DNA recognition by Cys2His2 zinc finger proteins.

By Scot A. Wolfe, L. Nekludova, C. Pabo. Annual Review of Biophysics and Biomolecular Structure, 2000

1,047 citations recorded by the source corpus.

Subfields: Molecular Biology, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/8585e45d63e75ff2a5dff318539603742c6089b1

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. David Baker
2. Justin Ashworth
3. Gabriele Varani
4. M. Holmes
5. Carlos F. Barbas III
6. Jerilyn A. Timlin
7. Jeffrey G. Mandell
8. J. Carney

In Radiology, Nuclear Medicine and Imaging

1. David Baker
2. Carlos F. Barbas III
3. Jeffrey G. Mandell
4. Frances H. Arnold

Citations in the corpus

• Zinc Finger Tools: custom DNA-binding domains for transcription factors and nucleases (2006, methodology): “Nonetheless, mutagenesis of the linker sequence TGEKP results in substantial loss of DNA-binding affinity (17).”
• TALENs: a widely applicable technology for targeted genome editing (2012, neutral): “83, 84 Engineered zinc fingers can be joined together into more extended arrays capable of recognizing longer DNA sequences.”
• Delivering CRISPR: a review of the challenges and approaches (2018, background): “ZFPs are common in eukaryotic cells and are associated with transcriptional regulation and protein–protein interactions (Wolfe et al., 2000; Urnov et al., 2010).”
• RNA-binding proteins: modular design for efficient function (2007, background): “CCHH zinc fingers interact with DNA primarily by forming direct hydrogen bonds to Watson–Crick base pairs in the major groove, using residues in their recognition α-heli”
• Sp1- and Krüppel-like transcription factors (2003, background): “X represents any amino acid and is a hydrophobic residue [24].”
• Structural basis for Klf4 recognition of methylated DNA (2014, background): “As in previously characterized DNA-binding ZnF structures (42), the DNA base contacts are made by the side chains in the N-terminal portion of the a helix, together with the residue immediately preceding the a helix.”
• Assessment of the optimization of affinity and specificity at protein–DNA interfaces (2009, background): “studies (1,17,18) have identified several key amino acid residues that play important roles in optimizing DNAbinding affinity and specificity for Zif268 and for the C2H2 zinc finger family as a whole.”
• Wilms tumor protein recognizes 5-carboxylcytosine within a specific DNA sequence (2014, positive): “It binds to the consensus sequence 5 9 - GCG(T/G)GGGCG-3 9 and has been used as a framework for engineering novel DNA-binding specificities (Wolfe et al. 2000; Klug 2010).”
• Genome editing with engineered zinc finger nucleases (2010, background): “This region contains a tandem array of Cys2-His2 finger”