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Volumn 16, Issue 3, 1998, Pages 262-266

Metal mediated sterol receptor-DNA complex association and dissociation determined by electrospray ionization mass spectrometry

Author keywords

Protein DNA interactions; Vitamin D receptor

Indexed keywords

DNA; DOUBLE STRANDED DNA; OSTEOPONTIN; VITAMIN D RECEPTOR; ZINC ION;

EID: 0031935288     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/nbt0398-262     Document Type: Article
Times cited : (51)

References (36)
  • 3
  • 4
    • 0030451142 scopus 로고    scopus 로고
    • Interaction of steroid hormone receptors with the transcription initiation complex
    • Beato, M. and Sanchez-Pacheco, A. 1996. Interaction of steroid hormone receptors with the transcription initiation complex. Endocr. Rev. 17:587-609.
    • (1996) Endocr. Rev. , vol.17 , pp. 587-609
    • Beato, M.1    Sanchez-Pacheco, A.2
  • 6
    • 0027498883 scopus 로고
    • On the mechanism of DNA binding by nuclear hormone receptors: A structural and functional perspective
    • Freedman, L.P. and Luisi, B.F. 1993. on the mechanism of DNA binding by nuclear hormone receptors: a structural and functional perspective. J. Cell. Biochem. 51:140-150.
    • (1993) J. Cell. Biochem. , vol.51 , pp. 140-150
    • Freedman, L.P.1    Luisi, B.F.2
  • 7
    • 0028927035 scopus 로고
    • The nuclear hormone receptor gene superfamily
    • Ribeiro, R.C., Kushner, P.J., and Baxter, J.D. 1995. The nuclear hormone receptor gene superfamily. Annu. Rev. Med. 46:443-453.
    • (1995) Annu. Rev. Med. , vol.46 , pp. 443-453
    • Ribeiro, R.C.1    Kushner, P.J.2    Baxter, J.D.3
  • 8
    • 0023769378 scopus 로고
    • The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain
    • Freedman, L.P., Luisi, B.F., Korszun, Z.R., Basavappa, R., Sigler, P.B., and Yamamoto, K.R. 1988. The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain. Nature 334:543-546.
    • (1988) Nature , vol.334 , pp. 543-546
    • Freedman, L.P.1    Luisi, B.F.2    Korszun, Z.R.3    Basavappa, R.4    Sigler, P.B.5    Yamamoto, K.R.6
  • 9
    • 0029099609 scopus 로고
    • 3. Interplay with retinoid and thyroid hormone signaling
    • 3. Interplay with retinoid and thyroid hormone signaling. Eur. J. Biochem. 231:517-527.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 517-527
    • Carlberg, C.1
  • 10
    • 0025923045 scopus 로고
    • 3 receptors: Structure and function in transcription
    • 3 receptors: structure and function in transcription. Annu. Rev. Nutr. 11:189-216.
    • (1991) Annu. Rev. Nutr. , vol.11 , pp. 189-216
    • Pike, J.W.1
  • 16
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn, J.B., Mann, M., Meng, C.K., Wong, S.F., and Whitehouse, C.M. 1990. Electrospray ionization for mass spectrometry of large biomolecules. Science 246:64-71.
    • (1990) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 17
    • 33846278908 scopus 로고    scopus 로고
    • New mass spectrometric methods for the study of noncovalent associations of biopolymers
    • Smith, R.D., Bruce, J.E., Wu, Q.Y., and Lei, Q.P. 1997. New mass spectrometric methods for the study of noncovalent associations of biopolymers. Chemical Society Reviews 26:191-202.
    • (1997) Chemical Society Reviews , vol.26 , pp. 191-202
    • Smith, R.D.1    Bruce, J.E.2    Wu, Q.Y.3    Lei, Q.P.4
  • 19
    • 0029946594 scopus 로고    scopus 로고
    • Direct measurement of oligonucleotide binding stoichiometry of gene v protein by mass spectrometry
    • Cheng, X., Harms, A.C., Goudreau, P.N., Terwilliger, T.C., and Smith, R.D. 1996. Direct measurement of oligonucleotide binding stoichiometry of gene V protein by mass spectrometry. Proc. Natl. Acad. Sci. USA 93:7022-7027.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7022-7027
    • Cheng, X.1    Harms, A.C.2    Goudreau, P.N.3    Terwilliger, T.C.4    Smith, R.D.5
  • 20
    • 0030621966 scopus 로고    scopus 로고
    • Studying noncovalent protein complexes by electrospray ionization mass spectrometry
    • Loo, J.A. 1997. Studying noncovalent protein complexes by electrospray ionization mass spectrometry. Mass Spectrometry Review 16:1-23.
    • (1997) Mass Spectrometry Review , vol.16 , pp. 1-23
    • Loo, J.A.1
  • 21
    • 0031213609 scopus 로고    scopus 로고
    • Investigation of calcium-induced, noncovalent association of calmodulin with mellitin by electrospray ionization mass spectrometry
    • Nemirovskiy, O.V., Ramanathan, R., and Gross, M.L. 1997. Investigation of calcium-induced, noncovalent association of calmodulin with mellitin by electrospray ionization mass spectrometry. Journal of the American Society of Mass Spectrometry 8:809-812.
    • (1997) Journal of the American Society of Mass Spectrometry , vol.8 , pp. 809-812
    • Nemirovskiy, O.V.1    Ramanathan, R.2    Gross, M.L.3
  • 23
    • 0031019986 scopus 로고    scopus 로고
    • Study of non-covalent enzyme-inhibitor complexes of aldose reductase by electrospray mass spectrometry
    • Potier, N., Barth, P., Tritsch, D., Biellmann, J.F., and Vandorsselaer, A. 1997. Study of non-covalent enzyme-inhibitor complexes of aldose reductase by electrospray mass spectrometry. Eur. J. Biochem. 243:274-282.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 274-282
    • Potier, N.1    Barth, P.2    Tritsch, D.3    Biellmann, J.F.4    Vandorsselaer, A.5
  • 24
    • 0029665001 scopus 로고    scopus 로고
    • 3. A ternary complex of the integrin α and β subunits and a divalent cation
    • 3. A ternary complex of the integrin α and β subunits and a divalent cation. J. Biol. Chem. 271:6017-6026.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6017-6026
    • Haas, T.A.1    Plow, E.F.2
  • 27
    • 0346917123 scopus 로고    scopus 로고
    • Mass spectrometric characterization of sequence-specific complexes of DNA and transcription factor PU.1 DNA binding domain
    • Cheng, X., Morin, P.E., Harms, A.C., Bruce, J.E., Ben-David, Y., and Smith, R.D. 1996. Mass spectrometric characterization of sequence-specific complexes of DNA and transcription factor PU.1 DNA binding domain. Anal. Biochem. 239:35-40.
    • (1996) Anal. Biochem. , vol.239 , pp. 35-40
    • Cheng, X.1    Morin, P.E.2    Harms, A.C.3    Bruce, J.E.4    Ben-David, Y.5    Smith, R.D.6
  • 28
    • 0029561623 scopus 로고
    • Metal replacement in DNA-binding zinc finger proteins and its relevance to mutagenicity and carcinogenicity through free radical generation
    • Sarkar, B. 1995. Metal replacement in DNA-binding zinc finger proteins and its relevance to mutagenicity and carcinogenicity through free radical generation. Nutrition 11:646-649.
    • (1995) Nutrition , vol.11 , pp. 646-649
    • Sarkar, B.1
  • 29
    • 0029919744 scopus 로고    scopus 로고
    • Inhibition of transcription factor IIIA-DNA interactions by xenobiotic metal ions
    • Hanas, J.S. and Gunn, C.G. 1996. Inhibition of transcription factor IIIA-DNA interactions by xenobiotic metal ions. Nucl. Acids Res. 24:924-930.
    • (1996) Nucl. Acids Res. , vol.24 , pp. 924-930
    • Hanas, J.S.1    Gunn, C.G.2
  • 30
    • 0025777670 scopus 로고
    • Transition metals modulate DNA-protein interactions of SP1 zinc finger domains with its cognate target site
    • Thiesen, H.J. and Bach, C. 1991. Transition metals modulate DNA-protein interactions of SP1 zinc finger domains with its cognate target site. Biochem. Biophys. Res. Commun. 176:551-557.
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 551-557
    • Thiesen, H.J.1    Bach, C.2
  • 31
    • 0029866646 scopus 로고    scopus 로고
    • The galvanization of biology: A growing appreciation for the roles of zinc
    • Berg, J.M. and Shi, Y. 1996. The galvanization of biology: a growing appreciation for the roles of zinc. Science 271:1081-1085.
    • (1996) Science , vol.271 , pp. 1081-1085
    • Berg, J.M.1    Shi, Y.2
  • 32
    • 0027269523 scopus 로고
    • Vitamin D-sensitive and quinacrine-sensitive zinc transport in human intestinal cell line Caco-2
    • Fleet, J.C., Turnbull, A.J., Bourcier, M., and Wood, R. J. 1993. Vitamin D-sensitive and quinacrine-sensitive zinc transport in human intestinal cell line Caco-2. Am. J. Physiol. 264:G1037-G1045.
    • (1993) Am. J. Physiol. , vol.264
    • Fleet, J.C.1    Turnbull, A.J.2    Bourcier, M.3    Wood, R.J.4
  • 33
    • 0029971595 scopus 로고    scopus 로고
    • Zinc transport in mammalian cells
    • Reyes, J.G. 1996. Zinc transport in mammalian cells. Am. J. Physiol. 270:C401-C410.
    • (1996) Am. J. Physiol. , vol.270
    • Reyes, J.G.1
  • 35
    • 0016196046 scopus 로고
    • Active transport of zinc and identification of zinc-binding protein in rat jejunal mucosa
    • Kowarski, S., Blair-Stanek, C.S., and Schachter, D. 1974. Active transport of zinc and identification of zinc-binding protein in rat jejunal mucosa. Am. J. Physiol. 226:401-407.
    • (1974) Am. J. Physiol. , vol.226 , pp. 401-407
    • Kowarski, S.1    Blair-Stanek, C.S.2    Schachter, D.3
  • 36
    • 0030942598 scopus 로고    scopus 로고
    • Determination of non-covalent metal ion/protein interactions using a microflow electrospray ionization mass spectrometry interface
    • Johnson, K.L., Veenstra, T.D., Tomlinson, A.J., Kumar, R., and Naylor, S. 1997. Determination of non-covalent metal ion/protein interactions using a microflow electrospray ionization mass spectrometry interface. Rapid Commun. Mass Spectrom. 11:939-942.
    • (1997) Rapid Commun. Mass Spectrom. , vol.11 , pp. 939-942
    • Johnson, K.L.1    Veenstra, T.D.2    Tomlinson, A.J.3    Kumar, R.4    Naylor, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.