An improved zinc-finger nuclease architecture for highly specific genome editing (Q28307951)

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Edward Rebar

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object named as

Edward J Rebar

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author name string

Jeffrey C Miller

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Michael C Holmes

2

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Jianbin Wang

3

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Dmitry Y Guschin

4

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Ya-Li Lee

5

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Igor Rupniewski

6

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Christian M Beausejour

7

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Nathaniel S Wang

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Kenneth A Kim

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Carl O Pabo

Hybrid restriction enzymes: zinc finger fusions to Fok I cleavage domain

12

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language of work or name

English

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publication date

July 2007

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published in

Nature Biotechnology

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volume

25

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issue

7

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page(s)

778-85

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cites work

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Enhancing Gene Targeting with Designed Zinc Finger Nucleases

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Targeted gene addition into a specified location in the human genome using designed zinc finger nucleases

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Homology-directed repair is a major double-strand break repair pathway in mammalian cells

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High-resolution structures of variant Zif268-DNA complexes: implications for understanding zinc finger-DNA recognition

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Zif268 protein-DNA complex refined at 1.6 A: a model system for understanding zinc finger-DNA interactions

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Rearrangement of side-chains in a Zif268 mutant highlights the complexities of zinc finger-DNA recognition

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A general strategy for selecting high-affinity zinc finger proteins for diverse DNA target sites

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Toward controlling gene expression at will: selection and design of zinc finger domains recognizing each of the 5'-GNN-3' DNA target sequences

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Highly specific zinc finger proteins obtained by directed domain shuffling and cell-based selection

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Design and selection of novel Cys2His2 zinc finger proteins

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A rapid, generally applicable method to engineer zinc fingers illustrated by targeting the HIV-1 promoter

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Genome maintenance mechanisms for preventing cancer

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Targeted mutagenesis using zinc-finger nucleases in Arabidopsis

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High-frequency homologous recombination in plants mediated by zinc-finger nucleases.

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Induction and repair of zinc-finger nuclease-targeted double-strand breaks in Caenorhabditis elegans somatic cells

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FokI dimerization is required for DNA cleavage

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FokI requires two specific DNA sites for cleavage

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Requirements for double-strand cleavage by chimeric restriction enzymes with zinc finger DNA-recognition domains

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Binding of two zinc finger nuclease monomers to two specific sites is required for effective double-strand DNA cleavage

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Purification and characterization of the FokI restriction endonuclease

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Zinc-finger protein-targeted gene regulation: genomewide single-gene specificity.

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Engineered zinc finger proteins for controlling stem cell fate

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Positive and negative regulation of endogenous genes by designed transcription factors

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Heritable endogenous gene regulation in plants with designed polydactyl zinc finger transcription factors

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Peptide 'Velcro': design of a heterodimeric coiled coil.

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Remodeling domain interfaces to enhance heterodimer formation

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Automated design of specificity in molecular recognition

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Specificity versus stability in computational protein design

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Structure of FokI has implications for DNA cleavage

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Computational design of a new hydrogen bond network and at least a 300-fold specificity switch at a protein-protein interface

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p53 binding protein 1 (53BP1) is an early participant in the cellular response to DNA double-strand breaks

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Computational redesign of protein-protein interaction specificity

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