphism in the human proteasome core particle PROS-27 gene
    • Sjakste T, Lauberte L, Collan Y, Savontaus M-L, Bajare A, Scherrer K, Sjakste N. Identification of an intronic TG repeat polymorphism in the human proteasome core particle PROS-27 gene. DNA Seq 2002; 13: 139-43.
    • (2002) DNA Seq , vol.13 , pp. 139-143
    • Sjakste, T.1    Lauberte, L.2    Collan, Y.3    Savontaus, M.-L.4    Bajare, A.5    Scherrer, K.6    Sjakste, N.7
  • 64
    • 18844480014 scopus 로고    scopus 로고
    • Involvement of all-trans-retinoic acid in the breakdown of retinoic acid receptors alpha and gamma through proteasomes in MCF-7 human breast cancer cells
    • Tanaka T, Rodriguez de la Concepcion ML, De Luca LM. Involvement of all-trans-retinoic acid in the breakdown of retinoic acid receptors alpha and gamma through proteasomes in MCF-7 human breast cancer cells. Biochem Pharmacol 2001; 61: 1347-55.
    • (2001) Biochem Pharmacol , vol.61 , pp. 1347-1355
    • Tanaka, T.1    Rodriguez de la Concepcion, M.L.2    De Luca, L.M.3
  • 65
    • 0034458955 scopus 로고    scopus 로고
    • Rat protein tyrosine phosphatase eta suppresses the neoplastic phenotype of retrovirally transformed thyroid cells through the stabilization of p27(Kipl)
    • Trapasso F, Iuliano R, Boccia A, Stella A, Visconti R, Bruni P, Baldassarre G, Santoro M, Viglietto G, Fusco A. Rat protein tyrosine phosphatase eta suppresses the neoplastic phenotype of retrovirally transformed thyroid cells through the stabilization of p27(Kipl). Mol Cell Biol 2000; 20: 9236-46.
    • (2000) Mol Cell Biol , vol.20 , pp. 9236-9246
    • Trapasso, F.1    Iuliano, R.2    Boccia, A.3    Stella, A.4    Visconti, R.5    Bruni, P.6    Baldassarre, G.7    Santoro, M.8    Viglietto, G.9    Fusco, A.10
  • 66
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-jun degradation in vivo is mediated by the delta domain
    • Treier M, Straszewski LM, Bohman D. Ubiquitin-dependent c-jun degradation in vivo is mediated by the delta domain. Cell 1994; 78: 787-90.
    • (1994) Cell , vol.78 , pp. 787-790
    • Treier, M.1    Straszewski, L.M.2    Bohman, D.3
  • 67
    • 0032980308 scopus 로고    scopus 로고
    • The prognostic significance of altered cyclin-dependent kinase inhibitors in human cancer
    • Tsihlias J, Kapusta L, Slingerland J. The prognostic significance of altered cyclin-dependent kinase inhibitors in human cancer. Ann Rev Med 1999; 50: 401-23.
    • (1999) Ann Rev Med , vol.50 , pp. 401-423
    • Tsihlias, J.1    Kapusta, L.2    Slingerland, J.3
  • 68
    • 0027480969 scopus 로고
    • Serum concentration and localization in tumor cells of proteasomes in patients with hematological malignancy and their pathophysiologic significance
    • Wada M, Kosaka M, Saito S, Sano T, Tanaka K, Ichihara A. Serum concentration and localization in tumor cells of proteasomes in patients with hematological malignancy and their pathophysiologic significance. J Lab Clin Med 1993; 121: 215-23.
    • (1993) J Lab Clin Med , vol.121 , pp. 215-223
    • Wada, M.1    Kosaka, M.2    Saito, S.3    Sano, T.4    Tanaka, K.5    Ichihara, A.6
  • 69
    • 0035797506 scopus 로고    scopus 로고
    • Both Rb and E7 are regulated by the ubiquitin proteasome pathway in HPV-containing cervical tumor cells
    • Wang J, Sampath A, Raychaudhuri P, Bagchi S. Both Rb and E7 are regulated by the ubiquitin proteasome pathway in HPV-containing cervical tumor cells. Oncogene 2001; 20: 4740-9.
    • (2001) Oncogene , vol.20 , pp. 4740-4749
    • Wang, J.1    Sampath, A.2    Raychaudhuri, P.3    Bagchi, S.4
  • 70
    • 0033600759 scopus 로고    scopus 로고
    • Cytoplasmically "sequestered" wild type p53 protein is resistant to Mdm2-mediated degradation
    • Zaika A, Marchenko N, Moll UM. Cytoplasmically "sequestered" wild type p53 protein is resistant to Mdm2-mediated degradation. J Biol Chem 1999; 274: 27474-80.
    • (1999) J Biol Chem , vol.274 , pp. 27474-27480
    • Zaika, A.1    Marchenko, N.2    Moll, U.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.