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Volumn 292, Issue 5, 1999, Pages 957-963

The N-terminal domain of MDM2 resembles calmodulin and its relatives

Author keywords

Capping box; Duplication; EF hand; Hydrogen bonds; MDM2

Indexed keywords

CALMODULIN; ONCOPROTEIN;

EID: 0033536618     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3125     Document Type: Article
Times cited : (5)

References (32)
  • 5
    • 0032579321 scopus 로고    scopus 로고
    • N terminus of murine p53 tumour suppressor is an independent regulatory domain affecting activation and thermostability
    • Hansen S., Lane D. P., Midgley C. A. N terminus of murine p53 tumour suppressor is an independent regulatory domain affecting activation and thermostability. J. Mol. Biol. 275:1998;575-588.
    • (1998) J. Mol. Biol. , vol.275 , pp. 575-588
    • Hansen, S.1    Lane, D.P.2    Midgley, C.A.3
  • 6
    • 0027204024 scopus 로고
    • Helix stop signals in proteins and peptides: The capping box
    • Harper E., Rose G. D. Helix stop signals in proteins and peptides: the capping box. Biochemistry. 32:1993;7605-7609.
    • (1993) Biochemistry , vol.32 , pp. 7605-7609
    • Harper, E.1    Rose, G.D.2
  • 7
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y., Maya R., Kazaz A., Oren M. Mdm2 promotes the rapid degradation of p53. Nature. 387:1997;296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 8
    • 0033521621 scopus 로고    scopus 로고
    • Association of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for p53
    • Hondo R., Yasuda H. Association of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for p53. EMBO J. 18:1999;22-27.
    • (1999) EMBO J. , vol.18 , pp. 22-27
    • Hondo, R.1    Yasuda, H.2
  • 9
    • 0030589509 scopus 로고    scopus 로고
    • Structure of the regulatory domain of scallop myosin at 2 Å resolution
    • Houdusse A., Silver M., Cohen C. Structure of the regulatory domain of scallop myosin at 2 Å resolution. Structure. 4:1996;1475-1490.
    • (1996) Structure , vol.4 , pp. 1475-1490
    • Houdusse, A.1    Silver, M.2    Cohen, C.3
  • 11
    • 0028678827 scopus 로고
    • Calcium binding proteins I: EF-hands
    • Kawasaki H., Kretsinger R. H. Calcium binding proteins I: EF-hands. Protein Profile. 1:1994;343-517.
    • (1994) Protein Profile , vol.1 , pp. 343-517
    • Kawasaki, H.1    Kretsinger, R.H.2
  • 14
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat M. H. G., Jones S., Vousden K. H. Regulation of p53 stability by Mdm2. Nature. 387:1997;299-303.
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.G.1    Jones, S.2    Vousden, K.H.3
  • 15
  • 16
    • 0030612360 scopus 로고    scopus 로고
    • MDM2-arbiter of p53's destruction
    • Lane D. P., Hall P. A. MDM2-arbiter of p53's destruction. Trends Biochem. Sci. 22:1997;372-374.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 372-374
    • Lane, D.P.1    Hall, P.A.2
  • 18
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures
    • Meador W. E., Means A. R., Quiocho F. A. Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures. Science. 262:1993;1718-1721.
    • (1993) Science , vol.262 , pp. 1718-1721
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 19
    • 0000302360 scopus 로고
    • Loops, bulges, turns and hairpins in proteins
    • Milner-White E. J., Poet R. Loops, bulges, turns and hairpins in proteins. Trends Biochem. Sci. 12:1987;189-192.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 189-192
    • Milner-White, E.J.1    Poet, R.2
  • 20
    • 0016430638 scopus 로고
    • Refinement of the structure of carp muscle parvalbumin
    • Moews P. C., Kretsinger R. H. Refinement of the structure of carp muscle parvalbumin. J. Mol. Biol. 91:1975;201-225.
    • (1975) J. Mol. Biol. , vol.91 , pp. 201-225
    • Moews, P.C.1    Kretsinger, R.H.2
  • 21
    • 0028961335 scopus 로고
    • Scop: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin A. G., Brenner S. E., Hubbard T., Chothia C. Scop: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247:1995;536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 24
    • 0032518917 scopus 로고    scopus 로고
    • Nucleo-cytoplamic shuffling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the HIV rev protein
    • Roth J., Dobbelstein M., Freedman D. A., Shenk T., Levine A. J. Nucleo-cytoplamic shuffling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the HIV rev protein. EMBO J. 17:1998;554-564.
    • (1998) EMBO J. , vol.17 , pp. 554-564
    • Roth, J.1    Dobbelstein, M.2    Freedman, D.A.3    Shenk, T.4    Levine, A.J.5
  • 26
    • 0029669991 scopus 로고    scopus 로고
    • The S100 family of EF-hand calcium binding proteins: Function and pathology
    • Schafer B. W., Heizmann C. W. The S100 family of EF-hand calcium binding proteins: function and pathology. Trends Biochem. Sci. 21:1996;14-140.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 14-140
    • Schafer, B.W.1    Heizmann, C.W.2
  • 27
    • 0027986703 scopus 로고
    • Sequence determinants of the capping box, a stabilising motif at the N-termini of α-helices
    • Seale J. W., Srinivasan R., Rose G. D. Sequence determinants of the capping box, a stabilising motif at the N-termini of α-helices. Protein Sci. 3:1994;1741-1745.
    • (1994) Protein Sci. , vol.3 , pp. 1741-1745
    • Seale, J.W.1    Srinivasan, R.2    Rose, G.D.3
  • 28
    • 0033559256 scopus 로고    scopus 로고
    • A Leucine-rich nuclear export signal in the p53 tetramerization domain: Regulation of subcellular localisation and p53 activity by NES masking
    • Stommel J. M., Marchenko N. D., Jimenz G. S., Moll U. M., Hope T. J., Wahl G. M. A Leucine-rich nuclear export signal in the p53 tetramerization domain: regulation of subcellular localisation and p53 activity by NES masking. EMBO J. 18:1999;1660-1672.
    • (1999) EMBO J. , vol.18 , pp. 1660-1672
    • Stommel, J.M.1    Marchenko, N.D.2    Jimenz, G.S.3    Moll, U.M.4    Hope, T.J.5    Wahl, G.M.6
  • 29
    • 0028970090 scopus 로고
    • Structure and function of transcriptional activation domains
    • Triezenberg S. J. Structure and function of transcriptional activation domains. Curr. Opin. Genet. Dev. 5:1995;190-193.
    • (1995) Curr. Opin. Genet. Dev. , vol.5 , pp. 190-193
    • Triezenberg, S.J.1
  • 30
    • 0033548459 scopus 로고    scopus 로고
    • A natural grouping of motifs with an aspartate or asparagine residue forming two hydrogen bonds to residues ahead of it in sequence: Their occurrence at α-helical N-termini and in other situations
    • Wan W.-Y., Milner-White E. J. A natural grouping of motifs with an aspartate or asparagine residue forming two hydrogen bonds to residues ahead of it in sequence: their occurrence at α-helical N-termini and in other situations. J. Mol. Biol. 286:1999a;1633-1649.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1633-1649
    • Wan, W.-Y.1    Milner-White, E.J.2
  • 31
    • 0033548705 scopus 로고    scopus 로고
    • A recurring two-hydrogen-bond motif incorporating a serine or threonine residue is found both at α-helical N-termini and in other situations
    • Wan W.-Y., Milner-White E. J. A recurring two-hydrogen-bond motif incorporating a serine or threonine residue is found both at α-helical N-termini and in other situations. J. Mol. Biol. 286:1999b;1651-1662.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1651-1662
    • Wan, W.-Y.1    Milner-White, E.J.2
  • 32
    • 0032549711 scopus 로고    scopus 로고
    • ARF promotes MDM2 degradation and stabilises p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumour suppression pathways
    • Zhang Y., Xiong Y., Yarborough W. G. ARF promotes MDM2 degradation and stabilises p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumour suppression pathways. Cell. 92:1998;725-734.
    • (1998) Cell , vol.92 , pp. 725-734
    • Zhang, Y.1    Xiong, Y.2    Yarborough, W.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.