메뉴 건너뛰기




Volumn 291, Issue 19, 2016, Pages 10293-10306

Quantification of cooperativity in heterodimer-DNA binding improves the accuracy of binding specificity models

Author keywords

[No Author keywords available]

Indexed keywords

BEHAVIORAL RESEARCH; BINDING SITES; BINS; BIOMOLECULES; CYTOLOGY; DIMERS; PROTEINS; TRANSCRIPTION;

EID: 84966333766     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.691154     Document Type: Article
Times cited : (18)

References (65)
  • 1
    • 32444446240 scopus 로고    scopus 로고
    • Gene regulatory networks and the evolution of animal body plans
    • Davidson, E. H., and Erwin, D. H. (2006) Gene regulatory networks and the evolution of animal body plans. Science 311, 796-800
    • (2006) Science , vol.311 , pp. 796-800
    • Davidson, E.H.1    Erwin, D.H.2
  • 2
    • 63849338777 scopus 로고    scopus 로고
    • Experimental advances in the characterization of metazoan gene regulatory networks
    • Deplancke, B. (2009) Experimental advances in the characterization of metazoan gene regulatory networks. Brief. Funct. Genomic Proteomic 8, 12-27
    • (2009) Brief. Funct. Genomic Proteomic , vol.8 , pp. 12-27
    • Deplancke, B.1
  • 4
    • 84868588824 scopus 로고    scopus 로고
    • Basic leucine zipper transcription factor Hac1 binds DNA in two distinct modes as revealed by microfluidic analyses
    • Fordyce, P. M., Pincus, D., Kimmig, P., Nelson, C. S., El-Samad, H., Walter, P., and DeRisi, J. L. (2012) Basic leucine zipper transcription factor Hac1 binds DNA in two distinct modes as revealed by microfluidic analyses. Proc. Natl. Acad. Sci. U.S.A. 109, E3084-E3093
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 3084-3093
    • Fordyce, P.M.1    Pincus, D.2    Kimmig, P.3    Nelson, C.S.4    El-Samad, H.5    Walter, P.6    DeRisi, J.L.7
  • 5
    • 0018199224 scopus 로고
    • DNase footprinting a simple method for the detection of protein-DNA binding specificity
    • Galas, D. J., and Schmitz, A. (1978) DNase footprinting a simple method for the detection of protein-DNA binding specificity. Nucleic Acids Res. 5, 3157-3170
    • (1978) Nucleic Acids Res. , vol.5 , pp. 3157-3170
    • Galas, D.J.1    Schmitz, A.2
  • 7
    • 67650594823 scopus 로고    scopus 로고
    • A multiparameter network reveals extensive divergence between C. Elegans bHLH transcription factors
    • Grove, C. A., De Masi, F., Barrasa, M. I., Newburger, D. E., Alkema, M. J., Bulyk, M. L., and Walhout, A. J. (2009) A multiparameter network reveals extensive divergence between C. elegans bHLH transcription factors. Cell 138, 314-327
    • (2009) Cell , vol.138 , pp. 314-327
    • Grove, C.A.1    De Masi, F.2    Barrasa, M.I.3    Newburger, D.E.4    Alkema, M.J.5    Bulyk, M.L.6    Walhout, A.J.7
  • 9
    • 84876955991 scopus 로고    scopus 로고
    • Genomic regions flanking E-box binding sites influenceDNA binding specificity of bHLH transcription factors through DNA shape
    • Gordân, R., Shen, N., Dror, I., Zhou, T., Horton, J., Rohs, R., and Bulyk, M. L. (2013) Genomic regions flanking E-box binding sites influenceDNA binding specificity of bHLH transcription factors through DNA shape. Cell Rep. 3, 1093-1104
    • (2013) Cell Rep. , vol.3 , pp. 1093-1104
    • Gordân, R.1    Shen, N.2    Dror, I.3    Zhou, T.4    Horton, J.5    Rohs, R.6    Bulyk, M.L.7
  • 10
    • 0142105387 scopus 로고    scopus 로고
    • Genetic analysis of NF-B/Rel transcription factors defines functional specificities
    • Hoffmann, A., Leung, T. H., and Baltimore, D. (2003) Genetic analysis of NF-B/Rel transcription factors defines functional specificities. EMBO J. 22, 5530-5539
    • (2003) EMBO J. , vol.22 , pp. 5530-5539
    • Hoffmann, A.1    Leung, T.H.2    Baltimore, D.3
  • 11
    • 84872588984 scopus 로고    scopus 로고
    • Methods for analysis of transcription factor DNA-binding specificity in vitro
    • Jolma, A., and Taipale, J. (2011) Methods for analysis of transcription factor DNA-binding specificity in vitro. Subcell. Biochem. 52, 155-173
    • (2011) Subcell. Biochem. , vol.52 , pp. 155-173
    • Jolma, A.1    Taipale, J.2
  • 12
    • 0031892994 scopus 로고    scopus 로고
    • Dimerization as a regulatory mechanism in signal transduction
    • Klemm, J. D., Schreiber, S. L., and Crabtree, G. R. (1998) Dimerization as a regulatory mechanism in signal transduction. Annu. Rev. Immunol. 16, 569-592
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 569-592
    • Klemm, J.D.1    Schreiber, S.L.2    Crabtree, G.R.3
  • 13
    • 0035253128 scopus 로고    scopus 로고
    • Retinoid X receptor and its partners in the nuclear receptor family
    • Rastinejad, F. (2001) Retinoid X receptor and its partners in the nuclear receptor family. Curr. Opin. Struct. Biol. 11, 33-38
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 33-38
    • Rastinejad, F.1
  • 14
    • 33744976395 scopus 로고    scopus 로고
    • A compendium of Caenorhabditis elegans regulatory transcription factors: A resource for mapping transcription regulatory networks
    • Reece-Hoyes, J. S., Deplancke, B., Shingles, J., Grove, C. A., Hope, I. A., and Walhout, A. J. (2005) A compendium of Caenorhabditis elegans regulatory transcription factors: A resource for mapping transcription regulatory networks. Genome Biol. 6, R110
    • (2005) Genome Biol. , vol.6 , pp. 110
    • Reece-Hoyes, J.S.1    Deplancke, B.2    Shingles, J.3    Grove, C.A.4    Hope, I.A.5    Walhout, A.J.6
  • 16
    • 0028294902 scopus 로고
    • Dimerization interfaces formed between the DNA binding domains determine the cooperative binding of RXR/RAR and RXR/TR heterodimers to DR5 and DR4 elements
    • Zechel, C., Shen, X. Q., Chambon, P., and Gronemeyer, H. (1994) Dimerization interfaces formed between the DNA binding domains determine the cooperative binding of RXR/RAR and RXR/TR heterodimers to DR5 and DR4 elements. EMBO J. 13, 1414-1424
    • (1994) EMBO J. , vol.13 , pp. 1414-1424
    • Zechel, C.1    Shen, X.Q.2    Chambon, P.3    Gronemeyer, H.4
  • 17
    • 84858329386 scopus 로고    scopus 로고
    • Deciphering the Sox-Oct partner code by quantitative cooperativity measurements
    • Ng, C. K., Li, N. X., Chee, S., Prabhakar, S., Kolatkar, P. R., and Jauch, R. (2012) Deciphering the Sox-Oct partner code by quantitative cooperativity measurements. Nucleic Acids Res. 40, 4933-4941
    • (2012) Nucleic Acids Res. , vol.40 , pp. 4933-4941
    • Ng, C.K.1    Li, N.X.2    Chee, S.3    Prabhakar, S.4    Kolatkar, P.R.5    Jauch, R.6
  • 19
    • 0028332036 scopus 로고
    • Differential recognition of target genes by nuclear receptor monomers, dimers, and heterodimers
    • Glass, C. K. (1994) Differential recognition of target genes by nuclear receptor monomers, dimers, and heterodimers. Endocr. Rev. 15, 391-407
    • (1994) Endocr. Rev. , vol.15 , pp. 391-407
    • Glass, C.K.1
  • 20
    • 0029946449 scopus 로고    scopus 로고
    • DNA-independent and DNA-dependent mechanisms regulate the differential heterodimerization of the isoforms of the thyroid hormone receptor with retinoid X receptor
    • Reginato, M. J., Zhang, J., and Lazar, M. A. (1996) DNA-independent and DNA-dependent mechanisms regulate the differential heterodimerization of the isoforms of the thyroid hormone receptor with retinoid X receptor. J. Biol. Chem. 271, 28199-28205
    • (1996) J. Biol. Chem. , vol.271 , pp. 28199-28205
    • Reginato, M.J.1    Zhang, J.2    Lazar, M.A.3
  • 21
    • 0020480251 scopus 로고
    • Use of the ?Perceptron? Algorithm to distinguish translational initiation sites in E. Coli
    • Stormo, G. D., Schneider, T. D., Gold, L., and Ehrenfeucht, A. (1982) Use of the ?Perceptron? algorithm to distinguish translational initiation sites in E. coli. Nucleic Acids Res. 10, 2997-3011
    • (1982) Nucleic Acids Res. , vol.10 , pp. 2997-3011
    • Stormo, G.D.1    Schneider, T.D.2    Gold, L.3    Ehrenfeucht, A.4
  • 22
    • 84863866025 scopus 로고    scopus 로고
    • Improved models for transcription factor binding site identification using nonindependent interactions
    • Zhao, Y., Ruan, S., Pandey, M., and Stormo, G. D. (2012) Improved models for transcription factor binding site identification using nonindependent interactions. Genetics 191, 781-790
    • (2012) Genetics , vol.191 , pp. 781-790
    • Zhao, Y.1    Ruan, S.2    Pandey, M.3    Stormo, G.D.4
  • 23
    • 33846467150 scopus 로고    scopus 로고
    • Asystems approach to measuring the binding energy landscapes of transcription factors
    • Maerkl, S. J., and Quake, S. R. (2007)Asystems approach to measuring the binding energy landscapes of transcription factors. Science 315, 233-237
    • (2007) Science , vol.315 , pp. 233-237
    • Maerkl, S.J.1    Quake, S.R.2
  • 24
    • 77955274518 scopus 로고    scopus 로고
    • PPAR-in adipocyte differentiation and metabolism-novel insights from genome-wide studies
    • Siersbaek, R., Nielsen, R., and Mandrup, S. (2010) PPAR-in adipocyte differentiation and metabolism-novel insights from genome-wide studies. FEBS Lett. 584, 3242-3249
    • (2010) FEBS Lett. , vol.584 , pp. 3242-3249
    • Siersbaek, R.1    Nielsen, R.2    Mandrup, S.3
  • 25
    • 0028641559 scopus 로고
    • Stimulation of adipogenesis in fibroblasts by PPAR-2, a lipid-activated transcription factor
    • Tontonoz, P., Hu, E., and Spiegelman, B. M. (1994) Stimulation of adipogenesis in fibroblasts by PPAR-2, a lipid-activated transcription factor. Cell 79, 1147-1156
    • (1994) Cell , vol.79 , pp. 1147-1156
    • Tontonoz, P.1    Hu, E.2    Spiegelman, B.M.3
  • 26
    • 73249134379 scopus 로고    scopus 로고
    • Experimental determination of the evolvability of a transcription factor
    • Maerkl, S. J., and Quake, S. R. (2009) Experimental determination of the evolvability of a transcription factor. Proc. Natl. Acad. Sci. U.S.A. 106, 18650-18655
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 18650-18655
    • Maerkl, S.J.1    Quake, S.R.2
  • 30
    • 55749101777 scopus 로고    scopus 로고
    • Genome-wide profiling of PPAR-:RXR and RNApolymerase II occupancy reveals temporal activation of distinct metabolic pathways and changes in RXR dimer composition during adipogenesis
    • Nielsen, R., Pedersen, T. A., Hagenbeek, D., Moulos, P., Siersbaek, R., Megens, E., Denissov, S., Børgesen, M., Francoijs, K. J., Mandrup, S., and Stunnenberg, H. G. (2008) Genome-wide profiling of PPAR-:RXR and RNApolymerase II occupancy reveals temporal activation of distinct metabolic pathways and changes in RXR dimer composition during adipogenesis. Genes Dev. 22, 2953-2967
    • (2008) Genes Dev. , vol.22 , pp. 2953-2967
    • Nielsen, R.1    Pedersen, T.A.2    Hagenbeek, D.3    Moulos, P.4    Siersbaek, R.5    Megens, E.6    Denissov, S.7    Børgesen, M.8    Francoijs, K.J.9    Mandrup, S.10    Stunnenberg, H.G.11
  • 31
    • 84860783115 scopus 로고    scopus 로고
    • Integrative genomics identifies the corepressor SMRT as a gatekeeper of adipogenesis through the transcription factors C/EBP and KAISO
    • Raghav, S. K., Waszak, S. M., Krier, I., Gubelmann, C., Isakova, A., Mikkelsen, T. S., and Deplancke, B. (2012) Integrative genomics identifies the corepressor SMRT as a gatekeeper of adipogenesis through the transcription factors C/EBP and KAISO. Mol. Cell 46, 335-350
    • (2012) Mol. Cell , vol.46 , pp. 335-350
    • Raghav, S.K.1    Waszak, S.M.2    Krier, I.3    Gubelmann, C.4    Isakova, A.5    Mikkelsen, T.S.6    Deplancke, B.7
  • 32
    • 84899799231 scopus 로고    scopus 로고
    • A comparative analysis of transcription factor binding models learned from PBM HT-SELEX and ChIP data
    • 10.1093/nar/gku117
    • Orenstein, Y., and Shamir, R. (2014) A comparative analysis of transcription factor binding models learned from PBM, HT-SELEX and ChIP data. Nucleic Acids Res. 10.1093/nar/gku117
    • (2014) Nucleic Acids Res.
    • Orenstein, Y.1    Shamir, R.2
  • 33
    • 44649137302 scopus 로고    scopus 로고
    • Identification of novel PPAR-target genes by integrated analysis of ChIP-on-chip and microarray expression data during adipocyte differentiation
    • Nakachi, Y., Yagi, K., Nikaido, I., Bono, H., Tonouchi, M., Schönbach, C., and Okazaki, Y. (2008) Identification of novel PPAR-target genes by integrated analysis of ChIP-on-chip and microarray expression data during adipocyte differentiation. Biochem. Biophys. Res. Commun. 372, 362-366
    • (2008) Biochem. Biophys. Res. Commun. , vol.372 , pp. 362-366
    • Nakachi, Y.1    Yagi, K.2    Nikaido, I.3    Bono, H.4    Tonouchi, M.5    Schönbach, C.6    Okazaki, Y.7
  • 35
    • 0029294531 scopus 로고
    • Peroxisome proliferator activated receptors: Transcriptional regulators of adipogenesis, lipid metabolism and more
    • Wahli, W., Braissant, O., and Desvergne, B. (1995) Peroxisome proliferator activated receptors: Transcriptional regulators of adipogenesis, lipid metabolism and more. Chem. Biol. 2, 261-266
    • (1995) Chem. Biol. , vol.2 , pp. 261-266
    • Wahli, W.1    Braissant, O.2    Desvergne, B.3
  • 37
    • 50449108231 scopus 로고    scopus 로고
    • The Pal3 promoter sequence is critical for the regulation of human renin gene transcription by peroxisome proliferator-activated receptor
    • Todorov, V. T., Desch, M., Schubert, T., and Kurtz, A. (2008) The Pal3 promoter sequence is critical for the regulation of human renin gene transcription by peroxisome proliferator-activated receptor-. Endocrinology 149, 4647-4657
    • (2008) Endocrinology , vol.149 , pp. 4647-4657
    • Todorov, V.T.1    Desch, M.2    Schubert, T.3    Kurtz, A.4
  • 38
    • 0035863060 scopus 로고    scopus 로고
    • Dual DNA-binding specificity of peroxisome-proliferator-activated receptor-controlled by heterodimer formation with retinoid X receptor
    • Okuno, M., Arimoto, E., Ikenobu, Y., Nishihara, T., and Imagawa, M. (2001) Dual DNA-binding specificity of peroxisome-proliferator-activated receptor-controlled by heterodimer formation with retinoid X receptor-. Biochem. J. 353, 193-198
    • (2001) Biochem. J. , vol.353 , pp. 193-198
    • Okuno, M.1    Arimoto, E.2    Ikenobu, Y.3    Nishihara, T.4    Imagawa, M.5
  • 41
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptors
    • Mangelsdorf, D. J., and Evans, R. M. (1995) The RXR heterodimers and orphan receptors. Cell 83, 841-850
    • (1995) Cell , vol.83 , pp. 841-850
    • Mangelsdorf, D.J.1    Evans, R.M.2
  • 42
    • 0029736983 scopus 로고    scopus 로고
    • Two distinct dimerization interfaces differentially modulate target gene specificity of nuclear hormone receptors
    • Perlmann, T., Umesono, K., Rangarajan, P. N., Forman, B. M., and Evans, R. M. (1996) Two distinct dimerization interfaces differentially modulate target gene specificity of nuclear hormone receptors. Mol. Endocrinol. 10, 958-966
    • (1996) Mol. Endocrinol. , vol.10 , pp. 958-966
    • Perlmann, T.1    Umesono, K.2    Rangarajan, P.N.3    Forman, B.M.4    Evans, R.M.5
  • 43
    • 0034161266 scopus 로고    scopus 로고
    • Structure of the RXR-RAR DNA-binding complex on the retinoic acid response element DR1
    • Rastinejad, F., Wagner, T., Zhao, Q., and Khorasanizadeh, S. (2000) Structure of the RXR-RAR DNA-binding complex on the retinoic acid response element DR1. EMBO J. 19, 1045-1054
    • (2000) EMBO J. , vol.19 , pp. 1045-1054
    • Rastinejad, F.1    Wagner, T.2    Zhao, Q.3    Khorasanizadeh, S.4
  • 46
    • 84859241581 scopus 로고    scopus 로고
    • Probing the informational and regulatory plasticity of a transcription factor DNA-binding domain
    • Shultzaberger, R. K., Maerkl, S. J., Kirsch, J. F., and Eisen, M. B. (2012) Probing the informational and regulatory plasticity of a transcription factor DNA-binding domain. PLoS Genet. 8, e1002614
    • (2012) PLoS Genet. , vol.8 , pp. e1002614
    • Shultzaberger, R.K.1    Maerkl, S.J.2    Kirsch, J.F.3    Eisen, M.B.4
  • 48
    • 0021531796 scopus 로고
    • Genetically structured models for lac promoter-operator function in the chromosome and in multicopy plasmids: Lac operator function
    • Lee, S. B., and Bailey, J. E. (1984) Genetically structured models for lac promoter-operator function in the chromosome and in multicopy plasmids: Lac operator function. Biotechnol. Bioeng. 26, 1372-1382
    • (1984) Biotechnol. Bioeng. , vol.26 , pp. 1372-1382
    • Lee, S.B.1    Bailey, J.E.2
  • 49
    • 84875619226 scopus 로고    scopus 로고
    • MAFFT multiple sequence alignment software, Version 7: Improvements in performance and usability
    • Katoh, K., and Standley, D. M. (2013) MAFFT multiple sequence alignment software, Version 7: Improvements in performance and usability. Mol. Biol. Evol. 30, 772-780
    • (2013) Mol. Biol. Evol. , vol.30 , pp. 772-780
    • Katoh, K.1    Standley, D.M.2
  • 50
    • 0028685490 scopus 로고
    • Fitting a mixture model by expectation maximization to discover motifs in biopolymers
    • Bailey, T. L., and Elkan, C. (1994) Fitting a mixture model by expectation maximization to discover motifs in biopolymers. Proc. Int. Conf. Intell. Syst. Mol. Biol. 2, 28-36
    • (1994) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.2 , pp. 28-36
    • Bailey, T.L.1    Elkan, C.2
  • 51
    • 84874072709 scopus 로고    scopus 로고
    • Crystal structures of the DNA-binding domain tetramer of the p53 tumor suppressor family member p73 bound to different full-site response elements
    • Ethayathulla, A. S., Nguyen, H. T., and Viadiu, H. (2013) Crystal structures of the DNA-binding domain tetramer of the p53 tumor suppressor family member p73 bound to different full-site response elements. J. Biol. Chem. 288, 4744-4754
    • (2013) J. Biol. Chem. , vol.288 , pp. 4744-4754
    • Ethayathulla, A.S.1    Nguyen, H.T.2    Viadiu, H.3
  • 53
    • 33745161824 scopus 로고    scopus 로고
    • Dimerization-induced corepressor binding and relaxed DNA-binding specificity are critical for PML/RARA-induced immortalization
    • Zhou, J., Pérès, L., Honoré, N., Nasr, R., Zhu, J., and De Thé, H. (2006) Dimerization-induced corepressor binding and relaxed DNA-binding specificity are critical for PML/RARA-induced immortalization. Proc. Natl. Acad. Sci. U.S.A. 103, 9238-9243
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 9238-9243
    • Zhou, J.1    Pérès, L.2    Honoré, N.3    Nasr, R.4    Zhu, J.5    De Thé, H.6
  • 54
    • 84895810018 scopus 로고    scopus 로고
    • Protein-DNA binding: Complexities and multi-protein codes
    • Siggers, T., and Gordân, R. (2014) Protein-DNA binding: Complexities and multi-protein codes. Nucleic Acids Res. 42, 2099-2111
    • (2014) Nucleic Acids Res. , vol.42 , pp. 2099-2111
    • Siggers, T.1    Gordân, R.2
  • 55
    • 0035830451 scopus 로고    scopus 로고
    • Kinetic studies of Fos. Jun. DNA complex formation: DNA binding prior to dimerization
    • Kohler, J. J., and Schepartz, A. (2001) Kinetic studies of Fos. Jun. DNA complex formation: DNA binding prior to dimerization. Biochemistry 40, 130-142
    • (2001) Biochemistry , vol.40 , pp. 130-142
    • Kohler, J.J.1    Schepartz, A.2
  • 56
    • 0031030809 scopus 로고    scopus 로고
    • Certain bZIP peptides bind DNA sequentially as monomers and dimerize on the DNA
    • Metallo, S. J., and Schepartz, A. (1997) Certain bZIP peptides bind DNA sequentially as monomers and dimerize on the DNA. Nat. Struct. Biol. 4, 115-117
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 115-117
    • Metallo, S.J.1    Schepartz, A.2
  • 57
    • 0029044997 scopus 로고
    • Structural determinants of nuclear receptor assembly on DNA direct repeats
    • Rastinejad, F., Perlmann, T., Evans, R. M., and Sigler, P. B. (1995) Structural determinants of nuclear receptor assembly on DNA direct repeats. Nature 375, 203-211
    • (1995) Nature , vol.375 , pp. 203-211
    • Rastinejad, F.1    Perlmann, T.2    Evans, R.M.3    Sigler, P.B.4
  • 58
    • 0029894315 scopus 로고    scopus 로고
    • Sequence requirements for high affinity retinoid X receptor-homodimer binding
    • Castelein, H., Janssen, A., Declercq, P. E., and Baes, M. (1996) Sequence requirements for high affinity retinoid X receptor-homodimer binding. Mol. Cell. Endocrinol. 119, 11-20
    • (1996) Mol. Cell. Endocrinol. , vol.119 , pp. 11-20
    • Castelein, H.1    Janssen, A.2    Declercq, P.E.3    Baes, M.4
  • 59
    • 84855937177 scopus 로고    scopus 로고
    • A mechanistic model for enzymatic saccharification of cellulose using continuous distribution kinetics I: Depolymerization by EGI and CBHI
    • Griggs, A. J., Stickel, J. J., and Lischeske, J. J. (2012) A mechanistic model for enzymatic saccharification of cellulose using continuous distribution kinetics I: Depolymerization by EGI and CBHI. Biotechnol. Bioeng. 109, 665-675
    • (2012) Biotechnol. Bioeng. , vol.109 , pp. 665-675
    • Griggs, A.J.1    Stickel, J.J.2    Lischeske, J.J.3
  • 60
    • 84883800631 scopus 로고    scopus 로고
    • Towards kinetic modeling of genome-scale metabolic networks without sacrificing stoichiometric, thermodynamic and physiological constraints
    • Chakrabarti, A., Miskovic, L., Soh, K. C., and Hatzimanikatis, V. (2013) Towards kinetic modeling of genome-scale metabolic networks without sacrificing stoichiometric, thermodynamic and physiological constraints. Biotechnol. J. 8, 1043-1057
    • (2013) Biotechnol. J. , vol.8 , pp. 1043-1057
    • Chakrabarti, A.1    Miskovic, L.2    Soh, K.C.3    Hatzimanikatis, V.4
  • 61
    • 77957930021 scopus 로고    scopus 로고
    • A mechanistic model of PCR for accurate quantification of quantitative PCR data
    • Boggy, G. J., and Woolf, P. J. (2010) A mechanistic model of PCR for accurate quantification of quantitative PCR data. PLoS ONE 5, e12355
    • (2010) PLoS ONE , vol.5 , pp. e12355
    • Boggy, G.J.1    Woolf, P.J.2
  • 62
    • 1242339621 scopus 로고    scopus 로고
    • Determination of binding constant of transcription factor myc-max/max-max and E-box DNA: The effect of inhibitors on the binding
    • Park, S., Chung, S., Kim, K. M., Jung, K.-C., Park, C., Hahm, E.-R., and Yang, C.-H. (2004) Determination of binding constant of transcription factor myc-max/max-max and E-box DNA: The effect of inhibitors on the binding. Biochim. Biophys. Acta 1670, 217-228
    • (2004) Biochim. Biophys. Acta , vol.1670 , pp. 217-228
    • Park, S.1    Chung, S.2    Kim, K.M.3    Jung, K.-C.4    Park, C.5    Hahm, E.-R.6    Yang, C.-H.7
  • 63
    • 77949867499 scopus 로고    scopus 로고
    • Kinetic analysis of the interaction of b/HLH/Z transcription factors Myc, Max, and Mad with cognate DNA
    • Ecevit, O., Khan, M. A., and Goss, D. J. (2010) Kinetic analysis of the interaction of b/HLH/Z transcription factors Myc, Max, and Mad with cognate DNA. Biochemistry 49, 2627-2635
    • (2010) Biochemistry , vol.49 , pp. 2627-2635
    • Ecevit, O.1    Khan, M.A.2    Goss, D.J.3
  • 64
    • 0032580207 scopus 로고    scopus 로고
    • Allosteric effects of DNA on transcriptional regulators
    • Lefstin, J. A., and Yamamoto, K. R. (1998) Allosteric effects of DNA on transcriptional regulators. Nature 392, 885-888
    • (1998) Nature , vol.392 , pp. 885-888
    • Lefstin, J.A.1    Yamamoto, K.R.2
  • 65
    • 4644252538 scopus 로고    scopus 로고
    • One nucleotide in a-B site can determine cofactor specificity for NF-B dimers
    • Leung, T. H., Hoffmann, A., and Baltimore, D. (2004) One nucleotide in a-B site can determine cofactor specificity for NF-B dimers. Cell 118, 453-464
    • (2004) Cell , vol.118 , pp. 453-464
    • Leung, T.H.1    Hoffmann, A.2    Baltimore, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.