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Volumn 48, Issue 27, 2009, Pages 6348-6360

Mechanism of strand-specific smooth muscle α-actin enhancer interaction by purine-rich element binding protein B (Purβ)

Author keywords

[No Author keywords available]

Indexed keywords

BAND SHIFT; BINDING PROTEINS; COOPERATIVITY; DNA COMPLEX; DNA STRUCTURE; DNA-BINDING SPECIFICITY; ELEMENT-BINDING PROTEINS; FLANKING REGIONS; INTRINSIC BINDING; MECHANICAL ANALYSIS; POLYPYRIMIDINE; SEQUENCE DETERMINANTS; SMOOTH MUSCLES; VASCULAR SMOOTH MUSCLE CELLS;

EID: 67650070487     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900708j     Document Type: Article
Times cited : (11)

References (62)
  • 1
    • 0026600969 scopus 로고
    • The HeLa pur factor binds single-stranded DNA at a specific element conserved in gene flanking regions and orgins of DNA replication
    • Bergemann, A. D., and Johnson, E. M. (1992) The HeLa pur factor binds single-stranded DNA at a specific element conserved in gene flanking regions and orgins of DNA replication. Mol. Cell. Biol. 12, 1257-1265.
    • (1992) Mol. Cell. Biol , vol.12 , pp. 1257-1265
    • Bergemann, A.D.1    Johnson, E.M.2
  • 2
    • 0026766653 scopus 로고
    • Binding of single-stranded oligonucleotides to a non-B-form DNA structure results in loss of promoter activity of the platelet-derived growth factor A-chain gene
    • Wang, Z. Y., Lin, X. H., Nobyuoshi, M., Qui, Q. Q., and Deuel, T. F. (1992) Binding of single-stranded oligonucleotides to a non-B-form DNA structure results in loss of promoter activity of the platelet-derived growth factor A-chain gene. J. Biol. Chem. 267, 13669-13674.
    • (1992) J. Biol. Chem , vol.267 , pp. 13669-13674
    • Wang, Z.Y.1    Lin, X.H.2    Nobyuoshi, M.3    Qui, Q.Q.4    Deuel, T.F.5
  • 3
    • 0029998428 scopus 로고    scopus 로고
    • Multiple single-stranded cis elements are associated with activated chromatin of the human c-myc gene in vivo
    • Michelotti, G. A., Michelotti, E. F., Pullner, A., Duncan, R. C., Eick, D., and Levens, D. (1996) Multiple single-stranded cis elements are associated with activated chromatin of the human c-myc gene in vivo. Mol. Cell. Biol. 16, 2656-2669.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 2656-2669
    • Michelotti, G.A.1    Michelotti, E.F.2    Pullner, A.3    Duncan, R.C.4    Eick, D.5    Levens, D.6
  • 4
    • 0031032680 scopus 로고    scopus 로고
    • Functional role of a conformationally flexible homopurine/homopyrimidine domain of the androgen receptor gene promoter interacting with Sp1 and a pyrimidine single strand DNA-binding protein
    • Chen, S., Supakar, P. C., Vellanoweth, R. L., Song, C. S., Chatterjee, B., and Roy, A. K. (1997) Functional role of a conformationally flexible homopurine/homopyrimidine domain of the androgen receptor gene promoter interacting with Sp1 and a pyrimidine single strand DNA-binding protein. Mol. Endocrinol. 11, 3-15.
    • (1997) Mol. Endocrinol , vol.11 , pp. 3-15
    • Chen, S.1    Supakar, P.C.2    Vellanoweth, R.L.3    Song, C.S.4    Chatterjee, B.5    Roy, A.K.6
  • 5
    • 0037192176 scopus 로고    scopus 로고
    • A polypyrimidine/polypurine tract within the Hmga2 minimal promoter: A common feature of many growth-related genes
    • Rustighi, A., Tessari, M. A., Vascotto, F., Sgarra, R., Giancotti, V., and Manfioletti, G. (2002) A polypyrimidine/polypurine tract within the Hmga2 minimal promoter: a common feature of many growth-related genes. Biochemistry 41, 1229-1240.
    • (2002) Biochemistry , vol.41 , pp. 1229-1240
    • Rustighi, A.1    Tessari, M.A.2    Vascotto, F.3    Sgarra, R.4    Giancotti, V.5    Manfioletti, G.6
  • 6
    • 27244435211 scopus 로고    scopus 로고
    • Facilitation of a structural transition in the polypurine/polypyrimidine tract within the proximal promoter region of the human VEGF gene by the presence of potassium and G-quadruplex-interactive agents
    • Sun, D., Guo, K., Rusche, J. J., and Hurley, L.H. (2005) Facilitation of a structural transition in the polypurine/polypyrimidine tract within the proximal promoter region of the human VEGF gene by the presence of potassium and G-quadruplex-interactive agents. Nucleic Acids Res. 33, 6070-6080.
    • (2005) Nucleic Acids Res , vol.33 , pp. 6070-6080
    • Sun, D.1    Guo, K.2    Rusche, J.J.3    Hurley, L.H.4
  • 7
    • 0027182876 scopus 로고
    • Specific binding of heterogeneous ribonucleoprotein particle protein K to the human c-myc promoter in vitro
    • Takimoto, M., Tomonaga, T., Matunis, M., Avigan, M., Krutzsch, H., Dreyfuss, G., and Levens, D. (1993) Specific binding of heterogeneous ribonucleoprotein particle protein K to the human c-myc promoter in vitro. J. Biol. Chem. 268, 18249-18258.
    • (1993) J. Biol. Chem , vol.268 , pp. 18249-18258
    • Takimoto, M.1    Tomonaga, T.2    Matunis, M.3    Avigan, M.4    Krutzsch, H.5    Dreyfuss, G.6    Levens, D.7
  • 8
    • 0028349865 scopus 로고
    • Identification and cDNA cloning of single-stranded DNA binding proteins that interact with the region upstream of the human c-myc gene
    • Negishi, Y., Nishita, Y., Saegusa, Y., Kakizaki, I., Galli, I., Kihara, F., Tamai, K., Miyajima, N., Iguchi-Ariga, S. M., and Ariga, H. (1994) Identification and cDNA cloning of single-stranded DNA binding proteins that interact with the region upstream of the human c-myc gene. Oncogene 9, 1133-1143.
    • (1994) Oncogene , vol.9 , pp. 1133-1143
    • Negishi, Y.1    Nishita, Y.2    Saegusa, Y.3    Kakizaki, I.4    Galli, I.5    Kihara, F.6    Tamai, K.7    Miyajima, N.8    Iguchi-Ariga, S.M.9    Ariga, H.10
  • 9
    • 0028909518 scopus 로고
    • Cellular nucleic acid binding protein regulates the CT element of the human c-myc protooncogene
    • Michelotti, E. F., Tomonaga, T., Krutzsch, H., and Levens, D. (1995) Cellular nucleic acid binding protein regulates the CT element of the human c-myc protooncogene. J. Biol. Chem. 270, 9494-9499.
    • (1995) J. Biol. Chem , vol.270 , pp. 9494-9499
    • Michelotti, E.F.1    Tomonaga, T.2    Krutzsch, H.3    Levens, D.4
  • 10
    • 0028897341 scopus 로고
    • The transcriptional regulatory protein, YB-1, promotes single-stranded regions in the DRA promoter
    • MacDonald, G. H., Itoh-Lindstrom, Y., and Ting, J. P. (1995) The transcriptional regulatory protein, YB-1, promotes single-stranded regions in the DRA promoter. J. Biol. Chem. 270, 3527-3533.
    • (1995) J. Biol. Chem , vol.270 , pp. 3527-3533
    • MacDonald, G.H.1    Itoh-Lindstrom, Y.2    Ting, J.P.3
  • 11
    • 0031940086 scopus 로고    scopus 로고
    • Role of single-stranded DNA regions and Y-box proteins in transcriptional regulation of viral and cellular genes
    • Swamynathan, S. K., Nambiar, A., and Guntaka, R. V. (1998) Role of single-stranded DNA regions and Y-box proteins in transcriptional regulation of viral and cellular genes. FASEB J. 12, 515-522.
    • (1998) FASEB J , vol.12 , pp. 515-522
    • Swamynathan, S.K.1    Nambiar, A.2    Guntaka, R.V.3
  • 12
    • 15744373012 scopus 로고    scopus 로고
    • Purα activates PDGF-A gene transcription via interactions with a G-rich, single-stranded region of the promoter
    • Zhang, Q., Pedigo, N., Shenoy, S., Khalili, K., and Kaetzel, D. M. (2005) Purα activates PDGF-A gene transcription via interactions with a G-rich, single-stranded region of the promoter. Gene 348, 25-32.
    • (2005) Gene , vol.348 , pp. 25-32
    • Zhang, Q.1    Pedigo, N.2    Shenoy, S.3    Khalili, K.4    Kaetzel, D.M.5
  • 13
    • 0037040986 scopus 로고    scopus 로고
    • Carlini, L. E., Getz, M. J., Strauch, A. R., and Kelm, R. J.Jr. (2002) Cryptic MCAT enhancer regulation in fibroblasts and smooth muscle cells. Suppression of TEF-1 mediated activation by the single-stranded DNA-binding proteins, Purα, Purβ, and MSY1. J. Biol. Chem. 277, 8682-8692.
    • Carlini, L. E., Getz, M. J., Strauch, A. R., and Kelm, R. J.Jr. (2002) Cryptic MCAT enhancer regulation in fibroblasts and smooth muscle cells. Suppression of TEF-1 mediated activation by the single-stranded DNA-binding proteins, Purα, Purβ, and MSY1. J. Biol. Chem. 277, 8682-8692.
  • 14
    • 0242581729 scopus 로고    scopus 로고
    • Single-stranded DNA-binding proteins Purα and Purβ bind to a purine-rich negative regulatory element of the α-myosin heavy chain gene and control transcriptional and translational regulation of gene expression
    • Gupta, M., Sueblinvong, V., Raman, J., Jeevanandam, J., and Gupta, M. P. (2003) Single-stranded DNA-binding proteins Purα and Purβ bind to a purine-rich negative regulatory element of the α-myosin heavy chain gene and control transcriptional and translational regulation of gene expression. J. Biol. Chem. 278, 44935-44948.
    • (2003) J. Biol. Chem , vol.278 , pp. 44935-44948
    • Gupta, M.1    Sueblinvong, V.2    Raman, J.3    Jeevanandam, J.4    Gupta, M.P.5
  • 15
    • 33846914356 scopus 로고    scopus 로고
    • Purα and Purβ collaborate with Sp3 to negatively regulate β-myosin heavy chain gene expression during skeletal muscle inactivity
    • Ji, J., Tsika, G. L., Rindt, H., Schreiber, K. L., McCarthy, J. J., Kelm, R. J.Jr., and Tsika, R. (2007) Purα and Purβ collaborate with Sp3 to negatively regulate β-myosin heavy chain gene expression during skeletal muscle inactivity. Mol. Cell. Biol. 27, 1531-1543.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 1531-1543
    • Ji, J.1    Tsika, G.L.2    Rindt, H.3    Schreiber, K.L.4    McCarthy, J.J.5    Kelm Jr., R.J.6    Tsika, R.7
  • 16
    • 0036267823 scopus 로고    scopus 로고
    • Reprogramming of vascular smooth muscle α-actin gene expression as an early indicator of dysfunctional remodeling following heart transplant
    • Subramanian, S. V., Kelm, R. J.Jr., Polikandriotis, J. A., Orosz, C. G., and Strauch, A. R. (2002) Reprogramming of vascular smooth muscle α-actin gene expression as an early indicator of dysfunctional remodeling following heart transplant. Cardiovasc. Res. 54, 539-548.
    • (2002) Cardiovasc. Res , vol.54 , pp. 539-548
    • Subramanian, S.V.1    Kelm Jr., R.J.2    Polikandriotis, J.A.3    Orosz, C.G.4    Strauch, A.R.5
  • 17
    • 4644308155 scopus 로고    scopus 로고
    • Induction of vascular smooth muscle α-actin gene transcription in transforming growth factor β1-activated myofibroblasts mediated by dynamic interplay between the Pur repressor proteins and Sp1/Smad coactivators
    • Subramanian, S. V., Polikandriotis, J. A., Kelm, R. J.Jr., David, J. J., Orosz, C. G., and Strauch, A. R. (2004) Induction of vascular smooth muscle α-actin gene transcription in transforming growth factor β1-activated myofibroblasts mediated by dynamic interplay between the Pur repressor proteins and Sp1/Smad coactivators. Mol. Biol. Cell 15, 4532-4543.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4532-4543
    • Subramanian, S.V.1    Polikandriotis, J.A.2    Kelm Jr., R.J.3    David, J.J.4    Orosz, C.G.5    Strauch, A.R.6
  • 19
    • 0028966571 scopus 로고
    • Negative regulation of the vascular smooth muscle α-actin gene in fibroblasts and myoblasts: Disruption of enhancer function by sequence-specific single-stranded DNA-binding proteins
    • Sun, S., Stoflet, E. S., Cogan, J. G., Strauch, A. R., and Getz, M. J. (1995) Negative regulation of the vascular smooth muscle α-actin gene in fibroblasts and myoblasts: disruption of enhancer function by sequence-specific single-stranded DNA-binding proteins. Mol. Cell. Biol. 15, 2429-2436.
    • (1995) Mol. Cell. Biol , vol.15 , pp. 2429-2436
    • Sun, S.1    Stoflet, E.S.2    Cogan, J.G.3    Strauch, A.R.4    Getz, M.J.5
  • 20
    • 0034685774 scopus 로고    scopus 로고
    • Altered sensitivity to single-strand-specific reagents associated with the genomic vascular smooth muscle α-actin promoter during myofibroblast differentiation
    • Becker, N. A., Kelm, R. J.Jr., Vrana, J. A., Getz, M. J., and Maher, L. J.III (2000) Altered sensitivity to single-strand-specific reagents associated with the genomic vascular smooth muscle α-actin promoter during myofibroblast differentiation. J. Biol. Chem. 275, 15384-15391.
    • (2000) J. Biol. Chem , vol.275 , pp. 15384-15391
    • Becker, N.A.1    Kelm Jr., R.J.2    Vrana, J.A.3    Getz, M.J.4    Maher III, L.J.5
  • 21
    • 0040143457 scopus 로고    scopus 로고
    • Molecular interactions between single-stranded DNA-binding proteins associated with an essential MCAT element in the mouse smooth muscle α-actin promoter
    • Kelm, R. J.Jr., Cogan, J. J., Elder, P. K., Strauch, A. R., and Getz, M. J. (1999) Molecular interactions between single-stranded DNA-binding proteins associated with an essential MCAT element in the mouse smooth muscle α-actin promoter. J. Biol. Chem. 274, 14238-14245.
    • (1999) J. Biol. Chem , vol.274 , pp. 14238-14245
    • Kelm Jr., R.J.1    Cogan, J.J.2    Elder, P.K.3    Strauch, A.R.4    Getz, M.J.5
  • 22
    • 0141643216 scopus 로고    scopus 로고
    • Structure/function analysis of mouse Purβ, a single-stranded DNA-binding repressor of vascular smooth muscle α-actin gene transcription
    • Kelm, R. J.Jr., Wang, S. X., Polikandriotis, J. A., and Strauch, A. R. (2003) Structure/function analysis of mouse Purβ, a single-stranded DNA-binding repressor of vascular smooth muscle α-actin gene transcription. J. Biol. Chem. 278, 38749-38757.
    • (2003) J. Biol. Chem , vol.278 , pp. 38749-38757
    • Kelm Jr., R.J.1    Wang, S.X.2    Polikandriotis, J.A.3    Strauch, A.R.4
  • 23
    • 33646378910 scopus 로고    scopus 로고
    • Nucleoprotein interactions governing cell type-dependent repression of the mouse smooth muscle α-actin promoter by single-stranded DNA-binding proteins Purα and Purβ
    • Knapp, A. M., Ramsey, J. E., Wang, S. X., Godburn, K. E., Strauch, A. R., and Kelm, R. J.Jr. (2006) Nucleoprotein interactions governing cell type-dependent repression of the mouse smooth muscle α-actin promoter by single-stranded DNA-binding proteins Purα and Purβ. J. Biol. Chem. 281, 7907-7918.
    • (2006) J. Biol. Chem , vol.281 , pp. 7907-7918
    • Knapp, A.M.1    Ramsey, J.E.2    Wang, S.X.3    Godburn, K.E.4    Strauch, A.R.5    Kelm Jr., R.J.6
  • 24
    • 37249046362 scopus 로고    scopus 로고
    • Knapp, A. M., Ramsey, J. E., Wang, S. X., Strauch, A. R., and Kelm, R. J.Jr. (2007) Structure-function analysis of mouse Purβ II. Conformation altering mutations disrupt single-stranded DNA and protein interactions crucial to smooth muscle α-actin gene repression. J. Biol. Chem. 282, 35899-35909.
    • Knapp, A. M., Ramsey, J. E., Wang, S. X., Strauch, A. R., and Kelm, R. J.Jr. (2007) Structure-function analysis of mouse Purβ II. Conformation altering mutations disrupt single-stranded DNA and protein interactions crucial to smooth muscle α-actin gene repression. J. Biol. Chem. 282, 35899-35909.
  • 25
    • 33847275685 scopus 로고    scopus 로고
    • Hydrodynamic studies on the quaternary structure of recombinant mouse Purβ
    • Ramsey, J. E., Daugherty, M. A., and Kelm, R. J.Jr. (2007) Hydrodynamic studies on the quaternary structure of recombinant mouse Purβ. J. Biol. Chem. 282, 1552-1560.
    • (2007) J. Biol. Chem , vol.282 , pp. 1552-1560
    • Ramsey, J.E.1    Daugherty, M.A.2    Kelm Jr., R.J.3
  • 26
    • 0024342726 scopus 로고
    • Direct solid phase sequencing of genomic and plasmid DNA using magnetic beads as solid support
    • Hultman, T., Stahl, S., Hornes, E., and Uhlen, M. (1989) Direct solid phase sequencing of genomic and plasmid DNA using magnetic beads as solid support. Nucleic Acids Res. 17, 4937-4946.
    • (1989) Nucleic Acids Res , vol.17 , pp. 4937-4946
    • Hultman, T.1    Stahl, S.2    Hornes, E.3    Uhlen, M.4
  • 27
    • 0028939479 scopus 로고
    • Metastable single-strand DNA conformational polymorphism analysis results in enhanced polymorphism detection
    • Kasuga, T., Cheng, J., and Mitchelson, K. R. (1995) Metastable single-strand DNA conformational polymorphism analysis results in enhanced polymorphism detection. PCR Methods Appl. 4, 227-233.
    • (1995) PCR Methods Appl , vol.4 , pp. 227-233
    • Kasuga, T.1    Cheng, J.2    Mitchelson, K.R.3
  • 28
    • 0030830141 scopus 로고    scopus 로고
    • Targeted overexpression of IGF-I evokes distinct patterns of organ remodeling in smooth muscle cell tissue beds of transgenic mice
    • Wang, J., Niu, W., Nikiforov, Y., Naito, S., Chernausek, S., Witte, D., LeRoith, D., Strauch, A., and Fagin, J. A. (1997) Targeted overexpression of IGF-I evokes distinct patterns of organ remodeling in smooth muscle cell tissue beds of transgenic mice. J. Clin. Invest. 100, 1425-1439.
    • (1997) J. Clin. Invest , vol.100 , pp. 1425-1439
    • Wang, J.1    Niu, W.2    Nikiforov, Y.3    Naito, S.4    Chernausek, S.5    Witte, D.6    LeRoith, D.7    Strauch, A.8    Fagin, J.A.9
  • 29
    • 38749146474 scopus 로고    scopus 로고
    • Predicting ultraviolet spectrum of single stranded and double stranded deoxyribonucleic acids
    • Tataurov, A. V., You, Y., and Owczarzy, R. (2008) Predicting ultraviolet spectrum of single stranded and double stranded deoxyribonucleic acids. Biophys. Chem. 133, 66-70.
    • (2008) Biophys. Chem , vol.133 , pp. 66-70
    • Tataurov, A.V.1    You, Y.2    Owczarzy, R.3
  • 31
    • 0025768548 scopus 로고
    • Determination of binding constants for cooperative site-specific protein-DNA interactions using the gel mobility-shift assay
    • Senear, D. F., and Brenowitz, M. (1991) Determination of binding constants for cooperative site-specific protein-DNA interactions using the gel mobility-shift assay. J. Biol. Chem. 266, 13661-13671.
    • (1991) J. Biol. Chem , vol.266 , pp. 13661-13671
    • Senear, D.F.1    Brenowitz, M.2
  • 32
    • 0030768931 scopus 로고    scopus 로고
    • The Hill equation revisited: Uses and misuses
    • Weiss, J. N. (1997) The Hill equation revisited: uses and misuses. FASEB J. 11, 835-841.
    • (1997) FASEB J , vol.11 , pp. 835-841
    • Weiss, J.N.1
  • 33
    • 0019878376 scopus 로고
    • Equilibria and kinetics of lac repressor-operator interactions by polyacrylamide gel electrophoresis
    • Fried, M., and Crothers, D. M. (1981) Equilibria and kinetics of lac repressor-operator interactions by polyacrylamide gel electrophoresis. Nucleic Acids Res. 9, 6505-6525.
    • (1981) Nucleic Acids Res , vol.9 , pp. 6505-6525
    • Fried, M.1    Crothers, D.M.2
  • 34
    • 0037424237 scopus 로고    scopus 로고
    • DNA-binding mechanism of O6-alkylguanine-DNA alkyltransferase. Effects of protein and DNA alkylation on complex stability
    • Rasimas, J. J., Pegg, A. E., and Fried, M. G. (2003) DNA-binding mechanism of O6-alkylguanine-DNA alkyltransferase. Effects of protein and DNA alkylation on complex stability. J. Biol. Chem. 278, 7973-7980.
    • (2003) J. Biol. Chem , vol.278 , pp. 7973-7980
    • Rasimas, J.J.1    Pegg, A.E.2    Fried, M.G.3
  • 35
    • 0001422329 scopus 로고
    • Quantitative model for gene regulation by lambda phage repressor
    • Ackers, G. K., Johnson, A. D., and Shea, M. A. (1982) Quantitative model for gene regulation by lambda phage repressor. Proc. Natl. Acad. Sci. U.S.A. 79, 1129-1133.
    • (1982) Proc. Natl. Acad. Sci. U.S.A , vol.79 , pp. 1129-1133
    • Ackers, G.K.1    Johnson, A.D.2    Shea, M.A.3
  • 36
    • 0022851259 scopus 로고
    • Energetics of cooperative protein-DNA interactions: Comparison between quantitative deoxyribonuclease footprint titration and filter binding
    • Senear, D. F., Brenowitz, M., Shea, M. A., and Ackers, G. K. (1986) Energetics of cooperative protein-DNA interactions: comparison between quantitative deoxyribonuclease footprint titration and filter binding. Biochemistry 25, 7344-7354.
    • (1986) Biochemistry , vol.25 , pp. 7344-7354
    • Senear, D.F.1    Brenowitz, M.2    Shea, M.A.3    Ackers, G.K.4
  • 38
    • 0022437260 scopus 로고
    • Quantitative DNase footprint titration: A method for studying protein-DNA interactions
    • Brenowitz, M., Senear, D. F., Shea, M. A., and Ackers, G. K. (1986) Quantitative DNase footprint titration: a method for studying protein-DNA interactions. Methods Enzymol. 130, 132-181.
    • (1986) Methods Enzymol , vol.130 , pp. 132-181
    • Brenowitz, M.1    Senear, D.F.2    Shea, M.A.3    Ackers, G.K.4
  • 39
    • 15044365667 scopus 로고    scopus 로고
    • Mechanism of DNA binding and localized strand separation by Purα and comparison with Pur family member, Purβ
    • Wortman, M. J., Johnson, E. M., and Bergemann, A. D. (2005) Mechanism of DNA binding and localized strand separation by Purα and comparison with Pur family member, Purβ. Biochim. Biophys. Acta 1743, 64-78.
    • (2005) Biochim. Biophys. Acta , vol.1743 , pp. 64-78
    • Wortman, M.J.1    Johnson, E.M.2    Bergemann, A.D.3
  • 40
    • 0038352888 scopus 로고    scopus 로고
    • Analysis of protein-DNA binding at equilibrium
    • Rippe, K. (1997) Analysis of protein-DNA binding at equilibrium. B.I.F. Futura 12, 20-26.
    • (1997) B.I.F. Futura , vol.12 , pp. 20-26
    • Rippe, K.1
  • 41
    • 0024971458 scopus 로고
    • Phenomenological theory of gel electrophoresis of protein-nucleic acid complexes
    • Cann, J. R. (1989) Phenomenological theory of gel electrophoresis of protein-nucleic acid complexes. J. Biol. Chem. 264, 17032-17040.
    • (1989) J. Biol. Chem , vol.264 , pp. 17032-17040
    • Cann, J.R.1
  • 42
    • 0037183986 scopus 로고    scopus 로고
    • Vascular smooth muscle α-actin gene transcription during myofibroblast differentiation requires Sp1/3 protein binding proximal to the MCAT enhancer
    • Cogan, J. G., Subramanian, S. V., Polikandriotis, J. A., Kelm, R. J. Jr., and Strauch, A. R. (2002) Vascular smooth muscle α-actin gene transcription during myofibroblast differentiation requires Sp1/3 protein binding proximal to the MCAT enhancer. J. Biol. Chem. 277, 36433-36442.
    • (2002) J. Biol. Chem , vol.277 , pp. 36433-36442
    • Cogan, J.G.1    Subramanian, S.V.2    Polikandriotis, J.A.3    Kelm Jr., R.J.4    Strauch, A.R.5
  • 43
    • 34547860091 scopus 로고    scopus 로고
    • The single-strand DNA/RNA-binding protein, Purβ, regulates serum response factor (SRF)-mediated cardiac muscle gene expression
    • Gupta, M., Sueblinvong, V., and Gupta, M. P. (2007) The single-strand DNA/RNA-binding protein, Purβ, regulates serum response factor (SRF)-mediated cardiac muscle gene expression. Can. J. Physiol. Pharmacol. 85, 349-359.
    • (2007) Can. J. Physiol. Pharmacol , vol.85 , pp. 349-359
    • Gupta, M.1    Sueblinvong, V.2    Gupta, M.P.3
  • 44
    • 0022476864 scopus 로고
    • Structure of DNase I at 2.0 Å resolution suggests a mechanism for binding to and cutting DNA
    • Suck, D., and Oefner, C. (1986) Structure of DNase I at 2.0 Å resolution suggests a mechanism for binding to and cutting DNA. Nature 321, 620-625.
    • (1986) Nature , vol.321 , pp. 620-625
    • Suck, D.1    Oefner, C.2
  • 45
    • 0031035170 scopus 로고    scopus 로고
    • The dependence of DNase I activity on the conformation of oligodeoxynucleotides
    • Sutton, D. H., Conn, G. L., Brown, T., and Lane, A. N. (1997) The dependence of DNase I activity on the conformation of oligodeoxynucleotides. Biochem. J. 321, 481-486.
    • (1997) Biochem. J , vol.321 , pp. 481-486
    • Sutton, D.H.1    Conn, G.L.2    Brown, T.3    Lane, A.N.4
  • 46
    • 39549097971 scopus 로고    scopus 로고
    • Brenowitz, M., Senear, D. F., and Kingston, R. E. (2001) DNase I footprint analysis of protein-DNA binding, Current Protocols in Molecular Biology , Chapter 12, Unit 12 14.
    • Brenowitz, M., Senear, D. F., and Kingston, R. E. (2001) DNase I footprint analysis of protein-DNA binding, Current Protocols in Molecular Biology , Chapter 12, Unit 12 14.
  • 47
    • 33644855967 scopus 로고    scopus 로고
    • Cooperative DNA binding by the B-isoform of human progesterone receptor: Thermodynamic analysis reveals strongly favorable and unfavorable contributions to assembly
    • Heneghan, A. F., Connaghan-Jones, K. D., Miura, M. T., and Bain, D. L. (2006) Cooperative DNA binding by the B-isoform of human progesterone receptor: thermodynamic analysis reveals strongly favorable and unfavorable contributions to assembly. Biochemistry 45, 3285-3296.
    • (2006) Biochemistry , vol.45 , pp. 3285-3296
    • Heneghan, A.F.1    Connaghan-Jones, K.D.2    Miura, M.T.3    Bain, D.L.4
  • 48
    • 0037058877 scopus 로고    scopus 로고
    • Cooperative binding of single-stranded telomeric DNA by the Pot1 protein of Schizosaccharomyces pombe
    • Lei, M., Baumann, P., and Cech, T. R. (2002) Cooperative binding of single-stranded telomeric DNA by the Pot1 protein of Schizosaccharomyces pombe. Biochemistry 41, 14560-14568.
    • (2002) Biochemistry , vol.41 , pp. 14560-14568
    • Lei, M.1    Baumann, P.2    Cech, T.R.3
  • 49
    • 34848844722 scopus 로고    scopus 로고
    • Coactivator assembly at the promoter: Efficient recruitment of SRC2 is coupled to cooperative DNA binding by the progesterone receptor
    • Heneghan, A. F., Connaghan-Jones, K. D., Miura, M. T., and Bain, D. L. (2007) Coactivator assembly at the promoter: efficient recruitment of SRC2 is coupled to cooperative DNA binding by the progesterone receptor. Biochemistry 46, 11023-11032.
    • (2007) Biochemistry , vol.46 , pp. 11023-11032
    • Heneghan, A.F.1    Connaghan-Jones, K.D.2    Miura, M.T.3    Bain, D.L.4
  • 50
    • 33847792712 scopus 로고    scopus 로고
    • Thermodynamic analysis of progesterone receptor-promoter interactions reveals a molecular model for isoform-specific function
    • Connaghan-Jones, K. D., Heneghan, A. F., Miura, M. T., and Bain, D. L. (2007) Thermodynamic analysis of progesterone receptor-promoter interactions reveals a molecular model for isoform-specific function. Proc. Natl. Acad. Sci. U.S.A. 104, 2187-2192.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 2187-2192
    • Connaghan-Jones, K.D.1    Heneghan, A.F.2    Miura, M.T.3    Bain, D.L.4
  • 51
    • 0035949647 scopus 로고    scopus 로고
    • DNA recognition by F factor TraI36: Highly sequence-specific binding of single-stranded DNA
    • Stern, J. C., and Schildbach, J. F. (2001) DNA recognition by F factor TraI36: highly sequence-specific binding of single-stranded DNA. Biochemistry 40, 11586-11595.
    • (2001) Biochemistry , vol.40 , pp. 11586-11595
    • Stern, J.C.1    Schildbach, J.F.2
  • 52
    • 0037150123 scopus 로고    scopus 로고
    • R150A mutant of F TraI relaxase domain: Reduced affinity and specificity for single-stranded DNA and altered fluorescence anisotropy of a bound labeled oligonucleotide
    • Harley, M. J., Toptygin, D., Troxler, T., and Schildbach, J. F. (2002) R150A mutant of F TraI relaxase domain: reduced affinity and specificity for single-stranded DNA and altered fluorescence anisotropy of a bound labeled oligonucleotide. Biochemistry 41, 6460-6468.
    • (2002) Biochemistry , vol.41 , pp. 6460-6468
    • Harley, M.J.1    Toptygin, D.2    Troxler, T.3    Schildbach, J.F.4
  • 53
    • 0014963741 scopus 로고
    • T4 bacteriophage gene 32: A structural protein in the replication and recombination of DNA
    • Alberts, B. M., and Frey, L. (1970) T4 bacteriophage gene 32: a structural protein in the replication and recombination of DNA. Nature 227, 1313-1318.
    • (1970) Nature , vol.227 , pp. 1313-1318
    • Alberts, B.M.1    Frey, L.2
  • 54
    • 0016778890 scopus 로고
    • Studies on the cooperative binding of the Escherichia coli DNA unwinding protein to single-stranded DNA
    • Ruyechan, W. T., and Wetmur, J. G. (1975) Studies on the cooperative binding of the Escherichia coli DNA unwinding protein to single-stranded DNA. Biochemistry 14, 5529-5534.
    • (1975) Biochemistry , vol.14 , pp. 5529-5534
    • Ruyechan, W.T.1    Wetmur, J.G.2
  • 55
    • 7544242666 scopus 로고    scopus 로고
    • The dynamic response of upstream DNA to transcription-generated torsional stress
    • Kouzine, F., Liu, J., Sanford, S., Chung, H. J., and Levens, D. (2004) The dynamic response of upstream DNA to transcription-generated torsional stress. Nat. Struct. Mol. Biol. 11, 1092-1100.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 1092-1100
    • Kouzine, F.1    Liu, J.2    Sanford, S.3    Chung, H.J.4    Levens, D.5
  • 56
    • 38849132828 scopus 로고    scopus 로고
    • The functional response of upstream DNA to dynamic supercoiling in vivo
    • Kouzine, F., Sanford, S., Elisha-Feil, Z., and Levens, D. (2008) The functional response of upstream DNA to dynamic supercoiling in vivo. Nat. Struct. Mol. Biol. 15, 146-154.
    • (2008) Nat. Struct. Mol. Biol , vol.15 , pp. 146-154
    • Kouzine, F.1    Sanford, S.2    Elisha-Feil, Z.3    Levens, D.4
  • 57
    • 0032539693 scopus 로고    scopus 로고
    • A unified view of polymer, dumbbell, and oligonucleotide DNA nearest-neighbor thermodynamics
    • SantaLucia, J. Jr. (1998) A unified view of polymer, dumbbell, and oligonucleotide DNA nearest-neighbor thermodynamics. Proc. Natl. Acad. Sci. U.S.A. 95, 1460-1465.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 1460-1465
    • SantaLucia Jr., J.1
  • 58
    • 0035145804 scopus 로고    scopus 로고
    • Helix-destabilizing properties of the human single-stranded DNA- and RNA-binding protein Purα
    • Darbinian, N., Gallia, G. L., and Khalili, K. (2001) Helix-destabilizing properties of the human single-stranded DNA- and RNA-binding protein Purα. J. Cell. Biochem. 80, 589-595.
    • (2001) J. Cell. Biochem , vol.80 , pp. 589-595
    • Darbinian, N.1    Gallia, G.L.2    Khalili, K.3
  • 60
    • 1242342944 scopus 로고    scopus 로고
    • YB-1 promotes strand separation in vitro of duplex DNA containing either mispaired bases or cisplatin modifications, exhibits endonucleolytic activities and binds several DNA repair proteins
    • Gaudreault, I., Guay, D., and Lebel, M. (2004) YB-1 promotes strand separation in vitro of duplex DNA containing either mispaired bases or cisplatin modifications, exhibits endonucleolytic activities and binds several DNA repair proteins. Nucleic Acids Res. 32, 316-327.
    • (2004) Nucleic Acids Res , vol.32 , pp. 316-327
    • Gaudreault, I.1    Guay, D.2    Lebel, M.3
  • 61
    • 0032964375 scopus 로고    scopus 로고
    • Reciprocal interaction between two cellular proteins, Purα and YB-1, modulates transcriptional activity of JCVCY in glial cells
    • Safak, M., Gallia, G. L., and Khalili, K. (1999) Reciprocal interaction between two cellular proteins, Purα and YB-1, modulates transcriptional activity of JCVCY in glial cells. Mol. Cell. Biol. 19, 2712-2723.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 2712-2723
    • Safak, M.1    Gallia, G.L.2    Khalili, K.3
  • 62
    • 0034636708 scopus 로고    scopus 로고
    • Regulation of the human fas promoter by YB-1, Purα and AP-1 transcription factors
    • Lasham, A., Lindridge, E., Rudert, F., Onrust, R., and Watson, J. (2000) Regulation of the human fas promoter by YB-1, Purα and AP-1 transcription factors. Gene 252, 1-13.
    • (2000) Gene , vol.252 , pp. 1-13
    • Lasham, A.1    Lindridge, E.2    Rudert, F.3    Onrust, R.4    Watson, J.5


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