메뉴 건너뛰기




Volumn 35, Issue 8, 2007, Pages 2573-2583

Concentration-dependent organization of DNA by the dinoflagellate histone-like protein HCc3

Author keywords

[No Author keywords available]

Indexed keywords

CELLULOSE; CONCATENATED DNA; HISTONE; HISTONE HCC3; POLYCATION; PROTOZOAL DNA; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; DNA; DNA BINDING PROTEIN; HISTONE LIKE PROTEIN HU, BACTERIA; HISTONE-LIKE PROTEIN HU, BACTERIA; PROTOZOAL PROTEIN;

EID: 34250364937     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkm165     Document Type: Article
Times cited : (45)

References (84)
  • 1
    • 0026685334 scopus 로고
    • Chromatins of low-protein content: Special features of their compaction and condensation
    • Kellenberger,E. and Arnold-Schulz-Gahmen,B. (1992) Chromatins of low-protein content: Special features of their compaction and condensation. FEMS Microbiol. Lett., 79, 361-370.
    • (1992) FEMS Microbiol. Lett , vol.79 , pp. 361-370
    • Kellenberger, E.1    Arnold-Schulz-Gahmen, B.2
  • 3
    • 0020135119 scopus 로고
    • Isolation and properties of isolated nuclei from the florida red tide dinoflagellate Gymnodinium breve (davis)
    • Rizzo,P.J., Jones,M. and Ray,S.M. (1982) Isolation and properties of isolated nuclei from the florida red tide dinoflagellate Gymnodinium breve (davis). J. Protozool., 29, 217-222.
    • (1982) J. Protozool , vol.29 , pp. 217-222
    • Rizzo, P.J.1    Jones, M.2    Ray, S.M.3
  • 5
    • 0025273643 scopus 로고
    • Basic nuclear proteins of the histone-less eukaryote Crypthecodinium cohnii (pyrrhophyta): Two-dimensional electrophoresis and DNA-binding properties
    • Vernet,G., Sala-Rovira,M., Maeder,M., Jacques,F. and Herzog,M. (1990) Basic nuclear proteins of the histone-less eukaryote Crypthecodinium cohnii (pyrrhophyta): Two-dimensional electrophoresis and DNA-binding properties. Biochim. Biophys. Acta, 1048, 281-289.
    • (1990) Biochim. Biophys. Acta , vol.1048 , pp. 281-289
    • Vernet, G.1    Sala-Rovira, M.2    Maeder, M.3    Jacques, F.4    Herzog, M.5
  • 6
    • 34447505477 scopus 로고
    • Etude au microscope electronique des plasmas contenant de l'acide deoxyribonucleique III. Variations ultra-structurales des chromosomes d'amphidinium
    • de Haller,G. and Kelienberger,E. (1964) Etude au microscope electronique des plasmas contenant de l'acide deoxyribonucleique III. Variations ultra-structurales des chromosomes d'amphidinium. J. Microsc., 3, 627-642.
    • (1964) J. Microsc , vol.3 , pp. 627-642
    • de Haller, G.1    Kelienberger, E.2
  • 7
    • 0001857067 scopus 로고
    • The chromosomes of dinoflagellates
    • Dodge,J.D. (1985) The chromosomes of dinoflagellates. Int. Rev. Cytol., 94, 5-20.
    • (1985) Int. Rev. Cytol , vol.94 , pp. 5-20
    • Dodge, J.D.1
  • 8
    • 84913281846 scopus 로고
    • Organization of the genetic material of phage, bacteria and dinoflagellates
    • Today, G, Ed, Pergamon Press, Oxford, The Hague, pp
    • Kellenberger,E. (1964) Organization of the genetic material of phage, bacteria and dinoflagellates. In: Today, G. (Ed.). Proceedings of the Eleventh International Congress of Genetics. Pergamon Press, Oxford, The Hague, pp. 309-321.
    • (1964) Proceedings of the Eleventh International Congress of Genetics , pp. 309-321
    • Kellenberger, E.1
  • 9
    • 0002568212 scopus 로고
    • Electron microscopy of the chromosomes of dinoflagellates in situ: Confirmation of Bouligand's liquid crystal hypothesis
    • Gautier,A., Michel-Salamin,L., Tosi-Couture,E., McDowall,A.W. and Dubochet,J. (1986) Electron microscopy of the chromosomes of dinoflagellates in situ: Confirmation of Bouligand's liquid crystal hypothesis. J. Ultrastruct. Mol. Struct. Res., 97, 10-30.
    • (1986) J. Ultrastruct. Mol. Struct. Res , vol.97 , pp. 10-30
    • Gautier, A.1    Michel-Salamin, L.2    Tosi-Couture, E.3    McDowall, A.W.4    Dubochet, J.5
  • 10
    • 0014378879 scopus 로고
    • The fibrillary structure and orientation of chromosomes in dinoflagellata
    • Bouligand,Y., Soyer,M.O. and Puiseux-Dao,S. (1968) The fibrillary structure and orientation of chromosomes in dinoflagellata. Chromosoma, 24, 251-287.
    • (1968) Chromosoma , vol.24 , pp. 251-287
    • Bouligand, Y.1    Soyer, M.O.2    Puiseux-Dao, S.3
  • 11
    • 0024744558 scopus 로고
    • Electron microscopy of liquid crystalline DNA: Direct evidence for cholesteric-like organization of DNA in dinoflagellate chromosomes
    • Rill,R.L., Livolant,F., Aldrich,H.C. and Davidson,M.W. (1989) Electron microscopy of liquid crystalline DNA: Direct evidence for cholesteric-like organization of DNA in dinoflagellate chromosomes. Chromosoma, 98, 280-286.
    • (1989) Chromosoma , vol.98 , pp. 280-286
    • Rill, R.L.1    Livolant, F.2    Aldrich, H.C.3    Davidson, M.W.4
  • 12
    • 23044512569 scopus 로고    scopus 로고
    • Proliferation of dinoflagellates: Blooming or bleaching
    • Wong,J.T. and Kwok,A.C. (2005) Proliferation of dinoflagellates: blooming or bleaching. Bioessays, 27, 730-740.
    • (2005) Bioessays , vol.27 , pp. 730-740
    • Wong, J.T.1    Kwok, A.C.2
  • 13
    • 0030395810 scopus 로고    scopus 로고
    • Condensed phases of DNA: Structures and phase transitions
    • Livolant,F. and Leforestier,A. (1996) Condensed phases of DNA: structures and phase transitions. Prog. Polym. Sci., 21, 1115-1164.
    • (1996) Prog. Polym. Sci , vol.21 , pp. 1115-1164
    • Livolant, F.1    Leforestier, A.2
  • 14
    • 0038143248 scopus 로고    scopus 로고
    • Histone-like proteins of the dinoflagellate Crypthecodinium cohnii have homologies to bacterial DNA-binding proteins
    • Wong,J.T., New,D.C., Wong,J.C. and Hung,V.K. (2003) Histone-like proteins of the dinoflagellate Crypthecodinium cohnii have homologies to bacterial DNA-binding proteins. Eukaryot. Cell, 2 646-650.
    • (2003) Eukaryot. Cell , vol.2 , pp. 646-650
    • Wong, J.T.1    New, D.C.2    Wong, J.C.3    Hung, V.K.4
  • 15
    • 0025837745 scopus 로고
    • Molecular cloning and immunolocalization of two variants of the major basic nuclear protein (HCC) from the histone-less eukaryote Crypthecodinium cohnii (pyrrhophyta)
    • Sala-Rovira,M., Geraud,M.L., Caput,D., Jacques,F., Soyer-Gobillard,M.O., Vernet,G. and Herzog,M. (1991) Molecular cloning and immunolocalization of two variants of the major basic nuclear protein (HCC) from the histone-less eukaryote Crypthecodinium cohnii (pyrrhophyta). Chromosoma, 100, 510-518.
    • (1991) Chromosoma , vol.100 , pp. 510-518
    • Sala-Rovira, M.1    Geraud, M.L.2    Caput, D.3    Jacques, F.4    Soyer-Gobillard, M.O.5    Vernet, G.6    Herzog, M.7
  • 16
    • 33747295520 scopus 로고    scopus 로고
    • Alveolata histone-like proteins have different evolutionary origins
    • Chan,Y.H., Kwok,A.C., Tsang,J.S. and Wong,J.T.Y. (2006) Alveolata histone-like proteins have different evolutionary origins. J. Evolution. Biol., 19, 1717-1721.
    • (2006) J. Evolution. Biol , vol.19 , pp. 1717-1721
    • Chan, Y.H.1    Kwok, A.C.2    Tsang, J.S.3    Wong, J.T.Y.4
  • 17
    • 0023041804 scopus 로고
    • Interaction of the Escherichia coli HU protein with DNA. Evidence for formation of nucleosome-like structures with altered DNA helical pitch
    • Broyles,S.S. and Pettijohn,D.E. (1986) Interaction of the Escherichia coli HU protein with DNA. Evidence for formation of nucleosome-like structures with altered DNA helical pitch. J. Mol. Biol., 187 47-60.
    • (1986) J. Mol. Biol , vol.187 , pp. 47-60
    • Broyles, S.S.1    Pettijohn, D.E.2
  • 18
    • 0018405881 scopus 로고    scopus 로고
    • Rouviere-Yaniv,J., Yaniv,M. and Germond,J.E. (1979) E. coli DNA binding protein HU forms nucleosomelike structure with circular double-stranded DNA. Cell, 17, 265-274.
    • Rouviere-Yaniv,J., Yaniv,M. and Germond,J.E. (1979) E. coli DNA binding protein HU forms nucleosomelike structure with circular double-stranded DNA. Cell, 17, 265-274.
  • 20
    • 0021346918 scopus 로고
    • Protein HU in the enzymatic replication of the chromosomal origin of Escherichia coli
    • Dixon,N.E. and Kornberg,A. (1984) Protein HU in the enzymatic replication of the chromosomal origin of Escherichia coli. Proc. Natl. Acad. Sci. USA, 81, 424-428.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 424-428
    • Dixon, N.E.1    Kornberg, A.2
  • 21
    • 0022545522 scopus 로고
    • Host protein requirements for in vitro site-specific DNA inversion
    • Johnson,R.C., Bruist,M.F. and Simon,M.I. (1986) Host protein requirements for in vitro site-specific DNA inversion. Cell, 46 531-539.
    • (1986) Cell , vol.46 , pp. 531-539
    • Johnson, R.C.1    Bruist, M.F.2    Simon, M.I.3
  • 22
    • 0028302290 scopus 로고
    • A second high affinity HU binding site in the phage Mu transpososome
    • Lavoie,B.D. and Chaconas,G. (1994) A second high affinity HU binding site in the phage Mu transpososome. J. Biol. Chem., 269, 15571-15576.
    • (1994) J. Biol. Chem , vol.269 , pp. 15571-15576
    • Lavoie, B.D.1    Chaconas, G.2
  • 23
    • 0023724433 scopus 로고
    • DNA dynamic flexibility and protein recognition: Differential stimulation by bacterial histone-like protein HU
    • Flashner,Y. and Gralla,J.D. (1988) DNA dynamic flexibility and protein recognition: Differential stimulation by bacterial histone-like protein HU. Cell, 54, 713-721.
    • (1988) Cell , vol.54 , pp. 713-721
    • Flashner, Y.1    Gralla, J.D.2
  • 25
    • 0023413620 scopus 로고
    • Histone-like proteins of bacteria
    • Drlica,K. and Rouviere-Yaniv,J. (1987) Histone-like proteins of bacteria. Microbiol. Rev., 51, 301-319.
    • (1987) Microbiol. Rev , vol.51 , pp. 301-319
    • Drlica, K.1    Rouviere-Yaniv, J.2
  • 26
    • 0028670214 scopus 로고
    • 1H, 13C, and 15N resonance assignments and secondary structure analysis of the HU protein from Bacillus stearothermophilus using two- and three-dimensional double- and triple-resonance heteronuclear magnetic resonance spectroscopy
    • Vis,H., Boelens,R., Mariani,M., Stroop,R., Vorgias,C.E., Wilson,K.S. and Kaptein,R. (1994) 1H, 13C, and 15N resonance assignments and secondary structure analysis of the HU protein from Bacillus stearothermophilus using two- and three-dimensional double- and triple-resonance heteronuclear magnetic resonance spectroscopy. Biochemistry, 33 14858-14870.
    • (1994) Biochemistry , vol.33 , pp. 14858-14870
    • Vis, H.1    Boelens, R.2    Mariani, M.3    Stroop, R.4    Vorgias, C.E.5    Wilson, K.S.6    Kaptein, R.7
  • 27
    • 0033119773 scopus 로고    scopus 로고
    • The high-resolution structure of DNA-binding protein HU from Bacillus stearothermophilus
    • White,S.W., Wilson,K.S., Appelt,K. and Tanaka,I. (1999) The high-resolution structure of DNA-binding protein HU from Bacillus stearothermophilus. Acta Cryst., D55, 801-809.
    • (1999) Acta Cryst , vol.D55 , pp. 801-809
    • White, S.W.1    Wilson, K.S.2    Appelt, K.3    Tanaka, I.4
  • 28
    • 0025769625 scopus 로고
    • Immunocytochemical localization of the DNA-binding protein HCC during the cell cycle of the histone-less dinoflagellate protoctista Crypthecodinium cohnii b
    • Geraud,M.-L., Sala-Rovira,M., Herzog,M. and Soyer-Gobillard,M.-O. (1991) Immunocytochemical localization of the DNA-binding protein HCC during the cell cycle of the histone-less dinoflagellate protoctista Crypthecodinium cohnii b. Biol. Cell, 71, 123-134.
    • (1991) Biol. Cell , vol.71 , pp. 123-134
    • Geraud, M.-L.1    Sala-Rovira, M.2    Herzog, M.3    Soyer-Gobillard, M.-O.4
  • 29
    • 0036073722 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a histone-like protein from the marine dinoflagellate Lingulodinium polyedrum (Dinophyceae)
    • Chudnovsky,Y., Li,J.F., Rizzo,P.J., Hastings,J.W. and Fagan,T.F. (2002) Cloning, expression, and characterization of a histone-like protein from the marine dinoflagellate Lingulodinium polyedrum (Dinophyceae). J. Phycol., 38, 543-550.
    • (2002) J. Phycol , vol.38 , pp. 543-550
    • Chudnovsky, Y.1    Li, J.F.2    Rizzo, P.J.3    Hastings, J.W.4    Fagan, T.F.5
  • 30
    • 34447525975 scopus 로고    scopus 로고
    • Use of DNA microcircles in protein-DNA binding studies
    • Travers,A and Buckle,M, eds, Oxford University Press, Hong Kong, 398pp
    • Payet,D. (2000) Use of DNA microcircles in protein-DNA binding studies. In Travers,A and Buckle,M. (eds), DNA-Protein Interactions: A Practical Approach. Oxford University Press, Hong Kong, 398pp.
    • (2000) DNA-Protein Interactions: A Practical Approach
    • Payet, D.1
  • 32
    • 1842289164 scopus 로고    scopus 로고
    • Superhelix dimensions of a 1868 base pair plasmid determined by scanning force microscopy in air and in aqueous solution
    • Rippe,K., Mucke,N. and Langowski,J. (1997) Superhelix dimensions of a 1868 base pair plasmid determined by scanning force microscopy in air and in aqueous solution. Nucleic Acids Res., 25, 1736-1744.
    • (1997) Nucleic Acids Res , vol.25 , pp. 1736-1744
    • Rippe, K.1    Mucke, N.2    Langowski, J.3
  • 33
    • 0031720087 scopus 로고    scopus 로고
    • Escherichia coli HU protein suppresses DNA-gyrase-mediated illegitimate recombination and SOS induction
    • Shanado,Y., Kato,J. and Ikeda,H. (1998) Escherichia coli HU protein suppresses DNA-gyrase-mediated illegitimate recombination and SOS induction. Genes Cells, 3, 511-520.
    • (1998) Genes Cells , vol.3 , pp. 511-520
    • Shanado, Y.1    Kato, J.2    Ikeda, H.3
  • 34
    • 0034855972 scopus 로고    scopus 로고
    • Evaluation of protein multiple alignments by SAM-T99 using the balibase multiple alignment test set
    • Karplus,K. and Hu,B. (2001) Evaluation of protein multiple alignments by SAM-T99 using the balibase multiple alignment test set. Bioinformat. 17, 713-720.
    • (2001) Bioinformat , vol.17 , pp. 713-720
    • Karplus, K.1    Hu, B.2
  • 35
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou,P.Y. and Fasman,G.D. (1978) Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol. Relat. Areas Mol. Biol., 47, 45-148.
    • (1978) Adv. Enzymol. Relat. Areas Mol. Biol , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 36
    • 0018093765 scopus 로고
    • Conformational preferences of amino acids in globular proteins
    • Levitt,M. (1978) Conformational preferences of amino acids in globular proteins. Biochemistry, 17, 4277-4285.
    • (1978) Biochemistry , vol.17 , pp. 4277-4285
    • Levitt, M.1
  • 37
    • 0001040367 scopus 로고
    • An algorithm for protein secondary structure prediction based on class prediction
    • Deleage,G. and Roux,B. (1987) An algorithm for protein secondary structure prediction based on class prediction. Protein Eng., 1 289-294.
    • (1987) Protein Eng , vol.1 , pp. 289-294
    • Deleage, G.1    Roux, B.2
  • 38
    • 0024267577 scopus 로고
    • Construction and characterization of the deletion mutant of hupA and hupB genes in Escherichia coli
    • Wada,M., Kano,Y., Ogawa,T., Okazaki,T. and Imamoto,F. (1988) Construction and characterization of the deletion mutant of hupA and hupB genes in Escherichia coli. J. Mol. Biol., 204, 581-591.
    • (1988) J. Mol. Biol , vol.204 , pp. 581-591
    • Wada, M.1    Kano, Y.2    Ogawa, T.3    Okazaki, T.4    Imamoto, F.5
  • 39
    • 10244243805 scopus 로고    scopus 로고
    • DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus
    • Ceci,P., Cellai,S., Falvo,E., Rivetti,C., Rossi,G.L. and Chiancone,E. (2004) DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus. Nucleic Acids Res., 32, 5935-5944.
    • (2004) Nucleic Acids Res , vol.32 , pp. 5935-5944
    • Ceci, P.1    Cellai, S.2    Falvo, E.3    Rivetti, C.4    Rossi, G.L.5    Chiancone, E.6
  • 40
    • 0034666271 scopus 로고    scopus 로고
    • H-NS mediated compaction of DNA visualised by atomic force microscopy
    • Dame,R.T., Wyman,C. and Goosen,N. (2000) H-NS mediated compaction of DNA visualised by atomic force microscopy. Nucleic Acids Res., 28 3504-3510.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3504-3510
    • Dame, R.T.1    Wyman, C.2    Goosen, N.3
  • 41
    • 0019347124 scopus 로고
    • An evaluation of the phylogenetic position of the dinoflagellate Crypthecodinium cohnii based on 5S rRNA characterization
    • Hinnebusch,A.G., Klotz,L.C., Blanken,R.L. and Loeblich,A.R.III. (1981) An evaluation of the phylogenetic position of the dinoflagellate Crypthecodinium cohnii based on 5S rRNA characterization. J. Mol. Evol., 17, 334-337.
    • (1981) J. Mol. Evol , vol.17 , pp. 334-337
    • Hinnebusch, A.G.1    Klotz, L.C.2    Blanken, R.L.3    Loeblich III, A.R.4
  • 42
    • 0019736665 scopus 로고
    • Comparative aspects of basic chromatin proteins in dinoflagellates
    • Rizzo,P.J. (1981) Comparative aspects of basic chromatin proteins in dinoflagellates. Biosystems, 14, 433-443.
    • (1981) Biosystems , vol.14 , pp. 433-443
    • Rizzo, P.J.1
  • 43
    • 0016224506 scopus 로고
    • Structural changes of dinoflagellate chromosomes by pronase and ribonuclease
    • Soyer,M.O. and Haapala,O.K. (1974) Structural changes of dinoflagellate chromosomes by pronase and ribonuclease. Chromosoma, 47, 179-192.
    • (1974) Chromosoma , vol.47 , pp. 179-192
    • Soyer, M.O.1    Haapala, O.K.2
  • 44
    • 27944511372 scopus 로고
    • The major histone-like protein from the nonphotosynthetic dinoflagellate Crypthecodinium cohnii (pyrrophyta) is present in stationary phase cultures
    • Rizzo,P.J., Choi,J. and Morris,R.L. (1984) The major histone-like protein from the nonphotosynthetic dinoflagellate Crypthecodinium cohnii (pyrrophyta) is present in stationary phase cultures. J. Phycol., 20, 95-100.
    • (1984) J. Phycol , vol.20 , pp. 95-100
    • Rizzo, P.J.1    Choi, J.2    Morris, R.L.3
  • 45
    • 0033057395 scopus 로고    scopus 로고
    • Archaeal nucleosome positioning sequence from Methanothermus fervidus
    • Pereira,S.L. and Reeve,J.N. (1999) Archaeal nucleosome positioning sequence from Methanothermus fervidus. J. Mol. Biol., 289, 675-681.
    • (1999) J. Mol. Biol , vol.289 , pp. 675-681
    • Pereira, S.L.1    Reeve, J.N.2
  • 46
    • 0034011209 scopus 로고    scopus 로고
    • Structure and functional relationships of archaeal and eukaryal histones and nucleosomes
    • Sandman,K. and Reeve,J.N. (2000) Structure and functional relationships of archaeal and eukaryal histones and nucleosomes. Arch. Microbiol. 173, 165-169.
    • (2000) Arch. Microbiol , vol.173 , pp. 165-169
    • Sandman, K.1    Reeve, J.N.2
  • 49
    • 33750527566 scopus 로고    scopus 로고
    • The architectural role of nucleoid-associated proteins in the organization of bacterial chromatin: A molecular perspective
    • Luijsterburg,M.S., Noom,M.C., Wuite,G.J. and Dame,R.T. (2006) The architectural role of nucleoid-associated proteins in the organization of bacterial chromatin: A molecular perspective. J. Struct. Biol., 156, 262-272.
    • (2006) J. Struct. Biol , vol.156 , pp. 262-272
    • Luijsterburg, M.S.1    Noom, M.C.2    Wuite, G.J.3    Dame, R.T.4
  • 50
    • 0030976054 scopus 로고    scopus 로고
    • The oligomeric structure of nucleoid protein H-NS is necessary for recognition of intrinsically curved DNA and for DNA bending
    • Spurio,R., Falconi,M., Brandi,A., Pon,C.L. and Gualerzi,C.O. (1997) The oligomeric structure of nucleoid protein H-NS is necessary for recognition of intrinsically curved DNA and for DNA bending. EMBO J. 16, 1795-1805.
    • (1997) EMBO J , vol.16 , pp. 1795-1805
    • Spurio, R.1    Falconi, M.2    Brandi, A.3    Pon, C.L.4    Gualerzi, C.O.5
  • 52
    • 0029975925 scopus 로고    scopus 로고
    • DNA aggregation induced by polyamines and cobalthexamine
    • Pelta,J., Livolant,F. and Sikorav,J.L. (1996) DNA aggregation induced by polyamines and cobalthexamine. J. Biol. Chem., 271, 5656-5662.
    • (1996) J. Biol. Chem , vol.271 , pp. 5656-5662
    • Pelta, J.1    Livolant, F.2    Sikorav, J.L.3
  • 53
    • 33747037252 scopus 로고    scopus 로고
    • Solubility and charge inversion of complexes of DNA and basic proteins
    • Raspaud,E., Pelta,J., de Frutos,M. and Livolant,F. (2006) Solubility and charge inversion of complexes of DNA and basic proteins. Phys. Rev. Lett., 97, 068103.
    • (2006) Phys. Rev. Lett , vol.97 , pp. 068103
    • Raspaud, E.1    Pelta, J.2    de Frutos, M.3    Livolant, F.4
  • 54
  • 55
    • 0000959868 scopus 로고    scopus 로고
    • Reentrant condensation of DNA induced by multivalent counterions
    • Nguyen,T.T., Rouzina,I. and Shklovskii,B.I. (2000) Reentrant condensation of DNA induced by multivalent counterions. J. Chem. Phys., 112, 2562-2568.
    • (2000) J. Chem. Phys , vol.112 , pp. 2562-2568
    • Nguyen, T.T.1    Rouzina, I.2    Shklovskii, B.I.3
  • 56
    • 0036055199 scopus 로고    scopus 로고
    • Colloquium: The physics of charge inversion in chemical and biological systems
    • Grosberg,A.Y., Nguyen,T.T. and Shklovskii,B.I. (2002) Colloquium: The physics of charge inversion in chemical and biological systems. Rev. Mod. Phys., 74, 329-345.
    • (2002) Rev. Mod. Phys , vol.74 , pp. 329-345
    • Grosberg, A.Y.1    Nguyen, T.T.2    Shklovskii, B.I.3
  • 57
    • 18344392110 scopus 로고    scopus 로고
    • Wigner crystal model of counterion induced bundle formation of rodlike polyelectrolytes
    • Shklovskii,B.I. (1999) Wigner crystal model of counterion induced bundle formation of rodlike polyelectrolytes. Phys. Rev. Lett., 82, 3268-3271.
    • (1999) Phys. Rev. Lett , vol.82 , pp. 3268-3271
    • Shklovskii, B.I.1
  • 58
    • 17844375109 scopus 로고    scopus 로고
    • Phase diagram of solution of oppositely charged polyelectrolytes
    • Zhang,R. and Shklovskii,B.I. (2005) Phase diagram of solution of oppositely charged polyelectrolytes. Physica A., 352, 216-238.
    • (2005) Physica A , vol.352 , pp. 216-238
    • Zhang, R.1    Shklovskii, B.I.2
  • 59
    • 0022431950 scopus 로고
    • Flexamine cobalt chloride promotes intermolecular ligation of blunt end DNA fragments by T4 DNA ligase
    • Rusche,J.R. and Howard-Flanders,P. (1985) Flexamine cobalt chloride promotes intermolecular ligation of blunt end DNA fragments by T4 DNA ligase. Nucleic Acids Res., 13, 1997-2008.
    • (1985) Nucleic Acids Res , vol.13 , pp. 1997-2008
    • Rusche, J.R.1    Howard-Flanders, P.2
  • 60
    • 0022742336 scopus 로고
    • Thermophilic HB8 DNA ligase: Effects of polyethylene glycols and polyamines on blunt-end ligation of DNA
    • Takahashi,M. and Uchida,T. (1986) Thermophilic HB8 DNA ligase: Effects of polyethylene glycols and polyamines on blunt-end ligation of DNA. J. Biochem., 100, 123-131.
    • (1986) J. Biochem , vol.100 , pp. 123-131
    • Takahashi, M.1    Uchida, T.2
  • 61
    • 0021925655 scopus 로고
    • Isolation of altered RecA polypeptides and interaction with ATP and DNA
    • Rusche,J.R., Konigsberg,W. and Howard-Flanders,P. (1985) Isolation of altered RecA polypeptides and interaction with ATP and DNA. J. Biol. Chem., 260, 949-955.
    • (1985) J. Biol. Chem , vol.260 , pp. 949-955
    • Rusche, J.R.1    Konigsberg, W.2    Howard-Flanders, P.3
  • 63
    • 30644480185 scopus 로고    scopus 로고
    • Atomic force microscopic study of aggregation of RecA-DNA nucleoprotein filaments into left-handed supercoiled bundles
    • Shi,W.-X. and Larson,R.G. (2005) Atomic force microscopic study of aggregation of RecA-DNA nucleoprotein filaments into left-handed supercoiled bundles. Nano Lett., 5, 2476-2481.
    • (2005) Nano Lett , vol.5 , pp. 2476-2481
    • Shi, W.-X.1    Larson, R.G.2
  • 65
    • 0033560941 scopus 로고    scopus 로고
    • Ethanol-induced structural transitions of DNA on mica
    • Fang,Y., Spisz,T.S. and Hoh,J.H. (1999) Ethanol-induced structural transitions of DNA on mica. Nucleic Acids Res., 27, 1943-1949.
    • (1999) Nucleic Acids Res , vol.27 , pp. 1943-1949
    • Fang, Y.1    Spisz, T.S.2    Hoh, J.H.3
  • 67
    • 0032846225 scopus 로고    scopus 로고
    • Cationic silanes stabilize intermediates in DNA condensation
    • Fang,Y. and Hoh,J.H. (1999) Cationic silanes stabilize intermediates in DNA condensation. FEBS Lett., 459, 173-176.
    • (1999) FEBS Lett , vol.459 , pp. 173-176
    • Fang, Y.1    Hoh, J.H.2
  • 68
    • 0030757526 scopus 로고    scopus 로고
    • Nanoscopic structure of DNA condensed for gene delivery
    • Dunlap,D.D., Maggi,A., Soria,M.R. and Monaco,L. (1997) Nanoscopic structure of DNA condensed for gene delivery. Nucleic Acids Res., 25, 3095-3101.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3095-3101
    • Dunlap, D.D.1    Maggi, A.2    Soria, M.R.3    Monaco, L.4
  • 69
    • 0027179724 scopus 로고
    • Mode of formation and structural features of DNA-cationic liposome complexes used for transfection
    • Gershon,H., Ghirlando,R., Guttman,S.B. and Minsky,A. (1993) Mode of formation and structural features of DNA-cationic liposome complexes used for transfection. Biochemistry, 32, 7143-7151.
    • (1993) Biochemistry , vol.32 , pp. 7143-7151
    • Gershon, H.1    Ghirlando, R.2    Guttman, S.B.3    Minsky, A.4
  • 72
    • 0032539631 scopus 로고    scopus 로고
    • A previously unidentified host protein protects retroviral DNA from autointegration
    • Lee,M.S. and Craigie,R. (1998) A previously unidentified host protein protects retroviral DNA from autointegration. Proc. Natl. Acad. Sci. USA, 95, 1528-1533.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1528-1533
    • Lee, M.S.1    Craigie, R.2
  • 73
    • 0343340048 scopus 로고    scopus 로고
    • Bacillus subtilis LrpC is a sequence-independent DNA-binding and DNA-bending protein which bridges DNA
    • Tapias,A., Lopez,G. and Ayora,S. (2000) Bacillus subtilis LrpC is a sequence-independent DNA-binding and DNA-bending protein which bridges DNA. Nucleic Acids Res., 28, 552-559.
    • (2000) Nucleic Acids Res , vol.28 , pp. 552-559
    • Tapias, A.1    Lopez, G.2    Ayora, S.3
  • 74
    • 33846025466 scopus 로고    scopus 로고
    • Right-handed DNA supercoiling by an octameric form of histone-like protein HU: Modulation of cellular transcription
    • Kar,S., Choi,E.J., Guo,F., Dimitriadis,E.K., Kotova,S.L. and Adhya,S. (2006) Right-handed DNA supercoiling by an octameric form of histone-like protein HU: Modulation of cellular transcription. J. Biol. Chem., 281, 40144-40153.
    • (2006) J. Biol. Chem , vol.281 , pp. 40144-40153
    • Kar, S.1    Choi, E.J.2    Guo, F.3    Dimitriadis, E.K.4    Kotova, S.L.5    Adhya, S.6
  • 78
  • 79
    • 17444369067 scopus 로고    scopus 로고
    • Remote control of gene transcription
    • West,A.G. and Fraser,P. (2005) Remote control of gene transcription. Hum. Mol. Genet., 14, R101-R111.
    • (2005) Hum. Mol. Genet , vol.14
    • West, A.G.1    Fraser, P.2
  • 80
    • 0032030770 scopus 로고    scopus 로고
    • Histone acetylation and transcriptional regulatory mechanisms
    • Struhl,K. (1998) Histone acetylation and transcriptional regulatory mechanisms. Genes Develop., 12, 599-606.
    • (1998) Genes Develop , vol.12 , pp. 599-606
    • Struhl, K.1
  • 81
    • 0029991026 scopus 로고    scopus 로고
    • Histone-like protein HU and bacterial DNA topology: Suppression of an HU deficiency by gyrase mutations
    • Malik,M., Bensaid,A., Rouviere-Yaniv,J. and Drlica,K. (1996) Histone-like protein HU and bacterial DNA topology: Suppression of an HU deficiency by gyrase mutations. J. Mol. Biol., 256, 66-76.
    • (1996) J. Mol. Biol , vol.256 , pp. 66-76
    • Malik, M.1    Bensaid, A.2    Rouviere-Yaniv, J.3    Drlica, K.4
  • 82
    • 0029939230 scopus 로고    scopus 로고
    • Cross-talk between topoisomerase I and HU in Escherichia coli
    • Bensaid,A., Almeida,A., Drlica,K. and Rouviere-Yaniv,J. (1996) Cross-talk between topoisomerase I and HU in Escherichia coli. J. Mol. Biol., 256, 292-300.
    • (1996) J. Mol. Biol , vol.256 , pp. 292-300
    • Bensaid, A.1    Almeida, A.2    Drlica, K.3    Rouviere-Yaniv, J.4
  • 83
    • 27944485346 scopus 로고    scopus 로고
    • Type II topoisomerase activities in both G1 and G2/M phases of the dinoflagellate cell cycle
    • Mak,C.K.M., Hung,V.K.L. and Wong,J.T.Y. (2005) Type II topoisomerase activities in both G1 and G2/M phases of the dinoflagellate cell cycle. Chromosoma, 114, 420-431.
    • (2005) Chromosoma , vol.114 , pp. 420-431
    • Mak, C.K.M.1    Hung, V.K.L.2    Wong, J.T.Y.3
  • 84
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame,C., Higgins,D.G. and Heringa,J. (2000) T-Coffee: A novel method for fast and accurate multiple sequence alignment. J. Mol. Biol., 302, 205-217.
    • (2000) J. Mol. Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.