메뉴 건너뛰기




Volumn 175, Issue 2, 2011, Pages 135-146

Structural insights into transcription complexes

Author keywords

Multi subunit complexes; Regulation of gene expression; Structural proteomics; Transcription factors

Indexed keywords

AMINO ACID; DNA POLYMERASE; ESTROGEN RELATED RECEPTOR ALPHA; GLYCINE; HISTONE H3; LAC REPRESSOR; LIVER RECEPTOR HOMOLOG 1; LYSINE; ORPHAN NUCLEAR RECEPTOR; PROLINE; PROTEIN; PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN ARGININE METHYLTRANSFERASE 4; PROTEIN P52; PROTEIN P8; RAP1 PROTEIN; RNA POLYMERASE II; SET1 PROTEIN; TAF3 PROTEIN; TRANSCRIPTION ELONGATION FACTOR; TRANSCRIPTION FACTOR ETS 1; TRANSCRIPTION FACTOR IID; TRANSCRIPTION FACTOR IIH; TRANSCRIPTION FACTOR MAFB; TRANSCRIPTION FACTOR SAGA; UNCLASSIFIED DRUG;

EID: 79960011480     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2011.04.015     Document Type: Review
Times cited : (11)

References (84)
  • 2
    • 77249119269 scopus 로고    scopus 로고
    • Structure-function relationships and crystal structures of the vitamin D receptor bound 2 alpha-methyl-(20S, 23S)- and 2 alpha-methyl-(20S, 23R)-epoxymethano-1 alpha, 25-dihydroxyvitamin D3
    • Antony P., Sigueiro R., Huet T., Sato Y., Ramalanjaona N., Rodrigues L.C., Mourino A., Moras D., Rochel N. Structure-function relationships and crystal structures of the vitamin D receptor bound 2 alpha-methyl-(20S, 23S)- and 2 alpha-methyl-(20S, 23R)-epoxymethano-1 alpha, 25-dihydroxyvitamin D3. J. Med. Chem. 2010, 53(3):1159-1171.
    • (2010) J. Med. Chem. , vol.53 , Issue.3 , pp. 1159-1171
    • Antony, P.1    Sigueiro, R.2    Huet, T.3    Sato, Y.4    Ramalanjaona, N.5    Rodrigues, L.C.6    Mourino, A.7    Moras, D.8    Rochel, N.9
  • 4
    • 19044367561 scopus 로고    scopus 로고
    • ETS-1 transcription factor binds cooperatively to the palindromic head to head ETS-binding sites of the stromelysin-1 promoter by counteracting autoinhibition
    • Baillat D., Begue A., Stehelin D., Aumercier M. ETS-1 transcription factor binds cooperatively to the palindromic head to head ETS-binding sites of the stromelysin-1 promoter by counteracting autoinhibition. J. Biol. Chem. 2002, 277(33):29386-29398.
    • (2002) J. Biol. Chem. , vol.277 , Issue.33 , pp. 29386-29398
    • Baillat, D.1    Begue, A.2    Stehelin, D.3    Aumercier, M.4
  • 6
    • 58149295717 scopus 로고    scopus 로고
    • Protein arginine methylation in mammals: who, what, and why
    • Bedford M.T., Clarke S.G. Protein arginine methylation in mammals: who, what, and why. Mol. Cell. 2009, 33(1):1-13.
    • (2009) Mol. Cell. , vol.33 , Issue.1 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 8
    • 0022884567 scopus 로고
    • Base substitution mutants of the lac operator: in vivo and in vitro affinities for lac repressor
    • Betz J.L., Sasmor H.M., Buck F., Insley M.Y., Caruthers M.H. Base substitution mutants of the lac operator: in vivo and in vitro affinities for lac repressor. Gene 1986, 50(1-3):123-132.
    • (1986) Gene , vol.50 , Issue.1-3 , pp. 123-132
    • Betz, J.L.1    Sasmor, H.M.2    Buck, F.3    Insley, M.Y.4    Caruthers, M.H.5
  • 10
    • 0036583638 scopus 로고    scopus 로고
    • Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator
    • Blanco A.G., Sola M., Gomis-Ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002, 10(5):701-713.
    • (2002) Structure , vol.10 , Issue.5 , pp. 701-713
    • Blanco, A.G.1    Sola, M.2    Gomis-Ruth, F.X.3    Coll, M.4
  • 13
    • 23044514646 scopus 로고    scopus 로고
    • Construction of a set Gateway-based destination vectors for high-throughput cloning and expression screening in Escherichia coli
    • Busso D., Delagoutte-Busso B., Moras D. Construction of a set Gateway-based destination vectors for high-throughput cloning and expression screening in Escherichia coli. Anal. Biochem. 2005, 343(2):313-321.
    • (2005) Anal. Biochem. , vol.343 , Issue.2 , pp. 313-321
    • Busso, D.1    Delagoutte-Busso, B.2    Moras, D.3
  • 16
    • 33947109474 scopus 로고    scopus 로고
    • Adaptability of the Vitamin D nuclear receptor to the synthetic ligand Gemini: remodelling the LBP with one side chain rotation
    • Ciesielski F., Rochel N., Moras D. Adaptability of the Vitamin D nuclear receptor to the synthetic ligand Gemini: remodelling the LBP with one side chain rotation. J. Steroid. Biochem. Mol. Biol. 2007, 103(3-5):235-242.
    • (2007) J. Steroid. Biochem. Mol. Biol. , vol.103 , Issue.3-5 , pp. 235-242
    • Ciesielski, F.1    Rochel, N.2    Moras, D.3
  • 21
    • 79959992840 scopus 로고    scopus 로고
    • Deciphering correct strategies for multiprotein complex assembly by co-expression: Application to complexes as large as the histone octamer. J. Struct. Biol
    • Diebold, M.L., Fribourg, S., Koch, M., Metzger, T., Romier, C., 2011. Deciphering correct strategies for multiprotein complex assembly by co-expression: Application to complexes as large as the histone octamer. J. Struct. Biol.
    • (2011)
    • Diebold, M.L.1    Fribourg, S.2    Koch, M.3    Metzger, T.4    Romier, C.5
  • 22
    • 78649717707 scopus 로고    scopus 로고
    • The structure of an Iws1/Spt6 complex reveals an interaction domain conserved in TFIIS, Elongin A and Med26
    • Diebold M.L., Koch M., Loeliger E., Cura V., Winston F., Cavarelli J., Romier C. The structure of an Iws1/Spt6 complex reveals an interaction domain conserved in TFIIS, Elongin A and Med26. EMBO J. 2010, 29(23):3979-3991.
    • (2010) EMBO J. , vol.29 , Issue.23 , pp. 3979-3991
    • Diebold, M.L.1    Koch, M.2    Loeliger, E.3    Cura, V.4    Winston, F.5    Cavarelli, J.6    Romier, C.7
  • 23
    • 78649684166 scopus 로고    scopus 로고
    • Noncanonical Tandem SH2 Enables Interaction of Elongation Factor Spt6 with RNA Polymerase II
    • Diebold M.L., Loeliger E., Koch M., Winston F., Cavarelli J., Romier C. Noncanonical Tandem SH2 Enables Interaction of Elongation Factor Spt6 with RNA Polymerase II. J. Biol. Chem. 2010, 285(49):38389-38398.
    • (2010) J. Biol. Chem. , vol.285 , Issue.49 , pp. 38389-38398
    • Diebold, M.L.1    Loeliger, E.2    Koch, M.3    Winston, F.4    Cavarelli, J.5    Romier, C.6
  • 24
    • 0035827305 scopus 로고    scopus 로고
    • The 14th Datta Lecture. TFIIH: from transcription to clinic
    • Egly J.M. The 14th Datta Lecture. TFIIH: from transcription to clinic. FEBS Lett. 2001, 498(2-3):124-128.
    • (2001) FEBS Lett. , vol.498 , Issue.2-3 , pp. 124-128
    • Egly, J.M.1
  • 25
    • 49349098683 scopus 로고    scopus 로고
    • Higher-throughtput approaches to crystallization and crystal structure determination
    • Fogg M.J., Wilkinson A.J. Higher-throughtput approaches to crystallization and crystal structure determination. Biochem. Soc. Trans. 2008, 36:771-775.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 771-775
    • Fogg, M.J.1    Wilkinson, A.J.2
  • 26
    • 3543148406 scopus 로고    scopus 로고
    • Expression screening, protein purification and NMR analysis of human protein domains for structural genomics
    • Folkers G.E., van Buuren B.N., Kaptein R. Expression screening, protein purification and NMR analysis of human protein domains for structural genomics. J. Struct. Funct. Genomics 2004, 5(1-2):119-131.
    • (2004) J. Struct. Funct. Genomics , vol.5 , Issue.1-2 , pp. 119-131
    • Folkers, G.E.1    van Buuren, B.N.2    Kaptein, R.3
  • 27
    • 0035697276 scopus 로고    scopus 로고
    • Structural studies of Ets-1/Pax5 complex formation on DNA
    • Garvie C.W., Hagman J., Wolberger C. Structural studies of Ets-1/Pax5 complex formation on DNA. Mol. Cell. 2001, 8(6):1267-1276.
    • (2001) Mol. Cell. , vol.8 , Issue.6 , pp. 1267-1276
    • Garvie, C.W.1    Hagman, J.2    Wolberger, C.3
  • 28
    • 0347928848 scopus 로고    scopus 로고
    • Structural analysis of the autoinhibition of Ets-1 and its role in protein partnerships
    • Garvie C.W., Pufall M.A., Graves B.J., Wolberger C. Structural analysis of the autoinhibition of Ets-1 and its role in protein partnerships. J. Biol. Chem. 2002, 277(47):45529-45536.
    • (2002) J. Biol. Chem. , vol.277 , Issue.47 , pp. 45529-45536
    • Garvie, C.W.1    Pufall, M.A.2    Graves, B.J.3    Wolberger, C.4
  • 32
    • 62349134544 scopus 로고    scopus 로고
    • Structural and evolutionary innovation of the heterodimerization interface between USP and the ecdysone receptor ECR in insects
    • Iwema T., Chaumot A., Studer R.A., Robinson-Rechavi M., Billas I.M., Moras D., Laudet V., Bonneton F. Structural and evolutionary innovation of the heterodimerization interface between USP and the ecdysone receptor ECR in insects. Mol. Biol. Evol. 2009, 26(4):753-768.
    • (2009) Mol. Biol. Evol. , vol.26 , Issue.4 , pp. 753-768
    • Iwema, T.1    Chaumot, A.2    Studer, R.A.3    Robinson-Rechavi, M.4    Billas, I.M.5    Moras, D.6    Laudet, V.7    Bonneton, F.8
  • 33
    • 71549150895 scopus 로고    scopus 로고
    • Baculovirus-insect cell expression systems
    • Jarvis D.L. Baculovirus-insect cell expression systems. Methods Enzymol. 2009, 463:191-222.
    • (2009) Methods Enzymol. , vol.463 , pp. 191-222
    • Jarvis, D.L.1
  • 34
    • 77954452645 scopus 로고    scopus 로고
    • Structure determination of the minimal complex between Tfb5 and Tfb2, two subunits of the yeast transcription/DNA-repair factor TFIIH: a retrospective study
    • Kainov D.E., Cura V., Vitorino M., Nierengarten H., Poussin P., Kieffer B., Cavarelli J., Poterszman A. Structure determination of the minimal complex between Tfb5 and Tfb2, two subunits of the yeast transcription/DNA-repair factor TFIIH: a retrospective study. Acta Crystallogr. D. Biol. Crystallogr. 2010, 66(Pt. 7):745-755.
    • (2010) Acta Crystallogr. D. Biol. Crystallogr. , vol.66 , Issue.PART. 7 , pp. 745-755
    • Kainov, D.E.1    Cura, V.2    Vitorino, M.3    Nierengarten, H.4    Poussin, P.5    Kieffer, B.6    Cavarelli, J.7    Poterszman, A.8
  • 37
    • 0037124326 scopus 로고    scopus 로고
    • Plasticity in protein-DNA recognition: lac repressor interacts with its natural operator 01 through alternative conformations of its DNA-binding domain
    • Kalodimos C.G., Bonvin A.M., Salinas R.K., Wechselberger R., Boelens R., Kaptein R. Plasticity in protein-DNA recognition: lac repressor interacts with its natural operator 01 through alternative conformations of its DNA-binding domain. EMBO J. 2002, 21(12):2866-2876.
    • (2002) EMBO J. , vol.21 , Issue.12 , pp. 2866-2876
    • Kalodimos, C.G.1    Bonvin, A.M.2    Salinas, R.K.3    Wechselberger, R.4    Boelens, R.5    Kaptein, R.6
  • 38
    • 0029670530 scopus 로고    scopus 로고
    • A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS-domain-DNA complex
    • Kodandapani R., Pio F., Ni C.Z., Piccialli G., Klemsz M., McKercher S., Maki R.A., Ely K.R. A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS-domain-DNA complex. Nature 1996, 380(6573):456-460.
    • (1996) Nature , vol.380 , Issue.6573 , pp. 456-460
    • Kodandapani, R.1    Pio, F.2    Ni, C.Z.3    Piccialli, G.4    Klemsz, M.5    McKercher, S.6    Maki, R.A.7    Ely, K.R.8
  • 39
    • 34548801789 scopus 로고    scopus 로고
    • The molecular basis of eukaryotic transcription
    • Kornberg R.D. The molecular basis of eukaryotic transcription. Proc. Natl. Acad. Sci. USA 2007, 104(32):12955-12961.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.32 , pp. 12955-12961
    • Kornberg, R.D.1
  • 40
    • 33847032959 scopus 로고    scopus 로고
    • SnapShot: Histone-modifying enzymes
    • Kouzarides T. SnapShot: Histone-modifying enzymes. Cell 2007, 128(4):802.
    • (2007) Cell , vol.128 , Issue.4 , pp. 802
    • Kouzarides, T.1
  • 44
    • 47949108983 scopus 로고    scopus 로고
    • Regulation of the transcription factor Ets-1 by DNA-mediated homo-dimerization
    • Lamber E.P., Vanhille L., Textor L.C., Kachalova G.S., Sieweke M.H., Wilmanns M. Regulation of the transcription factor Ets-1 by DNA-mediated homo-dimerization. EMBO J. 2008, 27(14):2006-2017.
    • (2008) EMBO J. , vol.27 , Issue.14 , pp. 2006-2017
    • Lamber, E.P.1    Vanhille, L.2    Textor, L.C.3    Kachalova, G.S.4    Sieweke, M.H.5    Wilmanns, M.6
  • 45
    • 74249102477 scopus 로고    scopus 로고
    • Structure of an RNA polymerase II-TFIIB complex and the transcription initiation mechanism
    • Liu X., Bushnell D.A., Wang D., Calero G., Kornberg R.D. Structure of an RNA polymerase II-TFIIB complex and the transcription initiation mechanism. Science 2010, 327(5962):206-209.
    • (2010) Science , vol.327 , Issue.5962 , pp. 206-209
    • Liu, X.1    Bushnell, D.A.2    Wang, D.3    Calero, G.4    Kornberg, R.D.5
  • 47
    • 0027339446 scopus 로고
    • Role of the sigma 70 subunit of RNA polymerase in transcriptional activation by activator protein PhoB in Escherichia coli
    • Makino K., Amemura M., Kim S.K., Nakata A., Shinagawa H. Role of the sigma 70 subunit of RNA polymerase in transcriptional activation by activator protein PhoB in Escherichia coli. Genes Dev. 1993, 7(1):149-160.
    • (1993) Genes Dev. , vol.7 , Issue.1 , pp. 149-160
    • Makino, K.1    Amemura, M.2    Kim, S.K.3    Nakata, A.4    Shinagawa, H.5
  • 48
    • 60549116406 scopus 로고    scopus 로고
    • Nuclear receptors: one big family
    • McEwan I. Nuclear receptors: one big family. Methods Mol. Biol. 2009, 505:3-18.
    • (2009) Methods Mol. Biol. , vol.505 , pp. 3-18
    • McEwan, I.1
  • 49
    • 43849110454 scopus 로고    scopus 로고
    • Quantitative proteomics reveals regulation of dynamic components within TATA-binding protein (TBP) transcription complexes
    • Mousson F., Kolkman A., Pijnappel W.W., Timmers H.T., Heck A.J. Quantitative proteomics reveals regulation of dynamic components within TATA-binding protein (TBP) transcription complexes. Mol. Cell Proteomics 2008, 7(5):845-852.
    • (2008) Mol. Cell Proteomics , vol.7 , Issue.5 , pp. 845-852
    • Mousson, F.1    Kolkman, A.2    Pijnappel, W.W.3    Timmers, H.T.4    Heck, A.J.5
  • 50
    • 0037123602 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex
    • Murakami K.S., Masuda S., Campbell E.A., Muzzin O., Darst S.A. Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex. Science 2002, 296(5571):1285-1290.
    • (2002) Science , vol.296 , Issue.5571 , pp. 1285-1290
    • Murakami, K.S.1    Masuda, S.2    Campbell, E.A.3    Muzzin, O.4    Darst, S.A.5
  • 51
    • 77955295584 scopus 로고    scopus 로고
    • Transcription factor IIH - the protein complex with multiple functions
    • Mydlikova Z., Gursky J., Pirsel M. Transcription factor IIH - the protein complex with multiple functions. Neoplasma 2010, 57(4):287-290.
    • (2010) Neoplasma , vol.57 , Issue.4 , pp. 287-290
    • Mydlikova, Z.1    Gursky, J.2    Pirsel, M.3
  • 52
    • 77955947553 scopus 로고    scopus 로고
    • Recent advances in the production of proteins in insect and mammalian cells for structural biology
    • Nettleship J.E., Assenberg R., Diprose J.M., Rahman-Huq N., Owens R.J. Recent advances in the production of proteins in insect and mammalian cells for structural biology. J. Struct. Biol. 2010, 172(1):55-65.
    • (2010) J. Struct. Biol. , vol.172 , Issue.1 , pp. 55-65
    • Nettleship, J.E.1    Assenberg, R.2    Diprose, J.M.3    Rahman-Huq, N.4    Owens, R.J.5
  • 54
    • 0028365289 scopus 로고
    • Quality and position of the three lac operators of E. coli define efficiency of repression
    • Oehler S., Amouyal M., Kolkhof P., von Wilcken-Bergmann B., Muller-Hill B. Quality and position of the three lac operators of E. coli define efficiency of repression. EMBO J. 1994, 13(14):3348-3355.
    • (1994) EMBO J. , vol.13 , Issue.14 , pp. 3348-3355
    • Oehler, S.1    Amouyal, M.2    Kolkhof, P.3    von Wilcken-Bergmann, B.4    Muller-Hill, B.5
  • 55
    • 0025343547 scopus 로고
    • The three operators of the lac operon cooperate in repression
    • Oehler S., Eismann E.R., Kramer H., Muller-Hill B. The three operators of the lac operon cooperate in repression. EMBO J. 1990, 9(4):973-979.
    • (1990) EMBO J. , vol.9 , Issue.4 , pp. 973-979
    • Oehler, S.1    Eismann, E.R.2    Kramer, H.3    Muller-Hill, B.4
  • 56
    • 77953711351 scopus 로고    scopus 로고
    • TFIIA and the transactivator Rap1 cooperate to commit TFIID for transcription initiation
    • Papai G., Tripathi M.K., Ruhlmann C., Layer J.H., Weil P.A., Schultz P. TFIIA and the transactivator Rap1 cooperate to commit TFIID for transcription initiation. Nature 2010, 465(7300):956-960.
    • (2010) Nature , vol.465 , Issue.7300 , pp. 956-960
    • Papai, G.1    Tripathi, M.K.2    Ruhlmann, C.3    Layer, J.H.4    Weil, P.A.5    Schultz, P.6
  • 58
    • 74549119439 scopus 로고    scopus 로고
    • Quantitative mass spectrometry of TATA binding protein-containing complexes and subunit phosphorylations during the cell cycle
    • Pijnappel W.P., Kolkman A., Baltissen M.P., Heck A.J., Timmers H.M. Quantitative mass spectrometry of TATA binding protein-containing complexes and subunit phosphorylations during the cell cycle. Proteome Sci. 2009, 7:46.
    • (2009) Proteome Sci. , vol.7 , pp. 46
    • Pijnappel, W.P.1    Kolkman, A.2    Baltissen, M.P.3    Heck, A.J.4    Timmers, H.M.5
  • 59
    • 77954088560 scopus 로고    scopus 로고
    • Vectors for recombinational cloning and gene expression in mammalian cells using modified vaccinia virus Ankara
    • Pradeau-Aubreton K., Ruff M., Garnier J.M., Schultz P., Drillien R. Vectors for recombinational cloning and gene expression in mammalian cells using modified vaccinia virus Ankara. Anal. Biochem. 2010, 404(1):103-105.
    • (2010) Anal. Biochem. , vol.404 , Issue.1 , pp. 103-105
    • Pradeau-Aubreton, K.1    Ruff, M.2    Garnier, J.M.3    Schultz, P.4    Drillien, R.5
  • 61
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut C., Shevchenko A., Rutz B., Wilm M., Mann M., Séraphin B. A generic protein purification method for protein complex characterization and proteome exploration. Nat Biotechnol. 1999, 17(10):1030-1032.
    • (1999) Nat Biotechnol. , vol.17 , Issue.10 , pp. 1030-1032
    • Rigaut, C.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Séraphin, B.6
  • 63
    • 67449102263 scopus 로고    scopus 로고
    • Specificity and affinity of Lac repressor for the auxiliary operators O2 and O3 are explained by the structures of their protein-DNA complexes
    • Romanuka J., Folkers G.E., Biris N., Tishchenko E., Wienk H., Bonvin A.M., Kaptein R., Boelens R. Specificity and affinity of Lac repressor for the auxiliary operators O2 and O3 are explained by the structures of their protein-DNA complexes. J. Mol. Biol. 2009, 390(3):478-489.
    • (2009) J. Mol. Biol. , vol.390 , Issue.3 , pp. 478-489
    • Romanuka, J.1    Folkers, G.E.2    Biris, N.3    Tishchenko, E.4    Wienk, H.5    Bonvin, A.M.6    Kaptein, R.7    Boelens, R.8
  • 64
    • 34247275734 scopus 로고    scopus 로고
    • Crystal structure, biochemical and genetic characterization of yeast and E. cuniculi TAF(II)5 N-terminal domain: implications for TFIID assembly
    • Romier C., James N., Birck C., Cavarelli J., Vivarès C., Collart M.A., Moras D. Crystal structure, biochemical and genetic characterization of yeast and E. cuniculi TAF(II)5 N-terminal domain: implications for TFIID assembly. J Mol Biol. 2007, 368(5):1292-1306.
    • (2007) J Mol Biol. , vol.368 , Issue.5 , pp. 1292-1306
    • Romier, C.1    James, N.2    Birck, C.3    Cavarelli, J.4    Vivarès, C.5    Collart, M.A.6    Moras, D.7
  • 65
    • 0025370340 scopus 로고
    • Symmetric lac operator derivatives: effects of half-operator sequence and spacing on repressor affinity
    • Sasmor H.M., Betz J.L. Symmetric lac operator derivatives: effects of half-operator sequence and spacing on repressor affinity. Gene 1990, 89(1):1-6.
    • (1990) Gene , vol.89 , Issue.1 , pp. 1-6
    • Sasmor, H.M.1    Betz, J.L.2
  • 68
    • 0035515347 scopus 로고    scopus 로고
    • The ETS-domain transcription factor family
    • Sharrocks A.D. The ETS-domain transcription factor family. Nat. Rev. Mol. Cell Biol. 2001, 2(11):827-837.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , Issue.11 , pp. 827-837
    • Sharrocks, A.D.1
  • 69
    • 70349780606 scopus 로고    scopus 로고
    • The emerging therapeutic potential of histone methyltransferase and demethylase inhibitors
    • Spannhoff A., Hauser A.T., Heinke R., Sippl W., Jung M. The emerging therapeutic potential of histone methyltransferase and demethylase inhibitors. ChemMedChem 2009, 4(10):1568-1582.
    • (2009) ChemMedChem , vol.4 , Issue.10 , pp. 1568-1582
    • Spannhoff, A.1    Hauser, A.T.2    Heinke, R.3    Sippl, W.4    Jung, M.5
  • 70
    • 0033573062 scopus 로고    scopus 로고
    • The solution structure of Lac repressor headpiece 62 complexed to a symmetrical lac operator
    • Spronk C.A., Bonvin A.M., Radha P.K., Melacini G., Boelens R., Kaptein R. The solution structure of Lac repressor headpiece 62 complexed to a symmetrical lac operator. Structure 1999, 7(12):1483-1492.
    • (1999) Structure , vol.7 , Issue.12 , pp. 1483-1492
    • Spronk, C.A.1    Bonvin, A.M.2    Radha, P.K.3    Melacini, G.4    Boelens, R.5    Kaptein, R.6
  • 73
    • 34249727764 scopus 로고    scopus 로고
    • Expression, purification, crystallization and preliminary crystallographic study of isolated modules of the mouse coactivator-associated arginine methyltransferase 1
    • Troffer-Charlier N., Cura V., Hassenboehler P., Moras D., Cavarelli J. Expression, purification, crystallization and preliminary crystallographic study of isolated modules of the mouse coactivator-associated arginine methyltransferase 1. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2007, 63(Pt. 4):330-333.
    • (2007) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.63 , Issue.PART. 4 , pp. 330-333
    • Troffer-Charlier, N.1    Cura, V.2    Hassenboehler, P.3    Moras, D.4    Cavarelli, J.5
  • 74
    • 35348916034 scopus 로고    scopus 로고
    • Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains
    • Troffer-Charlier N., Cura V., Hassenboehler P., Moras D., Cavarelli J. Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains. EMBO J. 2007, 26(20):4391-4401.
    • (2007) EMBO J. , vol.26 , Issue.20 , pp. 4391-4401
    • Troffer-Charlier, N.1    Cura, V.2    Hassenboehler, P.3    Moras, D.4    Cavarelli, J.5
  • 75
    • 77955962894 scopus 로고    scopus 로고
    • New baculovirus expression tools for recombinant protein complex production
    • Trowitzsch S., Bieniossek C., Nie Y., Garzoni F., Berger I. New baculovirus expression tools for recombinant protein complex production. J. Struct. Biol. 2010, 172(1):45-54.
    • (2010) J. Struct. Biol. , vol.172 , Issue.1 , pp. 45-54
    • Trowitzsch, S.1    Bieniossek, C.2    Nie, Y.3    Garzoni, F.4    Berger, I.5
  • 76
    • 77956184308 scopus 로고    scopus 로고
    • Applications of the restriction free (RF) cloning procedure for molecular manipulations and protein expression
    • Unger T., Jacobovitch Y., Dantes A., Bernheim R., Peleg Y. Applications of the restriction free (RF) cloning procedure for molecular manipulations and protein expression. J. Struct. Biol. 2010, 172(1):34-44.
    • (2010) J. Struct. Biol. , vol.172 , Issue.1 , pp. 34-44
    • Unger, T.1    Jacobovitch, Y.2    Dantes, A.3    Bernheim, R.4    Peleg, Y.5
  • 79
    • 0029883919 scopus 로고    scopus 로고
    • ETS1 and ETS2 in p53 regulation: spatial separation of ETS binding sites (EBS) modulate protein: DNA interaction
    • Venanzoni M.C., Robinson L.R., Hodge D.R., Kola I., Seth A. ETS1 and ETS2 in p53 regulation: spatial separation of ETS binding sites (EBS) modulate protein: DNA interaction. Oncogene 1996, 12(6):1199-1204.
    • (1996) Oncogene , vol.12 , Issue.6 , pp. 1199-1204
    • Venanzoni, M.C.1    Robinson, L.R.2    Hodge, D.R.3    Kola, I.4    Seth, A.5
  • 82
  • 83
    • 34548221891 scopus 로고    scopus 로고
    • Rtf1 is a multifunctional component of the Paf1 complex that regulates gene expression by directing cotranscriptional histone modification
    • Warner M.H., Roinick K.L., Arndt K.M. Rtf1 is a multifunctional component of the Paf1 complex that regulates gene expression by directing cotranscriptional histone modification. Mol. Cell Biol. 2007, 27(17):6103-6115.
    • (2007) Mol. Cell Biol. , vol.27 , Issue.17 , pp. 6103-6115
    • Warner, M.H.1    Roinick, K.L.2    Arndt, K.M.3
  • 84
    • 33846516797 scopus 로고    scopus 로고
    • The lactose repressor system: paradigms for regulation, allosteric behavior and protein folding
    • Wilson C.J., Zhan H., Swint-Kruse L., Matthews K.S. The lactose repressor system: paradigms for regulation, allosteric behavior and protein folding. Cell Mol. Life Sci. 2007, 64(1):3-16.
    • (2007) Cell Mol. Life Sci. , vol.64 , Issue.1 , pp. 3-16
    • Wilson, C.J.1    Zhan, H.2    Swint-Kruse, L.3    Matthews, K.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.