The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
A bacterial two-hybrid selection system for studying protein–DNA and protein–protein interactions
Open accessAbstract
We have developed a bacterial “two-hybrid” system that readily allows selection from libraries larger than 10 8 in size. Our bacterial system may be used to study either protein–DNA or protein—protein interactions, and it offers a number of potentially significant advantages over existing yeast-based one-hybrid and two-hybrid methods. We tested our system by selecting zinc finger variants (from a large randomized library) that bind tightly and specifically to desired DNA target sites. Our method allows sequence-specific zinc fingers to be isolated in a single selection step, and thus it should be more rapid than phage display strategies that typically require multiple enrichment/amplification cycles. Given the large library sizes our bacterial-based selection system can handle, this method should provide a powerful tool for identifying and optimizing protein–DNA and protein–protein interactions.
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Cites
A bacterial two-hybrid system based on a reconstituted signal transduction pathway
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DNA Recognition by Cys2His2 Zinc Finger Proteins
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Self-citationProtein-protein interactions: methods for detection and analysis.
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A General Strategy for Selecting High-Affinity Zinc Finger Proteins for Diverse DNA Target Sites
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Self-citationActivation of prokaryotic transcription through arbitrary protein–protein contacts
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Self-citationNucleotide sequence analysis of a gene encoding a streptomycin/spectinomycin adenyltransferase
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Self-citationTechnological advances in high-throughput screening
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Cited by
Durai, S. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki912 · Cited by 522
Targeted genome editing in human cells with zinc finger nucleases constructed via modular assembly
Kim, H. J., Lee, H. J., Kim, H., Cho, S. W., & Kim, J.-S. (2009) · Genome Research · doi:10.1101/gr.089417.108 · Cited by 466
Zinc-finger nucleases as a novel therapeutic strategy for targeting hepatitis B virus DNAs
Cradick, T. J., Keck, K., Bradshaw, S., Jamieson, A. C., & McCaffrey, A. P. (2010) · Molecular Therapy · doi:10.1038/mt.2010.20 · Cited by 184
Deconstruction of the Ras switching cycle through saturation mutagenesis
Bandaru, P., Shah, N. H., Bhattacharyya, M., Barton, J. P., Kondo, Y., Cofsky, J. C., Gee, C. L., Chakraborty, A. K., Kortemme, T., Ranganathan, R., et al. (2017) · eLife · doi:10.7554/elife.27810 · Cited by 117
“fused to the phage l-cI DNA binding domain (Dove et al., 1997; Joung et al., 2000).”
BackgroundMethodA systematic method for identifying small-molecule modulators of protein–protein interactions
Horswill, A. R., Savinov, S. N., & Benkovic, S. J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406999101 · Cited by 110
Metadata
- Authors
- Joung, J. K., Ramm, E. I., & Pabo, C. O.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-06-13
- Volume
- 97
- Issue
- 13
- Pages
- 7382-7387
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2132245233
- Cited by
- 357
- References
- 20
- FWCI
- 4.51
- Type
- journal article
- Language
- en
- Open access
- green
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