Relevant bibliographies by topics / DNase I Footprinting

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  1. Journal articles

Academic literature on the topic 'DNase I Footprinting'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "DNase I Footprinting"

1

Carey, M. F., C. L. Peterson, and S. T. Smale. "DNase I Footprinting." Cold Spring Harbor Protocols 2013, no. 5 (2013): pdb.prot074328. http://dx.doi.org/10.1101/pdb.prot074328.

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2

Ward, Brian, and James C. Dabrowiak. "Stability of DNase I in footprinting experiments." Nucleic Acids Research 16, no. 17 (1988): 8724. http://dx.doi.org/10.1093/nar/16.17.8724.

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3

Wilson, Douglas O., Peter Johnson, and Bruce R. McCord. "Nonradiochemical DNase I footprinting by capillary electrophoresis." ELECTROPHORESIS 22, no. 10 (2001): 1979–86. http://dx.doi.org/10.1002/1522-2683(200106)22:10<1979::aid-elps1979>3.0.co;2-a.

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4

Smith, Susan E., and Athanasios G. Papavassiliou. "A coupled Southwestern - DNase I footprinting assay." Nucleic Acids Research 20, no. 19 (1992): 5239–40. http://dx.doi.org/10.1093/nar/20.19.5239.

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5

Nagawa, Fumikiyo, Kei-ichiro Ishiguro, Akio Tsuboi, et al. "Footprint Analysis of the RAG Protein Recombination Signal Sequence Complex for V(D)J Type Recombination." Molecular and Cellular Biology 18, no. 1 (1998): 655–63. http://dx.doi.org/10.1128/mcb.18.1.655.

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ABSTRACT We have studied the interaction between recombination signal sequences (RSSs) and protein products of the truncated forms of recombination-activating genes (RAG) by gel mobility shift, DNase I footprinting, and methylation interference assays. Methylation interference with dimethyl sulfate demonstrated that binding was blocked by methylation in the nonamer at the second-position G residue in the bottom strand and at the sixth- and seventh-position A residues in the top strand. DNase I footprinting experiments demonstrated that RAG1 alone, or even a RAG1 homeodomain peptide, gave footp
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6

Wilson, D. O., P. Johnson, and B. R. McCord. "Non-radiochemical DNase I footprinting by capillary electrophoresis." Biochemical Society Transactions 28, no. 5 (2000): A366. http://dx.doi.org/10.1042/bst028a366a.

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7

Sandaltzopoulos, Raphael, and Peter B. Becker. "Solid phase DNase I footprinting: quick and versatile." Nucleic Acids Research 22, no. 8 (1994): 1511–12. http://dx.doi.org/10.1093/nar/22.8.1511.

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8

Nightingale, K. P., and K. R. Fox. "Interaction of bleomycin with a bent DNA fragment." Biochemical Journal 284, no. 3 (1992): 929–34. http://dx.doi.org/10.1042/bj2840929.

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The interaction of bleomycin with a kinetoplast DNA fragment has been examined using various footprinting techniques. This DNA adopts a bent structure and displays an unusually low gel mobility on account of its phased runs of adenines. The bleomycin-cobalt complex increases the mobility of this DNA fragment, in contrast with other DNAs which show a decreased rate of gel migration, suggesting that the antibiotic removes DNA bending, possibly via an unwinding mechanism. Removal of the bending is confirmed by hydroxy-radical footprinting which produces a more even ladder of bands in the presence
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9

ANGERS, Martin, Régen DROUIN, Magdalena BACHVAROVA, et al. "In vivo DNase I-mediated footprinting analysis along the human bradykinin B1 receptor (BDKRB1) gene promoter: evidence for cell-specific regulation." Biochemical Journal 389, no. 1 (2005): 37–46. http://dx.doi.org/10.1042/bj20042104.

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By applying in vivo dimethyl sulphate and UV light type C-footprinting analysis, we previously showed that specific DNA sequences in the −1349/+42 core promoter region of the inducible human BDKRB1 (bradykinin B1 receptor) gene correlated with its transcriptional activity. In the present study we used the highly sensitive DNase I in vivo footprinting approach to delineate more precisely the functional domains of the BDKRB1 gene promoter in human SMCs (smooth muscle cells). Human lymphocytes that do not express a functional BDKRB1 were also studied as a reference using dimethyl sulphate, UV lig
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10

Goodisman, Jerry, and James C. Dabrowiak. "Structural changes and enhancements in DNase I footprinting experiments." Biochemistry 31, no. 4 (1992): 1058–64. http://dx.doi.org/10.1021/bi00119a014.

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