메뉴 건너뛰기




Volumn , Issue , 2005, Pages 277-296

Roles for biotinylation of histones in chromatin structure

Author keywords

[No Author keywords available]

Indexed keywords


EID: 28844454813     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (1)

References (45)
  • 1
    • 0004050816 scopus 로고    scopus 로고
    • 3rd ed. San Diego, CA: Academic Press
    • A Wolffe. Chromatin. 3rd ed. San Diego, CA: Academic Press, 1998.
    • (1998) Chromatin
    • Wolffe, A.1
  • 2
    • 0022551060 scopus 로고
    • Histone hyperacetylation: Its effect on nucleosome conformation and stability
    • J Ausio, KE van Holde. Histone hyperacetylation: its effect on nucleosome conformation and stability. Biochemistry 25: 1421-1428, 1986.
    • (1986) Biochemistry , vol.25 , pp. 1421-1428
    • Ausio, J.1    Van Holde, K.E.2
  • 3
    • 0024003456 scopus 로고
    • A direct link between core histone acetylation and transcriptionally active chromatin
    • TR Hebbes, AW Thorne, C Crane-Robinson. A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J 7: 1395-1402, 1988.
    • (1988) EMBO J , vol.7 , pp. 1395-1402
    • Hebbes, T.R.1    Thorne, A.W.2    Crane-Robinson, C.3
  • 4
    • 0027465862 scopus 로고
    • A positive role for histone acetylation in transcription factor access to nuceloso-mal DNA
    • DY Lee, JJ Hayes, D Pruss, AP Wolffe. A positive role for histone acetylation in transcription factor access to nuceloso-mal DNA. Cell 72: 73-84, 1993.
    • (1993) Cell , vol.72 , pp. 73-84
    • Lee, D.Y.1    Hayes, J.J.2    Pruss, D.3    Wolffe, A.P.4
  • 6
    • 0023804599 scopus 로고
    • At least 60 ADP-ribosylated variant histones are present in nuclei from dimethylsulfate-treated and untreated cells
    • T Boulikas. At least 60 ADP-ribosylated variant histones are present in nuclei from dimethylsulfate-treated and untreated cells. EMBO J 7: 57-67, 1988.
    • (1988) EMBO J , vol.7 , pp. 57-67
    • Boulikas, T.1
  • 7
    • 0025136795 scopus 로고
    • Increase in histone poly(ADP-ribosylation) in mitogen-activated lymphoid cells
    • T Boulikas, B Bastin, P Boulikas, G Dupuis. Increase in histone poly(ADP-ribosylation) in mitogen-activated lymphoid cells. Exp Cell Res 187: 77-84, 1990.
    • (1990) Exp Cell Res , vol.187 , pp. 77-84
    • Boulikas, T.1    Bastin, B.2    Boulikas, P.3    Dupuis, G.4
  • 8
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • BD Strahl, CD Allis. The language of covalent histone modifications. Nature 403: 41-45, 2000.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 9
    • 0033848849 scopus 로고    scopus 로고
    • Histone acetylation and epigenetic code
    • BM Turner. Histone acetylation and epigenetic code. Bioessays 22: 836-845, 2000.
    • (2000) Bioessays , vol.22 , pp. 836-845
    • Turner, B.M.1
  • 10
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • T Jenuwein, CD Allis. Translating the histone code. Science 293: 1074-1080, 2001.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 11
    • 0034644473 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications
    • P Cheung, CD Allis, P Sassone-Corsi. Signaling to chromatin through histone modifications. Cell 103: 263-271, 2000.
    • (2000) Cell , vol.103 , pp. 263-271
    • Cheung, P.1    Allis, C.D.2    Sassone-Corsi, P.3
  • 13
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • JE Brownell, J Zhou, T Ranalli, R Kobayashi, DG Edmondson, SY Roth, CD Allis. Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 84: 843-851, 1996.
    • (1996) Cell , vol.84 , pp. 843-851
    • Brownell, J.E.1    Zhou, J.2    Ranalli, T.3    Kobayashi, R.4    Edmondson, D.G.5    Roth, S.Y.6    Allis, C.D.7
  • 14
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to a yeast transcriptional regulator Rpd3
    • J Taunton, CA Hassig, SL Schreiber. A mammalian histone deacetylase related to a yeast transcriptional regulator Rpd3. Science 272: 408-411, 1996.
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 15
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • V Allfrey, RM Faulkner, AE Mirsky. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc Soc Natl Acad Sci USA 51: 786-794, 1964.
    • (1964) Proc Soc Natl Acad Sci USA , vol.51 , pp. 786-794
    • Allfrey, V.1    Faulkner, R.M.2    Mirsky, A.E.3
  • 16
    • 0015576001 scopus 로고
    • Macro- and micronuclei of Tetrahymena pyri-formis: A model system for studying the structure of eukaryotic nuclei
    • MA Gorovsky. Macro- and micronuclei of Tetrahymena pyri-formis: a model system for studying the structure of eukaryotic nuclei. J Protozool 20: 19-25, 1973.
    • (1973) J Protozool , vol.20 , pp. 19-25
    • Gorovsky, M.A.1
  • 17
    • 0018116191 scopus 로고
    • Effect of histone acetylation on structure and in vitro transcription of chromatin
    • DJ Mathis, P Oudet, B Waslyk, P Chambon. Effect of histone acetylation on structure and in vitro transcription of chromatin. Nucleic Acids Res 5: 3523-3547, 1978.
    • (1978) Nucleic Acids Res , vol.5 , pp. 3523-3547
    • Mathis, D.J.1    Oudet, P.2    Waslyk, B.3    Chambon, P.4
  • 18
    • 0034730745 scopus 로고    scopus 로고
    • Ubiquitin-activating/conjugating activity of TAFn250, a mediator of activation of gene expression in Drosophila
    • n250, a mediator of activation of gene expression in Drosophila. Science 289: 2357-2360, 2000.
    • (2000) Science , vol.289 , pp. 2357-2360
    • Pham, A.-D.1    Sauer, F.2
  • 20
    • 0026776003 scopus 로고
    • Poly ADP-ribosylation: A histone shuttle mechanism in DNA excision repair
    • F Althaus. Poly ADP-ribosylation: a histone shuttle mechanism in DNA excision repair. J Cell Sci 102: 663-670, 1992.
    • (1992) J Cell Sci , vol.102 , pp. 663-670
    • Althaus, F.1
  • 21
    • 0009577682 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation of histone H1 correlates with internu-cleosomal DNA fragmentation during apoptosis
    • YS Yoon, JW Kim, KW Kang, YS Kim, KH Choi, CO Joe. Poly(ADP-ribosyl)ation of histone H1 correlates with internu-cleosomal DNA fragmentation during apoptosis. J Biol Chem 271: 9129-9134, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 9129-9134
    • Yoon, Y.S.1    Kim, J.W.2    Kang, K.W.3    Kim, Y.S.4    Choi, K.H.5    Joe, C.O.6
  • 22
    • 0018723423 scopus 로고
    • Poly(ADP-ribose) levels in carcinogen-treated cells
    • H Juarez-Salinas, JL Sims, MK Jacobson. Poly(ADP-ribose) levels in carcinogen-treated cells. Nature 282: 740-741, 1979.
    • (1979) Nature , vol.282 , pp. 740-741
    • Juarez-Salinas, H.1    Sims, J.L.2    Jacobson, M.K.3
  • 23
    • 2642517472 scopus 로고
    • Adenosine diphosphoribo-syltransferase in chromatin
    • DB McCormick, LD Wright, Eds., New York: Academic Press
    • Y Nishizuka, K Ueda, O Hayaishi. Adenosine diphosphoribo-syltransferase in chromatin. In: DB McCormick, LD Wright, Eds. Vitamins and Coenzymes. New York: Academic Press, 1971, pp 230-233.
    • (1971) Vitamins and Coenzymes , pp. 230-233
    • Nishizuka, Y.1    Ueda, K.2    Hayaishi, O.3
  • 24
    • 0028146934 scopus 로고
    • Dietary niacin deficiency lowers tissue poly(ADP-ribose) and NAD+ concentrations in Fischer-344 rats
    • JM Rawling, TM Jackson, ER Driscoll, JB Kirkland. Dietary niacin deficiency lowers tissue poly(ADP-ribose) and NAD+ concentrations in Fischer-344 rats. J Nutr 124: 1597-1603, 1994.
    • (1994) J Nutr , vol.124 , pp. 1597-1603
    • Rawling, J.M.1    Jackson, T.M.2    Driscoll, E.R.3    Kirkland, J.B.4
  • 26
    • 0029123092 scopus 로고
    • Histone H4 and the maintenance of genome integrity
    • PC Megee, BA Morgan, MM Smith. Histone H4 and the maintenance of genome integrity. Genes Dev 9: 1716-1727, 1995.
    • (1995) Genes Dev , vol.9 , pp. 1716-1727
    • Megee, P.C.1    Morgan, B.A.2    Smith, M.M.3
  • 27
    • 0028858269 scopus 로고
    • Biotinylation of histones by human serum biotinidase: Assessment of biotinyl-transferase activity in sera from normal individuals and children with biotinidase deficiency
    • J Hymes, K Fleischhauer, B Wolf. Biotinylation of histones by human serum biotinidase: assessment of biotinyl-transferase activity in sera from normal individuals and children with biotinidase deficiency. Biochem Mol Med 56: 76-83, 1995.
    • (1995) Biochem Mol Med , vol.56 , pp. 76-83
    • Hymes, J.1    Fleischhauer, K.2    Wolf, B.3
  • 28
    • 0032906144 scopus 로고    scopus 로고
    • Human biotinidase isn’t just for recycling biotin
    • J Hymes, B Wolf. Human biotinidase isn’t just for recycling biotin. J Nutr 129: 485S-489S, 1999.
    • (1999) J Nutr , vol.129 , pp. 485S-489S
    • Hymes, J.1    Wolf, B.2
  • 30
    • 0025987716 scopus 로고
    • Biotinidase deficiency
    • L Barness, F Oski, Eds., Chicago, IL: Medical Book Publishers
    • B Wolf, GS Heard. Biotinidase deficiency. In: L Barness, F Oski, Eds. Advances in Pediatrics. Chicago, IL: Medical Book Publishers, 1991, pp 1-21.
    • (1991) Advances in Pediatrics , pp. 1-21
    • Wolf, B.1    Heard, G.S.2
  • 31
    • 0036909261 scopus 로고    scopus 로고
    • Catalysis in the nitrilase superfamily
    • C Brenner. Catalysis in the nitrilase superfamily. Curr Opin Struct Biol 12: 775-782, 2002.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 775-782
    • Brenner, C.1
  • 32
    • 0032716106 scopus 로고    scopus 로고
    • Is pantetheinase the actual identity of mouse and human vanin-1 proteins
    • B Maras, D Barra, S Dupre, G Pitari. Is pantetheinase the actual identity of mouse and human vanin-1 proteins. FEBS Lett 461: 149-152, 1999.
    • (1999) FEBS Lett , vol.461 , pp. 149-152
    • Maras, B.1    Barra, D.2    Dupre, S.3    Pitari, G.4
  • 35
    • 0035542958 scopus 로고    scopus 로고
    • Conservation of biotinidase in mammals and identification of the putative biotinidase gene in
    • KL Swango, B Wolf. Conservation of biotinidase in mammals and identification of the putative biotinidase gene in Drosophila melanogaster. Mol Genet Metabol 74: 492-499, 2001.
    • (2001) Drosophila Melanogaster. Mol Genet Metabol , vol.74 , pp. 492-499
    • Swango, K.L.1    Wolf, B.2
  • 36
    • 0034797338 scopus 로고    scopus 로고
    • Biotinylation of histones in human cells: Effects of cell proliferation
    • JS Stanley, JB Griffin, J Zempleni. Biotinylation of histones in human cells: effects of cell proliferation. Eur J Biochem 268: 5424-5429, 2001.
    • (2001) Eur J Biochem , vol.268 , pp. 5424-5429
    • Stanley, J.S.1    Griffin, J.B.2    Zempleni, J.3
  • 37
    • 0033230283 scopus 로고    scopus 로고
    • Chemical synthesis of biotinylated histones and analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis/streptavidin-peroxidase
    • J Zempleni, DM Mock. Chemical synthesis of biotinylated histones and analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis/streptavidin-peroxidase. Arch Bio-chem Biophys 371: 83-88, 1999.
    • (1999) Arch Bio-Chem Biophys , vol.371 , pp. 83-88
    • Zempleni, J.1    Mock, D.M.2
  • 38
    • 0036246474 scopus 로고    scopus 로고
    • Biotin supply affects expression of biotin transporters, biotinylation of carboxylases, and metabolism of interleukin-2 in Jurkat cells
    • KC Manthey, JB Griffin, J Zempleni. Biotin supply affects expression of biotin transporters, biotinylation of carboxylases, and metabolism of interleukin-2 in Jurkat cells. J Nutr 132: 887-892, 2002.
    • (2002) J Nutr , vol.132 , pp. 887-892
    • Manthey, K.C.1    Griffin, J.B.2    Zempleni, J.3
  • 39
    • 0242567146 scopus 로고    scopus 로고
    • Expression of oncogenes depends on biotin in human small cell lung cancer cells NCI-H69
    • SB Scheerger, J Zempleni. Expression of oncogenes depends on biotin in human small cell lung cancer cells NCI-H69. Int J Vitam Nutr Res 73: 461-467, 2003.
    • (2003) Int J Vitam Nutr Res , vol.73 , pp. 461-467
    • Scheerger, S.B.1    Zempleni, J.2
  • 40
    • 1242353050 scopus 로고    scopus 로고
    • Biotin supply affects rates of cell proliferation, biotinylation of carboxylases and histones, and expression of the gene encoding the sodium-dependent multivitamin transporter in JAr choriocarcinoma cells
    • SERH Crisp, G Camporeale, BR White, CF Toombs, JB Griffin, HM Said, J Zempleni. Biotin supply affects rates of cell proliferation, biotinylation of carboxylases and histones, and expression of the gene encoding the sodium-dependent multivitamin transporter in JAr choriocarcinoma cells. Eur J Nutr 43: 23-31, 2004.
    • (2004) Eur J Nutr , vol.43 , pp. 23-31
    • Crisp, S.1    Camporeale, G.2    White, B.R.3    Toombs, C.F.4    Griffin, J.B.5    Said, H.M.6    Zempleni, J.7
  • 43
    • 0028796669 scopus 로고
    • Biotinylation of biotinidase following incubation with biocytin
    • J Hymes, K Fleischhauer, B Wolf. Biotinylation of biotinidase following incubation with biocytin. Clin Chim Acta 233: 39-45, 1995.
    • (1995) Clin Chim Acta , vol.233 , pp. 39-45
    • Hymes, J.1    Fleischhauer, K.2    Wolf, B.3
  • 45
    • 0002623801 scopus 로고    scopus 로고
    • Biotin
    • BA Bowman, RM Russell, Eds., 8th ed. Washington, D.C.: ILSI Press
    • J Zempleni. Biotin. In: BA Bowman, RM Russell, Eds. Present Knowledge in Nutrition. 8th ed. Washington, D.C.: ILSI Press, 2001, pp 241-252.
    • (2001) Present Knowledge in Nutrition , pp. 241-252
    • Zempleni, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.