메뉴 건너뛰기




Volumn 11, Issue 1, 2010, Pages 122-127

Interaction of tumor suppressor p53 with DNA and proteins

Author keywords

Cell lysates; Consensus sequence; DNA; Interaction; Metalloprotein; Monoclonal antibodies; p53

Indexed keywords

DOUBLE STRANDED DNA; METALLOTHIONEIN; MONOCLONAL ANTIBODY; MUTANT PROTEIN; PROTEIN; PROTEIN P53; RNA;

EID: 77950130203     PISSN: 13892010     EISSN: 18734316     Source Type: Journal    
DOI: 10.2174/138920110790725366     Document Type: Review
Times cited : (3)

References (52)
  • 1
    • 0035555650 scopus 로고    scopus 로고
    • Activation and activities of the p53 tumor suppressor protein
    • Balint, E.; Vousden, K. H. Activation and activities of the p53 tumor suppressor protein. Br. J. Cancer, 2002, 85, 1813-1823.
    • (2002) Br. J. Cancer , vol.85 , pp. 1813-1823
    • Balint, E.1    Vousden, K.H.2
  • 2
    • 0035902115 scopus 로고    scopus 로고
    • Proliferation, cell cycle and apoptosis in cancer
    • Evan, G. I.; Vousden, K. H. Proliferation, cell cycle and apoptosis in cancer. Nature, 2001, 411, 342-348.
    • (2001) Nature , vol.411 , pp. 342-348
    • Evan, G.I.1    Vousden, K.H.2
  • 4
    • 0027983669 scopus 로고
    • Crystal structure of p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Cho, Y.; Gorina, S.; Jeffrey, P. D.; Pavletich, N. P. Crystal structure of p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science, 1994, 265, 346-355.
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 5
    • 0027182946 scopus 로고
    • Functional domains of wild-type and mutant p53 proteins involved in transcriptional regulation, transdominant inhibition, and transformation suppression
    • Unger, T.; Mietz, J. A.; Scheffner, M.; Yee, C. L.; Howley, P. M. Functional domains of wild-type and mutant p53 proteins involved in transcriptional regulation, transdominant inhibition, and transformation suppression. Mol. Cell. Biol., 1993, 13, 5186-5194.
    • (1993) Mol. Cell. Biol , vol.13 , pp. 5186-5194
    • Unger, T.1    Mietz, J.A.2    Scheffner, M.3    Yee, C.L.4    Howley, P.M.5
  • 6
    • 0027174586 scopus 로고
    • Use of the two-hybrid system to identify the domain of p53 involved in oligomerization
    • Iwabuchi, K.; Li, B.; Bartel, P.; Fields, S. Use of the two-hybrid system to identify the domain of p53 involved in oligomerization. Oncogene, 1993, 8, 1693-1696.
    • (1993) Oncogene , vol.8 , pp. 1693-1696
    • Iwabuchi, K.1    Li, B.2    Bartel, P.3    Fields, S.4
  • 8
    • 0030941458 scopus 로고    scopus 로고
    • p53, the cellular gatekeeper for growth and division
    • Levine, A. J. p53, the cellular gatekeeper for growth and division. Cell, 1997, 88, 323-331.
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 9
    • 0028204538 scopus 로고
    • The 1993 Walter Hubert Lecture: The role of the p53 tumor-suppressor gene in tumorigenesis
    • Levine, A. J.; Perry, M. E.; Chang, A.; Silver, A.; Dittmer, D.; Wu, M .; Welsh, D. The 1993 Walter Hubert Lecture: the role of the p53 tumor-suppressor gene in tumorigenesis. Br. J. Cancer, 1994, 69, 409-416.
    • (1994) Br. J. Cancer , vol.69 , pp. 409-416
    • Levine, A.J.1    Perry, M.E.2    Chang, A.3    Silver, A.4    Dittmer, D.5    Wu, M.6    Welsh, D.7
  • 11
    • 0024452546 scopus 로고    scopus 로고
    • Takahashi, T.; Nau, M. M.; Chiba, I.; Birrer, M. J.; Rosenberg, R. K.; Vinocour, M.; Levitt, M.; Pass, H.; Gazdar, A. F.; Minna, J. D. p53: a frequent target for genetic abnormalities in lung cancer. Science, 1989, 246, 491-494.
    • Takahashi, T.; Nau, M. M.; Chiba, I.; Birrer, M. J.; Rosenberg, R. K.; Vinocour, M.; Levitt, M.; Pass, H.; Gazdar, A. F.; Minna, J. D. p53: a frequent target for genetic abnormalities in lung cancer. Science, 1989, 246, 491-494.
  • 12
    • 0027756186 scopus 로고    scopus 로고
    • Harris, C. C. p53: at the crossroads of molecular carcinogenesis and risk assessment. Science, 1993, 262, 1980-1981.
    • Harris, C. C. p53: at the crossroads of molecular carcinogenesis and risk assessment. Science, 1993, 262, 1980-1981.
  • 14
    • 0032526426 scopus 로고    scopus 로고
    • How p53 binds DNA as a tetramer
    • Mclure, K. G.; Lee, P. W. K. How p53 binds DNA as a tetramer. EMBO J., 1998, 17, 3342-3350.
    • (1998) EMBO J , vol.17 , pp. 3342-3350
    • Mclure, K.G.1    Lee, P.W.K.2
  • 17
    • 0026650531 scopus 로고
    • A transcriptionally active DNA-binding site for human p53 protein complexes
    • Funk, W. D.; Pak, D. T.; Karas, R. H.; Wright, W. E.; Shay, J. W. A transcriptionally active DNA-binding site for human p53 protein complexes. Mol. Cell. Biol., 1992, 12, 2866-2871.
    • (1992) Mol. Cell. Biol , vol.12 , pp. 2866-2871
    • Funk, W.D.1    Pak, D.T.2    Karas, R.H.3    Wright, W.E.4    Shay, J.W.5
  • 18
    • 0026702212 scopus 로고
    • Wild-type p53 medicates positive regulation of gene expression through a specific DNA sequence element
    • Zambetti, G. P.; Bargonetti, J.; Walker, K.; Prives, C ; Levine, A. J. Wild-type p53 medicates positive regulation of gene expression through a specific DNA sequence element. Genes Dev., 1992, 6, 1143-1152.
    • (1992) Genes Dev , vol.6 , pp. 1143-1152
    • Zambetti, G.P.1    Bargonetti, J.2    Walker, K.3    Prives, C.4    Levine, A.J.5
  • 19
    • 0027244853 scopus 로고
    • The p53 MDM2 autoregulatory feedback loop
    • Wu, X. W.; Hayle, J. H.; Olson, D.; Levine, A. J. The p53 MDM2 autoregulatory feedback loop. Genes Dev., 1993, 7, 1126-1132.
    • (1993) Genes Dev , vol.7 , pp. 1126-1132
    • Wu, X.W.1    Hayle, J.H.2    Olson, D.3    Levine, A.J.4
  • 20
    • 0028883179 scopus 로고
    • Tumor suppressor p53 is a direct transcriptional activator of the human Bax gene
    • Miyashita, T.; Reed, J. C. Tumor suppressor p53 is a direct transcriptional activator of the human Bax gene. Cell, 1995, 80, 293-299.
    • (1995) Cell , vol.80 , pp. 293-299
    • Miyashita, T.1    Reed, J.C.2
  • 24
    • 0343775742 scopus 로고    scopus 로고
    • Specific modulation of p53 binding to consensus sequence within supercoiled DNA by monoclonal antibodies
    • Brazda, V.; Palecek, J.; Posisilova, S.; Vojtesek, B.; Palecek, E. Specific modulation of p53 binding to consensus sequence within supercoiled DNA by monoclonal antibodies. Biochem. Biophys. Res. Commun., 2000, 267, 934-939.
    • (2000) Biochem. Biophys. Res. Commun , vol.267 , pp. 934-939
    • Brazda, V.1    Palecek, J.2    Posisilova, S.3    Vojtesek, B.4    Palecek, E.5
  • 25
    • 0033544705 scopus 로고    scopus 로고
    • DNA bending due to specific p53 and p53 core domain-DNA interactions visualized by electron microscopy
    • Cherny, D. I.; Striker, G.; Subramaniam, V.; Jett, S. D.; Palecek, E.; Jovin, T. M. DNA bending due to specific p53 and p53 core domain-DNA interactions visualized by electron microscopy. J. Mol. Biol., 1999, 294, 1015-1026.
    • (1999) J. Mol. Biol , vol.294 , pp. 1015-1026
    • Cherny, D.I.1    Striker, G.2    Subramaniam, V.3    Jett, S.D.4    Palecek, E.5    Jovin, T.M.6
  • 26
    • 38849110131 scopus 로고    scopus 로고
    • Capture of p53 by electrodes modified with consensus DNA deplexes and amplified voltammetric detection using ferrocene-capped gold nanoparticle/streptavidin conjugates
    • Wang, J.; Zhu, X.; Tu, Q.; Guo, Q.; Zarui, C. S.; Momand, J.; Sun, X. Z.; Zhou, F. Capture of p53 by electrodes modified with consensus DNA deplexes and amplified voltammetric detection using ferrocene-capped gold nanoparticle/streptavidin conjugates. Anal. Chem., 2008, 80, 769-774.
    • (2008) Anal. Chem , vol.80 , pp. 769-774
    • Wang, J.1    Zhu, X.2    Tu, Q.3    Guo, Q.4    Zarui, C.S.5    Momand, J.6    Sun, X.Z.7    Zhou, F.8
  • 27
    • 0033081465 scopus 로고    scopus 로고
    • p53 DNA binding can be modulated by factors that alter the conformational equilibrium
    • Mclure, K. G.; Lee, P. W. K. p53 DNA binding can be modulated by factors that alter the conformational equilibrium. EMBO J., 1999, 18, 763-770.
    • (1999) EMBO J , vol.18 , pp. 763-770
    • Mclure, K.G.1    Lee, P.W.K.2
  • 29
    • 42649114958 scopus 로고    scopus 로고
    • Mickael electrophilic addition of biotin to sulfhydryl groups
    • Hare, J. L.; Lee, E. Mickael electrophilic addition of biotin to sulfhydryl groups. Biochemistry, 1998, 28, 574-580.
    • (1998) Biochemistry , vol.28 , pp. 574-580
    • Hare, J.L.1    Lee, E.2
  • 30
    • 0041561065 scopus 로고    scopus 로고
    • Amplified voltammetric detection of DNA hybridization via oxidation of ferrocene caps on gold nanoparticle/streptavidin conjugates
    • Wang, J.; Li, J.; Baca, A. J.; Hu, J.; Zhou, F.; Yan, W.; Pang, D. Amplified voltammetric detection of DNA hybridization via oxidation of ferrocene caps on gold nanoparticle/streptavidin conjugates. Anal. Chem., 2003, 75, 3941-3945.
    • (2003) Anal. Chem , vol.75 , pp. 3941-3945
    • Wang, J.1    Li, J.2    Baca, A.J.3    Hu, J.4    Zhou, F.5    Yan, W.6    Pang, D.7
  • 31
    • 1042301988 scopus 로고    scopus 로고
    • Attachment of ferrocene-capped gold nanoparticle/streptavidin conjugates onto electrode surfaces covered with biotinylated biomolecules for enhanced voltammetric analysis
    • Baca, A. J.; Zhou, F.; Wang, J.; Hu, J.; Li, J.; Wang, J.; Chikneyan, Z. S. Attachment of ferrocene-capped gold nanoparticle/streptavidin conjugates onto electrode surfaces covered with biotinylated biomolecules for enhanced voltammetric analysis. Electroanalysis, 2004, 16, 73-80.
    • (2004) Electroanalysis , vol.16 , pp. 73-80
    • Baca, A.J.1    Zhou, F.2    Wang, J.3    Hu, J.4    Li, J.5    Wang, J.6    Chikneyan, Z.S.7
  • 33
    • 0000609633 scopus 로고
    • Surface plasmons in thin films
    • Economou, E. N. Surface plasmons in thin films. Phys. Rev., 1969, 182, 539-554.
    • (1969) Phys. Rev , vol.182 , pp. 539-554
    • Economou, E.N.1
  • 34
    • 0000195696 scopus 로고
    • Surface plasma oscillations at silver surfaces with thin transparent and absorbing coatings
    • Pockrand, I. Surface plasma oscillations at silver surfaces with thin transparent and absorbing coatings. Surf. Sci., 1978, 72, 577-588.
    • (1978) Surf. Sci , vol.72 , pp. 577-588
    • Pockrand, I.1
  • 37
    • 0023659137 scopus 로고
    • New metal chelate adsorbent selective for proteins and peptides containing neighboring histidine residues
    • Hochuli, E.; Doebeli, H.; Schacher, A. New metal chelate adsorbent selective for proteins and peptides containing neighboring histidine residues. J. Chromatogr., 1987, 411, 177-184.
    • (1987) J. Chromatogr , vol.411 , pp. 177-184
    • Hochuli, E.1    Doebeli, H.2    Schacher, A.3
  • 38
    • 0037102326 scopus 로고    scopus 로고
    • Oncolumn tris(2-carboxyethyl)phosphine reduction and IC5-maleimide labeling during purification of a RpoC fragment on a nickel-nitrilotriacetic acid column
    • Bergendahl, V.; Anthony, L. C.; Heyduk, T.; Burgess, R. R. Oncolumn tris(2-carboxyethyl)phosphine reduction and IC5-maleimide labeling during purification of a RpoC fragment on a nickel-nitrilotriacetic acid column. Anal. Biochem., 2002, 307, 368-374.
    • (2002) Anal. Biochem , vol.307 , pp. 368-374
    • Bergendahl, V.1    Anthony, L.C.2    Heyduk, T.3    Burgess, R.R.4
  • 39
    • 70450014859 scopus 로고    scopus 로고
    • Simultaneous and label-free determination of wild-type and mutant p53 at a single surface plasmon resonance chip preimmobilized with consensus DNA and monoclonal antibody
    • Wang, Y.; Zhu, X.; Wu, M.; Xia, N.; Wang, J.; Zhou, F. Simultaneous and label-free determination of wild-type and mutant p53 at a single surface plasmon resonance chip preimmobilized with consensus DNA and monoclonal antibody. Anal. Chem., 2009, 81, 8441-8446.
    • (2009) Anal. Chem , vol.81 , pp. 8441-8446
    • Wang, Y.1    Zhu, X.2    Wu, M.3    Xia, N.4    Wang, J.5    Zhou, F.6
  • 40
    • 33947463103 scopus 로고
    • A cadmium protein from equine kidney cortex
    • Margoshes, M.; Vallee, B. L. A cadmium protein from equine kidney cortex. J. Am. Chem. Soc., 1957, 79, 4813-4814.
    • (1957) J. Am. Chem. Soc , vol.79 , pp. 4813-4814
    • Margoshes, M.1    Vallee, B.L.2
  • 41
    • 0022555879 scopus 로고
    • Metallothionein
    • Hamer, D. H. Metallothionein. Annu. Rev. Biochem., 1986, 55, 913-951.
    • (1986) Annu. Rev. Biochem , vol.55 , pp. 913-951
    • Hamer, D.H.1
  • 42
    • 0036838489 scopus 로고    scopus 로고
    • Studies of metal binding reactions in metallothioneins by spectroscopic, molecular biology, and molecular modeling techniques
    • Chan, J.; Huang, Z.; Merrifield, M. E.; Salgado, M. T.; Stillman, M. J. Studies of metal binding reactions in metallothioneins by spectroscopic, molecular biology, and molecular modeling techniques. Coord. Chem. Rev., 2002, 233-234, 319-339.
    • (2002) Coord. Chem. Rev , vol.233-234 , pp. 319-339
    • Chan, J.1    Huang, Z.2    Merrifield, M.E.3    Salgado, M.T.4    Stillman, M.J.5
  • 43
    • 0345276580 scopus 로고    scopus 로고
    • Metallothioneins in human tumors and potential roles in carcinogenesis
    • Cherian, M. G.; Jayasurya, A.; Bay, B.-H. Metallothioneins in human tumors and potential roles in carcinogenesis. Mutat. Res., 2003, 533, 201-209.
    • (2003) Mutat. Res , vol.533 , pp. 201-209
    • Cherian, M.G.1    Jayasurya, A.2    Bay, B.-H.3
  • 45
    • 0034597536 scopus 로고    scopus 로고
    • Metalloregulation of the tumor suppressor protein p53: Zinc mediates the renaturation of p53 after exposure to metal chelators in vitro and in intact cells
    • Meplan, C.; Richard, M.-J.; Hainaut, P. Metalloregulation of the tumor suppressor protein p53: zinc mediates the renaturation of p53 after exposure to metal chelators in vitro and in intact cells. Oncogene, 2000, 19, 5227-5236.
    • (2000) Oncogene , vol.19 , pp. 5227-5236
    • Meplan, C.1    Richard, M.-J.2    Hainaut, P.3
  • 46
    • 0026323592 scopus 로고
    • Metal removal from mammalian metallothioneins
    • Hunziker, P. E. Metal removal from mammalian metallothioneins. Methods Enzymol., 1991, 205, 451-452.
    • (1991) Methods Enzymol , vol.205 , pp. 451-452
    • Hunziker, P.E.1
  • 47
    • 0032584186 scopus 로고    scopus 로고
    • Control of zinc transfer between thionein, metallothionein, and zinc proteins
    • Jacob, C.; Maret, W.; Vallee, B. L. Control of zinc transfer between thionein, metallothionein, and zinc proteins. Proc. Natl. Acad. Sci. USA, 1998, 95, 3489-3494.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3489-3494
    • Jacob, C.1    Maret, W.2    Vallee, B.L.3
  • 48
    • 71449125480 scopus 로고    scopus 로고
    • Studies of interaction of tumor suppressor p53 with apo-MT using surface plasmon resonance
    • Xia, N.; Liu, L.; Yi, X.; Wang, J. Studies of interaction of tumor suppressor p53 with apo-MT using surface plasmon resonance. Anal. Bioanal. Chem., 2009, 395, 2569-2575.
    • (2009) Anal. Bioanal. Chem , vol.395 , pp. 2569-2575
    • Xia, N.1    Liu, L.2    Yi, X.3    Wang, J.4
  • 49
    • 32344433407 scopus 로고    scopus 로고
    • Interaction of metallothionein with tumor suppressor p53 protein
    • Ostrakhovitch, E. A.; Olsson, P.-E.; Jiang, S.; Cherian, M. G. Interaction of metallothionein with tumor suppressor p53 protein. FEBS Lett., 2006, 580, 1235-1238.
    • (2006) FEBS Lett , vol.580 , pp. 1235-1238
    • Ostrakhovitch, E.A.1    Olsson, P.-E.2    Jiang, S.3    Cherian, M.G.4
  • 51
    • 0035914136 scopus 로고    scopus 로고
    • p53 unfolding detected by CD but not by tryptophan fluorescence
    • Nichols, N. M.; Matthews, K. S. p53 unfolding detected by CD but not by tryptophan fluorescence. Biochem. Biophys. Res. Commun., 2001, 288, 111-115.
    • (2001) Biochem. Biophys. Res. Commun , vol.288 , pp. 111-115
    • Nichols, N.M.1    Matthews, K.S.2
  • 52
    • 0037007442 scopus 로고    scopus 로고
    • Refolding and structural characterization of the human p53 tumor suppressor protein
    • Bell, S.; Hansen, S.; Buchner, J. Refolding and structural characterization of the human p53 tumor suppressor protein. Biophys. Chem., 2002, 96, 243-257.
    • (2002) Biophys. Chem , vol.96 , pp. 243-257
    • Bell, S.1    Hansen, S.2    Buchner, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.