메뉴 건너뛰기




Volumn 5, Issue 8, 1998, Pages 439-445

A β-sheet peptide inhibitor of E47 dimerization and DNA binding

Author keywords

BHLH; Dimerization inhibition helix; Peptide; Sheet

Indexed keywords


EID: 0031851117     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(98)90160-0     Document Type: Article
Times cited : (22)

References (35)
  • 1
    • 0027994197 scopus 로고
    • Modulation of transcription factor-DNA interactions by anticancer drugs
    • Broggini, M. & D'Incalci, M. (1994). Modulation of transcription factor-DNA interactions by anticancer drugs. Anti-Cancer Drug Design 9, 373-387.
    • (1994) Anti-Cancer Drug Design , vol.9 , pp. 373-387
    • Broggini, M.1    D'Incalci, M.2
  • 2
    • 0026026263 scopus 로고
    • DNA intercalating antitumor agents
    • Baguley, B.C. (1991). DNA intercalating antitumor agents, Anti-Cancer Drug Design 6, 1-35.
    • (1991) Anti-Cancer Drug Design , vol.6 , pp. 1-35
    • Baguley, B.C.1
  • 3
    • 0030444841 scopus 로고    scopus 로고
    • DNA complexing minor groove-binding ligands: Antitumour and antimicrobial drug design
    • Pindur, U. & Fischer, G. (1996). DNA complexing minor groove-binding ligands: antitumour and antimicrobial drug design. Curr. Med. Chem. 3, 379-406.
    • (1996) Curr. Med. Chem. , vol.3 , pp. 379-406
    • Pindur, U.1    Fischer, G.2
  • 4
    • 0032576722 scopus 로고    scopus 로고
    • Recognition of the four Watson-Crick base pairs in the DNA minor groove by synthetic ligands
    • White, S., Szewczyk, J.W., Turner, J.M., Baird, E.E. & Dervan, P.B. (1998). Recognition of the four Watson-Crick base pairs in the DNA minor groove by synthetic ligands. Nature 391, 468-471.
    • (1998) Nature , vol.391 , pp. 468-471
    • White, S.1    Szewczyk, J.W.2    Turner, J.M.3    Baird, E.E.4    Dervan, P.B.5
  • 5
    • 0031431502 scopus 로고    scopus 로고
    • Antisense oligonucleotide therapeutics for human leukemia
    • Gewirtz, A.M. (1997). Antisense oligonucleotide therapeutics for human leukemia. Crit. Rev. Oncogenesis 8, 93-109.
    • (1997) Crit. Rev. Oncogenesis , vol.8 , pp. 93-109
    • Gewirtz, A.M.1
  • 6
    • 0027106198 scopus 로고
    • DNA triple-helix formation-an approach to artificial gene repressors
    • Maher, J.L. (1992). DNA triple-helix formation-an approach to artificial gene repressors. BioEssays 14, 807-815.
    • (1992) BioEssays , vol.14 , pp. 807-815
    • Maher, J.L.1
  • 7
    • 13144271454 scopus 로고    scopus 로고
    • Nucleic acid ligands based on carbohydrates
    • Hunziker, J. (1996). Nucleic acid ligands based on carbohydrates. Chimia 391, 468-471.
    • (1996) Chimia , vol.391 , pp. 468-471
    • Hunziker, J.1
  • 9
    • 0023239517 scopus 로고
    • Functional inactivation of genes by dominant negative mutations
    • Herskowitz, I. (1987). Functional inactivation of genes by dominant negative mutations. Nature 329, 219-222.
    • (1987) Nature , vol.329 , pp. 219-222
    • Herskowitz, I.1
  • 11
    • 0023280348 scopus 로고
    • Protein-binding sites in Ig gene enhancers determine transcriptional activity and inducibility
    • Lenardo, M., Pierce, J.W., & Baltimore, D. (1987). Protein-binding sites in Ig gene enhancers determine transcriptional activity and inducibility, Science 236, 1573-1577.
    • (1987) Science , vol.236 , pp. 1573-1577
    • Lenardo, M.1    Pierce, J.W.2    Baltimore, D.3
  • 12
    • 0030658039 scopus 로고    scopus 로고
    • Oncogenic transcription factors in human acute leukemias
    • Look, A.T. (1997). Oncogenic transcription factors in human acute leukemias. Science 278, 1059-1064.
    • (1997) Science , vol.278 , pp. 1059-1064
    • Look, A.T.1
  • 13
    • 0024554495 scopus 로고
    • A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins
    • Murre, C., McCaw, P.S., & Baltimore, D. (1989). A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins. Cell 56, 777-783.
    • (1989) Cell , vol.56 , pp. 777-783
    • Murre, C.1    McCaw, P.S.2    Baltimore, D.3
  • 14
    • 0028329080 scopus 로고
    • Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer
    • Ellenberger, T., Fass, D., Arnaud, M., & Harrison, S.C. (1994). Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer. Genes Dev. 8, 970-980.
    • (1994) Genes Dev. , vol.8 , pp. 970-980
    • Ellenberger, T.1    Fass, D.2    Arnaud, M.3    Harrison, S.C.4
  • 15
    • 0026538243 scopus 로고
    • Molecular characterization of helix-loop-helix peptides
    • Anthony-Cahill, S.J., et al., & DeGrado, W.F. (1992). Molecular characterization of helix-loop-helix peptides. Science 255, 979-983.
    • (1992) Science , vol.255 , pp. 979-983
    • Anthony-Cahill, S.J.1    DeGrado, W.F.2
  • 16
    • 0028307093 scopus 로고
    • Structure and function of helix-loop-helix proteins
    • Murre, C., et al., & Stuiver, M.H. (1994). Structure and function of helix-loop-helix proteins. Biochim. Biophys. Acta. 1218, 129-135.
    • (1994) Biochim. Biophys. Acta , vol.1218 , pp. 129-135
    • Murre, C.1    Stuiver, M.H.2
  • 17
    • 0025238437 scopus 로고
    • The protein Id: A negative regulator of helix-loop-helix DNA binding proteins
    • Benezra, R., Davis, R.L., Lokshon, D., Turner, D.L. & Weintraub, H. (1990). The protein Id: a negative regulator of helix-loop-helix DNA binding proteins. Cell 61, 49-59.
    • (1990) Cell , vol.61 , pp. 49-59
    • Benezra, R.1    Davis, R.L.2    Lokshon, D.3    Turner, D.L.4    Weintraub, H.5
  • 18
    • 0030754089 scopus 로고    scopus 로고
    • Differential Interactions of Id proteins with basic-helix -loop-helix transcription factors
    • Langlands, K., Yin, X., Anand, G. & Prochownik, E.V. (1997). Differential Interactions of Id proteins with basic-helix -loop-helix transcription factors. J. Biol. Chem. 272, 19785-19793.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19785-19793
    • Langlands, K.1    Yin, X.2    Anand, G.3    Prochownik, E.V.4
  • 19
    • 0029163156 scopus 로고
    • Synthesis of the basic-helix-loop-helix region of the immunoglobulin enhancer binding protein E47 and evaluation of its structural and DNA binding properties
    • Bishop, P., Jones, C., Ghosh, I. & Chmielewki, J. (1995). Synthesis of the basic-helix-loop-helix region of the immunoglobulin enhancer binding protein E47 and evaluation of its structural and DNA binding properties. Int. J. Pept. Protein Res., 46, 149-154.
    • (1995) Int. J. Pept. Protein Res. , vol.46 , pp. 149-154
    • Bishop, P.1    Jones, C.2    Ghosh, I.3    Chmielewki, J.4
  • 20
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N. & Fasman, G.D. (1969). Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8, 4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 21
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • Chou, P.Y., & Fasman, G.D. (1974). Prediction of protein conformation. Biochemistry 13, 222-245.
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 22
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins
    • Chou, P.Y., & Fasman, G.D. (1974). Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins. Biochemistry 13, 211-222.
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 23
    • 0028175780 scopus 로고
    • Thermodynamic scale for the beta-sheet forming tendencies of the amino-acids
    • Smith., C.K., Withka, J.M., & Regan, L.A. (1994). Thermodynamic scale for the beta-sheet forming tendencies of the amino-acids. Biochemistry 33, 5510-5517.
    • (1994) Biochemistry , vol.33 , pp. 5510-5517
    • Smith, C.K.1    Withka, J.M.2    Regan, L.A.3
  • 24
    • 0027998757 scopus 로고
    • Context is a major determinant of beta-sheet propensity
    • Minor, D.I., & Kim, P.S. (1994). Context is a major determinant of beta-sheet propensity. Nature 371, 264-267.
    • (1994) Nature , vol.371 , pp. 264-267
    • Minor, D.I.1    Kim, P.S.2
  • 25
    • 0030864812 scopus 로고    scopus 로고
    • Engineering peptides and proteins that undergo alpha-to-beta transitions
    • Mihara, H. & Takahashi, Y. (1997). Engineering peptides and proteins that undergo alpha-to-beta transitions. Curr. Opin. Struct. Biol. 7, 501-508.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 501-508
    • Mihara, H.1    Takahashi, Y.2
  • 26
    • 0031317466 scopus 로고    scopus 로고
    • Molecular and chemical basis of prion-related diseases
    • Ng, S. B. L., & Doig, A. J. (1997). Molecular and chemical basis of prion-related diseases. Chem. Soc. Rev. 26, 425-432.
    • (1997) Chem. Soc. Rev. , vol.26 , pp. 425-432
    • Ng, S.B.L.1    Doig, A.J.2
  • 27
    • 0027332116 scopus 로고
    • Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins
    • Pan, K.-M., et al., & Prusiner, S.B. (1993). Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc. Natl Acad. Sci. USA 90, 10962-10966.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 10962-10966
    • Pan, K.-M.1    Prusiner, S.B.2
  • 28
    • 0028925377 scopus 로고
    • Prion protein-peptides induce alpha-helix to beta-sheet Conformational transitions
    • Nguyen, J., Baldwin, M.A., Cohen, F.E., & Prusiner S.B. (1995). Prion protein-peptides induce alpha-helix to beta-sheet Conformational transitions. Biochemistry 34, 4186-4192.
    • (1995) Biochemistry , vol.34 , pp. 4186-4192
    • Nguyen, J.1    Baldwin, M.A.2    Cohen, F.E.3    Prusiner, S.B.4
  • 29
    • 0029865623 scopus 로고    scopus 로고
    • Context-dependent secondary structure formation of a designed protein sequence
    • Minor, D.L. & Kim, P.S. (1996). Context-dependent secondary structure formation of a designed protein sequence. Nature 380, 730-734.
    • (1996) Nature , vol.380 , pp. 730-734
    • Minor, D.L.1    Kim, P.S.2
  • 30
    • 0030986375 scopus 로고    scopus 로고
    • Protein alchemy: Changing beta-sheet into alpha-helix
    • Dalal, S., Balasubramanian, S. & Regan, L. (1997). Protein alchemy: Changing beta-sheet into alpha-helix. Nat. Struct. Biol. 4, 548-552.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 548-552
    • Dalal, S.1    Balasubramanian, S.2    Regan, L.3
  • 31
    • 45949123116 scopus 로고
    • Solid-phase synthesis of protected peptide fragments using a trialkoxydiphenyl-methylester resin
    • Rink, H., (1987). Solid-phase synthesis of protected peptide fragments using a trialkoxydiphenyl-methylester resin. Tetrahedron Lett. 28, 3787-3790.
    • (1987) Tetrahedron Lett. , vol.28 , pp. 3787-3790
    • Rink, H.1
  • 32
    • 0002186442 scopus 로고
    • (Gross, E. & Meienhofer, J. eds) Academic Press, New York
    • Atherton, E. & Sheppard, R.C. (1987). In The Peptides. (Gross, E. & Meienhofer, J. eds) Vol. 9, pp 1-38. Academic Press, New York.
    • (1987) The Peptides , vol.9 , pp. 1-38
    • Atherton, E.1    Sheppard, R.C.2
  • 33
    • 0028859980 scopus 로고
    • Basic-helix-loop-helix region of Tal: Evaluation of structure and DNA affinity
    • Bishop, P., Ghosh, I., Jones, C. & Chmielewski, J. (1995). Basic-helix-loop-helix region of Tal: evaluation of structure and DNA affinity. J. Am. Chem. Soc. 117, 8283-8284.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8283-8284
    • Bishop, P.1    Ghosh, I.2    Jones, C.3    Chmielewski, J.4
  • 34
    • 0030055692 scopus 로고    scopus 로고
    • Differential self assembly of amphiphilic helical peptides
    • Lutgring, R.A., Lipton, M. & Chmielewski, J. (1996). Differential self assembly of amphiphilic helical peptides. Amino Adds 10, 295-304.
    • (1996) Amino Adds , vol.10 , pp. 295-304
    • Lutgring, R.A.1    Lipton, M.2    Chmielewski, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.