Length-encoded multiplex binding site determination: application to zinc finger proteins.
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Summary
An oligonucleotide library search procedure in which the identity of each member is encoded in the length of oligon nucleotides is described, which allows binding-site preferences to be evaluated via DNA length determination by denaturing gel electrophoresis.
- Type
- article
- Published
- 1994-11-08
- Cited by
- 68
- References
- 3
- Access
- Open access
- OpenAlex
- https://openalex.org/W2113582390
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:22995197
Keywords
Zinc finger, Zinc finger nuclease, Oligonucleotide, Multiplex, Computational biology
References
Cited by
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- Histone peptide AKRHRK enhances H(2)O(2)-induced DNA damage and alters its site specificity.
- A zinc finger directory for high-affinity DNA recognition.
- Combining structure-based design with phage display to create new Cys(2)His(2) zinc finger dimers.
- Role of Promoter DNA Sequence Variations on the Binding of EGR1 Transcription Factor
- Human zinc fingers as building blocks in the construction of artificial transcription factors
- Prediction of DNA-binding proteins from relational features
- Binding Studies with Mutants of Zif268
- The 5′‐untranslated RNA of the human dhfr minor transcript alters transcription pre‐initiation complex assembly at the major (core) promoter
- The Galvanization of Biology: A Growing Appreciation for the Roles of Zinc
- Physical basis of a protein-DNA recognition code.
- Theoretical studies on interactions between low energy electrons and protein-DNA fragments: valence anions of AT-amino acids side chain complexes.
- Zinc-finger-based artificial transcription factors and their applications.
- Probing the DNA-binding affinity and specificity of designed zinc finger proteins.
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