Evidence map›Paper›PMID 29718463›Full record

ReviewNucleic acids research2018

Engineering altered protein-DNA recognition specificity.

Adam J Bogdanove, Andrew Bohm, Jeffrey C Miller, Richard D Morgan, Barry L Stoddard

Abstract readReview
In one paragraph

Review in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. RNA sequence design and protein-DNA specificity prediction with NA-MPNN.bioRxiv : the preprint server for biology · 2025
    Article
  5. Engineering Protein-Polyelectrolyte Interactions for Cellular Applications.Annual review of chemical and biomolecular engineering · 2025
    Review
  6. Article
  7. Review
  8. Dynamics in Cre-loxP site-specific recombination.Current opinion in structural biology · 2024
    Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Adam J BogdanovePlant Pathology and Plant-Microbe Biology Section, School of Integrative Plant Science, Cornell University, Ithaca, NY 14853, USA.
Andrew BohmSackler School of Graduate Biomedical Sciences, Tufts University, 136 Harrison Avenue, Boston, MA 02111, USA.
Jeffrey C MillerSangamo Therapeutics Inc. 501 Canal Blvd., Richmond, CA 94804, USA.
Richard D MorganNew England Biolabs, Inc., 240 County Road, Ipswich, MA 01938, USA.
Barry L StoddardDivision of Basic Sciences, Fred Hutchinson Cancer Research Center, 1100 Fairview Ave. N., Seattle, WA 98019, USA.

Funding

MegaTALS: hyperspecific reagents for targeted gene modification and correctionR01GM105691 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI STODDARD, BARRY L. · 2014 to 2022
$2.7M
A structure-based approach to accelerated recombinase engineeringR01AI150499 · NIAID · TUFTS UNIVERSITY BOSTON · PI BOHM, ALEX ANDREW · 2020 to 2021
$495k
A structure-based approach to accelerated recombinase engineeringR01GM126149 · NIGMS · TUFTS UNIVERSITY BOSTON · PI BOHM, ALEX ANDREW · 2018 to 2019
$495k
NIAID NIH HHS R01 AI150499NIGMS NIH HHS R01 GM105691NIGMS NIH HHS R01 GM126149
6 · The paper itself

Abstract

Protein engineering is used to generate novel protein folds and assemblages, to impart new properties and functions onto existing proteins, and to enhance our understanding of principles that govern protein structure. While such approaches can be employed to reprogram protein-protein interactions, modifying protein-DNA interactions is more difficult. This may be related to the structural features of protein-DNA interfaces, which display more charged groups, directional hydrogen bonds, ordered solvent molecules and counterions than comparable protein interfaces. Nevertheless, progress has been made in the redesign of protein-DNA specificity, much of it driven by the development of engineered enzymes for genome modification. Here, we summarize the creation of novel DNA specificities for zinc finger proteins, meganucleases, TAL effectors, recombinases and restriction endonucleases. The ease of re-engineering each system is related both to the modularity of the protein and the extent to which the proteins have evolved to be capable of readily modifying their recognition specificities in response to natural selection. The development of engineered DNA binding proteins that display an ideal combination of activity, specificity, deliverability, and outcomes is not a fully solved problem, however each of the current platforms offers unique advantages, offset by behaviors and properties requiring further study and development.

Indexed as

Base PairingDeoxyribonucleasesDNADNA-Binding ProteinsDNA CleavageDNA Restriction EnzymesGene EditingProtein EngineeringRecombinant ProteinsRecombinasesTranscription Activator-Like EffectorsZinc FingersDeoxyribonucleasesDNADNA-Binding ProteinsDNA Restriction EnzymesRecombinant ProteinsRecombinasesTranscription Activator-Like Effectors

Identifiers

PMID29718463
PMCPMC6007267

What OpenQuestion holds

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LicenceCC BY-NC
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.