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Foguel, D., Silva, J. L. (1994) Cold denaturation of a repressor-operator complex: the role of entropy in protein-DNA recognition. Proceedings of the National Academy of Sciences, 91 (17) 8244-8247 doi:10.1073/pnas.91.17.8244

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Reference TypeJournal (article/letter/editorial)
TitleCold denaturation of a repressor-operator complex: the role of entropy in protein-DNA recognition.
JournalProceedings of the National Academy of Sciences
AuthorsFoguel, D.Author
Silva, J. L.Author
Year1994 (August 16)Volume91
Issue17
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.91.17.8244Search in ResearchGate
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Mindat Ref. ID1543907Long-form Identifiermindat:1:5:1543907:9
GUID0
Full ReferenceFoguel, D., Silva, J. L. (1994) Cold denaturation of a repressor-operator complex: the role of entropy in protein-DNA recognition. Proceedings of the National Academy of Sciences, 91 (17) 8244-8247 doi:10.1073/pnas.91.17.8244
Plain TextFoguel, D., Silva, J. L. (1994) Cold denaturation of a repressor-operator complex: the role of entropy in protein-DNA recognition. Proceedings of the National Academy of Sciences, 91 (17) 8244-8247 doi:10.1073/pnas.91.17.8244
In(1994, August) Proceedings of the National Academy of Sciences Vol. 91 (17) Proceedings of the National Academy of Sciences

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Lima, L. M. T. R., Foguel, D., Silva, J. L. (2000) DNA tightens the dimeric DNA-binding domain of human papillomavirus E2 protein without changes in volume. Proceedings of the National Academy of Sciences, 97 (26) 14289-14294 doi:10.1073/pnas.250352197
Huang, L., Sera, T., Schultz, P. G. (1994) A permutational approach toward protein-DNA recognition. Proceedings of the National Academy of Sciences, 91 (9) 3969-3973 doi:10.1073/pnas.91.9.3969
Kelley, R. L., Yanofsky, C. (1985) Mutational studies with the trp repressor of Escherichia coli support the helix-turn-helix model of repressor recognition of operator DNA. Proceedings of the National Academy of Sciences, 82 (2) 483-487 doi:10.1073/pnas.82.2.483
Lia, G., Bensimon, D., Croquette, V., Allemand, J.-F., Dunlap, D., Lewis, D. E. A., Adhya, S., Finzi, L. (2003) Supercoiling and denaturation in Gal repressor/heat unstable nucleoid protein (HU)-mediated DNA looping. Proceedings of the National Academy of Sciences, 100 (20) 11373-11377 doi:10.1073/pnas.2034851100
Yang, W., Ni, L., Somerville, R. L. (1993) A stationary-phase protein of Escherichia coli that affects the mode of association between the trp repressor protein and operator-bearing DNA. Proceedings of the National Academy of Sciences, 90 (12) 5796-5800 doi:10.1073/pnas.90.12.5796
Le Cam, E., Frechon, D., Barray, M., Fourcade, A., Delain, E. (1994) Observation of binding and polymerization of Fur repressor onto operator-containing DNA with electron and atomic force microscopes. Proceedings of the National Academy of Sciences, 91 (25) 11816-11820 doi:10.1073/pnas.91.25.11816
Swigon, D., Coleman, B. D., Olson, W. K. (2006) Modeling the Lac repressor-operator assembly: The influence of DNA looping on Lac repressor conformation. Proceedings of the National Academy of Sciences, 103 (26) 9879-9884 doi:10.1073/pnas.0603557103
Suwa, A., Hirakata, M., Takeda, Y., Jesch, S. A., Mimori, T., Hardin, J. A. (1994) DNA-dependent protein kinase (Ku protein-p350 complex) assembles on double-stranded DNA. Proceedings of the National Academy of Sciences, 91 (15) 6904-6908 doi:10.1073/pnas.91.15.6904
Ferrao-Gonzales, A. D., Souto, S. O., Silva, J. L., Foguel, D. (2000) The preaggregated state of an amyloidogenic protein: Hydrostatic pressure converts native transthyretin into the amyloidogenic state. Proceedings of the National Academy of Sciences, 97 (12) 6445-6450 doi:10.1073/pnas.97.12.6445
Frattini, M. G., Laimins, L. A. (1994) Binding of the human papillomavirus E1 origin-recognition protein is regulated through complex formation with the E2 enhancer-binding protein. Proceedings of the National Academy of Sciences, 91 (26) 12398-12402 doi:10.1073/pnas.91.26.12398
Ryu, S. (1994) Corrections: An Arcane Role of DNA in Transcription Activation. Proceedings of the National Academy of Sciences, 91 (23) 11281 doi:10.1073/pnas.91.23.11281b
 
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