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Volumn 17, Issue 1, 2005, Pages 11-21

Binding of natively unfolded HIF-1α ODD domain to p53

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; HYPOXIA INDUCIBLE FACTOR 1; POLYMER; PROTEIN P53; PROTEIN SUBUNIT;

EID: 11344292626     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2004.11.019     Document Type: Article
Times cited : (94)

References (54)
  • 5
    • 0016169865 scopus 로고
    • Determination of the helix and beta form of proteins in aqueous solution by circular dichroism
    • Chen Y.H., Yang J.T., Chau K.H. Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. Biochemistry. 13:1974;3350-3359
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3
  • 6
    • 0038529602 scopus 로고    scopus 로고
    • Direct interactions between HIF-1 alpha and Mdm2 modulate p53 function
    • Chen D., Li M., Luo J., Gu W. Direct interactions between HIF-1 alpha and Mdm2 modulate p53 function. J. Biol. Chem. 278:2003;13595-13598
    • (2003) J. Biol. Chem. , vol.278 , pp. 13595-13598
    • Chen, D.1    Li, M.2    Luo, J.3    Gu, W.4
  • 9
    • 0017701075 scopus 로고
    • Nonspecific interaction of lac repressor with DNA: An association reaction driven by counterion release
    • deHaseth P.L., Lohman T.M., Record M.T. Jr. Nonspecific interaction of lac repressor with DNA. an association reaction driven by counterion release Biochemistry. 16:1977;4783-4790
    • (1977) Biochemistry , vol.16 , pp. 4783-4790
    • Dehaseth, P.L.1    Lohman, T.M.2    Record Jr., M.T.3
  • 11
    • 0030956737 scopus 로고    scopus 로고
    • Fluorescence methods for studying equilibrium macromolecule-ligand interactions
    • Eftink M.R. Fluorescence methods for studying equilibrium macromolecule-ligand interactions. Methods Enzymol. 278:1997;221-257
    • (1997) Methods Enzymol. , vol.278 , pp. 221-257
    • Eftink, M.R.1
  • 16
    • 0037424614 scopus 로고    scopus 로고
    • Computational simulation of the statistical properties of unfolded proteins
    • Goldenberg D.P. Computational simulation of the statistical properties of unfolded proteins. J. Mol. Biol. 326:2003;1615-1633
    • (2003) J. Mol. Biol. , vol.326 , pp. 1615-1633
    • Goldenberg, D.P.1
  • 17
    • 0028110809 scopus 로고
    • Hypoxia induces accumulation of p53 protein, but activation of a G1-phase checkpoint by low-oxygen conditions is independent of p53 status
    • Graeber T.G., Peterson J.F., Tsai M., Monica K., Fornace A.J. Jr., Giaccia A.J. Hypoxia induces accumulation of p53 protein, but activation of a G1-phase checkpoint by low-oxygen conditions is independent of p53 status. Mol. Cell. Biol. 14:1994;6264-6277
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6264-6277
    • Graeber, T.G.1    Peterson, J.F.2    Tsai, M.3    Monica, K.4    Fornace Jr., A.J.5    Giaccia, A.J.6
  • 19
    • 0031927441 scopus 로고    scopus 로고
    • Tumor hypoxia and the cell cycle: Implications for malignant progression and response to therapy
    • Green S.L., Giaccia A.J. Tumor hypoxia and the cell cycle. implications for malignant progression and response to therapy Cancer J. Sci. Am. 4:1998;218-223
    • (1998) Cancer J. Sci. Am. , vol.4 , pp. 218-223
    • Green, S.L.1    Giaccia, A.J.2
  • 21
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser M. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30:1996;405-439
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 24
    • 0029944965 scopus 로고    scopus 로고
    • Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1
    • Jiang B.H., Rue E., Wang G.L., Roe R., Semenza G.L. Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1. J. Biol. Chem. 271:1996;17771-17778
    • (1996) J. Biol. Chem. , vol.271 , pp. 17771-17778
    • Jiang, B.H.1    Rue, E.2    Wang, G.L.3    Roe, R.4    Semenza, G.L.5
  • 25
    • 0030787469 scopus 로고    scopus 로고
    • Transactivation and inhibitory domains of hypoxia-inducible factor 1alpha. Modulation of transcriptional activity by oxygen tension
    • Jiang B.H., Zheng J.Z., Leung S.W., Roe R., Semenza G.L. Transactivation and inhibitory domains of hypoxia-inducible factor 1alpha. Modulation of transcriptional activity by oxygen tension. J. Biol. Chem. 272:1997;19253-19260
    • (1997) J. Biol. Chem. , vol.272 , pp. 19253-19260
    • Jiang, B.H.1    Zheng, J.Z.2    Leung, S.W.3    Roe, R.4    Semenza, G.L.5
  • 26
    • 0347723910 scopus 로고    scopus 로고
    • Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations
    • Joerger A.C., Allen M.D., Fersht A.R. Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations. J. Biol. Chem. 279:2004;1291-1296
    • (2004) J. Biol. Chem. , vol.279 , pp. 1291-1296
    • Joerger, A.C.1    Allen, M.D.2    Fersht, A.R.3
  • 27
    • 0032538797 scopus 로고    scopus 로고
    • Signal transduction in hypoxic cells: Inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1alpha
    • Kallio P.J., Okamoto K., O'Brien S., Carrero P., Makino Y., Tanaka H., Poellinger L. Signal transduction in hypoxic cells. inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1alpha EMBO J. 17:1998;6573-6586
    • (1998) EMBO J. , vol.17 , pp. 6573-6586
    • Kallio, P.J.1    Okamoto, K.2    O'Brien, S.3    Carrero, P.4    Makino, Y.5    Tanaka, H.6    Poellinger, L.7
  • 29
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch
    • Lando D., Peet D.J., Whelan D.A., Gorman J.J., Whitelaw M.L. Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch. Science. 295:2002;858-861
    • (2002) Science , vol.295 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3    Gorman, J.J.4    Whitelaw, M.L.5
  • 30
    • 0035095521 scopus 로고    scopus 로고
    • Large-scale purification of a stable form of recombinant tobacco etch virus protease
    • Lucast, L.J., Batey, R.T., and Doudna, J.A. (2001). Large-scale purification of a stable form of recombinant tobacco etch virus protease. Biotechniques 30, 544-546, 548, 550 passim.
    • (2001) Biotechniques , vol.30 , pp. 544-546
    • Lucast, L.J.1    Batey, R.T.2    Doudna, J.A.3
  • 31
    • 0035887011 scopus 로고    scopus 로고
    • FIH-1: A novel protein that interacts with HIF-1alpha and vhl to mediate repression of HIF-1 transcriptional activity
    • Mahon P.C., Hirota K., Semenza G.L. FIH-1. a novel protein that interacts with HIF-1alpha and vhl to mediate repression of HIF-1 transcriptional activity Genes Dev. 15:2001;2675-2686
    • (2001) Genes Dev. , vol.15 , pp. 2675-2686
    • Mahon, P.C.1    Hirota, K.2    Semenza, G.L.3
  • 32
    • 0026633117 scopus 로고
    • Natural polypeptides in left-handed helical conformation. A circular dichroism study of the linker histones' C-terminal fragments and beta-endorphin
    • Makarov A.A., Lobachov V.M., Adzhubei I.A., Esipova N.G. Natural polypeptides in left-handed helical conformation. A circular dichroism study of the linker histones' C-terminal fragments and beta-endorphin. FEBS Lett. 306:1992;63-65
    • (1992) FEBS Lett. , vol.306 , pp. 63-65
    • Makarov, A.A.1    Lobachov, V.M.2    Adzhubei, I.A.3    Esipova, N.G.4
  • 33
    • 0035903468 scopus 로고    scopus 로고
    • Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation
    • Masson N., Willam C., Maxwell P.H., Pugh C.W., Ratcliffe P.J. Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation. EMBO J. 20:2001;5197-5206
    • (2001) EMBO J. , vol.20 , pp. 5197-5206
    • Masson, N.1    Willam, C.2    Maxwell, P.H.3    Pugh, C.W.4    Ratcliffe, P.J.5
  • 34
    • 0037035851 scopus 로고    scopus 로고
    • Structure of an HIF-1alpha-pVHL complex: Hydroxyproline recognition in signaling
    • Min J.H., Yang H., Ivan M., Gertler F., Kaelin W.G. Jr., Pavletich N.P. Structure of an HIF-1alpha-pVHL complex. hydroxyproline recognition in signaling Science. 296:2002;1886-1889
    • (2002) Science , vol.296 , pp. 1886-1889
    • Min, J.H.1    Yang, H.2    Ivan, M.3    Gertler, F.4    Kaelin Jr., W.G.5    Pavletich, N.P.6
  • 35
    • 0037066755 scopus 로고    scopus 로고
    • Biogenesis of p53 involves cotranslational dimerization of monomers and posttranslational dimerization of dimers. Implications on the dominant negative effect
    • Nicholls C.D., McLure K.G., Shields M.A., Lee P.W. Biogenesis of p53 involves cotranslational dimerization of monomers and posttranslational dimerization of dimers. Implications on the dominant negative effect. J. Biol. Chem. 277:2002;12937-12945
    • (2002) J. Biol. Chem. , vol.277 , pp. 12937-12945
    • Nicholls, C.D.1    McLure, K.G.2    Shields, M.A.3    Lee, P.W.4
  • 36
    • 3042779529 scopus 로고    scopus 로고
    • P53 cannot be induced by hypoxia alone but responds to the hypoxic microenvironment
    • Pan Y., Oprysko P.R., Asham A.M., Koch C.J., Simon M.C. p53 cannot be induced by hypoxia alone but responds to the hypoxic microenvironment. Oncogene. 23:2004;4975-4983
    • (2004) Oncogene , vol.23 , pp. 4975-4983
    • Pan, Y.1    Oprysko, P.R.2    Asham, A.M.3    Koch, C.J.4    Simon, M.C.5
  • 37
    • 0035119625 scopus 로고    scopus 로고
    • Chemical shifts in denatured proteins: Resonance assignments for denatured ubiquitin and comparisons with other denatured proteins
    • Peti W., Smith L.J., Redfield C., Schwalbe H. Chemical shifts in denatured proteins. resonance assignments for denatured ubiquitin and comparisons with other denatured proteins J. Biomol. NMR. 19:2001;153-165
    • (2001) J. Biomol. NMR , vol.19 , pp. 153-165
    • Peti, W.1    Smith, L.J.2    Redfield, C.3    Schwalbe, H.4
  • 42
    • 0034901463 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1: Oxygen homeostasis and disease pathophysiology
    • Semenza G.L. Hypoxia-inducible factor 1. oxygen homeostasis and disease pathophysiology Trends Mol. Med. 7:2001;345-350
    • (2001) Trends Mol. Med. , vol.7 , pp. 345-350
    • Semenza, G.L.1
  • 43
    • 0030460724 scopus 로고    scopus 로고
    • Hypoxia response elements in the aldolase A, enolase 1, and lactate dehydrogenase a gene promoters contain essential binding sites for hypoxia-inducible factor 1
    • Semenza G.L., Jiang B.H., Leung S.W., Passantino R., Concordet J.P., Maire P., Giallongo A. Hypoxia response elements in the aldolase A, enolase 1, and lactate dehydrogenase A gene promoters contain essential binding sites for hypoxia-inducible factor 1. J. Biol. Chem. 271:1996;32529-32537
    • (1996) J. Biol. Chem. , vol.271 , pp. 32529-32537
    • Semenza, G.L.1    Jiang, B.H.2    Leung, S.W.3    Passantino, R.4    Concordet, J.P.5    Maire, P.6    Giallongo, A.7
  • 44
    • 0027733616 scopus 로고
    • Use of fast size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule
    • Uversky V. Use of fast size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule. Biochemistry. 32:1993;13288-13298
    • (1993) Biochemistry , vol.32 , pp. 13288-13298
    • Uversky, V.1
  • 45
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • a
    • Uversky V. Natively unfolded proteins. a point where biology waits for physics Protein Sci. 11:2002;739-756. a
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.1
  • 46
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • b
    • Uversky V.N. What does it mean to be natively unfolded? Eur. J. Biochem. 269:2002;2-12. b
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 47
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky V.N., Gillespie J.R., Fink A.L. Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins. 41:2000;415-427
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 48
    • 0029051439 scopus 로고
    • Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension
    • Wang G.L., Jiang B.H., Rue E.A., Semenza G.L. Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. Proc. Natl. Acad. Sci. USA. 92:1995;5510-5514
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5510-5514
    • Wang, G.L.1    Jiang, B.H.2    Rue, E.A.3    Semenza, G.L.4
  • 50
    • 0032535077 scopus 로고    scopus 로고
    • Up-regulation of hypoxia-inducible factor-1alpha is not sufficient for hypoxic/anoxic p53 induction
    • Wenger R.H., Camenisch G., Desbaillets I., Chilov D., Gassmann M. Up-regulation of hypoxia-inducible factor-1alpha is not sufficient for hypoxic/anoxic p53 induction. Cancer Res. 58:1998;5678-5680
    • (1998) Cancer Res. , vol.58 , pp. 5678-5680
    • Wenger, R.H.1    Camenisch, G.2    Desbaillets, I.3    Chilov, D.4    Gassmann, M.5
  • 52
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright P.E., Dyson H.J. Intrinsically unstructured proteins. re-assessing the protein structure-function paradigm J. Mol. Biol. 293:1999;321-331
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 54
    • 0036829096 scopus 로고    scopus 로고
    • Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators
    • Zor T., Mayr B.M., Dyson H.J., Montminy M.R., Wright P.E. Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators. J. Biol. Chem. 277:2002;42241-42248
    • (2002) J. Biol. Chem. , vol.277 , pp. 42241-42248
    • Zor, T.1    Mayr, B.M.2    Dyson, H.J.3    Montminy, M.R.4    Wright, P.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.