Evidence map›Paper›PMID 23248739›Full record

ArticleCurrent chemical genomics2012

Development of a dehalogenase-based protein fusion tag capable of rapid, selective and covalent attachment to customizable ligands.

Lance P Encell, Rachel Friedman Ohana, Kris Zimmerman, Paul Otto, Gediminas Vidugiris, Monika G Wood, Georgyi V Los, Mark G McDougall, Chad Zimprich, Natasha Karassina and 17 more

Abstract read
In one paragraph

Article in Current chemical genomics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing 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

76 citing papers in PubMed.

  1. Article
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  9. Optogenetic control of PLC-γ1 activity polarizes cell motility.bioRxiv : the preprint server for biology · 2025
    Article
  10. Conformational plasticity of a BiP-GRP94 chaperone complex.Nature structural & molecular biology · 2025
    Article
  11. Review
  12. Article
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  15. Chemigenetic Far-Red Labels and CaJournal of the American Chemical Society · 2024
    Article
  16. Article
  17. CaCommunications biology · 2024
    Article
  18. Article
  19. Article
  20. Article

16 more citing papers are in PubMed but not listed here.

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

27 authors.

Lance P EncellPromega Corporation, Madison, WI, USA.
Rachel Friedman Ohana
Kris Zimmerman
Paul Otto
Gediminas Vidugiris
Monika G Wood
Georgyi V Los
Mark G McDougall
Chad Zimprich
Natasha Karassina
Randall D Learish
Robin Hurst
James Hartnett
Sarah Wheeler
Pete Stecha
Jami English
Kate Zhao
Jacqui Mendez
Hélène A Benink
Nancy Murphy
Danette L Daniels
Michael R Slater
Marjeta Urh
Aldis Darzins
Dieter H Klaubert
Robert F Bulleit
Keith V Wood

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Our fundamental understanding of proteins and their biological significance has been enhanced by genetic fusion tags, as they provide a convenient method for introducing unique properties to proteins so that they can be examinedin isolation. Commonly used tags satisfy many of the requirements for applications relating to the detection and isolation of proteins from complex samples. However, their utility at low concentration becomes compromised if the binding affinity for a detection or capture reagent is not adequate to produce a stable interaction. Here, we describe HaloTag® (HT7), a genetic fusion tag based on a modified haloalkane dehalogenase designed and engineered to overcome the limitation of affinity tags by forming a high affinity, covalent attachment to a binding ligand. HT7 and its ligand have additional desirable features. The tag is relatively small, monomeric, and structurally compatible with fusion partners, while the ligand is specific, chemically simple, and amenable to modular synthetic design. Taken together, the design features and molecular evolution of HT7 have resulted in a superior alternative to common tags for the overexpression, detection, and isolation of target proteins.

Indexed as

Affinity tagdehalogenaseDhaAdirected evolutionfusion tagHaloTagprotein captureprotein/cellular imagingprotein detectionprotein engineeringprotein isolationprotein labelingprotein purification.

Identifiers

PMID23248739
PMCPMC3520037

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Registered trials

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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.